<i>CORYNEBACTERIUM GLUTAMICUM</i> GENES ENCODING PROTEINS INVOLVED IN CARBON METABOLISM AND ENERGY PRODUCTION

Abstract: Isolated nucleic acid molecules, designated SMP nucleic acid molecules, which encode novel SMP proteins from <i>Corynebacterium glutamicum</i> are described. The invention also provides antisense nucleic acid molecules, recombinant expression vectors containing SMP nucleic acid molecules, and host cells into which the expression vectors have been introduced. The invention still further provides isolated SMP proteins, mutated SMP proteins, fusion proteins, antigenic peptides and methods for the improvement of production of a desired compound from <i>C. glutamicum</i> based on genetic engineering of SMP genes in this organism.

Description: CORYNEBACTERIUM GLUTAMICUM GENES ENCODING PROTEINS INVOLVED IN CARBON METABOLISM AND ENERGY PRODUCTION Related Applications This application claims priority to prior U.S. Provisional Patent Application Serial No. 60/141031, filed June 25, 1999, U.S. Provisional Patent Application Serial No. 60/143208, filed July 9, 1999, and U.S. Provisional Patent Application Serial No. 60/151572, filed August 31, 1999. This application also claims priority to prior German Patent Application No. 19931412.8, filed July 8, 1999, German Patent Application No. 19931413.6, filed July 8, 1999, German Patent Application No. 19931419.5, filed July 8, 1999, German Patent Application No. 19931420.9, filed July 8, 1999, German Patent Application No. 19931424.1, filed July 8, 1999, German Patent Application No. 19931428.4 , filed July 8, 1999, German Patent Application No. 19931431.4, filed July 8, 1999, German Patent Application No. 19931433.0, filed July 8, 1999, German Patent Application No. 19931434.9, filed July 8, 1999, German Patent Application No. 19931510.8, filed July 8, 1999, German Patent Application No. 19931562.0, filed July 8, 1999, German Patent Application No. 19931634.1, filed July 8, 1999, German Patent Application No. 19932180.9, filed July 9, 1999, German Patent Application No. 19932227.9, filed July 9, 1999, German Patent Application No. 19932230.9, filed July 9, 1999, German Patent Application No. 19932924.9, filed July 14, 1999, German Patent Application No. 19932973.7, filed July 14, 1999, German Patent Application No. 19933005.0, filed July 14, 1999, German Patent Application No. 19940765.7, filed August 27, 1999, German Patent Application No. 19942076.9, filed September 3, 1999, German Patent Application No. 19942079.3, filed September 3, 1999, German Patent Application No. 19942086.6, filed September 3, 1999, German Patent Application No. 19942087.4, filed September 3, 1999, German Patent Application No. 19942088.2, filed September 3, 1999, German Patent Application No. 19942095.5, filed September 3, 1999, German Patent Application No. 19942123.4, filed September 3, 1999, and German Patent Application No. 19942125.0, filed September 3, 1999. The entire contents of all of the aforementioned application are hereby expressly incorporated herein by this reference. 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 sugar metabolism and oxidative phosphorylation (SMP) 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 SMP 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 SMP nucleic acids of the invention, or modification of the sequence of the SMP 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 SMP 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 SMP 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. The SMP proteins encoded by the novel nucleic acid molecules of the invention are capable of, for example, performing a function involved in the metabolism of carbon compounds such as sugars or in the generation of energy molecules by processes such as oxidative phosphorylation in Corynebacterium glutamicum. Given the availability of cloning vectors for use in Corynebacterium glutamicum, such as those disclosed in Sinskey et al, U.S. Patent 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 SMP 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. The degradation of high-energy carbon molecules such as sugars, and the conversion of compounds such as NADH and FADH 2 to compounds containing high energy phosphate bonds via oxidative phosphorylation results in a number of compounds which themselves may be desirable fine chemicals, such as pyruvate, ATP, NADH, and a number of intermediate sugar compounds. Further, the energy molecules (such as ATP) and the reducing equivalents (such as NADH or NADPH) produced by these metabolic pathways are utilized in the cell to drive reactions which would otherwise be energetically unfavorable. Such unfavorable reactions include many biosynthetic pathways for fine chemicals. By improving the ability of the cell to utilize a particular sugar (e.g., by manipulating the genes encoding enzymes involved in the degradation and conversion of that sugar into energy for the cell), one may increase the amount of energy available to permit unfavorable, yet desired metabolic reactions (e.g., the biosynthesis of a desired fine chemical) to occur. The mutagenesis of one or more SMP genes of the invention may also result in SMP proteins having altered activities which indirectly impact the production of one or more desired fine chemicals from C. glutamicum. For example, by increasing the efficiency of utilization of one or more sugars (such that the conversion of the sugar to useful energy molecules is improved), or by increasing the efficiency of conversion of reducing equivalents to useful energy molecules (e.g., by improving the efficiency of oxidative phosphorylation, or the activity of the ATP synthase), one can increase the amount of these high-energy compounds available to the cell to drive normally unfavorable metabolic processes. These processes include the construction of cell walls, transcription, translation, and the biosynthesis of compounds necessary for growth and division of the cells (e.g., nucleotides, amino acids, vitamins, lipids, etc.) (Lengeler et al. (1999) Biology of Prokaryotes, Thieme Verlag: Stuttgart, p. 88-109; 913-918; 875-899). By improving the growth and multiplication of these engineered cells, it is possible to increase both the viability of the cells in large-scale culture, and also to improve their rate of division, such that a relatively larger number of cells can survive in fermentor culture. The yield, production, or efficiency of production may be increased, at least due to the presence of a greater number of viable cells, each producing the desired fine chemical. Also, many of the degradation products produced during sugar metabolism are utilized by the cell as precursors or intermediates in the production of other desirable products, such as fine chemicals. So, by increasing the ability of the cell to metabolize sugars, the number of these degradation products available to the cell for other processes should also be increased. The invention provides novel nucleic acid molecules which encode proteins, referred to herein as SMP proteins, which are capable of, for example, performing a function involved in the metabolism of carbon compounds such as sugars and the generation of energy molecules by processes such as oxidative phosphorylation in Corynebacterium glutamicum. Nucleic acid molecules encoding an SMP protein are referred to herein as SMP nucleic acid molecules. In a preferred embodiment, the SMP protein participates in the conversion of carbon molecules and degradation products thereof to energy which is utilized by the cell for metabolic processes. 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 SMP protein or biologically active portions thereof, as well as nucleic acid fragments suitable as primers or hybridization probes for the detection or amplification of SMP- encoding nucleic acid (e.g. , DNA or mRNA). In particularly preferred embodiments, the isolated nucleic acid molecule comprises one of the nucleotide sequences set forth as the odd-numbered SEQ ID NOs in the Sequence Listing (e.g., SEQ ID NO:l, SEQ ID NO:3, SEQ ID NO:5, SEQ ID NO:7....), 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 as an odd-numbered SEQ ID NO in the Sequence Listing (e.g., SEQ ID NO:l, SEQ ID NO:3, SEQ ID NO:5, SEQ ID NO:7....), or a portion thereof. In other preferred embodiments, the isolated nucleic acid molecule encodes one of the amino acid sequences set forth as an even- numbered SEQ ID NO in the Sequence Listing (e.g., SEQ ID NO:2, SEQ ID NO:4, SEQ ID NO:6, SEQ ID NO:8....).. The preferred SMP proteins of the present invention also preferably possess at least one of the SMP 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 the invention (e.g., a sequence having an even-numbered SEQ ID NO: in the Sequence Listing), e.g., sufficiently homologous to an amino acid sequence of the invention such that the protein or portion thereof maintains an SMP activity. Preferably, the protein or portion thereof encoded by the nucleic acid molecule maintains the ability to perform a function involved in the metabolism of carbon compounds such as sugars or the generation of energy molecules (e.g., ATP) by processes such as oxidative phosphorylation in Corynebacterium glutamicum. 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 the invention (e.g. , an entire amino acid sequence selected those having an even-numbered SEQ ID NO in the Sequence Listing). In another preferred embodiment, the protein is a full length C. glutamicum protein which is substantially homologous to an entire amino acid sequence of the invention (encoded by an open reading frame shown in the corresponding odd- numbered SEQ ID NOs in the Sequence Listing (e.g. , SEQ ID NO: 1 , SEQ ID NO:3, SEQ ID NO:5, SEQ ID NO:7....). In another preferred embodiment, the isolated nucleic acid molecule is derived from C. glutamicum and encodes a protein (e.g., an SMP 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 the invention (e.g., a sequence of one of the even-numbered SEQ ID NOs in the Sequence Listing) and is able to perform a function involved in the metabolism of carbon compounds such as sugars or the generation of energy molecules (e.g. , ATP) by processes such as oxidative phosphorylation 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 the invention (e.g., a sequence of an odd- numbered SEQ ID NO in the Sequence Listing) 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 SMP 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 SMP protein by culturing the host cell in a suitable medium. The SMP 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 SMP 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 SMP sequence as a transgene. In another embodiment, an endogenous SMP gene within the genome of the microorganism has been altered, e.g., functionally disrupted, by homologous recombination with an altered SMP gene. In another embodiment, an