Patent Publication Number: US-2007111232-A1

Title: Corynebacterium glutamicum genes encoding proteins involved in homeostasis and adaptation

Description:
RELATED APPLICATIONS  
      This application is a divisional of U.S. application Ser. No. 10/454,437, filed Jun. 4, 2003 which is a continuation of U.S. application Ser. No. 09/602,777, filed Jun. 23, 2000, now U.S. Pat. No. 6,831,165, issued Dec. 14, 2004, which claims priority to prior filed U.S. Provisional Patent Application Ser. No. 60/141,031, filed Jun. 25, 1999. This application also claims priority to prior filed German Patent Application No. 19931636.8, filed Jul. 8, 1999, German Patent Application No. 19932125.6, filed Jul. 9, 1999, German Patent Application No. 19932126.4, filed Jul. 9, 1999, German Patent Application No. 19932127.2, filed Jul. 9, 1999, German Patent Application No. 19932128.0, filed Jul. 9, 1999, German Patent Application No. 19932129.9, filed Jul. 9, 1999, German Patent Application No. 19932226.0, filed Jul. 9, 1999, German Patent Application No. 19932920.6, filed Jul. 14, 1999, German Patent Application No. 19932922.2, filed Jul. 14, 1999, German Patent Application No. 19932924.9, filed Jul. 14, 1999, German Patent Application No. 19932928.1, filed Jul. 14, 1999, German Patent Application No. 19932930.3, filed Jul. 14, 1999, German Patent Application No. 19932933.8, filed Jul. 14, 1999, German Patent Application No. 19932935.4, filed Jul. 14, 1999, German Patent Application No. 19932973.7, filed Jul. 14, 1999, German Patent Application No. 19933002.6, filed Jul. 14, 1999, German Patent Application No. 19933003.4, filed Jul. 14, 1999, German Patent Application No. 19933005.0, filed Jul. 14, 1999, German Patent Application No. 19933006.9, filed Jul. 14, 1999, German Patent Application No. 19941378.9, filed Aug. 31, 1999, German Patent Application No. 19941379.7, filed Aug. 31, 1999, German Patent Application No. 19941390.8, filed Aug. 31, 1999, German Patent Application No. 19941391.6, filed Aug. 31, 1999, and German Patent Application No. 19942088.2, filed Sep. 3, 1999. The entire contents of each of the aforementioned applications are hereby expressly incorporated herein by this reference. 
    
    
     INCORPORATION OF MATERIAL SUBMITTED ON COMPACT DISCS  
      This application incorporates herein by reference the material contained on the compact discs submitted herewith as part of this application. Specifically, the file “seqlistcorrected” (1.45 MB) contained on each of Copy 1, Copy 2 and the CRF copy of the Sequence Listing is hereby incorporated herein by reference. This file was created on Jul. 31, 2006. In addition, the files “Appendix A” (430 KB) and “Appendix B” (151 KB) contained on each of the compact disks entitled “Appendices Copy 1” and “Appendices Copy 2” are hereby incorporated herein by reference. Each of these files were created on Jul. 31, 2006.  
     BACKGROUND OF THE INVENTION  
      Certain products and by-products of naturally-occurring metabolic processes in cells have utility in a wide array of industries, including the food, feed, cosmetics, and pharmaceutical industries. These molecules, collectively termed ‘fine chemicals’, include organic acids, both proteinogenic and non-proteinogenic amino acids, nucleotides and nucleosides, lipids and fatty acids, diols, carbohydrates, aromatic compounds, vitamins and cofactors, and enzymes. Their production is most conveniently performed through the large-scale culture of bacteria developed to produce and secrete large quantities of one or more desired molecules. One particularly useful organism for this purpose is  Corynebacterium glutamicum , a gram positive, nonpathogenic bacterium. Through strain selection, a number of mutant strains have been developed which produce an array of desirable compounds. However, selection of strains improved for the production of a particular molecule is a time-consuming and difficult process.  
     SUMMARY OF THE INVENTION  
      The invention provides novel bacterial nucleic acid molecules which have a variety of uses. These uses include the identification of microorganisms which can be used to produce fine chemicals, the modulation of fine chemical production in  C. glutamicum  or related bacteria, the typing or identification of  C. glutamicum  or related bacteria, as reference points for mapping the  C. glutamicum  genome, and as markers for transformation. These novel nucleic acid molecules encode proteins, referred to herein as homeostasis and adaptation (HA) proteins.  
       C. glutamicum  is a gram positive, aerobic bacterium which is commonly used in industry for the large-scale production of a variety of fine chemicals, and also for the degradation of hydrocarbons (such as in petroleum spills) and for the oxidation of terpenoids. The HA nucleic acid molecules of the invention, therefore, can be used to identify microorganisms which can be used to produce fine chemicals, e.g., by fermentation processes. Modulation of the expression of the HA nucleic acids of the invention, or modification of the sequence of the HA nucleic acid molecules of the invention, can be used to modulate the production of one or more fine chemicals from a microorganism (e.g., to improve the yield or production of one or more fine chemicals from a  Corynebacterium  or  Brevibacterium  species).  
      The HA nucleic acids of the invention may also be used to identify an organism as being  Corynebacterium glutamicum  or a close relative thereof, or to identify the presence of  C. glutamicum  or a relative thereof in a mixed population of microorganisms. The invention provides the nucleic acid sequences of a number of  C. glutamicum  genes; by probing the extracted genomic DNA of a culture of a unique or mixed population of microorganisms under stringent conditions with a probe spanning a region of a  C. glutamicum  gene which is unique to this organism, one can ascertain whether this organism is present. Although  Corynebacterium glutamicum  itself is nonpathogenic, it is related to species pathogenic in humans, such as  Corynebacterium diphtheriae  (the causative agent of diphtheria); the detection of such organisms is of significant clinical relevance.  
      The HA nucleic acid molecules of the invention may also serve as reference points for mapping of the  C. glutamicum  genome, or of genomes of related organisms. Similarly, these molecules, or variants or portions thereof, may serve as markers for genetically engineered  Corynebacterium  or  Brevibacterium  species.  
      e.g. The HA proteins encoded by the novel nucleic acid molecules of the invention are capable of, for example, performing a function involved in the maintenance of homeostasis in  C. glutamicum , or in the ability of this microorganism to adapt to different environmental conditions. Given the availability of cloning vectors for use in  Corynebacterium glutamicum , such as those disclosed in Sinskey et al., U.S. Pat. No. 4,649,119, and techniques for genetic manipulation of  C. glutamicum  and the related  Brevibacterium  species (e.g.,  lactofermentum ) (Yoshihama et al,  J. Bacteriol.  162: 591-597 (1985); Katsumata et al.,  J. Bacteriol.  159: 306-311 (1984); and Santamaria et al.,  J. Gen. Microbiol.  130: 2237-2246 (1984)), the nucleic acid molecules of the invention may be utilized in the genetic engineering of this organism to make it a better or more efficient producer of one or more fine chemicals. This improved production or efficiency of production of a fine chemical may be due to a direct effect of manipulation of a gene of the invention, or it may be due to an indirect effect of such manipulation.  
      There are a number of mechanisms by which the alteration of an HA protein of the invention may directly affect the yield, production, and/or efficiency of production of a fine chemical from a  C. glutamicum  strain incorporating such an altered protein. For example, by engineering enzymes which modify or degrade aromatic or aliphatic compounds such that these enzymes are increased or decreased in activity or number, it may be possible to modulate the production of one or more fine chemicals which are the modification or degradation products of these compounds. Similarly, enzymes involved in the metabolism of inorganic compounds provide key molecules (e.g. phosphorous, sulfur, and nitrogen molecules) for the biosynthesis of such fine chemicals as amino acids, vitamins, and nucleic acids. By altering the activity or number of these enzymes in  C. glutamicum , it may be possible to increase the conversion of these inorganic compounds (or to use alternate inorganic compounds) to thus permit improved rates of incorporation of inorganic atoms into these fine chemicals. Genetic engineering of  C. glutamicum  enzymes involved in general cellular processes may also directly improve fine chemical production, since many of these enzymes directly modify fine chemicals (e.g., amino acids) or the enzymes which are involved in fine chemical synthesis or secretion. Modulation of the activity or number of cellular proteases may also have a direct effect on fine chemical production, since many proteases may degrade fine chemicals or enzymes involved in fine chemical production or breakdown.  
      Further, the aforementioned enzymes which participate in aromatic/aliphatic compound modification or degradation, general biocatalysis, inorganic compound metabolism or proteolysis are each themselves fine chemicals, desirable for their activity in various in vitro industrial applications. By altering the number of copies of the gene for one or more of these enzymes in  C. glutamicum  it may be possible to increase the number of these proteins produced by the cell, thereby increasing the potential yield or efficiency of production of these proteins from large-scale  C. glutamicum  or related bacterial cultures.  
      The alteration of an HA protein of the invention may also indirectly affect the yield, production, and/or efficiency of production of a fine chemical from a  C. glutamicum  strain incorporating such an altered protein. For example, by modulating the activity and/or number of those proteins involved in the construction or rearrangement of the cell wall, it may be possible to modify the structure of the cell wall itself such that the cell is able to better withstand the mechanical and other stresses present during large-scale fermentative culture. Also, large-scale growth of  C. glutamicum  requires significant cell wall production. Modulation of the activity or number of cell wall biosynthetic or degradative enzymes may allow more rapid rates of cell wall biosynthesis, which in turn may permit increased growth rates of this microorganism in culture and thereby increase the number of cells producing the desired fine chemical.  
      By modifying the HA enzymes of the invention, one may also indirectly impact the yield, production, or efficiency of production of one or more fine chemicals from  C. glutamicum . For example, many of the general enzymes in  C. glutamicum  may have a significant impact on global cellular processes (e.g., regulatory processes) which in turn have a significant effect on fine chemical metabolism. Similarly, proteases, enzymes which modify or degrade possibly toxic aromatic or aliphatic compounds, and enzymes which promote the metabolism of inorganic compounds all serve to increase the viability of  C. glutamicum . The proteases aid in the selective removal of misfolded or misregulated proteins, such as those that might occur under the relatively stressful environmental conditions encountered during large-scale fermentor culture. By altering these proteins, it may be possible to further enhance this activity and to improve the viability of  C. glutamicum  in culture. The aromatic/aliphatic modification or degradation proteins not only serve to detoxify these waste compounds (which may be encountered as impurities in culture medium or as waste products from cells themselves), but also to permit the cells to utilize alternate carbon sources if the optimal carbon source is limiting in the culture. By increasing their number and/or activity, the survival of  C. glutamicum  cells in culture may be enhanced. The inorganic metabolism proteins of the invention supply the cell with inorganic molecules required for all protein and nucleotide (among others) synthesis, and thus are critical for the overall viability of the cell. An increase in the number of viable cells producing one or more desired fine chemicals in large-scale culture should result in a concomitant increase in the yield, production, and/or efficiency of production of the fine chemical in the culture.  
      The invention provides novel nucleic acid molecules which encode proteins, referred to herein as HA proteins, which are capable of, for example, performing a function involved in the maintenance of homeostasis in  C. glutamicum , or of participating in the ability of this microorganism to adapt to different environmental conditions. Nucleic acid molecules encoding an HA protein are referred to herein as HA nucleic acid molecules. In a preferred embodiment, an HA protein participates in  C. glutamicum  cell wall biosynthesis or rearrangements, metabolism of inorganic compounds, modification or degradation of aromatic or aliphatic compounds, or possesses a  C. glutamicum  enzymatic or proteolytic activity. Examples of such proteins include those encoded by the genes set forth in Table 1.  
      Accordingly, one aspect of the invention pertains to isolated nucleic acid molecules (e.g., cDNAs, DNAs, or RNAs) comprising a nucleotide sequence encoding an HA protein or biologically active portions thereof, as well as nucleic acid fragments suitable as primers or hybridization probes for the detection or amplification of HA-encoding nucleic acids (e.g., DNA or mRNA). In particularly preferred embodiments, the isolated nucleic acid molecule comprises one of the nucleotide sequences set forth in Appendix A or the coding region or a complement thereof of one of these nucleotide sequences. In other particularly preferred embodiments, the isolated nucleic acid molecule of the invention comprises a nucleotide sequence which hybridizes to or is at least about 50%, preferably at least about 60%, more preferably at least about 70%, 80% or 90%, and even more preferably at least about 95%, 96%, 97%, 98%, 99% or more homologous to a nucleotide sequence set forth in Appendix A, or a portion thereof. In other preferred embodiments, the isolated nucleic acid molecule encodes one of the amino acid sequences set forth in Appendix B. The preferred HA proteins of the present invention also preferably possess at least one of the HA activities described herein.  
      In another embodiment, the isolated nucleic acid molecule encodes a protein or portion thereof wherein the protein or portion thereof includes an amino acid sequence which is sufficiently homologous to an amino acid sequence of Appendix B, e.g., sufficiently homologous to an amino acid sequence of Appendix B such that the protein or portion thereof maintains an HA activity. Preferably, the protein or portion thereof encoded by the nucleic acid molecule maintains the ability to participate in the maintenance of homeostasis in  C. glutamicum , or to perform a function involved in the adaptation of this microorganism to different environmental conditions. In one embodiment, the protein encoded by the nucleic acid molecule is at least about 50%, preferably at least about 60%, and more preferably at least about 70%, 80%, or 90% and most preferably at least about 95%, 96%, 97%, 98%, or 99% or more homologous to an amino acid sequence of Appendix B (e.g., an entire amino acid sequence selected from those sequences set forth in Appendix B). In another preferred embodiment, the protein is a full length  C. glutamicum  protein which is substantially homologous to an entire amino acid sequence of Appendix B (encoded by an open reading frame shown in Appendix A).  
      In another preferred embodiment, the isolated nucleic acid molecule is derived from  C. glutamicum  and encodes a protein (e.g., an HA fusion protein) which includes a biologically active domain which is at least about 50% or more homologous to one of the amino acid sequences of Appendix B and is able to participate in the repair or recombination of DNA, in the transposition of genetic material, in gene expression (i.e., the processes of transcription or translation), in protein folding, or in protein secretion in  Corynebacterium glutamicum , or has one or more of the activities set forth in Table 1, and which also includes heterologous nucleic acid sequences encoding a heterologous polypeptide or regulatory regions.  
      In another embodiment, the isolated nucleic acid molecule is at least 15 nucleotides in length and hybridizes under stringent conditions to a nucleic acid molecule comprising a nucleotide sequence of Appendix A. Preferably, the isolated nucleic acid molecule corresponds to a naturally-occurring nucleic acid molecule. More preferably, the isolated nucleic acid encodes a naturally-occurring  C. glutamicum  HA protein, or a biologically active portion thereof.  
      Another aspect of the invention pertains to vectors, e.g., recombinant expression vectors, containing the nucleic acid molecules of the invention, and host cells into which such vectors have been introduced. In one embodiment, such a host cell is used to produce an HA protein by culturing the host cell in a suitable medium. The HA protein can be then isolated from the medium or the host cell.  
      Yet another aspect of the invention pertains to a genetically altered microorganism in which an HA gene has been introduced or altered. In one embodiment, the genome of the microorganism has been altered by introduction of a nucleic acid molecule of the invention encoding wild-type or mutated HA sequence as a transgene. In another embodiment, an endogenous HA gene within the genome of the microorganism has been altered, e.g., functionally disrupted, by homologous recombination with an altered HA gene. In another embodiment, an endogenous or introduced HA gene in a microorganism has been altered by one or more point mutations, deletions, or inversions, but still encodes a functional HA protein. In still another embodiment, one or more of the regulatory regions (e.g., a promoter, repressor, or inducer) of an HA gene in a microorganism has been altered (e.g., by deletion, truncation, inversion, or point mutation) such that the expression of the HA gene is modulated. In a preferred embodiment, the microorganism belongs to the genus  Corynebacterium  or  Brevibacterium , with  Corynebacterium glutamicum  being particularly preferred. In a preferred embodiment, the microorganism is also utilized for the production of a desired compound, such as an amino acid, with lysine being particularly preferred.  
      In another aspect, the invention provides a method of identifying the presence or activity of  Cornyebacterium diphtheriae  in a subject. This method includes detection of one or more of the nucleic acid or amino acid sequences of the invention (e.g., the sequences set forth in Appendix A or Appendix B) in a subject, thereby detecting the presence or activity of  Corynebacterium diphtheriae  in the subject.  
      Still another aspect of the invention pertains to an isolated HA protein or a portion, e.g., a biologically active portion, thereof. In a preferred embodiment, the isolated HA protein or portion thereof can participate in the maintenance of homeostasis in  C. glutamicum , or can perform a function involved in the adaptation of this microorganism to different environmental conditions. In another preferred embodiment, the isolated HA protein or portion thereof is sufficiently homologous to an amino acid sequence of Appendix B such that the protein or portion thereof maintains the ability to participate in the maintenance of homeostasis in  C. glutamicum , or to perform a function involved in the adaptation of this microorganism to different environmental conditions.  
      The invention also provides an isolated preparation of an HA protein. In preferred embodiments, the HA protein comprises an amino acid sequence of Appendix B. In another preferred embodiment, the invention pertains to an isolated full length protein which is substantially homologous to an entire amino acid sequence of Appendix B (encoded by an open reading frame set forth in Appendix A). In yet another embodiment, the protein is at least about 50%, preferably at least about 60%, and more preferably at least about 70%, 80%, or 90%, and most preferably at least about 95%, 96%, 97%, 98%, or 99% or more homologous to an entire amino acid sequence of Appendix B. In other embodiments, the isolated HA protein comprises an amino acid sequence which is at least about 50% or more homologous to one of the amino acid sequences of Appendix B and is able to participate in the maintenance of homeostasis in  C. glutamicum , or to perform a function involved in the adaptation of this microorganism to different environmental conditions, or has one or more of the activities set forth in Table 1.  
      Alternatively, the isolated HA protein can comprise an amino acid sequence which is encoded by a nucleotide sequence which hybridizes, e.g., hybridizes under stringent conditions, or is at least about 50%, preferably at least about 60%, more preferably at least about 70%, 80%, or 90%, and even more preferably at least about 95%, 96%, 97%, 98,%, or 99% or more homologous, to a nucleotide sequence of Appendix B. It is also preferred that the preferred forms of HA proteins also have one or more of the HA bioactivities described herein.  
      The HA polypeptide, or a biologically active portion thereof, can be operatively linked to a non-HA polypeptide to form a fusion protein. In preferred embodiments, this fusion protein has an activity which differs from that of the HA protein alone. In other preferred embodiments, this fusion protein participates in the maintenance of homeostasis in  C. glutamicum , or performs a function involved in the adaptation of this microorganism to different environmental conditions. In particularly preferred embodiments, integration of this fusion protein into a host cell modulates production of a desired compound from the cell.  
      In another aspect, the invention provides methods for screening molecules which modulate the activity of an HA protein, either by interacting with the protein itself or a substrate or binding partner of the HA protein, or by modulating the transcription or translation of an HA nucleic acid molecule of the invention.  
      Another aspect of the invention pertains to a method for producing a fine chemical. This method involves the culturing of a cell containing a vector directing the expression of an HA nucleic acid molecule of the invention, such that a fine chemical is produced. In a preferred embodiment, this method further includes the step of obtaining a cell containing such a vector, in which a cell is transfected with a vector directing the expression of an HA nucleic acid. In another preferred embodiment, this method further includes the step of recovering the fine chemical from the culture. In a particularly preferred embodiment, the cell is from the genus  Corynebacterium  or  Brevibacterium , or is selected from those strains set forth in Table 3.  
      Another aspect of the invention pertains to methods for modulating production of a molecule from a microorganism. Such methods include contacting the cell with an agent which modulates HA protein activity or HA nucleic acid expression such that a cell associated activity is altered relative to this same activity in the absence of the agent. In a preferred embodiment, the cell is modulated for one or more  C. glutamicum  processes involved in cell wall biosynthesis or rearrangements, metabolism of inorganic compounds, modification or degradation of aromatic or aliphatic compounds, or enzymatic or proteolytic activities. The agent which modulates HA protein activity can be an agent which stimulates HA protein activity or HA nucleic acid expression. Examples of agents which stimulate HA protein activity or HA nucleic acid expression include small molecules, active HA proteins, and nucleic acids encoding HA proteins that have been introduced into the cell. Examples of agents which inhibit HA activity or expression include small molecules and antisense HA nucleic acid molecules.  
      Another aspect of the invention pertains to methods for modulating yields of a desired compound from a cell, involving the introduction of a wild-type or mutant HA gene into a cell, either maintained on a separate plasmid or integrated into the genome of the host cell. If integrated into the genome, such integration can be random, or it can take place by homologous recombination such that the native gene is replaced by the introduced copy, causing the production of the desired compound from the cell to be modulated. In a preferred embodiment, said yields are increased. In another preferred embodiment, said chemical is a fine chemical. In a particularly preferred embodiment, said fine chemical is an amino acid. In especially preferred embodiments, said amino acid is L-lysine. 
    
    
     DETAILED DESCRIPTION OF THE INVENTION  
      The present invention provides HA nucleic acid and protein molecules which are involved in  C. glutamicum  cell wall biosynthesis or rearrangements, metabolism of inorganic compounds, modification or degradation of aromatic or aliphatic compounds, or that have a  C. glutamicum  enzymatic or proteolytic activity. The molecules of the invention may be utilized in the modulation of production of fine chemicals from microorganisms, such as  C. glutamicum , either directly (e.g., where overexpression or optimization of activity of a protein involved in the production of a fine chemical (e.g., an enzyme) has a direct impact on the yield, production, and/or efficiency of production of a fine chemical from the modified  C. glutamicum ), or an indirect impact which nonetheless results in an increase of yield, production, and/or efficiency of production of the desired compound (e.g., where modulation of the activity or number of copies of a  C. glutamicum  aromatic or aliphatic modification or degradation protein results in an increase in the viability of  C. glutamicum  cells, which in turn permits increased production in a large-scale culture setting). Aspects of the invention are further explicated below.  
      I. Fine Chemicals  
      The term ‘fine chemical’ is art-recognized and includes molecules produced by an organism which have applications in various industries, such as, but not limited to, the pharmaceutical, agriculture, and cosmetics industries. Such compounds include organic acids, such as tartaric acid, itaconic acid, and diaminopimelic acid, both proteinogenic and non-proteinogenic amino acids, purine and pyrimidine bases, nucleosides, and nucleotides (as described e.g. in Kuninaka, A. (1996) Nucleotides and related compounds, p. 561-612, in Biotechnology vol. 6, Rehm et al., eds. VCH: Weinheim, and references contained therein), lipids, both saturated and unsaturated fatty acids (e.g., arachidonic acid), diols (e.g., propane diol, and butane diol), carbohydrates (e.g., hyaluronic acid and trehalose), aromatic compounds (e.g., aromatic amines, vanillin, and indigo), vitamins and cofactors (as described in Ullmann&#39;s Encyclopedia of Industrial Chemistry, vol. A27, “Vitamins”, p. 443-613 (1996) VCH: Weinheim and references therein; and Ong, A. S., Niki, E. &amp; Packer, L. (1995) “Nutrition, Lipids, Health, and Disease” Proceedings of the UNESCO/Confederation of Scientific and Technological Associations in Malaysia, and the Society for Free Radical Research—Asia, held Sep. 1-3, 1994 at Penang, Malaysia, AOCS Press, (1995)), enzymes, polyketides (Cane et al. (1998)  Science  282: 63-68), and all other chemicals described in Gutcho (1983) Chemicals by Fermentation, Noyes Data Corporation, ISBN: 0818805086 and references therein. The metabolism and uses of certain of these fine chemicals are further explicated below.  
      A. Amino Acid Metabolism and Uses  
      Amino acids comprise the basic structural units of all proteins, and as such are essential for normal cellular functioning in all organisms. The term “amino acid” is art-recognized. The proteinogenic amino acids, of which there are 20 species, serve as structural units for proteins, in which they are linked by peptide bonds, while the nonproteinogenic amino acids (hundreds of which are known) are not normally found in proteins (see Ulmann&#39;s Encyclopedia of Industrial Chemistry, vol. A2, p. 57-97 VCH: Weinheim (1985)). Amino acids may be in the D- or L-optical configuration, though L-amino acids are generally the only type found in naturally-occurring proteins. Biosynthetic and degradative pathways of each of the 20 proteinogenic amino acids have been well characterized in both prokaryotic and eukaryotic cells (see, for example, Stryer, L. Biochemistry, 3 rd  edition, pages 578-590 (1988)). The ‘essential’ amino acids (histidine, isoleucine, leucine, lysine, methionine, phenylalanine, threonine, tryptophan, and valine), so named because they are generally a nutritional requirement due to the complexity of their biosyntheses, are readily converted by simple biosynthetic pathways to the remaining 11 ‘nonessential’ amino acids (alanine, arginine, asparagine, aspartate, cysteine, glutamate, glutamine, glycine, proline, serine, and tyrosine). Higher animals do retain the ability to synthesize some of these amino acids, but the essential amino acids must be supplied from the diet in order for normal protein synthesis to occur.  
      Aside from their function in protein biosynthesis, these amino acids are interesting chemicals in their own right, and many have been found to have various applications in the food, feed, chemical, cosmetics, agriculture, and pharmaceutical industries. Lysine is an important amino acid in the nutrition not only of humans, but also of monogastric animals such as poultry and swine. Glutamate is most commonly used as a flavor additive (mono-sodium glutamate, MSG) and is widely used throughout the food industry, as are aspartate, phenylalanine, glycine, and cysteine. Glycine, L-methionine and tryptophan are all utilized in the pharmaceutical industry. Glutamine, valine, leucine, isoleucine, histidine, arginine, proline, serine and alanine are of use in both the pharmaceutical and cosmetics industries. Threonine, tryptophan, and D/L-methionine are common feed additives. (Leuchtenberger, W. (1996) Amino aids—technical production and use, p. 466-502 in Rehm et al. (eds.) Biotechnology vol. 6, chapter 14a, VCH: Weinheim). Additionally, these amino acids have been found to be useful as precursors for the synthesis of synthetic amino acids and proteins, such as N-acetylcysteine, S-carboxymethyl-L-cysteine, (S)-5-hydroxytryptophan, and others described in Ulmann&#39;s Encyclopedia of Industrial Chemistry, vol. A2, p. 57-97, VCH: Weinheim, 1985.  
      The biosynthesis of these natural amino acids in organisms capable of producing them, such as bacteria, has been well characterized (for review of bacterial amino acid biosynthesis and regulation thereof, see Umbarger, H. E. (1978)  Ann. Rev. Biochem.  47: 533-606). Glutamate is synthesized by the reductive amination of α-ketoglutarate, an intermediate in the citric acid cycle. Glutamine, proline, and arginine are each subsequently produced from glutamate. The biosynthesis of serine is a three-step process beginning with 3-phosphoglycerate (an intermediate in glycolysis), and resulting in this amino acid after oxidation, transamination, and hydrolysis steps. Both cysteine and glycine are produced from serine; the former by the condensation of homocysteine with serine, and the latter by the transferal of the side-chain β-carbon atom to tetrahydrofolate, in a reaction catalyzed by serine transhydroxymethylase. Phenylalanine, and tyrosine are synthesized from the glycolytic and pentose phosphate pathway precursors erythrose 4-phosphate and phosphoenolpyruvate in a 9-step biosynthetic pathway that differ only at the final two steps after synthesis of prephenate. Tryptophan is also produced from these two initial molecules, but its synthesis is an 11-step pathway. Tyrosine may also be synthesized from phenylalanine, in a reaction catalyzed by phenylalanine hydroxylase. Alanine, valine, and leucine are all biosynthetic products of pyruvate, the final product of glycolysis. Aspartate is formed from oxaloacetate, an intermediate of the citric acid cycle. Asparagine, methionine, threonine, and lysine are each produced by the conversion of aspartate. Isoleucine is formed from threonine. A complex 9-step pathway results in the production of histidine from 5-phosphoribosyl-1-pyrophosphate, an activated sugar.  
      Amino acids in excess of the protein synthesis needs of the cell cannot be stored, and are instead degraded to provide intermediates for the major metabolic pathways of the cell (for review see Stryer, L. Biochemistry 3 rd  ed. Ch. 21 “Amino Acid Degradation and the Urea Cycle” p. 495-516 (1988)). Although the cell is able to convert unwanted amino acids into useful metabolic intermediates, amino acid production is costly in terms of energy, precursor molecules, and the enzymes necessary to synthesize them. Thus it is not surprising that amino acid biosynthesis is regulated by feedback inhibition, in which the presence of a particular amino acid serves to slow or entirely stop its own production (for overview of feedback mechanisms in amino acid biosynthetic pathways, see Stryer, L. Biochemistry, 3 rd  ed. Ch. 24: “Biosynthesis of Amino Acids and Heme” p. 575-600 (1988)). Thus, the output of any particular amino acid is limited by the amount of that amino acid present in the cell.  
      B. Vitamin, Cofactor, and Nutraceutical Metabolism and Uses  
      Vitamins, cofactors, and nutraceuticals comprise another group of molecules which the higher animals have lost the ability to synthesize and so must ingest, although they are readily synthesized by other organisms such as bacteria. These molecules are either bioactive substances themselves, or are precursors of biologically active substances which may serve as electron carriers or intermediates in a variety of metabolic pathways. Aside from their nutritive value, these compounds also have significant industrial value as coloring agents, antioxidants, and catalysts or other processing aids. (For an overview of the structure, activity, and industrial applications of these compounds, see, for example, Ullman&#39;s Encyclopedia of Industrial Chemistry, “Vitamins” vol. A27, p. 443-613, VCH: Weinheim, 1996.) The term “vitamin” is art-recognized, and includes nutrients which are required by an organism for normal functioning, but which that organism cannot synthesize by itself. The group of vitamins may encompass cofactors and nutraceutical compounds. The language “cofactor” includes nonproteinaceous compounds required for a normal enzymatic activity to occur. Such compounds may be organic or inorganic; the cofactor molecules of the invention are preferably organic. The term “nutraceutical” includes dietary supplements having health benefits in plants and animals, particularly humans. Examples of such molecules are vitamins, antioxidants, and also certain lipids (e.g., polyunsaturated fatty acids).  
      The biosynthesis of these molecules in organisms capable of producing them, such as bacteria, has been largely characterized (Ullman&#39;s Encyclopedia of Industrial Chemistry, “Vitamins” vol. A27, p. 443-613, VCH: Weinheim, 1996; Michal, G. (1999) Biochemical Pathways: An Atlas of Biochemistry and Molecular Biology, John Wiley &amp; Sons; Ong, A. S., Niki, E. &amp; Packer, L. (1995) “Nutrition, Lipids, Health, and Disease” Proceedings of the UNESCO/Confederation of Scientific and Technological Associations in Malaysia, and the Society for Free Radical Research—Asia, held Sep. 1-3, 1994 at Penang, Malaysia, AOCS Press: Champaign, Ill. X, 374 S).  
      Thiamin (vitamin B 1 ) is produced by the chemical coupling of pyrimidine and thiazole moieties. Riboflavin (vitamin B 2 ) is synthesized from guanosine-5′-triphosphate (GTP) and ribose-5′-phosphate. Riboflavin, in turn, is utilized for the synthesis of flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD). The family of compounds collectively termed ‘vitamin B 6 ’ (e.g., pyridoxine, pyridoxamine, pyridoxa-5′-phosphate, and the commercially used pyridoxin hydrochloride) are all derivatives of the common structural unit, 5-hydroxy-6-methylpyridine. Pantothenate (pantothenic acid, (R)-(+)-N-(2,4-dihydroxy-3,3-dimethyl-1-oxobutyl)-β-alanine) can be produced either by chemical synthesis or by fermentation. The final steps in pantothenate) biosynthesis consist of the ATP-driven condensation of β-alanine and pantoic acid. The enzymes responsible for the biosynthesis steps for the conversion to pantoic acid, to β-alanine and for the condensation to panthotenic acid are known. The metabolically active form of pantothenate is Coenzyme A, for which the biosynthesis proceeds in 5 enzymatic steps. Pantothenate, pyridoxal-5′-phosphate, cysteine and ATP are the precursors of Coenzyme A. These enzymes not only catalyze the formation of panthothante, but also the production of (R)-pantoic acid, (R)-pantolacton, (R)-panthenol (provitamin B 5 ), pantetheine (and its derivatives) and coenzyme A.  
      Biotin biosynthesis from the precursor molecule pimeloyl-CoA in microorganisms has been studied in detail and several of the genes involved have been identified. Many of the corresponding proteins have been found to also be involved in Fe-cluster synthesis and are members of the nifS class of proteins. Lipoic acid is derived from octanoic acid, and serves as a coenzyme in energy metabolism, where it becomes part of the pyruvate dehydrogenase complex and the α-ketoglutarate dehydrogenase complex. The folates are a group of substances which are all derivatives of folic acid, which is turn is derived from L-glutamic acid, p-amino-benzoic acid and 6-methylpterin. The biosynthesis of folic acid and its derivatives, starting from the metabolism intermediates guanosine-5′-triphosphate (GTP), L-glutamic acid and p-amino-benzoic acid has been studied in detail in certain microorganisms.  
      Corrinoids (such as the cobalamines and particularly vitamin B 12 ) and porphyrines belong to a group of chemicals characterized by a tetrapyrole ring system. The biosynthesis of vitamin B 12  is sufficiently complex that it has not yet been completely characterized, but many of the enzymes and substrates involved are now known. Nicotinic acid (nicotinate), and nicotinamide are pyridine derivatives which are also termed ‘niacin’. Niacin is the precursor of the important coenzymes NAD (nicotinamide adenine dinucleotide) and NADP (nicotinamide adenine dinucleotide phosphate) and their reduced forms.  
      The large-scale production of these compounds has largely relied on cell-free chemical syntheses, though some of these chemicals have also been produced by large-scale culture of microorganisms, such as riboflavin, Vitamin B 6 , pantothenate, and biotin. Only Vitamin B 12  is produced solely by fermentation, due to the complexity of its synthesis. In vitro methodologies require significant inputs of materials and time, often at great cost.  
      C. Purine, Pyrimidine, Nucleoside and Nucleotide Metabolism and Uses  
      Purine and pyrimidine metabolism genes and their corresponding proteins are important targets for the therapy of tumor diseases and viral infections. The language “purine” or “pyrimidine” includes the nitrogenous bases which are constituents of nucleic acids, co-enzymes, and nucleotides. The term “nucleotide” includes the basic structural units of nucleic acid molecules, which are comprised of a nitrogenous base, a pentose sugar (in the case of RNA, the sugar is ribose; in the case of DNA, the sugar is D-deoxyribose), and phosphoric acid. The language “nucleoside” includes molecules which serve as precursors to nucleotides, but which are lacking the phosphoric acid moiety that nucleotides possess. By inhibiting the biosynthesis of these molecules, or their mobilization to form nucleic acid molecules, it is possible to inhibit RNA and DNA synthesis; by inhibiting this activity in a fashion targeted to cancerous cells, the ability of tumor cells to divide and replicate may be inhibited. Additionally, there are nucleotides which do not form nucleic acid molecules, but rather serve as energy stores (i.e., AMP) or as coenzymes (i.e., FAD and NAD).  
      Several publications have described the use of these chemicals for these medical indications, by influencing purine and/or pyrimidine metabolism (e.g. Christopherson, R. I. and Lyons, S. D. (1990) “Potent inhibitors of de novo pyrimidine and purine biosynthesis as chemotherapeutic agents.”  Med. Res. Reviews  10: 505-548). Studies of enzymes involved in purine and pyrimidine metabolism have been focused on the development of new drugs which can be used, for example, as immunosuppressants or anti-proliferants (Smith, J. L., (1995) “Enzymes in nucleotide synthesis.”  Curr. Opin. Struct. Biol.  5: 752-757; (1995)  Biochem Soc. Transact.  23: 877-902). However, purine and pyrimidine bases, nucleosides and nucleotides have other utilities: as intermediates in the biosynthesis of several fine chemicals (e.g., thiamine, S-adenosyl-methionine, folates, or riboflavin), as energy carriers for the cell (e.g., ATP or GTP), and for chemicals themselves, commonly used as flavor enhancers (e.g., IMP or GMP) or for several medicinal applications (see, for example, Kuninaka, A. (1996) Nucleotides and Related Compounds in Biotechnology vol. 6, Rehm et al., eds. VCH: Weinheim, p. 561-612). Also, enzymes involved in purine, pyrimidine, nucleoside, or nucleotide metabolism are increasingly serving as targets against which chemicals for crop protection, including fungicides, herbicides and insecticides, are developed.  
      The metabolism of these compounds in bacteria has been characterized (for reviews see, for example, Zalkin, H. and Dixon, J. E. (1992) “de novo purine nucleotide biosynthesis”, in: Progress in Nucleic Acid Research and Molecular Biology, vol. 42, Academic Press: p. 259-287; and Michal, G. (1999) “Nucleotides and Nucleosides”, Chapter 8 in: Biochemical Pathways: An Atlas of Biochemistry and Molecular Biology, Wiley: New York). Purine metabolism has been the subject of intensive research, and is essential to the normal functioning of the cell. Impaired purine metabolism in higher animals can cause severe disease, such as gout. Purine nucleotides are synthesized from ribose-5-phosphate, in a series of steps through the intermediate compound inosine-5′-phosphate (IMP), resulting in the production of guanosine-5′-monophosphate (GMP) or adenosine-5′-monophosphate (AMP), from which the triphosphate forms utilized as nucleotides are readily formed. These compounds are also utilized as energy stores, so their degradation provides energy for many different biochemical processes in the cell. Pyrimidine biosynthesis proceeds by the formation of uridine-5′-monophosphate (UMP) from ribose-5-phosphate. UMP, in turn, is converted to cytidine-5′-triphosphate (CTP). The deoxy-forms of all of these nucleotides are produced in a one step reduction reaction from the diphosphate ribose form of the nucleotide to the diphosphate deoxyribose form of the nucleotide. Upon phosphorylation, these molecules are able to participate in DNA synthesis.  
      D. Trehalose Metabolism and Uses  
      Trehalose consists of two glucose molecules, bound in α,α-1,1 linkage. It is commonly used in the food industry as a sweetener, an additive for dried or frozen foods, and in beverages. However, it also has applications in the pharmaceutical, cosmetics and biotechnology industries (see, for example, Nishimoto et al., (1998) U.S. Pat. No. 5,759,610; Singer, M. A. and Lindquist, S. (1998)  Trends Biotech.  16: 460-467; Paiva, C. L. A. and Panek, A. D. (1996)  Biotech. Ann. Rev.  2: 293-314; and Shiosaka, M. (1997) J. Japan 172: 97-102). Trehalose is produced by enzymes from many microorganisms and is naturally released into the surrounding medium, from which it can be collected using methods known in the art.  
      II. Maintenance of Homeostasis in  C. glutamicum  and Environmental Adaptation  
      The metabolic and other biochemical processes by which cells function are sensitive to environmental conditions such as temperature, pressure, solute concentration, and availability of oxygen. When one or more such environmental condition is perturbed or altered in a fashion that is incompatible with the normal functioning of these cellular processes, the cell must act to maintain an intracellular environment which will permit them to occur despite the hostile extracellular environment. Gram positive bacterial cells, such as  C. glutamicum  cells, have a number of mechanisms by which internal homeostasis may be maintained despite unfavorable extracellular conditions. These include a cell wall, proteins which are able to degrade possibly toxic aromatic and aliphatic compounds, mechanisms of proteolysis whereby misfolded or misregulated proteins may be rapidly destroyed, and catalysts which permit intracellular reactions to occur which would not normally take place under the conditions optimal for bacterial growth.  
      Aside from merely surviving in a hostile environment, bacterial cells (e.g.  C. glutamicum  cells) are also frequently able to adapt such that they are able to take advantage of such conditions. For example, cells in an environment lacking desired carbon sources may be able to adapt to growth on a less-suitable carbon source. Also, cells may be able to utilize less desirable inorganic compounds when the commonly utilized ones are unavailable.  C. glutamicum  cells possess a number of genes which permit them to adapt to utilize inorganic and organic molecules which they would normally not encounter under optimal growth conditions as nutrients and precursors for metabolism. Aspects of cellular processes involved in homeostasis and adaptation are further explicated below.  
      A. Modification and Degradation of Aromatic and Aliphatic Compounds  
      Bacterial cells are routinely exposed to a variety of aromatic and aliphatic compounds in nature. Aromatic compounds are organic molecules having a cyclic ring structure, while aliphatic compounds are organic molecules having open chain structures rather than ring structures. Such compounds may arise as by-products of industrial processes (e.g., benzene or toluene), but may also be produced by certain microorganisms (e.g., alcohols). Many of these compounds are toxic to cells, particularly the aromatic compounds, which are highly reactive due to the high-energy ring structure. Thus, certain bacteria have developed mechanisms by which they are able to modify or degrade these compounds such that they are no longer hazardous to the cell. Cells may possess enzymes that are able to, for example, hydroxylate, isomerize, or methylate aromatic or aliphatic compounds such that they are either rendered less toxic, or such that the modified form is able to be processed by standard cellular waste and degradation pathways. Also, cells may possess enzymes which are able to specifically degrade one or more such potentially hazardous substance, thereby protecting the cell. Principles and examples of these types of modification and degradation processes in bacteria are described in several publications, e.g., Sahm, H. (1999) “Procaryotes in Industrial Production” in Lengeler, J. W. et al., eds. Biology of the Procaryotes, Thieme Verlag: Stuttgart; and Schlegel, H. G. (1992) Allgemeine Mikrobiologie, Thieme: Stuttgart).  
      Aside from simply inactivating hazardous aromatic or aliphatic compounds, many bacteria have evolved to be able to utilize these compounds as carbon sources for continued metabolism when the preferred carbon sources of the cell are not available. For example,  Pseudomonas  strains able to utilize toluene, benzene, and 1,10-dichlorodecane as carbon sources are known (Chang, B. V. et al. (1997)  Chemosphere  35(12): 2807-2815; Wischnak, C. et al. (1998)  Appl. Environ. Microbiol.  64(9): 3507-3511; Churchill, S. A. et al. (1999)  Appl. Environ. Microbiol.  65(2): 549-552). There are similar examples from many other bacterial species which are known in the art.  
      The ability of certain bacteria to modify or degrade aromatic and aliphatic compounds has begun to be exploited. Petroleum is a complex mixture of chemicals which includes aliphatic molecules and aromatic compounds. By applying bacteria having the ability to degrade or modify these toxic compounds to an oil spill, for example, it is possible to eliminate much of the environmental damage with high efficiency and low cost (see, for example, Smith, M. R. (1990) “The biodegradation of aromatic hydrocarbons by bacteria”  Biodegradation  1(2-3): 191-206; and Suyama, T. et al. (1998) “Bacterial isolates degrading aliphatic polycarbonates,”  FEMS Microbiol. Lett.  161(2): 255-261).  
      B. Metabolism of Inorganic Compounds  
      Cells (e.g., bacterial cells) contain large quantities of different molecules, such as water, inorganic ions, and organic substances (e.g., proteins, sugars, and other macromolecules). The bulk of the mass of a typical cell consists of only 4 types of atoms: carbon, oxygen, hydrogen, and nitrogen. Although they represent a smaller percentage of the content of a cell, inorganic substances are equally as important to the proper functioning of the cell. Such molecules include phosphorous, sulfur, calcium, magnesium, iron, zinc, manganese, copper, molybdenum, tungsten, and cobalt. Many of these compounds are critical for the construction of important molecules, such as nucleotides (phosphorous) and amino acids (nitrogen and sulfur). Others of these inorganic ions serve as cofactors for enzymic reactions or contribute to osmotic pressure. All such molecules must be taken up by the bacterium from the surrounding environment.  
      For each of these inorganic compounds it is desirable for the bacterium to take up the form which can be most readily used by the standard metabolic machinery of the cell. However, the bacterium may encounter environments in which these preferred forms are not readily available. In order to survive under these circumstances, it is important for bacteria to have additional biochemical mechanisms which are able to convert less metabolically active but readily available forms of these inorganic compounds to ones which may be used in cellular metabolism. Bacteria frequently possess a number of genes encoding enzymes for this purpose, which are not expressed unless the desired inorganic species are not available. Thus, these genes for the metabolism of various inorganic compounds serve as another tool which bacteria may use to adapt to suboptimal environmental conditions.  
      After carbon, the most important element in the cell is nitrogen. A typical bacterial cell contains between 12-15% nitrogen. It is a constituent of amino acids and nucleotides, as well as many other important molecules in the cell. Further, nitrogen may serve as a substitute for oxygen as a terminal electron acceptor in energy metabolism. Good sources of nitrogen include many organic and inorganic compounds, such ammonia gas or ammonia salts (e.g., NH 4 Cl, (NH 4 ) 2 SO 4 , or NH 4 OH), nitrates, urea, amino acids, or complex nitrogen sources like corn steep liquor, soy bean flour, soy bean protein, yeast extract, meat extract, etc. Ammonia nitrogen is fixed by the action of particular enzymes: glutamate dehydrogenase, glutamine synthase, and glutamine-2-oxoglutarate aminotransferase. The transfer of amino-nitrogen from one organic molecule to another is accomplished by the aminotransferases, a class of enzymes which transfer one amino group from an alpha-amino acid to an alpha-keto acid. Nitrate may be reduced via nitrate reductase, nitrite reductase, and further redox enzymes until it is converted to molecular nitrogen or ammonia, which may be readily utilized by the cell in standard metabolic pathways.  
      Phosphorous is typically found intracellularly in both organic and inorganic forms, and may be taken up by the cell in either of these forms as well, though most microorganisms preferentially take up inorganic phosphate. The conversion of organic phosphate to a form which the cell can utilize requires the action of phosphatases (e.g., phytases, which hydrolyze phyate-yielding phosphate and inositol derivatives). Phosphate is a key element in the synthesis of nucleic acids, and also has a significant role in cellular energy metabolism (e.g., in the synthesis of ATP, ADP, and AMP).  
      Sulfur is a requirement for the synthesis of amino acids (e.g., methionine and cysteine), vitamins (e.g., thiamine, biotin, and lipoic acid) and iron sulfur proteins. Bacteria obtain sulfur primarily from inorganic sulfate, though thiosulfate, sulfite, and sulfide are also commonly utilized. Under conditions where these compounds may not be readily available, many bacteria express genes which enable them to utilize sulfonate compounds such as 2-aminosulfonate (taurine) (Kertesz, M. A. (1993) “Proteins induced by sulfate limitation in  Escherichia coli, Pseudomonas putida , or  Staphylococcus aureus.” J. Bacteriol.  175: 1187-1190).  
      Other inorganic atoms, e.g., metal or calcium ions, are also critical for the viability of cells. Iron, for example, plays a key role in redox reactions and is a cofactor of iron-sulfur proteins, heme proteins, and cytochromes. The uptake of iron into bacterial cells may be accomplished by the action of siderophores, chelating agents which bind extracellular iron ions and translocate them to the interior of the cell. For reference on the metabolism of iron and other inorganic compounds, see: Lengeler et al. (1999) Biology of Prokaryotes, Thieme Verlag: Stuttgart; Neidhardt, F. C. et al., eds.  Escherichia coli  and  Salmonella . ASM Press: Washington, D.C.; Sonenshein, A. L. et al., eds. (199?)  Bacillus subtilis  and Other Gram-Positive Bacteria, ASM Press: Washington, D.C.; Voet, D. and Voet, J. G. (1992) Biochemie, VCH: Weinheim; Brock, T. D. and Madigan, M. T. (1991) Biology of Microorgansisms, 6 th  ed. Prentice Hall: Englewood Cliffs, p. 267-269; Rhodes, P. M. and Stanbury, P. F. Applied Microbial Physiology—A Practical Approach, Oxford Univ. Press: Oxford.  
      C. Enzymes and Proteolysis  
      The intracellular conditions for which bacteria such as  C. glutamicum  are optimized are frequently not conditions under which many biochemical reactions would normally take place. In order to make such reactions proceed under physiological conditions, cells utilize enzymes. Enzymes are proteinaceous biological catalysts, spatially orienting reacting molecules or providing a specialized environment such that the energy barrier to a biochemical reaction is lowered. Different enzymes catalyze different reactions, and each enzyme may be the subject of transcriptional, translational, or posttranslational regulation such that the reaction will only take place under appropriate conditions and at specified times. Enzymes may contribute to the degradation (e.g., the proteases), synthesis (e.g., the synthases), or modification (e.g., transferases or isomerases) of compounds, all of which enable the production of necessary compounds within the cell. This, in turn, contributes to the maintenance of cellular homeostasis.  
      However, the fact that enzymes are optimized for activity under the physiological conditions at which the bacterium is most viable means that when environmental conditions are perturbed, there is a significant possibility that enzyme activity will also be perturbed. For example, changes in temperature may result in aberrantly folded proteins, and the same is true for changes of pH—protein folding is largely dependent on electrostatic and hydrophobic interactions of amino acids within the polypeptide chain, so any alteration to the charges on individual amino acids (as might be brought about by a change in cellular pH) may have a profound effect on the ability of the protein to correctly fold. Changes in temperature effectively change the amount of kinetic energy that the polypeptide molecule possesses, which affects the ability of the polypeptide to settle into a correctly folded, energetically stable configuration. Misfolded proteins may be harmful to the cell for two reasons. First, the aberrantly folded protein may have a similarly aberrant activity, or no activity whatsoever. Second, misfolded proteins may lack the conformational regions necessary for proper regulation by other cellular systems and thus may continue to be active but in an uncontrolled fashion.  
      The cell has a mechanism by which misfolded enzymes and regulatory proteins may be rapidly destroyed before any damage occurs to the cell: proteolysis. Proteins such as those of the la/Ion family and those of the Clp family specifically recognize and degrade misfolded proteins (see, e.g., Sherman, M. Y., Goldberg, A. L. (1999)  EXS  77: 57-78 and references therein and Porankiewicz J. (1999)  Molec. Microbiol.  32(3): 449-58, and references therein; Neidhardt, F. C., et al. (1996)  E. coli  and  Salmonella , ASM Press: Washington, D.C. and references therein; and Pritchard, G. G., and Coolbear, T. (1993)  FEMS Microbiol. Rev.  12(1-3): 179-206 and references therein). These enzymes bind to misfolded or unfolded proteins and degrade them in an ATP-dependent manner. Proteolysis thus serves as an important mechanism employed by the cell to prevent damage to normal cellular functions upon environmental changes, and it further permits cells to survive under conditions and in environments which would otherwise be toxic due to misregulated and/or aberrant enzyme or regulatory activity.  
      Proteolysis also has important functions in the cell under optimal environmental conditions. Within normal metabolic processes, proteases aid in the hydrolysis of peptide bonds, in the catabolism of complex molecules to provide necessary degradation products, and in protein modification. Secreted proteases play an important role in the catabolism of external nutrients even prior to the entry of these compounds into the cell. Further, proteolytic activity itself may serve regulatory functions; sporulation in  B. subtilis  and cell cycle progression in  Caulobacter  spp. are known to be regulated by key proteolytic events in each of these species (Gottesman, S. (1999)  Curr. Opin. Microbiol.  2(2): 142-147). Thus, proteolytic processes are key for cellular survival under both suboptimal and optimal environmental conditions, and contribute to the overall maintenance of homeostasis in cells.  
      D. Cell Wall Production and Rearrangements  
      While the biochemical machinery of the cell may be able to readily adapt to different and possibly unfavorable environments, cells still require a general mechanism by which they may be protected from the environment. For many bacteria, the cell wall affords such protection, and also plays roles in adhesion, cell growth and division, and transport of desired solutes and waste materials.  
      In order to function, cells require intracellular concentrations of metabolites and other molecules that are substantially higher than those of the surrounding media. Since these metabolites are largely prevented from leaving the cell due to the presence of the hydrophobic membrane, the tendency of the system is for water molecules to enter the cell from the external medium such that the interior concentrations of solutes match the exterior concentrations. Water molecules are readily able to cross the cellular membrane, and this membrane is not able to withstand the resulting swelling and pressure, which may lead to osmotic lysis of the cell. The rigidity of the cell wall greatly improves the ability of the cell to tolerate these pressures, and offers a further barrier to the unwanted diffusion of these metabolites and desired solutes from the cell. Similarly, the cell wall also serves to prevent unwanted material from entering the cell.  
      The cell wall also participates in a number of other cellular processes, such as adhesion and cell growth and division. Due to the fact that the cell wall completely surrounds the cell, any interaction of the cell with its surroundings must be mediated by the cell wall. Thus, the cell wall must participate in any adherence of the cell to other cells and to desired surfaces. Further, the cell cannot grow or divide without concomitant changes in the cell wall. Since the protection that the wall affords requires its presence during growth, morphogenesis and multiplication, one of the key steps in cell division is cell wall synthesis within the cell such that a new cell divides from the old. Thus, frequently cell wall biosynthesis is regulated in tandem with cell growth and cell division (see, e.g., Sonenshein, A. L. et al, eds. (1993)  Bacillus subtilis  and Other Gram-Positive Bacteria, ASM: Washington, D.C.).  
      The structure of the cell wall varies between gram-positive and gram-negative bacteria. However, in both types, the fundamental structural unit of the wall remains similar: an overlapping lattice of two polysaccharides, N-acetyl glucosamine (NAG) and N-acetyl muramic acid (NAM) which are cross-linked by amino acids (most commonly L-alanine, D-glutamate, diaminopimelic acid, and D-alanine), termed ‘peptidoglycan’. The processes involved in the synthesis of the cell wall are known (see, e.g., Michal, G., ed. (1999) Biochemical Pathways: An Atlas of Biochemistry and Molecular Biology, Wiley: New York).  
      In gram-negative bacteria, the inner cellular membrane is coated by a single-layered peptidoglycan (approximately 10 nm thick), termed the murein-sacculus. This peptidoglycan structure is very rigid, and its structure determines the shape of the organism. The outer surface of the murein-sacculus is covered with an outer membrane, containing porins and other membrane proteins, phospholipids, and lipopolysaccharides. To maintain a tight association with the outer membrane, the gram-negative cell wall also has interspersed lipid molecules which serve to anchor it to the surrounding membrane.  
      In gram-positive bacteria, such as  Corynebacterium glutamicum , the cytoplasmic membrane is covered by a multi-layered peptidoglycan, which ranges from 20-80 nm in thickness (see, e.g., Lengeler et al. (1999) Biology of Prokaryotes Thieme Verlag: Stuttgart, p. 913-918, p. 875-899, and p. 88-109 and references therein). The gram-positive cell wall also contains teichoic acid, a polymer of glycerol or ribitol linked through phosphate groups. Teichoic acid is also able to associate with amino acids, and forms covalent bonds with muramic acid. Also present in the cell wall may be lipoteichoic acids and teichuronic acids. If present, cellular surface structures such as flagella or capsules will be anchored in this layer as well.  
      III. Elements and Methods of the Invention  
      The present invention is based, at least in part, on the discovery of novel molecules, referred to herein as HA nucleic acid and protein molecules, which participate in the maintenance of homeostasis in  C. glutamicum , or which perform a function involved in the adaptation of this microorganism to different environmental conditions. In one embodiment, the HA molecules participate in  C. glutamicum  cell wall biosynthesis or rearrangements, in the metabolism of inorganic compounds, in the modification or degradation of aromatic or aliphatic compounds, or have an enzymatic or proteolytic activity. In a preferred embodiment, the activity of the HA molecules of the present invention with regard to  C. glutamicum  cell wall biosynthesis or rearrangements, metabolism of inorganic compounds, modification or degradation of aromatic or aliphatic compounds, or enzymatic or proteolytic activity has an impact on the production of a desired fine chemical by this organism. In a particularly preferred embodiment, the HA molecules of the invention are modulated in activity, such that the  C. glutamicum  cellular processes in which the HA molecules participate (e.g.,  C. glutamicum  cell wall biosynthesis or rearrangements, metabolism of inorganic compounds, modification or degradation of aromatic or aliphatic compounds, or enzymatic or proteolytic activity) are also altered in activity, resulting either directly or indirectly in a modulation of the yield, production, and/or efficiency of production of a desired fine chemical by  C. glutamicum.    
      The language, “HA protein” or “HA polypeptide” includes proteins which participate in a number of cellular processes related to  C. glutamicum  homeostasis or the ability of  C. glutamicum  cells to adapt to unfavorable environmental conditions. For example, an HA protein may be involved in  C. glutamicum  cell wall biosynthesis or rearrangements, in the metabolism of inorganic compounds in  C. glutamicum , in the modification or degradation of aromatic or aliphatic compounds in  C. glutamicum , or have a  C. glutamicum  enzymatic or proteolytic activity. Examples of HA proteins include those encoded by the HA genes set forth in Table 1 and Appendix A. The terms “HA gene” or “HA nucleic acid sequence” include nucleic acid sequences encoding an HA protein, which consist of a coding region and also corresponding untranslated 5′ and 3′ sequence regions. Examples of HA genes include those set forth in Table 1. The terms “production” or “productivity” are art-recognized and include the concentration of the fermentation product (for example, the desired fine chemical) formed within a given time and a given fermentation volume (e.g., kg product per hour per liter). The term “efficiency of production” includes the time required for a particular level of production to be achieved (for example, how long it takes for the cell to attain a particular rate of output of a fine chemical). The term “yield” or “product/carbon yield” is art-recognized and includes the efficiency of the conversion of the carbon source into the product (i.e., fine chemical). This is generally written as, for example, kg product per kg carbon source. By increasing the yield or production of the compound, the quantity of recovered molecules, or of useful recovered molecules of that compound in a given amount of culture over a given amount of time is increased. The terms “biosynthesis” or a “biosynthetic pathway” are art-recognized and include the synthesis of a compound, preferably an organic compound, by a cell from intermediate compounds in what may be a multistep and highly regulated process. The terms “degradation” or a “degradation pathway” are art-recognized and include the breakdown of a compound, preferably an organic compound, by a cell to degradation products (generally speaking, smaller or less complex molecules) in what may be a multistep and highly regulated process. The language “metabolism” is art-recognized and includes the totality of the biochemical reactions that take place in an organism. The metabolism of a particular compound, then, (e.g., the metabolism of an amino acid such as glycine) comprises the overall biosynthetic, modification, and degradation pathways in the cell related to this compound. The term “homeostasis” is art-recognized and includes all of the mechanisms utilized by a cell to maintain a constant intracellular environment despite the prevailing extracellular environmental conditions. A non-limiting example of such processes is the utilization of a cell wall to prevent osmotic lysis due to high intracellular solute concentrations. The term “adaptation” or “adaptation to an environmental condition” is art-recognized and includes mechanisms utilized by the cell to render the cell able to survive under nonpreferred environmental conditions (generally speaking, those environmental conditions in which one or more favored nutrients are absent, or in which an environmental condition such as temperature, pH, osmolarity, oxygen percentage and the like fall outside of the optimal survival range of the cell). Many cells, including  C. glutamicum  cells, possess genes encoding proteins which are expressed under such environmental conditions and which permit continued growth in such suboptimal conditions.  
      In another embodiment, the HA molecules of the invention are capable of modulating the production of a desired molecule, such as a fine chemical, in a microorganism such as  C. glutamicum . There are a number of mechanisms by which the alteration of an HA protein of the invention may directly affect the yield, production, and/or efficiency of production of a fine chemical from a  C. glutamicum  strain incorporating such an altered protein. For example, by engineering enzymes which modify or degrade aromatic or aliphatic compounds such that these enzymes are increased or decreased in activity or number, it may be possible to modulate the production of one or more fine chemicals which are the modification or degradation products of these compounds. Similarly, enzymes involved in the metabolism of inorganic compounds provide key molecules (e.g. phosphorous, sulfur, and nitrogen molecules) for the biosynthesis of such fine chemicals as amino acids, vitamins, and nucleic acids. By altering the activity or number of these enzymes in  C. glutamicum , it may be possible to increase the conversion of these inorganic compounds (or to use alternate inorganic compounds) to thus permit improved rates of incorporation of inorganic atoms into these fine chemicals. Genetic engineering of  C. glutamicum  enzymes involved in general cellular processes may also directly improve fine chemical production, since many of these enzymes directly modify fine chemicals (e.g., amino acids) or the enzymes which are involved in fine chemical synthesis or secretion. Modulation of the activity or number of cellular proteases may also have a direct effect on fine chemical production, since many proteases may degrade fine chemicals or enzymes involved in fine chemical production or breakdown.  
      Further, the aforementioned enzymes which participate in aromatic/aliphatic compound modification or degradation, general biocatalysis, inorganic compound metabolism or proteolysis are each themselves fine chemicals, desirable for their activity in various in vitro industrial applications. By altering the number of copies of the gene for one or more of these enzymes in  C. glutamicum  it may be possible to increase the number of these proteins produced by the cell, thereby increasing the potential yield or efficiency of production of these proteins from large-scale  C. glutamicum  or related bacterial cultures.  
      The alteration of an HA protein of the invention may also indirectly affect the yield, production, and/or efficiency of production of a fine chemical from a  C. glutamicum  strain incorporating such an altered protein. For example, by modulating the activity and/or number of those proteins involved in the construction or rearrangement of the cell wall, it may be possible to modify the structure of the cell wall itself such that the cell is able to better withstand the mechanical and other stresses present during large-scale fermentative culture. Also, large-scale growth of  C. glutamicum  requires significant cell wall production. Modulation of the activity or number of cell wall biosynthetic or degradative enzymes may allow more rapid rates of cell wall biosynthesis, which in turn may permit increased growth rates of this microorganism in culture and thereby increase the number of cells producing the desired fine chemical.  
      By modifying the HA enzymes of the invention, one may also indirectly impact the yield, production, or efficiency of production of one or more fine chemicals from  C. glutamicum . For example, many of the general enzymes in  C. glutamicum  may have a significant impact on global cellular processes (e.g., regulatory processes) which in turn have a significant effect on fine chemical metabolism. Similarly, proteases, enzymes which modify or degrade possibly toxic aromatic or aliphatic compounds, and enzymes which promote the metabolism of inorganic compounds all serve to increase the viability of  C. glutamicum . The proteases aid in the selective removal of misfolded or misregulated proteins, such as those that might occur under the relatively stressful environmental conditions encountered during large-scale fermentor culture. By altering these proteins, it may be possible to further enhance this activity and to improve the viability of  C. glutamicum  in culture. The aromatic/aliphatic modification or degradation proteins not only serve to detoxify these waste compounds (which may be encountered as impurities in culture medium or as waste products from cells themselves), but also to permit the cells to utilize alternate carbon sources if the optimal carbon source is limiting in the culture. By increasing their number and/or activity, the survival of  C. glutamicum  cells in culture may be enhanced. The inorganic metabolism proteins of the invention supply the cell with inorganic molecules required for all protein and nucleotide (among others) synthesis, and thus are critical for the overall viability of the cell. An increase in the number of viable cells producing one or more desired fine chemicals in large-scale culture should result in a concomitant increase in the yield, production, and/or efficiency of production of the fine chemical in the culture.  
      The isolated nucleic acid sequences of the invention are contained within the genome of a  Corynebacterium glutamicum  strain available through the American Type Culture Collection, given designation ATCC 13032. The nucleotide sequence of the isolated  C. glutamicum  HA DNAs and the predicted amino acid sequences of the  C. glutamicum  HA proteins are shown in Appendices A and B, respectively. Computational analyses were performed which classified and/or identified these nucleotide sequences as sequences which encode proteins that participate in  C. glutamicum  cell wall biosynthesis or rearrangements, metabolism of inorganic compounds, modification or degradation of aromatic or aliphatic compounds, or that have a  C. glutamicum  enzymatic or proteolytic activity.  
      The present invention also pertains to proteins which have an amino acid sequence which is substantially homologous to an amino acid sequence of Appendix B. As used herein, a protein which has an amino acid sequence which is substantially homologous to a selected amino acid sequence is least about 50% homologous to the selected amino acid sequence, e.g., the entire selected amino acid sequence. A protein which has an amino acid sequence which is substantially homologous to a selected amino acid sequence can also be least about 50-60%, preferably at least about 60-70%, and more preferably at least about 70-80%, 80-90%, or 90-95%, and most preferably at least about 96%, 97%, 98%, 99% or more homologous to the selected amino acid sequence.  
      The HA protein or a biologically active portion or fragment thereof of the invention can participate in the maintenance of homeostasis in  C. glutamicum , or can perform a function involved in the adaptation of this microorganism to different environmental conditions, or have one or more of the activities set forth in Table 1.  
      Various aspects of the invention are described in further detail in the following subsections.  
      A. Isolated Nucleic Acid Molecules  
      One aspect of the invention pertains to isolated nucleic acid molecules that encode HA polypeptides or biologically active portions thereof, as well as nucleic acid fragments sufficient for use as hybridization probes or primers for the identification or amplification of HA-encoding nucleic acid (e.g., HA DNA). As used herein, the term “nucleic acid molecule” is intended to include DNA molecules (e.g., cDNA or genomic DNA) and RNA molecules (e.g., mRNA) and analogs of the DNA or RNA generated using nucleotide analogs. This term also encompasses untranslated sequence located at both the 3′ and 5′ ends of the coding region of the gene: at least about 100 nucleotides of sequence upstream from the 5′ end of the coding region and at least about 20 nucleotides of sequence downstream from the 3′end of the coding region of the gene. The nucleic acid molecule can be single-stranded or double-stranded, but preferably is double-stranded DNA. An “isolated” nucleic acid molecule is one which is separated from other nucleic acid molecules which are present in the natural source of the nucleic acid. Preferably, an “isolated” nucleic acid is free of sequences which naturally flank the nucleic acid (i.e., sequences located at the 5′ and 3′ ends of the nucleic acid) in the genomic DNA of the organism from which the nucleic acid is derived. For example, in various embodiments, the isolated HA nucleic acid molecule can contain less than about 5 kb, 4 kb, 3 kb, 2 kb, 1 kb, 0.5 kb or 0.1 kb of nucleotide sequences which naturally flank the nucleic acid molecule in genomic DNA of the cell from which the nucleic acid is derived (e.g., a  C. glutamicum  cell). Moreover, an “isolated” nucleic acid molecule, such as a DNA molecule, can be substantially free of other cellular material, or culture medium when produced by recombinant techniques, or chemical precursors or other chemicals when chemically synthesized.  
      A nucleic acid molecule of the present invention, e.g., a nucleic acid molecule having a nucleotide sequence of Appendix A, or a portion thereof, can be isolated using standard molecular biology techniques and the sequence information provided herein. For example, a  C. glutamicum  HA DNA can be isolated from a  C. glutamicum  library using all or portion of one of the sequences of Appendix A as a hybridization probe and standard hybridization techniques (e.g., as described in Sambrook, J., Fritsh, E. F., and Maniatis, T.  Molecular Cloning: A Laboratory Manual.  2nd, ed., Cold Spring Harbor Laboratory, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y., 1989). Moreover, a nucleic acid molecule encompassing all or a portion of one of the sequences of Appendix A can be isolated by the polymerase chain reaction using oligonucleotide primers designed based upon this sequence (e.g., a nucleic acid molecule encompassing all or a portion of one of the sequences of Appendix A can be isolated by the polymerase chain reaction using oligonucleotide primers designed based upon this same sequence of Appendix A). For example, mRNA can be isolated from normal endothelial cells (e.g., by the guanidinium-thiocyanate extraction procedure of Chirgwin et al. (1979)  Biochemistry  18: 5294-5299) and DNA can be prepared using reverse transcriptase (e.g., Moloney MLV reverse transcriptase, available from Gibco/BRL, Bethesda, Md.; or AMV reverse transcriptase, available from Seikagaku America, Inc., St. Petersburg, Fla.). Synthetic oligonucleotide primers for polymerase chain reaction amplification can be designed based upon one of the nucleotide sequences shown in Appendix A. A nucleic acid of the invention can be amplified using cDNA or, alternatively, genomic DNA, as a template and appropriate oligonucleotide primers according to standard PCR amplification techniques. The nucleic acid so amplified can be cloned into an appropriate vector and characterized by DNA sequence analysis. Furthermore, oligonucleotides corresponding to an HA nucleotide sequence can be prepared by standard synthetic techniques, e.g., using an automated DNA synthesizer.  
      In a preferred embodiment, an isolated nucleic acid molecule of the invention comprises one of the nucleotide sequences shown in Appendix A. The sequences of Appendix A correspond to the  Corynebacterium glutamicum  HA DNAs of the invention. This DNA comprises sequences encoding HA proteins (i.e., the “coding region”, indicated in each sequence in Appendix A), as well as 5′ untranslated sequences and 3′ untranslated sequences, also indicated in Appendix A. Alternatively, the nucleic acid molecule can comprise only the coding region of any of the sequences in Appendix A.  
      For the purposes of this application, it will be understood that each of the sequences set forth in Appendix A has an identifying RXA, RXN, RXS, or RXC number having the designation “RXA,” “RXN,” “RXS, or “RXC” followed by 5 digits (i.e., RXA02458, RXN00249, RXS00153, or RXC00963). Each of these sequences comprises up to three parts: a 5′ upstream region, a coding region, and a downstream region. Each of these three regions is identified by the same RXA, RXN, RXS, or RXC designation to eliminate confusion. The recitation “one of the sequences in Appendix A”, then, refers to any of the sequences in Appendix A, which may be distinguished by their differing RXA, RXN, RXS, or RXC designations. The coding region of each of these sequences is translated into a corresponding amino acid sequence, which is set forth in Appendix B. The sequences of Appendix B are identified by the same RXA, RXN, RXS, or RXC designations as Appendix A, such that they can be readily correlated. For example, the amino acid sequences in Appendix B designated RXA02458, RXN00249, RXS00153, and RXC00963 are translations of the coding regions of the nucleotide sequences of nucleic acid molecules RXA02458, RXN00249, RXS00153, and RXC00963, respectively, in Appendix A. Each of the RXA, RXN, RXS, and RXC nucleotide and amino acid sequences of the invention has also been assigned a SEQ ID NO, as indicated in Table 1.  
      Several of the genes of the invention are “F-designated genes”. An F-designated gene includes those genes set forth in Table 1 which have an ‘F’ in front of the RXA, RXN, RXS, or RXC designation. For example, SEQ ID NO:5, designated, as indicated on Table 1, as “F RXA00249”, is an F-designated gene, as are SEQ ID NOs: 11, 15, and 33 (designated on Table 1 as “F RXA02264”, “F RXA02274”, and “F RXA00675”, respectively).  
      In one embodiment, the nucleic acid molecules of the present invention are not intended to include those compiled in Table 2. In the case of the dapD gene, a sequence for this gene was published in Wehrmann, A., et al. (1998)  J. Bacteriol.  180(12): 3159-3165. However, the sequence obtained by the inventors of the present application is significantly longer than the published version. It is believed that the published version relied on an incorrect start codon, and thus represents only a fragment of the actual coding region.  
      In another preferred embodiment, an isolated nucleic acid molecule of the invention comprises a nucleic acid molecule which is a complement of one of the nucleotide sequences shown in Appendix A, or a portion thereof. A nucleic acid molecule which is complementary to one of the nucleotide sequences shown in Appendix A is one which is sufficiently complementary to one of the nucleotide sequences shown in Appendix A such that it can hybridize to one of the nucleotide sequences shown in Appendix A, thereby forming a stable duplex.  
      In still another preferred embodiment, an isolated nucleic acid molecule of the invention comprises a nucleotide sequence which is at least about 50%, 51%, 52%, 53%, 54%, 55%, 56%, 57%, 58%, 59%, or 60%, preferably at least about 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, or 70%%, more preferably at least about 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, or 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, or 90%, or 91%, 92%, 93%, 94%, and even more preferably at least about 95%, 96%, 97%, 98%, 99% or more homologous to a nucleotide sequence shown in Appendix A, or a portion thereof. Ranges and identity values intermediate to the above-recited ranges, (e.g., 70-90% identical or 80-95% identical) are also intended to be encompassed by the present invention. For example, ranges of identity values using a combination of any of the above values recited as upper and/or lower limits are intended to be included. In an additional preferred embodiment, an isolated nucleic acid molecule of the invention comprises a nucleotide sequence which hybridizes, e.g., hybridizes under stringent conditions, to one of the nucleotide sequences shown in Appendix A, or a portion thereof.  
      Moreover, the nucleic acid molecule of the invention can comprise only a portion of the coding region of one of the sequences in Appendix A, for example a fragment which can be used as a probe or primer or a fragment encoding a biologically active portion of an HA protein. The nucleotide sequences determined from the cloning of the HA genes from  C. glutamicum  allows for the generation of probes and primers designed for use in identifying and/or cloning HA homologues in other cell types and organisms, as well as HA homologues from other  Corynebacteria  or related species. The probe/primer typically comprises substantially purified oligonucleotide. The oligonucleotide typically comprises a region of nucleotide sequence that hybridizes under stringent conditions to at least about 12, preferably about 25, more preferably about 40, 50 or 75 consecutive nucleotides of a sense strand of one of the sequences set forth in Appendix A, an anti-sense sequence of one of the sequences set forth in Appendix A, or naturally occurring mutants thereof. Primers based on a nucleotide sequence of Appendix A can be used in PCR reactions to clone HA homologues. Probes based on the HA nucleotide sequences can be used to detect transcripts or genomic sequences encoding the same or homologous proteins. In preferred embodiments, the probe further comprises a label group attached thereto, e.g. the label group can be a radioisotope, a fluorescent compound, an enzyme, or an enzyme co-factor. Such probes can be used as a part of a diagnostic test kit for identifying cells which misexpress an HA protein, such as by measuring a level of an HA-encoding nucleic acid in a sample of cells, e.g., detecting HA mRNA levels or determining whether a genomic HA gene has been mutated or deleted.  
      In one embodiment, the nucleic acid molecule of the invention encodes a protein or portion thereof which includes an amino acid sequence which is sufficiently homologous to an amino acid sequence of Appendix B such that the protein or portion thereof maintains the ability to participate in the maintenance of homeostasis in  C. glutamicum , or to perform a function involved in the adaptation of this microorganism to different environmental conditions. As used herein, the language “sufficiently homologous” refers to proteins or portions thereof which have amino acid sequences which include a minimum number of identical or equivalent (e.g., an amino acid residue which has a similar side chain as an amino acid residue in one of the sequences of Appendix B) amino acid residues to an amino acid sequence of Appendix B such that the protein or portion thereof is able to participate in the maintenance of homeostasis in  C. glutamicum , or to perform a function involved in the adaptation of this microorganism to different environmental conditions. Proteins involved in  C. glutamicum  cell wall biosynthesis or rearrangements, metabolism of inorganic compounds, modification or degradation of aromatic or aliphatic compounds, or that have a  C. glutamicum  enzymatic or proteolytic activity, as described herein, may play a role in the production and secretion of one or more fine chemicals. Examples of such activities are also described herein. Thus, “the function of an HA protein” contributes either directly or indirectly to the yield, production, and/or efficiency of production of one or more fine chemicals. Examples of HA protein activities are set forth in Table 1.  
      In another embodiment, the protein is at least about 50-60%, preferably at least about 60-70%, and more preferably at least about 70-80%, 80-90%, 90-95%, and most preferably at least about 96%, 97%, 98%, 99% or more homologous to an entire amino acid sequence of Appendix B.  
      Portions of proteins encoded by the HA nucleic acid molecules of the invention are preferably biologically active portions of one of the HA proteins. As used herein, the term “biologically active portion of an HA protein” is intended to include a portion, e.g., a domain/motif, of an HA protein that can participate in the maintenance of homeostasis in  C. glutamicum , or that can perform a function involved in the adaptation of this microorganism to different environmental conditions, or has an activity as set forth in Table 1. To determine whether an HA protein or a biologically active portion thereof can participate in  C. glutamicum  cell wall biosynthesis or rearrangements, metabolism of inorganic compounds, modification or degradation of aromatic or aliphatic compounds, or has a  C. glutamicum  enzymatic or proteolytic activity, an assay of enzymatic activity may be performed. Such assay methods are well known to those of ordinary skill in the art, as detailed in Example 8 of the Exemplification.  
      Additional nucleic acid fragments encoding biologically active portions of an HA protein can be prepared by isolating a portion of one of the sequences in Appendix B, expressing the encoded portion of the HA protein or peptide (e.g., by recombinant expression in vitro) and assessing the activity of the encoded portion of the HA protein or peptide.  
      The invention further encompasses nucleic acid molecules that differ from one of the nucleotide sequences shown in Appendix A (and portions thereof) due to degeneracy of the genetic code and thus encode the same HA protein as that encoded by the nucleotide sequences shown in Appendix A. In another embodiment, an isolated nucleic acid molecule of the invention has a nucleotide sequence encoding a protein having an amino acid sequence shown in Appendix B. In a still further embodiment, the nucleic acid molecule of the invention encodes a full length  C. glutamicum  protein which is substantially homologous to an amino acid sequence of Appendix B (encoded by an open reading frame shown in Appendix A).  
      It will be understood by one of ordinary skill in the art that in one embodiment the sequences of the invention are not meant to include the sequences of the prior art, such as those Genbank sequences set forth in Tables 2 or 4 which were available prior to the present invention. In one embodiment, the invention includes nucleotide and amino acid sequences having a percent identity to a nucleotide or amino acid sequence of the invention which is greater than that of a sequence of the prior art (e.g., a Genbank sequence (or the protein encoded by such a sequence) set forth in Tables 2 or 4). For example, the invention includes a nucleotide sequence which is greater than and/or at least 39% identical to the nucleotide sequence designated RXA00471 (SEQ ID NO:293), a nucleotide sequence which is greater than and/or at least 41% identical to the nucleotide sequence designated RXA00500 (SEQ ID NO:143), and a nucleotide sequence which is greater than and/or at least 35% identical to the nucleotide sequence designated RXA00502 (SEQ ID NO:147). One of ordinary skill in the art would be able to calculate the lower threshold of percent identity for any given sequence of the invention by examining the GAP-calculated percent identity scores set forth in Table 4 for each of the three top hits for the given sequence, and by subtracting the highest GAP-calculated percent identity from 100 percent. One of ordinary skill in the art will also appreciate that nucleic acid and amino acid sequences having percent identities greater than the lower threshold so calculated (e.g., at least 50%, 51%, 52%, 53%, 54%, 55%, 56%, 57%, 58%, 59%, or 60%, preferably at least about 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, or 70%, more preferably at least about 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, or 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, or 90%, or 91%, 92%, 93%, 94%, and even more preferably at least about 95%, 96%, 97%, 98%, 99% or more identical) are also encompassed by the invention.  
      In addition to the  C. glutamicum  HA nucleotide sequences shown in Appendix A, it will be appreciated by those of ordinary skill in the art that DNA sequence polymorphisms that lead to changes in the amino acid sequences of HA proteins may exist within a population (e.g., the  C. glutamicum  population). Such genetic polymorphism in the HA gene may exist among individuals within a population due to natural variation. As used herein, the terms “gene” and “recombinant gene” refer to nucleic acid molecules comprising an open reading frame encoding an HA protein, preferably a  C. glutamicum  HA protein. Such natural variations can typically result in 1-5% variance in the nucleotide sequence of the HA gene. Any and all such nucleotide variations and resulting amino acid polymorphisms in HA that are the result of natural variation and that do not alter the functional activity of HA proteins are intended to be within the scope of the invention.  
      Nucleic acid molecules corresponding to natural variants and non- C. glutamicum  homologues of the  C. glutamicum  HA DNA of the invention can be isolated based on their homology to the  C. glutamicum  HA nucleic acid disclosed herein using the  C. glutamicum  DNA, or a portion thereof, as a hybridization probe according to standard hybridization techniques under stringent hybridization conditions. Accordingly, in another embodiment, an isolated nucleic acid molecule of the invention is at least 15 nucleotides in length and hybridizes under stringent conditions to the nucleic acid molecule comprising a nucleotide sequence of Appendix A. In other embodiments, the nucleic acid is at least 30, 50, 100, 250 or more nucleotides in length. As used herein, the term “hybridizes under stringent conditions” is intended to describe conditions for hybridization and washing under which nucleotide sequences at least 60% homologous to each other typically remain hybridized to each other. Preferably, the conditions are such that sequences at least about 65%, more preferably at least about 70%, and even more preferably at least about 75% or more homologous to each other typically remain hybridized to each other. Such stringent conditions are known to those of ordinary skill in the art and can be found in  Current Protocols in Molecular Biology , John Wiley &amp; Sons, N.Y. (1989), 6.3.1-6.3.6. A preferred, non-limiting example of stringent hybridization conditions are hybridization in 6× sodium chloride/sodium citrate (SSC) at about 45° C., followed by one or more washes in 0.2×SSC, 0.1% SDS at 50-65° C. Preferably, an isolated nucleic acid molecule of the invention that hybridizes under stringent conditions to a sequence of Appendix A corresponds to a naturally-occurring nucleic acid molecule. As used herein, a “naturally-occurring” nucleic acid molecule refers to an RNA or DNA molecule having a nucleotide sequence that occurs in nature (e.g., encodes a natural protein). In one embodiment, the nucleic acid encodes a natural  C. glutamicum  HA protein.  
      In addition to naturally-occurring variants of the HA sequence that may exist in the population, one of ordinary skill in the art will further appreciate that changes can be introduced by mutation into a nucleotide sequence of Appendix A, thereby leading to changes in the amino acid sequence of the encoded HA protein, without altering the functional ability of the HA protein. For example, nucleotide substitutions leading to amino acid substitutions at “non-essential” amino acid residues can be made in a sequence of Appendix A. A “non-essential” amino acid residue is a residue that can be altered from the wild-type sequence of one of the HA proteins (Appendix B) without altering the activity of said HA protein, whereas an “essential” amino acid residue is required for HA protein activity. Other amino acid residues, however, (e.g., those that are not conserved or only semi-conserved in the domain having HA activity) may not be essential for activity and thus are likely to be amenable to alteration without altering HA activity.  
      Accordingly, another aspect of the invention pertains to nucleic acid molecules encoding HA proteins that contain changes in amino acid residues that are not essential for HA activity. Such HA proteins differ in amino acid sequence from a sequence contained in Appendix B yet retain at least one of the HA activities described herein. In one embodiment, the isolated nucleic acid molecule comprises a nucleotide sequence encoding a protein, wherein the protein comprises an amino acid sequence at least about 50% homologous to an amino acid sequence of Appendix B and is capable of participating in the maintenance of homeostasis in  C. glutamicum , or of performing a function involved in the adaptation of this microorganism to different environmental conditions, or has one or more of the activities set forth in Table 1. Preferably, the protein encoded by the nucleic acid molecule is at least about 50-60% homologous to one of the sequences in Appendix B, more preferably at least about 60-70% homologous to one of the sequences in Appendix B, even more preferably at least about 70-80%, 80-90%, 90-95% homologous to one of the sequences in Appendix B, and most preferably at least about 96%, 97%, 98%, or 99% homologous to one of the sequences in Appendix B.  
      To determine the percent homology of two amino acid sequences (e.g., one of the sequences of Appendix B and a mutant form thereof) or of two nucleic acids, the sequences are aligned for optimal comparison purposes (e.g., gaps can be introduced in the sequence of one protein or nucleic acid for optimal alignment with the other protein or nucleic acid). The amino acid residues or nucleotides at corresponding amino acid positions or nucleotide positions are then compared. When a position in one sequence (e.g., one of the sequences of Appendix B) is occupied by the same amino acid residue or nucleotide as the corresponding position in the other sequence (e.g., a mutant form of the sequence selected from Appendix B), then the molecules are homologous at that position (i.e., as used herein amino acid or nucleic acid “homology” is equivalent to amino acid or nucleic acid “identity”). The percent homology between the two sequences is a function of the number of identical positions shared by the sequences (i.e., % homology=#of identical positions/total #of positions×100).  
      An isolated nucleic acid molecule encoding an HA protein homologous to a protein sequence of Appendix B can be created by introducing one or more nucleotide substitutions, additions or deletions into a nucleotide sequence of Appendix A such that one or more amino acid substitutions, additions or deletions are introduced into the encoded protein. Mutations can be introduced into one of the sequences of Appendix A by standard techniques, such as site-directed mutagenesis and PCR-mediated mutagenesis. Preferably, conservative amino acid substitutions are made at one or more predicted non-essential amino acid residues. A “conservative amino acid substitution” is one in which the amino acid residue is replaced with an amino acid residue having a similar side chain. Families of amino acid residues having similar side chains have been defined in the art. These families include amino acids with basic side chains (e.g., lysine, arginine, histidine), acidic side chains (e.g., aspartic acid, glutamic acid), uncharged polar side chains (e.g., glycine, asparagine, glutamine, serine, threonine, tyrosine, cysteine), nonpolar side chains (e.g., alanine, valine, leucine, isoleucine, proline, phenylalanine, methionine, tryptophan), beta-branched side chains (e.g., threonine, valine, isoleucine) and aromatic side chains (e.g., tyrosine, phenylalanine, tryptophan, histidine). Thus, a predicted nonessential amino acid residue in an HA protein is preferably replaced with another amino acid residue from the same side chain family. Alternatively, in another embodiment, mutations can be introduced randomly along all or part of an HA coding sequence, such as by saturation mutagenesis, and the resultant mutants can be screened for an HA activity described herein to identify mutants that retain HA activity. Following mutagenesis of one of the sequences of Appendix A, the encoded protein can be expressed recombinantly and the activity of the protein can be determined using, for example, assays described herein (see Example 8 of the Exemplification).  
      In addition to the nucleic acid molecules encoding HA proteins described above, another aspect of the invention pertains to isolated nucleic acid molecules which are antisense thereto. An “antisense” nucleic acid comprises a nucleotide sequence which is complementary to a “sense” nucleic acid encoding a protein, e.g., complementary to the coding strand of a double-stranded DNA molecule or complementary to an mRNA sequence. Accordingly, an antisense nucleic acid can hydrogen bond to a sense nucleic acid. The antisense nucleic acid can be complementary to an entire HA coding strand, or to only a portion thereof. In one embodiment, an antisense nucleic acid molecule is antisense to a “coding region” of the coding strand of a nucleotide sequence encoding an HA protein. The term “coding region” refers to the region of the nucleotide sequence comprising codons which are translated into amino acid residues (e.g., the entire coding region of SEQ ID NO. 3 (RXN00249) comprises nucleotides 1 to 957). In another embodiment, the antisense nucleic acid molecule is antisense to a “noncoding region” of the coding strand of a nucleotide sequence encoding HA. The term “noncoding region” refers to 5′ and 3′ sequences which flank the coding region that are not translated into amino acids (i.e., also referred to as 5′ and 3′ untranslated regions).  
      Given the coding strand sequences encoding HA disclosed herein (e.g., the sequences set forth in Appendix A), antisense nucleic acids of the invention can be designed according to the rules of Watson and Crick base pairing. The antisense nucleic acid molecule can be complementary to the entire coding region of HA mRNA, but more preferably is an oligonucleotide which is antisense to only a portion of the coding or noncoding region of HA mRNA. For example, the antisense oligonucleotide can be complementary to the region surrounding the translation start site of HA mRNA. An antisense oligonucleotide can be, for example, about 5, 10, 15, 20, 25, 30, 35, 40, 45 or 50 nucleotides in length. An antisense nucleic acid of the invention can be constructed using chemical synthesis and enzymatic ligation reactions using procedures known in the art. For example, an antisense nucleic acid (e.g., an antisense oligonucleotide) can be chemically synthesized using naturally occurring nucleotides or variously modified nucleotides designed to increase the biological stability of the molecules or to increase the physical stability of the duplex formed between the antisense and sense nucleic acids, e.g., phosphorothioate derivatives and acridine substituted nucleotides can be used. Examples of modified nucleotides which can be used to generate the antisense nucleic acid include 5-fluorouracil, 5-bromouracil, 5-chlorouracil, 5-iodouracil, hypoxanthine, xanthine, 4-acetylcytosine, 5-(carboxyhydroxylmethyl) uracil, 5-carboxymethylaminomethyl-2-thiouridine, 5-carboxymethylaminomethyluracil, dihydrouracil, beta-D-galactosylqueosine, inosine, N6-isopentenyladenine, 1-methylguanine, 1-methylinosine, 2,2-dimethylguanine, 2-methyladenine, 2-methylguanine, 3-methylcytosine, 5-methylcytosine, N6-adenine, 7-methylguanine, 5-methylaminomethyluracil, 5-methoxyaminomethyl-2-thiouracil, beta-D-mannosylqueosine, 5′-methoxycarboxymethyluracil, 5-methoxyuracil, 2-methylthio-N-6-isopentenyladenine, uracil-5-oxyacetic acid (v), wybutoxosine, pseudouracil, queosine, 2-thiocytosine, 5-methyl-2-thiouracil, 2-thiouracil, 4-thiouracil, 5-methyluracil, uracil-5-oxyacetic acid methylester, uracil-5-oxyacetic acid (v), 5-methyl-2-thiouracil, 3-(3-amino-3-N-2-carboxypropyl) uracil, (acp3)w, and 2,6-diaminopurine. Alternatively, the antisense nucleic acid can be produced biologically using an expression vector into which a nucleic acid has been subcloned in an antisense orientation (i.e., RNA transcribed from the inserted nucleic acid will be of an antisense orientation to a target nucleic acid of interest, described further in the following subsection).  
      The antisense nucleic acid molecules of the invention are typically administered to a cell or generated in situ such that they hybridize with or bind to cellular mRNA and/or genomic DNA encoding an HA protein to thereby inhibit expression of the protein, e.g., by inhibiting transcription and/or translation. The hybridization can be by conventional nucleotide complementarity to form a stable duplex, or, for example, in the case of an antisense nucleic acid molecule which binds to DNA duplexes, through specific interactions in the major groove of the double helix. The antisense molecule can be modified such that it specifically binds to a receptor or an antigen expressed on a selected cell surface, e.g., by linking the antisense nucleic acid molecule to a peptide or an antibody which binds to a cell surface receptor or antigen. The antisense nucleic acid molecule can also be delivered to cells using the vectors described herein. To achieve sufficient intracellular concentrations of the antisense molecules, vector constructs in which the antisense nucleic acid molecule is placed under the control of a strong prokaryotic, viral, or eukaryotic promoter are preferred.  
      In yet another embodiment, the antisense nucleic acid molecule of the invention is an α-anomeric nucleic acid molecule. An α-anomeric nucleic acid molecule forms specific double-stranded hybrids with complementary RNA in which, contrary to the usual P-units, the strands run parallel to each other (Gaultier et al. (1987)  Nucleic Acids. Res.  15:6625-6641). The antisense nucleic acid molecule can also comprise a 2′-o-methylribonucleotide (Inoue et al. (1987)  Nucleic Acids Res.  15:6131-6148) or a chimeric RNA-DNA analogue (Inoue et al. (1987)  FEBS Lett.  215:327-330).  
      In still another embodiment, an antisense nucleic acid of the invention is a ribozyme. Ribozymes are catalytic RNA molecules with ribonuclease activity which are capable of cleaving a single-stranded nucleic acid, such as an mRNA, to which they have a complementary region. Thus, ribozymes (e.g., hammerhead ribozymes (described in Haselhoff and Gerlach (1988)  Nature  334:585-591)) can be used to catalytically cleave HA mRNA transcripts to thereby inhibit translation of HA mRNA. A ribozyme having specificity for an HA-encoding nucleic acid can be designed based upon the nucleotide sequence of an HA DNA molecule disclosed herein (i.e., SEQ ID NO. 3 (RXN00249) Appendix A). For example, a derivative of a  Tetrahymena  L-19 IVS RNA can be constructed in which the nucleotide sequence of the active site is complementary to the nucleotide sequence to be cleaved in an HA-encoding mRNA. See, e.g., Cech et al. U.S. Pat. No. 4,987,071 and Cech et al. U.S. Pat. No. 5,116,742. Alternatively, HA mRNA can be used to select a catalytic RNA having a specific ribonuclease activity from a pool of RNA molecules. See, e.g., Bartel, D. and Szostak, J. W. (1993)  Science  261:1411-1418.  
      Alternatively, HA gene expression can be inhibited by targeting nucleotide sequences complementary to the regulatory region of an HA nucleotide sequence (e.g., an HA promoter and/or enhancers) to form triple helical structures that prevent transcription of an HA gene in target cells. See generally, Helene, C. (1991)  Anticancer Drug Des.  6(6):569-84; Helene, C. et al. (1992)  Ann. N.Y. Acad. Sci.  660:27-36; and Maher, L. J. (1992)  Bioassays  14(12):807-15.  
      B. Recombinant Expression Vectors and Host Cells  
      Another aspect of the invention pertains to vectors, preferably expression vectors, containing a nucleic acid encoding an HA protein (or a portion thereof). As used herein, the term “vector” refers to a nucleic acid molecule capable of transporting another nucleic acid to which it has been linked. One type of vector is a “plasmid”, which refers to a circular double stranded DNA loop into which additional DNA segments can be ligated. Another type of vector is a viral vector, wherein additional DNA segments can be ligated into the viral genome. Certain vectors are capable of autonomous replication in a host cell into which they are introduced (e.g., bacterial vectors having a bacterial origin of replication and episomal mammalian vectors). Other vectors (e.g., non-episomal mammalian vectors) are integrated into the genome of a host cell upon introduction into the host cell, and thereby are replicated along with the host genome. Moreover, certain vectors are capable of directing the expression of genes to which they are operatively linked. Such vectors are referred to herein as “expression vectors”. In general, expression vectors of utility in recombinant DNA techniques are often in the form of plasmids. In the present specification, “plasmid” and “vector” can be used interchangeably as the plasmid is the most commonly used form of vector. However, the invention is intended to include such other forms of expression vectors, such as viral vectors (e.g., replication defective retroviruses, adenoviruses and adeno-associated viruses), which serve equivalent functions.  
      The recombinant expression vectors of the invention comprise a nucleic acid of the invention in a form suitable for expression of the nucleic acid in a host cell, which means that the recombinant expression vectors include one or more regulatory sequences, selected on the basis of the host cells to be used for expression, which are operatively linked to the nucleic acid sequence to be expressed. Within a recombinant expression vector, “operably linked” is intended to mean that the nucleotide sequence of interest is linked to the regulatory sequence(s) in a manner which allows for expression of the nucleotide sequence (e.g., in an in vitro transcription/translation system or in a host cell when the vector is introduced into the host cell). The term “regulatory sequence” is intended to include promoters, enhancers and other expression control elements (e.g., polyadenylation signals). Such regulatory sequences are described, for example, in Goeddel;  Gene Expression Technology: Methods in Enzymology  185, Academic Press, San Diego, Calif. (1990). Regulatory sequences include those which direct constitutive expression of a nucleotide sequence in many types of host cell and those which direct expression of the nucleotide sequence only in certain host cells. Preferred regulatory sequences are, for example, promoters such as cos-, tac-, trp-, tet-, trp-tet-, lpp-, lac-, lpp-lac-, lacI q , T7-, T5-, T3-, gal-, trc-, ara-, SP6—, arny, SPO2, λ-P R - or λP L , which are used preferably in bacteria. Additional regulatory sequences are, for example, promoters from yeasts and fungi, such as ADC1, MFα, AC, P-60, CYC1, GAPDH, TEF, rp28, ADH, promoters from plants such as CaMV/35S, SSU, OCS, lib4, usp, STLS1, B33, nos or ubiquitin- or phaseolin-promoters. It is also possible to use artificial promoters. It will be appreciated by those of ordinary skill in the art that the design of the expression vector can depend on such factors as the choice of the host cell to be transformed, the level of expression of protein desired, etc. The expression vectors of the invention can be introduced into host cells to thereby produce proteins or peptides, including fusion proteins or peptides, encoded by nucleic acids as described herein (e.g., HA proteins, mutant forms of HA proteins, fusion proteins, etc.).  
      The recombinant expression vectors of the invention can be designed for expression of HA proteins in prokaryotic or eukaryotic cells. For example, HA genes can be expressed in bacterial cells such as  C. glutamicum , insect cells (using baculovirus expression vectors), yeast and other fungal cells (see Romanos, M. A. et al. (1992) “Foreign gene expression in yeast: a review”,  Yeast  8: 423-488; van den Hondel, C. A. M. J. J. et al. (1991) “Heterologous gene expression in filamentous fungi” in: More Gene Manipulations in Fungi, J. W. Bennet &amp; L. L. Lasure, eds., p. 396-428: Academic Press: San Diego; and van den Hondel, C. A. M. J. J. &amp; Punt, P. J. (1991) “Gene transfer systems and vector development for filamentous fungi, in: Applied Molecular Genetics of Fungi, Peberdy, J. F. et al., eds., p. 1-28, Cambridge University Press: Cambridge), algae and multicellular plant cells (see Schmidt, R. and Willmitzer, L. (1988) High efficiency  Agrobacterium tumefaciens —mediated transformation of  Arabidopsis thaliana  leaf and cotyledon explants”  Plant Cell Rep.:  583-586), or mammalian cells. Suitable host cells are discussed further in Goeddel,  Gene Expression Technology: Methods in Enzymology  185, Academic Press, San Diego, Calif. (1990). Alternatively, the recombinant expression vector can be transcribed and translated in vitro, for example using T7 promoter regulatory sequences and T7 polymerase.  
      Expression of proteins in prokaryotes is most often carried out with vectors containing constitutive or inducible promoters directing the expression of either fusion or non-fusion proteins. Fusion vectors add a number of amino acids to a protein encoded therein, usually to the amino terminus of the recombinant protein but also to the C-terminus or fused within suitable regions in the proteins. Such fusion vectors typically serve three purposes: 1) to increase expression of recombinant protein; 2) to increase the solubility of the recombinant protein; and 3) to aid in the purification of the recombinant protein by acting as a ligand in affinity purification. Often, in fusion expression vectors, a proteolytic cleavage site is introduced at the junction of the fusion moiety and the recombinant protein to enable separation of the recombinant protein from the fusion moiety subsequent to purification of the fusion protein. Such enzymes, and their cognate recognition sequences, include Factor Xa, thrombin and enterokinase.  
      Typical fusion expression vectors include pGEX (Pharmacia Biotech Inc; Smith, D. B. and Johnson, K. S. (1988)  Gene  67:31-40), pMAL (New England Biolabs, Beverly, Mass.) and pRIT5 (Pharmacia, Piscataway, N.J.) which fuse glutathione S-transferase (GST), maltose E binding protein, or protein A, respectively, to the target recombinant protein. In one embodiment, the coding sequence of the HA protein is cloned into a pGEX expression vector to create a vector encoding a fusion protein comprising, from the N-terminus to the C-terminus, GST-thrombin cleavage site-X protein. The fusion protein can be purified by affinity chromatography using glutathione-agarose resin. Recombinant HA protein unfused to GST can be recovered by cleavage of the fusion protein with thrombin.  
      Examples of suitable inducible non-fusion  E. coli  expression vectors include pTrc (Amann et al., (1988)  Gene  69:301-315) pLG338, pACYC184, pBR322, pUC18, pUC19, pKC30, pRep4, pHS1, pHS2, pPLc236, pMBL24, pLG200, pUR290, pIN-III113-B1, λgt11, pBdCl, and pET 11d (Studier et al.,  Gene Expression Technology: Methods in Enzymology  185, Academic Press, San Diego, Calif. (1990) 60-89; and Pouwels et al., eds. (1985) Cloning Vectors. Elsevier: New York IBSN 0 444 904018). Target gene expression from the pTrc vector relies on host RNA polymerase transcription from a hybrid trp-lac fusion promoter. Target gene expression from the pET 11d vector relies on transcription from a T7 gn10-lac fusion promoter mediated by a coexpressed viral RNA polymerase (T7 gn1). This viral polymerase is supplied by host strains BL21(DE3) or HMS174(DE3) from a resident λ prophage harboring a T7 gn1 gene under the transcriptional control of the lacUV 5 promoter. For transformation of other varieties of bacteria, appropriate vectors may be selected. For example, the plasmids pIJ101, pIJ364, pIJ702 and pIJ361 are known to be useful in transforming  Streptomyces , while plasmids pUB110, pC194, or pBD214 are suited for transformation of  Bacillus  species. Several plasmids of use in the transfer of genetic information into  Corynebacterium  include pHM1519, pBL1, pSA77, or pAJ667 (Pouwels et al., eds. (1985) Cloning Vectors. Elsevier: New York IBSN 0 444 904018).  
      One strategy to maximize recombinant protein expression is to express the protein in a host bacteria with an impaired capacity to proteolytically cleave the recombinant protein (Gottesman, S.,  Gene Expression Technology: Methods in Enzymology  185, Academic Press, San Diego, Calif. (1990) 119-128). Another strategy is to alter the nucleic acid sequence of the nucleic acid to be inserted into an expression vector so that the individual codons for each amino acid are those preferentially utilized in the bacterium chosen for expression, such as  C. glutamicum  (Wada et al. (1992)  Nucleic Acids Res.  20: 2111-2118). Such alteration of nucleic acid sequences of the invention can be carried out by standard DNA synthesis techniques.  
      In another embodiment, the HA protein expression vector is a yeast expression vector. Examples of vectors for expression in yeast  S. cerevisiae  include pYepSec1 (Baldari, et al., (1987)  Embo J.  6:229-234), 2μ, pAG-1, Yep6, Yep13, pEMBLYe23, pMFa (Kurjan and Herskowitz, (1982)  Cell  30:933-943), pJRY88 (Schultz et al., (1987)  Gene  54:113-123), and pYES2 (Invitrogen Corporation, San Diego, Calif.). Vectors and methods for the construction of vectors appropriate for use in other fungi, such as the filamentous fungi, include those detailed in: van den Hondel, C. A. M. J. J. &amp; Punt, P. J. (1991) “Gene transfer systems and vector development for filamentous fungi, in: Applied Molecular Genetics of Fungi, J. F. Peberdy, et al., eds., p. 1-28, Cambridge University Press: Cambridge, and Pouwels et al., eds. (1985) Cloning Vectors. Elsevier: New York (IBSN 0 444 904018).  
      Alternatively, the HA proteins of the invention can be expressed in insect cells using baculovirus expression vectors. Baculovirus vectors available for expression of proteins in cultured insect cells (e.g., Sf 9 cells) include the pAc series (Smith et al. (1983)  Mol. Cell. Biol.  3:2156-2165) and the pVL series (Lucklow and Summers (1989)  Virology  170:31-39).  
      In another embodiment, the HA proteins of the invention may be expressed in unicellular plant cells (such as algae) or in plant cells from higher plants (e.g., the spermatophytes, such as crop plants). Examples of plant expression vectors include those detailed in: Becker, D., Kemper, E., Schell, J. and Masterson, R. (1992) “New plant binary vectors with selectable markers located proximal to the left border”,  Plant Mol. Biol.  20: 1195-1197; and Bevan, M. W. (1984) “Binary  Agrobacterium  vectors for plant transformation”,  Nucl. Acid. Res.  12: 8711-8721, and include pLGV23, pGHlac+, pBIN19, pAK2004, and pDH51 (Pouwels et al., eds. (1985) Cloning Vectors. Elsevier: New York IBSN 0 444 904018).  
      In yet another embodiment, a nucleic acid of the invention is expressed in mammalian cells using a mammalian expression vector. Examples of mammalian expression vectors include pCDM8 (Seed, B. (1987)  Nature  329:840) and pMT2PC (Kaufman et al. (1987)  EMBO J.  6:187-195). When used in mammalian cells, the expression vector&#39;s control functions are often provided by viral regulatory elements. For example, commonly used promoters are derived from polyoma, Adenovirus 2, cytomegalovirus and Simian Virus 40. For other suitable expression systems for both prokaryotic and eukaryotic cells see chapters 16 and 17 of Sambrook, J., Fritsh, E. F., and Maniatis, T.  Molecular Cloning: A Laboratory Manual.  2 nd, ed., Cold Spring Harbor Laboratory , Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y., 1989.  
      In another embodiment, the recombinant mammalian expression vector is capable of directing expression of the nucleic acid preferentially in a particular cell type (e.g., tissue-specific regulatory elements are used to express the nucleic acid). Tissue-specific regulatory elements are known in the art. Non-limiting examples of suitable tissue-specific promoters include the albumin promoter (liver-specific; Pinkert et al. (1987)  Genes Dev.  1:268-277), lymphoid-specific promoters (Calame and Eaton (1988)  Adv. Immunol.  43:235-275), in particular promoters of T cell receptors (Winoto and Baltimore (1989)  EMBO J.  8:729-733) and immunoglobulins (Baneiji et al. (1983)  Cell  33:729-740; Queen and Baltimore (1983)  Cell  33:741-748), neuron-specific promoters (e.g., the neurofilament promoter; Byrne and Ruddle (1989)  PNAS  86:5473-5477), pancreas-specific promoters (Edlund et al. (1985)  Science  230:912-916), and mammary gland-specific promoters (e.g., milk whey promoter; U.S. Pat. No. 4,873,316 and European Application Publication No. 264,166). Developmentally-regulated promoters are also encompassed, for example the murine hox promoters (Kessel and Gruss (1990)  Science  249:374-379) and the α-fetoprotein promoter (Campes and Tilghman (1989)  Genes Dev.  3:537-546).  
      The invention further provides a recombinant expression vector comprising a DNA molecule of the invention cloned into the expression vector in an antisense orientation. That is, the DNA molecule is operatively linked to a regulatory sequence in a manner which allows for expression (by transcription of the DNA molecule) of an RNA molecule which is antisense to HA mRNA. Regulatory sequences operatively linked to a nucleic acid cloned in the antisense orientation can be chosen which direct the continuous expression of the antisense RNA molecule in a variety of cell types, for instance viral promoters and/or enhancers, or regulatory sequences can be chosen which direct constitutive, tissue specific or cell type specific expression of antisense RNA. The antisense expression vector can be in the form of a recombinant plasmid, phagemid or attenuated virus in which antisense nucleic acids are produced under the control of a high efficiency regulatory region, the activity of which can be determined by the cell type into which the vector is introduced. For a discussion of the regulation of gene expression using antisense genes see Weintraub, H. et al., Antisense RNA as a molecular tool for genetic analysis,  Reviews—Trends in Genetics , Vol. 1(1) (1986).  
      Another aspect of the invention pertains to host cells into which a recombinant expression vector of the invention has been introduced. The terms “host cell” and “recombinant host cell” are used interchangeably herein. It is understood that such terms refer not only to the particular subject cell but to the progeny or potential progeny of such a cell. Because certain modifications may occur in succeeding generations due to either mutation or environmental influences, such progeny may not, in fact, be identical to the parent cell, but are still included within the scope of the term as used herein.  
      A host cell can be any prokaryotic or eukaryotic cell. For example, an HA protein can be expressed in bacterial cells such as  C. glutamicum , insect cells, yeast or mammalian cells (such as Chinese hamster ovary cells (CHO) or COS cells). Other suitable host cells are known to those of ordinary skill in the art. Microorganisms related to  Corynebacterium glutamicum  which may be conveniently used as host cells for the nucleic acid and protein molecules of the invention are set forth in Table 3.  