endogenous or introduced SMP gene in a microorganism has been altered by one or more point mutations, deletions, or inversions, but still encodes a functional SMP protein. In still another embodiment, one or more of the regulatory regions (e.g., a promoter, repressor, or inducer) of an SMP gene in a microorganism has been altered (e.g., by deletion, truncation, inversion, or point mutation) such that the expression of the SMP 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 the Sequence Listing as SEQ ID NOs 1 through 782) 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 SMP protein or a portion, e.g., a biologically active portion, thereof. In a preferred embodiment, the isolated SMP protein or portion thereof is capable of performing a function involved in the metabolism of carbon compounds such as sugars or in the generation of energy molecules (e.g., ATP) by processes such as oxidative phosphorylation in Corynebacterium glutamicum. In another preferred embodiment, the isolated SMP protein or portion thereof is sufficiently homologous to an amino acid sequence of the invention (e.g. , a sequence of an even-numbered SEQ ID NO: in the Sequence Listing) such that the protein or portion thereof maintains the ability to perform a function involved in the metabolism of carbon compounds such as sugars or in the generation of energy molecules (e.g., ATP) by processes such as oxidative phosphorylation in Corynebacterium glutamicum. The invention also provides an isolated preparation of an SMP protein. In preferred embodiments, the SMP protein comprises an amino acid sequence of the invention (e.g., a sequence of an even-numbered SEQ ID NO: of the Sequence Listing). In another preferred embodiment, the invention pertains to an isolated full length protein which is substantially homologous to an entire amino acid sequence of the invention (e.g., a sequence of an even-numbered SEQ ID NO: of the Sequence Listing) (encoded by an open reading frame set forth in a corresponding odd-numbered SEQ ID NO: of the Sequence Listing). 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 the invention (e.g., a sequence of an even-numbered SEQ ID NO: of the Sequence Listing). In other embodiments, the isolated SMP protein comprises an amino acid sequence which is at least about 50% or more homologous to one of the amino acid sequences of the invention (e.g., a sequence of an even-numbered SEQ ID NO: of the Sequence Listing) and is able to perform a function involved in the metabolism of carbon compounds such as sugars or in the generation of energy molecules (e.g., ATP) by processes such as oxidative phosphorylation in Corynebacterium glutamicum, or has one or more of the activities set forth in Table 1. Alternatively, the isolated SMP 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%o, 97%, 98,%, or 99% or more homologous to a nucleotide sequence of one of the even-numbered SEQ ID NOs set forth in the Sequence Listing. It is also preferred that the preferred forms of SMP proteins also have one or more of the SMP bioactivities described herein. The SMP polypeptide, or a biologically active portion thereof, can be operatively linked to a non-SMP polypeptide to form a fusion protein. In preferred embodiments, this fusion protein has an activity which differs from that of the SMP protein alone. In other preferred embodiments, this fusion protein performs a function involved in the metabolism of carbon compounds such as sugars or in the generation of energy molecules (e.g., ATP) by processes such as oxidative phosphorylation in Corynebacterium glutamicum. 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 SMP protein, either by interacting with the protein itself or a substrate or binding partner of the SMP protein, or by modulating the transcription or translation of an SMP 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 SMP 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 SMP 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 SMP protein activity or SMP 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 carbon metabolism pathways or for the production of energy through processes such as oxidative phosphorylation, such that the yields or rate of production of a desired fine chemical by this microorganism is improved. The agent which modulates SMP protein activity can be an agent which stimulates SMP protein activity or SMP nucleic acid expression. Examples of agents which stimulate SMP protein activity or SMP nucleic acid expression include small molecules, active SMP proteins, and nucleic acids encoding SMP proteins that have been introduced into the cell. Examples of agents which inhibit SMP activity or expression include small molecules and antisense SMP 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 SMP 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 SMP nucleic acid and protein molecules which are involved in the metabolism of carbon compounds such as sugars and the generation of energy molecules by processes such as oxidative phosphorylation in Corynebacterium glutamicum. 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 a glycolytic pathway protein has a direct impact on the yield, production, and/or efficiency of production of, e.g., pyruvate from modified C. glutamicum), or may have 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 proteins involved in oxidative phosphorylation results in alterations in the amount of energy available to perform necessary metabolic processes and other cellular functions, such as nucleic acid and protein biosynthesis and transcription/translation). Aspects of the invention are further explicated below. L 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's Encyclopedia of Industrial Chemistry, vol. A27, "Vitamins", p. 443-613 (1996) VCH: Weinheim and references therein; and Ong, A.S., Niki, E. & 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 Sept. 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'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'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-l-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 r 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'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'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 & Sons; Ong, A.S., Niki, E. & 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 Sept. 1-3, 1994 at Penang, Malaysia, AOCS Press: Champaign, IL X, 374 S). Thiamin (vitamin Bi) 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 ' (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-l -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 Bι 2 ) and porphyrines belong to a group of chemicals characterized by a tetrapyrole ring system. The biosynthesis of vitamin Bι 2 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 , 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 (/. e. , AMP) or as coenzymes (/ ' . 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, -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. Patent 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. Sugar and Carbon Molecule Utilization and Oxidative Phosphorylation Carbon is a critically important element for the formation of all organic compounds, and thus is a nutritional requirement not only for the growth and division of C. glutamicum, but also for the overproduction of fine chemicals from this microorganism. Sugars, such as mono-, di-, or polysaccharides, are particularly good carbon sources, and thus standard growth media typically contain one or more of: glucose, fructose, mannose, galactose, ribose, sorbose, ribulose, lactose, maltose, sucrose, raffmose, starch, or cellulose (Ullmann' s Encyclopedia of Industrial Chemistry (1987) vol. A9, "Enzymes", VCH: Weinheim). Alternatively, more complex forms of sugar may be utilized in the media, such as molasses, or other by-products of sugar refinement. Other compounds aside from the sugars may be used as alternate carbon sources, including alcohols (e.g., ethanol or methanol), alkanes, sugar alcohols, fatty acids, and organic acids (e.g., acetic acid or lactic acid). For a review of carbon sources and their utilization by microorganisms in culture, see: Ullman's Encyclopedia of Industrial Chemistry (1987) vol. A9, "Enzymes", VCH: Weinheim; Stoppok, E. and Buchholz, K. (1996) "Sugar-based raw materials for fermentation applications" in Biotechnology (Rehm, H.J. et al, eds.) vol. 6, VCH: Weinheim, p. 5-29; Rehm, H.J. (1980) Industrielle Mikrobiologie, Springer: Berlin; Bartholomew, W.H., and Reiman, H.B. (1979). Economics of Fermentation Processes, in: Peppier, H.J. and Perlman, D., eds. Microbial Technology 2 nd ed., vol. 2, chapter 18, Academic Press: New York; and Kockova-Kratachvilova, A. (1981) Characteristics of Industrial Microorganisms, in: Rehm, H.J. and Reed, G., eds. Handbook of Biotechnology, vol. 1, chapter 1, Verlag Chemie: Weinheim. After uptake, these energy-rich carbon molecules must be processed such that they are able to be degraded by one of the major sugar metabolic pathways. Such pathways lead directly to useful degradation products, such as ribose-5-phosphate and phosphoenolpyruvate, which may be subsequently converted to pyruvate. Three of the most important pathways in bacteria for sugar metabolism include the Embden- Meyerhoff-Pamas (EMP) pathway (also known as the glycolytic or fructose bisphosphate pathway), the hexosemonophosphate (HMP) pathway (also known as the pentose shunt or pentose phosphate pathway), and the Entner-Doudoroff (ED) pathway (for review, see Michal, G. (1999) Biochemical Pathways: An Atlas of Biochemistry and Molecular Biology, Wiley: New York, and Stryer, L. (1988) Biochemistry, Chapters 13-19, Freeman: New York, and references therein). The EMP pathway converts hexose molecules to pyruvate, and in the process produces 2 molecules of ATP and 2 molecules of NADH. Starting with glucose-1- phosphate (which may be either directly taken up from the medium, or alternatively may be generated from glycogen, starch, or cellulose), the glucose molecule is isomerized to fructose-6-phosphate, is phosphorylated, and split into two 3 -carbon molecules of glyceraldehyde-3 -phosphate. After dehydrogenation, phosphorylation, and successive rearrangements, pyruvate results. The HMP pathway converts glucose to reducing equivalents, such as NADPH, and produces pentose and tetrose compounds which are necessary as intermediates and precursors in a number of other metabolic pathways. In the HMP pathway, glucose-6- phosphate is converted to ribulose-5-phosphate by two successive dehydrogenase reactions (which also release two NADPH molecules), and a carboxylation step. Ribulose-5-phosphate may also be converted to xyulose-5 -phosphate and ribose-5- phosphate; the former can undergo a series of biochemical steps to glucose-6-phosphate, which may enter the EMP pathway, while the latter is commonly utilized as an intermediate in other biosynthetic pathways within the cell. The ED pathway begins with the compound glucose or gluconate, which is subsequently phosphorylated and dehydrated to form 2-dehydro-3-deoxy-6-P-gluconate. Glucuronate and galacturonate may also be converted to 2-dehydro-3-deoxy-6-P- gluconate through more complex biochemical pathways. This product molecule is subsequently cleaved into glyceraldehyde-3 -P and pyruvate; glyceraldehyde-3 -P may itself also be converted to pyruvate. The EMP and HMP pathways share many features, including intermediates and enzymes. The EMP pathway provides the greatest amount of ATP, but it does not produce ribose-5-phosphate, an important precursor for, e.g., nucleic acid biosynthesis, nor does it produce erythrose-4-phosphate, which is important for amino acid biosynthesis. Microorganisms that are capable of using only the EMP pathway for glucose utilization are thus not able to grow on simple media with glucose as the sole carbon source. They are referred to as fastidious organisms, and their growth requires inputs of complex organic compounds, such as those found in yeast extract. In contrast, the HMP pathway produces all of the precursors necessary for both nucleic acid and amino acid biosynthesis, yet yields only half the amount of ATP energy that the EMP pathway does. The HMP pathway also produces NADPH, which may be used for redox reactions in biosynthetic pathways. The HMP pathway does not directly produce pyruvate, however, and thus these microorganisms must also possess this portion of the EMP pathway. It is therefore not surprising that a number of microorganisms, particularly the facultative anerobes, have evolved such that they possess both of these pathways. The ED pathway has thus far has only been found in bacteria. Although this pathway is linked partly to the HMP pathway in the reverse direction for precursor formation, the ED pathway directly forms pyruvate by the aldolase cleavage of 3- ketodeoxy-6-phosphogluconate. The ED pathway can exist on its own and is utilized by the majority of strictly aerobic microorganisms. The net result is similar to that of the HMP pathway, although one mole of ATP can be formed only if the carbon atoms are converted into pyruvate, instead of into precursor molecules. The pyruvate molecules produced through any of these pathways can be readily converted into energy via the Krebs cycle (also known as the citric acid cycle, the citrate cycle, or the tricarboxylic acid cycle (TCA cycle)). In this process, pyruvate is first decarboxylated, resulting in the production of one molecule of NADH, 1 molecule of acetyl-CoA, and 1 molecule of CO . The acetyl group of acetyl Co A then reacts with the 4 carbon unit, oxaolacetate, leading to the formation of citric acid, a 6 carbon organic acid. Dehydration and two additional CO 2 molecules are released. Ultimately, oxaloacetate is regenerated and can serve again as an acetyl acceptor, thus completing the cycle. The electrons released during the oxidation of intermediates in the TC A cycle are transferred to NAD + to yield NADH. During respiration, the electrons from NADH are transferred to molecular oxygen or other terminal electron acceptors. This process is catalyzed by the respiratory chain, an electron transport system containing both integral membrane proteins and membrane associated proteins. This system serves two basic functions: first, to accept electrons from an electron donor and to transfer them to an electron acceptor, and second, to conserve some of the energy released during electron transfer by the synthesis of ATP. Several types of oxidation-reduction enzymes and electron transport proteins are known to be involved in such processes, including the NADH dehydrogenases, flavin-containing electron carriers, iron sulfur proteins, and cytochromes. The NADH dehydrogenases are located at the cytoplasmic surface of the plasma membrane, and transfer hydrogen atoms from NADH to flavoproteins, in turn accepting electrons from NADH. The flavoproteins are a group of electron carriers possessing a flavin prosthetic group which is alternately reduced and oxidized as it accepts and transfers electrons. Three flavins are known to participate in these reactions: riboflavin, flavin-adenine dinucleotide (FAD) and flavin-mononucleotide (FMN). Iron sulfur proteins contain a cluster of iron and sulfur atoms which are not bonded to a heme group, but which still are able to participate in dehydration and rehydration reactions. Succinate dehydrogenase and aconitase are exemplary iron-sulfur proteins; their iron-sulfur complexes serve to accept and transfer electrons as part of the overall electron-transport chain. The cytochromes are proteins containing an iron porphyrin ring (heme). There are a number of different classes of cytochromes, differing in their reduction potentials. Functionally, these cytochromes form pathways in which electrons may be transferred to other cytochromes having increasingly more positive reduction potentials. A further class of non-protein electron carriers is known: the lipid-soluble quinones (e.g., coenzyme Q). These molecules also serve as hydrogen atom acceptors and electron donors. The action of the respiratory chain generates a proton gradient across the cell membrane, resulting in proton motive force. This force is utilized by the cell to synthesize ATP, via the membrane-spanning enzyme, ATP synthase. This enzyme is a multiprotein complex in which the transport of H + molecules through the membrane results in the physical rotation of the intracellular subunits and concomitant phosphorylation of ADP to form ATP (for review, see Fillingame, R.H. and Divall, S. (1999) Novartis Found. Symp. 221 : 218-229, 229-234). Non-hexose carbon substrates may also serve as carbon and energy sources for cells. Such substrates may first be converted to hexose sugars in the gluconeogenesis pathway, where glucose is first synthesized by the cell and then is degraded to produce energy. The starting material for this reaction is phosphoenolpyruvate (PEP), which is one of the key intermediates in the glycolytic pathway. PEP may be formed from substrates other than sugars, such as acetic acid, or by decarboxylation of oxaloacetate (itself an intermediate in the TCA cycle). By reversing the glycolytic pathway (utilizing a cascade of enzymes different than those of the original glycolysis pathway), glucose-6- phosphate may be formed. The conversion of pyruvate to glucose requires the utilization of 6 high energy phosphate bonds, whereas glycolysis only produces 2 ATP in the conversion of glucose to pyruvate. However, the complete oxidation of glucose (glycolysis, conversion of pyruvate into acetyl CoA, citric acid cycle, and oxidative phosphorylation) yields between 36-38 ATP, so the net loss of high energy phosphate bonds experienced during gluconeogenesis is offset by the overall greater gain in such high-energy molecules produced by the oxidation of glucose. 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 SMP nucleic acid and protein molecules, which participate in the conversion of sugars to useful degradation products and energy (e.g., ATP) in C. glutamicum or which may participate in the production of useful energy-rich molecules (e.g., ATP) by other processes, such as oxidative phosphorylation. In one embodiment, the SMP molecules participate in the metabolism of carbon compounds such as sugars or the generation of energy molecules (e.g., ATP) by processes such as oxidative phosphorylation in Corynebacterium glutamicum. In a preferred embodiment, the activity of the SMP molecules of the present invention to contribute to carbon metabolism or energy production in C. glutamicum has an impact on the production of a desired fine chemical by this organism. In a particularly preferred embodiment, the SMP molecules of the invention are modulated in activity, such that the C. glutamicum metabolic and energetic pathways in which the SMP proteins of the invention participate are modulated in yield, production, and/or efficiency of production, which either directly or indirectly modulates the yield, production, and/or efficiency of production of a desired fine chemical by C. glutamicum. The language, "SMP protein" or "SMP polypeptide" includes proteins which are capable of performing a function involved in the metabolism of carbon compounds such as sugars and the generation of energy molecules by processes such as oxidative phosphorylation in Corynebacterium glutamicum. Examples of SMP proteins include those encoded by the SMP genes set forth in Table 1 and by the odd-numbered SEQ ID NOs. The terms "SMP gene" or "SMP nucleic acid sequence" include nucleic acid sequences encoding an SMP protein, which consist of a coding region and also corresponding untranslated 5' and 3' sequence regions. Examples of SMP 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 term "degradation product" is art- recognized and includes breakdown products of a compound. Such products may themselves have utility as precursor (starting point) or intermediate molecules necessary for the biosynthesis of other compounds by the cell. 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. In another embodiment, the SMP 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 SMP protein of the invention may directly affect the yield, production, and/or efficiency of production of a fine chemical from a C. glutamicum strain incoφorating such an altered protein. The degradation of high-energy carbon molecules such as sugars, and the conversion of compounds such as NADH and F ADH to more useful forms via oxidative phosphorylation results in a number of compounds which themselves may be desirable fine chemicals, such as pyruvate, ATP, NADH, and a number of intermediate sugar compounds. Further, the energy molecules (such as ATP) and the reducing equivalents (such as NADH or NADPH) produced by these metabolic pathways are utilized in the cell to drive reactions which would otherwise be energetically unfavorable. Such unfavorable reactions include many biosynthetic pathways for fine chemicals. By improving the ability of the cell to utilize a particular sugar (e.g., by manipulating the genes encoding enzymes involved in the degradation and conversion of that sugar into energy for the cell), one may increase the amount of energy available to permit unfavorable, yet desired metabolic reactions (e.g., the biosynthesis of a desired fine chemical) to occur. The mutagenesis of one or more SMP genes of the invention may also result in SMP proteins having altered activities which indirectly impact the production of one or more desired fine chemicals from C. glutamicum. For example, by increasing the efficiency of utilization of one or more sugars (such that the conversion of the sugar to useful energy molecules is improved), or by increasing the efficiency