      Vector DNA can be introduced into prokaryotic or eukaryotic cells via conventional transformation or transfection techniques. As used herein, the terms “transformation” and “transfection”, “conjugation” and “transduction” are intended to refer to a variety of art-recognized techniques for introducing foreign nucleic acid (e.g., linear DNA or RNA (e.g., a linearized vector or a gene construct alone without a vector) or nucleic acid in the form of a vector (e.g., a plasmid, phage, phasmid, phagemid, transposon or other DNA) into a host cell, including calcium phosphate or calcium chloride co-precipitation, DEAE-dextran-mediated transfection, lipofection, natural competence, chemical-mediated transfer, or electroporation. Suitable methods for transforming or transfecting host cells can be found in Sambrook, et al. ( Molecular Cloning: A Laboratory Manual.  2 nd, ed., Cold Spring Harbor Laboratory , Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y., 1989), and other laboratory manuals.  
      For stable transfection of mammalian cells, it is known that, depending upon the expression vector and transfection technique used, only a small fraction of cells may integrate the foreign DNA into their genome. In order to identify and select these integrants, a gene that encodes a selectable marker (e.g., resistance to antibiotics) is generally introduced into the host cells along with the gene of interest. Preferred selectable markers include those which confer resistance to drugs, such as G418, hygromycin and methotrexate. Nucleic acid encoding a selectable marker can be introduced into a host cell on the same vector as that encoding an HA protein or can be introduced on a separate vector. Cells stably transfected with the introduced nucleic acid can be identified by, for example, drug selection (e.g., cells that have incorporated the selectable marker gene will survive, while the other cells die).  
      To create a homologous recombinant microorganism, a vector is prepared which contains at least a portion of an HA gene into which a deletion, addition or substitution has been introduced to thereby alter, e.g., functionally disrupt, the HA gene. Preferably, this HA gene is a  Corynebacterium glutamicum  HA gene, but it can be a homologue from a related bacterium or even from a mammalian, yeast, or insect source. In a preferred embodiment, the vector is designed such that, upon homologous recombination, the endogenous HA gene is functionally disrupted (i.e., no longer encodes a functional protein; also referred to as a “knock out” vector). Alternatively, the vector can be designed such that, upon homologous recombination, the endogenous HA gene is mutated or otherwise altered but still encodes functional protein (e.g., the upstream regulatory region can be altered to thereby alter the expression of the endogenous HA protein). In the homologous recombination vector, the altered portion of the HA gene is flanked at its 5′ and 3′ ends by additional nucleic acid of the HA gene to allow for homologous recombination to occur between the exogenous HA gene carried by the vector and an endogenous HA gene in a microorganism. The additional flanking HA nucleic acid is of sufficient length for successful homologous recombination with the endogenous gene. Typically, several kilobases of flanking DNA (both at the 5′ and 3′ ends) are included in the vector (see e.g., Thomas, K. R., and Capecchi, M. R. (1987) Cell 51: 503 for a description of homologous recombination vectors). The vector is introduced into a microorganism (e.g., by electroporation) and cells in which the introduced HA gene has homologously recombined with the endogenous HA gene are selected, using art-known techniques.  
      In another embodiment, recombinant microorganisms can be produced which contain selected systems which allow for regulated expression of the introduced gene. For example, inclusion of an HA gene on a vector placing it under control of the lac operon permits expression of the HA gene only in the presence of IPTG. Such regulatory systems are well known in the art.  
      In another embodiment, an endogenous HA gene in a host cell is disrupted (e.g., by homologous recombination or other genetic means known in the art) such that expression of its protein product does not occur. In another embodiment, an endogenous or introduced HA gene in a host cell has been altered by one or more point mutations, deletions, or inversions, but still encodes a functional HA protein. In still another embodiment, one or more of the regulatory regions (e.g., a promoter, repressor, or inducer) of an HA gene in a microorganism has been altered (e.g., by deletion, truncation, inversion, or point mutation) such that the expression of the HA gene is modulated. One of ordinary skill in the art will appreciate that host cells containing more than one of the described HA gene and protein modifications may be readily produced using the methods of the invention, and are meant to be included in the present invention.  
      A host cell of the invention, such as a prokaryotic or eukaryotic host cell in culture, can be used to produce (i.e., express) an HA protein. Accordingly, the invention further provides methods for producing HA proteins using the host cells of the invention. In one embodiment, the method comprises culturing the host cell of invention (into which a recombinant expression vector encoding an HA protein has been introduced, or into which genome has been introduced a gene encoding a wild-type or altered HA protein) in a suitable medium until HA protein is produced. In another embodiment, the method further comprises isolating HA proteins from the medium or the host cell.  
      C. Isolated HA Proteins  
      Another aspect of the invention pertains to isolated HA proteins, and biologically active portions thereof. An “isolated” or “purified” protein or biologically active portion thereof is substantially free of cellular material when produced by recombinant DNA techniques, or chemical precursors or other chemicals when chemically synthesized. The language “substantially free of cellular material” includes preparations of HA protein in which the protein is separated from cellular components of the cells in which it is naturally or recombinantly produced. In one embodiment, the language “substantially free of cellular material” includes preparations of HA protein having less than about 30% (by dry weight) of non-HA protein (also referred to herein as a “contaminating protein”), more preferably less than about 20% of non-HA protein, still more preferably less than about 10% of non-HA protein, and most preferably less than about 5% non-HA protein. When the HA protein or biologically active portion thereof is recombinantly produced, it is also preferably substantially free of culture medium, i.e., culture medium represents less than about 20%, more preferably less than about 10%, and most preferably less than about 5% of the volume of the protein preparation. The language “substantially free of chemical precursors or other chemicals” includes preparations of HA protein in which the protein is separated from chemical precursors or other chemicals which are involved in the synthesis of the protein. In one embodiment, the language “substantially free of chemical precursors or other chemicals” includes preparations of HA protein having less than about 30% (by dry weight) of chemical precursors or non-HA chemicals, more preferably less than about 20% chemical precursors or non-HA chemicals, still more preferably less than about 10% chemical precursors or non-HA chemicals, and most preferably less than about 5% chemical precursors or non-HA chemicals. In preferred embodiments, isolated proteins or biologically active portions thereof lack contaminating proteins from the same organism from which the HA protein is derived. Typically, such proteins are produced by recombinant expression of, for example, a  C. glutamicum  HA protein in a microorganism such as  C. glutamicum.    
      An isolated HA protein or a portion thereof of the invention can participate in the repair or recombination of DNA, in the transposition of genetic material, in gene expression (i.e., the processes of transcription or translation), in protein folding, or in protein secretion in  Corynebacterium glutamicum , or has one or more of the activities set forth in Table 1. In preferred embodiments, the protein or portion thereof comprises an amino acid sequence which is sufficiently homologous to an amino acid sequence of Appendix B such that the protein or portion thereof maintains the ability to participate in the maintenance of homeostasis in  C. glutamicum , or to perform a function involved in the adaptation of this microorganism to different environmental conditions. The portion of the protein is preferably a biologically active portion as described herein. In another preferred embodiment, an HA protein of the invention has an amino acid sequence shown in Appendix B. In yet another preferred embodiment, the HA protein has an amino acid sequence which is encoded by a nucleotide sequence which hybridizes, e.g., hybridizes under stringent conditions, to a nucleotide sequence of Appendix A. In still another preferred embodiment, the HA protein has an amino acid sequence which is encoded by a nucleotide sequence that is at least about 50%, 51%, 52%, 53%, 54%, 55%, 56%, 57%, 58%, 59%, or 60%, preferably at least about 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, or 70%, more preferably at least about 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, or 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, or 90%, or 91%, 92%, 93%, 94%, and even more preferably at least about 95%, 96%, 97%, 98%, 99% % or more homologous to one of the nucleic acid sequences of Appendix A, or a portion thereof. Ranges and identity values intermediate to the above-recited values, (e.g., 70-90% identical or 80-95% identical) are also intended to be encompassed by the present invention. For example, ranges of identity values using a combination of any of the above values recited as upper and/or lower limits are intended to be included. The preferred HA proteins of the present invention also preferably possess at least one of the HA activities described herein. For example, a preferred HA protein of the present invention includes an amino acid sequence encoded by a nucleotide sequence which hybridizes, e.g., hybridizes under stringent conditions, to a nucleotide sequence of Appendix A, and which can participate in the maintenance of homeostasis in  C. glutamicum , or can perform a function involved in the adaptation of this microorganism to different environmental conditions, or which has one or more of the activities set forth in Table 1.  
      In other embodiments, the HA protein is substantially homologous to an amino acid sequence of Appendix B and retains the functional activity of the protein of one of the sequences of Appendix B yet differs in amino acid sequence due to natural variation or mutagenesis, as described in detail in subsection I above. Accordingly, in another embodiment, the HA protein is a protein which comprises an amino acid sequence which is at least about 50%, 51%, 52%, 53%, 54%, 55%, 56%, 57%, 58%, 59%, or 60%, preferably at least about 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, or 70%, more preferably at least about 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, or 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, or 90%, or 91%, 92%, 93%, 94%, and even more preferably at least about 95%, 96%, 97%, 98%, 99% or more homologous to an entire amino acid sequence of Appendix B and which has at least one of the HA activities described herein. Ranges and identity values intermediate to the above-recited values, (e.g., 70-90% identical or 80-95% identical) are also intended to be encompassed by the present invention. For example, ranges of identity values using a combination of any of the above values recited as upper and/or lower limits are intended to be included. In another embodiment, the invention pertains to a full length  C. glutamicum  protein which is substantially homologous to an entire amino acid sequence of Appendix B.  
      Biologically active portions of an HA protein include peptides comprising amino acid sequences derived from the amino acid sequence of an HA protein, e.g., the an amino acid sequence shown in Appendix B or the amino acid sequence of a protein homologous to an HA protein, which include fewer amino acids than a full length HA protein or the full length protein which is homologous to an HA protein, and exhibit at least one activity of an HA protein. Typically, biologically active portions (peptides, e.g., peptides which are, for example, 5, 10, 15, 20, 30, 35, 36, 37, 38, 39, 40, 50, 100 or more amino acids in length) comprise a domain or motif with at least one activity of an HA protein. Moreover, other biologically active portions, in which other regions of the protein are deleted, can be prepared by recombinant techniques and evaluated for one or more of the activities described herein. Preferably, the biologically active portions of an HA protein include one or more selected domains/motifs or portions thereof having biological activity.  
      HA proteins are preferably produced by recombinant DNA techniques. For example, a nucleic acid molecule encoding the protein is cloned into an expression vector (as described above), the expression vector is introduced into a host cell (as described above) and the HA protein is expressed in the host cell. The HA protein can then be isolated from the cells by an appropriate purification scheme using standard protein purification techniques. Alternative to recombinant expression, an HA protein, polypeptide, or peptide can be synthesized chemically using standard peptide synthesis techniques. Moreover, native HA protein can be isolated from cells (e.g., endothelial cells), for example using an anti-HA antibody, which can be produced by standard techniques utilizing an HA protein or fragment thereof of this invention.  
      The invention also provides HA chimeric or fusion proteins. As used herein, an HA “chimeric protein” or “fusion protein” comprises an HA polypeptide operatively linked to a non-HA polypeptide. An “HA polypeptide” refers to a polypeptide having an amino acid sequence corresponding to an HA protein, whereas a “non-HA polypeptide” refers to a polypeptide having an amino acid sequence corresponding to a protein which is not substantially homologous to the HA protein, e.g., a protein which is different from the HA protein and which is derived from the same or a different organism. Within the fusion protein, the term “operatively linked” is intended to indicate that the HA polypeptide and the non-HA polypeptide are fused in-frame to each other. The non-HA polypeptide can be fused to the N-terminus or C-terminus of the HA polypeptide. For example, in one embodiment the fusion protein is a GST-HA fusion protein in which the HA sequences are fused to the C-terminus of the GST sequences. Such fusion proteins can facilitate the purification of recombinant HA proteins. In another embodiment, the fusion protein is an HA protein containing a heterologous signal sequence at its N-terminus. In certain host cells (e.g., mammalian host cells), expression and/or secretion of an HA protein can be increased through use of a heterologous signal sequence.  
      Preferably, an HA chimeric or fusion protein of the invention is produced by standard recombinant DNA techniques. For example, DNA fragments coding for the different polypeptide sequences are ligated together in-frame in accordance with conventional techniques, for example by employing blunt-ended or stagger-ended termini for ligation, restriction enzyme digestion to provide for appropriate termini, filling-in of cohesive ends as appropriate, alkaline phosphatase treatment to avoid undesirable joining, and enzymatic ligation. In another embodiment, the fusion gene can be synthesized by conventional techniques including automated DNA synthesizers. Alternatively, PCR amplification of gene fragments can be carried out using anchor primers which give rise to complementary overhangs between two consecutive gene fragments which can subsequently be annealed and reamplified to generate a chimeric gene sequence (see, for example,  Current Protocols in Molecular Biology , eds. Ausubel et al. John Wiley &amp; Sons: 1992). Moreover, many expression vectors are commercially available that already encode a fusion moiety (e.g., a GST polypeptide). An HA-encoding nucleic acid can be cloned into such an expression vector such that the fusion moiety is linked in-frame to the HA protein.  
      Homologues of the HA protein can be generated by mutagenesis, e.g., discrete point mutation or truncation of the HA protein. As used herein, the term “homologue” refers to a variant form of the HA protein which acts as an agonist or antagonist of the activity of the HA protein. An agonist of the HA protein can retain substantially the same, or a subset, of the biological activities of the HA protein. An antagonist of the HA protein can inhibit one or more of the activities of the naturally occurring form of the HA protein, by, for example, competitively binding to a downstream or upstream member of a biochemical cascade which includes the HA protein, by binding to a target molecule with which the HA protein interacts, such that no functional interaction is possible, or by binding directly to the HA protein and inhibiting its normal activity.  
      In an alternative embodiment, homologues of the HA protein can be identified by screening combinatorial libraries of mutants, e.g., truncation mutants, of the HA protein for HA protein agonist or antagonist activity. In one embodiment, a variegated library of HA variants is generated by combinatorial mutagenesis at the nucleic acid level and is encoded by a variegated gene library. A variegated library of HA variants can be produced by, for example, enzymatically ligating a mixture of synthetic oligonucleotides into gene sequences such that a degenerate set of potential HA sequences is expressible as individual polypeptides, or alternatively, as a set of larger fusion proteins (e.g., for phage display) containing the set of HA sequences therein. There are a variety of methods which can be used to produce libraries of potential HA homologues from a degenerate oligonucleotide sequence. Chemical synthesis of a degenerate gene sequence can be performed in an automatic DNA synthesizer, and the synthetic gene then ligated into an appropriate expression vector. Use of a degenerate set of genes allows for the provision, in one mixture, of all of the sequences encoding the desired set of potential HA sequences. Methods for synthesizing degenerate oligonucleotides are known in the art (see, e.g., Narang, S. A. (1983)  Tetrahedron  39:3; Itakura et al. (1984)  Annu. Rev. Biochem.  53:323; Itakura et al. (1984)  Science  198:1056; Ike et al. (1983)  Nucleic Acid Res.  11:477.  
      In addition, libraries of fragments of the HA protein coding can be used to generate a variegated population of HA fragments for screening and subsequent selection of homologues of an HA protein. In one embodiment, a library of coding sequence fragments can be generated by treating a double stranded PCR fragment of an HA coding sequence with a nuclease under conditions wherein nicking occurs only about once per molecule, denaturing the double stranded DNA, renaturing the DNA to form double stranded DNA which can include sense/antisense pairs from different nicked products, removing single stranded portions from reformed duplexes by treatment with S1 nuclease, and ligating the resulting fragment library into an expression vector. By this method, an expression library can be derived which encodes N-terminal, C-terminal and internal fragments of various sizes of the HA protein.  
      Several techniques are known in the art for screening gene products of combinatorial libraries made by point mutations or truncation, and for screening cDNA libraries for gene products having a selected property. Such techniques are adaptable for rapid screening of the gene libraries generated by the combinatorial mutagenesis of HA homologues. The most widely used techniques, which are amenable to high through-put analysis, for screening large gene libraries typically include cloning the gene library into replicable expression vectors, transforming appropriate cells with the resulting library of vectors, and expressing the combinatorial genes under conditions in which detection of a desired activity facilitates isolation of the vector encoding the gene whose product was detected. Recursive ensemble mutagenesis (REM), a new technique which enhances the frequency of functional mutants in the libraries, can be used in combination with the screening assays to identify HA homologues (Arkin and Yourvan (1992)  PNAS  89:7811-7815; Delgrave et al. (1993)  Protein Engineering  6(3):327-331).  
      In another embodiment, cell based assays can be exploited to analyze a variegated HA library, using methods well known in the art.  
      D. Uses and Methods of the Invention  
      The nucleic acid molecules, proteins, protein homologues, fusion proteins, primers, vectors, and host cells described herein can be used in one or more of the following methods: identification of  C. glutamicum  and related organisms; mapping of genomes of organisms related to  C. glutamicum ; identification and localization of  C. glutamicum  sequences of interest; evolutionary studies; determination of HA protein regions required for function; modulation of an HA protein activity; modulation of the metabolism of one or more inorganic compounds; modulation of the modification or degradation of one or more aromatic or aliphatic compounds; modulation of cell wall synthesis or rearrangements; modulation of enzyme activity or proteolysis; and modulation of cellular production of a desired compound, such as a fine chemical.  
      The HA nucleic acid molecules of the invention have a variety of uses. First, they may be used to identify an organism as being  Corynebacterium glutamicum  or a close relative thereof. Also, they may be used to identify the presence of  C. glutamicum  or a relative thereof in a mixed population of microorganisms. The invention provides the nucleic acid sequences of a number of  C. glutamicum  genes; by probing the extracted genomic DNA of a culture of a unique or mixed population of microorganisms under stringent conditions with a probe spanning a region of a  C. glutamicum  gene which is unique to this organism, one can ascertain whether this organism is present. Although  Corynebacterium glutamicum  itself is nonpathogenic, it is related to pathogenic species, such as  Corynebacterium diphtheriae. Corynebacterium diphtheriae  is the causative agent of diphtheria, a rapidly developing, acute, febrile infection which involves both local and systemic pathology. In this disease, a local lesion develops in the upper respiratory tract and involves necrotic injury to epithelial cells; the bacilli secrete toxin which is disseminated through this lesion to distal susceptible tissues of the body. Degenerative changes brought about by the inhibition of protein synthesis in these tissues, which include heart, muscle, peripheral nerves, adrenals, kidneys, liver and spleen, result in the systemic pathology of the disease. Diphtheria continues to have high incidence in many parts of the world, including Africa, Asia, Eastern Europe and the independent states of the former Soviet Union. An ongoing epidemic of diphtheria in the latter two regions has resulted in at least 5,000 deaths since 1990.  
      In one embodiment, the invention provides a method of identifying the presence or activity of  Cornyebacterium diphtheriae  in a subject. This method includes detection of one or more of the nucleic acid or amino acid sequences of the invention (e.g., the sequences set forth in Appendix A or Appendix B) in a subject, thereby detecting the presence or activity of  Corynebacterium diphtheriae  in the subject.  C. glutamicum  and  C. diphtheriae  are related bacteria, and many of the nucleic acid and protein molecules in  C. glutamicum  are homologous to  C. diphtheriae  nucleic acid and protein molecules, and can therefore be used to detect  C. diphtheriae  in a subject.  
      The nucleic acid and protein molecules of the invention may also serve as markers for specific regions of the genome. This has utility not only in the mapping of the genome, but also for functional studies of  C. glutamicum  proteins. For example, to identify the region of the genome to which a particular  C. glutamicum  DNA-binding protein binds, the  C. glutamicum  genome could be digested, and the fragments incubated with the DNA-binding protein. Those which bind the protein may be additionally probed with the nucleic acid molecules of the invention, preferably with readily detectable labels; binding of such a nucleic acid molecule to the genome fragment enables the localization of the fragment to the genome map of  C. glutamicum , and, when performed multiple times with different enzymes, facilitates a rapid determination of the nucleic acid sequence to which the protein binds. Further, the nucleic acid molecules of the invention may be sufficiently homologous to the sequences of related species such that these nucleic acid molecules may serve as markers for the construction of a genomic map in related bacteria, such as  Brevibacterium lactofermentum.    
      The HA nucleic acid molecules of the invention are also useful for evolutionary and protein structural studies. The processes involved in adaptation and the maintenance of homeostasis in which the molecules of the invention participate are utilized by a wide variety of species; by comparing the sequences of the nucleic acid molecules of the present invention to those encoding similar enzymes from other organisms, the evolutionary relatedness of the organisms can be assessed. Similarly, such a comparison permits an assessment of which regions of the sequence are conserved and which are not, which may aid in determining those regions of the protein which are essential for the functioning of the enzyme. This type of determination is of value for protein engineering studies and may give an indication of what the protein can tolerate in terms of mutagenesis without losing function.  
      Manipulation of the HA nucleic acid molecules of the invention may result in the production of HA proteins having functional differences from the wild-type HA proteins. These proteins may be improved in efficiency or activity, may be present in greater numbers in the cell than is usual, or may be decreased in efficiency or activity.  
      The invention provides methods for screening molecules which modulate the activity of an HA protein, either by interacting with the protein itself or a substrate or binding partner of the HA protein, or by modulating the transcription or translation of an HA nucleic acid molecule of the invention. In such methods, a microorganism expressing one or more HA proteins of the invention is contacted with one or more test compounds, and the effect of each test compound on the activity or level of expression of the HA protein is assessed.  
      The modulation of activity or number of HA proteins involved in cell wall biosynthesis or rearrangements may impact the production, yield, and/or efficiency of production of one or more fine chemicals from  C. glutamicum  cells. For example, by altering the activity of these proteins, it may be possible to modulate the structure or thickness of the cell wall. The cell wall serves in large measure as a protective device against osmotic lysis and external sources of injury; by modifying the cell wall it may be possible to increase the ability of  C. glutamicum  to withstand the mechanical and shear force stresses encountered by this microorganism during large-scale fermentor culture. Further, each  C. glutamicum  cell is surrounded by a thick cell wall, and thus, a significant portion of the biomass present in large scale culture consists of cell wall. By increasing the rate at which the cell wall is synthesized or by activating cell wall synthesis (through genetic engineering of the HA cell wall proteins of the invention) it may be possible to improve the growth rate of the microorganism. Similarly, by decreasing the activity or number of proteins involved in the degradation of cell wall or by decreasing the repression of cell wall biosynthesis, an overall increase in cell wall production may be achieved. An increase in the number of viable  C. glutamicum  cells (as may be accomplished by any of the foregoing described protein alterations) should result in increased numbers of cells producing the desired fine chemical in large-scale fermentor culture, which should permit increased yields or efficiency of production of these compounds from the culture.  
      The modulation of activity or number of  C. glutamicum  HA proteins that participate in the modification or degradation of aromatic or aliphatic compounds may also have direct or indirect impacts on the production of one or more fine chemicals from these cells. Certain aromatic or aliphatic modification or degradation products are desirable fine chemicals (e.g., organic acids or modified aromatic and aliphatic compounds); thus, by modifying the enzymes which perform these modifications (e.g., hydroxylation, methylation, or isomerization) or degradation reactions, it may be possible to increase the yields of these desired compounds. Similarly, by decreasing the activity or number of proteins involved in pathways which further degrade the modified or breakdown products of the aforementioned reactions it may be possible to improve the yields of these fine chemicals from  C. glutamicum  cells in culture.  
      These aromatic and aliphatic modification and degradative enzymes are themselves fine chemicals. In purified form, these enzymes may be used to degrade aromatic and aliphatic compounds (e.g., toxic chemicals such as petroleum products), either for the bioremediation of polluted sites, for the engineered decomposition of wastes, or for the large-scale and economically feasible production of desired modified aromatic or aliphatic compounds or their breakdown products, some of which may be conveniently used as carbon or energy sources for other fine chemical-producing compounds in culture (see, e.g., Faber, K. (1995) Biotransformations in Organic Chemistry, Springer: Berlin and references therein; and Roberts, S. M., ed. (1992-1996) Preparative Biotransformations, Wiley: Chichester, and references therein). By genetically altering these proteins such that their regulation by other cellular mechanisms is lessened or abolished, it may be possible to increase the overall number or activity of these proteins, thereby improving not only the yield of these fine chemicals but also the activity of these harvested proteins.  
      The modification of these aromatic and aliphatic modifying and degradation enzymes may also have an indirect effect on the production of one or more fine chemical. Many aromatic and aliphatic compounds (such as those that may be encountered as impurities in culture media or as waste products from cellular metabolism) are toxic to cells; by modifying and/or degrading these compounds such that they may be readily removed or destroyed, cellular viability should be increased. Further, these enzymes may modify or degrade these compounds in such a manner that the resulting products may enter the normal carbon metabolism pathways of the cell, thus rendering the cell able to use these compounds as alternate carbon or energy sources. In large-scale culture situations, when there may be limiting amounts of optimal carbon sources, these enzymes provide a method by which cells may continue to grow and divide using aromatic or aliphatic compounds as nutrients. In either case, the resulting increase in the number of  C. glutamicum  cells in the culture producing the desired fine chemical should in turn result in increased yields or efficiency of production of the fine chemical(s).  
      Modifications in activity or number of HA proteins involved in the metabolism of inorganic compounds may also directly or indirectly affect the production of one or more fine chemicals from  C. glutamicum  or related bacterial cultures. For example, many desirable fine chemicals, such as nucleic acids, amino acids, cofactors and vitamins (e.g., thiamine, biotin, and lipoic acid) cannot be synthesized without inorganic molecules such as phosphorous, nitrate, sulfate, and iron. The inorganic metabolism proteins of the invention permit the cell to obtain these molecules from a variety of inorganic compounds and to divert them into various fine chemical biosynthetic pathways. Therefore, by increasing the activity or number of enzymes involved in the metabolism of these inorganic compounds, it may be possible to increase the supply of these possibly limiting inorganic molecules, thereby directly increasing the production or efficiency of production of various fine chemicals from  C. glutamicum  cells containing such altered proteins. Modification of the activity or number of inorganic metabolism enzymes of the invention may also render  C. glutamicum  able to better utilize limited inorganic compound supplies, or to utilize nonoptimal inorganic compounds to synthesize amino acids, vitamins, cofactors, or nucleic acids, all of which are necessary for continued growth and replication of the cell. By improving the viability of these cells in large-scale culture, the number of  C. glutamicum  cells producing one or more fine chemicals in the culture may also be increased, in turn increasing the yields or efficiency of production of one or more fine chemicals.  
       C. glutamicum  enzymes for general processes are themselves desirable fine chemicals. The specific properties of enzymes (i.e., regio- and stereospecificity, among others) make them useful catalysts for chemical reactions in vitro. Either whole  C. glutamicum  cells may be incubated with an appropriate substrate such that the desired product is produced by enzymes in the cell, or the desired enzymes may be overproduced and purified from  C. glutamicum  cultures (or those of a related bacterium) and subsequently utilized in in vitro reactions in an industrial setting (either in solution or immobilized on a suitable immobile phase). In either situation, the enzyme can either be a natural  C. glutamicum  protein, or it may be mutagenized to have an altered activity; typical industrial uses for such enzymes include as catalysts in the chemical industry (e.g., for synthetic organic chemistry) as food additives, as feed components, for fruit processing, for leather preparation, in detergents, in analysis and medicine, and in the textile industry (see, e.g., Yamada, H. (1993) “Microbial reactions for the production of useful organic compounds,”  Chimica  47: 5-10; Roberts, S. M. (1998) Preparative biotransformations: the employment of enzymes and whole-cells in synthetic chemistry,”  J. Chem. Soc. Perkin Trans.  1: 157-169; Zaks, A. and Dodds, D. R. (1997) “Application of biocatalysis and biotransformations to the synthesis of pharmaceuticals,” DDT2: 513-531; Roberts, S. M. and Williamson, N. M. (1997) “The use of enzymes for the preparation of biologically active natural products and analogues in optically active form,”  Curr. Organ. Chemistry  1:1-20; Faber, K. (1995) Biotransformations in Organic Chemistry, Springer: Berlin; Roberts, S. M., ed. (1992-96) Preparative Biotransformations, Wiley: Chichester; Cheetham, P. S. J. (1995) “The applications of enzymes in industry” in: Handbook of Enzyme Biotechnology, 3 rd  ed., Wiseman, A., ed., Elis: Horwood, p. 419-552; and Ullmann&#39;s Encyclopedia of Industrial Chemistry (1987), vol. A9, Enzymes, p. 390-457). Thus, by increasing the activity or number of these enzymes, it may be possible to also increase the ability of the cell to convert supplied substrates to desired products, or to overproduce these enzymes for increased yields in large-scale culture. Further, by mutagenizing these proteins it may be possible to remove feedback inhibition or other repressive cellular regulatory controls such that greater numbers of these enzymes may be produced and activated by the cell, thereby leading to greater yields, production, or efficiency of production of these fine chemical proteins from large-scale cultures. Further, manipulation of these enzymes may alter the activity of one or more  C. glutamicum  metabolic pathways, such as those for the biosynthesis or secretion of one or more fine chemicals.  
      Mutagenesis of the proteolytic enzymes of the invention such that they are altered in activity or number may also directly or indirectly affect the yield, production, and/or efficiency of production of one or more fine chemicals from  C. glutamicum . For example, by increasing the activity or number of these proteins, it may be possible to increase the ability of the bacterium to survive in large-scale culture, due to an increased ability of the cell to rapidly degrade proteins misfolded in response to the high temperatures, nonoptimal pH, and other stresses encountered during fermentor culture. Increased numbers of cells in these cultures may result in increased yields or efficiency of production of one or more desired fine chemicals, due to the relatively larger number of cells producing these compounds in the culture. Also,  C. glutamicum  cells possess multiple cell-surface proteases which serve to break down external nutrients into molecules which may be more readily incorporated by the cells as carbon/energy sources or nutrients of other kinds. An increase in activity or number of these enzymes may improve this turnover and increase the levels of available nutrients, thereby improving cell growth or production. Thus, modifications of the proteases of the invention may indirectly impact  C. glutamicum  fine chemical production.  
      A more direct impact on fine chemical production in response to the modification of one or more of the proteases of the invention may occur when these proteases are involved in the production or degradation of a desired fine chemical. By decreasing the activity of a protease which degrades a fine chemical or a protein involved in the synthesis of a fine chemical it may be possible to increase the levels of that fine chemical (due to the decreased degradation or increased synthesis of the compound). Similarly, by increasing the activity of a protease which degrades a compound to result in a fine chemical or a protein involved in the degradation of a fine chemical, a similar result should be achieved: increased levels of the desired fine chemical from  C. glutamicum  cells containing these engineered proteins.  
      The aforementioned mutagenesis strategies for HA proteins to result in increased yields of a fine chemical from  C. glutamicum  are not meant to be limiting; variations on these strategies will be readily apparent to one of ordinary skill in the art. Using such strategies, and incorporating the mechanisms disclosed herein, the nucleic acid and protein molecules of the invention may be utilized to generate  C. glutamicum  or related strains of bacteria expressing mutated HA nucleic acid and protein molecules such that the yield, production, and/or efficiency of production of a desired compound is improved. This desired compound may be any product produced by  C. glutamicum , which includes the final products of biosynthesis pathways and intermediates of naturally-occurring metabolic pathways, as well as molecules which do not naturally occur in the metabolism of  C. glutamicum , but which are produced by a  C. glutamicum  strain of the invention.  
      This invention is further illustrated by the following examples which should not be construed as limiting. The contents of all references, patent applications, patents, published patent applications, Tables, Appendices, and the sequence listing cited throughout this application are hereby incorporated by reference.  
     EXEMPLIFICATION  
     Example 1  
     Preparation of Total Genomic DNA of  Corynebacterium glutamicum  ATCC 13032  
      A culture of  Corynebacterium glutamicum  (ATCC 13032) was grown overnight at 30° C. with vigorous shaking in BHI medium (Difco). The cells were harvested by centrifugation, the supernatant was discarded and the cells were resuspended in 5 ml buffer-I (5% of the original volume of the culture—all indicated volumes have been calculated for 100 ml of culture volume). Composition of buffer-I: 140.34 g/l sucrose, 2.46 g/l MgSO 4 x7H 2 O, 10 ml/l KH 2 PO 4  solution (100 g/l, adjusted to pH 6.7 with KOH), 50 ml/l M12 concentrate (10 g/l (NH 4 ) 2 SO 4 , 1 g/l NaCl, 2 g/l MgSO 4 x7H 2 O, 0.2 g/l CaCl 2 , 0.5 g/l yeast extract (Difco), 10 ml/l trace-elements-mix (200 mg/l FeSO 4 xH 2 O, 10 mg/l ZnSO 4 x7H 2 O, 3 mg/l MnCl 2 x4H 2 O, 30 mg/l H 3 BO 3  20 mg/l CoCl 2 x6H 2 O, 1 mg/l NiCl 2 x6H 2 O, 3 mg/l Na 2 MoO 4 x2H 2 O, 500 mg/l complexing agent (EDTA or critic acid), 100 ml/l vitamins-mix (0.2 mg/l biotin, 0.2 mg/l folic acid, 20 mg/l p-amino benzoic acid, 20 mg/l riboflavin, 40 mg/l ca-panthothenate, 140 mg/l nicotinic acid, 40 mg/l pyridoxole hydrochloride, 200 mg/l myo-inositol). Lysozyme was added to the suspension to a final concentration of 2.5 mg/ml. After an approximately 4 h incubation at 37° C., the cell wall was degraded and the resulting protoplasts are harvested by centrifugation. The pellet was washed once with 5 ml buffer-I and once with 5 ml TE-buffer (10 mM Tris-HCl, 1 mM EDTA, pH 8). The pellet was resuspended in 4 ml TE-buffer and 0.5 ml SDS solution (10%) and 0.5 ml NaCl solution (5 M) are added. After adding of proteinase K to a final concentration of 200 μg/ml, the suspension is incubated for ca. 18 h at 37° C. The DNA was purified by extraction with phenol, phenol-chloroform-isoamylalcohol and chloroform-isoamylalcohol using standard procedures. Then, the DNA was precipitated by adding 1/50 volume of 3 M sodium acetate and 2 volumes of ethanol, followed by a 30 min incubation at −20° C. and a 30 min centrifugation at 12,000 rpm in a high speed centrifuge using a SS34 rotor (Sorvall). The DNA was dissolved in 1 ml TE-buffer containing 20 μg/ml RNaseA and dialysed at 4° C. against 1000 ml TE-buffer for at least 3 hours. During this time, the buffer was exchanged 3 times. To aliquots of 0.4 ml of the dialysed DNA solution, 0.4 ml of 2 M LiCl and 0.8 ml of ethanol are added. After a 30 min incubation at −20° C., the DNA was collected by centrifugation (13,000 rpm, Biofuge Fresco, Heraeus, Hanau, Germany). The DNA pellet was dissolved in TE-buffer. DNA prepared by this procedure could be used for all purposes, including southern blotting or construction of genomic libraries.  
     Example 2  
     Construction of Genomic Libraries in  Escherichia coli  of  Corynebacterium glutamicum  ATCC13032  
      Using DNA prepared as described in Example 1, cosmid and plasmid libraries were constructed according to known and well established methods (see e.g., Sambrook, J. et al. (1989) “Molecular Cloning: A Laboratory Manual”, Cold Spring Harbor Laboratory Press, or Ausubel, F. M. et al. (1994) “Current Protocols in Molecular Biology”, John Wiley &amp; Sons.)  
      Any plasmid or cosmid could be used. Of particular use were the plasmids pBR322 (Sutcliffe, J. G. (1979)  Proc. Natl. Acad. Sci. USA,  75:3737-3741); pACYC177 (Change &amp; Cohen (1978)  J. Bacteriol  134:1141-1156), plasmids of the pBS series (pBSSK+, pBSSK− and others; Stratagene, LaJolla, USA), or cosmids as SuperCos1 (Stratagene, LaJolla, USA) or Lorist6 (Gibson, T. J., Rosenthal A. and Waterson, R. H. (1987)  Gene  53:283-286. Gene libraries specifically for use in  C. glutamicum  may be constructed using plasmid pSL109 (Lee, H.-S. and A. J. Sinskey (1994)  J. Microbiol. Biotechnol.  4: 256-263).  
     Example 3  
     DNA Sequencing and Computational Functional Analysis  
      Genomic libraries as described in Example 2 were used for DNA sequencing according to standard methods, in particular by the chain termination method using ABI377 sequencing machines (see e.g., Fleischman, R. D. et al. (1995) “Whole-genome Random Sequencing and Assembly of  Haemophilus Influenzae  Rd., Science, 269:496-512). Sequencing primers with the following nucleotide sequences were used: 5′-GGAAACAGTATGACCATG-3′ or 5′-GTAAAACGACGGCCAGT-3′.  
     Example 4  
     In Vivo Mutagenesis  
      In vivo mutagenesis of  Corynebacterium glutamicum  can be performed by passage of plasmid (or other vector) DNA through  E. coli  or other microorganisms (e.g.  Bacillus  spp. or yeasts such as  Saccharomyces cerevisiae ) which are impaired in their capabilities to maintain the integrity of their genetic information. Typical mutator strains have mutations in the genes for the DNA repair system (e.g., mutHLS, mutD, mutT, etc.; for reference, see Rupp, W. D. (1996) DNA repair mechanisms, in:  Escherichia coli  and  Salmonella , p. 2277-2294, ASM: Washington.) Such strains are well known to those of ordinary skill in the art. The use of such strains is illustrated, for example, in Greener, A. and Callahan, M. (1994)  Strategies  7: 32-34.  
     Example 5  
     DNA Transfer Between  Escherichia coli  and  Corynebacterium glutamicum    
      Several  Corynebacterium  and  Brevibacterium  species contain endogenous plasmids (as e.g., pHM1519 or pBL1) which replicate autonomously (for review see, e.g., Martin, J. F. et al. (1987)  Biotechnology,  5:137-146). Shuttle vectors for  Escherichia coli  and  Corynebacterium glutamicum  can be readily constructed by using standard vectors for  E. coli  (Sambrook, J. et al. (1989), “Molecular Cloning: A Laboratory Manual”, Cold Spring Harbor Laboratory Press or Ausubel, F. M. et al. (1994) “Current Protocols in Molecular Biology”, John Wiley &amp; Sons) to which a origin or replication for and a suitable marker from  Corynebacterium glutamicum  is added. Such origins of replication are preferably taken from endogenous plasmids isolated from  Corynebacterium  and  Brevibacterium  species. Of particular use as transformation markers for these species are genes for kanamycin resistance (such as those derived from the Tn5 or Tn903 transposons) or chloramphenicol (Winnacker, E. L. (1987) “From Genes to Clones—Introduction to Gene Technology, VCH, Weinheim). There are numerous examples in the literature of the construction of a wide variety of shuttle vectors which replicate in both  E. coli  and  C. glutamicum , and which can be used for several purposes, including gene over-expression (for reference, see e.g., Yoshihama, M. et al. (1985)  J. Bacteriol.  162:591-597, Martin J. F. et al. (1987)  Biotechnology,  5:137-146 and Eikmanns, B. J. et al. (1991)  Gene,  102:93-98).  
      Using standard methods, it is possible to clone a gene of interest into one of the shuttle vectors described above and to introduce such a hybrid vectors into strains of  Corynebacterium glutamicum . Transformation of  C. glutamicum  can be achieved by protoplast transformation (Kastsumata, R. et al. (1984)  J. Bacteriol.  159306-311), electroporation (Liebl, E. et al. (1989)  FEMS Microbiol. Letters,  53:399-303) and in cases where special vectors are used, also by conjugation (as described e.g. in Schafer, A et al. (1990)  J. Bacteriol.  172:1663-1666). It is also possible to transfer the shuttle vectors for  C. glutamicum  to  E. coli  by preparing plasmid DNA from  C. glutamicum  (using standard methods well-known in the art) and transforming it into  E. coli . This transformation step can be performed using standard methods, but it is advantageous to use an Mcr-deficient  E. coli  strain, such as NM522 (Gough &amp; Murray (1983)  J. Mol. Biol.  166:1-19).  
      Genes may be overexpressed in  C. glutamicum  strains using plasmids which comprise pCG1 (U.S. Pat. No. 4,617,267) or fragments thereof, and optionally the gene for kanamycin resistance from TN903 (Grindley, N. D. and Joyce, C. M. (1980)  Proc. Natl. Acad. Sci. USA  77(12): 7176-7180). In addition, genes may be overexpressed in  C. glutamicum  strains using plasmid pSL109 (Lee, H.-S. and A. J. Sinskey (1994)  J. Microbiol. Biotechnol.  4: 256-263).  
      Aside from the use of replicative plasmids, gene overexpression can also be achieved by integration into the genome. Genomic integration in  C. glutamicum  or other  Corynebacterium  or  Brevibacterium  species may be accomplished by well-known methods, such as homologous recombination with genomic region(s), restriction endonuclease mediated integration (REMI) (see, e.g., DE Patent 19823834), or through the use of transposons. It is also possible to modulate the activity of a gene of interest by modifying the regulatory regions (e.g., a promoter, a repressor, and/or an enhancer) by sequence modification, insertion, or deletion using site-directed methods (such as homologous recombination) or methods based on random events (such as transposon mutagenesis or REMI). Nucleic acid sequences which function as transcriptional terminators may also be inserted 3′ to the coding region of one or more genes of the invention; such terminators are well-known in the art and are described, for example, in Winnacker, E. L. (1987) From Genes to Clones—Introduction to Gene Technology. VCH: Weinheim.  
     Example 6  
     Assessment of the Expression of the Mutant Protein  
      Observations of the activity of a mutated protein in a transformed host cell rely on the fact that the mutant protein is expressed in a similar fashion and in a similar quantity to that of the wild-type protein. A useful method to ascertain the level of transcription of the mutant gene (an indicator of the amount of mRNA available for translation to the gene product) is to perform a Northern blot (for reference see, for example, Ausubel et al. (1988) Current Protocols in Molecular Biology, Wiley: New York), in which a primer designed to bind to the gene of interest is labeled with a detectable tag (usually radioactive or chemiluminescent), such that when the total RNA of a culture of the organism is extracted, run on gel, transferred to a stable matrix and incubated with this probe, the binding and quantity of binding of the probe indicates the presence and also the quantity of mRNA for this gene. This information is evidence of the degree of transcription of the mutant gene. Total cellular RNA can be prepared from  Corynebacterium glutamicum  by several methods, all well-known in the art, such as that described in Bormann, E. R. et al. (1992)  Mol. Microbiol.  6: 317-326.  
      To assess the presence or relative quantity of protein translated from this mRNA, standard techniques, such as a Western blot, may be employed (see, for example, Ausubel et al. (1988) Current Protocols in Molecular Biology, Wiley: New York). In this process, total cellular proteins are extracted, separated by gel electrophoresis, transferred to a matrix such as nitrocellulose, and incubated with a probe, such as an antibody, which specifically binds to the desired protein. This probe is generally tagged with a chemiluminescent or colorimetric label which may be readily detected. The presence and quantity of label observed indicates the presence and quantity of the desired mutant protein present in the cell.  
     Example 7  
     Growth of Genetically Modified  Corynebacterium glutamicum —Media and Culture Conditions  
      Genetically modified  Corynebacteria  are cultured in synthetic or natural growth media. A number of different growth media for  Corynebacteria  are both well-known and readily available (Lieb et al. (1989)  Appl. Microbiol. Biotechnol.,  32:205-210; von der Osten et al. (1998)  Biotechnology Letters,  11:11-16; Patent DE 4,120,867; Liebl (1992) “The Genus  Corynebacterium , in: The Procaryotes, Volume II, Balows, A. et al., eds. Springer-Verlag). These media consist of one or more carbon sources, nitrogen sources, inorganic salts, vitamins and trace elements. Preferred carbon sources are sugars, such as mono-, di-, or polysaccharides. For example, glucose, fructose, mannose, galactose, ribose, sorbose, ribulose, lactose, maltose, sucrose, raffinose, starch or cellulose serve as very good carbon sources. It is also possible to supply sugar to the media via complex compounds such as molasses or other by-products from sugar refinement. It can also be advantageous to supply mixtures of different carbon sources. Other possible carbon sources are alcohols and organic acids, such as methanol, ethanol, acetic acid or lactic acid. Nitrogen sources are usually organic or inorganic nitrogen compounds, or materials which contain these compounds. Exemplary nitrogen sources include ammonia gas or ammonia salts, such as NH 4 Cl or (NH 4 ) 2 SO 4 , NH 4 OH, nitrates, urea, amino acids or complex nitrogen sources like corn steep liquor, soy bean flour, soy bean protein, yeast extract, meat extract and others.  
      Inorganic salt compounds which may be included in the media include the chloride-, phosphorous- or sulfate-salts of calcium, magnesium, sodium, cobalt, molybdenum, potassium, manganese, zinc, copper and iron. Chelating compounds can be added to the medium to keep the metal ions in solution. Particularly useful chelating compounds include dihydroxyphenols, like catechol or protocatechuate, or organic acids, such as citric acid. It is typical for the media to also contain other growth factors, such as vitamins or growth promoters, examples of which include biotin, riboflavin, thiamin, folic acid, nicotinic acid, pantothenate and pyridoxin. Growth factors and salts frequently originate from complex media components such as yeast extract, molasses, corn steep liquor and others. The exact composition of the media compounds depends strongly on the immediate experiment and is individually decided for each specific case. Information about media optimization is available in the textbook “Applied Microbiol. Physiology, A Practical Approach (eds. P. M. Rhodes, P. F. Stanbury, IRL Press (1997) pp. 53-73, ISBN 0 19 963577 3). It is also possible to select growth media from commercial suppliers, like standard 1 (Merck) or BHI (grain heart infusion, DIFCO) or others.  
      All medium components are sterilized, either by heat (20 minutes at 1.5 bar and 121° C.) or by sterile filtration. The components can either be sterilized together or, if necessary, separately. All media components can be present at the beginning of growth, or they can optionally be added continuously or batchwise.  
      Culture conditions are defined separately for each experiment. The temperature should be in a range between 15° C. and 45° C. The temperature can be kept constant or can be altered during the experiment. The pH of the medium should be in the range of 5 to 8.5, preferably around 7.0, and can be maintained by the addition of buffers to the media. An exemplary buffer for this purpose is a potassium phosphate buffer. Synthetic buffers such as MOPS, HEPES, ACES and others can alternatively or simultaneously be used. It is also possible to maintain a constant culture pH through the addition of NaOH or NH 4 OH during growth. If complex medium components such as yeast extract are utilized, the necessity for additional buffers may be reduced, due to the fact that many complex compounds have high buffer capacities. If a fermentor is utilized for culturing the micro-organisms, the pH can also be controlled using gaseous ammonia.  
      The incubation time is usually in a range from several hours to several days. This time is selected in order to permit the maximal amount of product to accumulate in the broth. The disclosed growth experiments can be carried out in a variety of vessels, such as microtiter plates, glass tubes, glass flasks or glass or metal fermentors of different sizes. For screening a large number of clones, the microorganisms should be cultured in microtiter plates, glass tubes or shake flasks, either with or without baffles. Preferably 100 ml shake flasks are used, filled with 10% (by volume) of the required growth medium. The flasks should be shaken on a rotary shaker (amplitude 25 mm) using a speed-range of 100-300 rpm. Evaporation losses can be diminished by the maintenance of a humid atmosphere; alternatively, a mathematical correction for evaporation losses should be performed.  
      If genetically modified clones are tested, an unmodified control clone or a control clone containing the basic plasmid without any insert should also be tested. The medium is inoculated to an OD 600  of 0.5-1.5 using cells grown on agar plates, such as CM plates (10 g/l glucose, 2,5 g/l NaCl, 2 g/l urea, 10 g/l polypeptone, 5 g/l yeast extract, 5 g/l meat extract, 22 g/l NaCl, 2 g/l urea, 10 g/l polypeptone, 5 g/l yeast extract, 5 g/l meat extract, 22 g/l agar, pH 6.8 with 2M NaOH) that had been incubated at 30° C. Inoculation of the media is accomplished by either introduction of a saline suspension of  C. glutamicum  cells from CM plates or addition of a liquid preculture of this bacterium.  
     Example 8  
     In Vitro Analysis of the Function of Mutant Proteins  
      The determination of activities and kinetic parameters of enzymes is well established in the art. Experiments to determine the activity of any given altered enzyme must be tailored to the specific activity of the wild-type enzyme, which is well within the ability of one of ordinary skill in the art. Overviews about enzymes in general, as well as specific details concerning structure, kinetics, principles, methods, applications and examples for the determination of many enzyme activities may be found, for example, in the following references: Dixon, M., and Webb, E. C., (1979) Enzymes. Longmans: London; Fersht, (1985) Enzyme Structure and Mechanism. Freeman: New York; Walsh, (1979) Enzymatic Reaction Mechanisms. Freeman: San Francisco; Price, N. C., Stevens, L. (1982) Fundamentals of Enzymology. Oxford Univ. Press: Oxford; Boyer, P. D., ed. (1983) The Enzymes, 3 rd  ed. Academic Press: New York; Bisswanger, H., (1994) Enzymkinetik, 2 nd  ed. VCH: Weinheim (ISBN 3527300325); Bergmeyer, H. U., Bergmeyer, J., Graβ1, M., eds. (1983-1986) Methods of Enzymatic Analysis, 3 rd  ed., vol. I-XII, Verlag Chemie: Weinheim; and Ullmann&#39;s Encyclopedia of Industrial Chemistry (1987) vol. A9, “Enzymes”. VCH: Weinheim, p. 352-363.  
      The activity of proteins which bind to DNA can be measured by several well-established methods, such as DNA band-shift assays (also called gel retardation assays). The effect of such proteins on the expression of other molecules can be measured using reporter gene assays (such as that described in Kolmar, H. et al. (1995)  EMBO J.  14: 3895-3904 and references cited therein). Reporter gene test systems are well known and established for applications in both pro- and eukaryotic cells, using enzymes such as beta-galactosidase, green fluorescent protein, and several others.  
      The determination of activity of membrane-transport proteins can be performed according to techniques such as those described in Gennis, R. B. (1989) “Pores, Channels and Transporters”, in Biomembranes, Molecular Structure and Function, Springer: Heidelberg, p. 85-137; 199-234; and 270-322.  
     Example 9  
     Analysis of Impact of Mutant Protein on the Production of the Desired Product  
      The effect of the genetic modification in  C. glutamicum  on production of a desired compound (such as an amino acid) can be assessed by growing the modified microorganism under suitable conditions (such as those described above) and analyzing the medium and/or the cellular component for increased production of the desired product (i.e., an amino acid). Such analysis techniques are well known to one of ordinary skill in the art, and include spectroscopy, thin layer chromatography, staining methods of various kinds, enzymatic and microbiological methods, and analytical chromatography such as high performance liquid chromatography (see, for example, Ullman, Encyclopedia of Industrial Chemistry, vol. A2, p. 89-90 and p. 443-613, VCH: Weinheim (1985); Fallon, A. et al., (1987) “Applications of HPLC in Biochemistry” in: Laboratory Techniques in Biochemistry and Molecular Biology, vol. 17; Rehm et al. (1993) Biotechnology, vol. 3, Chapter III: “Product recovery and purification”, page 469-714, VCH: Weinheim; Belter, P. A. et al. (1988) Bioseparations: downstream processing for biotechnology, John Wiley and Sons; Kennedy, J. F. and Cabral, J. M. S. (1992) Recovery processes for biological materials, John Wiley and Sons; Shaeiwitz, J. A. and Henry, J. D. (1988) Biochemical separations, in: Ulmann&#39;s Encyclopedia of Industrial Chemistry, vol. B3, Chapter 11, page 1-27, VCH: Weinheim; and Dechow, F. J. (1989) Separation and purification techniques in biotechnology, Noyes Publications.)  
      In addition to the measurement of the final product of fermentation, it is also possible to analyze other components of the metabolic pathways utilized for the production of the desired compound, such as intermediates and side-products, to determine the overall efficiency of production of the compound. Analysis methods include measurements of nutrient levels in the medium (e.g., sugars, hydrocarbons, nitrogen sources, phosphate, and other ions), measurements of biomass composition and growth, analysis of the production of common metabolites of biosynthetic pathways, and measurement of gasses produced during fermentation. Standard methods for these measurements are outlined in Applied Microbial Physiology, A Practical Approach, P. M. Rhodes and P. F. Stanbury, eds., IRL Press, p. 103-129; 131-163; and 165-192 (ISBN: 0199635773) and references cited therein.  
     Example 10  
     Purification of the Desired Product from  C. glutamicum  Culture  
      Recovery of the desired product from the  C. glutamicum  cells or supernatant of the above-described culture can be performed by various methods well known in the art. If the desired product is not secreted from the cells, the cells can be harvested from the culture by low-speed centrifugation, the cells can be lysed by standard techniques, such as mechanical force or sonication. The cellular debris is removed by centrifugation, and the supernatant fraction containing the soluble proteins is retained for further purification of the desired compound. If the product is secreted from the  C. glutamicum  cells, then the cells are removed from the culture by low-speed centrifugation, and the supernate fraction is retained for further purification.  
      The supernatant fraction from either purification method is subjected to chromatography with a suitable resin, in which the desired molecule is either retained on a chromatography resin while many of the impurities in the sample are not, or where the impurities are retained by the resin while the sample is not. Such chromatography steps may be repeated as necessary, using the same or different chromatography resins. One of ordinary skill in the art would be well-versed in the selection of appropriate chromatography resins and in their most efficacious application for a particular molecule to be purified. The purified product may be concentrated by filtration or ultrafiltration, and stored at a temperature at which the stability of the product is maximized.  
      There are a wide array of purification methods known to the art and the preceding method of purification is not meant to be limiting. Such purification techniques are described, for example, in Bailey, J. E. &amp; Ollis, D. F. Biochemical Engineering Fundamentals, McGraw-Hill: New York (1986).  
      The identity and purity of the isolated compounds may be assessed by techniques standard in the art. These include high-performance liquid chromatography (HPLC), spectroscopic methods, staining methods, thin layer chromatography, NIRS, enzymatic assay, or microbiologically. Such analysis methods are reviewed in: Patek et al. (1994)  Appl. Environ. Microbiol.  60: 133-140; Malakhova et al. (1996)  Biotekhnologiya  11: 27-32; and Schmidt et al. (1998)  Bioprocess Engineer.  19: 67-70. Ulmann&#39;s Encyclopedia of Industrial Chemistry, (1996) vol. A27, VCH: Weinheim, p. 89-90, p. 521-540, p. 540-547, p. 559-566, 575-581 and p. 581-587; Michal, G. (1999) Biochemical Pathways: An Atlas of Biochemistry and Molecular Biology, John Wiley and Sons; Fallon, A. et al. (1987) Applications of HPLC in Biochemistry in: Laboratory Techniques in Biochemistry and Molecular Biology, vol. 17.  
     Example 11  
     Analysis of the Gene Sequences of the Invention  
      The comparison of sequences and determination of percent homology between two sequences are art-known techniques, and can be accomplished using a mathematical algorithm, such as the algorithm of Karlin and Altschul (1990)  Proc. Natl. Acad. Sci. USA  87:2264-68, modified as in Karlin and Altschul (1993)  Proc. Natl. Acad. Sci. USA  90:5873-77. Such an algorithm is incorporated into the NBLAST and XBLAST programs (version 2.0) of Altschul, et al. (1990)  J. Mol. Biol.  215:403-10. BLAST nucleotide searches can be performed with the NBLAST program, score=100, wordlength=12 to obtain nucleotide sequences homologous to HA nucleic acid molecules of the invention. BLAST protein searches can be performed with the XBLAST program, score=50, wordlength=3 to obtain amino acid sequences homologous to HA protein molecules of the invention. To obtain gapped alignments for comparison purposes, Gapped BLAST can be utilized as described in Altschul et al., (1997)  Nucleic Acids Res.  25(17):3389-3402. When utilizing BLAST and Gapped BLAST programs, one of ordinary skill in the art will know how to optimize the parameters of the program (e.g., XBLAST and NBLAST) for the specific sequence being analyzed.  
      Another example of a mathematical algorithm utilized for the comparison of sequences is the algorithm of Meyers and Miller ((1988)  Comput. Appl. Biosci.  4: 11-17). Such an algorithm is incorporated into the ALIGN program (version 2.0) which is part of the GCG sequence alignment software package. When utilizing the ALIGN program for comparing amino acid sequences, a PAM120 weight residue table, a gap length penalty of 12, and a gap penalty of 4 can be used. Additional algorithms for sequence analysis are known in the art, and include ADVANCE and ADAM. described in Torelli and Robotti (1994)  Comput. Appl. Biosci.  10:3-5; and FASTA, described in Pearson and Lipman (1988)  P.N.A.S.  85:2444-8.  
      The percent homology between two amino acid sequences can also be accomplished using the GAP program in the GCG software package (available at http://www.gcg.com), using either a Blosum 62 matrix or a PAM250 matrix, and a gap weight of 12, 10, 8, 6, or 4 and a length weight of 2, 3, or 4. The percent homology between two nucleic acid sequences can be accomplished using the GAP program in the GCG software package, using standard parameters, such as a gap weight of 50 and a length weight of 3.  
      A comparative analysis of the gene sequences of the invention with those present in Genbank has been performed using techniques known in the art (see, e.g., Bexevanis and Ouellette, eds. (1998) Bioinformatics: A Practical Guide to the Analysis of Genes and Proteins. John Wiley and Sons: New York). The gene sequences of the invention were compared to genes present in Genbank in a three-step process. In a first step, a BLASTN analysis (e.g., a local alignment analysis) was performed for each of the sequences of the invention against the nucleotide sequences present in Genbank, and the top 500 hits were retained for further analysis. A subsequent FASTA search (e.g., a combined local and global alignment analysis, in which limited regions of the sequences are aligned) was performed on these 500 hits. Each gene sequence of the invention was subsequently globally aligned to each of the top three FASTA hits, using the GAP program in the GCG software package (using standard parameters). In order to obtain correct results, the length of the sequences extracted from Genbank were adjusted to the length of the query sequences by methods well-known in the art. The results of this analysis are set forth in Table 4. The resulting data is identical to that which would have been obtained had a GAP (global) analysis alone been performed on each of the genes of the invention in comparison with each of the references in Genbank, but required significantly reduced computational time as compared to such a database-wide GAP (global) analysis. Sequences of the invention for which no alignments above the cutoff values were obtained are indicated on Table 4 by the absence of alignment information. It will further be understood by one of ordinary skill in the art that the GAP alignment homology percentages set forth in Table 4 under the heading “% homology (GAP)” are listed in the European numerical format, wherein a ‘,’ represents a decimal point. For example, a value of “40,345” in this column represents “40.345%”.  
     Example 12  
     Construction and Operation of DNA Microarrays  
      The sequences of the invention may additionally be used in the construction and application of DNA microarrays (the design, methodology, and uses of DNA arrays are well known in the art, and are described, for example, in Schena, M. et al. (1995)  Science  270: 467-470; Wodicka, L. et al. (1997)  Nature Biotechnology  15: 1359-1367; DeSaizieu, A. et al. (1998)  Nature Biotechnology  16: 45-48; and DeRisi, J. L. et al. (1997)  Science  278: 680-686).  
      DNA microarrays are solid or flexible supports consisting of nitrocellulose, nylon, glass, silicone, or other materials. Nucleic acid molecules may be attached to the surface in an ordered manner. After appropriate labeling, other nucleic acids or nucleic acid mixtures can be hybridized to the immobilized nucleic acid molecules, and the label may be used to monitor and measure the individual signal intensities of the hybridized molecules at defined regions. This methodology allows the simultaneous quantification of the relative or absolute amount of all or selected nucleic acids in the applied nucleic acid sample or mixture. DNA microarrays, therefore, permit an analysis of the expression of multiple (as many as 6800 or more) nucleic acids in parallel (see, e.g., Schena, M. (1996)  BioEssays  18(5): 427-431).  
      The sequences of the invention may be used to design oligonucleotide primers which are able to amplify defined regions of one or more  C. glutamicum  genes by a nucleic acid amplification reaction such as the polymerase chain reaction. The choice and design of the 5′ or 3′ oligonucleotide primers or of appropriate linkers allows the covalent attachment of the resulting PCR products to the surface of a support medium described above (and also described, for example, Schena, M. et al. (1995)  Science  270: 467-470).  
      Nucleic acid microarrays may also be constructed by in situ oligonucleotide synthesis as described by Wodicka, L. et al. (1997)  Nature Biotechnology  15: 1359-1367. By photolithographic methods, precisely defined regions of the matrix are exposed to light. Protective groups which are photolabile are thereby activated and undergo nucleotide addition, whereas regions that are masked from light do not undergo any modification. Subsequent cycles of protection and light activation permit the synthesis of different oligonucleotides at defined positions. Small, defined regions of the genes of the invention may be synthesized on microarrays by solid phase oligonucleotide synthesis.  
      The nucleic acid molecules of the invention present in a sample or mixture of nucleotides may be hybridized to the microarrays. These nucleic acid molecules can be labeled according to standard methods. In brief, nucleic acid molecules (e.g., mRNA molecules or DNA molecules) are labeled by the incorporation of isotopically or fluorescently labeled nucleotides, e.g., during reverse transcription or DNA synthesis. Hybridization of labeled nucleic acids to microarrays is described (e.g., in Schena, M. et al. (1995) supra; Wodicka, L. et al. (1997), supra; and DeSaizieu A. et al. (1998), supra). The detection and quantification of the hybridized molecule are tailored to the specific incorporated label. Radioactive labels can be detected, for example, as described in Schena, M. et al. (1995) supra) and fluorescent labels may be detected, for example, by the method of Shalon et al. (1996)  Genome Research  6: 639-645).  
      The application of the sequences of the invention to DNA microarray technology, as described above, permits comparative analyses of different strains of  C. glutamicum  or other  Corynebacteria . For example, studies of inter-strain variations based on individual transcript profiles and the identification of genes that are important for specific and/or desired strain properties such as pathogenicity, productivity and stress tolerance are facilitated by nucleic acid array methodologies. Also, comparisons of the profile of expression of genes of the invention during the course of a fermentation reaction are possible using nucleic acid array technology.  
     Example 13  
     Analysis of the Dynamics of Cellular Protein Populations (Proteomics)  
      The genes, compositions, and methods of the invention may be applied to study the interactions and dynamics of populations of proteins, termed ‘proteomics’. Protein populations of interest include, but are not limited to, the total protein population of  C. glutamicum  (e.g., in comparison with the protein populations of other organisms), those proteins which are active under specific environmental or metabolic conditions (e.g., during fermentation, at high or low temperature, or at high or low pH), or those proteins which are active during specific phases of growth and development.  
      Protein populations can be analyzed by various well-known techniques, such as gel electrophoresis. Cellular proteins may be obtained, for example, by lysis or extraction, and may be separated from one another using a variety of electrophoretic techniques. Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) separates proteins largely on the basis of their molecular weight. Isoelectric focusing polyacrylamide gel electrophoresis (IEF-PAGE) separates proteins by their isoelectric point (which reflects not only the amino acid sequence but also posttranslational modifications of the protein). Another, more preferred method of protein analysis is the consecutive combination of both IEF-PAGE and SDS-PAGE, known as 2-D-gel electrophoresis (described, for example, in Hermann et al. (1998)  Electrophoresis  19: 3217-3221; Fountoulakis et al. (1998)  Electrophoresis  19: 1193-1202; Langen et al. (1997)  Electrophoresis  18: 1184-1192; Antelmann et al. (1997)  Electrophoresis  18: 1451-1463). Other separation techniques may also be utilized for protein separation, such as capillary gel electrophoresis; such techniques are well known in the art.  
      Proteins separated by these methodologies can be visualized by standard techniques, such as by staining or labeling. Suitable stains are known in the art, and include Coomassie Brilliant Blue, silver stain, or fluorescent dyes such as Sypro Ruby (Molecular Probes). The inclusion of radioactively labeled amino acids or other protein precursors (e.g.,  35 S-methionine,  35 S-cysteine,  14 C-labelled amino acids,  15 N-amino acids,  15 NO 3  or  15 NH 4   +  or  13 C-labelled amino acids) in the medium of  C. glutamicum  permits the labeling of proteins from these cells prior to their separation. Similarly, fluorescent labels may be employed. These labeled proteins can be extracted, isolated and separated according to the previously described techniques.  
      Proteins visualized by these techniques can be further analyzed by measuring the amount of dye or label used. The amount of a given protein can be determined quantitatively using, for example, optical methods and can be compared to the amount of other proteins in the same gel or in other gels. Comparisons of proteins on gels can be made, for example, by optical comparison, by spectroscopy, by image scanning and analysis of gels, or through the use of photographic films and screens. Such techniques are well-known in the art.  
      To determine the identity of any given protein, direct sequencing or other standard techniques may be employed. For example, N- and/or C-terminal amino acid sequencing (such as Edman degradation) may be used, as may mass spectrometry (in particular MALDI or ESI techniques (see, e.g., Langen et al. (1997)  Electrophoresis  18: 1184-1192)). The protein sequences provided herein can be used for the identification of  C. glutamicum  proteins by these techniques.  
      The information obtained by these methods can be used to compare patterns of protein presence, activity, or modification between different samples from various biological conditions (e.g., different organisms, time points of fermentation, media conditions, or different biotopes, among others). Data obtained from such experiments alone, or in combination with other techniques, can be used for various applications, such as to compare the behavior of various organisms in a given (e.g., metabolic) situation, to increase the productivity of strains which produce fine chemicals or to increase the efficiency of the production of fine chemicals.  
     EQUIVALENTS  
      Those of ordinary skill in the art will recognize, or will be able to ascertain using no more than routine experimentation, many equivalents to the specific embodiments of the invention described herein. Such equivalents are intended to be encompassed by the following claims.  
               TABLE 1                          Genes in the Application                                         Nucleic   Amino                           Acid   Acid       SEQ   SEQ   Identification       ID NO   ID NO   Code   Contig.   NT Start   NT Stop   Function                                                 1   2   RXA02548   GR00727   3   293   SULFATE ADENYLATE TRANSFERASE SUBUNIT 2 (EC 2.7.7.4)       3   4   RXN00249   VV0057   36825   35869   ADENYLYLSULFATE KINASE (EC 2.7.1.25)       5   6   F RXA00249   GR00037   8837   7884   ADENYLYLSULFATE KINASE (EC 2.7.1.25)       7   8   RXA01073   GR00300   1274   2104   NH(3)-DEPENDENT NAD(+) SYNTHETASE (EC 6.3.5.1)                 Urease                                         9   10   RXN02913   VV0020   8998   8513   UREASE BETA SUBUNIT (EC 3.5.1.5)       11   12   F RXA02264   GR00655   123   4   UREASE ALPHA SUBUNIT (EC 3.5.1.5)       13   14   RXN02274   VV0020   8509   6800   UREASE ALPHA SUBUNIT (EC 3.5.1.5)       15   16   F RXA02274   GR00656   3   1604   UREASE ALPHA SUBUNIT (EC 3.5.1.5)       17   18   RXA02265   GR00655   452   153   UREASE GAMMA SUBUNIT (EC 3.5.1.5)       19   20   RXA02278   GR00656   3420   4268   UREASE OPERON URED PROTEIN       21   22   RXA02275   GR00656   1632   2102   UREASE ACCESSORY PROTEIN UREE       23   24   RXA02276   GR00656   2105   2782   UREASE ACCESSORY PROTEIN UREF       25   26   RXA02277   GR00656   2802   3416   UREASE ACCESSORY PROTEIN UREG       27   28   RXA02603   GR00742   7742   8737   4-HYDROXYBENZOATE OCTAPRENYLTRANSFERASE (EC 2.5.1.—)       29   30   RXA01385   GR00406   5320   3440   PHENOL 2 MONOOXYGENASE (EC 1.14.13.7)                 Proteolysis                                         31   32   RXN00675   VV0005   33258   34049   METHIONINE AMINOPEPTIDASE (EC 3.4.11.18)       33   34   F RXA00675   GR00178   2   484   METHIONINE AMINOPEPTIDASE (EC 3.4.11.18)       35   36   RXA01609   GR00449   2740   3612   METHIONINE AMINOPEPTIDASE (EC 3.4.11.18)       37   38   RXA01358   GR00393   5337   6857   ATP-DEPENDENT PROTEASE LA (EC 3.4.21.53)       39   40   RXA01458   GR00420   3225   2176   ATP-DEPENDENT PROTEASE LA (EC 3.4.21.53)       41   42   RXA01654   GR00459   986   1981   (AL022121) putative alkaline serine protease [Mycobacterium tuberculosis]       43   44   RXN01868   VV0127   9980   11905   ZINC METALLOPROTEASE (EC 3.4.24.—)       45   46   F RXA01868   GR00534   1640   30   ZINC METALLOPROTEASE (EC 3.4.24.—)       47   48   F RXA01869   GR00534   1954   1652   ZINC METALLOPROTEASE (EC 3.4.24.—)       49   50   RXN03028   VV0008   41156   43930   ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPA       51   52   F RXA02470   GR00715   2216   3196   ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPA       53   54   F RXA02471   GR00715   3159   4991   ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPA       55   56   RXA02630   GR00748   2654   1332   (AL021999) putative serine protease [Mycobacterium tuberculosis]       57   58   RXA02834   GR00823   3   497   ATPases with chaperone activity, ATP-dependent protease subunit       59   60   RXA00112   GR00016   3687   2497   PROBABLE PERIPLASMIC SERINE PROTEASE DO-LIKE PRECURSOR       61   62   RXA00566   GR00152   742   137   ATP-DEPENDENT CLP PROTEASE PROTEOLYTIC                               SUBUNIT (EC 3.4.21.92)       63   64   RXA00567   GR00152   1388   798   ATP-DEPENDENT CLP PROTEASE PROTEOLYTIC                               SUBUNIT (EC 3.4.21.92)       65   66   RXN03094   VV0057   1794   43   CLPB PROTEIN       67   68   F RXA01668   GR00464   2205   3920   CLPB PROTEIN       69   70   RXN01120   VV0182   5678   4401   ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPX       71   72   F RXA01120   GR00310   2349   1072   ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPX       73   74   RXA00744   GR00202   10722   9781   Periplasmic serine proteases       75   76   RXA00844   GR00228   3620   4453   Hypothetical Secretory Serine Protease (EC 3.4.21.—)       77   78   RXA01151   GR00324   862   5   ATP-dependent Zn proteases       79   80   RXA02317   GR00665   9664   9053   PEPTIDASE E (EC 3.4.—.—)       81   82   RXA02644   GR00751   767   117   XAA-PRO DIPEPTIDASE (EC 3.4.13.9)       83   84   RXN02820   VV0131   4799   6109   GAMMA-GLUTAMYLTRANSPEPTIDASE (EC 2.3.2.2)       85   86   F RXA02820   GR00801   1   507   GAMMA-GLUTAMYLTRANSPEPTIDASE (EC 2.3.2.2)       87   88   F RXA02000   GR00589   3430   3933   GAMMA-GLUTAMYLTRANSPEPTIDASE (EC 2.3.2.2)       89   90   RXN03178   VV0334   921   121   PENICILLIN-BINDING PROTEIN 5* PRECURSOR                               (D-ALANYL-D-ALANINE CARBOXYPEPTIDASE) (EC 3.4.16.4)       91   92   F RXA02859   GR10005   846   121   PENICILLIN-BINDING PROTEIN 5* PRECURSOR                               (D-ALANYL-D-ALANINE CARBOXYPEPTIDASE) (EC 3.4.16.4)       93   94   RXA00137   GR00022   738   1826   XAA-PRO AMINOPEPTIDASE (EC 3.4.11.9)       95   96   RXN00499   VV0086   8158   9438   PROLINE IMINOPEPTIDASE (EC 3.4.11.5)       97   98   F RXA00499   GR00125   3   959   PROLINE IMINOPEPTIDASE       99   100   RXN00877   VV0099   2221   3885   PEPTIDYL-DIPEPTIDASE DCP (EC 3.4.15.5)       101   102   F RXA00877   GR00242   3   1067   PEPTIDYL-DIPEPTIDASE DCP (EC 3.4.15.5)       103   104   RXN01014   VV0209   13328   10728   AMINOPEPTIDASE N (EC 3.4.11.2)       105   106   F RXA01014   GR00289   3   1580   AMINOPEPTIDASE N (EC 3.4.11.2)       107   108   F RXA01018   GR00290   2289   3152   AMINOPEPTIDASE N (EC 3.4.11.2)       109   110   RXA01147   GR00323   1353   94   VACUOLAR AMINOPEPTIDASE I PRECURSOR (EC 3.4.11.1)       111   112   RXA01161   GR00329   1253   117   XAA-PRO AMINOPEPTIDASE (EC 3.4.11.9)       113   114   RXN01181   VV0065   1   957   AMINOPEPTIDASE A/I (EC 3.4.11.1)       115   116   F RXA01181   GR00337   1   957   AMINOPEPTIDASE       117   118   RXN01277   VV0009   32155   34158   PROLYL ENDOPEPTIDASE (EC 3.4.21.26)       119   120   F RXA01277   GR00368   1738   50   PROLYL ENDOPEPTIDASE (EC 3.4.21.26)       121   122   RXA01914   GR00548   125   550   AMINOPEPTIDASE       123   124   RXA02048   GR00624   207   1580   AMINOPEPTIDASE N (EC 3.4.11.2)       125   126   RXN00621   VV0135   5853   5071   PROTEASE II (EC 3.4.21.83)       127   128   F RXA00621   GR00163   4075   4857   PTRB periplasmic protease       129   130   RXN00622   VV0135   5150   3735   PROTEASE II (EC 3.4.21.83)       131   132   F RXA00622   GR00163   4778   6193   PTRB periplasmic protease       133   134   RXN00982   VV0149   7596   6091   (L42758) proteinase [Streptomyces lividans]       135   136   F RXA00977   GR00275   1647   2660   (L42758) proteinase [Streptomyces lividans]       137   138   F RXA00982   GR00276   5194   4949   (L42758) proteinase [Streptomyces lividans]       139   140   RXA00152   GR00023   7175   5880   HFLC PROTEIN (EC 3.4.—.—)       141   142   RXA02558   GR00731   4939   3965   HFLC PROTEIN (EC 3.4.—.—)       143   144   RXA00500   GR00125   969   1643   O-SIALOGLYCOPROTEIN ENDOPEPTIDASE (EC 3.4.24.57)       145   146   RXA00501   GR00125   1643   2149   O-SIALOGLYCOPROTEIN ENDOPEPTIDASE (EC 3.4.24.57)       147   148   RXA00502   GR00125   2156   3187   O-SIALOGLYCOPROTEIN ENDOPEPTIDASE (EC 3.4.24.57)                 Enzymes in general                                         149   150   RXN02589   VV0098   16346   17110   Hypothetical Methyltransferase (EC 2.1.1.—)       151   152   F RXA02589   GR00741   13804   13040   Predicted S-adenosylmethionine-dependent methyltransferase       153   154   RXA00226   GR00032   26836   26012   SAM-dependent methyltransferases       155   156   RXN01885   VV0184   2004   2804   Hypothetical Methyltransferase (EC 2.1.1.—)       157   158   F RXA01885   GR00539   1589   2389   SAM-dependent methyltransferases       159   160   RXA02592   GR00741   18477   17707   SAM-dependent methyltransferases       161   162   RXN01795   VV0093   722   1318   MODIFIKATION METHYLASE (EC 2.1.1.73)       163   164   F RXA01795   GR00507   706   1140   MODIFICATION METHYLASE (EC 2.1.1.73)       165   166   RXA01214   GR00351   1640   3130   LACCASE 1 PRECURSOR (EC 1.10.3.2)       167   168   RXA01250   GR00364   592   5   LACCASE 1 PRECURSOR (EC 1.10.3.2)       169   170   RXA02477   GR00715   10581   11201   CARBONIC ANHYDRASE (EC 4.2.1.1)       171   172   RXN00833   GR00225   374   6   THIOL PEROXIDASE (EC 1.11.1.—)       173   174   F RXA00833   GR00225   374   6   THIOL PEROXIDASE (EC 1.11.1.—)       175   176   RXA01224   GR00354   4186   5208   2-NITROPROPANE DIOXYGENASE (EC 1.13.11.32)       177   178   RXA01182   GR00337   1363   971   Hypothetical Oxidoreductase       179   180   RXA02531   GR00726   1226   1936   Hypothetical Oxidoreductase       181   182   RXN00689   VV0005   22416   20926   BETAINE-ALDEHYDE DEHYDROGENASE PRECURSOR (EC 1.2.1.8)       183   184   F RXA00689   GR00180   1401   775   BETAINE-ALDEHYDE DEHYDROGENASE PRECURSOR (EC 1.2.1.8)       185   186   RXN03128   VV0120   3   857   MORPHINE 6-DEHYDROGENASE (EC 1.1.1.218)       187   188   F RXA02192   GR00643   2   523   MORPHINE 6-DEHYDROGENASE (EC 1.1.1.218)       189   190   RXA02351   GR00679   132   1070   NITRILOTRIACETATE MONOOXYGENASE                               COMPONENT A (EC 1.14.13.—)       191   192   RXN00905   VV0238   8075   8875   N-ACYL-L-AMINO ACID AMIDOHYDROLASE (EC 3.5.1.14)       193   194   F RXA00905   GR00247   2   694   N-ACYL-L-AMINO ACID AMIDOHYDROLASE (EC 3.5.1.14)       195   196   RXA00906   GR00247   630   1133   N-ACYL-L-AMINO ACID AMIDOHYDROLASE (EC 3.5.1.14)       197   198   RXA00907   GR00247   1143   1265   N-ACYL-L-AMINO ACID AMIDOHYDROLASE (EC 3.5.1.14)       199   200   RXA02101   GR00631   3104   1842   N-ACYL-L-AMINO ACID AMIDOHYDROLASE (EC 3.5.1.14)       201   202   RXN02565   VV0154   14299   13034   N-ACYL-L-AMINO ACID AMIDOHYDROLASE (EC 3.5.1.14)       203   204   F RXA02565   GR00733   1   342   N-ACYL-L-AMINO ACID AMIDOHYDROLASE (EC 3.5.1.14)       205   206   F RXA02567   GR00734   3   740   N-ACYL-L-AMINO ACID AMIDOHYDROLASE (EC 3.5.1.14)       207   208   RXN03077   VV0043   1729   2913   N-ACYL-L-AMINO ACID AMIDOHYDROLASE (EC 3.5.1.14)       209   210   F RXA02855   GR10002   1693   2877   N-ACYL-L-AMINO ACID AMIDOHYDROLASE (EC 3.5.1.14),                               hippurate hydrolase       211   212   RXA00026   GR00003   3657   5042   Hypothetical Amidohydrolase (EC 3.5.1.—)       213   214   RXA01971   GR00569   963   133   Hypothetical Metal-Dependent Hydrolase       215   216   RXA01802   GR00509   3461   4291   Predicted hydrolases (HAD superfamily)       217   218   RXN00866   VV0258   3557   4522   Predicted Zn-dependent hydrolases       219   220   F RXA00866   GR00236   3555   4499   Predicted Zn-dependent hydrolases       221   222   RXA02410   GR00703   792   127   Predicted Zn-dependent hydrolases       223   224   RXA00961   GR00267   2   433   SALICYLATE HYDROXYLASE (EC 1.14.13.1)       225   226   RXA00111   GR00016   930   1922   SOLUBLE EPOXIDE HYDROLASE (SEH) (EC 3.3.2.3)       227   228   RXA01932   GR00555   6479   5583   ACETYL-HYDROLASE (EC 3.1.1.—)       229   230   RXA02574   GR00739   833   1840   PUTATIVE SECRETED HYDROLASE       231   232   RXN00983   VV0231   1796   321   SIALIDASE PRECURSOR (EC 3.2.1.18)       233   234   F RXA00983   GR00278   1200   4   SIALIDASE PRECURSOR (EC 3.2.1.18)       235   236   RXA00984   GR00278   1716   1300   SIALIDASE PRECURSOR (EC 3.2.1.18)       237   238   RXN02513   VV0193   737   6   SIALIDASE PRECURSOR (EC 3.2.1.18)       239   240   F RXA02513   GR00722   93   824   SIALIDASE PRECURSOR (EC 3.2.1.18)       241   242   RXA00903   GR00246   637   5   Putative epimerase       243   244   RXA01224   GR00354   4186   5208   2-NITROPROPANE DIOXYGENASE (EC 1.13.11.32)       245   246   RXA01571   GR00438   1360   1959   ALCOHOL DEHYDROGENASE (EC 1.1.1.1)       247   248   RXN02478   VV0119   7564   6350   SIALIDASE PRECURSOR (EC 3.2.1.18)       249   250   RXN00343   VV0125   1118   6   3-OXOSTEROID 1-DEHYDROGENASE (EC 1.3.99.4)       251   252   RXN01555   VV0135   29820   28861   3-OXOSTEROID 1-DEHYDROGENASE (EC 1.3.99.4)       253   254   RXN01166   VV0117   18142   16838   EXTRACELLULAR LIPASE PRECURSOR (EC 3.1.1.3)       255   256   RXN02001   VV0326   630   1787   N-ACYL-L-AMINO ACID AMIDOHYDROLASE (EC 3.5.1.14)       257   258   RXN03145   VV0142   7561   7115   4-OXALOCROTONATE TAUTOMERASE (EC 5.3.2.—)       259   260   RXN01466   VV0019   7050   6091   ARYLESTERASE (EC 3.1.1.2)       261   262   RXN01145   VV0077   7538   6525   KETOL-ACID REDUCTOISOMERASE (EC 1.1.1.86)       263   264   RXN03088   VV0052   3431   3817   Hypothetical Methyltransferase (EC 2.1.1.—)       265   266   RXN02952   VV0320   1032   1547   PUTATIVE REDUCTASE       267   268   RXN00513   VV0092   1573   653   CARBOXYVINYL-CARBOXYPHOSPHONATE                               PHOSPHORYLMUTASE (EC 2.7.8.23)       269   270   RXN01152   VV0136   1740   907   PROTEIN-L-ISOASPARTATE O-METHYLTRANSFERASE (EC 2.1.1.77)       271   272   RXN00787   VV0321   3736   5637   D-AMINO ACID DEHYDROGENASE LARGE SUBUNIT (EC 1.4.99.1)                 N-metabolism                                         273   274   RXN01302   VV0148   2837   2385   NITRATE REDUCTASE ALPHA CHAIN (EC 1.7.99.4)       275   276   F RXA01302   GR00376   370   5   NITRATE REDUCTASE ALPHA CHAIN (EC 1.7.99.4)       277   278   RXN01308   VV0148   2406   4   NITRATE REDUCTASE ALPHA CHAIN (EC 1.7.99.4)       279   280   F RXA01307   GR00377   686   6   NITRATE REDUCTASE ALPHA CHAIN (EC 1.7.99.4)       281   282   F RXA01308   GR00378   1211   6   NITRATE REDUCTASE ALPHA CHAIN (EC 1.7.99.4)       283   284   RXN01309   VV0158   1   801   NITRATE REDUCTASE ALPHA CHAIN (EC 1.7.99.4)       285   286   F RXA01309   GR00379   719   51   NITRATE REDUCTASE ALPHA CHAIN (EC 1.7.99.4)       287   288   RXA02017   GR00610   1731   1048   NITRATE REDUCTASE ALPHA CHAIN (EC 1.7.99.4)       289   290   RXA02018   GR00610   2788   1739   NITRATE REDUCTASE BETA CHAIN (EC 1.7.99.4)       291   292   RXA02016   GR00610   1036   260   NITRATE REDUCTASE GAMMA CHAIN (EC 1.7.99.4)       293   294   RXA00471   GR00119   2997   3686   NITRATE/NITRITE RESPONSE REGULATOR PROTEIN NARL       295   296   RXA00133   GR00021   201   1013   NITRATE/NITRITE RESPONSE REGULATOR PROTEIN NARP       297   298   RXA00650   GR00169   4017   3382   NITRATE/NITRITE RESPONSE REGULATOR PROTEIN NARP       299   300   RXA01189   GR00339   2545   1937   NITRATE/NITRITE RESPONSE REGULATOR PROTEIN NARP       301   302   RXA01607   GR00449   123   752   NITRATE/NITRITE RESPONSE REGULATOR PROTEIN NARP       303   304   RXN00470   VV0086   27401   28669   NITRATE/NITRITE SENSOR PROTEIN NARX (EC 2.7.3.—)       305   306   F RXA00470   GR00119   1752   2951   NITRATE/NITRITE SENSOR PROTEIN NARX (EC 2.7.3.—)       307   308   RXA00756   GR00203   2932   1937   N UTILIZATION SUBSTANCE PROTEIN A       309   310   RXA00139   GR00022   2514   3224   N UTILIZATION SUBSTANCE PROTEIN B       311   312   RXA01303   GR00376   1724   390   NITRITE EXTRUSION PROTEIN       313   314   RXA01412   GR00412   620   417   NITROGEN FIXATION PROTEIN FIXI (PROBABLE E1-E2 TYPE                               CATION ATPASE) (EC 3.6.1.—)       315   316   RXA00773   GR00205   3208   4350   NITROGEN REGULATION PROTEIN NIFR3       317   318   RXA02746   GR00764   1   267   NITROGEN REGULATORY PROTEIN P-II       319   320   RXA02745   GR00763   15350   14472   NODULATION ATP-BINDING PROTEIN I       321   322   RXN00820   VV0054   19455   19817   NODULATION PROTEIN N       323   324   F RXA00820   GR00221   1007   1369   NODULATION PROTEIN N       325   326   RXA01059   GR00296   8782   9390   OXYGEN-INSENSITIVE NAD(P)H NITROREDUCTASE (EC 1.—.—.—)       327   328   RXN01386   VV0008   39246   38317   NITRILASE REGULATOR       329   330   RXN00073   VV0154   2369   687   FERREDOXIN-NITRITE REDUCTASE (EC 1.7.7.1)       331   332   RXN03131   VV0127   276   4   RHIZOPINE CATABOLISM PROTEIN MOCC       333   334   RXS00153   VV0167   4195   4620   NODULATION PROTEIN                 Urease       Phosphate and Phosphonate metabolism                                         335   336   RXN01716   VV0319   3259   2774   EXOPOLYPHOSPHATASE (EC 3.6.1.11)       337   338   RXN02972   VV0319   2763   2353   EXOPOLYPHOSPHATASE (EC 3.6.1.11)       339   340   RXN00663   VV0142   10120   11493   PHOH PROTEIN HOMOLOG       341   342   RXN00778   VV0103   18126   19250   PHOSPHATE-BINDING PERIPLASMIC PROTEIN PRECURSOR       343   344   RXN00250   VV0189   286   1032   DEDA PROTEIN - ALKALINE PHOSPHATASE LIKE PROTEIN                 Sulfate metabolism                                         345   346   RXA00072   GR00012   446   6   PHOSPHOADENOSINE PHOSPHOSULFATE REDUCTASE (EC 1.8.99.4)       347   348   RXA00793   GR00211   1469   2644   SULFATE STARVATION-INDUCED PROTEIN 6       349   350   RXA01192   GR00342   161   733   SULFATE STARVATION-INDUCED PROTEIN 6       351   352   RXA00715   GR00188   2120   2914   THIOSULFATE SULFURTRANSFERASE (EC 2.8.1.1)       353   354   RXA01664   GR00463   1306   485   THIOSULFATE SULFURTRANSFERASE (EC 2.8.1.1)       355   356   RXN02334   VV0141   7939   7217   THIOSULFATE SULFURTRANSFERASE (EC 2.8.1.1)       357   358   F RXA02334   GR00672   2   355   THIOSULFATE SULFURTRANSFERASE (EC 2.8.1.1)                 Fe-Metabolism                                         359   360   RXN01499   VV0008   7034   3213   ENTEROBACTIN SYNTHETASE COMPONENT F       361   362   RXN01997   VV0084   33308   33793   FERRITIN                 Mg Metabolism                                         363   364   RXA01848   GR00524   1532   789   MAGNESIUM-CHELATASE SUBUNIT CHLI       365   366   RXN01849   VV0139   16415   17515   MAGNESIUM-CHELATASE SUBUNIT CHLI       367   368   F RXA01849   GR00524   2004   1555   MAGNESIUM-CHELATASE SUBUNIT CHLI       369   370   F RXA01691   GR00474   570   4   MAGNESIUM-CHELATASE SUBUNIT CHLI       371   372   RXN00665   VV0252   135   635   MG2+/CITRATE COMPLEX SECONDARY TRANSPORTER                 Modification and degradation of aromatic compounds                                         373   374   RXN03026   VV0007   28635   28901   3-DEHYDROQUINATE DEHYDRATASE (EC 4.2.1.10)       375   376   RXN02908   VV0025   8507   8247   O-SUCCINYLBENZOIC ACID—COA LIGASE (EC 6.2.1.26)       377   378   RXN03000   VV0235   570   4   SALICYLATE HYDROXYLASE (EC 1.14.13.1)       379   380   RXN03036   VV0014   671   6   PROTOCATECHUATE 3,4-DIOXYGENASE BETA CHAIN (EC 1.13.11.3)       381   382   RXN02974   VV0229   12631   12437   4-NITROPHENYLPHOSPHATASE (EC 3.1.3.41)       383   384   RXN00393   VV0025   7241   6348   1,4-DIHYDROXY-2-NAPHTHOATE                               OCTAPRENYLTRANSFERASE (EC 2.5.—.—)       385   386   RXN00948   VV0107   4266   5384   12-oxophytodienoate reductase (EC 1.3.1.42)       387   388   RXN01923   VV0020   3384   4133   2-HYDROXY-6-OXO-6-PHENYLHEXA-2,4-DIENOATE                               HYDROLASE (EC 3.7.1.—)       389   390   RXN00398   VV0025   14633   13884   2-PYRONE-4,6-DICARBOXYLATE LACTONASE (EC 3.1.1.57)       391   392   RXN02813   VV0128   13120   14118   3-CARBOXY-CIS,CIS-MUCONATE CYCLOISOMERASE                               HOMOLOG (EC 5.5.1.2)       393   394   RXN00136   VV0134   13373   14467   3-DEHYDROQUINATE SYNTHASE (EC 4.6.1.3)       395   396   RXN02508   VV0007   26733   28586   3-DEHYDROSHIKIMATE DEHYDRATASE (EC 4.2.1.—)       397   398   RXN02839   VV0362   3   449   4-HYDROXYBENZOATE OCTAPRENYLTRANSFERASE (EC 2.5.1.—)       399   400   RXN00639   VV0128   7858   8712   CATECHOL 1,2-DIOXYGENASE (EC 1.13.11.1)       401   402   RXN02530   VV0057   5469   6125   DIMETHYLANILINE MONOOXYGENASE                               (N-OXIDE FORMING) 1 (EC 1.14.13.8)       403   404   RXN00434   VV0112   12078   11212   QUINONE OXIDOREDUCTASE (EC 1.6.5.5)       405   406   RXN01619   VV0050   24649   23675   QUINONE OXIDOREDUCTASE (EC 1.6.5.5)       407   408   RXN01842   VV0234   1615   2532   QUINONE OXIDOREDUCTASE (EC 1.6.5.5)       409   410   RXN00641   VV0128   7440   5950   TOLUATE 1,2-DIOXYGENASE ALPHA SUBUNIT (EC 1.14.12.—)       411   412   RXN01993   VV0182   16   1143   VANILLATE DEMETHYLASE (EC 1.14.—.—)       413   414   RXN00658   VV0083   15705   16397   PHENOL 2-MONOOXYGENASE (EC 1.14.13.7)       415   416   RXN00178   VV0174   14670   15554   hydroxyquinol 1,2-dioxygenase (EC 1.13.11.37)       417   418   RXN01461   VV0128   12414   13025   PROTOCATECHUATE 3,4-DIOXYGENASE ALPHA CHAIN (EC 1.13.11.3)       419   420   RXN01653   VV0321   12867   11407   DIBENZOTHIOPHENE DESULFURIZATION ENZYME A       421   422   RXN02053   VV0009   39448   40026   DRGA PROTEIN       423   424   RXN00177   VV0174   13589   14656   MALEYLACETATE REDUCTASE (EC 1.3.1.32)       425   426   RXC00963   VV0249   1816   2652   PROTEIN involved in degradation of aromatic compounds                 Modification and degradation of aliphatic compounds                                         427   428   RXN00299   VV0176   43379   42402   ALKANAL MONOOXYGENASE ALPHA CHAIN (EC 1.14.14.3)       429   430   F RXA00299   GR00048   7376   6633   ALKANAL MONOOXYGENASE ALPHA CHAIN (EC 1.14.14.3)       431   432   RXA00332   GR00057   16086   15385   ALKANAL MONOOXYGENASE ALPHA CHAIN (EC 1.14.14.3)       433   434   RXA01838   GR00519   2   820   ALKANAL MONOOXYGENASE ALPHA CHAIN (EC 1.14.14.3)       435   436   RXA02643   GR00750   1603   560   ALKANAL MONOOXYGENASE ALPHA CHAIN (EC 1.14.14.3)       437   438   RXA01933   GR00555   6590   7192   2-HALOALKANOIC ACID DEHALOGENASE I (EC 3.8.1.2)       439   440   RXA02351   GR00679   132   1070   NITRILOTRIACETATE MONOOXYGENASE                               COMPONENT A (EC 1.14.13.—)                  
 
     
       
         
           
               
             
               
                 TABLE 2 
               
             
            
               
                   
               
               
                   
               
               
                 GENES IDENTIFIED FROM GENBANK 
               
            
           
           
               
               
               
               
            
               
                 GenBank ™ 
                   
                   
                   
               
               
                 Accession No. 
                 Gene Name 
                 Gene Function 
                 Reference 
               
               
                   
               
               
                 A09073 
                 ppg 
                 Phosphoenol pyruvate carboxylase 
                 Bachmann, B. et al. “DNA fragment coding for phosphoenolpyruvat 
               
               
                   
                   
                   
                 corboxylase, recombinant DNA carrying said fragment, strains carrying the 
               
               
                   
                   
                   
                 recombinant DNA and method for producing L-aminino acids using said strains,” Patent: EP 0358940-A 
               
               
                   
                   
                   
                 3 Mar. 21, 1990 
               
               
                 A45579, 
                   
                 Threonine dehydratase 
                 Moeckel, B. et al. “Production of L-isoleucine by means of recombinant 
               
               
                 A45581, 
                   
                   
                 micro-organisms with deregulated threonine dehydratase,” Patent: WO 
               
               
                 A45583, 
                   
                   
                 9519442-A 5 Jul. 20, 1995 
               
               
                 A45585 
               
               
                 A45587 
               
               
                 AB003132 
                 murC; ftsQ; ftsZ 
                   
                 Kobayashi, M. et al. “Cloning, sequencing, and characterization of the ftsZ 
               
               
                   
                   
                   
                 gene from coryneform bacteria,” Biochem. Biophys. Res. Commun., 
               
               
                   
                   
                   
                 236(2): 383-388 (1997) 
               
               
                 AB015023 
                 murC; ftsQ 
                   
                 Wachi, M. et al. “A murC gene from  Coryneform bacteria ,” Appl. Microbiol. 
               