of conversion of reducing equivalents to useful energy molecules (e.g., by improving the efficiency of oxidative phosphorylation, or the activity of the ATP synthase), one can increase the amount of these high-energy compounds available to the cell to drive normally unfavorable metabolic processes. These processes include the construction of cell walls, transcription, translation, and the biosynthesis of compounds necessary for growth and division of the cells (e.g., nucleotides, amino acids, vitamins, lipids, etc.) (Lengeler et al. (1999) Biology of Prokaryotes, Thieme Verlag: Stuttgart, p. 88-109; 913-918; 875-899). By improving the growth and multiplication of these engineered cells, it is possible to increase both the viability of the cells in large-scale culture, and also to improve their rate of division, such that a relatively larger number of cells can survive in fermentor culture. The yield, production, or efficiency of production may be increased, at least due to the presence of a greater number of viable cells, each producing the desired fine chemical. Further, a number of the degradation and intermediate compounds produced during sugar metabolism are necessary precursors and intermediates for other biosynthetic pathways throughout the cell. For example, many amino acids are synthesized directly from compounds normally resulting from glycolysis or the TCA cycle (e.g., serine is synthesized from 3-phosphoglycerate, an intermediate in glycolysis). Thus, by increasing the efficiency of conversion of sugars to useful energy molecules, it is also possible to increase the amount of useful degradation products as well. 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 SMP DNAs and the predicted amino acid sequences of the C. glutamicum SMP proteins are shown in the Sequence Listing as odd-numbered SEQ ID NOs and even-numbered SEQ ID NOs, respectively. Computational analyses were performed which classified and/or identified these nucleotide sequences as sequences which encode proteins having a function involved in the metabolism of carbon compounds such as sugars or in the generation of energy molecules by processes such as oxidative phosphorylation in Corynebacterium glutamicum. The present invention also pertains to proteins which have an amino acid sequence which is substantially homologous to an amino acid sequence of the invention (e.g, the sequence of an even-numbered SEQ ID NO of the Sequence Listing). 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. An SMP protein or a biologically active portion or fragment thereof of the invention can participate in the metabolism of carbon compounds such as sugars or in the generation of energy molecules (e.g., ATP) by processes such as oxidative phosphorylation in Corynebacterium glutamicum, or can 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 SMP 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 SMP-encoding nucleic acid (e.g., SMP 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 SMP nucleic acid molecule can contain less than about 5 kb, 4kb, 3kb, 2kb, 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 an odd-numbered SEQ ID NO of the Sequence Listing, or a portion thereof, can be isolated using standard molecular biology techniques and the sequence information provided herein. For example, a C. glutamicum SMP DNA can be isolated from a C. glutamicum library using all or portion of one of the odd-numbered SEQ ID NO sequences of the Sequence Listing 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, NY, 1989). Moreover, a nucleic acid molecule encompassing all or a portion of one of the nucleic acid sequences of the invention (e.g., an odd-numbered SEQ ID NO:) 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 nucleic acid sequences of the invention (e.g., an odd-numbered SEQ ID NO of the Sequence Listing) can be isolated by the polymerase chain reaction using oligonucleotide primers designed based upon this same sequence). 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, FL). Synthetic oligonucleotide primers for polymerase chain reaction amplification can be designed based upon one of the nucleotide sequences shown in the Sequence Listing. 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 SMP 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 the Sequence Listing. The nucleic acid sequences of the invention, as set forth in the Sequence Listing , correspond to the Corynebacterium glutamicum SMP DNAs of the invention. This DNA comprises sequences encoding SMP proteins (i.e., the "coding region", indicated in each odd- numbered SEQ ID NO: sequence in the Sequence Listing), as well as 5' untranslated sequences and 3' untranslated sequences, also indicated in each odd-numbered SEQ ID NO: in the Sequence Listing.. Alternatively, the nucleic acid molecule can comprise only the coding region of any of the sequences in nucleic acid sequences of the Sequence Listing. For the purposes of this application, it will be understood that each of the nucleic acid and amino acid sequences set forth in the Sequence Listing has an identifying RXA, RXN, or RXS number having the designation "RXA," "RXN," or "RXS" followed by 5 digits (i.e., RXA01626, RXN00043, or RXS0735). Each of the nucleic acid 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, or RXS designation to eliminate confusion. The recitation "one of the odd-numbered sequences of the Sequence Listing", then, refers to any of the nucleic acid sequences in the Sequence Listing, which may also be distinguished by their differing RXA, RXN, or RXS designations. The coding region of each of these sequences is translated into a corresponding amino acid sequence, which is also set forth in the Sequence Listing, as an even-numbered SEQ ID NO: immediately following the corresponding nucleic acid sequence . For example, the coding region for RXA02735 is set forth in SEQ ID NO:l, while the amino acid sequence which it encodes is set forth as SEQ ID NO:2. The sequences of the nucleic acid molecules of the invention are identified by the same RXA, RXN, or RXS designations as the amino acid molecules which they encode, such that they can be readily correlated. For example, the amino acid sequence designated RXA00042 is a translation of the coding region of the nucleotide sequence of nucleic acid molecule RXA00042, and the amino acid sequence designated RXN00043 is a translation of the coding region of the nucleotide sequence of nucleic acid molecule RXN00043. The correspondence between the RXA, RXN and RXS nucleotide and amino acid sequences of the invention and their assigned SEQ ID NOs is set forth 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 RXAdesignation. For example, SEQ ID NO:l 1, designated, as indicated on Table 1, as "F RXA01312", is an F-designated gene, as are SEQ ID NOs: 29, 33, and 39 (designated on Table 1 as "F RXA02803", "F RXA02854", and "F RXA01365", 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 of the invention (e.g., a sequence of an odd-numbered SEQ ID NO: of the Sequence Listing), or a portion thereof A nucleic acid molecule which is complementary to one of the nucleotide sequences of the invention is one which is sufficiently complementary to one of the nucleotide sequences shown in the Sequence Listing (e.g., the sequence of an odd-numbered SEQ ID NO:) such that it can hybridize to one of the nucleotide sequences of the invention, 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 of the invention (e.g., a sequence of an odd-numbered SEQ ID NO: of the Sequence Listing), 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 of the invention, or a portion thereof. Moreover, the nucleic acid molecule of the invention can comprise only a portion of the coding region of the sequence of one of the odd-numbered SEQ ID NOs of the Sequence Listing, for example a fragment which can be used as a probe or primer or a fragment encoding a biologically active portion of an SMP protein. The nucleotide sequences determined from the cloning of the SMP genes from C. glutamicum allows for the generation of probes and primers designed for use in identifying and/or cloning SMP homologues in other cell types and organisms, as well as SMP 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 nucleotide sequences of the invention (e.g., a sequence of one of the odd-numbered SEQ ID NOs of the Sequence Listing), an anti-sense sequence of one of these sequences, or naturally occurring mutants thereof. Primers based on a nucleotide sequence of the invention can be used in PCR reactions to clone SMP homologues. Probes based on the SMP 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 SMP protein, such as by measuring a level of an SMP-encoding nucleic acid in a sample of cells, e.g., detecting SMP mRNA levels or determining whether a genomic SMP 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 the invention (e.g. , a sequence of an even- numbered SEQ ID NO of the Sequence Listing) such that the protein or portion thereof maintains the ability to perform a function involved in the metabolism of carbon compounds such as sugars or in the generation of energy molecules (e.g., ATP) by processes such as oxidative phosphorylation in Corynebacterium glutamicum. 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 a sequence of one of the even-numbered SEQ ID NOs of the Sequence Listing) amino acid residues to an amino acid sequence of the invention such that the protein or portion thereof is able to perform a function involved in the metabolism of carbon compounds such as sugars or in the generation of energy molecules (e.g., ATP) by processes such as oxidative phosphorylation in Corynebacterium glutamicum. Protein members of such sugar metabolic pathways or energy producing systems, 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 SMP protein" contributes either directly or indirectly to the yield, production, and/or efficiency of production of one or more fine chemicals. Examples of SMP 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 the invention(e.g. , a sequence of an even-numbered SEQ ID NO: of the Sequence Listing). Portions of proteins encoded by the SMP nucleic acid molecules of the invention are preferably biologically active portions of one of the SMP proteins. As used herein, the term "biologically active portion of an SMP protein" is intended to include a portion, e.g., a domain/motif, of an SMP protein that participates in the metabolism of carbon compounds such as sugars, or in energy-generating pathways in C. glutamicum, or has an activity as set forth in Table 1. To determine whether an SMP protein or a biologically active portion thereof can participate in the metabolism of carbon compounds or in the production of energy-rich molecules in C. glutamicum, 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 SMP protein can be prepared by isolating a portion of one of the amino acid sequences of the invention (e.g., a sequence of an even-numbered SEQ ID NO: of the Sequence Listing), expressing the encoded portion of the SMP protein or peptide (e.g. , by recombinant expression in vitro) and assessing the activity of the encoded portion of the SMP protein or peptide. The invention further encompasses nucleic acid molecules that differ from one of the nucleotide sequences of the invention (e.g., a sequence of an odd-numbered SEQ ID NO: of the Sequence Listing) (and portions thereof) due to degeneracy of the genetic code and thus encode the same SMP protein as that encoded by the nucleotide sequences of the invention. 