               
                   
                   
                   
                 Biotechnol., 51(2): 223-228 (1999) 
               
               
                 AB018530 
                 dtsR 
                   
                 Kimura, E. et al. “Molecular cloning of a novel gene, dtsR, which rescues the 
               
               
                   
                   
                   
                 detergent sensitivity of a mutant derived from  Brevibacterium   
               
               
                   
                   
                   
                   lactofermentum ,” Biosci. Biotechnol. Biochem., 60(10): 1565-1570 (1996) 
               
               
                 AB018531 
                 dtsR1; dtsR2 
               
               
                 AB020624 
                 murI 
                 D-glutamate racemase 
               
               
                 AB023377 
                 tkt 
                 transketolase 
               
               
                 AB024708 
                 gltB; gltD 
                 Glutamine 2-oxoglutarate aminotransferase 
               
               
                   
                   
                 large and small subunits 
               
               
                 AB025424 
                 acn 
                 aconitase 
               
               
                 AB027714 
                 rep 
                 Replication protein 
               
               
                 AB027715 
                 rep; aad 
                 Replication protein; aminoglycoside 
               
               
                   
                   
                 adenyltransferase 
               
               
                 AF005242 
                 argC 
                 N-acetylglutamate-5-semialdehyde 
               
               
                   
                   
                 dehydrogenase 
               
               
                 AF005635 
                 glnA 
                 Glutamine synthetase 
               
               
                 AF030405 
                 hisF 
                 cyclase 
               
               
                 AF030520 
                 argG 
                 Argininosuccinate synthetase 
               
               
                 AF031518 
                 argF 
                 Ornithine carbamolytransferase 
               
               
                 AF036932 
                 aroD 
                 3-dehydroquinate dehydratase 
               
               
                 AF038548 
                 pyc 
                 Pyruvate carboxylase 
               
               
                 AF038651 
                 dciAE; apt; rel 
                 Dipeptide-binding protein; adenine 
                 Wehmeier, L. et al. “The role of the  Corynebacterium glutamicum  rel gene in 
               
               
                   
                   
                 phosphoribosyltransferase; GTP 
                 (p)ppGpp metabolism,” Microbiology, 144: 1853-1862 (1998) 
               
               
                   
                   
                 pyrophosphokinase 
               
               
                 AF041436 
                 argR 
                 Arginine repressor 
               
               
                 AF045998 
                 impA 
                 Inositol monophosphate phosphatase 
               
               
                 AF048764 
                 argH 
                 Argininosuccinate lyase 
               
               
                 AF049897 
                 argC; argJ; argB; argD; argF; 
                 N-acetylglutamylphosphate reductase; 
               
               
                   
                 argR; argG; argH 
                 ornithine acetyltransferase; N- 
               
               
                   
                   
                 acetylglutamate kinase; acetylornithine 
               
               
                   
                   
                 transminase; ornithine 
               
               
                   
                   
                 carbamoyltransferase; arginine repressor; 
               
               
                   
                   
                 argininosuccinate synthase; 
               
               
                   
                   
                 argininosuccinate lyase 
               
               
                 AF050109 
                 inhA 
                 Enoyl-acyl carrier protein reductase 
               
               
                 AF050166 
                 hisG 
                 ATP phosphoribosyltransferase 
               
               
                 AF051846 
                 hisA 
                 Phosphoribosylformimino-5-amino-1- 
               
               
                   
                   
                 phosphoribosyl-4-imidazolecarboxamide 
               
               
                   
                   
                 isomerase 
               
               
                 AF052652 
                 metA 
                 Homoserine O-acetyltransferase 
                 Park, S. et al. “Isolation and analysis of metA, a methionine biosynthetic gene 
               
               
                   
                   
                   
                 encoding homoserine acetyltransferase in  Corynebacterium glutamicum ,” Mol. 
               
               
                   
                   
                   
                 Cells., 8(3): 286-294 (1998) 
               
               
                 AF053071 
                 aroB 
                 Dehydroquinate synthetase 
               
               
                 AF060558 
                 hisH 
                 Glutamine amidotransferase 
               
               
                 AF086704 
                 hisE 
                 Phosphoribosyl-ATP- 
               
               
                   
                   
                 pyrophosphohydrolase 
               
               
                 AF114233 
                 aroA 
                 5-enolpyruvylshikimate 3-phosphate 
               
               
                   
                   
                 synthase 
               
               
                 AF116184 
                 panD 
                 L-aspartate-alpha-decarboxylase precursor 
                 Dusch, N. et al. “Expression of the  Corynebacterium glutamicum  panD gene 
               
               
                   
                   
                   
                 encoding L-aspartate-alpha-decarboxylase leads to pantothenate 
               
               
                   
                   
                   
                 overproduction in  Escherichia coli ,” Appl. Environ. Microbiol., 65(4)1530-1539 
               
               
                   
                   
                   
                 (1999) 
               
               
                 AF124518 
                 aroD; aroE 
                 3-dehydroquinase; shikimate 
               
               
                   
                   
                 dehydrogenase 
               
               
                 AF124600 
                 aroC; aroK; aroB; 
                 Chorismate synthase; shikimate kinase; 3- 
               
               
                   
                 pepQ 
                 dehydroquinate synthase; putative 
               
               
                   
                   
                 cytoplasmic peptidase 
               
               
                 AF145897 
                 inhA 
               
               
                 AF145898 
                 inhA 
               
               
                 AJ001436 
                 ectP 
                 Transport of ectoine, glycine betaine, 
                 Peter, H. et al. “ Corynebacterium glutamicum  is equipped with four secondary 
               
               
                   
                   
                 proline 
                 carriers for compatible solutes: Identification, sequencing, and characterization 
               
               
                   
                   
                   
                 of the proline/ectoine uptake system, ProP, and the ectoine/proline/glycine betaine carrier, EctP,” J. Bacteriol., 
               
               
                   
                   
                   
                 180(22): 6005-6012 (1998) 
               
               
                 AJ004934 
                 dapD 
                 Tetrahydrodipicolinate succinylase 
                 Wehrmann, A. et al. “Different modes of diaminopimelate synthesis and their 
               
               
                   
                   
                 (incomplete i ) 
                 role in cell wall integrity: A study with  Corynebacterium glutamicum ,” J. Bacteriol., 180(12): 
               
               
                   
                   
                   
                 3159-3165 (1998) 
               
               
                 AJ007732 
                 ppc; secG; amt; ocd; 
                 Phosphoenolpyruvate-carboxylase; ?; high 
               
               
                   
                 soxA 
                 affinity ammonium uptake protein; putative 
               
               
                   
                   
                 ornithine-cyclodecarboxylase; sarcosine 
               
               
                   
                   
                 oxidase 
               
               
                 AJ010319 
                 ftsY, glnB, glnD; srp; 
                 Involved in cell division; PII protein; 
                 Jakoby, M. et al. “Nitrogen regulation in  Corynebacterium glutamicum ; 
               
               
                   
                 amtP 
                 uridylyltransferase (uridylyl-removing 
                 Isolation of genes involved in biochemical characterization of corresponding 
               
               
                   
                   
                 enzmye); signal recognition particle; low 
                 proteins,” FEMS Microbiol., 173(2): 303-310 (1999) 
               
               
                   
                   
                 affinity ammonium uptake protein 
               
               
                 AJ132968 
                 cat 
                 Chloramphenicol aceteyl transferase 
               
               
                 AJ224946 
                 mqo 
                 L-malate: quinone oxidoreductase 
                 Molenaar, D. et al. “Biochemical and genetic characterization of the 
               
               
                   
                   
                   
                 membrane-associated malate dehydrogenase (acceptor) from  Corynebacterium   
               
               
                   
                   
                   
                   glutamicum ,” Eur. J. Biochem., 254(2): 395-403 (1998) 
               
               
                 AJ238250 
                 ndh 
                 NADH dehydrogenase 
               
               
                 AJ238703 
                 porA 
                 Porin 
                 Lichtinger, T. et al. “Biochemical and biophysical characterization of the cell 
               
               
                   
                   
                   
                 wall porin of  Corynebacterium glutamicum : The channel is formed by a low 
               
               
                   
                   
                   
                 molecular mass polypeptide,” Biochemistry, 37(43): 15024-15032 (1998) 
               
               
                 D17429 
                   
                 Transposable element IS31831 
                 Vertes, A. A. et al. “Isolation and characterization of IS31831, a transposable 
               
               
                   
                   
                   
                 element from  Corynebacterium glutamicum ,” Mol. Microbiol., 11(4): 739-746 
               
               
                   
                   
                   
                 (1994) 
               
               
                 D84102 
                 odhA 
                 2-oxoglutarate dehydrogenase 
                 Usuda, Y. et al. “Molecular cloning of the  Corynebacterium glutamicum   
               
               
                   
                   
                   
                 ( Brevibacterium lactofermentum  AJ12036) odhA gene encoding a novel type of 2-oxoglutarate 
               
               
                   
                   
                   
                 dehydrogenase,” Microbiology, 142: 3347-3354 (1996) 
               
               
                 E01358 
                 hdh; hk 
                 Homoserine dehydrogenase; homoserine 
                 Katsumata, R. et al. “Production of L-thereonine and L-isoleucine,” Patent: JP 
               
               
                   
                   
                 kinase 
                 1987232392-A 1 Oct. 12, 1987 
               
               
                 E01359 
                   
                 Upstream of the start codon of homoserine 
                 Katsumata, R. et al. “Production of L-thereonine and L-isoleucine,” Patent: JP 
               
               
                   
                   
                 kinase gene 
                 1987232392-A 2 Oct. 12, 1987 
               
               
                 E01375 
                   
                 Tryptophan operon 
               
               
                 E01376 
                 trpL; trpE 
                 Leader peptide; anthranilate synthase 
                 Matsui, K. et al. “Tryptophan operon, peptide and protein coded thereby, 
               
               
                   
                   
                   
                 utilization of tryptophan operon gene expression and production of 
               
               
                   
                   
                   
                 tryptophan,” Patent: JP 1987244382-A 1 Oct. 24, 1987 
               
               
                 E01377 
                   
                 Promoter and operator regions of 
                 Matsui, K. et al. “Tryptophan operon, peptide and protein coded thereby, 
               
               
                   
                   
                 tryptophan operon 
                 utilization of tryptophan operon gene expression and production of 
               
               
                   
                   
                   
                 tryptophan,” Patent: JP 1987244382-A 1 Oct. 24, 1987 
               
               
                 E03937 
                   
                 Biotin-synthase 
                 Hatakeyama, K. et al. “DNA fragment containing gene capable of coding 
               
               
                   
                   
                   
                 biotin synthetase and its utilization,” Patent: JP 1992278088-A 1 Oct. 02, 1992 
               
               
                 E04040 
                   
                 Diamino pelargonic acid aminotransferase 
                 Kohama, K. et al. “Gene coding diaminopelargonic acid aminotransferase and 
               
               
                   
                   
                   
                 desthiobiotin synthetase and its utilization,” Patent: JP 1992330284-A 1 
               
               
                   
                   
                   
                 Nov. 18, 1992 
               
               
                 E04041 
                   
                 Desthiobiotinsynthetase 
                 Kohama, K. et al. “Gene coding diaminopelargonic acid aminotransferase and 
               
               
                   
                   
                   
                 desthiobiotin synthetase and its utilization,” Patent: JP 1992330284-A 1 
               
               
                   
                   
                   
                 Nov. 18, 1992 
               
               
                 E04307 
                   
                 Flavum aspartase 
                 Kurusu, Y. et al. “Gene DNA coding aspartase and utilization thereof,” Patent: JP 1993030977-A 
               
               
                   
                   
                   
                 1 Feb. 09, 1993 
               
               
                 E04376 
                   
                 Isocitric acid lyase 
                 Katsumata, R. et al. “Gene manifestation controlling DNA,” Patent: JP 
               
               
                   
                   
                   
                 1993056782-A 3 Mar. 09, 1993 
               
               
                 E04377 
                   
                 Isocitric acid lyase N-terminal fragment 
                 Katsumata, R. et al. “Gene manifestation controlling DNA,” Patent: JP 
               
               
                   
                   
                   
                 1993056782-A 3 Mar. 09, 1993 
               
               
                 E04484 
                   
                 Prephenate dehydratase 
                 Sotouchi, N. et al. “Production of L-phenylalanine by fermentation,” Patent: JP 
               
               
                   
                   
                   
                 1993076352-A 2 Mar. 30, 1993 
               
               
                 E05108 
                   
                 Aspartokinase 
                 Fugono, N. et al. “Gene DNA coding Aspartokinase and its use,” Patent: JP 
               
               
                   
                   
                   
                 1993184366-A 1 Jul. 27, 1993 
               
               
                 E05112 
                   
                 Dihydro-dipichorinate synthetase 
                 Hatakeyama, K. et al. “Gene DNA coding dihydrodipicolinic acid synthetase 
               
               
                   
                   
                   
                 and its use,” Patent: JP 1993184371-A 1 Jul. 27, 1993 
               
               
                 E05776 
                   
                 Diaminopimelic acid dehydrogenase 
                 Kobayashi, M. et al. “Gene DNA coding Diaminopimelic acid dehydrogenase 
               
               
                   
                   
                   
                 and its use,” Patent: JP 1993284970-A 1 Nov. 02, 1993 
               
               
                 E05779 
                   
                 Threonine synthase 
                 Kohama, K. et al. “Gene DNA coding threonine synthase and its use,” Patent: 
               
               
                   
                   
                   
                 JP 1993284972-A 1 Nov. 02, 1993 
               
               
                 E06110 
                   
                 Prephenate dehydratase 
                 Kikuchi, T. et al. “Production of L-phenylalanine by fermentation method,” 
               
               
                   
                   
                   
                 Patent: JP 1993344881-A 1 Dec. 27, 1993 
               
               
                 E06111 
                   
                 Mutated Prephenate dehydratase 
                 Kikuchi, T. et al. “Production of L-phenylalanine by fermentation method,” 
               
               
                   
                   
                   
                 Patent: JP 1993344881-A 1 Dec. 27, 1993 
               
               
                 E06146 
                   
                 Acetohydroxy acid synthetase 
                 Inui, M. et al. “Gene capable of coding Acetohydroxy acid synthetase and its 
               
               
                   
                   
                   
                 use,” Patent: JP 1993344893-A 1 Dec. 27, 1993 
               
               
                 E06825 
                   
                 Aspartokinase 
                 Sugimoto, M. et al. “Mutant aspartokinase gene,” patent: JP 1994062866-A 1 
               
               
                   
                   
                   
                 Mar. 08, 1994 
               
               
                 E06826 
                   
                 Mutated aspartokinase alpha subunit 
                 Sugimoto, M. et al. “Mutant aspartokinase gene,” patent: JP 1994062866-A 1 
               
               
                   
                   
                   
                 Mar. 08, 1994 
               
               
                 E06827 
                   
                 Mutated aspartokinase alpha subunit 
                 Sugimoto, M. et al. “Mutant aspartokinase gene,” patent: JP 1994062866-A 1 
               
               
                   
                   
                   
                 Mar. 08, 1994 
               
               
                 E07701 
                 secY 
                   
                 Honno, N. et al. “Gene DNA participating in integration of membraneous 
               
               
                   
                   
                   
                 protein to membrane,” Patent: JP 1994169780-A 1 Jun. 21, 1994 
               
               
                 E08177 
                   
                 Aspartokinase 
                 Sato, Y. et al. “Genetic DNA capable of coding Aspartokinase released from 
               
               
                   
                   
                   
                 feedback inhibition and its utilization,” Patent: JP 1994261766-A 1 Sep. 20, 1994 
               
               
                 E08178, 
                   
                 Feedback inhibition-released Aspartokinase 
                 Sato, Y. et al. “Genetic DNA capable of coding Aspartokinase released from 
               
               
                 E08179, 
                   
                   
                 feedback inhibition and its utilization,” Patent: JP 1994261766-A 1 Sep. 20, 1994 
               
               
                 E08180, 
               
               
                 E08181, 
               
               
                 E08182 
               
               
                 E08232 
                   
                 Acetohydroxy-acid isomeroreductase 
                 Inui, M. et al. “Gene DNA coding acetohydroxy acid isomeroreductase,” Patent: JP 1994277067-A 
               
               
                   
                   
                   
                 1 Oct. 04, 1994 
               
               
                 E08234 
                 secE 
                   
                 Asai, Y. et al. “Gene DNA coding for translocation machinery of protein,” 
               
               
                   
                   
                   
                 Patent: JP 1994277073-A 1 Oct. 04, 1994 
               
               
                 E08643 
                   
                 FT aminotransferase and desthiobiotin 
                 Hatakeyama, K. et al. “DNA fragment having promoter function in 
               
               
                   
                   
                 synthetase promoter region 
                   coryneform bacterium ,” Patent: JP 1995031476-A 1 Feb. 03, 1995 
               
               
                 E08646 
                   
                 Biotin synthetase 
                 Hatakeyama, K. et al. “DNA fragment having promoter function in 
               
               
                   
                   
                   
                   coryneform bacterium ,” Patent: JP 1995031476-A 1 Feb. 03, 1995 
               
               
                 E08649 
                   
                 Aspartase 
                 Kohama, K. et al “DNA fragment having promoter function in  coryneform   
               
               
                   
                   
                   
                   bacterium ,” Patent: JP 1995031478-A 1 Feb. 03, 1995 
               
               
                 E08900 
                   
                 Dihydrodipicolinate reductase 
                 Madori, M. et al. “DNA fragment containing gene coding Dihydrodipicolinate 
               
               
                   
                   
                   
                 acid reductase and utilization thereof,” Patent: JP 1995075578-A 1 Mar. 20, 1995 
               
               
                 E08901 
                   
                 Diaminopimelic acid decarboxylase 
                 Madori, M. et al. “DNA fragment containing gene coding Diaminopimelic acid 
               
               
                   
                   
                   
                 decarboxylase and utilization thereof,” Patent: JP 1995075579-A 1 Mar. 20, 1995 
               
               
                 E12594 
                   
                 Serine hydroxymethyltransferase 
                 Hatakeyama, K. et al. “Production of L-trypophan,” Patent: JP 1997028391-A 
               
               
                   
                   
                   
                 1 Feb. 4, 1997 
               
               
                 E12760, 
                   
                 transposase 
                 Moriya, M. et al. “Amplification of gene using artificial transposon,” Patent: 
               
               
                 E12759, 
                   
                   
                 JP 1997070291-A Mar. 18, 1997 
               
               
                 E12758 
               
               
                 E12764 
                   
                 Arginyl-tRNA synthetase; diaminopimelic 
                 Moriya, M. et al. “Amplification of gene using artificial transposon,” Patent: 
               
               
                   
                   
                 acid decarboxylase 
                 JP 1997070291-A Mar. 18, 1997 
               
               
                 E12767 
                   
                 Dihydrodipicolinic acid synthetase 
                 Moriya, M. et al. “Amplification of gene using artificial transposon,” Patent: 
               
               
                   
                   
                   
                 JP 1997070291-A Mar. 18, 1997 
               
               
                 E12770 
                   
                 aspartokinase 
                 Moriya, M. et al. “Amplification of gene using artificial transposon,” Patent: 
               
               
                   
                   
                   
                 JP 1997070291-A Mar. 18, 1997 
               
               
                 E12773 
                   
                 Dihydrodipicolinic acid reductase 
                 Moriya, M. et al. “Amplification of gene using artificial transposon,” Patent: 
               
               
                   
                   
                   
                 JP 1997070291-A Mar. 18, 1997 
               
               
                 E13655 
                   
                 Glucose-6-phosphate dehydrogenase 
                 Hatakeyama, K. et al. “Glucose-6-phosphate dehydrogenase and DNA capable 
               
               
                   
                   
                   
                 of coding the same,” Patent: JP 1997224661-A 1 Sep. 02, 1997 
               
               
                 L01508 
                 IlvA 
                 Threonine dehydratase 
                 Moeckel, B. et al. “Functional and structural analysis of the threonine 
               
               
                   
                   
                   
                 dehydratase of  Corynebacterium glutamicum ,” J. Bacteriol., 174: 8065-8072 
               
               
                   
                   
                   
                 (1992) 
               
               
                 L07603 
                 EC 4.2.1.15 
                 3-deoxy-D-arabinoheptulosonate-7- 
                 Chen, C. et al. “The cloning and nucleotide sequence of  Corynebacterium   
               
               
                   
                   
                 phosphate synthase 
                   glutamicum  3-deoxy-D-arabinoheptulosonate-7-phosphate synthase gene,” 
               
               
                   
                   
                   
                 FEMS Microbiol. Lett., 107: 223-230 (1993) 
               
               
                 L09232 
                 IlvB; ilvN; ilvC 
                 Acetohydroxy acid synthase large subunit; 
                 Keilhauer, C. et al. “Isoleucine synthesis in  Corynebacterium glutamicum : 
               
               
                   
                   
                 Acetohydroxy acid synthase small subunit; 
                 molecular analysis of the ilvB-ilvN-ilvC operon,” J. Bacteriol., 175(17): 5595-5603 
               
               
                   
                   
                 Acetohydroxy acid isomeroreductase 
                 (1993) 
               
               
                 L18874 
                 PtsM 
                 Phosphoenolpyruvate sugar 
                 Fouet, A et al. “ Bacillus subtilis  sucrose-specific enzyme II of the 
               
               
                   
                   
                 phosphotransferase 
                 phosphotransferase system: expression in  Escherichia coli  and homology to 
               
               
                   
                   
                   
                 enzymes II from enteric bacteria,” PNAS USA, 84(24): 8773-8777 (1987); Lee, J. K. 
               
               
                   
                   
                   
                 et al. “Nucleotide sequence of the gene encoding the  Corynebacterium glutamicum  mannose enzyme 
               
               
                   
                   
                   
                 II and analyses of the deduced protein 
               
               
                   
                   
                   
                 sequence,” FEMS Microbiol. Lett., 119(1-2): 137-145 (1994) 
               
               
                 L27123 
                 aceB 
                 Malate synthase 
                 Lee, H-S. et al. “Molecular characterization of aceB, a gene encoding malate 
               
               
                   
                   
                   
                 synthase in  Corynebacterium glutamicum ,” J. Microbiol. Biotechnol., 
               
               
                   
                   
                   
                 4(4): 256-263 (1994) 
               
               
                 L27126 
                   
                 Pyruvate kinase 
                 Jetten, M. S. et al. “Structural and functional analysis of pyruvate kinase from 
               
               
                   
                   
                   
                   Corynebacterium glutamicum ,” Appl. Environ. Microbiol., 60(7): 2501-2507 
               
               
                   
                   
                   
                 (1994) 
               
               
                 L28760 
                 aceA 
                 Isocitrate lyase 
               
               
                 L35906 
                 dtxr 
                 Diphtheria toxin repressor 
                 Oguiza, J. A. et al. “Molecular cloning, DNA sequence analysis, and 
               
               
                   
                   
                   
                 characterization of the  Corynebacterium diphtheriae  dtxR from  Brevibacterium   
               
               
                   
                   
                   
                   lactofermentum ,” J. Bacteriol., 177(2): 465-467 (1995) 
               
               
                 M13774 
                   
                 Prephenate dehydratase 
                 Follettie, M. T. et al. “Molecular cloning and nucleotide sequence of the 
               
               
                   
                   
                   
                   Corynebacterium glutamicum  pheA gene,” J. Bacteriol., 167: 695-702 (1986) 
               
               
                 M16175 
                 5S rRNA 
                   
                 Park, Y-H. et al. “Phylogenetic analysis of the coryneform bacteria by 56 
               
               
                   
                   
                   
                 rRNA sequences,” J. Bacteriol., 169: 1801-1806 (1987) 
               
               
                 M16663 
                 trpE 
                 Anthranilate synthase, 5′ end 
                 Sano, K. et al. “Structure and function of the trp operon control regions of 
               
               
                   
                   
                   
                   Brevibacterium lactofermentum , a glutamic-acid-producing bacterium,” Gene, 
               
               
                   
                   
                   
                 52: 191-200 (1987) 
               
               
                 M16664 
                 trpA 
                 Tryptophan synthase, 3′end 
                 Sano, K. et al. “Structure and function of the trp operon control regions of 
               
               
                   
                   
                   
                   Brevibacterium lactofermentum , a glutamic-acid-producing bacterium,” Gene, 
               
               
                   
                   
                   
                 52: 191-200 (1987) 
               
               
                 M25819 
                   
                 Phosphoenolpyruvate carboxylase 
                 O&#39;Regan, M. et al. “Cloning and nucleotide sequence of the 
               
               
                   
                   
                   
                 Phosphoenolpyruvate carboxylase-coding gene of  Corynebacterium   
               
               
                   
                   
                   
                   glutamicum  ATCC13032,” Gene, 77(2): 237-251 (1989) 
               
               
                 M85106 
                   
                 23S rRNA gene insertion sequence 
                 Roller, C. et al. “Gram-positive bacteria with a high DNA G + C content are 
               
               
                   
                   
                   
                 characterized by a common insertion within their 23S rRNA genes,” J. Gen. 
               
               
                   
                   
                   
                 Microbiol., 138: 1167-1175 (1992) 
               
               
                 M85107, 
                   
                 23S rRNA gene insertion sequence 
                 Roller, C. et al. “Gram-positive bacteria with a high DNA G + C content are 
               
               
                 M85108 
                   
                   
                 characterized by a common insertion within their 23S rRNA genes,” J. Gen. 
               
               
                   
                   
                   
                 Microbiol., 138: 1167-1175 (1992) 
               
               
                 M89931 
                 aecD; brnQ; yhbw 
                 Beta C-S lyase; branched-chain amino acid 
                 Rossol, I. et al. “The  Corynebacterium glutamicum  aecD gene encodes a C-S 
               
               
                   
                   
                 uptake carrier; hypothetical protein yhbw 
                 lyase with alpha, beta-elimination activity that degrades aminoethylcysteine,” 
               
               
                   
                   
                   
                 J. Bacteriol., 174(9): 2968-2977 (1992); Tauch, A. et al. “Isoleucine uptake in 
               
               
                   
                   
                   
                   Corynebacterium glutamicum  ATCC 13032 is directed by the brnQ gene 
               
               
                   
                   
                   
                 product,” Arch. Microbiol., 169(4): 303-312 (1998) 
               
               
                 S59299 
                 trp 
                 Leader gene (promoter) 
                 Herry, D. M. et al. “Cloning of the trp gene cluster from a tryptophan-hyperproducing strain of 
               
               
                   
                   
                   
                   Corynebacterium glutamicum : identification of a 
               
               
                   
                   
                   
                 mutation in the trp leader sequence,” Appl. Environ. Microbiol., 59(3): 791-799 
               
               
                   
                   
                   
                 (1993) 
               
               
                 U11545 
                 trpD 
                 Anthranilate phosphoribosyltransferase 
                 O&#39;Gara, J. P. and Dunican, L. K. (1994) Complete nucleotide sequence of the 
               
               
                   
                   
                   
                   Corynebacterium glutamicum  ATCC 21850 tpD gene.” Thesis, Microbiology 
               
               
                   
                   
                   
                 Department, University College Galway, Ireland. 
               
               
                 U13922 
                 cglIM; cglIR; clgIIR 
                 Putative type II 5-cytosoine 
                 Schafer, A. et al. “Cloning and characterization of a DNA region encoding a 
               
               
                   
                   
                 methyltransferase; putative type II 
                 stress-sensitive restriction system from  Corynebacterium glutamicum  ATCC 
               
               
                   
                   
                 restriction endonuclease; putative type I or 
                 13032 and analysis of its role in intergeneric conjugation with  Escherichia   
               
               
                   
                   
                 type III restriction endonuclease 
                 coli,” J. Bacteriol., 176(23): 7309-7319 (1994); Schafer, A. et al. “The 
               
               
                   
                   
                   
                   Corynebacterium glutamicum  cglIM gene encoding a 5-cytosine in an McrBC- 
               
               
                   
                   
                   
                 deficient  Escherichia coli  strain,” Gene, 203(2): 95-101 (1997) 
               
               
                 U14965 
                 recA 
               
               
                 U31224 
                 ppx 
                   
                 Ankri, S. et al. “Mutations in the  Corynebacterium glutamicumproline   
               
               
                   
                   
                   
                 biosynthetic pathway: A natural bypass of the proA step,” J. Bacteriol., 
               
               
                   
                   
                   
                 178(15): 4412-4419 (1996) 
               
               
                 U31225 
                 proC 
                 L-proline: NADP+ 5-oxidoreductase 
                 Ankri, S. et al. “Mutations in the  Corynebacterium glutamicumproline   
               
               
                   
                   
                   
                 biosynthetic pathway: A natural bypass of the proA step,” J. Bacteriol., 
               
               
                   
                   
                   
                 178(15): 4412-4419 (1996) 
               
               
                 U31230 
                 obg; proB; unkdh 
                 ?; gamma glutamyl kinase; similar to D- 
                 Ankri, S. et al. “Mutations in the  Corynebacterium glutamicumproline   
               
               
                   
                   
                 isomer specific 2-hydroxyacid 
                 biosynthetic pathway: A natural bypass of the proA step,” J. Bacteriol., 
               
               
                   
                   
                 dehydrogenases 
                 178(15): 4412-4419 (1996) 
               
               
                 U31281 
                 bioB 
                 Biotin synthase 
                 Serebriiskii, I. G., “Two new members of the bio B superfamily: Cloning, 
               
               
                   
                   
                   
                 sequencing and expression of bio B genes of  Methylobacillus flagellatum  and 
               
               
                   
                   
                   
                   Corynebacterium glutamicum ,” Gene, 175: 15-22 (1996) 
               
               
                 U35023 
                 thtR; accBC 
                 Thiosulfate sulfurtransferase; acyl CoA 
                 Jager, W. et al. “A  Corynebacterium glutamicum  gene encoding a two-domain 
               
               
                   
                   
                 carboxylase 
                 protein similar to biotin carboxylases and biotin-carboxyl-carrier proteins,” 
               
               
                   
                   
                   
                 Arch. Microbiol., 166(2); 76-82 (1996) 
               
               
                 U43535 
                 cmr 
                 Multidrug resistance protein 
                 Jager, W. et al. “A  Corynebacterium glutamicum  gene conferring multidrug 
               
               
                   
                   
                   
                 resistance in the heterologous host  Escherichia coli ,” J. Bacteriol., 
               
               
                   
                   
                   
                 179(7): 2449-2451 (1997) 
               
               
                 U43536 
                 clpB 
                 Heat shock ATP-binding protein 
               
               
                 U53587 
                 aphA-3 
                 3′5″-aminoglycoside phosphotransferase 
               
               
                 U89648 
                   
                   Corynebacterium glutamicum  unidentified 
               
               
                   
                   
                 sequence involved in histidine biosynthesis, 
               
               
                   
                   
                 partial sequence 
               
               
                 X04960 
                 trpA; trpB; trpC; trpD; 
                 Tryptophan operon 
                 Matsui, K. et al. “Complete nucleotide and deduced amino acid sequences of 
               
               
                   
                 trpE; trpG; trpL 
                   
                 the  Brevibacterium lactofermentum  tryptophan operon,” Nucleic Acids Res., 
               
               
                   
                   
                   
                 14(24): 10113-10114 (1986) 
               
               
                 X07563 
                 lys A 
                 DAP decarboxylase (meso-diaminopimelate 
                 Yeh, P. et al. “Nucleic sequence of the lysA gene of  Corynebacterium   
               
               
                   
                   
                 decarboxylase, EC 4.1.1.20) 
                   glutamicum  and possible mechanisms for modulation of its expression,” Mol. 
               
               
                   
                   
                   
                 Gen. Genet., 212(1): 112-119 (1988) 
               
               
                 X14234 
                 EC 4.1.1.31 
                 Phosphoenolpyruvate carboxylase 
                 Eikmanns, B. J. et al. “The Phosphoenolpyruvate carboxylase gene of 
               
               
                   
                   
                   
                   Corynebacterium glutamicum : Molecular cloning, nucleotide sequence, and 
               
               
                   
                   
                   
                 expression,” Mol. Gen. Genet., 218(2): 330-339 (1989); Lepiniec, L. et al. 
               
               
                   
                   
                   
                 “Sorghum Phosphoenolpyruvate carboxylase gene family: structure, function 
               
               
                   
                   
                   
                 and molecular evolution,” Plant. Mol. Biol., 21 (3): 487-502 (1993) 
               
               
                 X17313 
                 fda 
                 Fructose-bisphosphate aldolase 
                 Von der Osten, C. H. et al. “Molecular cloning, nucleotide sequence and fine- 
               
               
                   
                   
                   
                 structural analysis of the  Corynebacterium glutamicum  fda gene: structural 
               
               
                   
                   
                   
                 comparison of  C. glutamicum  fructose-1,6-biphosphate aldolase to class I and class II aldolases,” Mol. 
               
               
                   
                   
                   
                 Microbiol., 
               
               
                 X53993 
                 dapA 
                 L-2,3-dihydrodipicolinate synthetase (EC 
                 Bonnassie, S. et al. “Nucleic sequence of the dapA gene from 
               
               
                   
                   
                 4.2.1.52) 
                   Corynebacterium glutamicum ,” Nucleic Acids Res., 18(21): 6421 (1990) 
               
               
                 X54223 
                   
                 AttB-related site 
                 Cianciotto, N. et al. “DNA sequence homology between att B-related sites of 
               
               
                   
                   
                   
                   Corynebacterium diphtheriae ,  Corynebacterium ulcerans ,  Corynebacterium   
               
               
                   
                   
                   
                   glutamicum , and the attP site of lambdacorynephage,” FEMS. Microbiol, 
               
               
                   
                   
                   
                 Lett., 66: 299-302 (1990) 
               
               
                 X54740 
                 argS; lysA 
                 Arginyl-tRNA synthetase; Diaminopimelate 
                 Marcel, T. et al. “Nucleotide sequence and organization of the upstream region 
               
               
                   
                   
                 decarboxylase 
                 of the  Corynebacterium glutamicum  lysA gene,” Mol. Microbiol., 4(11): 1819-1830 
               
               
                   
                   
                   
                 (1990) 
               
               
                 X55994 
                 trpL; trpE 
                 Putative leader peptide; anthranilate 
                 Heery, D. M. et al. “Nucleotide sequence of the  Corynebacterium glutamicum   
               
               
                   
                   
                 synthase component 1 
                 trpE gene,” Nucleic Acids Res., 18(23): 7138 (1990) 
               
               
                 X56037 
                 thrC 
                 Threonine synthase 
                 Han, K. S. et al. “The molecular structure of the  Corynebacterium glutamicum   
               
               
                   
                   
                   
                 threonine synthase gene,” Mol. Microbiol., 4(10): 1693-1702 (1990) 
               
               
                 X56075 
                 attB-related site 
                 Attachment site 
                 Cianciotto, N. et al. “DNA sequence homology between att B-related sites of 
               
               
                   
                   
                   
                   Corynebacterium diphtheriae ,  Corynebacterium ulcerans ,  Corynebacterium   
               
               
                   
                   
                   
                   glutamicum , and the attP site of lambdacorynephage,” FEMS. Microbiol, 
               
               
                   
                   
                   
                 Lett., 66: 299-302 (1990) 
               
               
                 X57226 
                 lysC-alpha; lysC-beta; 
                 Aspartokinase-alpha subunit; 
                 Kalinowski, J. et al. “Genetic and biochemical analysis of the Aspartokinase 
               
               
                   
                 asd 
                 Aspartokinase-beta subunit; aspartate beta 
                 from  Corynebacterium glutamicum ,” Mol. Microbiol., 5(5): 1197-1204 (1991); 
               
               
                   
                   
                 semialdehyde dehydrogenase 
                 Kalinowski, J. et al. “Aspartokinase genes lysC alpha and lysC beta overlap 
               
               
                   
                   
                   
                 and are adjacent to the aspertate beta-semialdehyde dehydrogenase gene asd in 
               
               
                   
                   
                   
                   Corynebacterium glutamicum ,” Mol. Gen. Genet., 224(3): 317-324 (1990) 
               
               
                 X59403 
                 gap; pgk; tpi 
                 Glyceraldehyde-3-phosphate; 
                 Eikmanns, B. J. “Identification, sequence analysis, and expression of a 
               
               
                   
                   
                 phosphoglycerate kinase; triosephosphate 
                   Corynebacterium glutamicum  gene cluster encoding the three glycolytic 
               
               
                   
                   
                 isomerase 
                 enzymes glyceraldehyde-3-phosphate dehydrogenase, 3-phosphoglycerate 
               
               
                   
                   
                   
                 kinase, and triosephosphate isomeras,” J. Bacteriol., 174(19): 6076-6086 
               
               
                   
                   
                   
                 (1992) 
               
               
                 X59404 
                 gdh 
                 Glutamate dehydrogenase 
                 Bormann, E. R. et al. “Molecular analysis of the  Corynebacterium glutamicum   
               
               
                   
                   
                   
                 gdh gene encoding glutamate dehydrogenase,” Mol. Microbiol., 6(3): 317-326 
               
               
                   
                   
                   
                 (1992) 
               
               
                 X60312 
                 lysI 
                 L-lysine permease 
                 Seep-Feldhaus, A. H. et al. “Molecular analysis of the  Corynebacterium   
               
               
                   
                   
                   
                   glutamicum  lysI gene involved in lysine uptake,” Mol. Microbiol., 5(12): 2995-3005 
               
               
                   
                   
                   
                 (1991) 
               
               
                 X66078 
                 cop1 
                 Ps1 protein 
                 Joliff, G. et al. “Cloning and nucleotide sequence of the csp1 gene encoding 
               
               
                   
                   
                   
                 PS1, one of the two major secreted proteins of  Corynebacterium glutamicum : 
               
               
                   
                   
                   
                 The deduced N-terminal region of PS1 is similar to the  Mycobacterium  antigen 
               
               
                   
                   
                   
                 85 complex,” Mol. Microbiol., 6(16): 2349-2362 (1992) 
               
               
                 X66112 
                 glt 
                 Citrate synthase 
                 Eikmanns, B. J. et al. “Cloning sequence, expression and transcriptional 
               
               
                   
                   
                   
                 analysis of the  Corynebacterium glutamicum  gltA gene encoding citrate 
               
               
                   
                   
                   
                 synthase,” Microbiol., 140: 1817-1828 (1994) 
               
               
                 X67737 
                 dapB 
                 Dihydrodipicolinate reductase 
               
               
                 X69103 
                 csp2 
                 Surface layer protein PS2 
                 Peyret, J. L. et al. “Characterization of the cspB gene encoding PS2, an ordered 
               
               
                   
                   
                   
                 surface-layer protein in  Corynebacterium glutamicum ,” Mol. Microbiol., 
               
               
                   
                   
                   
                 9(1): 97-109 (1993) 
               
               
                 X69104 
                   
                 IS3 related insertion element 
                 Bonamy, C. et al. “Identification of IS1206, a  Corynebacterium glutamicum   
               
               
                   
                   
                   
                 IS3-related insertion sequence and phylogenetic analysis,” Mol. Microbiol., 
               
               
                   
                   
                   
                 14(3): 571-581 (1994) 
               
               
                 X70959 
                 leuA 
                 Isopropylmalate synthase 
                 Patek, M. et al. “Leucine synthesis in  Corynebacterium glutamicum : enzyme 
               
               
                   
                   
                   
                 activities, structure of leuA, and effect of leuA inactivation on lysine synthesis,” Appl. Environ. 
               
               
                   
                   
                   
                 Microbiol., 60(1): 133-140 (1994) 
               
               
                 X71489 
                 icd 
                 Isocitrate dehydrogenase (NADP+) 
                 Eikmanns, B. J. et al. “Cloning sequence analysis, expression, and inactivation 
               
               
                   
                   
                   
                 of the  Corynebacterium glutamicum  icd gene encoding isocitrate 
               
               
                   
                   
                   
                 dehydrogenase and biochemical characterization of the enzyme,” J. Bacteriol., 
               
               
                   
                   
                   
                 177(3): 774-782 (1995) 
               
               
                 X72855 
                 GDHA 
                 Glutamate dehydrogenase (NADP+) 
               
               
                 X75083, 
                 mtrA 
                 5-methyltryptophan resistance 
                 Heery, D. M. et al. “A sequence from a tryptophan-hyperproducing strain of 
               
               
                 X70584 
                   
                   
                   Corynebacterium glutamicum  encoding resistance to 5-methyltryptophan,” 
               
               
                   
                   
                   
                 Biochem. Biophys. Res. Commun., 201(3): 1255-1262 (1994) 
               
               
                 X75085 
                 recA 
                   
                 Fitzpatrick, R. et al. “Construction and characterization of recA mutant strains 
               
               
                   
                   
                   
                 of  Corynebacterium glutamicum  and  Brevibacterium lactofermentum ,” Appl. 
               
               
                   
                   
                   
                 Microbiol. Biotechnol., 42(4): 575-580 (1994) 
               
               
                 X75504 
                 aceA; thiX 
                 Partial Isocitrate lyase; ? 
                 Reinscheid, D. J. et al. “Characterization of the isocitrate lyase gene from 
               
               
                   
                   
                   
                   Corynebacterium glutamicum  and biochemical analysis of the enzyme,” J. 
               
               
                   
                   
                   
                 Bacteriol., 176(12): 3474-3483 (1994) 
               
               
                 X76875 
                   
                 ATPase beta-subunit 
                 Ludwig, W. et al. “Phylogenetic relationships of bacteria based on comparative 
               
               
                   
                   
                   
                 sequence analysis of elongation factor Tu and ATP-synthase beta-subunit 
               
               
                   
                   
                   
                 genes,” Antonie Van Leeuwenhoek, 64: 285-305 (1993) 
               
               
                 X77034 
                 tuf 
                 Elongation factor Tu 
                 Ludwig, W. et al. “Phylogenetic relationships of bacteria based on comparative 
               
               
                   
                   
                   
                 sequence analysis of elongation factor Tu and ATP-synthase beta-subunit 
               
               
                   
                   
                   
                 genes,” Antonie Van Leeuwenhoek, 64: 285-305 (1993) 
               
               
                 X77384 
                 recA 
                   
                 Billman-Jacobe, H. “Nucleotide sequence of a recA gene from 
               
               
                   
                   
                   
                   Corynebacterium glutamicum ,” DNA Seq., 4(6): 403-404 (1994) 
               
               
                 X78491 
                 aceB 
                 Malate synthase 
                 Reinscheid, D. J. et al. “Malate synthase from  Corynebacterium glutamicum   
               
               
                   
                   
                   
                 pta-ack operon encoding phosphotransacetylase: sequence analysis,” 
               
               
                   
                   
                   
                 Microbiology, 140: 3099-3108 (1994) 
               
               
                 X80629 
                 16S rDNA 
                 16S ribosomal RNA 
                 Rainey, F. A. et al. “Phylogenetic analysis of the genera  Rhodococcus  and 
               
               
                   
                   
                   
                   Norcardia  and evidence for the evolutionary origin of the genus  Norcardia   
               
               
                   
                   
                   
                 from within the radiation of  Rhodococcus  species,” Microbiol., 141: 523-528 
               
               
                   
                   
                   
                 (1995) 
               
               
                 X81191 
                 gluA; gluB; gluC; 
                 Glutamate uptake system 
                 Kronemeyer, W. et al. “Structure of the gluABCD cluster encoding the 
               
               
                   
                 gluD 
                   
                 glutamate uptake system of  Corynebacterium glutamicum ,” J. Bacteriol., 
               
               
                   
                   
                   
                 177(5): 1152-1158 (1995) 
               
               
                 X81379 
                 dapE 
                 Succinyldiaminopimelate desuccinylase 
                 Wehrmann, A. et al. “Analysis of different DNA fragments of 
               
               
                   
                   
                   
                   Corynebacterium glutamicum  complementing dapE of  Escherichia coli ,” Microbiology, 40: 3349-56 (1994) 
               
               
                 X82061 
                 16S rDNA 
                 16S ribosomal RNA 
                 Ruimy, R. et al. “Phylogeny of the genus  Corynebacterium  deduced from 
               
               
                   
                   
                   
                 analyses of small-subunit ribosomal DNA sequences,” Int. J. Syst. Bacteriol., 
               
               
                   
                   
                   
                 45(4): 740-746 (1995) 
               
               
                 X82928 
                 asd; lysC 
                 Aspartate-semialdehyde dehydrogenase; ? 
                 Serebrijski, I. et al. “Multicopy suppression by asd gene and osmotic stress- 
               
               
                   
                   
                   
                 dependent complementation by heterologous proA in proA mutants,” J. 
               
               
                   
                   
                   
                 Bacteriol., 177(24): 7255-7260 (1995) 
               
               
                 X82929 
                 proA 
                 Gamma-glutamyl phosphate reductase 
                 Serebrijski, I. et al. “Multicopy suppression by asd gene and osmotic stress- 
               
               
                   
                   
                   
                 dependent complementation by heterologous proA in proA mutants,” J. 
               
               
                   
                   
                   
                 Bacteriol., 177(24): 7255-7260 (1995) 
               
               
                 X84257 
                 16S rDNA 
                 16S ribosomal RNA 
                 Pascual, C. et al. “Phylogenetic analysis of the genus  Corynebacterium  based 
               
               
                   
                   
                   
                 on 16S rRNA gene sequences,” Int. J. Syst. Bacteriol., 45(4): 724-728 (1995) 
               
               
                 X85965 
                 aroP; dapE 
                 Aromatic amino acid permease; ? 
                 Wehrmann, A. et al. “Functional analysis of sequences adjacent to dapE of 
               
               
                   
                   
                   
                   Corynebacterium  glutamicumproline reveals the presence of aroP, which 
               
               
                   
                   
                   
                 encodes the aromatic amino acid transporter,” J. Bacteriol., 177(20): 5991-5993 
               
               
                   
                   
                   
                 (1995) 
               
               
                 X86157 
                 argB; argC; argD; 
                 Acetylglutamate kinase; N-acetyl-gamma- 
                 Sakanyan, V. et al. “Genes and enzymes of the acetyl cycle of arginine 
               
               
                   
                 argF; argJ 
                 glutamyl-phosphate reductase; 
                 biosynthesis in  Corynebacterium glutamicum : enzyme evolution in the early 
               
               
                   
                   
                 acetylornithine aminotransferase; ornithine 
                 steps of the arginine pathway,” Microbiology, 142: 99-108 (1996) 
               
               
                   
                   
                 carbamoyltransferase; glutamate N- 
               
               
                   
                   
                 acetyltransferase 
               
               
                 X89084 
                 pta; ackA 
                 Phosphate acetyltransferase; acetate kinase 
                 Reinscheid, D. J. et al. “Cloning, sequence analysis, expression and inactivation 
               
               
                   
                   
                   
                 of the  Corynebacterium glutamicum  pta-ack operon encoding 
               
               
                   
                   
                   
                 phosphotransacetylase and acetate kinase,” Microbiology, 145: 503-513 (1999) 
               
               
                 X89850 
                 attB 
                 Attachment site 
                 Le Marrec, C. et al. “Genetic characterization of site-specific integration 
               
               
                   
                   
                   
                 functions of phi AAU2 infecting “ Arthrobacter aureus  C70,” J. Bacteriol., 
               
               
                   
                   
                   
                 178(7): 1996-2004 (1996) 
               
               
                 X90356 
                   
                 Promoter fragment F1 
                 Patek, M. et al. “Promoters from  Corynebacterium glutamicum : cloning, 
               
               
                   
                   
                   
                 molecular analysis and search for a consensus motif,” Microbiology, 
               
               
                   
                   
                   
                 142: 1297-1309 (1996) 
               
               
                 X90357 
                   
                 Promoter fragment F2 
                 Patek, M. et al. “Promoters from  Corynebacterium glutamicum : cloning, 
               
               
                   
                   
                   
                 molecular analysis and search for a consensus motif,” Microbiology, 
               
               
                   
                   
                   
                 142: 1297-1309 (1996) 
               
               
                 X90358 
                   
                 Promoter fragment F10 
                 Patek, M. et al. “Promoters from  Corynebacterium glutamicum : cloning, 
               
               
                   
                   
                   
                 molecular analysis and search for a consensus motif,” Microbiology, 
               
               
                   
                   
                   
                 142: 1297-1309 (1996) 
               
               
                 X90359 
                   
                 Promoter fragment F13 
                 Patek, M. et al. “Promoters from  Corynebacterium glutamicum : cloning, 
               
               
                   
                   
                   
                 molecular analysis and search for a consensus motif,” Microbiology, 
               
               
                   
                   
                   
                 142: 1297-1309 (1996) 
               
               
                 X90360 
                   
                 Promoter fragment F22 
                 Patek, M. et al. “Promoters from  Corynebacterium glutamicum : cloning, 
               
               
                   
                   
                   
                 molecular analysis and search for a consensus motif,” Microbiology, 
               
               
                   
                   
                   
                 142: 1297-1309 (1996) 
               
               
                 X90361 
                   
                 Promoter fragment F34 
                 Patek, M. et al. “Promoters from  Corynebacterium glutamicum : cloning, 
               
               
                   
                   
                   
                 molecular analysis and search for a consensus motif,” Microbiology, 
               
               
                   
                   
                   
                 142: 1297-1309 (1996) 
               
               
                 X90362 
                   
                 Promoter fragment F37 
                 Patek, M. et al. “Promoters from  Corynebacterium glutamicum : cloning, 
               
               
                   
                   
                   
                 molecular analysis and search for a consensus motif,” Microbiology, 142: 1297-1309 (1996) 
               
               
                 X90363 
                   
                 Promoter fragment F45 
                 Patek, M. et al. “Promoters from  Corynebacterium glutamicum : cloning, 
               
               
                   
                   
                   
                 molecular analysis and search for a consensus motif,” Microbiology, 
               
               
                   
                   
                   
                 142: 1297-1309 (1996) 
               
               
                 X90364 
                   
                 Promoter fragment F64 
                 Patek, M. et al. “Promoters from  Corynebacterium glutamicum : cloning, 
               
               
                   
                   
                   
                 molecular analysis and search for a consensus motif,” Microbiology, 
               
               
                   
                   
                   
                 142: 1297-1309 (1996) 
               
               
                 X90365 
                   
                 Promoter fragment F75 
                 Patek, M. et al. “Promoters from  Corynebacterium glutamicum : cloning, 
               
               
                   
                   
                   
                 molecular analysis and search for a consensus motif,” Microbiology, 
               
               
                   
                   
                   
                 142: 1297-1309 (1996) 
               
               
                 X90366 
                   
                 Promoter fragment PF101 
                 Patek, M. et al. “Promoters from  Corynebacterium glutamicum : cloning, 
               
               
                   
                   
                   
                 molecular analysis and search for a consensus motif,” Microbiology, 
               
               
                   
                   
                   
                 142: 1297-1309 (1996) 
               
               
                 X90367 
                   
                 Promoter fragment PF104 
                 Patek, M. et al. “Promoters from  Corynebacterium glutamicum : cloning, 
               
               
                   
                   
                   
                 molecular analysis and search for a consensus motif,” Microbiology, 
               
               
                   
                   
                   
                 142: 1297-1309 (1996) 
               
               
                 X90368 
                   
                 Promoter fragment PF109 
                 Patek, M. et al. “Promoters from  Corynebacterium glutamicum : cloning, 
               
               
                   
                   
                   
                 molecular analysis and search for a consensus motif,” Microbiology, 
               
               
                   
                   
                   
                 142: 1297-1309 (1996) 
               
               
                 X93513 
                 amt 
                 Ammonium transport system 
                 Siewe, R. M. et al. “Functional and genetic characterization of the (methyl) 
               
               
                   
                   
                   
                 ammonium uptake carrier of  Corynebacterium glutamicum ,” J. Biol. Chem., 
               
               
                   
                   
                   
                 271(10): 5398-5403 (1996) 
               
               
                 X93514 
                 betP 
                 Glycine betaine transport system 
                 Peter, H. et al. “Isolation, characterization, and expression of the 
               
               
                   
                   
                   
                   Corynebacterium glutamicum  betP gene, encoding the transport system for the 
               
               
                   
                   
                   
                 compatible solute glycine betaine,” J. Bacteriol., 178(17): 5229-5234 (1996) 
               
               
                 X95649 
                 orf4 
                   
                 Patek, M. et al. “Identification and transcriptional analysis of the dapB-ORF2- 
               
               
                   
                   
                   
                 dapA-ORF4 operon of  Corynebacterium glutamicum , encoding two enzymes 
               
               
                   
                   
                   
                 involved in L-lysine synthesis,” Biotechnol. Lett., 19: 1113-1117 (1997) 
               
               
                 X96471 
                 lysE; lysG 
                 Lysine exporter protein; Lysine export 
                 Vrljic, M. et al. “A new type of transporter with a new type of cellular 
               
               
                   
                   
                 regulator protein 
                 function: L-lysine export from  Corynebacterium glutamicum ,” Mol. 
               
               
                   
                   
                   
                 Microbiol., 22(5): 815-826 (1996) 
               
               
                 X96580 
                 panB; panC; xylB 
                 3-methyl-2-oxobutanoate 
                 Sahm, H. et al. “D-pantothenate synthesis in  Corynebacterium glutamicum  and 
               
               
                   
                   
                 hydroxymethyltransferase; pantoate-beta- 
                 use of panBC and genes encoding L-valine synthesis for D-pantothenate 
               
               
                   
                   
                 alanine ligase; xylulokinase 
                 overproduction,” Appl. Environ. Microbiol., 65(5): 1973-1979 (1999) 
               
               
                 X96962 
                   
                 Insertion sequence IS1207 and transposase 
               
               
                 X99289 
                   
                 Elongation factor P 
                 Ramos, A. et al. “Cloning, sequencing and expression of the gene encoding 
               
               
                   
                   
                   
                 elongation factor P in the amino-acid producer  Brevibacterium lactofermentum   
               
               
                   
                   
                   
                 ( Corynebacterium glutamicum  ATCC 13869),” Gene, 198: 217-222 (1997) 
               
               
                 Y00140 
                 thrB 
                 Homoserine kinase 
                 Mateos, L. M. et al. “Nucleotide sequence of the homoserine kinase (thrB) gene 
               
               
                   
                   
                   
                 of the  Brevibacterium lactofermentum ,” Nucleic Acids Res., 15(9): 3922 (1987) 
               
               
                 Y00151 
                 ddh 
                 Meso-diaminopimelate D-dehydrogenase 
                 Ishino, S. et al. “Nucleotide sequence of the meso-diaminopimelate D- 
               
               
                   
                   
                 (EC 1.4.1.16) 
                 dehydrogenase gene from  Corynebacterium glutamicum ,” Nucleic Acids Res., 
               
               
                   
                   
                   
                 15(9): 3917 (1987) 
               
               
                 Y00476 
                 thrA 
                 Homoserine dehydrogenase 
                 Mateos, L. M. et al. “Nucleotide sequence of the homoserine dehydrogenase 
               
               
                   
                   
                   
                 (thrA) gene of the  Brevibacterium lactofermentum ,” Nucleic Acids Res., 15(24): 10598 (1987) 
               
               
                 Y00546 
                 hom; thrB 
                 Homoserine dehydrogenase; homoserine 
                 Peoples, O. P. et al. “Nucleotide sequence and fine structural analysis of the 
               
               
                   
                   
                 kinase 
                   Corynebacterium glutamicum  hom-thrB operon,” Mol. Microbiol., 2(1): 63-72 
               
               
                   
                   
                   
                 (1988) 
               
               
                 Y08964 
                 murC; ftsQ/divD; ftsZ 
                 UPD-N-acetylmuramate-alanine ligase; 
                 Honrubia, M. P. et al. “Identification, characterization, and chromosomal 
               
               
                   
                   
                 division initiation protein or cell division 
                 organization of the ftsZ gene from  Brevibacterium lactofermentum ,” Mol. Gen. 
               
               
                   
                   
                 protein; cell division protein 
                 Genet., 259(1): 97-104 (1998) 
               
               
                 Y09163 
                 putP 
                 High affinity proline transport system 
                 Peter, H. et al. “Isolation of the putP gene of  Corynebacterium   
               
               
                   
                   
                   
                   glutamicumproline  and characterization of a low-affinity uptake system for 
               
               
                   
                   
                   
                 compatible solutes,” Arch. Microbiol., 168(2): 143-151 (1997) 
               
               
                 Y09548 
                 pyc 
                 Pyruvate carboxylase 
                 Peters-Wendisch, P. G. et al. “Pyruvate carboxylase from  Corynebacterium   
               
               
                   
                   
                   
                   glutamicum : characterization, expression and inactivation of the pyc gene,” 
               
               
                   
                   
                   
                 Microbiology, 144: 915-927 (1998) 
               
               
                 Y09578 
                 leuB 
                 3-isopropylmalate dehydrogenase 
                 Patek, M. et al. “Analysis of the leuB gene from  Corynebacterium   
               
               
                   
                   
                   
                   glutamicum ,” Appl. Microbiol. Biotechnol., 50(1): 42-47 (1998) 
               
               
                 Y12472 
                   
                 Attachment site bacteriophage Phi-16 
                 Moreau, S. et al. “Site-specific integration of corynephage Phi-16: The 
               
               
                   
                   
                   
                 construction of an integration vector,” Microbiol., 145: 539-548 (1999) 
               
               
                 Y12537 
                 proP 
                 Proline/ectoine uptake system protein 
                 Peter, H. et al. “ Corynebacterium glutamicum  is equipped with four secondary 
               
               
                   
                   
                   
                 carriers for compatible solutes: Identification, sequencing, and characterization 
               
               
                   
                   
                   
                 of the proline/ectoine uptake system, ProP, and the ectoine/proline/glycine 
               
               
                   
                   
                   
                 betaine carrier, EctP,” J. Bacteriol., 180(22): 6005-6012 (1998) 
               
               
                 Y13221 
                 glnA 
                 Glutamine synthetase I 
                 Jakoby, M. et al. “Isolation of  Corynebacterium glutamicum  glnA gene 
               
               
                   
                   
                   
                 encoding glutamine synthetase I,” FEMS Microbiol. Lett., 154(1): 81-88 (1997) 
               
               
                 Y16642 
                 lpd 
                 Dihydrolipoamide dehydrogenase 
               
               
                 Y18059 
                   
                 Attachment site Corynephage 304L 
                 Moreau, S. et al. “Analysis of the integration functions of &amp;phi; 304L: An 
               
               
                   
                   
                   
                 integrase module among corynephages,” Virology, 255(1): 150-159 (1999) 
               
               
                 Z21501 
                 argS; lysA 
                 Arginyl-tRNA synthetase; diaminopimelate 
                 Oguiza, J. A. et al. “A gene encoding arginyl-tRNA synthetase is located in the 
               
               
                   
                   
                 decarboxylase (partial) 
                 upstream region of the lysA gene in  Brevibacterium lactofermentum : 
               
               
                   
                   
                   
                 Regulation of argS-lysA cluster expression by arginine,” J. Bacteriol., 
               
               
                   
                   
                   
                 175(22): 7356-7362 (1993) 
               
               
                 Z21502 
                 dapA; dapB 
                 Dihydrodipicolinate synthase; 
                 Pisabarro, A. et al. “A cluster of three genes (dapA, orf2, and dapB) of 
               
               
                   
                   
                 dihydrodipicolinate reductase 
                   Brevibacterium lactofermentum  encodes dihydrodipicolinate reductase, and a 
               
               
                   
                   
                   
                 third polypeptide of unknown function,” J. Bacteriol., 175(9): 2743-2749 
               
               
                   
                   
                   
                 (1993) 
               
               
                 Z29563 
                 thrC 
                 Threonine synthase 
                 Malumbres, M. et al. “Analysis and expression of the thrC gene of the encoded 
               
               
                   
                   
                   
                 threonine synthase,” Appl. Environ. Microbiol., 60(7)2209-2219 (1994) 
               
               
                 Z46753 
                 16S rDNA 
                 Gene for 16S ribosomal RNA 
               
               
                 Z49822 
                 sigA 
                 SigA sigma factor 
                 Oguiza, J. A. et al “Multiple sigma factor genes in  Brevibacterium   
               
               
                   
                   
                   
                   lactofermentum : Characterization of sigA and sigB,” J. Bacteriol., 178(2): 550-553 
               
               
                   
                   
                   
                 (1996) 
               
               
                 Z49823 
                 galE; dtxR 
                 Catalytic activity UDP-galactose 4- 
                 Oguiza, J. A. et al “The galE gene encoding the UDP-galactose 4-epimerase of 
               
               
                   
                   
                 epimerase; diphtheria toxin regulatory 
                   Brevibacterium lactofermentum  is coupled transcriptionally to the dmdR 
               
               
                   
                   
                 protein 
                 gene,” Gene, 177: 103-107 (1996) 
               
               
                 Z49824 
                 orfl; sigB 
                 ?; SigB sigma factor 
                 Oguiza, J. A. et al “Multiple sigma factor genes in  Brevibacterium   
               
               
                   
                   
                   
                   lactofermentum : Characterization of sigA and sigB,” J. Bacteriol., 178(2): 550-553 
               
               
                   
                   
                   
                 (1996) 
               
               
                 Z66534 
                   
                 Transposase 
                 Correia, A. et al. “Cloning and characterization of an IS-like element present in 
               
               
                   
                   
                   
                 the genome of  Brevibacterium lactofermentum  ATCC 13869,” Gene, 
               
               
                   
                   
                   
                 170(1): 91-94 (1996) 
               
               
                   
               
               
                     1 A sequence for this gene was published in the indicated reference. However, the sequence obtained by the inventors of the present application is significantly longer than the published version. It is believed that the published version relied on an incorrect start codon, and thus represents only a fragment of the actual coding region.    
               
            
           
         
       
     
     
       
         
           
               
             
               
                 TABLE 3 
               
             
            
               
                   
               
               
                   
               
               
                   Corynebacterium  and  Brevibacterium  Strains Which May be Used in the Practice of the Invention 
               
            
           
           
               
               
               
               
               
               
               
               
               
               
            
               
                 Genus 
                 species 
                 ATCC 
                 FERM 
                 NRRL 
                 CECT 
                 NCIMB 
                 CBS 
                 NCTC 
                 DSMZ 
               
               
                   
               
            
           
           
               
               
               
               
               
               
               
               
               
               
            
               
                 
                   Brevibacterium 
                 
                 
                   ammoniagenes 
                 
                 21054 
                   
                   
                   
                   
                   
                   
                   
               
               
                 
                   Brevibacterium 
                 
                 
                   ammoniagenes 
                 
                 19350 
               
               
                 
                   Brevibacterium 
                 
                 
                   ammoniagenes 
                 
                 19351 
               
               
                 
                   Brevibacterium 
                 
                 
                   ammoniagenes 
                 
                 19352 
               
               
                 
                   Brevibacterium 
                 
                 
                   ammoniagenes 
                 
                 19353 
               
               
                 
                   Brevibacterium 
                 
                 
                   ammoniagenes 
                 
                 19354 
               
               
                 
                   Brevibacterium 
                 
                 
                   ammoniagenes 
                 
                 19355 
               
               
                 
                   Brevibacterium 
                 
                 
                   ammoniagenes 
                 
                 19356 
               
               
                 
                   Brevibacterium 
                 
                 
                   ammoniagenes 
                 
                 21055 
               
               
                 
                   Brevibacterium 
                 
                 
                   ammoniagenes 
                 
                 21077 
               
               
                 
                   Brevibacterium 
                 
                 
                   ammoniagenes 
                 
                 21553 
               
               
                 
                   Brevibacterium 
                 
                 
                   ammoniagenes 
                 
                 21580 
               
               
                 
                   Brevibacterium 
                 
                 
                   ammoniagenes 
                 
                 39101 
               
               
                 
                   Brevibacterium 
                 
                 
                   butanicum 
                 
                 21196 
               
               
                 
                   Brevibacterium 
                 
                 
                   divaricatum 
                 
                 21792 
                 P928 
               
               
                 
                   Brevibacterium 
                 
                 
                   flavum 
                 
                 21474 
               
               
                 
                   Brevibacterium 
                 
                 
                   flavum 
                 
                 21129 
               
               
                 
                   Brevibacterium 
                 
                 
                   flavum 
                 
                 21518 
               
               
                 
                   Brevibacterium 
                 
                 
                   flavum 
                 
                   
                   
                 B11474 
               
               
                 
                   Brevibacterium 
                 
                 
                   flavum 
                 
                   
                   
                 B11472 
               
               
                 
                   Brevibacterium 
                 
                 
                   flavum 
                 
                 21127 
               
               
                 
                   Brevibacterium 
                 
                 
                   flavum 
                 
                 21128 
               
               
                 
                   Brevibacterium 
                 
                 
                   flavum 
                 
                 21427 
               
               
                 
                   Brevibacterium 
                 
                 
                   flavum 
                 
                 21475 
               
               
                 
                   Brevibacterium 
                 
                 
                   flavum 
                 
                 21517 
               
               
                 
                   Brevibacterium 
                 
                 
                   flavum 
                 
                 21528 
               
               
                 
                   Brevibacterium 
                 
                 
                   flavum 
                 
                 21529 
               
               
                 
                   Brevibacterium 
                 
                 
                   flavum 
                 
                   
                   
                 B11477 
               
               
                 
                   Brevibacterium 
                 
                 
                   flavum 
                 
                   
                   
                 B11478 
               
               
                 
                   Brevibacterium 
                 
                 
                   flavum 
                 
                 21127 
               
               
                 
                   Brevibacterium 
                 
                 
                   flavum 
                 
                   
                   
                 B11474 
               
               
                 
                   Brevibacterium 
                 
                 
                   healii 
                 
                 15527 
               
               
                 
                   Brevibacterium 
                 
                 
                   keto 
                   glutamicum 
                 
                 21004 
               
               
                 
                   Brevibacterium 
                 
                 
                   keto 
                   glutamicum 
                 
                 21089 
               
               
                 
                   Brevibacterium 
                 
                 
                   ketosoreductum 
                 
                 21914 
               
               
                 
                   Brevibacterium 
                 
                 
                   lactofermentum 
                 
                   
                   
                   
                 70 
               
               
                 
                   Brevibacterium 
                 
                 
                   lactofermentum 
                 
                   
                   
                   
                 74 
               
               
                 
                   Brevibacterium 
                 
                 
                   lactofermentum 
                 
                   
                   
                   
                 77 
               
               
                 
                   Brevibacterium 
                 
                 
                   lactofermentum 
                 
                 21798 
               
               
                 
                   Brevibacterium 
                 
                 
                   lactofermentum 
                 
                 21799 
               
               
                 
                   Brevibacterium 
                 
                 
                   lactofermentum 
                 
                 21800 
               
               
                 
                   Brevibacterium 
                 
                 
                   lactofermentum 
                 
                 21801 
               
               
                 
                   Brevibacterium 
                 
                 
                   lactofermentum 
                 
                   
                   
                 B11470 
               
               
                 
                   Brevibacterium 
                 
                 
                   lactofermentum 
                 
                   
                   
                 B11471 
               
               
                 
                   Brevibacterium 
                 
                 
                   lactofermentum 
                 
                 21086 
               
               
                 
                   Brevibacterium 
                 
                 
                   lactofermentum 
                 
                 21420 
               
               
                 
                   Brevibacterium 
                 
                 
                   lactofermentum 
                 
                 21086 
               
               
                 
                   Brevibacterium 
                 
                 
                   lactofermentum 
                 
                 31269 
               
               
                 
                   Brevibacterium 
                 
                 
                   linens 
                 
                 9174 
               
               
                 
                   Brevibacterium 
                 
                 
                   linens 
                 
                 19391 
               
               
                 
                   Brevibacterium 
                 
                 
                   linens 
                 
                 8377 
               
               
                 
                   Brevibacterium 
                 
                 
                   paraffinolyticum 
                 
                   
                   
                   
                   
                 11160 
               
               
                 
                   Brevibacterium 
                 
                 spec. 
                   
                   
                   
                   
                   
                 717.73 
               
               
                 
                   Brevibacterium 
                 
                 spec. 
                   
                   
                   
                   
                   
                 717.73 
               
               
                 
                   Brevibacterium 
                 
                 spec. 
                 14604 
               
               
                 
                   Brevibacterium 
                 
                 spec. 
                 21860 
               
               
                 
                   Brevibacterium 
                 
                 spec. 
                 21864 
               
               
                 
                   Brevibacterium 
                 
                 spec. 
                 21865 
               
               
                 
                   Brevibacterium 
                 
                 spec. 
                 21866 
               
               
                 
                   Brevibacterium 
                 
                 spec. 
                 19240 
               
               
                 
                   Corynebacterium 
                 
                 
                   acetoacidophilum 
                 
                 21476 
               
               
                 
                   Corynebacterium 
                 
                 
                   acetoacidophilum 
                 
                 13870 
               
               
                 
                   Corynebacterium 
                 
                 
                   aceto 
                   glutamicum 
                 
                   
                   
                 B11473 
               
               
                 
                   Corynebacterium 
                 
                 
                   aceto 
                   glutamicum 
                 
                   
                   
                 B11475 
               
               
                 
                   Corynebacterium 
                 
                 
                   aceto 
                   glutamicum 
                 
                 15806 
               
               
                 
                   Corynebacterium 
                 
                 
                   aceto 
                   glutamicum 
                 
                 21491 
               
               
                 
                   Corynebacterium 
                 
                 
                   aceto 
                   glutamicum 
                 
                 31270 
               
               
                 
                   Corynebacterium 
                 
                 
                   acetophilum 
                 
                   
                   
                 B3671 
               
               
                 
                   Corynebacterium 
                 
                 
                   ammoniagenes 
                 
                 6872 
                   
                   
                   
                   
                   
                 2399 
               
               
                 
                   Corynebacterium 
                 
                 
                   ammoniagenes 
                 
                 15511 
               
               
                 
                   Corynebacterium 
                 
                 
                   fujiokense 
                 
                 21496 
               
               
                 
                   Corynebacterium 
                 
                 
                   glutamicum 
                 
                 14067 
               
               
                 
                   Corynebacterium 
                 
                 
                   glutamicum 
                 
                 39137 
               
               
                 
                   Corynebacterium 
                 
                 
                   glutamicum 
                 
                 21254 
               
               
                 
                   Corynebacterium 
                 
                 
                   glutamicum 
                 
                 21255 
               
               
                 
                   Corynebacterium 
                 
                 
                   glutamicum 
                 
                 31830 
               
               
                 
                   Corynebacterium 
                 
                 
                   glutamicum 
                 
                 13032 
               
               
                 
                   Corynebacterium 
                 
                 
                   glutamicum 
                 
                 14305 
               
               
                 
                   Corynebacterium 
                 
                 
                   glutamicum 
                 
                 15455 
               
               
                 
                   Corynebacterium 
                 
                 
                   glutamicum 
                 
                 13058 
               
               
                 
                   Corynebacterium 
                 
                 
                   glutamicum 
                 
                 13059 
               
               
                 
                   Corynebacterium 
                 
                 
                   glutamicum 
                 
                 13060 
               
               
                 
                   Corynebacterium 
                 
                 
                   glutamicum 
                 
                 21492 
               
               
                 
                   Corynebacterium 
                 
                 
                   glutamicum 
                 
                 21513 
               
               
                 
                   Corynebacterium 
                 
                 
                   glutamicum 
                 
                 21526 
               
               
                 
                   Corynebacterium 
                 
                 
                   glutamicum 
                 
                 21543 
               
               
                 
                   Corynebacterium 
                 
                 
                   glutamicum 
                 
                 13287 
               
               
                 
                   Corynebacterium 
                 
                 
                   glutamicum 
                 
                 21851 
               
               
                 
                   Corynebacterium 
                 
                 
                   glutamicum 
                 
                 21253 
               
               
                 
                   Corynebacterium 
                 
                 
                   glutamicum 
                 
                 21514 
               
               
                 
                   Corynebacterium 
                 
                 
                   glutamicum 
                 
                 21516 
               
               
                 
                   Corynebacterium 
                 
                 
                   glutamicum 
                 
                 21299 
               
               
                 
                   Corynebacterium 
                 
                 
                   glutamicum 
                 
                 21300 
               
               
                 
                   Corynebacterium 
                 
                 
                   glutamicum 
                 
                 39684 
               
               
                 
                   Corynebacterium 
                 
                 
                   glutamicum 
                 
                 21488 
               
               
                 
                   Corynebacterium 
                 
                 
                   glutamicum 
                 
                 21649 
               
               
                 
                   Corynebacterium 
                 
                 
                   glutamicum 
                 
                 21650 
               
               
                 
                   Corynebacterium 
                 
                 
                   glutamicum 
                 
                 19223 
               
               
                 
                   Corynebacterium 
                 
                 
                   glutamicum 
                 
                 13869 
               
               
                 
                   Corynebacterium 
                 
                 
                   glutamicum 
                 
                 21157 
               
               
                 
                   Corynebacterium 
                 
                 
                   glutamicum 
                 
                 21158 
               
               
                 
                   Corynebacterium 
                 
                 
                   glutamicum 
                 
                 21159 
               
               
                 
                   Corynebacterium 
                 
                 
                   glutamicum 
                 
                 21355 
               
               
                 
                   Corynebacterium 
                 
                 
                   glutamicum 
                 
                 31808 
               
               
                 
                   Corynebacterium 
                 
                 
                   glutamicum 
                 
                 21674 
               
               
                 
                   Corynebacterium 
                 
                 
                   glutamicum 
                 
                 21562 
               
               
                 
                   Corynebacterium 
                 
                 
                   glutamicum 
                 
                 21563 
               
               
                 
                   Corynebacterium 
                 
                 
                   glutamicum 
                 
                 21564 
               
               
                 
                   Corynebacterium 
                 
                 
                   glutamicum 
                 
                 21565 
               
               
                 
                   Corynebacterium 
                 
                 
                   glutamicum 
                 
                 21566 
               
               
                 
                   Corynebacterium 
                 
                 
                   glutamicum 
                 
                 21567 
               
               
                 
                   Corynebacterium 
                 
                 
                   glutamicum 
                 
                 21568 
               
               
                 
                   Corynebacterium 
                 
                 
                   glutamicum 
                 
                 21569 
               
               
                 
                   Corynebacterium 
                 
                 
                   glutamicum 
                 
                 21570 
               
               
                 
                   Corynebacterium 
                 
                 
                   glutamicum 
                 
                 21571 
               
               
                 
                   Corynebacterium 
                 
                 
                   glutamicum 
                 
                 21572 
               
               
                 
                   Corynebacterium 
                 
                 
                   glutamicum 
                 
                 21573 
               
               
                 
                   Corynebacterium 
                 
                 
                   glutamicum 
                 
                 21579 
               
               
                 
                   Corynebacterium 
                 
                 
                   glutamicum 
                 
                 19049 
               
               
                 
                   Corynebacterium 
                 
                 
                   glutamicum 
                 
                 19050 
               
               
                 
                   Corynebacterium 
                 
                 
                   glutamicum 
                 
                 19051 
               
               
                 
                   Corynebacterium 
                 
                 
                   glutamicum 
                 
                 19052 
               
               
                 
                   Corynebacterium 
                 
                 
                   glutamicum 
                 
                 19053 
               
               
                 
                   Corynebacterium 
                 
                 
                   glutamicum 
                 
                 19054 
               
               
                 
                   Corynebacterium 
                 
                 
                   glutamicum 
                 
                 19055 
               
               
                 
                   Corynebacterium 
                 
                 
                   glutamicum 
                 
                 19056 
               
               
                 
                   Corynebacterium 
                 
                 
                   glutamicum 
                 
                 19057 
               
               
                 
                   Corynebacterium 
                 
                 
                   glutamicum 
                 
                 19058 
               
               
                 
                   Corynebacterium 
                 
                 
                   glutamicum 
                 
                 19059 
               
               
                 
                   Corynebacterium 
                 
                 
                   glutamicum 
                 
                 19060 
               
               
                 
                   Corynebacterium 
                 
                 
                   glutamicum 
                 
                 19185 
               
               
                 
                   Corynebacterium 
                 
                 
                   glutamicum 
                 
                 13286 
               
               
                 
                   Corynebacterium 
                 
                 
                   glutamicum 
                 
                 21515 
               
               
                 
                   Corynebacterium 
                 
                 
                   glutamicum 
                 
                 21527 
               
               
                 
                   Corynebacterium 
                 
                 
                   glutamicum 
                 
                 21544 
               
               
                 
                   Corynebacterium 
                 
                 
                   glutamicum 
                 
                 21492 
               
               
                 
                   Corynebacterium 
                 
                 
                   glutamicum 
                 
                   
                   
                 B8183 
               
               
                 
                   Corynebacterium 
                 
                 
                   glutamicum 
                 
                   
                   
                 B8182 
               
               
                 
                   Corynebacterium 
                 
                 
                   glutamicum 
                 
                   
                   
                 B12416 
               
               
                 
                   Corynebacterium 
                 
                 
                   glutamicum 
                 
                   
                   
                 B12417 
               
               
                 
                   Corynebacterium 
                 
                 
                   glutamicum 
                 
                   
                   
                 B12418 
               
               
                 
                   Corynebacterium 
                 
                 
                   glutamicum 
                 
                   
                   
                 B11476 
               
               
                 
                   Corynebacterium 
                 
                 
                   glutamicum 
                 
                 21608 
               
               
                 
                   Corynebacterium 
                 
                 
                   lilium 
                 
                   
                 P973 
               
               
                 
                   Corynebacterium 
                 
                 
                   nitrilophilus 
                 
                 21419 
                   
                   
                   
                 11594 
               
               
                 
                   Corynebacterium 
                 
                 spec. 
                   
                 P4445 
               
               
                 
                   Corynebacterium 
                 
                 spec. 
                   
                 P4446 
               
               
                 
                   Corynebacterium 
                 
                 spec. 
                 31088 
               
               
                 
                   Corynebacterium 
                 
                 spec. 
                 31089 
               
               
                 
                   Corynebacterium 
                 
                 spec. 
                 31090 
               
               
                 
                   Corynebacterium 
                 
                 spec. 
                 31090 
               
               
                 
                   Corynebacterium 
                 
                 spec. 
                 31090 
               
               
                 
                   Corynebacterium 
                 
                 spec. 
                 15954 
                   
                   
                   
                   
                   
                   
                 20145 
               
               
                 
                   Corynebacterium 
                 
                 spec. 
                 21857 
               
               
                 
                   Corynebacterium 
                 
                 spec. 
                 21862 
               
               
                 
                   Corynebacterium 
                 
                 spec. 
                 21863 
               
               
                   
               
               
                   ATCC: American Type Culture Collection, Rockville, MD, USA    
               
               
                   FERM: Fermentation Research Institute, Chiba, Japan    
               
               
                   NRRL: ARS Culture Collection, Northern Regional Research Laboratory, Peoria, IL, USA    
               
               
                   CECT: Coleccion Espanola de Cultivos Tipo, Valencia, Spain    
               
               
                   NCIMB: National Collection of Industrial and Marine Bacteria Ltd., Aberdeen, UK    
               
               
                   CBS: Centraalbureau voor Schimmelcultures, Baarn, NL    
               
               
                   NCTC: National Collection of Type Cultures, London, UK    
               
               
                   DSMZ: Deutsche Sammlung von Mikroorganismen und Zellkulturen, Braunschweig, Germany    
               
               
                   For reference see Sugawara, H. et al. (1993) World directory of collections of cultures of microorganisms: Bacteria, fungi and yeasts (4 th  edn), World federation for culture collections world data center on microorganisms, Saimata, Japen.    
               
            
           
         
       
     
     
       
         
           
               
             
               
                 TABLE 4 
               
             
            
               
                   
               
               
                   
               
               
                 ALIGNMENT RESULTS 
               
            
           
           
               
               
               
               
               
               
               
               
               
            
               
                   
                 length 
                   
                   
                   
                   
                   
                 % homology 
                 Date of 
               
               
                 ID # 
                 (NT) 
                 Genbank Hit 
                 Length 
                 Accession 
                 Name of Genbank Hit 
                 Source of Genbank Hit 
                 (GAP) 
                 Deposit 
               
               
                   
               
            
           
           
               
               
               
               
               
               
               
               
               
            
               
                 rxa00026 
                 1509 
                 GB_RO: MMHC310M6 
                 158405 
                 AF109906 
                   Mus musculus  MHC class III region RD gene, partial cds; Bf, C2, G9A, 
                 
                   Mus musculus 
                 
                 38,003 
                 10-DEC-1998 
               
               
                   
                   
                   
                   
                   
                 NG22, G9, HSP70, HSP70, HSC70t, and smRNP genes, complete 
               
               
                   
                   
                   
                   
                   
                 cds; G7A gene, partial cds; and unknown genes. 
               
               
                   
                   
                 GB_HTG2: AC007029 
                 119007 
                 AC007029 
                   Homo sapiens  clone DJ0855F16, *** SEQUENCING IN PROGRESS 
                 
                   Homo sapiens 
                 
                 37,943 
                 7-Apr-99 
               
               
                   
                   
                   
                   
                   
                 ***, 1 unordered pieces. 
               
               
                   
                   
                 GB_HTG2: AC007029 
                 119007 
                 AC007029 
                   Homo sapiens  clone DJ0855F16, *** SEQUENCING IN PROGRESS 
                 
                   Homo sapiens 
                 
                 37,943 
                 7-Apr-99 
               
               
                   
                   
                   
                   
                   
                 ***, 1 unordered pieces. 
               
               
                 rxa00072 
               
               
                 rxa00111 
                 1116 
                 GB_BA1: SAUSIGA 
                 2748 
                 M94370 
                   Stigmatella aurantiaca  sigma factor (sigA) gene, complete cds. 
                 
                   Stigmatella aurantiaca 
                 
                 40,435 
                 16-Aug-94 
               
               
                   
                   
                 GB_BA1: SC5B8 
                 28500 
                 AL022374 
                   Streptomyces coelicolor  cosmid 5B8. 
                 
                   Streptomyces coelicolor 
                 
                 40,090 
                 22-Apr-98 
               
               
                   
                   
                 GB_BA2: AE001767 
                 9086 
                 AE001767 
                   Thermotoga maritima  section 79 of 136 of the complete genome. 
                 
                   Thermotoga maritima 
                 
                 35,091 
                 2-Jun-99 
               
               
                 rxa00112 
                 1314 
                 GB_EST35: AU075536 
                 418 
                 AU075536 
                 AU075536 Rice shoot  Oryza sativa  cDNA clone S0028_2Z, mRNA 
                 
                   Oryza sativa 
                 
                 39,423 
                 7-Jul-99 
               
               
                   
                   
                   
                   
                   
                 sequence. 
               
               
                   
                   
                 GB_GSS9: AQ157585 
                 647 
                 AQ157585 
                 nbxb0009B16r CUGI Rice BAC Library  Oryza sativa  genomic clone 
                 
                   Oryza sativa 
                 
                 40,867 
                 12-Sep-98 
               
               
                   
                   
                   
                   
                   
                 nbxb0009B16r, genomic survey sequence. 
               
               
                   
                   
                 GB_GSS14: AQ510314 
                 542 
                 AQ510314 
                 nbxb0095O05f CUGI Rice BAC Library  Oryza sativa  genomic clone 
                 
                   Oryza sativa 
                 
                 39,372 
                 04-MAY-1999 
               
               
                   
                   
                   
                   
                   
                 nbxb0095O05f, genomic survey sequence. 
               
               
                 rxa00133 
                 936 
                 GB_BA1: SC2G5 
                 38404 
                 AL035478 
                   Streptomyces coelicolor  cosmid 2G5. 
                 
                   Streptomyces coelicolor 
                 
                 41,170 
                 11-Jun-99 
               
               
                   
                   
                 GB_EST7: W64291 
                 515 
                 W64291 
                 md98h12.r1 Soares mouse embryo NbME13.5 14.5  Mus musculus   
                 
                   Mus musculus 
                 
                 35,306 
                 10-Jun-96 
               
               
                   
                   
                   
                   
                   
                 cDNA clone IMAGE: 386087 5′ similar to gb: L26528  Mus musculus   
               
               
                   
                   
                   
                   
                   
                 Rab11b mRNA, complete cds (MOUSE);, mRNA sequence. 
               
               
                   
                   
                 GB_PR3: AC005624 
                 39594 
                 AC005624 
                   Homo sapiens  chromosome 19, cosmid R30017, complete sequence. 
                 
                   Homo sapiens 
                 
                 39,054 
                 6-Sep-98 
               
               
                 rxa00137 
                 1212 
                 GB_BA2: AF124600 
                 4115 
                 AF124600 
                   Corynebacterium glutamicum  chorismate synthase (aroC), shikimate 
                 
                   Corynebacterium 
                 
                 99,867 
                 04-MAY-1999 
               
               
                   
                   
                   
                   
                   
                 kinase (aroK), and 3-dehydroquinate synthase (aroB) genes, complete 
                 
                   glutamicum 
                 
               
               
                   
                   
                   
                   
                   
                 cds; and putative cytoplasmic peptidase (pepQ) gene, partial cds. 
               
               
                   
                   
                 GB_BA1: MTCY159 
                 33818 
                 Z83863 
                   Mycobacterium tuberculosis  H37Rv complete genome; segment 
                 
                   Mycobacterium 
                 
                 40,959 
                 17-Jun-98 
               
               
                   
                   
                   
                   
                   
                 111/162. 
                 
                   tuberculosis 
                 
               
               
                   
                   
                 GB_BA1: MT3DEHQ 
                 3437 
                 X59509 
                   M. tuberculosis , genes for 3-dehydroquinate synthase and 3- 
                 
                   Mycobacterium 
                 
                 52,583 
                 30-Jun-93 
               
               
                   
                   
                   
                   
                   
                 dehydroquinase. 
                 
                   tuberculosis 
                 
               
               
                 rxa00139 
                 834 
                 GB_BA1: BLELONP 
                 738 
                 X99289 
                   B. lactofermentum  gene encoding elongation factor P. 
                 
                   Corynebacterium 
                 
                 100,000 
                 1-Nov-97 
               
               
                   
                   
                   
                   
                   
                   
                 
                   glutamicum 
                 
               
               
                   
                   
                 GB_PL1: SPAC24C9 
                 38666 
                 Z98601 
                   S. pombe  chromosome I cosmid c24C9. 
                 
                   Schizosaccharomyces 
                 
                 35,230 
                 24-Feb-99 
               
               
                   
                   
                   
                   
                   
                   
                 
                   pombe 
                 
               
               
                   
                   
                 GB_HTG1: CEY102A5_1 
                 110000 
                 Z99711 
                   Caenorhabditis elegans  chromosome V clone Y102A5, *** 
                 
                   Caenorhabditis elegans 
                 
                 37,775 
                 Z99711 
               
               
                   
                   
                   
                   
                   
                 SEQUENCING IN PROGRESS ***, in unordered pieces. 
               
               
                 rxa00152 
                 1419 
                 GB_BA1: MTCY277 
                 38300 
                 Z79701 
                   Mycobacterium tuberculosis  H37Rv complete genome; segment 
                 
                   Mycobacterium 
                 
                 58,500 
                 17-Jun-98 
               
               
                   
                   
                   
                   
                   
                 65/162. 
                 
                   tuberculosis 
                 
               
               
                   
                   
                 GB_BA1: MSGY456 
                 37316 
                 AD000001 
                   Mycobacterium tuberculosis  sequence from clone y456. 
                 
                   Mycobacterium 
                 
                 38,913 
                 03-DEC-1996 
               
               
                   
                   
                   
                   
                   
                   
                 
                   tuberculosis 
                 
               
               
                   
                   
                 GB_BA2: AF002133 
                 15437 
                 AF002133 
                   Mycobacterium avium  strain GIR10 transcriptional regulator (mav81) 
                 
                   Mycobacterium avium 
                 
                 64,009 
                 26-MAR-1998 
               
               
                   
                   
                   
                   
                   
                 gene, partial cds, aconitase (acn), invasin 1 (inv1), invasin 2 (inv2), 
               
               
                   
                   
                   
                   
                   
                 transcriptional regulator (moxR), ketoacyl-reductase (fabG), enoyl- 
               
               
                   
                   
                   
                   
                   
                 reductase (inhA) and ferrochelatase (mav272) genes, complete cds. 
               
               
                 rxa00226 
                 948 
                 GB_PR3: AC005756 
                 43299 
                 AC005756 
                   Homo sapiens  chromosome 19, fosmid 39347, complete sequence. 
                 
                   Homo sapiens 
                 
                 36,209 
                 02-OCT-1998 
               
               
                   
                   
                 GB_GSS5: AQ818463 
                 413 
                 AQ818463 
                 HS_5250_A2_B08_SP6E RPCI-11 Human Male BAC Library  Homo   
                 
                   Homo sapiens 
                 
                 37,288 
                 26-Aug-99 
               
               
                   
                   
                   
                   
                   
                   sapiens  genomic clone Plate = 826 Col = 16 Row = C, genomic survey 
               
               
                   
                   
                   
                   
                   
                 sequence. 
               
               
                   
                   
                 GB_GSS5: AQ782337 
                 832 
                 AQ782337 
                 HS_3184_B1_H12_T7C CIT Approved Human Genomic Sperm 
                 
                   Homo sapiens 
                 
                 35,917 
                 2-Aug-99 
               
               
                   
                   
                   
                   
                   
                 Library D  Homo sapiens  genomic clone Plate = 3184 Col = 23 Row = P, 
               
               
                   
                   
                   
                   
                   
                 genomic survey sequence. 
               
               
                 rxa00249 
                 980 
                 GB_BA2: AF035608 
                 3614 
                 AF035608 
                   Pseudomonas aeruginosa  ATP sulfurylase small subunit (cysD) and 
                 
                   Pseudomonas aeruginosa 
                 
                 50,205 
                 1-Jun-98 
               
               
                   
                   
                   
                   
                   
                 ATP sulfurylase GTP-binding subunit/APS kinase (cysN) genes, 
               
               
                   
                   
                   
                   
                   
                 complete cds. 
               
               
                   
                   
                 GB_BA1: AB017641 
                 17101 
                 AB017641 
                   Micromonospora griseorubida  gene for polyketide synthase, complete 
                 
                   Micromonospora 
                 
                 40,266 
                 2-Apr-99 
               
               
                   
                   
                   
                   
                   
                 cds. 
                 
                   griseorubida 
                 
               
               
                   
                   
                 GB_BA2: AF002133 
                 15437 
                 AF002133 
                   Mycobacterium avium  strain GIR10 transcriptional regulator (mav81) 
                 
                   Mycobacterium avium 
                 
                 38,429 
                 26-MAR-1998 
               
               
                   
                   
                   
                   
                   
                 gene, partial cds, aconitase (acn), invasin 1 (inv1), invasin 2 (inv2), 
               
               
                   
                   
                   
                   
                   
                 transcriptional regulator (moxR), ketoacyl-reductase (fabG), enoyl- 
               
               
                   
                   
                   
                   
                   
                 reductase (inhA) and ferrochelatase (mav272) genes, complete cds. 
               
               
                 rxa00299 
                 1101 
                 GB_BA2: CORCSLYS 
                 2821 
                 M89931 
                   Corynebacterium glutamicum  beta C-S lyase (aecD) and branched- 
                 
                   Corynebacterium 
                 
                 100,000 
                 4-Jun-98 
               
               
                   
                   
                   
                   
                   
                 chain amino acid uptake carrier (brnQ) genes, complete cds, and 
                 
                   glutamicum 
                 
               
               
                   
                   
                   
                   
                   
                 hypothetical protein Yhbw (yhbw) gene, partial cds. 
               
               
                   
                   
                 GB_BA1: CGECTP 
                 2719 
                 AJ001436 
                   Corynebacterium glutamicum  ectP gene. 
                 
                   Corynebacterium 
                 
                 41,143 
                 20-Nov-98 
               
               
                   
                   
                   
                   
                   
                   
                 
                   glutamicum 
                 
               
               
                   
                   
                 GB_BA2: AF181035 
                 5922 
                 AF181035 
                   Rhodobacter sphaeroides  glycogen utilization operon, complete 
                 
                   Rhodobacter sphaeroides 
                 
                 36,701 
                 7-Sep-99 
               
               
                   
                   
                   
                   
                   
                 sequence. 
               
               
                 rxa00332 
                 825 
                 GB_BA1: CGTHRC 
                 3120 
                 X56037 
                   Corynebacterium glutamicum  thrC gene for threonine synthase (EC 
                 
                   Corynebacterium 
                 
                 37,730 
                 17-Jun-97 
               
               
                   
                   
                   
                   
                   
                 4.2.99.2). 
                 
                   glutamicum 
                 
               
               
                   
                   
                 GB_PAT: I09078 
                 3146 
                 I09078 
                 Sequence 4 from Patent WO 8809819. 
                 Unknown. 
                 38,700 
                 02-DEC-1994 
               
               
                   
                   
                 GB_PR3: HSJ333B15 
                 73666 
                 AL109954 
                 Human DNA sequence from clone 333B15 on chromosome 20, 
                 
                   Homo sapiens 
                 
                 37,203 
                 23-Nov-99 
               
               
                   
                   
                   
                   
                   
                 complete sequence. 
               
               
                 rxa00470 
                 1392 
                 GB_PL2: DCPCNAM 
                 865 
                 X62977 
                   D. carota  mRNA for proliferating cell nuclear antigen (PCNA). 
                 
                   Daucus carota 
                 
                 37,914 
                 30-Sep-99 
               
               
                   
                   
                 GB_PL2: AC006267 
                 101644 
                 AC006267 
                   Arabidopsis thaliana  BAC F9M13 from chromosome IV near 21.5 cM, 
                 
                   Arabidopsis thaliana 
                 
                 36,158 
                 27-Apr-99 
               
               
                   
                   
                   
                   
                   
                 complete sequence. 
               
               
                   
                   
                 GB_BA1: TT10SARNA 
                 721 
                 Y15063 
                   Thermus thermophilus  10Sa RNA gene. 
                 
                   Thermus thermophilus 
                 
                 39,494 
                 18-Aug-98 
               
               
                 rxa00471 
                 813 
                 GB_BA1: SERERYAA 
                 11219 
                 M63676 
                   S. erythraea  first ORF of eryA gene, complete cds. 
                 
                   Saccharopolyspora 
                 
                 38,781 
                 26-Apr-93 
               
               
                   
                   
                   
                   
                   
                   
                 
                   erythraea 
                 
               
               
                   
                   
                 GB_PAT: AR049367 
                 11219 
                 AR049367 
                 Sequence 1 from patent U.S. Pat. No. 5824513. 
                 Unknown. 
                 38,781 
                 29-Sep-99 
               
               
                   
                   
                 GB_BA1: SERERYAA 
                 11219 
                 M63676 
                   S. erythraea  first ORF of eryA gene, complete cds. 
                 
                   Saccharopolyspora 
                 
                 38,205 
                 26-Apr-93 
               
               
                   
                   
                   
                   
                   
                   
                 
                   erythraea 
                 
               
               
                 rxa00499 
                 1404 
                 GB_PR4: AC007206 
                 42732 
                 AC007206 
                   Homo sapiens  chromosome 19, cosmid R27370, complete sequence. 
                 
                   Homo sapiens 
                 
                 34,982 
                 4-Apr-99 
               
               
                   
                   
                 GB_EST26: AI344735 
                 462 
                 AI344735 
                 qp05a10.x1 NCI_CGAP_Kid5 Homo sapiens cDNA clone 
                 
                   Homo sapiens 
                 
                 42,675 
                 2-Feb-99 
               
               
                   
                   
                   
                   
                   
                 IMAGE: 1917114 3′ similar to gb: M15800 T-LYMPHOCYTE 
               
               
                   
                   
                   
                   
                   
                 MATURATION-ASSOCIATED PROTEIN (HUMAN);, mRNA 
               
               
                   
                   
                   
                   
                   
                 sequence. 
               
               
                   
                   
                 GB_PR4: AC006479 
                 161837 
                 AC006479 
                   Homo sapiens  clone DJ1051J04, complete sequence. 
                 
                   Homo sapiens 
                 
                 38,462 
                 11-Nov-99 
               
               
                 rxa00500 
                 798 
                 GB_PR4: AC006111 
                 190825 
                 AC006111 
                   Homo sapiens  chromosome 16 clone RPCI-11_461A8, complete 
                 
                   Homo sapiens 
                 
                 40,736 
                 3-Jul-99 
               
               
                   
                   
                   
                   
                   
                 sequence. 
               
               
                   
                   
                 GB_HTG2: AF128834 
                 196589 
                 AF128834 
                   Homo sapiens  chromosome 8 clone BAC 57G24 map 8p12, *** 
                 
                   Homo sapiens 
                 
                 34,062 
                 28-Feb-99 
               
               
                   
                   
                   
                   
                   
                 SEQUENCING IN PROGRESS ***, in unordered pieces. 
               
               
                   
                   
                 GB_HTG2: AF128834 
                 196589 
                 AF128834 
                   Homo sapiens  chromosome 8 clone BAC 57G24 map 8p12, *** 
                 
                   Homo sapiens 
                 
                 34,062 
                 28-Feb-99 
               
               
                   
                   
                   
                   
                   
                 SEQUENCING IN PROGRESS ***, in unordered pieces. 
               
               
                 rxa00501 
                 630 
                 GB_BA1: D86429 
                 5925 
                 D86429 
                   Saccharopolyspora rectivirgula  gene for beta-galactosidase, complete 
                 
                   Saccharopolyspora 
                 
                 53,871 
                 09-DEC-1998 
               
               
                   
                   
                   
                   
                   
                 cds. 
                 
                   rectivirgula 
                 
               
               
                   
                   
                 GB_HTG1: HS1099D15 
                 1301 
                 AL035456 
                   Homo sapiens  chromosome 20 clone RP5-1099D15, *** 
                 
                   Homo sapiens 
                 
                 33,546 
                 23-Nov-99 
               
               
                   
                   
                   
                   
                   
                 SEQUENCING IN PROGRESS ***, in unordered pieces. 
               
               
                   
                   
                 GB_HTG1: HS1099D15 
                 1301 
                 AL035456 
                   Homo sapiens  chromosome 20 clone RP5-1099D15, *** 
                 
                   Homo sapiens 
                 
                 33,546 
                 23-Nov-99 
               
               
                   
                   
                   
                   
                   
                 SEQUENCING IN PROGRESS ***, in unordered pieces. 
               
               
                 rxa00502 
                 1155 
                 GB_BA2: U00015 
                 42325 
                 U00015 
                   Mycobacterium leprae  cosmid B1620. 
                 
                   Mycobacterium leprae 
                 
                 34,783 
                 01-MAR-1994 
               
               
                   
                   
                 GB_BA1: U00020 
                 36947 
                 U00020 
                   Mycobacterium leprae  cosmid B229. 
                 
                   Mycobacterium leprae 
                 
                 34,900 
                 01-MAR-1994 
               
               
                   
                   
                 GB_HTG1: HS179I15 
                 210672 
                 Z84464 
                   Homo sapiens  chromosome 13 clone 179I15, *** SEQUENCING IN 
                 
                   Homo sapiens 
                 
                 32,898 
                 22-Jan-97 
               
               
                   
                   
                   
                   
                   
                 PROGRESS ***, in unordered pieces. 
               
               
                 rxa00566 
                 729 
                 GB_BA1: MTV008 
                 63033 
                 AL021246 
                   Mycobacterium tuberculosis  H37Rv complete genome; segment 
                 
                   Mycobacterium 
                 
                 37,011 
                 17-Jun-98 
               
               
                   
                   
                   
                   
                   
                 108/162. 
                 
                   tuberculosis 
                 
               
               
                   
                   
                 GB_BA2: AF071885 
                 2188 
                 AF071885 
                   Streptomyces coelicolor  ATP-dependent Clp protease proteolytic 
                 
                   Streptomyces coelicolor 
                 
                 62,963 
                 29-Jun-99 
               
               
                   
                   
                   
                   
                   
                 subunit 1 (clpP1) and ATP-dependent Clp protease proteolytic subunit 
               
               
                   
                   
                   
                   
                   
                 2 (clpP2) genes, complete cds; and ATP-dependent Clp 
               
               
                   
                   
                   
                   
                   
                 protease ATP-binding subunit Clpx (clpX) gene, partial cds. 
               
               
                   
                   
                 GB_BA2: AF013216 
                 15742 
                 AF013216 
                   Myxococcus xanthus  Dog (dog), isocitrate lyase (icl), Mls (mls), Ufo 
                 
                   Myxococcus xanthus 
                 
                 54,683 
                 28-Jan-98 
               
               
                   
                   
                   
                   
                   
                 (ufo), fumarate hydratase (fhy), and proteosome major subunit (clpP) 
               
               
                   
                   
                   
                   
                   
                 genes, complete cds; and acyl-CoA oxidase (aco) gene, partial cds. 
               
               
                 rxa00567 
                 714 
                 GB_BA1: MTV008 
                 63033 
                 AL021246 
                   Mycobacterium tuberculosis  H37Rv complete genome; segment 
                 
                   Mycobacterium 
                 
                 42,090 
                 17-Jun-98 
               
               
                   
                   
                   
                   
                   
                 108/162. 
                 
                   tuberculosis 
                 
               
               
                   
                   
                 GB_BA1: CGBPHI16 
                 962 
                 Y12472 
                   C. glutamicum  DNA, attachment site bacteriophage Phi-16. 
                 
                   Corynebacterium 
                 
                 40,000 
                 05-MAR-1999 
               
               
                   
                   
                   
                   
                   
                   
                 
                   glutamicum 
                 
               
               
                   
                   
                 GB_BA1: ECOCLPPA 
                 1236 
                 J05534 
                   Escherichia coli  ATP-dependent clp protease proteolytic component 
                 
                   Escherichia coli 
                 
                 52,119 
                 26-Apr-93 
               
               
                   
                   
                   
                   
                   
                 (clpP) gene, complete cds. 
               
               
                 rxa00621 
                 906 
                 GB_EST1: D36491 
                 360 
                 D36491 
                 CELK033GYF Yuji Kohara unpublished cDNA  Caenorhabditis elegans   
                 
                   Caenorhabditis elegans 
                 
                 40,390 
                 8-Aug-94 
               
               
                   
                   
                   
                   
                   
                 cDNA clone yk33g11 5′, mRNA sequence. 
               
               
                   
                   
                 GB_IN2: CELC16A3 
                 34968 
                 U41534 
                   Caenorhabditis elegans  cosmid C16A3. 
                 
                   Caenorhabditis elegans 
                 
                 35,477 
                 18-MAY-1999 
               
               
                   
                   
                 GB_HTG3: AC009311 
                 160198 
                 AC009311 
                   Homo sapiens  clone NH0311L03, *** SEQUENCING IN PROGRESS 
                 
                   Homo sapiens 
                 
                 38,636 
                 13-Aug-99 
               
               
                   
                   
                   
                   
                   
                 ***, 3 unordered pieces. 
               
               
                 rxa00622 
                 1539 
                 GB_BA1: AB004795 
                 3039 
                 AB004795 
                   Pseudomonas  sp. gene for dipeptidyl aminopeptidase, complete cds. 
                   Pseudomonas  sp. 
                 54,721 
                 5-Feb-99 
               
               
                   
                   
                 GB_BA1: MBOPII 
                 2392 
                 D38405 
                   Moraxella lacunata  gene for protease II, complete cds. 
                 