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 the Sequence Listing (e.g., an even-numbered SEQ ID NO:). 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 of the invention (encoded by an open reading frame shown in an odd-numbered SEQ ID NO: of the Sequence Listing). 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 58% identical to the nucleotide sequence designated RXA00014 (SEQ ID NO:41), a nucleotide sequence which is greater than and/or at least %> identical to the nucleotide sequence designated RXA00195 (SEQ ID NO:399), and a nucleotide sequence which is greater than and/or at least 42% identical to the nucleotide sequence designated RXA00196 (SEQ ID NO:401). 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%o, 99%) or more identical) are also encompassed by the invention. In addition to the C. glutamicum SMP nucleotide sequences set forth in the Sequence Listing as odd-numbered SEQ ID NOs, it will be appreciated by those of ordinary skill in the art that DNA sequence polymoφhisms that lead to changes in the amino acid sequences of SMP proteins may exist within a population (e.g., the C. glutamicum population). Such genetic polymoφhism in the SMP 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 SMP protein, preferably a C. glutamicum SMP protein. Such natural variations can typically result in 1-5% variance in the nucleotide sequence of the SMP gene. Any and all such nucleotide variations and resulting amino acid polymoφhisms in SMP that are the result of natural variation and that do not alter the functional activity of SMP 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 SMP DNA of the invention can be isolated based on their homology to the C. glutamicum SMP 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 of an odd-numbered SEQ ID NO: of the Sequence Listing. 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 & Sons, N.Y. (1989), 6.3.1-6.3.6. A preferred, non-limiting example of stringent hybridization conditions are hybridization in 6X sodium chloride/sodium citrate (SSC) at about 45°C, followed by one or more washes in 0.2 X SSC, 0.1% SDS at 50-65°C. Preferably, an isolated nucleic acid molecule of the invention that hybridizes under stringent conditions to a nucleotide sequence of the invention 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 SMP protein. In addition to naturally-occurring variants of the SMP 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 the invention, thereby leading to changes in the amino acid sequence of the encoded SMP protein, without altering the functional ability of the SMP protein. For example, nucleotide substitutions leading to amino acid substitutions at "non-essential" amino acid residues can be made in a nucleotide sequence of the invention. A "non-essential" amino acid residue is a residue that can be altered from the wild-type sequence of one of the SMP proteins (e.g., an even-numbered SEQ ID NO: of the Sequence Listing) without altering the activity of said SMP protein, whereas an "essential" amino acid residue is required for SMP protein activity. Other amino acid residues, however, (e.g., those that are not conserved or only semi-conserved in the domain having SMP activity) may not be essential for activity and thus are likely to be amenable to alteration without altering SMP activity. Accordingly, another aspect of the invention pertains to nucleic acid molecules encoding SMP proteins that contain changes in amino acid residues that are not essential for SMP activity. Such SMP proteins differ in amino acid sequence from a sequence of an even-numbered SEQ ID NO: of the Sequence Listing yet retain at least one of the SMP 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 the invention and is capable of participate in the metabolism of carbon compounds such as sugars, or in the biosynthesis of high-energy compounds in C. glutamicum, or has one or more activities set forth in Table 1. Preferably, the protein encoded by the nucleic acid molecule is at least about 50-60% homologous to the amino acid sequence of one of the odd-numbered SEQ ID NOs of the Sequence Listing, more preferably at least about 60- 70% homologous to one of these sequences, even more preferably at least about 70- 80%, 80-90%), 90-95%) homologous to one of these sequences, and most preferably at least about 96%>, 97%, 98%, or 99% homologous to one of the amino acid sequences of the invention. To determine the percent homology of two amino acid sequences (e.g., one of the amino acid sequences of the invention and a mutant form thereof) or of two nucleic acids, the sequences are aligned for optimal comparison puφoses (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 amino acid sequences the invention) 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 amino acid sequence), 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 x 100). An isolated nucleic acid molecule encoding an SMP protein homologous to a protein sequence of the invention (e.g., a sequence of an even-numbered SEQ ID NO: of the Sequence Listing) can be created by introducing one or more nucleotide substitutions, additions or deletions into a nucleotide sequence of the invention 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 nucleotide sequences of the invention 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 SMP 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 SMP coding sequence, such as by saturation mutagenesis, and the resultant mutants can be screened for an SMP activity described herein to identify mutants that retain SMP activity. Following mutagenesis of the nucleotide sequence of one of the odd-numbered SEQ ID NOs of the Sequence Listing, 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 SMP 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 SMP 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 SMP 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 NO. 3 (RXA01626) comprises nucleotides 1 to 345). In another embodiment, the antisense nucleic acid molecule is antisense to a "noncoding region" of the coding strand of a nucleotide sequence encoding SMP. 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 SMP disclosed herein (e.g., the sequences set forth as odd-numbered SEQ ID NOs in the Sequence Listing), 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 SMP mRNA, but more preferably is an oligonucleotide which is antisense to only a portion of the coding or noncoding region of SMP mRNA. For example, the antisense oligonucleotide can be complementary to the region surrounding the translation start site of SMP 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-N6-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 SMP 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 β-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 SMP mRNA transcripts to thereby inhibit translation of SMP mRNA. A ribozyme having specificity for an SMP-encoding nucleic acid can be designed based upon the nucleotide sequence of an SMP cDNA disclosed herein (i. e. , SEQ ID NO. 3 (RXA01626)). 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 SMP-encoding mRNA. See, e.g., Cech et al. U.S. Patent No. 4,987,071 and Cech et al. U.S. Patent No. 5,116,742. Alternatively, SMP 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, SMP gene expression can be inhibited by targeting nucleotide sequences complementary to the regulatory region of an SMP nucleotide sequence (e.g., an SMP promoter and/or enhancers) to form triple helical structures that prevent transcription of an SMP 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 SMP 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 retro viruses, adeno viruses 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 is 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, CA (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-, tφ-, tet-, tφ-tet-, lpp-, lac-, lpp-lac-, lacl q -, T7-, T5-, T3-, gal-, trc-, ara-, SP6-, arny, SPO2, λ-P R - or λ P , 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, φ28, 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., SMP proteins, mutant forms of SMP proteins, fusion proteins, etc.). The recombinant expression vectors of the invention can be designed for expression of SMP proteins in prokaryotic or eukaryotic cells. For example, SMP 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 & L.L. Lasure, eds., p. 396-428: Academic Press: San Diego; and van den Hondel, C.A.M.J.J. & 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, CA (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 puφoses: 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 Ine; Smith, D.B. and Johnson, K.S. (1988) Gene 67:31-40), pMAL (New England Biolabs, Beverly, MA) and pRIT5 (Pharmacia, Piscataway, NJ) 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 SMP 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 SMP 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, pHSl, pHS2, pPLc236, pMBL24, pLG200, pUR290, pIN- III 113-B1, λgtl 1, pBdCl, and pET 1 Id (Studier et al, Gene Expression Technology: Methods in Enzymology 185, Academic Press, San Diego, California (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 tφ-lac fusion promoter. Target gene expression from the pET l id vector relies on transcription from a T7 gnlO-lac fusion promoter mediated by a coexpressed viral RNA polymerase (T7 gnl). This viral polymerase is supplied by host strains BL21 (DE3) or HMS 174(DE3) from a resident λ prophage harboring a T7 gnl 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 pIJlOl, pIJ364, pIJ702 and pIJ361 are known to be useful in transforming Streptomyces, while plasmids pUBl 10, pC194, or pBD214 are suited for transformation of Bacillus species. Several plasmids of use in the transfer of genetic information into Corynebacterium include pHM1519, pBLl, 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, California (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 SMP protein expression vector is a yeast expression vector. Examples of vectors for expression in yeast S. cerevisiae include pYepSecl (Baldari, et al, (1987) Embo J. 6:229-234), 2 μ, pAG-1, Yep6, Yepl3, pEMBLYe23, pMFa (Kurjan and Herskowitz, (1982) Cell 30:933-943), pJRY88 (Schultz et al, (1987) Gene 54:113-123), and pYES2 (Invitrogen Coφoration, San Diego, CA). 