                   Moraxella lacunata 
                 
                 50,167 
                 8-Feb-99 
               
               
                   
                   
                 GB_IN2: AF078916 
                 2960 
                 AF078916 
                   Trypanosoma brucei brucei  oligopeptidase B (opb) gene, complete 
                 
                   Trypanosoma brucei 
                 
                 48,076 
                 08-OCT-1999 
               
               
                   
                   
                   
                   
                   
                 cds. 
                 
                   brucei 
                 
               
               
                 rxa00650 
                 759 
                 GB_BA2: AF161327 
                 2021 
                 AF161327 
                   Corynebacterium diphtheriae  histidine kinase ChrS (chrS) and 
                 
                   Corynebacterium 
                 
                 51,319 
                 9-Sep-99 
               
               
                   
                   
                   
                   
                   
                 response regulator ChrA (chrA) genes, complete cds. 
                 
                   diphtheriae 
                 
               
               
                   
                   
                 GB_PL2: ATAC006533 
                 99188 
                 AC006533 
                   Arabidopsis thaliana  chromosome II BAC F20M17 genomic sequence, 
                 
                   Arabidopsis thaliana 
                 
                 38,051 
                 26-MAY-1999 
               
               
                   
                   
                   
                   
                   
                 complete sequence. 
               
               
                   
                   
                 GB_PL2: ATAC006533 
                 99188 
                 AC006533 
                   Arabidopsis thaliana  chromosome II BAC F20M17 genomic sequence, 
                 
                   Arabidopsis thaliana 
                 
                 35,403 
                 26-MAY-1999 
               
               
                   
                   
                   
                   
                   
                 complete sequence. 
               
               
                 rxa00675 
                 915 
                 GB_BA1: SC3C8 
                 33095 
                 AL023861 
                   Streptomyces coelicolor  cosmid 3C8. 
                 
                   Streptomyces coelicolor 
                 
                 36,836 
                 15-Jan-99 
               
               
                   
                   
                 GB_PR3: AC005736 
                 215441 
                 AC005736 
                   Homo sapiens  chromosome 16, BAC clone 462G18 (LANL), complete 
                 
                   Homo sapiens 
                 
                 42,027 
                 01-OCT-1998 
               
               
                   
                   
                   
                   
                   
                 sequence. 
               
               
                   
                   
                 GB_IN2: AC005719 
                 188357 
                 AC005719 
                   Drosophila melanogaster , chromosome 2L, region 38A5-38B4, BAC 
                 
                   Drosophila melanogaster 
                 
                 35,531 
                 27-OCT-1999 
               
               
                   
                   
                   
                   
                   
                 clone BACR48M05, complete sequence. 
               
               
                 rxa00689 
                 1614 
                 GB_PAT: E07294 
                 2975 
                 E07294 
                 genomic DNA encoding dehydrogenase of  Bacillus   
                 
                   Bacillus 
                 
                 45,677 
                 29-Sep-97 
               
               
                   
                   
                   
                   
                   
                 
                   stearothermophilus. 
                 
                 
                   stearothermophilus 
                 
               
               
                   
                   
                 GB_BA1: BACALDHT 
                 1975 
                 D13846 
                   B. stearothermophilus  aldhT gene for aldehyde dehydrogenase, 
                 
                   Bacillus 
                 
                 45,677 
                 20-Feb-99 
               
               
                   
                   
                   
                   
                   
                 complete cds. 
                 
                   stearothermophilus 
                 
               
               
                   
                   
                 GB_BA2: PPU96338 
                 5276 
                 U96338 
                   Pseudomonas putida  NCIMB 9866 plasmid pRA4000 p-cresol 
                 
                   Pseudomonas putida 
                 
                 44,317 
                 13-MAY-1999 
               
               
                   
                   
                   
                   
                   
                 degradative pathway genes, p-hydroxybenzaldehyde dehydrogenase 
               
               
                   
                   
                   
                   
                   
                 (pchA), p-cresol methylhydroxylase, cytochrome subunit precursor 
               
               
                   
                   
                   
                   
                   
                 (pchC), unknown (pchX) and p-cresol methylhydroxylase, flavoprotein 
               
               
                   
                   
                   
                   
                   
                 subunit (pchF) genes, complete cds. 
               
               
                 rxa00715 
                 918 
                 GB_EST30: AI647104 
                 218 
                 AI647104 
                 vn15c01.y1 Stratagene mouse heart (#937316)  Mus musculus  cDNA 
                 
                   Mus musculus 
                 
                 58,511 
                 29-Apr-99 
               
               
                   
                   
                   
                   
                   
                 clone IMAGE: 1021248 5′, mRNA sequence. 
               
               
                   
                   
                 GB_EST17: AA636159 
                 447 
                 AA636159 
                 vn15c01.r1 Stratagene mouse heart (#937316)  Mus musculus  cDNA 
                 
                   Mus musculus 
                 
                 41,195 
                 22-OCT-1997 
               
               
                   
                   
                   
                   
                   
                 clone IMAGE: 1021248 5′, mRNA sequence. 
               
               
                   
                   
                 GB_EST10: AA184468 
                 583 
                 AA184468 
                 mt52h05.r1 Stratagene mouse embryonic carcinoma (#937317)  Mus   
                 
                   Mus musculus 
                 
                 40,426 
                 12-Feb-97 
               
               
                   
                   
                   
                   
                   
                   musculus  cDNA clone IMAGE: 633561 5′ similar to gb: D10918 Mouse 
               
               
                   
                   
                   
                   
                   
                 mRNA for ubiquitin like protein, partial sequence (MOUSE);, mRNA 
               
               
                   
                   
                   
                   
                   
                 sequence. 
               
               
                 rxa00744 
                 1065 
                 GB_HTG3: AC009855 
                 167592 
                 AC009855 
                   Homo sapiens  clone 1_C_5, *** SEQUENCING IN PROGRESS ***, 
                 
                   Homo sapiens 
                 
                 36,673 
                 3-Sep-99 
               
               
                   
                   
                   
                   
                   
                 13 unordered pieces. 
               
               
                   
                   
                 GB_HTG3: AC009855 
                 167592 
                 AC009855 
                   Homo sapiens  clone 1_C_5, *** SEQUENCING IN PROGRESS ***, 
                 
                   Homo sapiens 
                 
                 36,673 
                 3-Sep-99 
               
               
                   
                   
                   
                   
                   
                 13 unordered pieces. 
               
               
                   
                   
                 GB_PR4: AC005082 
                 169739 
                 AC005082 
                   Homo sapiens  clone RG271G13, complete sequence. 
                 
                   Homo sapiens 
                 
                 39,557 
                 8-Sep-99 
               
               
                 rxa00756 
                 1119 
                 GB_BA1: MLCB596 
                 38426 
                 AL035472 
                   Mycobacterium leprae  cosmid B596. 
                 
                   Mycobacterium leprae 
                 
                 54,562 
                 27-Aug-99 
               
               
                   
                   
                 GB_GSS12: AQ368028 
                 652 
                 AQ368028 
                 toxb0001N11rCUGI Tomato BAC Library  Lycopersicon esculentum   
                 
                   Lycopersicon esculentum 
                 
                 42,657 
                 5-Feb-99 
               
               
                   
                   
                   
                   
                   
                 genomic clone toxb0001N11r, genomic survey sequence. 
               
               
                   
                   
                 GB_HTG3: AC008067 
                 151242 
                 AC008067 
                   Homo sapiens  clone NH0303104, *** SEQUENCING IN PROGRESS 
                 
                   Homo sapiens 
                 
                 37,239 
                 8-Sep-99 
               
               
                   
                   
                   
                   
                   
                 ***, 2 unordered pieces. 
               
               
                 rxa00773 
                 1266 
                 GB_BA1: MLU15182 
                 40123 
                 U15182 
                   Mycobacterium leprae  cosmid B2266. 
                 
                   Mycobacterium leprae 
                 
                 36,616 
                 09-MAR-1995 
               
               
                   
                   
                 GB_BA1: MSGL611CS 
                 37769 
                 L78822 
                   Mycobacterium leprae  cosmid L611 DNA sequence. 
                 
                   Mycobacterium leprae 
                 
                 35,714 
                 15-Jun-96 
               
               
                   
                   
                 GB_GSS14: AQ578181 
                 728 
                 AQ578181 
                 nbxb0083P08r CUGI Rice BAC Library  Oryza sativa  genomic clone 
                 
                   Oryza sativa 
                 
                 39,246 
                 2-Jun-99 
               
               
                   
                   
                   
                   
                   
                 nbxb0083P08r, genomic survey sequence. 
               
               
                 rxa00793 
                 1299 
                 GB_GSS5: AQ769737 
                 519 
                 AQ769737 
                 HS_3160_A2_G04_T7C CIT Approved Human Genomic Sperm 
                 
                   Homo sapiens 
                 
                 37,765 
                 28-Jul-99 
               
               
                   
                   
                   
                   
                   
                 Library D  Homo sapiens  genomic clone Plate = 3160 Col = 8 Row = M, 
               
               
                   
                   
                   
                   
                   
                 genomic survey sequence. 
               
               
                   
                   
                 GB_BA1: RTU08434 
                 2400 
                 U08434 
                   Rhizobium trifolii  orotate phosphoribosyltransferase (pyrE) and 
                 
                   Rhizobium trifolii 
                 
                 40,700 
                 16-Apr-97 
               
               
                   
                   
                   
                   
                   
                 fructokinase (frk) genes, complete cds. 
               
               
                   
                   
                 GB_EST31: F33810 
                 243 
                 F33810 
                 HSPD27491 HM3  Homo sapiens  cDNA clone s3000041E12, mRNA 
                 
                   Homo sapiens 
                 
                 41,564 
                 13-MAY-1999 
               
               
                   
                   
                   
                   
                   
                 sequence. 
               
               
                 rxa00820 
                 486 
                 GB_PR4: AC005868 
                 96180 
                 AC005868 
                   Homo sapiens  12q24.2 PAC RPCI5-944M2 (Roswell Park Cancer 
                 
                   Homo sapiens 
                 
                 32,298 
                 27-Feb-99 
               
               
                   
                   
                   
                   
                   
                 Institute Human PAC Library) complete sequence. 
               
               
                   
                   
                 GB_EST8: AA000903 
                 396 
                 AA000903 
                 mg38b04.r1 Soares mouse embryo NbME13.5 14.5  Mus musculus   
                 
                   Mus musculus 
                 
                 42,045 
                 18-Jul-96 
               
               
                   
                   
                   
                   
                   
                 cDNA clone IMAGE: 426031 5′, mRNA sequence. 
               
               
                   
                   
                 GB_EST25: AI317789 
                 696 
                 AI317789 
                 uj20g09.y1 Sugano mouse embryo mewa  Mus musculus  cDNA clone 
                 
                   Mus musculus 
                 
                 38,557 
                 17-DEC-1998 
               
               
                   
                   
                   
                   
                   
                 IMAGE: 1920544 5′ similar to WP: C13C4.5 CE08130 SUGAR 
               
               
                   
                   
                   
                   
                   
                 TRANSPORTER;, mRNA sequence. 
               
               
                 rxa00833 
                 618 
                 GB_PH: BPH6589 
                 41489 
                 AJ006589 
                 Bacteriophage phi-C31 complete genome. 
                 Bacteriophage phi-C31 
                 41,806 
                 29-Apr-99 
               
               
                   
                   
                 GB_HTG2: AC006887 
                 215801 
                 AC006887 
                   Caenorhabditis elegans  clone Y59H11, *** SEQUENCING IN 
                 
                   Caenorhabditis elegans 
                 
                 35,798 
                 24-Feb-99 
               
               
                   
                   
                   
                   
                   
                 PROGRESS ***, 3 unordered pieces. 
               
               
                   
                   
                 GB_HTG2: AC006887 
                 215801 
                 AC006887 
                   Caenorhabditis elegans  clone Y59H11, *** SEQUENCING IN 
                 
                   Caenorhabditis elegans 
                 
                 35,798 
                 24-Feb-99 
               
               
                   
                   
                   
                   
                   
                 PROGRESS ***, 3 unordered pieces. 
               
               
                 rxa00844 
                 957 
                 GB_GSS15: AQ605195 
                 459 
                 AQ605195 
                 HS_2136_B1_C12_T7C CIT Approved Human Genomic Sperm 
                 
                   Homo sapiens 
                 
                 38,074 
                 10-Jun-99 
               
               
                   
                   
                   
                   
                   
                 Library D  Homo sapiens  genomic clone Plate = 2136 Col = 23 Row = F, 
               
               
                   
                   
                   
                   
                   
                 genomic survey sequence. 
               
               
                   
                   
                 GB_HTG1: CNS00M8S 
                 214599 
                 AL079302 
                   Homo sapiens  chromosome 14 clone R-1089B7, *** SEQUENCING 
                 
                   Homo sapiens 
                 
                 38,120 
                 15-OCT-1999 
               
               
                   
                   
                   
                   
                   
                 IN PROGRESS ***, in ordered pieces. 
               
               
                   
                   
                 GB_HTG1: CNS00M8S 
                 214599 
                 AL079302 
                   Homo sapiens  chromosome 14 clone R-1089B7, *** SEQUENCING 
                 
                   Homo sapiens 
                 
                 38,120 
                 15-OCT-1999 
               
               
                   
                   
                   
                   
                   
                 IN PROGRESS ***, in ordered pieces. 
               
               
                 rxa00866 
                 1066 
                 GB_BA1: CGORF4GEN 
                 2398 
                 X95649 
                   C. glutamicum  ORF4 gene. 
                 
                   Corynebacterium 
                 
                 99,273 
                 10-MAR-1998 
               
               
                   
                   
                   
                   
                   
                   
                 
                   glutamicum 
                 
               
               
                   
                   
                 GB_BA1: BLDAPAB 
                 3572 
                 Z21502 
                   B. lactofermentum  dapA and dapB genes for dihydrodipicolinate 
                 
                   Corynebacterium 
                 
                 99,301 
                 16-Aug-93 
               
               
                   
                   
                   
                   
                   
                 synthase and dihydrodipicolinate reductase. 
                 
                   glutamicum 
                 
               
               
                   
                   
                 GB_PAT: E14517 
                 1411 
                 E14517 
                 DNA encoding  Brevibacterium  dihydrodipicolinic acid reductase. 
                 
                   Corynebacterium 
                 
                 99,659 
                 28-Jul-99 
               
               
                   
                   
                   
                   
                   
                   
                 
                   glutamicum 
                 
               
               
                 rxa00877 
                 1788 
                 GB_PAT: I92050 
                 567 
                 I92050 
                 Sequence 17 from patent U.S. Pat. No. 5726299. 
                 Unknown. 
                 62,787 
                 01-DEC-1998 
               
               
                   
                   
                 GB_PAT: I78760 
                 567 
                 I78760 
                 Sequence 16 from patent U.S. Pat. No. 5693781. 
                 Unknown. 
                 62,787 
                 3-Apr-98 
               
               
                   
                   
                 GB_BA2: AE000426 
                 10240 
                 AE000426 
                   Escherichia coli  K-12 MG1655 section 316 of 400 of the complete 
                 
                   Escherichia coli 
                 
                 36,456 
                 12-Nov-98 
               
               
                   
                   
                   
                   
                   
                 genome. 
               
               
                 rxa00903 
                 733 
                 GB_BA2: AE001598 
                 11136 
                 AE001598 
                   Chlamydia pneumoniae  section 14 of 103 of the complete genome. 
                 
                   Chlamydophila 
                 
                 32,782 
                 08-MAR-1999 
               
               
                   
                   
                   
                   
                   
                   
                 
                   pneumoniae 
                 
               
               
                   
                   
                 GB_PL2: AF079370 
                 2897 
                 AF079370 
                   Kluyveromyces lactis  invertase (INV1) gene, complete cds. 
                 
                   Kluyveromyces lactis 
                 
                 35,849 
                 4-Aug-99 
               
               
                   
                   
                 GB_BA2: AE001598 
                 11136 
                 AE001598 
                   Chlamydia pneumoniae  section 14 of 103 of the complete genome. 
                 
                   Chlamydophila 
                 
                 40,138 
                 08-MAR-1999 
               
               
                   
                   
                   
                   
                   
                   
                 
                   pneumoniae 
                 
               
               
                 rxa00905 
                 924 
                 GB_PR2: HSQ15C24 
                 73192 
                 AJ239325 
                   Homo sapiens  chromosome 21 from cosmids LLNLc116 1C16 and 
                 
                   Homo sapiens 
                 
                 35,076 
                 28-Sep-99 
               
               
                   
                   
                   
                   
                   
                 LLNLc116 15C24 map 21q22.3 region D21S171-LA161, complete 
               
               
                   
                   
                   
                   
                   
                 sequence. 
               
               
                   
                   
                 GB_GSS4: AQ691923 
                 446 
                 AQ691923 
                 HS_5400_B2_G04_SP6E RPCI-11 Human Male BAC Library  Homo   
                 
                   Homo sapiens 
                 
                 33,500 
                 6-Jul-99 
               
               
                   
                   
                   
                   
                   
                   sapiens  genomic clone Plate = 976 Col = 8 Row = N, genomic survey 
               
               
                   
                   
                   
                   
                   
                 sequence. 
               
               
                   
                   
                 GB_EST37: AI967802 
                 479 
                 AI967802 
                 Ljirnpest12-930-d6 Ljirnp Lambda HybriZap two-hybrid library  Lotus   
                 
                   Lotus japonicus 
                 
                 41,127 
                 24-Aug-99 
               
               
                   
                   
                   
                   
                   
                   japonicus  cDNA clone LP930-12-d6 5′ similar to 60S ribosomal protein 
               
               
                   
                   
                   
                   
                   
                 L7A, mRNA sequence. 
               
               
                 rxa00906 
                 627 
                 GB_PAT: I78750 
                 588 
                 I78750 
                 Sequence 6 from patent U.S. Pat. No. 5693781. 
                 Unknown. 
                 97,071 
                 3-Apr-98 
               
               
                   
                   
                 GB_PAT: I92039 
                 588 
                 I92039 
                 Sequence 6 from patent U.S. Pat. No. 5726299. 
                 Unknown. 
                 97,071 
                 01-DEC-1998 
               
               
                   
                   
                 GB_PR3: HS929C8 
                 139190 
                 AL020994 
                 Human DNA sequence from clone 929C8 on chromosome 22q12.1-12.3 
                 
                   Homo sapiens 
                 
                 39,016 
                 23-Nov-99 
               
               
                   
                   
                   
                   
                   
                 Contains CA repeat, GSS, STS, complete sequence. 
               
               
                 rxa00907 
                 246 
                 GB_PAT: I78750 
                 588 
                 I78750 
                 Sequence 6 from patent U.S. Pat. No. 5693781. 
                 Unknown. 
                 97,561 
                 3-Apr-98 
               
               
                   
                   
                 GB_PAT: I92039 
                 588 
                 I92039 
                 Sequence 6 from patent U.S. Pat. No. 5726299. 
                 Unknown. 
                 97,561 
                 01-DEC-1998 
               
               
                   
                   
                 GB_PAT: I78750 
                 588 
                 I78750 
                 Sequence 6 from patent U.S. Pat. No. 5693781. 
                 Unknown. 
                 37,222 
                 3-Apr-98 
               
               
                 rxa00961 
                 455 
                 GB_BA1: AB032799 
                 9077 
                 AB032799 
                   Chromobacterium violaceum  violacein biosynthetic gene cluster (vio 
                 
                   Chromobacterium 
                 
                 39,868 
                 02-OCT-1999 
               
               
                   
                   
                   
                   
                   
                 A, vio B, vio C, vio D), complete cds. 
                 
                   violaceum 
                 
               
               
                   
                   
                 GB_BA2: AF172851 
                 10094 
                 AF172851 
                   Chromobacterium violaceum  violacein biosynthetic gene cluster, 
                 
                   Chromobacterium 
                 
                 42,760 
                 30-Aug-99 
               
               
                   
                   
                   
                   
                   
                 complete sequence. 
                 
                   violaceum 
                 
               
               
                   
                   
                 GB_BA1: AB032799 
                 9077 
                 AB032799 
                   Chromobacterium violaceum  violacein biosynthetic gene cluster (vio 
                 
                   Chromobacterium 
                 
                 39,551 
                 02-OCT-1999 
               
               
                   
                   
                   
                   
                   
                 A, vio B, vio C, vio D), complete cds. 
                 
                   violaceum 
                 
               
               
                 rxa00982 
                 1629 
                 GB_BA1: BLARGS 
                 2501 
                 Z21501 
                   B. lactofermentum  argS and lysA genes for arginyl-tRNA synthetase 
                 
                   Corynebacterium 
                 
                 39,003 
                 28-DEC-1993 
               
               
                   
                   
                   
                   
                   
                 and diaminopimelate decarboxylase (partial). 
                 
                   glutamicum 
                 
               
               
                   
                   
                 GB_BA1: CGXLYSA 
                 2344 
                 X54740 
                   Corynebacterium glutamicum  argS-lysA operon gene for the upstream 
                 
                   Corynebacterium 
                 
                 41,435 
                 30-Jun-93 
               
               
                   
                   
                   
                   
                   
                 region of the arginyl-tRNA synthetase and diaminopimelate 
                 
                   glutamicum 
                 
               
               
                   
                   
                   
                   
                   
                 decarboxylase (EC 4.1.1.20). 
               
               
                   
                   
                 GB_PAT: E14508 
                 3579 
                 E14508 
                 DNA encoding  Brevibacterium  diaminopimelic acid decarboxylase and 
                 
                   Corynebacterium 
                 
                 40,566 
                 28-Jul-99 
               
               
                   
                   
                   
                   
                   
                 arginyl-tRNA synthase. 
                 
                   glutamicum 
                 
               
               
                 rxa00983 
                 1599 
                 GB_HTG2: AC008152 
                 24000 
                 AC008152 
                   Leishmania major  chromosome 35 clone L7936 strain Friedlin, *** 
                 
                   Leishmania major 
                 
                 38,658 
                 28-Jul-99 
               
               
                   
                   
                   
                   
                   
                 SEQUENCING IN PROGRESS ***, 4 unordered pieces. 
               
               
                   
                   
                 GB_HTG2: AC008152 
                 24000 
                 AC008152 
                   Leishmania major  chromosome 35 clone L7936 strain Friedlin, *** 
                 
                   Leishmania major 
                 
                 38,658 
                 28-Jul-99 
               
               
                   
                   
                   
                   
                   
                 SEQUENCING IN PROGRESS ***, 4 unordered pieces. 
               
               
                   
                   
                 GB_HTG3: AC008648 
                 87249 
                 AC008648 
                   Homo sapiens  chromosome 5 clone CIT978SKB_186E14, *** 
                 
                   Homo sapiens 
                 
                 36,102 
                 3-Aug-99 
               
               
                   
                   
                   
                   
                   
                 SEQUENCING IN PROGRESS ***, 22 unordered pieces. 
               
               
                 rxa00984 
                 440 
                 GB_BA1: MVINED 
                 3098 
                 D01045 
                   Micromonospora viridifaciens  DNA for nedR protein and 
                 
                   Micromonospora 
                 
                 59,226 
                 2-Feb-99 
               
               
                   
                   
                   
                   
                   
                 neuraminidase, complete cds. 
                 
                   viridifaciens 
                 
               
               
                   
                   
                 GB_PAT: E02375 
                 1881 
                 E02375 
                 Neuraminidase gene. 
                 
                   Micromonospora 
                 
                 59,226 
                 29-Sep-97 
               
               
                   
                   
                   
                   
                   
                   
                 
                   viridifaciens 
                 
               
               
                   
                   
                 GB_PR4: HUAC004513 
                 101311 
                 AC004513 
                   Homo sapiens  Chromosome 16 BAC clone CIT987SK-A-926E7, 
                 
                   Homo sapiens 
                 
                 41,204 
                 23-Nov-99 
               
               
                   
                   
                   
                   
                   
                 complete sequence. 
               
               
                 rxa01014 
                 2724 
                 GB_BA1: MTV008 
                 63033 
                 AL021246 
                   Mycobacterium tuberculosis  H37Rv complete genome; segment 
                 
                   Mycobacterium 
                 
                 56,167 
                 17-Jun-98 
               
               
                   
                   
                   
                   
                   
                 108/162. 
                 tuberculosis 
               
               
                   
                   
                 GB_BA1: STMAMPEPN 
                 2849 
                 L23172 
                   Streptomyces lividans  aminopeptidase N gene, complete cds. 
                 
                   Streptomyces lividans 
                 
                 57,067 
                 18-MAY-1994 
               
               
                   
                   
                 GB_BA1: SC7H2 
                 42655 
                 AL109732 
                   Streptomyces coelicolor  cosmid 7H2. 
                 
                   Streptomyces coelicolor 
                 
                 37,551 
                 2-Aug-99 
               
               
                   
                   
                   
                   
                   
                   
                 A3(2) 
               
               
                 rxa01059 
                 732 
                 GB_HTG3: AC008154 
                 172241 
                 AC008154 
                   Homo sapiens  chromosome 7, *** SEQUENCING IN PROGRESS ***, 
                 
                   Homo sapiens 
                 
                 39,499 
                 8-Sep-99 
               
               
                   
                   
                   
                   
                   
                 26 unordered pieces. 
               
               
                   
                   
                 GB_HTG3: AC008154 
                 172241 
                 AC008154 
                   Homo sapiens  chromosome 7, *** SEQUENCING IN PROGRESS ***, 
                 
                   Homo sapiens 
                 
                 39,499 
                 8-Sep-99 
               
               
                   
                   
                   
                   
                   
                 26 unordered pieces. 
               
               
                   
                   
                 GB_EST32: AI756574 
                 299 
                 AI756574 
                 ea02f10.y1  Eimeria  M5-6 Merozoite stage  Eimeria tenella  cDNA 5′, 
                 
                   Eimeria tenella 
                 
                 37,793 
                 23-Jun-99 
               
               
                   
                   
                   
                   
                   
                 mRNA sequence. 
               
               
                 rxa01073 
                 954 
                 GB_BA1: BACOUTB 
                 1004 
                 M15811 
                   Bacillus subtilis  outB gene encoding a sporulation protein, complete 
                 
                   Bacillus subtilis 
                 
                 53,723 
                 26-Apr-93 
               
               
                   
                   
                   
                   
                   
                 cds. 
               
               
                   
                   
                 GB_PR4: AC007938 
                 167237 
                 AC007938 
                   Homo sapiens  clone UWGC: djs201 from 7q31, complete sequence. 
                 
                   Homo sapiens 
                 
                 34,322 
                 1-Jul-99 
               
               
                   
                   
                 GB_PL2: ATAC006282 
                 92577 
                 AC006282 
                   Arabidopsis thaliana  chromosome II BAC F13K3 genomic sequence, 
                 
                   Arabidopsis thaliana 
                 
                 36,181 
                 13-MAR-1999 
               
               
                   
                   
                   
                   
                   
                 complete sequence. 
               
               
                 rxa01120 
                 1401 
                 GB_BA1: MTV008 
                 63033 
                 AL021246 
                   Mycobacterium tuberculosis  H37Rv complete genome; segment 
                 
                   Mycobacterium 
                 
                 36,715 
                 17-Jun-98 
               
               
                   
                   
                   
                   
                   
                 108/162. 
                 
                   tuberculosis 
                 
               
               
                   
                   
                 GB_BA1: CAJ10321 
                 6710 
                 AJ010321 
                   Caulobacter crescentus  partial tig gene and clpP, cicA, clpX, lon 
                 
                   Caulobacter crescentus 
                 
                 63,311 
                 01-OCT-1998 
               
               
                   
                   
                   
                   
                   
                 genes. 
               
               
                   
                   
                 GB_BA2: AF150957 
                 4440 
                 AF150957 
                   Azospirillum brasilense  trigger factor (tig), heat-shock protein ClpP 
                 
                   Azospirillum brasilense 
                 
                 60,613 
                 7-Jun-99 
               
               
                   
                   
                   
                   
                   
                 (clpP), and heat-shock protein ClpX (clpX) genes, complete cds; and 
               
               
                   
                   
                   
                   
                   
                 Lon protease (lon) gene, partial cds. 
               
               
                 rxa01147 
                 1383 
                 GB_PR3: HS408N23 
                 97916 
                 Z98048 
                 Human DNA sequence from PAC 408N23 on chromosome 22q13. 
                 
                   Homo sapiens 
                 
                 34,567 
                 23-Nov-99 
               
               
                   
                   
                   
                   
                   
                 Contains HIP, HSC70-INTERACTING PROTEIN (PROGESTERONE 
               
               
                   
                   
                   
                   
                   
                 RECEPTOR-ASSOCIATED P48 PROTEIN), ESTs and STS. 
               
               
                   
                   
                 GB_BA2: AE001227 
                 26849 
                 AE001227 
                   Treponema pallidum  section 43 of 87 of the complete genome. 
                 
                   Treponema pallidum 
                 
                 37,564 
                 16-Jul-98 
               
               
                   
                   
                 GB_PR3: HS408N23 
                 97916 
                 Z98048 
                 Human DNA sequence from PAC 408N23 on chromosome 22q13. 
                 
                   Homo sapiens 
                 
                 34,911 
                 23-Nov-99 
               
               
                   
                   
                   
                   
                   
                 Contains HIP, HSC70-INTERACTING PROTEIN (PROGESTERONE 
               
               
                   
                   
                   
                   
                   
                 RECEPTOR-ASSOCIATED P48 PROTEIN), ESTs and STS. 
               
               
                 rxa01151 
                 958 
                 GB_BA1: MTCY261 
                 27322 
                 Z97559 
                   Mycobacterium tuberculosis  H37Rv complete genome; segment 
                 
                   Mycobacterium 
                 
                 38,789 
                 17-Jun-98 
               
               
                   
                   
                   
                   
                   
                 95/162. 
                 
                   tuberculosis 
                 
               
               
                   
                   
                 GB_HTG4: AC009849 
                 114993 
                 AC009849 
                   Drosophila melanogaster  chromosome 2 clone BACR07H08 (D864) 
                 
                   Drosophila melanogaster 
                 
                 39,213 
                 25-OCT-1999 
               
               
                   
                   
                   
                   
                   
                 RPCI-98 07.H.8 map 31B-31C strain y; cn bw sp, *** SEQUENCING 
               
               
                   
                   
                   
                   
                   
                 IN PROGRESS ***, 55 unordered pieces. 
               
               
                   
                   
                 GB_HTG4: AC009849 
                 114993 
                 AC009849 
                   Drosophila melanogaster  chromosome 2 clone BACR07H08 (D864) 
                 
                   Drosophila melanogaster 
                 
                 39,213 
                 25-OCT-1999 
               
               
                   
                   
                   
                   
                   
                 RPCI-98 07.H.8 map 31B-31C strain y; cn bw sp, *** SEQUENCING 
               
               
                   
                   
                   
                   
                   
                 IN PROGRESS ***, 55 unordered pieces. 
               
               
                 rxa01161 
                 1260 
                 GB_BA2: AF176799 
                 2943 
                 AF176799 
                   Lactobacillus pentosus  PepQ (pepQ) and catabolite control protein A 
                 
                   Lactobacillus pentosus 
                 
                 37,043 
                 5-Sep-99 
               
               
                   
                   
                   
                   
                   
                 (ccpA) genes, complete cds. 
               
               
                   
                   
                 GB_BA2: AF012084 
                 3082 
                 AF012084 
                   Lactobacillus helveticus  prolidase (pepQ) gene, complete cds. 
                 
                   Lactobacillus helveticus 
                 
                 46,796 
                 1-Jul-98 
               
               
                   
                   
                 GB_EST32: AI728955 
                 611 
                 AI728955 
                 BNLGHi12114 Six-day Cotton fiber  Gossypium hirsutum  cDNA 5′ 
                 
                   Gossypium hirsutum 
                 
                 37,647 
                 11-Jun-99 
               
               
                   
                   
                   
                   
                   
                 similar to (AC004481) putative permease [ Arabidopsis thaliana ], 
               
               
                   
                   
                   
                   
                   
                 mRNA sequence. 
               
               
                 rxa01181 
                 980 
                 GB_BA1: MLCB22 
                 40281 
                 Z98741 
                   Mycobacterium leprae  cosmid B22. 
                 
                   Mycobacterium leprae 
                 
                 61,570 
                 22-Aug-97 
               
               
                   
                   
                 GB_BA1: MTCY190 
                 34150 
                 Z70283 
                   Mycobacterium tuberculosis  H37Rv complete genome; segment 
                 
                   Mycobacterium 
                 
                 60,434 
                 17-Jun-98 
               
               
                   
                   
                   
                   
                   
                 98/162. 
                 
                   tuberculosis 
                 
               
               
                   
                   
                 GB_BA1: SC5F7 
                 40024 
                 AL096872 
                   Streptomyces coelicolor  cosmid 5F7. 
                 
                   Streptomyces coelicolor 
                 
                 57,011 
                 22-Jul-99 
               
               
                   
                   
                   
                   
                   
                   
                 A3(2) 
               
               
                 rxa01182 
                 516 
                 GB_HTG1: CEY116A8_2 
                 110000 
                 Z98858 
                   Caenorhabditis elegans  chromosome IV clone Y116A8, *** 
                 
                   Caenorhabditis elegans 
                 
                 34,843 
                 26-Oct-99 
               
               
                   
                   
                   
                   
                   
                 SEQUENCING IN PROGRESS ***, in unordered pieces. 
               
               
                   
                   
                 GB_HTG1: CEY116A8_2 
                 110000 
                 Z98858 
                   Caenorhabditis elegans  chromosome IV clone Y116A8, *** 
                 
                   Caenorhabditis elegans 
                 
                 34,843 
                 26-Oct-99 
               
               
                   
                   
                   
                   
                   
                 SEQUENCING IN PROGRESS ***, in unordered pieces. 
               
               
                   
                   
                 GB_IN1: CEY116A8C 
                 260341 
                 AL117204 
                   Caenorhabditis elegans  cosmid Y116A8C, complete sequence. 
                 
                   Caenorhabditis elegans 
                 
                 34,843 
                 19-Nov-99 
               
               
                 rxa01189 
                 732 
                 GB_BA1: D90915 
                 130001 
                 D90915 
                   Synechocystis  sp. PCC6803 complete genome, 17/27, 2137259-2267259. 
                   Synechocystis  sp. 
                 36,538 
                 7-Feb-99 
               
               
                   
                   
                 GB_BA1: D90915 
                 130001 
                 D90915 
                   Synechocystis  sp. PCC6803 complete genome, 17/27, 2137259-2267259. 
                   Synechocystis  sp. 
                 34,512 
                 7-Feb-99 
               
               
                   
                   
                 GB_HTG3: AC010515 
                 41038 
                 AC010515 
                   Homo sapiens  chromosome 19 clone LLNL-R_249H9, *** 
                 
                   Homo sapiens 
                 
                 33,564 
                 15-Sep-99 
               
               
                   
                   
                   
                   
                   
                 SEQUENCING IN PROGRESS ***, 31 unordered pieces. 
               
               
                 rxa01192 
                 681 
                 GB_OM: CFP180RRC 
                 5425 
                 X87224 
                   Canis familiaris  mRNA for ribosome receptor, p180. 
                 
                   Canis familiaris 
                 
                 41,229 
                 22-Jan-99 
               
               
                   
                   
                 GB_OM: CFP180RRC 
                 5425 
                 X87224 
                   Canis familiaris  mRNA for ribosome receptor, p180. 
                 
                   Canis familiaris 
                 
                 38,187 
                 22-Jan-99 
               
               
                 rxa01214 
                 1614 
                 GB_IN1: CEY47D3A 
                 199814 
                 AL117202 
                   Caenorhabditis elegans  cosmid Y47D3A, complete sequence. 
                 
                   Caenorhabditis elegans 
                 
                 36,604 
                 19-Nov-99 
               
               
                   
                   
                 GB_PR4: AC006039 
                 176257 
                 AC006039 
                   Homo sapiens  clone NH0319F03, complete sequence. 
                 
                   Homo sapiens 
                 
                 34,984 
                 05-MAY-1999 
               
               
                   
                   
                 GB_PR4: AC006039 
                 176257 
                 AC006039 
                   Homo sapiens  clone NH0319F03, complete sequence. 
                 
                   Homo sapiens 
                 
                 35,951 
                 05-MAY-1999 
               
               
                 rxa01224 
                 1146 
                 GB_EST22: AI070047 
                 479 
                 AI070047 
                 UI-R-C1-In-f-08-0-UI.s1 UI-R-C1  Rattus norvegicus  cDNA clone UI-R- 
                 
                   Rattus norvegicus 
                 
                 36,975 
                 5-Jul-99 
               
               
                   
                   
                   
                   
                   
                 C1-In-f-08-0-UI 3′, mRNA sequence. 
               
               
                   
                   
                 GB_RO: S75965 
                 625 
                 S75965 
                 THP = Tamm-Horsfall protein {promoter} [rats, Genomic, 625 nt]. 
                   Rattus  sp. 
                 34,400 
                 27-Jul-95 
               
               
                   
                   
                 GB_EST5: H96951 
                 459 
                 H96951 
                 yu01g03.r1 Soares_pineal_gland_N3HPG  Homo sapiens  cDNA clone 
                 
                   Homo sapiens 
                 
                 32,969 
                 11-DEC-1995 
               
               
                   
                   
                   
                   
                   
                 IMAGE: 232564 5′, mRNA sequence. 
               
               
                 rxa01250 
                 588 
                 GB_PL1: NEULCCB 
                 2656 
                 M18334 
                   N. crassa  (strain TS) laccase gene, complete cds. 
                 
                   Neurospora crassa 
                 
                 44,330 
                 03-MAY-1994 
               
               
                   
                   
                 GB_OV: MTRACOMPL 
                 16714 
                 Y16884 
                   Rhea americana  complete mitochondrial genome. 
                 
                   Mitochondrion Rhea 
                 
                 35,094 
                 19-Jul-99 
               
               
                   
                   
                   
                   
                   
                   
                 
                   americana 
                 
               
               
                   
                   
                 GB_OV: AF090339 
                 16704 
                 AF090339 
                   Rhea americana  mitochondrion, complete genome. 
                 
                   Mitochondrion Rhea 
                 
                 35,094 
                 27-MAY-1999 
               
               
                   
                   
                   
                   
                   
                   
                 
                   americana 
                 
               
               
                 rxa01277 
                 2127 
                 GB_PL2: AF111709 
                 52684 
                 AF111709 
                   Oryza sativa  subsp. indica Retrosat 1 retrotransposon and Ty3-Gypsy 
                   Oryza sativa  subsp.  indica   
                 37,410 
                 26-Apr-99 
               
               
                   
                   
                   
                   
                   
                 type Retrosat 2 retrotransposon, complete sequences; and unknown 
               
               
                   
                   
                   
                   
                   
                 genes. 
               
               
                   
                   
                 GB_IN1: CELZC250 
                 34372 
                 AF003383 
                   Caenorhabditis elegans  cosmid ZC250. 
                 
                   Caenorhabditis elegans 
                 
                 35,506 
                 14-MAY-1997 
               
               
                   
                   
                 GB_EST1: Z14808 
                 331 
                 Z14808 
                 CEL5E4 Chris Martin sorted cDNA library  Caenorhabditis elegans   
                 
                   Caenorhabditis elegans 
                 
                 36,890 
                 19-Jun-97 
               
               
                   
                   
                   
                   
                   
                 cDNA clone cm5e4 5′, mRNA sequence. 
               
               
                 rxa01302 
                 576 
                 GB_BA1: MTCI65 
                 34331 
                 Z95584 
                   Mycobacterium tuberculosis  H37Rv complete genome; segment 
                 
                   Mycobacterium 
                 
                 59,298 
                 17-Jun-98 
               
               
                   
                   
                   
                   
                   
                 50/162. 
                 
                   tuberculosis 
                 
               
               
                   
                   
                 GB_BA1: MSGY348 
                 40056 
                 AD000020 
                   Mycobacterium tuberculosis  sequence from clone y348. 
                 
                   Mycobacterium 
                 
                 59,227 
                 10-DEC-1996 
               
               
                   
                   
                   
                   
                   
                   
                 
                   tuberculosis 
                 
               
               
                   
                   
                 GB_BA1: SC5C7 
                 41906 
                 AL031515 
                   Streptomyces coelicolor  cosmid 5C7. 
                 
                   Streptomyces coelicolor 
                 
                 39,261 
                 7-Sep-98 
               
               
                 rxa01303 
                 1458 
                 GB_BA1: TTAJ5043 
                 837 
                 AJ225043 
                   Thermus thermophilus  partial narK gene. 
                 
                   Thermus thermophilus 
                 
                 55,245 
                 18-Jun-98 
               
               
                   
                   
                 GB_PL2: AC010675 
                 84723 
                 AC010675 
                   Arabidopsis thaliana  chromosome I BAC T17F3 genomic sequence, 
                 
                   Arabidopsis thaliana 
                 
                 37,058 
                 11-Nov-99 
               
               
                   
                   
                   
                   
                   
                 complete sequence. 
               
               
                   
                   
                 GB_GSS9: AQ170862 
                 518 
                 AQ170862 
                 HS_3165_B2_F03_T7 CIT Approved Human Genomic Sperm Library 
                 
                   Homo sapiens 
                 
                 38,610 
                 17-OCT-1998 
               
               
                   
                   
                   
                   
                   
                 D  Homo sapiens  genomic clone Plate = 3165 Col = 6 Row = L, genomic 
               
               
                   
                   
                   
                   
                   
                 survey sequence. 
               
               
                 rxa01308 
                 2503 
                 GB_BA1: D90757 
                 17621 
                 D90757 
                   Escherichia coli  genomic DNA. (27.3-27.7 min). 
                 
                   Escherichia coli 
                 
                 55,445 
                 7-Feb-99 
               
               
                   
                   
                 GB_BA1: D90787 
                 15942 
                 D90787 
                   E. coli  genomic DNA, Kohara clone #276(33.0-33.3 min.). 
                 
                   Escherichia coli 
                 
                 36,815 
                 29-MAY-1997 
               
               
                   
                   
                 GB_BA1: D90758 
                 13860 
                 D90758 
                   Escherichia coli  genomic DNA. (27.6-27.9 min). 
                 
                   Escherichia coli 
                 
                 54,942 
                 7-Feb-99 
               
               
                 rxa01309 
                 824 
                 GB_BA1: SCJ12 
                 35302 
                 AL109989 
                   Streptomyces coelicolor  cosmid J12. 
                 
                   Streptomyces coelicolor 
                 
                 62,423 
                 24-Aug-99 
               
               
                   
                   
                   
                   
                   
                   
                 A3(2) 
               
               
                   
                   
                 GB_BA1: BSNARYWI 
                 12450 
                 Z49884 
                   B. subtilis  nar[G, H, I, J, K], ywi[C, D, E] and argS genes. 
                 
                   Bacillus subtilis 
                 
                 57,447 
                 24-Jun-98 
               
               
                   
                   
                 GB_BA1: BSUB0020 
                 212150 
                 Z99123 
                   Bacillus subtilis  complete genome (section 20 of 21): from 3798401 to 
                 
                   Bacillus subtilis 
                 
                 37,129 
                 26-Nov-97 
               
               
                   
                   
                   
                   
                   
                 4010550. 
               
               
                 rxa01358 
                 1644 
                 GB_GSS11: AQ260413 
                 453 
                 AQ260413 
                 CITBI-E1-2510B12.TF CITBI-E1  Homo sapiens  genomic clone 
                 
                   Homo sapiens 
                 
                 41,531 
                 24-OCT-1998 
               
               
                   
                   
                   
                   
                   
                 2510B12, genomic survey sequence. 
               
               
                   
                   
                 GB_EST20: AA840582 
                 326 
                 AA840582 
                 vw77h07.r1 Stratagene mouse heart (#937316)  Mus musculus  cDNA 
                 
                   Mus musculus 
                 
                 42,901 
                 27-Feb-98 
               
               
                   
                   
                   
                   
                   
                 clone IMAGE: 1261021 5′ similar to gb: J04181 Mouse A-X actin 
               
               
                   
                   
                   
                   
                   
                 mRNA, complete cds (MOUSE);, mRNA sequence. 
               
               
                   
                   
                 GB_PAT: A39944 
                 3836 
                 A39944 
                 Sequence 1 from Patent WO9421807. 
                 unidentified 
                 38,764 
                 05-MAR-1997 
               
               
                 rxa01385 
                 2004 
                 GB_BA1: FVBPENTA 
                 2519 
                 M98557 
                   Flavobacterium  sp. pentachlorophenol 4-monooxygenase gene, 
                   Flavobacterium  sp. 
                 40,855 
                 26-Apr-93 
               
               
                   
                   
                   
                   
                   
                 complete mRNA. 
               
               
                   
                   
                 GB_PAT: I19994 
                 2516 
                 I19994 
                 Sequence 2 from patent U.S. Pat. No. 5512478. 
                 Unknown. 
                 40,855 
                 07-OCT-1996 
               
               
                   
                   
                 GB_BA2: AF059680 
                 2410 
                 AF059680 
                   Sphingomonas  sp. UG30 pentachlorophenol 4-monooxygenase 
                   Sphingomonas  sp. UG30 
                 42,993 
                 27-Apr-99 
               
               
                   
                   
                   
                   
                   
                 (pcpB) gene, complete cds; and pentachlorophenol 4-monooxygenase 
               
               
                   
                   
                   
                   
                   
                 reductase (pcpD) gene, partial cds. 
               
               
                 rxa01412 
                 327 
                 GB_GSS12: AQ332469 
                 459 
                 AQ332469 
                 HS_5003_A1_H08_SP6E RPCI11 Human Male BAC Library  Homo   
                 
                   Homo sapiens 
                 
                 38,208 
                 06-MAR-1999 
               
               
                   
                   
                   
                   
                   
                   sapiens  genomic clone Plate = 579 Col = 15 Row = O, genomic survey 
               
               
                   
                   
                   
                   
                   
                 sequence. 
               
               
                   
                   
                 GB_EST27: AA998532 
                 453 
                 AA998532 
                 UI-R-C0-ic-d-11-0-UI.s1 UI-R-C0  Rattus norvegicus  cDNA clone UI-R- 
                 
                   Rattus norvegicus 
                 
                 39,336 
                 09-MAR-1999 
               
               
                   
                   
                   
                   
                   
                 C0-ic-d-11-0-UI 3′, mRNA sequence. 
               
               
                   
                   
                 GB_HTG1: HSA342D11 
                 178183 
                 AL121748 
                   Homo sapiens  chromosome 10 clone RP11-342D11, *** 
                 
                   Homo sapiens 
                 
                 40,550 
                 23-Nov-99 
               
               
                   
                   
                   
                   
                   
                 SEQUENCING IN PROGRESS ***, in unordered pieces. 
               
               
                 rxa01458 
                 1173 
                 GB_BA2: AE000745 
                 15085 
                 AE000745 
                   Aquifex aeolicus  section 77 of 109 of the complete genome. 
                 
                   Aquifex aeolicus 
                 
                 37,694 
                 25-MAR-1998 
               
               
                   
                   
                 GB_BA2: AE000745 
                 15085 
                 AE000745 
                   Aquifex aeolicus  section 77 of 109 of the complete genome. 
                 
                   Aquifex aeolicus 
                 
                 35,567 
                 25-MAR-1998 
               
               
                 rxa01571 
                 723 
                 GB_BA1: AB011413 
                 12070 
                 AB011413 
                   Streptomyces griseus  genes for Orf2, Orf3, Orf4, Orf5, AfsA, Orf8, 
                 
                   Streptomyces griseus 
                 
                 57,500 
                 7-Aug-98 
               
               
                   
                   
                   
                   
                   
                 partial and complete cds. 
               
               
                   
                   
                 GB_BA1: AB011413 
                 12070 
                 AB011413 
                   Streptomyces griseus  genes for Orf2, Orf3, Orf4, Orf5, AfsA, Orf8, 
                 
                   Streptomyces griseus 
                 
                 35,655 
                 7-Aug-98 
               
               
                   
                   
                   
                   
                   
                 partial and complete cds. 
               
               
                 rxa01607 
                 753 
                 GB_PR4: AC005005 
                 133893 
                 AC005005 
                   Homo sapiens  PAC clone DJ412A9 from 22, complete sequence. 
                 
                   Homo sapiens 
                 
                 38,399 
                 02-MAR-1999 
               
               
                   
                   
                 GB_HTG3: AC008257 
                 109187 
                 AC008257 
                   Drosophila melanogaster  chromosome 2 clone BACR08A11 (D916) 
                 
                   Drosophila melanogaster 
                 
                 33,741 
                 08-OCT-1999 
               
               
                   
                   
                   
                   
                   
                 RPCI-98 08.A.11 map 42A-42A strain y; cn bw sp, *** SEQUENCING 
               
               
                   
                   
                   
                   
                   
                 IN PROGRESS ***, 93 unordered pieces. 
               
               
                   
                   
                 GB_HTG3: AC008257 
                 109187 
                 AC008257 
                   Drosophila melanogaster  chromosome 2 clone BACR08A11 (D916) 
                 
                   Drosophila melanogaster 
                 
                 33,741 
                 08-OCT-1999 
               
               
                   
                   
                   
                   
                   
                 RPCI-98 08.A.11 map 42A-42A strain y; cn bw sp, *** SEQUENCING 
               
               
                   
                   
                   
                   
                   
                 IN PROGRESS ***, 93 unordered pieces. 
               
               
                 rxa01609 
                 996 
                 GB_BA1: MTV003 
                 13246 
                 AL008883 
                   Mycobacterium tuberculosis  H37Rv complete genome; segment 
                 
                   Mycobacterium 
                 
                 39,369 
                 17-Jun-98 
               
               
                   
                   
                   
                   
                   
                 125/162. 
                 
                   tuberculosis 
                 
               
               
                   
                   
                 GB_BA1: MSGB1529CS 
                 36985 
                 L78824 
                   Mycobacterium leprae  cosmid B1529 DNA sequence. 
                 
                   Mycobacterium leprae 
                 
                 60,624 
                 15-Jun-96 
               
               
                   
                   
                 GB_BA1: AB024601 
                 14807 
                 AB024601 
                   Pseudomonas aeruginosa  dapD gene for tetrahydrodipicolinate N- 
                 
                   Pseudomonas aeruginosa 
                 
                 41,603 
                 12-MAR-1999 
               
               
                   
                   
                   
                   
                   
                 succinyletransferase, complete cds, strain PAO1. 
               
               
                 rxa01654 
                 1119 
                 GB_GSS4: AQ704352 
                 532 
                 AQ704352 
                 HS_2147_A2_H04_MR CIT Approved Human Genomic Sperm 
                 
                   Homo sapiens 
                 
                 37,838 
                 7-Jul-99 
               
               
                   
                   
                   
                   
                   
                 Library D  Homo sapiens  genomic clone Plate = 2147 Col = 8 Row = O, 
               
               
                   
                   
                   
                   
                   
                 genomic survey sequence. 
               
               
                   
                   
                 GB_RO: MMAE000663 
                 250611 
                 AE000663 
                   Mus musculus  TCR beta locus from bases 1 to 250611 (section 1 of 
                 
                   Mus musculus 
                 
                 35,799 
                 4-Sep-97 
               
               
                   
                   
                   
                   
                   
                 3) of the complete sequence. 
               
               
                   
                   
                 GB_EST23: AI158428 
                 511 
                 AI158428 
                 ud24f12.r1 Soares 2NbMT  Mus musculus  cDNA clone 
                 
                   Mus musculus 
                 
                 41,337 
                 30-Sep-98 
               
               
                   
                   
                   
                   
                   
                 IMAGE: 1446863 5′, mRNA sequence. 
               
               
                 rxa01664 
                 945 
                 GB_OV: AF026198 
                 63155 
                 AF026198 
                   Fugu rubripes  neural cell adhesion molecule L1 homolog (L1-CAM) 
                 
                   Fugu rubripes 
                 
                 35,187 
                 02-MAY-1998 
               
               
                   
                   
                   
                   
                   
                 gene, complete cds; putative protein 1 (PUT1) gene, partial cds; 
               
               
                   
                   
                   
                   
                   
                 mitosis-specific chromosome segregation protein SMC1 homolog 
               
               
                   
                   
                   
                   
                   
                 (SMC1) gene, complete cds; and calcium channel alpha-1 subunit 
               
               
                   
                   
                   
                   
                   
                 homolog (CCA1) and putative protein 2 (PUT2) genes, partial cds, 
               
               
                   
                   
                   
                   
                   
                 complete sequence. 
               
               
                   
                   
                 GB_PR3: AC004466 
                 122186 
                 AC004466 
                   Homo sapiens  12q13.1 PAC RPCI5-1057I20 (Roswell Park Cancer 
                 
                   Homo sapiens 
                 
                 37,382 
                 17-Sep-98 
               
               
                   
                   
                   
                   
                   
                 Institute Human PAC library) complete sequence. 
               
               
                   
                   
                 GB_PR3: AC004466 
                 122186 
                 AC004466 
                   Homo sapiens  12q13.1 PAC RPCI5-1057I20 (Roswell Park Cancer 
                 
                   Homo sapiens 
                 
                 37,325 
                 17-Sep-98 
               
               
                   
                   
                   
                   
                   
                 Institute Human PAC library) complete sequence. 
               
               
                 rxa01795 
                 720 
                 GB_BA2: CGU13922 
                 4412 
                 U13922 
                   Corynebacterium glutamicum  putative type II 5-cytosoine 
                 
                   Corynebacterium 
                 
                 99,444 
                 3-Feb-98 
               
               
                   
                   
                   
                   
                   
                 methyltransferase (cgIIM) and putative type II restriction endonuclease 
                 glutamicum 
               
               
                   
                   
                   
                   
                   
                 (cgIIR) and putative type I or type III restriction endonuclease (clgIIR) 
               
               
                   
                   
                   
                   
                   
                 genes, complete cds. 
               
               
                   
                   
                 GB_BA1: S86113 
                 1044 
                 S86113 
                 ORF 1 [ Neisseria gonorrhoeae , Genomic, 1044 nt]. 
                 
                   Neisseria gonorrhoeae 
                 
                 58,320 
                 07-MAY-1993 
               
               
                   
                   
                 GB_PAT: I22080 
                 850 
                 I22080 
                 Sequence 1 from patent U.S. Pat. No. 5525717. 
                 Unknown. 
                 57,722 
                 07-OCT-1996 
               
               
                 rxa01802 
                 954 
                 GB_BA2: AE001519 
                 14062 
                 AE001519 
                   Helicobacter pylori , strain J99 section 80 of 132 of the complete 
                   Helicobacter pylori  J99 
                 33,510 
                 20-Jan-99 
               
               
                   
                   
                   
                   
                   
                 genome. 
               
               
                   
                   
                 GB_GSS5: AQ774071 
                 552 
                 AQ774071 
                 HS_2269_B1_C10_T7C CIT Approved Human Genomic Sperm 
                 
                   Homo sapiens 
                 
                 37,967 
                 29-Jul-99 
               
               
                   
                   
                   
                   
                   
                 Library D  Homo sapiens  genomic clone Plate = 2269 Col = 19 Row = F, 
               
               
                   
                   
                   
                   
                   
                 genomic survey sequence. 
               
               
                   
                   
                 GB_PR4: AC007459 
                 40907 
                 AC007459 
                   Homo sapiens  chromosome 16 clone 306C6, complete sequence. 
                 
                   Homo sapiens 
                 
                 39,140 
                 04-MAY-1999 
               
               
                 rxa01838 
                 842 
                 GB_BA1: SCE15 
                 26440 
                 AL049707 
                   Streptomyces coelicolor  cosmid E15. 
                 
                   Streptomyces coelicolor 
                 
                 36,297 
                 22-Apr-99 
               
               
                   
                   
                 GB_HTG3: AC009545 
                 165042 
                 AC009545 
                   Homo sapiens  chromosome 11 clone 131_J_04 map 11, *** 
                 
                   Homo sapiens 
                 
                 37,651 
                 01-OCT-1999 
               
               
                   
                   
                   
                   
                   
                 SEQUENCING IN PROGRESS ***, 8 unordered pieces. 
               
               
                   
                   
                 GB_HTG3: AC009545 
                 165042 
                 AC009545 
                   Homo sapiens  chromosome 11 clone 131_J_04 map 11, *** 
                 
                   Homo sapiens 
                 
                 37,651 
                 01-OCT-1999 
               
               
                   
                   
                   
                   
                   
                 SEQUENCING IN PROGRESS ***, 8 unordered pieces. 
               
               
                 rxa01848 
                 867 
                 GB_BA1: MTCY24A1 
                 20270 
                 Z95207 
                   Mycobacterium tuberculosis  H37Rv complete genome; segment 
                 
                   Mycobacterium 
                 
                 38,270 
                 17-Jun-98 
               
               
                   
                   
                   
                   
                   
                 124/162. 
                 
                   tuberculosis 
                 
               
               
                   
                   
                 GB_EST21: C89252 
                 587 
                 C89252 
                 C89252 Mouse early blastocyst cDNA  Mus musculus  cDNA clone 
                 
                   Mus musculus 
                 
                 37,219 
                 28-MAY-1998 
               
               
                   
                   
                   
                   
                   
                 01B00061JC08, mRNA sequence. 
               
               
                   
                   
                 GB_EST14: AA423340 
                 457 
                 AA423340 
                 ve39d04.r1 Soares mouse mammary gland NbMMG  Mus musculus   
                 
                   Mus musculus 
                 
                 38,377 
                 16-OCT-1997 
               
               
                   
                   
                   
                   
                   
                 cDNA clone IMAGE: 820519 5′, mRNA sequence. 
               
               
                 rxa01849 
                 1224 
                 GB_BA1: MTCY24A1 
                 20270 
                 Z95207 
                   Mycobacterium tuberculosis  H37Rv complete genome; segment 
                 
                   Mycobacterium 
                 
                 39,950 
                 17-Jun-98 
               
               
                   
                   
                   
                   
                   
                 124/162. 
                 
                   tuberculosis 
                 
               
               
                   
                   
                 GB_BA2: RCPHSYNG 
                 45959 
                 Z11165 
                   R. capsulatus  complete photosynthesis gene cluster. 
                 
                   Rhodobacter capsulatus 
                 
                 37,344 
                 2-Sep-99 
               
               
                   
                   
                 GB_BA1: RSP010302 
                 40707 
                 AJ010302 
                   Rhodobacter sphaeroides  photosynthetic gene cluster. 
                 
                   Rhodobacter sphaeroides 
                 
                 40,898 
                 27-Aug-99 
               
               
                 rxa01868 
                 2049 
                 GB_BA1: MTV033 
                 21620 
                 AL021928 
                   Mycobacterium tuberculosis  H37Rv complete genome; segment 
                 
                   Mycobacterium 
                 
                 38,679 
                 17-Jun-98 
               
               
                   
                   
                   
                   
                   
                 11/162. 
                 
                   tuberculosis 
                 
               
               
                   
                   
                 GB_BA1: MLCL622 
                 42498 
                 Z95398 
                   Mycobacterium leprae  cosmid L622. 
                 
                   Mycobacterium leprae 
                 
                 38,911 
                 24-Jun-97 
               
               
                   
                   
                 GB_BA1: MSGB983CS 
                 36788 
                 L78828 
                   Mycobacterium leprae  cosmid B983 DNA sequence. 
                 
                   Mycobacterium leprae 
                 
                 38,933 
                 15-Jun-96 
               
               
                 rxa01885 
                 924 
                 GB_BA1: MTCY1A10 
                 25949 
                 Z95387 
                   Mycobacterium tuberculosis  H37Rv complete genome; segment 
                 
                   Mycobacterium 
                 
                 51,094 
                 17-Jun-98 
               
               
                   
                   
                   
                   
                   
                 117/162. 
                 
                   tuberculosis 
                 
               
               
                   
                   
                 GB_PR3: HSU220B11 
                 41247 
                 Z69908 
                 Human DNA sequence from cosmid cU220B11, between markers 
                 
                   Homo sapiens 
                 
                 39,038 
                 23-Nov-99 
               
               
                   
                   
                   
                   
                   
                 DXS6791 and DXS8038 on chromosome X. 
               
               
                   
                   
                 GB_BA1: PDU17435 
                 993 
                 U17435 
                   Paracoccus denitrificans  Fnr-like transcriptional activator (nnr) gene, 
                 
                   Paracoccus denitrificans 
                 
                 39,390 
                 19-Jul-95 
               
               
                   
                   
                   
                   
                   
                 complete cds. 
               
               
                 rxa01914 
                 526 
                 GB_PR3: AC005796 
                 43843 
                 AC005796 
                   Homo sapiens  chromosome 19, cosmid R31408, complete sequence. 
                 
                   Homo sapiens 
                 
                 34,961 
                 06-OCT-1998 
               
               
                   
                   
                 GB_PR3: HS390C10 
                 114231 
                 AL008721 
                   Homo sapiens  DNA sequence from BAC 390C10 on chromosome 
                 
                   Homo sapiens 
                 
                 39,600 
                 23-Nov-99 
               
               
                   
                   
                   
                   
                   
                 22q11.21-12.1. Contains an Immunoglobulin LIKE gene and a 
               
               
                   
                   
                   
                   
                   
                 pseudogene similar to Beta Crystallin. Contains ESTs, STSs, GSSs 
               
               
                   
                   
                   
                   
                   
                 and taga and tat repeat polymorphisms, complete sequence. 
               
               
                   
                   
                 GB_PR3: AC005796 
                 43843 
                 AC005796 
                   Homo sapiens  chromosome 19, cosmid R31408, complete sequence. 
                 
                   Homo sapiens 
                 
                 37,725 
                 06-OCT-1998 
               
               
                 rxa01932 
                 1020 
                 GB_PR3: AC003025 
                 112309 
                 AC003025 
                 Human Chromosome 11p12.2 PAC clone pDJ466a11, complete 
                 
                   Homo sapiens 
                 
                 35,585 
                 23-Jul-98 
               
               
                   
                   
                   
                   
                   
                 sequence. 
               
               
                   
                   
                 GB_GSS3: B78728 
                 312 
                 B78728 
                 CIT-HSP-431E3.TV CIT-HSP  Homo sapiens  genomic clone 431E3, 
                 
                   Homo sapiens 
                 
                 38,907 
                 25-Jun-98 
               
               
                   
                   
                   
                   
                   
                 genomic survey sequence. 
               
               
                   
                   
                 GB_PR3: AC003025 
                 112309 
                 AC003025 
                 Human Chromosome 11p12.2 PAC clone pDJ466a11, complete 
                 
                   Homo sapiens 
                 
                 35,859 
                 23-Jul-98 
               
               
                   
                   
                   
                   
                   
                 sequence. 
               
               
                 rxa01933 
                 726 
                 GB_HTG1: HS74O16 
                 169401 
                 AL110119 
                   Homo sapiens  chromosome 21 clone RPCIP704O1674 map 21q21, 
                 
                   Homo sapiens 
                 
                 35,302 
                 27-Aug-99 
               
               
                   
                   
                   
                   
                   
                 *** SEQUENCING IN PROGRESS ***, in unordered pieces. 
               
               
                   
                   
                 GB_HTG1: HS74O16 
                 169401 
                 AL110119 
                   Homo sapiens  chromosome 21 clone RPCIP704O1674 map 21q21, 
                 
                   Homo sapiens 
                 
                 35,302 
                 27-Aug-99 
               
               
                   
                   
                   
                   
                   
                 *** SEQUENCING IN PROGRESS ***, in unordered pieces. 
               
               
                   
                   
                 GB_PR4: AC006032 
                 170282 
                 AC006032 
                   Homo sapiens  BAC clone NH0115E20 from Y, complete sequence. 
                 
                   Homo sapiens 
                 
                 37,640 
                 27-Feb-99 
               
               
                 rxa01971 
                 954 
                 GB_HTG3: AC008230 
                 108469 
                 AC008230 
                   Drosophila melanogaster  chromosome 2 clone BACR17I17 (D934) 
                 
                   Drosophila melanogaster 
                 
                 35,466 
                 10-Aug-99 
               
               
                   
                   
                   
                   
                   
                 RPCI-98 17.I.17 map 53A-53C strain y; cn bw sp, *** SEQUENCING 
               
               
                   
                   
                   
                   
                   
                 IN PROGRESS ***, 108 unordered pieces. 
               
               
                   
                   
                 GB_HTG3: AC008230 
                 108469 
                 AC008230 
                   Drosophila melanogaster  chromosome 2 clone BACR17I17 (D934) 
                 
                   Drosophila melanogaster 
                 
                 35,466 
                 10-Aug-99 
               
               
                   
                   
                   
                   
                   
                 RPCI-98 17.I.17 map 53A-53C strain y; cn bw sp, *** SEQUENCING 
               
               
                   
                   
                   
                   
                   
                 IN PROGRESS***, 108 unordered pieces. 
               
               
                   
                   
                 GB_PR3: AF064860 
                 165382 
                 AF064860 
                   Homo sapiens  chromosome 21q22.3 PAC 70I24, complete sequence. 
                 
                   Homo sapiens 
                 
                 39,716 
                 2-Jun-98 
               
               
                 rxa02016 
                 900 
                 GB_EST2: D48846 
                 459 
                 D48846 
                 RICS15292A Rice green shoot  Oryza sativa  cDNA, mRNA sequence. 
                 
                   Oryza sativa 
                 
                 37,118 
                 2-Aug-95 
               
               
                   
                   
                 GB_GSS10: AQ195886 
                 595 
                 AQ195886 
                 RPCI11-66O13.TJ RPCI-11  Homo sapiens  genomic clone RPCI-11- 
                 
                   Homo sapiens 
                 
                 41,000 
                 20-Apr-99 
               
               
                   
                   
                   
                   
                   
                 66O13, genomic survey sequence. 
               
               
                   
                   
                 GB_GSS10: AQ195886 
                 595 
                 AQ195886 
                 RPCI11-66O13.TJ RPCI-11  Homo sapiens  genomic clone RPCI-11- 
                 
                   Homo sapiens 
                 
                 34,790 
                 20-Apr-99 
               
               
                   
                   
                   
                   
                   
                 66O13, genomic survey sequence. 
               
               
                 rxa02017 
                 807 
                 GB_EST20: AA855266 
                 406 
                 AA855266 
                 vw70b08.r1 Stratagene mouse heart (#937316)  Mus musculus  cDNA 
                 
                   Mus musculus 
                 
                 42,638 
                 06-MAR-1998 
               
               
                   
                   
                   
                   
                   
                 clone IMAGE: 1260279 5′, mRNA sequence. 
               
               
                   
                   
                 GB_EST20: AA855266 
                 406 
                 AA855266 
                 vw70b08.r1 Stratagene mouse heart (#937316)  Mus musculus  cDNA 
                 
                   Mus musculus 
                 
                 37,183 
                 06-MAR-1998 
               
               
                   
                   
                   
                   
                   
                 clone IMAGE: 1260279 5′, mRNA sequence. 
               
               
                 rxa02018 
                 1073 
                 GB_BA1: SC5C7 
                 41906 
                 AL031515 
                   Streptomyces coelicolor  cosmid 5C7. 
                 
                   Streptomyces coelicolor 
                 
                 41,732 
                 7-Sep-98 
               
               
                   
                   
                 GB_BA1: MTCI65 
                 34331 
                 Z95584 
                   Mycobacterium tuberculosis  H37Rv complete genome; segment 
                 
                   Mycobacterium 
                 
                 62,395 
                 17-Jun-98 
               
               
                   
                   
                   
                   
                   
                 50/162. 
                 
                   tuberculosis 
                 
               
               
                   
                   
                 GB_BA1: SCJ12 
                 35302 
                 AL109989 
                   Streptomyces coelicolor  cosmid J12. 
                 
                   Streptomyces coelicolor 
                 
                 61,603 
                 24-Aug-99 
               
               
                   
                   
                   
                   
                   
                   
                 A3(2) 
               
               
                 rxa02048 
                 1497 
                 GB_PAT: E15823 
                 2323 
                 E15823 
                 DNA encoding cell surface protein from  Corynebacterium   
                 
                   Corynebacterium 
                 
                 53,942 
                 28-Jul-99 
               
               
                   
                   
                   
                   
                   
                   ammoniagenes . 
                 
                   ammoniagenes 
                 
               
               
                   
                   
                 GB_OM: SSAMPTDN 
                 3387 
                 Z29522 
                   S. scrofa  mRNA for aminopeptidase N. 
                 
                   Sus scrofa 
                 
                 42,672 
                 26-Sep-94 
               
               
                   
                   
                 GB_OV: D87992 
                 3181 
                 D87992 
                   Gallus gallus  mRNA for aminopeptidase Ey, complete cds. 
                 
                   Gallus gallus 
                 
                 41,554 
                 5-Jun-99 
               
               
                 rxa02101 
                 1386 
                 GB_BA1: AP000064 
                 247695 
                 AP000064 
                 A eropyrum pernix  genomic DNA, section 7/7. 
                 
                   Aeropyrum pernix 
                 
                 39,882 
                 22-Jun-99 
               
               
                   
                   
                 GB_PL2: ATAC006587 
                 79262 
                 AC006587 
                   Arabidopsis thaliana  chromosome II BAC T17D12 genomic sequence, 
                 
                   Arabidopsis thaliana 
                 
                 38,490 
                 23-MAR-1999 
               
               
                   
                   
                   
                   
                   
                 complete sequence. 
               
               
                   
                   
                 GB_PL2: ATAC006587 
                 79262 
                 AC006587 
                   Arabidopsis thaliana  chromosome II BAC T17D12 genomic sequence, 
                 
                   Arabidopsis thaliana 
                 
                 34,863 
                 23-MAR-1999 
               
               
                   
                   
                   
                   
                   
                 complete sequence. 
               
               
                 rxa02265 
                 423 
                 GB_BA2: AF120718 
                 4137 
                 AF120718 
                   Lactobacillus fermentum  urease operon, partial sequence. 
                 
                   Lactobacillus fermentum 
                 
                 56,265 
                 31-MAR-1999 
               
               
                   
                   
                 GB_PAT: E03531 
                 2896 
                 E03531 
                 DNA sequence coding for acid urease. 
                 
                   Lactobacillus fermentum 
                 
                 56,265 
                 29-Sep-97 
               
               
                   
                   
                 GB_BA1: LBAAURE 
                 2896 
                 D10605 
                   L. fermentum  gene for acid urease. 
                 
                   Lactobacillus fermentum 
                 
                 56,265 
                 2-Feb-99 
               
               
                 rxa02276 
                 801 
                 GB_GSS10: AQ242920 
                 451 
                 AQ242920 
                 HS_2061_A1_E08_MR CIT Approved Human Genomic Sperm 
                 
                   Homo sapiens 
                 
                 37,916 
                 03-OCT-1998 
               
               
                   
                   
                   
                   
                   
                 Library D  Homo sapiens  genomic clone Plate = 2061 Col = 15 Row = I, 
               
               
                   
                   
                   
                   
                   
                 genomic survey sequence. 
               
               
                   
                   
                 GB_IN1: SLMMTPMF 
                 14503 
                 D29637 
                   Physarum polycephalum  mitochondrial DNA. 
                 
                   Mitochondrion Physarum 
                 
                 40,335 
                 12-MAY-1999 
               
               
                   
                   
                   
                   
                   
                   
                 
                   polycephalum 
                 
               
               
                   
                   
                 GB_IN2: AF012249 
                 5542 
                 AF012249 
                   Physarum polycephalum  strain aux2-S region of mitochondria derived 
                 Mitochondrion Physarum 
                 40,335 
                 08-MAY-1998 
               
               
                   
                   
                   
                   
                   
                 from mF plasmid, including URFA′, URFC, URFD, URFE, URFF, and 
                 
                   polycephalum 
                 
               
               
                   
                   
                   
                   
                   
                 URFG genes, complete cds, and URFH gene, partial cds. 
               
               
                 rxa02277 
                 738 
                 GB_BA2: AF048784 
                 681 
                 AF048784 
                   Actinomyces naeslundii  urease accessory protein (ureG) gene, 
                 
                   Actinomyces naeslundii 
                 
                 66,814 
                 9-Feb-99 
               
               
                   
                   
                   
                   
                   
                 complete cds. 
               
               
                   
                   
                 GB_BA2: AF056321 
                 5482 
                 AF056321 
                   Actinomyces naeslundii  urease gamma subunit UreA (ureA), urease 
                 
                   Actinomyces naeslundii 
                 
                 63,686 
                 9-Feb-99 
               
               
                   
                   
                   
                   
                   
                 beta subunit UreB (ureB), urease alpha subunit UreC (ureC), urease 
               
               
                   
                   
                   
                   
                   
                 accessory protein UreE (ureE), urease accessory protein UreF 
               
               
                   
                   
                   
                   
                   
                 (ureF), urease accessory protein UreG (ureG), and urease accessory 
               
               
                   
                   
                   
                   
                   
                 protein UreD (ureD) genes, complete cds. 
               
               
                   
                   
                 GB_BA2: SSU35248 
                 5773 
                 U35248 
                   Streptococcus salivarius  ure cluster nickel transporter homolog (urel) 
                 
                   Streptococcus salivarius 
                 
                 61,931 
                 26-Jan-96 
               
               
                   
                   
                   
                   
                   
                 gene, partial cds, and urease beta subunit (ureA), gamma subunit 
               
               
                   
                   
                   
                   
                   
                 (ureB), alpha subunit (ureC), and accessory proteins (ureE), (ureF), 
               
               
                   
                   
                   
                   
                   
                 (ureG), and (ureD) genes, complete cds. 
               
               
                 rxa02278 
                 972 
                 GB_GSS3: B49054 
                 543 
                 B49054 
                 RPCI11-4I13.TV RPCI-11  Homo sapiens  genomic clone RPCI-11- 
                 
                   Homo sapiens 
                 
                 39,161 
                 8-Apr-99 
               
               
                   
                   
                   
                   
                   
                 4I13, genomic survey sequence. 
               
               
                   
                   
                 GB_PL1: PMCMSGI 
                 3363 
                 L27092 
                   Pneumocystis carinii  B-cell receptor (msgl) gene, 3′ end. 
                 
                   Pneumocystis carinii 
                 
                 39,819 
                 26-Sep-94 
               
               
                   
                   
                 GB_PL2: AF038556 
                 12792 
                 AF038556 
                   Pneumocystis carinii  f. sp. hominis variant regions of major surface 
                   Pneumocystis carinii  f. sp. 
                 33,832 
                 10-Sep-98 
               
               
                   
                   
                   
                   
                   
                 glycoproteins (msg1, msg3, msg4) genes, partial cds. 
                 hominis 
               
               
                 rxa02317 
                 735 
                 GB_GSS8: AQ051031 
                 914 
                 AQ051031 
                 nbxb0004dG10r CUGI Rice BAC Library  Oryza sativa  genomic clone 
                 
                   Oryza sativa 
                 
                 32,299 
                 24-MAR-1999 
               
               
                   
                   
                   
                   
                   
                 nbxb0004N20r, genomic survey sequence. 
               
               
                   
                   
                 GB_GSS8: AQ051031 
                 914 
                 AQ051031 
                 nbxb0004dG10r CUGI Rice BAC Library  Oryza sativa  genomic clone 
                 
                   Oryza sativa 
                 
                 34,573 
                 24-MAR-1999 
               
               
                   
                   
                   
                   
                   
                 nbxb0004N20r, genomic survey sequence. 
               
               
                 rxa02334 
                 746 
                 GB_BA1: CGU35023 
                 3195 
                 U35023 
                   Corynebacterium glutamicum  thiosulfate sulfurtransferase (thtR) gene, 
                 
                   Corynebacterium 
                 
                 100,000 
                 16-Jan-97 
               
               
                   
                   
                   
                   
                   
                 partial cds, acyl CoA carboxylase (accBC) gene, complete cds. 
                 
                   glutamicum 
                 
               
               
                   
                   
                 GB_BA1: MTCY71 
                 42729 
                 Z92771 
                   Mycobacterium tuberculosis  H37Rv complete genome; segment 
                 
                   Mycobacterium 
                 
                 60,380 
                 10-Feb-99 
               
               
                   
                   
                   
                   
                   
                 141/162. 
                 
                   tuberculosis 
                 
               
               
                   
                   
                 GB_BA1: U00012 
                 33312 
                 U00012 
                   Mycobacterium leprae  cosmid B1308. 
                 Mycobacterium leprae 
                 37,660 
                 30-Jan-96 
               
               
                 rxa02351 
                 1039 
                 GB_HTG2: HS225E12 
                 126464 
                 AL031772 
                   Homo sapiens  chromosome 6 clone RP1-225E12 map q24, *** 
                 
                   Homo sapiens 
                 
                 35,973 
                 03-DEC-1999 
               
               
                   
                   
                   
                   
                   
                 SEQUENCING IN PROGRESS ***, in unordered pieces. 
               
               
                   
                   
                 GB_HTG2: HS225E12 
                 126464 
                 AL031772 
                   Homo sapiens  chromosome 6 clone RP1-225E12 map q24, *** 
                 
                   Homo sapiens 
                 
                 35,973 
                 03-DEC-1999 
               
               
                   
                   
                   
                   
                   
                 SEQUENCING IN PROGRESS ***, in unordered pieces. 
               
               
                   
                   
                 GB_HTG2: HS225E12 
                 126464 
                 AL031772 
                   Homo sapiens  chromosome 6 clone RP1-225E12 map q24, *** 
                 
                   Homo sapiens 
                 
                 36,992 
                 03-DEC-1999 
               
               
                   
                   
                   
                   
                   
                 SEQUENCING IN PROGRESS ***, in unordered pieces. 
               
               
                 rxa02410 
                 789 
                 GB_BA1: AB020624 
                 1605 
                 AB020624 
                   Corynebacterium glutamicum  murl gene for D-glutamate racemase, 
                 
                   Corynebacterium 
                 
                 99,227 
                 24-Jul-99 
               
               
                   
                   
                   
                   
                   
                 complete cds. 
                 
                   glutamicum 
                 
               
               
                   
                   
                 GB_EST4: H51527 
                 294 
                 H51527 
                 yo33b09.s1 Soares adult brain N2b4HB55Y  Homo sapiens  cDNA 
                 
                   Homo sapiens 
                 
                 40,411 
                 18-Sep-95 
               
               
                   
                   
                   
                   
                   
                 clone IMAGE: 179705 3′, mRNA sequence. 
               
               
                   
                   
                 GB_GSS1: CNS003CM 
                 1101 
                 AL064136 
                   Drosophila melanogaster  genome survey sequence T7 end of BAC # 
                 
                   Drosophila melanogaster 
                 
                 37,674 
                 3-Jun-99 
               
               
                   
                   
                   
                   
                   
                 BACR08C19 of RPCI-98 library from  Drosophila melanogaster  (fruit 
               
               
                   
                   
                   
                   
                   
                 fly), genomic survey sequence. 
               
               
                 rxa02477 
                 744 
                 GB_HTG4: AC010054 
                 130191 
                 AC010054 
                   Drosophila melanogaster  chromosome 3L/74E2 clone RPCI98-15E10, 
                 
                   Drosophila melanogaster 
                 
                 37,466 
                 16-OCT-1999 
               
               
                   
                   
                   
                   
                   
                 *** SEQUENCING IN PROGRESS ***, 70 unordered pieces. 
               
               
                   
                   
                 GB_HTG4: AC010054 
                 130191 
                 AC010054 
                   Drosophila melanogaster  chromosome 3L/74E2 clone RPCI98-15E10, 
                 
                   Drosophila melanogaster 
                 
                 37,466 
                 16-OCT-1999 
               
               
                   
                   
                   
                   
                   
                 *** SEQUENCING IN PROGRESS ***, 70 unordered pieces. 
               
               
                   
                   
                 GB_HTG4: AC009375 
                 137069 
                 AC009375 
                   Drosophila melanogaster  chromosome 3L/75A1 clone RPCI98-44L18, 
                 
                   Drosophila melanogaster 
                 
                 39,118 
                 16-OCT-1999 
               
               
                   
                   
                   
                   
                   
                 *** SEQUENCING IN PROGRESS ***, 59 unordered pieces. 
               
               
                 rxa02513 
                 832 
                 GB_BA1: MTER260 
                 373 
                 X92572 
                   M. terrae  gene for 32 kDa protein (partial). 
                 
                   Mycobacterium terrae 
                 
                 42,895 
                 15-Jan-98 
               
               
                   
                   
                 GB_PL1: AB019229 
                 84294 
                 AB019229 
                   Arabidopsis thaliana  genomic DNA, chromosome 3, P1 clone: 
                 
                   Arabidopsis thaliana 
                 
                 36,084 
                 20-Nov-99 
               
               
                   
                   
                   
                   
                   
                 MDC16, complete sequence. 
               
               
                   
                   
                 GB_PL1: AB019229 
                 84294 
                 AB019229 
                   Arabidopsis thaliana  genomic DNA, chromosome 3, P1 clone: 
                 
                   Arabidopsis thaliana 
                 
                 35,244 
                 20-Nov-99 
               
               
                   
                   
                   
                   
                   
                 MDC16, complete sequence. 
               
               
                 rxa02531 
                 834 
                 GB_BA1: CGLATTB 
                 271 
                 X89850 
                   C. glutamicum  DNA for attB region. 
                 
                   Corynebacterium 
                 
                 40,590 
                 8-Aug-96 
               
               
                   
                   
                   
                   
                   
                   
                 
                   glutamicum 
                 
               
               
                   
                   
                 GB_EST11: AA239557 
                 423 
                 AA239557 
                 mv25f04.r1 GuayWoodford Beier mouse kidney day 0  Mus musculus   
                 
                   Mus musculus 
                 
                 38,760 
                 12-MAR-1997 
               
               
                   
                   
                   
                   
                   
                 cDNA clone IMAGE: 656095 5′ similar to gb: X52634 Murine tlm 
               
               
                   
                   
                   
                   
                   
                 oncogene for tlm protein (MOUSE);, mRNA sequence. 
               
               
                   
                   
                 GB_BA1: RSPYPPCL 
                 6500 
                 AJ002398 
                   Rhodobacter sphaeroides  pyp and pcl genes, and orfA, orfB, orfC, 
                 
                   Rhodobacter sphaeroides 
                 
                 37,091 
                 17-DEC-1998 
               
               
                   
                   
                   
                   
                   
                 orfD, orfE, orfF. 
               
               
                 rxa02548 
                 314 
                 GB_BA2: AF127374 
                 63734 
                 AF127374 
                   Streptomyces lavendulae  LinA homolog, cytochrome P450 
                 
                   Streptomyces lavendulae 
                 
                 66,242 
                 27-MAY-1999 
               
               
                   
                   
                   
                   
                   
                 hydroxylase ORF4, cytochrome P450 hydroxylase ORF3, MitT (mitT), 
               
               
                   
                   
                   
                   
                   
                 MitS (mitS), MitR (mitR), MitQ (mitQ), MitP (mitP), MitO (mitO), MitN 
               
               
                   
                   
                   
                   
                   
                 (mitN), MitM (mitM), MitL (mitL), MitK (mitK), MitJ (mitJ), MitI (mitI), 
               
               
                   
                   
                   
                   
                   
                 MitH (mitH), MitG (mitG), MitF (mitF), MitE (mitE), MitD (mitD), MitC 
               
               
                   
                   
                   
                   
                   
                 (mitC), MitB (mitB), MitA (mitA), MmcA (mmcA), MmcB (mmcB), 
               
               
                   
                   
                   
                   
                   
                 MmcC (mmcC), MmcD (mmcD), MmcE (mmcE), MmcF (mmcF), 
               
               
                   
                   
                   
                   
                   
                 MmcG (mmcG), MmcH (mmcH), MmcI (mmcI), MmcJ (mmcJ), MmcK 
               
               
                   
                   
                   
                   
                   
                 (mmcK), MmcL (mmcL), MmcM (mmcM), MmcN (mmcN), MmcO 
               
               
                   
                   
                   
                   
                   
                 (mmcO), Mrd (mrd), MmcP (mmcP), MmcQ (mmcQ), MmcR (mmcR), 
               
               
                   
                   
                   
                   
                   
                 MmcS (mmcS), MmcT (mmcT), MmcU (mmcU), MmcV (mmcV), Mct 
               
               
                   
                   
                   
                   
                   
                 (mct), MmcW (mmcW), MmcX (mmcX), and MmcY (mmcY) genes, 
               
               
                   
                   
                   
                   
                   
                 complete cds; and unknown genes. 
               
               
                   
                   
                 GB_BA2: AF127374 
                 63734 
                 AF127374 
                   Streptomyces lavendulae  LinA homolog, cytochrome P450 
                 
                   Streptomyces lavendulae 
                 
                 38,411 
                 27-MAY-1999 
               
               
                   
                   
                   
                   
                   
                 hydroxylase ORF4, cytochrome P450 hydroxylase ORF3, MitT (mitT), 
               
               
                   
                   
                   
                   
                   
                 MitS (mitS), MitR (mitR), MitQ (mitQ), MitP (mitP), MitO (mitO), MitN 
               
               
                   
                   
                   
                   
                   
                 (mitN), MitM (mitM), MitL (mitL), MitK (mitK), MitJ (mitJ), MitI (mitI), 
               
               
                   
                   
                   
                   
                   
                 MitH (mitH), MitG (mitG), MitF (mitF), MitE (mitE), MitD (mitD), MitC 
               
               
                   
                   
                   
                   
                   
                 (mitC), MitB (mitB), MitA (mitA), MmcA (mmcA), MmcB (mmcB), 
               
               
                   
                   
                   
                   
                   
                 MmcC (mmcC), MmcD (mmcD), MmcE (mmcE), MmcF (mmcF), 
               
               
                   
                   
                   
                   
                   
                 MmcG (mmcG), MmcH (mmcH), MmcI (mmcI), MmcJ (mmcJ), MmcK 
               
               
                   
                   
                   
                   
                   
                 (mmcK), MmcL (mmcL), MmcM (mmcM), MmcN (mmcN), MmcO 
               
               
                   
                   
                   
                   
                   
                 (mmcO), Mrd (mrd), MmcP (mmcP), MmcQ (mmcQ), MmcR (mmcR), 
               
               
                   
                   
                   
                   
                   
                 MmcS (mmcS), MmcT (mmcT), MmcU (mmcU), MmcV (mmcV), Mct 
               
               
                   
                   
                   
                   
                   
                 (mct), MmcW (mmcW), MmcX (mmcX), and MmcY (mmcY) genes, 
               
               
                   
                   
                   
                   
                   
                 complete cds; and unknown genes. 
               
               
                   
                   
                 GB_GSS4: AQ741886 
                 742 
                 AQ741886 
                 HS_5569_B2_B02_SP6 RPCI-11 Human Male BAC Library  Homo   
                 
                   Homo sapiens 
                 
                 38,907 
                 16-Jul-99 
               
               
                   
                   
                   
                   
                   
                   sapiens  genomic clone Plate = 1145 Col = 4 Row = D, genomic survey 
               
               
                   
                   
                   
                   
                   
                 sequence. 
               
               
                 rxa02558 
                 1098 
                 GB_EST18: AA567307 
                 741 
                 AA567307 
                 HL01004.5prime HL  Drosophila melanogaster  head BlueScript 
                 
                   Drosophila melanogaster 
                 
                 38,736 
                 28-Nov-98 
               
               
                   
                   
                   
                   
                   
                   Drosophila melanogaster  cDNA clone HL01004 5prime, mRNA 
               
               
                   
                   
                   
                   
                   
                 sequence. 
               
               
                   
                   
                 GB_EST27: AI402394 
                 630 
                 AI402394 
                 GH21610.5prime GH  Drosophila melanogaster  head pOT2  Drosophila   
                 
                   Drosophila melanogaster 
                 
                 41,308 
                 8-Feb-99 
               
               
                   
                   
                   
                   
                   
                   melanogaster  cDNA clone GH21610 5prime, mRNA sequence. 
               
               
                   
                   
                 GB_GSS10: AQ237646 
                 715 
                 AQ237646 
                 RPCI11-61I9.TJB RPCI-11  Homo sapiens  genomic clone RPCI-11- 
                 
                   Homo sapiens 
                 
                 44,340 
                 21-Apr-99 
               
               
                   
                   
                   
                   
                   
                 61I9, genomic survey sequence. 
               
               
                 rxa02565 
                 1389 
                 GB_EST32: AI726448 
                 562 
                 AI726448 
                 BNLGHi5854 Six-day Cotton fiber  Gossypium hirsutum  cDNA 5′ 
                 
                   Gossypium hirsutum 
                 
                 37,003 
                 11-Jun-99 
               
               
                   
                   
                   
                   
                   
                 similar to (U53418) UDP-glucose dehydrogenase [ Glycine max ], 
               
               
                   
                   
                   
                   
                   
                 mRNA sequence. 
               
               
                   
                   
                 GB_EST32: AI726198 
                 608 
                 AI726198 
                 BNLGHi5243 Six-day Cotton fiber  Gossypium hirsutum  cDNA 5′ 
                 
                   Gossypium hirsutum 
                 
                 40,925 
                 11-Jun-99 
               
               
                   
                   
                   
                   
                   
                 similar to (U53418) UDP-glucose dehydrogenase [ Glycine max ], 
               
               
                   
                   
                   
                   
                   
                 mRNA sequence. 
               
               
                   
                   
                 GB_PR4: AC002992 
                 154848 
                 AC002992 
                   Homo sapiens  chromosome Y, clone 203M13, complete sequence. 
                 
                   Homo sapiens 
                 
                 38,039 
                 13-OCT-1999 
               
               
                 rxa02574 
                 1131 
                 GB_EST4: H29653 
                 415 
                 H29653 
                 ym58f01.r1 Soares infant brain 1NIB  Homo sapiens  cDNA clone 
                 
                   Homo sapiens 
                 
                 39,036 
                 17-Jul-95 
               
               
                   
                   
                   
                   
                   
                 IMAGE: 52678 5′ similar to SP: OXDD_BOVIN P31228 D-ASPARTATE 
               
               
                   
                   
                   
                   
                   
                 OXIDASE;, mRNA sequence. 
               
               
                   
                   
                 GB_PR3: HSDJ261K5 
                 131974 
                 AL050350 
                 Human DNA sequence from clone 261K5 on chromosome 6q21-22.1. 
                 
                   Homo sapiens 
                 
                 35,957 
                 23-Nov-99 
               
               
                   
                   
                   
                   
                   
                 Contains the 3′ part of the gene for a novel organic cation transporter 
               
               
                   
                   
                   
                   
                   
                 (BAC ORF RG331P03), the DDO gene for D-aspartate oxidase (EC 
               
               
                   
                   
                   
                   
                   
                 1.4.3.1), ESTs, STSs, GSSs and two putative CpG islands, complete 
               
               
                   
                   
                   
                   
                   
                 sequence. 
               
               
                   
                   
                 GB_EST2: R20147 
                 494 
                 R20147 
                 yg18h02.r1 Soares infant brain 1NIB  Homo sapiens  cDNA clone 
                 
                   Homo sapiens 
                 
                 36,437 
                 17-Apr-95 
               
               
                   
                   
                   
                   
                   
                 IMAGE: 32866 5′ similar to SP: OXDD_BOVIN P31228 D-ASPARTATE 
               
               
                   
                   
                   
                   
                   
                 OXIDASE;, mRNA sequence. 
               
               
                 rxa02589 
                 888 
                 GB_HTG1: CEY6E2 
                 186306 
                 Z96799 
                   Caenorhabditis elegans  chromosome V clone Y6E2, *** 
                 
                   Caenorhabditis elegans 
                 
                 37,979 
                 02-OCT-1997 
               
               
                   
                   
                   
                   
                   
                 SEQUENCING IN PROGRESS ***, in unordered pieces. 
               
               
                   
                   
                 GB_HTG1: CEY6E2 
                 186306 
                 Z96799 
                   Caenorhabditis elegans  chromosome V clone Y6E2, *** 
                 
                   Caenorhabditis elegans 
                 
                 37,979 
                 02-OCT-1997 
               
               
                   
                   
                   
                   
                   
                 SEQUENCING IN PROGRESS ***, in unordered pieces. 
               
               
                   
                   
                 GB_HTG3: AC011690 
                 72277 
                 AC011690 
                   Homo sapiens  clone 17_E_13, LOW-PASS SEQUENCE SAMPLING. 
                 
                   Homo sapiens 
                 
                 35,814 
                 10-OCT-1999 
               
               
                 rxa02592 
                 894 
                 GB_BA1: MSGB983CS 
                 36788 
                 L78828 
                   Mycobacterium leprae  cosmid B983 DNA sequence. 
                 Mycobacterium leprae 
                 53,235 
                 15-Jun-96 
               
               
                   
                   
                 GB_GSS9: AQ170723 
                 487 
                 AQ170723 
                 HS_2270_B2_F05_MR CIT Approved Human Genomic Sperm Library 
                 
                   Homo sapiens 
                 
                 39,666 
                 16-OCT-1998 
               
               
                   
                   
                   
                   
                   
                 D  Homo sapiens  genomic clone Plate = 2270 Col = 10 Row = L, genomic 
               
               
                   
                   
                   
                   
                   
                 survey sequence. 
               
               
                   
                   
                 GB_GSS12: AQ349397 
                 791 
                 AQ349397 
                 RPCI11-118H16.TJ RPCI-11  Homo sapiens  genomic clone RPCI-11- 
                 
                   Homo sapiens 
                 
                 34,204 
                 07-MAY-1999 
               
               
                   
                   
                   
                   
                   
                 118H16, genomic survey sequence. 
               
               
                 rxa02603 
                 1119 
                 GB_BA1: MTV026 
                 23740 
                 AL022076 
                   Mycobacterium tuberculosis  H37Rv complete genome; segment 
                 
                   Mycobacterium 
                 
                 37,975 
                 24-Jun-99 
               
               
                   
                   
                   
                   
                   
                 157/162. 
                 
                   tuberculosis 
                 
               
               
                   
                   
                 GB_IN2: AC005714 
                 177740 
                 AC005714 
                   Drosophila melanogaster , chromosome 2R, region 58D4-58E2, BAC 
                 
                   Drosophila melanogaster 
                 
                 41,226 
                 01-MAY-1999 
               
               
                   
                   
                   
                   
                   
                 clone BACR48M13, complete sequence. 
               
               
                   
                   
                 GB_EST19: AA775050 
                 218 
                 AA775050 
                 ac76e10.s1 Stratagene lung (#937210)  Homo sapiens  cDNA clone 
                 
                   Homo sapiens 
                 
                 40,826 
                 5-Feb-98 
               
               
                   
                   
                   
                   
                   
                 IMAGE: 868554 3′ similar to gb: Y00371_rna1 HEAT SHOCK 
               
               
                   
                   
                   
                   
                   
                 COGNATE 71 KD PROTEIN (HUMAN);, mRNA sequence. 
               
               
                 rxa02630 
                 1446 
                 GB_BA1: MLCL373 
                 37304 
                 AL035500 
                   Mycobacterium leprae  cosmid L373. 
                 
                   Mycobacterium leprae 
                 
                 49,015 
                 27-Aug-99 
               
               
                   
                   
                 GB_BA1: MTV044 
                 16150 
                 AL021999 
                   Mycobacterium tuberculosis  H37Rv complete genome; segment 
                 
                   Mycobacterium 
                 
                 49,192 
                 17-Jun-98 
               
               
                   
                   
                   
                   
                   
                 45/162. 
                 
                   tuberculosis 
                 
               
               
                   
                   
                 GB_BA1: MLU15180 
                 38675 
                 U15180 
                   Mycobacterium leprae  cosmid B1756. 
                 
                   Mycobacterium leprae 
                 
                 45,621 
                 09-MAR-1995 
               
               
                 rxa02643 
                 1167 
                 GB_EST37: AI950576 
                 308 
                 AI950576 
                 wx52e08.x1 NCI_CGAP_Lu28  Homo sapiens  cDNA clone 
                 
                   Homo sapiens 
                 
                 40,909 
                 6-Sep-99 
               
               
                   
                   
                   
                   
                   
                 IMAGE: 2547302 3′, mRNA sequence. 
               
               
                   
                   
                 GB_EST37: AI950576 
                 308 
                 AI950576 
                 wx52e08.x1 NCI_CGAP_Lu28  Homo sapiens  cDNA clone 
                 
                   Homo sapiens 
                 
                 40,288 
                 6-Sep-99 
               
               
                   
                   
                   
                   
                   
                 IMAGE: 2547302 3′, mRNA sequence. 
               
               
                 rxa02644 
                 774 
                 GB_EST34: AV149547 
                 302 
                 AV149547 
                 AV149547 Mus musculus C57BL/6J 10-11 day embryo  Mus musculus   
                 
                   Mus musculus 
                 
                 38,627 
                 5-Jul-99 
               
               
                   
                   
                   
                   
                   
                 cDNA clone 2810489D03, mRNA sequence. 
               
               
                   
                   
                 GB_EST35: AV156221 
                 271 
                 AV156221 
                 AV156221  Mus musculus  head C57BL/6J 12-day embryo  Mus   
                 
                   Mus musculus 
                 
                 33,990 
                 7-Jul-99 
               
               
                   
                   
                   
                   
                   
                   musculus  cDNA clone 3000001C24, mRNA sequence. 
               
               
                   
                   
                 GB_EST32: AV054919 
                 274 
                 AV054919 
                 AV054919  Mus musculus  pancreas C57BL/6J adult  Mus musculus   
                 
                   Mus musculus 
                 
                 36,585 
                 23-Jun-99 
               
               
                   
                   
                   
                   
                   
                 cDNA clone 1810033C08, mRNA sequence. 
               
               
                 rxa02745 
                 902 
                 GB_BA1: MTV007 
                 32806 
                 AL021184 
                   Mycobacterium tuberculosis  H37Rv complete genome; segment 
                 
                   Mycobacterium 
                 
                 39,298 
                 17-Jun-98 
               
               
                   
                   
                   
                   
                   
                 64/162. 
                 
                   tuberculosis 
                 
               
               
                   
                   
                 GB_BA2: AF027770 
                 30683 
                 AF027770 
                   Mycobacterium smegmatis  FxbA (fxbA) gene, partial cds; FxbB (fxbB), 
                 
                   Mycobacterium smegmatis 
                 
                 55,125 
                 03-DEC-1998 
               
               
                   
                   
                   
                   
                   
                 FxbC (fxbC), and FxuD (fxtD) genes, complete cds; and unknown 
               
               
                   
                   
                   
                   
                   
                 genes. 
               
               
                   
                   
                 GB_BA2: SAU43537 
                 3938 
                 U43537 
                   Streptomyces argillaceus  mithramycin resistance determinant, ATP- 
                 
                   Streptomyces argillaceus 
                 
                 46,868 
                 5-Sep-96 
               
               
                   
                   
                   
                   
                   
                 binding protein (mtrA) and membrane protein (mtrB) genes, complete 
               
               
                   
                   
                   
                   
                   
                 cds. 
               
               
                 rxa02746 
                 290 
                 GB_BA1: CAJ10319 
                 5368 
                 AJ010319 
                   Corynebacterium glutamicum  amtP, glnB, glnD genes and partial ftsY 
                 
                   Corynebacterium 
                 
                 100,000 
                 14-MAY-1999 
               
               
                   
                   
                   
                   
                   
                 and srp genes. 
                 
                   glutamicum 
                 
               
               
                   
                   
                 GB_BA1: MTCY338 
                 29372 
                 Z74697 
                   Mycobacterium tuberculosis  H37Rv complete genome; segment 
                 
                   Mycobacterium 
                 
                 39,785 
                 17-Jun-98 
               
               
                   
                   
                   
                   
                   
                 127/162. 
                 
                   tuberculosis 
                 
               
               
                   
                   
                 GB_HTG3: AC008733 
                 216140 
                 AC008733 
                   Homo sapiens  chromosome 19 clone CITB-E1_2525J15, *** 
                 
                   Homo sapiens 
                 
                 35,688 
                 3-Aug-99 
               
               
                   
                   
                   
                   
                   
                 SEQUENCING IN PROGRESS ***, 72 unordered pieces. 
               
               
                 rxa02820 
                 1411 
                 GB_BA1: BFU64514 
                 3837 
                 U64514 
                   Bacillus firmus  dppABC operon, dipeptide transporter protein dppA 
                 
                   Bacillus firmus 
                 
                 36,859 
                 1-Feb-97 
               
               
                   
                   
                   
                   
                   
                 gene, partial cds, and dipeptide transporter proteins dppB and dppC 
               
               
                   
                   
                   
                   
                   
                 genes, complete cds. 
               
               
                   
                   
                 GB_IN1: CET04C10 
                 20958 
                 Z69885 
                   Caenorhabditis elegans  cosmid T04C10, complete sequence. 
                 
                   Caenorhabditis elegans 
                 
                 35,934 
                 2-Sep-99 
               
               
                   
                   
                 GB_EST35: AI823090 
                 720 
                 AI823090 
                 L30-944T3 Ice plant Lambda Uni-Zap XR expression library, 30 hours 
                 
                   Mesembryanthemum 
                 
                 35,770 
                 21-Jul-99 
               
               
                   
                   
                   
                   
                   
                 NaCl treatment  Mesembryanthemum crystallinum  cDNA clone L30- 
                 
                   crystallinum 
                 
               
               
                   
                   
                   
                   
                   
                 944 5′ similar to 60S ribosomal protein L36 (AC004684)[ Arabidopsis   
               
               
                   
                   
                   
                   
                   
                   thaliana ], mRNA sequence. 
               
               
                 rxa02834 
                 518 
                 GB_BA1: CJY13333 
                 3315 
                 Y13333 
                   Campylobacter jejuni  clpB gene. 
                 
                   Campylobacter jejuni 
                 
                 53,400 
                 12-Apr-99 
               
               
                   
                   
                 GB_BA2: AF065404 
                 181654 
                 AF065404 
                   Bacillus anthracis  virulence plasmid PX01, complete sequence. 
                 
                   Bacillus anthracis 
                 
                 45,168 
                 20-OCT-1999 
               
               
                   
                   
                 GB_PL2: AC006601 
                 110684 
                 AC006601 
                   Arabidopsis thaliana  chromosome V map near 60.5 cM, complete 
                 
                   Arabidopsis thaliana 
                 
                 36,680 
                 22-Feb-99 
               
               
                   
                   
                   
                   
                   
                 sequence.