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. & 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 SMP 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 SMP 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'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. 2nd, ed., Cold Spring Harbor Laboratory, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, 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 (Banerji 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. Patent 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 SMP 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 SMP 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 one 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. 2nd, ed., Cold Spring Harbor Laboratory, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, 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 SMP 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 incoφorated 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 SMP gene into which a deletion, addition or substitution has been introduced to thereby alter, e.g., functionally disrupt, the SMP gene. Preferably, this SMP gene is a Corynebacterium glutamicum SMP 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 SMP gene is functionally disrupted (/. 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 SMP 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 SMP protein). In the homologous recombination vector, the altered portion of the SMP gene is flanked at its 5' and 3' ends by additional nucleic acid of the SMP gene to allow for homologous recombination to occur between the exogenous SMP gene carried by the vector and an endogenous SMP gene in a microorganism. The additional flanking SMP 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 SMP gene has homologously recombined with the endogenous SMP 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 SMP gene on a vector placing it under control of the lac operon permits expression of the SMP gene only in the presence of IPTG. Such regulatory systems are well known in the art. In another embodiment, an endogenous SMP 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 SMP gene in a host cell has been altered by one or more point mutations, deletions, or inversions, but still encodes a functional SMP protein. In still another embodiment, one or more of the regulatory regions (e.g., a promoter, repressor, or inducer) of an SMP gene in a microorganism has been altered (e.g., by deletion, truncation, inversion, or point mutation) such that the expression of the SMP gene is modulated. One of ordinary skill in the art will appreciate that host cells containing more than one of the described SMP 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 SMP protein. Accordingly, the invention further provides methods for producing SMP 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 SMP protein has been introduced, or into which genome has been introduced a gene encoding a wild-type or altered SMP protein) in a suitable medium until SMP protein is produced. In another embodiment, the method further comprises isolating SMP proteins from the medium or the host cell. C. Isolated SMP Proteins Another aspect of the invention pertains to isolated SMP 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 SMP 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 SMP protein having less than about 30% (by dry weight) of non-SMP protein (also referred to herein as a "contaminating protein"), more preferably less than about 20%> of non-SMP protein, still more preferably less than about 10%> of non-SMP protein, and most preferably less than about 5% non-SMP protein. When the SMP 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 SMP 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 SMP protein having less than about 30%> (by dry weight) of chemical precursors or non-SMP chemicals, more preferably less than about 20%) chemical precursors or non-SMP chemicals, still more preferably less than about 10% chemical precursors or non-SMP chemicals, and most preferably less than about 5% chemical precursors or non-SMP chemicals. In preferred embodiments, isolated proteins or biologically active portions thereof lack contaminating proteins from the same organism from which the SMP protein is derived. Typically, such proteins are produced by recombinant expression of, for example, a C. glutamicum SMP protein in a microorganism such as C. glutamicum. An isolated SMP protein or a portion thereof of the invention can participate in the metabolism of carbon compounds such as sugars, or in the production of energy compounds (e.g., by oxidative phosphorylation) utilized to drive unfavorable metabolic pathways, 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 the invention (e.g., a sequence of an even-numbered SEQ ID NO: of the Sequence Listing) such that the protein or portion thereof maintains the ability to perform a function involved in the metabolism of carbon compounds such as sugars or in the generation of energy molecules by processes such as oxidative phosphorylation in Corynebacterium glutamicum. The portion of the protein is preferably a biologically active portion as described herein. In another preferred embodiment, an SMP protein of the invention has an amino acid sequence set forth as an even-numbered SEQ ID NO: of the Sequence Listing. In yet another preferred embodiment, the SMP 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 the invention (e.g., a sequence of an odd-numbered SEQ ID NO: of the Sequence Listing). In still another preferred embodiment, the SMP 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 the invention, 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 ofany of the above values recited as upper and/or lower limits are intended to be included. The preferred SMP proteins of the present invention also preferably possess at least one of the SMP activities described herein. For example, a preferred SMP 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 the invention, and which can perform a function involved in the metabolism of carbon compounds such as sugars or in the generation of energy molecules (e.g., ATP) by processes such as oxidative phosphorylation in Corynebacterium glutamicum, or which has one or more of the activities set forth in Table 1. In other embodiments, the SMP protein is substantially homologous to an amino acid sequence of of the invention (e.g., a sequence of an even-numbered SEQ ID NO: of the Sequence Listing)and retains the functional activity of the protein of one of the amino acid sequences of the invention 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 SMP 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%o, 97%, 98%, 99% or more homologous to an entire amino acid sequence of the invention and which has at least one of the SMP 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 the invention. Biologically active portions of an SMP protein include peptides comprising amino acid sequences derived from the amino acid sequence of an SMP protein, e.g., an amino acid sequence of an even-numbered SEQ ID NO: of the Sequence Listing or the amino acid sequence of a protein homologous to an SMP protein, which include fewer amino acids than a full length SMP protein or the full length protein which is homologous to an SMP protein, and exhibit at least one activity of an SMP 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 SMP 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 SMP protein include one or more selected domains/motifs or portions thereof having biological activity. SMP 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 SMP protein is expressed in the host cell. The SMP protein can then be isolated from the cells by an appropriate purification scheme using standard protein purification techniques. Alternative to recombinant expression, an SMP protein, polypeptide, or peptide can be synthesized chemically using standard peptide synthesis techniques. Moreover, native SMP protein can be isolated from cells (e.g., endothelial cells), for example using an anti-SMP antibody, which can be produced by standard techniques utilizing an SMP protein or fragment thereof of this invention. The invention also provides SMP chimeric or fusion proteins. As used herein, an SMP "chimeric protein" or "fusion protein" comprises an SMP polypeptide operatively linked to a non-SMP polypeptide. An "SMP polypeptide" refers to a polypeptide having an amino acid sequence corresponding to an SMP protein, whereas a "non-SMP polypeptide" refers to a polypeptide having an amino acid sequence corresponding to a protein which is not substantially homologous to the SMP protein, e.g., a protein which is different from the SMP 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 SMP polypeptide and the non-SMP polypeptide are fused in-frame to each other. The non-SMP polypeptide can be fused to the N-terminus or C-terminus of the SMP polypeptide. For example, in one embodiment the fusion protein is a GST- SMP fusion protein in which the SMP sequences are fused to the C-terminus of the GST sequences. Such fusion proteins can facilitate the purification of recombinant SMP proteins. In another embodiment, the fusion protein is an SMP 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 SMP protein can be increased through use of a heterologous signal sequence. Preferably, an SMP 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, Ausubel et al, eds. John Wiley & Sons: 1992). Moreover, many expression vectors are commercially available that already encode a fusion moiety (e.g., a GST polypeptide). An SMP-encoding nucleic acid can be cloned into such an expression vector such that the fusion moiety is linked in-frame to the SMP protein. Homologues of the SMP protein can be generated by mutagenesis, e.g., discrete point mutation or truncation of the SMP protein. As used herein, the term "homologue" refers to a variant form of the SMP protein which acts as an agonist or antagonist of the activity of the SMP protein. An agonist of the SMP protein can retain substantially the same, or a subset, of the biological activities of the SMP protein. An antagonist of the SMP protein can inhibit one or more of the activities of the naturally occurring form of the SMP protein, by, for example, competitively binding to a downstream or upstream member of the sugar molecule metabolic cascade or the energy-producing pathway which includes the SMP protein. In an alternative embodiment, homologues of the SMP protein can be identified by screening combinatorial libraries of mutants, e.g., truncation mutants, of the SMP protein for SMP protein agonist or antagonist activity. In one embodiment, a variegated library of SMP variants is generated by combinatorial mutagenesis at the nucleic acid level and is encoded by a variegated gene library. A variegated library of SMP variants can be produced by, for example, enzymatically ligating a mixture of synthetic oligonucleotides into gene sequences such that a degenerate set of potential SMP sequences is expressible as individual polypeptides, or alternatively, as a set of larger fusion proteins (e.g., for phage display) containing the set of SMP sequences therein. There are a variety of methods which can be used to produce libraries of potential SMP 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 SMP 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 SMP protein coding can be used to generate a variegated population of SMP fragments for screening and subsequent selection of homologues of an SMP protein. In one embodiment, a library of coding sequence fragments can be generated by treating a double stranded PCR fragment of an SMP 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 S 1 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 SMP 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 SMP 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 SMP homologues (Arkin and Yourvan (1992) PNAS 59:7811-7815; Delgrave et al. (1993) Protein Engineering 6(3):327-331). In another embodiment, cell based assays can be exploited to analyze a variegated SMP 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 SMP protein regions required for function; modulation of an SMP protein activity; modulation of the metabolism of one or more sugars; modulation of high-energy molecule production in a cell (i. e. , ATP, NADPH); and modulation of cellular production of a desired compound, such as a fine chemical. The SMP 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 as odd-numbered or even-numbered SEQ ID NOs, respectively, in the Sequence Listing) 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 SMP nucleic acid molecules of the invention are also useful for evolutionary and protein structural studies. The metabolic and energy-releasing processes in which the molecules of the invention participate are utilized by a wide variety of prokaryotic and eukaryotic cells; 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 SMP nucleic acid molecules of the invention may result in the production of SMP proteins having functional differences from the wild-type SMP 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 SMP protein, either by interacting with the protein itself or a substrate or binding partner of the SMP protein, or by modulating the transcription or translation of an SMP nucleic acid molecule of the invention. In such methods, a microorganism expressing one or more SMP 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 SMP protein is assessed. There are a number of mechanisms by which the alteration of an SMP protein of the invention may directly affect the yield, production, and/or efficiency of production of a fine chemical from a C. glutamicum strain incoφorating such an altered protein. The degradation of high-energy carbon molecules such as sugars, and the conversion of compounds such as NADH and FADH 2 to more useful forms via oxidative phosphorylation results in a number of compounds which themselves may be desirable fine chemicals, such as pyruvate, ATP, NADH, and a number of intermediate sugar compounds. Further, the energy molecules (such as ATP) and the reducing equivalents (such as NADH or NADPH) produced by these metabolic pathways are utilized in the cell to drive reactions which would otherwise be energetically unfavorable. Such unfavorable reactions include many biosynthetic pathways for fine chemicals. By improving the ability of the cell to utilize a particular sugar (e.g., by manipulating the genes encoding enzymes involved in the degradation and conversion of that sugar into energy for the cell), one may increase the amount of energy available to permit unfavorable, yet desired metabolic reactions (e.g., the biosynthesis of a desired fine chemical) to occur. Further, modulation of one or more pathways involved in sugar utilization permits optimization of the conversion of the energy contained within the sugar molecule to the production of one or more desired fine chemicals. For example, by reducing the activity of enzymes involved in, for example, gluconeogenesis, more ATP is available to drive desired biochemical reactions (such as fine chemical biosyntheses) in the cell. Also, the overall production of energy molecules from sugars may be modulated to ensure that the cell maximizes its energy production from each sugar molecule. Inefficient sugar utilization can lead to excess CO 2 production and excess energy, which may result in futile metabolic cycles. By improving the metabolism of sugar molecules, the cell should be able to function more efficiently, with a need for fewer carbon molecules. This should result in an improved fine chemical product: sugar molecule ratio (improved carbon yield), and permits a decrease in the amount of sugars that must be added to the medium in large-scale fermentor culture of such engineered C. glutamicum. The mutagenesis of one or more SMP genes of the invention may also result in SMP proteins having altered activities which indirectly impact the production of one or more desired fine chemicals from C. glutamicum. For example, by increasing the efficiency of utilization of one or more sugars (such that the conversion of the sugar to useful energy molecules is improved), or by increasing the efficiency of conversion of reducing equivalents to useful energy molecules (e.g., by improving the efficiency of oxidative phosphorylation, or the activity of the ATP synthase), one can increase the amount of these high-energy compounds available to the cell to drive normally unfavorable metabolic processes. These processes include the construction of cell walls, transcription, translation, and the biosynthesis of compounds necessary for growth and division of the cells (e.g., nucleotides, amino acids, vitamins, lipids, etc.) (Lengeler et al. (1999) Biology of Prokaryotes, Thieme Verlag: Stuttgart, p. 88-109; 913-918; 875-899). By improving the growth and multiplication of these engineered cells, it is possible to increase both the viability of the cells in large-scale culture, and also to improve their rate of division, such that a relatively larger number of cells can survive in fermentor culture. The yield, production, or efficiency of production may be increased, at least due to the presence of a greater number of viable cells, each producing the desired fine chemical. Further, many of the degradation products produced during sugar metabolism are themselves utilized by the cell as precursors or intermediates for the production of a number of other useful compounds, some of which are fine chemicals. For example, pyruvate is converted into the amino acid alanine, and ribose-5-phosphate is an integral part of, for example, nucleotide molecules. The amount and efficiency of sugar metabolism, then, has a profound effect on the availability of these degradation products in the cell. By increasing the ability of the cell to process sugars, either in terms of efficiency of existing pathways (e.g., by engineering enzymes involved in these pathways such that they are optimized in activity), or by increasing the availability of the enzymes involved in such pathways (e.g., by increasing the number of these enzymes present in the cell), it is possible to also increase the availability of these degradation products in the cell, which should in turn increase the production of many different other desirable compounds in the cell (e.g., fine chemicals). The aforementioned mutagenesis strategies for SMP 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 incoφorating 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 SMP 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, and the sequence listing cited throughout this application are hereby incoφorated by reference. TABLE 1: GENES IN THE APPLICATION HMP: Nucleic Acid Ammo Acid Identification Code Contig NT Start NT Stop Function SEQ ID NO SEQ ID NO 1 2 RXS02735 W0074 14576 15280 6-Phosphoglucolactonase 3 4 RXA01626 GR00452 4270 3926 L-nbulose-phosphate 4-epιmerase 5 6 RXA02245 GR00654 13639 14295 RIBULOSE-PHOSPHATE 3-EPIMERASE (EC 5 1 3 1) 7 8 RXA01015 GR00290 346 5 RIBOSE 5-PHOSPHATE ISOMERASE (EC 5 3 1 6) TCA: Nucleic Acid Ammo Acid Identification Code Contig NT Start NT Stop Function SEQ ID NO SEQ ID NO 9 10 RXN01312 W0082 20803 18785 SUCCINATE DEHYDROGENASE FLAVOPROTEIN SUBUNIT (EC 1 3 99 1) 11 12 F RXA01312 GR00380 2690 1614 SUCCINATE DEHYDROGENASE FLAVOPROTEIN SUBUNIT (EC 1 3 99 1 ) 13 14 RXN00231 W0083 15484 14015 SUCCINATE-SEMIALDEHYDE DEHYDROGENASE (NADP+) (EC 12116) 15 16 RXA01311 GR00380 1611 865 SUCCINATE DEHYDROGENASE IRON-SULFUR PROTEIN (EC 13991) 17 18 RXA01535 GR00427 1354 2760 FUMARATE HYDRATASE PRECURSOR (EC 4212) 19 20 RXA00517 GR00131 1407 2447 MALATE DEHYDROGENASE (EC 11137) (EC 11182) 21 22 RXA01350 GR00392 1844 2827 MALATE DEHYDROGENASE (EC 11137) EMB-Pathway Identification Code Contig NT Start NT Stop Function 23 24 RXA02149 GR00639 17786 18754 GLUCOKINASE (EC 2 7 1 2) 25 26 RXA01814 GR00515 2571 910 PHOSPHOGLUCOMUTASE (EC 5422)/ PHOSPHOMANNOMUTASE (EC 54 2 8) 27 28 RXN02803 W0086 1 657 PHOSPHOGLUCOMUTASE (EC 5422)/ PHOSPHOMANNOMUTASE (EC 54 2 8) 29 30 F RXA02803 GR00784 2 400 PHOSPHOGLUCOMUTASE (EC 5422)/ PHOSPHOMANNOMUTASE (EC 5 4 2 8) 31 32 RXN03076 W0043 1624 35 PHOSPHOGLUCOMUTASE (EC 5422)/ PHOSPHOMANNOMUTASE (EC 54 2 8) 33 34 F RXA02854 GR10002 1588 5 PHOSPHOGLUCOMUTASE (EC 5422)/ PHOSPHOMANNOMUTASE (EC 5 4 2 8) 35 36 RXA00511 GR00129 1 513 PHOSPHOGLUCOMUTASE (EC 5422)/ PHOSPHOMANNOMUTASE (EC 5 4 2 8) Table 1 (continued) Nucleic Acid Ammo Acid Identification Code Contig NT Start NT Stop SEQ ID NO SEQ ID NO 37 38 RXN01365 W0091 1476 103 PHOSPHOGLUCOMUTASE (EC 5422) / PHOSPHOMANNOMUTASE (EC 5428) 39 40 F RXA01365 GR00397 897 4 PHOSPHOGLUCOMUTASE (EC 5422) / PHOSPHOMANNOMUTASE (EC 5428) 41 42 RXA00098 GR00014 6525 8144 GLUCOSE-6-PHOSPHATE ISOMERASE (GPI) (EC 5319) 43 44 RXA01989 GR00578 1 630 GLUCOSE-6-PHOSPHATE ISOMERASE A (GPI A) (EC 5319) 45 46 RXA00340 GR00059 1549 2694 PHOSPHOGLYCERATE MUTASE (EC 5421) 47 48 RXA02492 GR00720 2201 2917 PHOSPHOGLYCERATE MUTASE (EC 5421) 49 50 RXA00381 GR00082 1451 846 PHOSPHOGLYCERATE MUTASE (EC 5421) 51 52 RXA02122 GR00636 6511 5813 PHOSPHOGLYCERATE MUTASE (EC 5421) 53 54 RXA00206 GR00032 6171 5134 6-PHOSPHOFRUCTOKINASE (EC 27111) 55 56 RXA01243 GR00359 2302 3261 1-PHOSPHOFRUCTOKINASE (EC 27156) 57 58 RXA01882 GR00538 1165 2154 1-PHOSPHOFRUCTOKINASE (EC 27156) 59 60 RXA01702 GR00479 1397 366 FRUCTOSE-BISPHOSPHATE ALDOLASE (EC 41213) 61 62 RXA02258 GR00654 26451 27227 TRIOSEPHOSPHATE ISOMERASE (EC 5311) 63 64 RXN01225 W0064 6382 4943 GLYCERALDEHYDE 3-PHOSPHATE DEHYDROGENASE (EC 12112) 65 66 F RXA01225 GR00354 5302 6741 GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE HOMOLOG 67 68 RXA02256 GR00654 23934 24935 GLYCERALDEHYDE 3-PHOSPHATE DEHYDROGENASE (EC 12112) 69 70 RXA02257 GR00654 25155 26369 PHOSPHOGLYCERATE KINASE (EC 2723) 71 72 RXA00235 GR00036 2365 1091 ENOLASE (EC 42111) 73 74 RXA01093 GR00306 1552 122 PYRUVATE KINASE (EC 27140) 75 76 RXN02675 W0098 72801 70945 PYRUVATE KINASE (EC 27140) 77 78 F RXA02675 GR00754 2 364 PYRUVATE KINASE (EC 27140) 79 80 F RXA02695 GR00755 2949 4370 PYRUVATE KINASE (EC 27140) 81 82 RXA00682 GR00179 5299 3401 PHOSPHOENOLPYRUVATE SYNTHASE (EC 2792) 83 84 RXA00683 GR00179 6440 5349 PHOSPHOENOLPYRUVATE SYNTHASE (EC 2792) 85 86 RXN00635 W0135 22708 20972 PYRUVATE DEHYDROGENASE (CYTOCHROME) (EC 1222) 87 88 F RXA02807 GR00788 88 552 PYRUVATE DEHYDROGENASE (CYTOCHROME) (EC 1222) 89 90 F RXA00635 GR00167 3 923 PYRUVATE DEHYDROGENASE (CYTOCHROME) (EC 1222) 91 92 RXN03044 W0019 1391 2221 PYRUVATE DEHYDROGENASE E1 COMPONENT (EC 1241) 93 94 F RXA02852 GR00852 3 281 PYRUVATE DEHYDROGENASE E1 COMPONENT (EC 1241) 95 96 F RXA00268 GR00041 125 955 PYRUVATE DEHYDROGENASE E1 COMPONENT (EC 1241) 97 98 RXN03086 W0049 2243 2650 PYRUVATE DEHYDROGENASE E1 COMPONENT (EC 1241) 99 100 F RXA02887 GR10022 411 4 PYRUVATE DEHYDROGENASE E1 COMPONENT (EC 1241) 101 102 RXN03043 W0019 1 1362 PYRUVATE DEHYDROGENASE E1 COMPONENT (EC 1241) 103 104 F RXA02897 GR10039 1291 5 PYRUVATE DEHYDROGENASE E1 COMPONENT (EC 1241) 105 106 RXN03083 W0047 88 1110 DIHYDROLIPOAMIDE DEHYDROGENASE (EC 1814) 107 108 F RXA02853 GR10001 89 1495 DIHYDROLIPOAMIDE DEHYDROGENASE (EC 1814) 109 110 RXA02259 GR00654 27401 30172 PHOSPHOENOLPYRUVATE CARBOXYLASE (EC 41131) 111 112 RXN02326 W0047 4500 5315 PYRUVATE CARBOXYLASE (EC 6411) 113 114 F RXA02326 GR00668 5338 4523 PYRUVATE CARBOXYLASE 115 116 RXN02327 W0047 3533 4492 PYRUVATE CARBOXYLASE (EC 6411) 117 118 F RXA02327 GR00668 6305 5346 PYRUVATE CARBOXYLASE 119 120 RXN02328 W0047 1842 3437 PYRUVATE CARBOXYLASE (EC 6411) 121 122 F RXA02328 GR00668 7783 6401 PYRUVATE CARBOXYLASE (EC 6411) 123 124 RXN01048 W0079 12539 11316 MALIC ENZYME (EC 11139) Table 1 (continued) Nucleic Acid Ammo Acid Identification Code Contig NT Start NT Stop Function SEQ ID NO SEQ ID NO 125 126 F RXA01048 GR00296 3 290 MALIC ENZYME (EC 1 1 1 39) 127 128 F RXA00290 GR00046 4693 5655 MALIC ENZYME (EC 1 1 1 39) 129 130 RXA02694 GR00755 1879 2820 L-LACTATE DEHYDROGENASE (EC 1 1 1 27) 131 132 RXN00296 W0176 35763 38606 D-LACTATE DEHYDROGENASE (CYTOCHROME) (EC 1 1 2 4) 133 134 F RXA00296 GR00048 3 2837 D-LACTATE DEHYDROGENASE (CYTOCHROME) (EC 1 1 2 4) 135 136 RXA01901 GR00544 4158 5417 L-LACTATE DEHYDROGENASE (CYTOCHROME) (EC 1 1 2 3) 137 138 RXN01952 W0105 9954 11666 D-LACTATE DEHYDROGENASE (EC 1 1 1 28) 139 140 F RXA01952 GR00562 1 216 D-LACTATE DEHYDROGENASE (EC 1 1 1 28) 141 142 F RXA01955 GR00562 4611 6209 D-LACTATE DEHYDROGENASE (EC 1 1 1 28) 143 144 RXA00293 GR00047 2645 1734 D-3-PHOSPHOGLYCERATE DEHYDROGENASE (EC 1 1 1 95) 145 146 RXN01130 W0157 6138 5536 D-3-PHOSPHOGLYCERATE DEHYDROGENASE (EC 1 1 1 95) 147 148 F RXA01130 GR00315 2 304 D-3-PHOSPHOGLYCERATE DEHYDROGENASE (EC 1 1 1 95) 149 150 RXN03112 W0085 509 6 D-3-PHOSPHOGLYCERATE DEHYDROGENASE (EC 1 1 1 95) 151 152 F RXA01133 GR00316 568 1116 D-3-PHOSPHOGLYCERATE DEHYDROGENASE (EC 1 1 1 95) 153 154 RXN00871 W0127 3127 2240 IOLB PROTEIN 155 156 F RXA00871 GR00239 2344 3207 IOLB PROTEIN D-FRUCTOSE 1 ,6-BISPHOSPHATE = GLYCERONE-CC PHOSPHATE + D- GLYCERALDEHYDE 3-PHOSPHATE 157 158 RXN02829 W0354 287 559 IOLS PROTEIN 159 160 F RXA02829 GR00816 287 562 IOLS PROTEIN 161 162 RXN01468 W0019 7474 8298 NAGD PROTEIN 163 164 F RXA01468 GR00422 1250 2074 PUTATIVE N-GLYCERALDEHYDE-2-PHOSPHOTRANSFERASE 165 166 RXA00794 GR00211 3993 2989 GLPX PROTEIN 167 168 RXN02920 W0213 6135 5224 D-3-PHOSPHOGLYCERATE DEHYDROGENASE (EC 1 1 1 95) 169 170 F RXA02379 GR00690 1390 686 D-3-PHOSPHOGLYCERATE DEHYDROGENASE (EC 1 1 1 95) 171 172 RXN02688 W0098 59053 58385 PHOSPHOGLYCERATE MUTASE (EC 5 4 2 1) 173 174 RXN03087 W0052 3216 3428 PYRUVATE CARBOXYLASE (EC 6 4 1 1 ) 175 176 RXN03186 W0377 310 519 PYRUVATE DEHYDROGENASE E1 COMPONENT (EC 1 2 4 1) 177 178 RXN03187 W0382 3 281 PYRUVATE DEHYDROGENASE E1 COMPONENT (EC 1 2 4 1 ) 179 180 RXN02591 W0098 14370 12541 PHOSPHOENOLPYRUVATE CARBOXYKINASE [GTP] (EC 4 1 1 32) 181 182 RXS01260 W0009 3477 2296 LIPOAMIDE DEHYDROGENASE COMPONENT (E3) OF BRANCHED- CHAIN ALPHA-KETO ACID DEHYDROGENASE COMPLEX (EC 1 8 1 4) 183 184 RXS01261 W0009 3703 3533 LIPOAMIDE DEHYDROGENASE COMPONENT (E3) OF BRANCHED- CHAIN ALPHA-KETO ACID DEHYDROGENASE COMPLEX (EC 1 8 1 4) Glycerol metabolism Nucleic Acid Ammo Acid Identification Code Contig NT Start NT Stop Function SEQ ID NO SEQ ID NO 185 186 RXA02640 GR00749 1400 2926 GLYCEROL KINASE (EC 2 7 1 30) 187 188 RXN01025 W0143 5483 4488 GLYCEROL-3-PHOSPHATE DEHYDROGENASE (NAD(P)+) (EC 1 1 1 94) 189 190 F RXA01025 GR00293 939 1853 GLYCEROL-3-PHOSPHATE DEHYDROGENASE (NAD(P)+) (EC 1 1 1 94) 191 192 RXA01851 GR00525 3515 1830 AEROBIC GLYCEROL-3-PHOSPHATE DEHYDROGENASE (EC 1 1 99 5) 193 194 RXA01242 GR00359 1526 2302 GLYCEROL-3-PHOSPHATE REGULON REPRESSOR 195 196 RXA02288 GR00661 992 147 GLYCEROL-3-PHOSPHATE REGULON REPRESSOR Table 1 (continued) Nucleic Acid Ammo Acid Identification Code Contig NT Start NT Stop Function SEQ ID NO SEQ ID NO 197 198 RXN01891 W0122 24949 24086 GLYCEROL-3-PHOSPHATE-BINDING PERIPLASMIC PROTEIN PRECURSOR 199 200 F RXA01891 GR00541 1736 918 GLYCEROL-3-PHOSPHATE-BINDING PERIPLASMIC PROTEIN PRECURSOR 201 202 RXA02414 GR00703 3808 3062 Uncharacteπzed protein involved in glycerol metabolism (homolog of Drosop ila rhomboid) 203 204 RXN01580 W0122 22091 22807 Glycerophosphoryl diester phosphodiesterase Acetate metabolism Nucleic Acid Ammo Acid Identification Code Contig NT Start NT Stop Function SEQ ID NO SEQ ID NO 205 206 RXA01436 GR00418 2547 1357 ACETATE KINASE (EC 2 7 2 1) 207 208 RXA00686 GR00179 8744 7941 ACETATE OPERON REPRESSOR 209 210 RXA00246 GR00037 4425 3391 ALCOHOL DEHYDROGENASE (EC 1 1 1 1) 211 212 RXA01571 GR00438 1360 1959 ALCOHOL DEHYDROGENASE (EC 1 1 1 1) 213 214 RXA01572 GR00438 1928 2419 ALCOHOL DEHYDROGENASE (EC 1 1 1 1) 215 216 RXA01758 GR00498 3961 2945 ALCOHOL DEHYDROGENASE (EC 1 1 1 1) 217 218 RXA02539 GR00726 11676 10159 ALDEHYDE DEHYDROGENASE (EC 219 220 RXN03061 W0034 108 437 ALDEHYDE DEHYDROGENASE (EC 1 2 1 3) 221 222 RXN03150 W0155 10678 10055 ALDEHYDE DEHYDROGENASE (EC 1 2 1 3) 223 224 RXN01340 W0033 3 860 ALDEHYDE DEHYDROGENASE (EC 1 2 1 3) 225 226 RXN01498 W0008 1598 3160 ALDEHYDE DEHYDROGENASE (EC 1 2 1 3) 227 228 RXN02674 W0315 15614 14163 ALDEHYDE DEHYDROGENASE (EC 1 2 1 3) 229 230 RXN00868 W0127 2230 320 ACETOLACTATE SYNTHASE LARGE SUBUNIT (EC 4 1 3 18) 231 232 RXN01143 W0077 9372 8254 ACETOLACTATE SYNTHASE LARGE SUBUNIT (EC 4 1 3 18) 233 234 RXN01146 W0264 243 935 ACETOLACTATE SYNTHASE LARGE SUBUNIT (EC 4 1 3 18) 235 236 RXN01144 W0077 8237 7722 ACETOLACTATE SYNTHASE SMALL SUBUNIT (EC 4 1 3 18) Butanediol, diacetyl and acetoin formation Nucleic Acid Ammo Acid Identification Code Contig NT Start NT Stop Function SEQ ID NO SEQ ID NO 237 238 RXA02474 GR00715 8082 7309 (S,S)-butane-2,3-dιol dehydrogenase (EC 1 1 1 76) 239 240 RXA02453 GR00710 6103 5351 ACETOIN(DIACETYL) REDUCTASE (EC 1 1 1 5) 241 242 RXS01758 W0112 27383 28399 ALCOHOL DEHYDROGENASE (EC 1 1 1 1) Table 1 (continued) HMP-Cycle Nucleic Acid Ammo Acid Identification Code Contig NT Start NT Stop SEQ ID NO SEQ ID NO 243 244 RXA02737 GR00763 3312 1771 GLUCOSE-6-PHOSPHATE 1 -DEHYDROGENASE (EC 1 1 1 49) 245 246 RXA02738 GR00763 4499 3420 TRANSALDOLASE (EC 2 2 1 2) 247 248 RXA02739 GR00763 6769 4670 TRANSKETOLASE (EC 2 2 1 1 ) 249 250 RXA00965 GR00270 1232 510 6-PHOSPHOGLUCONATE DEHYDROGENASE, DECARBOXYLATING (EC 1 1 1 44) 251 252 RXN00999 W0106 2817 1366 6-PHOSPHOGLUCONATE DEHYDROGENASE, DECARBOXYLATING (EC 1 1 1 44) 253 254 F RXA00999 GR00283 3012 4448 6-PHOSPHOGLUCONATE DEHYDROGENASE, DECARBOXYLATING (EC 1 1 1 44) Nucleotide sugar conversion Nucleic Acid Amino Acid Identification Code Contig NT Start NT Stop Function SEQ ID NO SEQ ID NO 255 256 RXN02596 W0098 48784 47582 UDP-GALACTOPYRANOSE MUTASE (EC 5 4 99 9) 257 258 F RXA02596 GR00742 1 489 UDP-GALACTOPYRANOSE MUTASE (EC 5 4 99 9) 259 260 F RXA02642 GR00749 5383 5880 UDP-GALACTOPYRANOSE MUTASE (EC 5 4 99 9) 261 262 RXA02572 GR00737 2 646 UDP-GLUCOSE 6-DEHYDROGENASE (EC 1 1 1 22) 263 264 RXA02485 GR00718 2345 3445 UDP-N-ACETYLENOLPYRUVOYLGLUCOSAMINE REDUCTASE (EC 1 1 1 158) 265 266 RXA01216 GR00352 2302 1202 UDP-N-ACETYLGLUCOSAMINE PYROPHOSPHORYLASE (EC 2 7 7 23) 267 268 RXA01259 GR00367 987 130 UTP-GLUCOSE-1-PHOSPHATE URIDYLYLTRANSFERASE (EC 2 7 7 9) 269 270 RXA02028 GR00616 573 998 UTP-GLUCOSE-1 -PHOSPHATE URIDYLYLTRANSFERASE (EC 2 7 7 9) 271 272 RXA01262 GR00367 8351 7191 GDP-MANNOSE 6-DEHYDROGENASE (EC 1 1 1 132) 273 274 RXA01377 GR00400 3935 5020 MANNOSE-1 -PHOSPHATE GUANYLTRANSFERASE (EC 2 7 7 13) 275 276 RXA02063 GR00626 3301 4527 GLUCOSE-1 -PHOSPHATE ADENYLYLTRANSFERASE (EC 2 7 7 27) 277 278 RXN00014 W0048 8848 9627 GLUCOSE-1 -PHOSPHATE THYMIDYLYLTRANSFERASE (EC 2 7 7 24) 279 280 F RXA00014 GR00002 4448 5227 GLUCOSE-1 -PHOSPHATE THYMIDYLYLTRANSFERASE (EC 2 7 7 24) 281 282 RXA01570 GR00438 427 1281 GLUCOSE-1-PHOSPHATE THYMIDYLYLTRANSFERASE (EC 2 7 7 24) 283 284 RXA02666 GR00753 7260 6493 D-RIBITOL-5-PHOSPHATE CYTIDYLYLTRANSFERASE (EC 2 7 7 40) 285 286 RXA00825 GR00222 222 1154 DTDP-GLUCOSE 4,6-DEHYDRATASE (EC 4 2 1 46) Inositol and ribitol metabolism Nucleic Acid Ammo Acid Identification Code Contig NT Start NT Stop Function SEQ ID NO SEQ ID NO 287 288 RXA01887 GR00539 4219 3209 MYO-INOSITOL 2-DEHYDROGENASE (EC 1 1 1 18) Table 1 (continued) Nucleic Acid Ammo Acid Identification Code Contig NT Start NT Stop Function SEQ ID NO SEQ ID NO 289 290 RXN00013 W0048 7966 8838 MYO-INOSITOL-1 (OR 4)-MONOPHOSPHATASE 1 (EC 3 1 3 25) 291 292 F RXA00013 GR00002 3566 4438 MYO-INOSITOL-1 (OR 4)-MONOPHOSPHATASE 1 (EC 3 1 3 25) 293 294 RXA01099 GR00306 6328 5504 INOSITOL MONOPHOSPHATE PHOSPHATASE 295 296 RXN01332 W0273 579 4 MYO-INOSITOL 2-DEHYDROGENASE (EC 1 1 1 18) 297 298 F RXA01332 GR00388 552 4 MYO-INOSITOL 2-DEHYDROGENASE (EC 1 1 1 18) 299 300 RXA01632 GR00454 2338 3342 MYO-INOSITOL 2-DEHYDROGENASE (EC 1 1 1 18) 301 302 RXA01633 GR00454 3380 4462 MYO-INOSITOL 2-DEHYDROGENASE (EC 1 1 1 18) 303 304 RXN01406 W0278 2999 1977 MYO-INOSITOL 2-DEHYDROGENASE (EC 1 1 1 18) 305 306 RXN01630 W0050 48113 47037 MYO-INOSITOL 2-DEHYDROGENASE (EC 1 1 1 18) 307 308 RXN00528 W0079 23406 22318 MYO-INOSITOL-1 -PHOSPHATE SYNTHASE (EC 5 5 1 4) 309 310 RXN03057 W0028 7017 7688 MYO-INOSITOL 2-DEHYDROGENASE (EC 1 1 1 18) 311 312 F RXA02902 GR10040 10277 10948 GLUCOSE-FRUCTOSE OXIDOREDUCTASE PRECURSOR (EC 1 1 99 28) 313 314 RXA00251 GR00038 931 224 RIBITOL 2-DEHYDROGENASE (EC 1 1 1 56) Utilization of sugars Nucleic Acid Ammo Acid Identification Code Contig NT Start NT Stop Function SEQ ID NO SEQ ID NO 315 316 RXN02654 W0090 12206 13090 GLUCOSE 1 -DEHYDROGENASE (EC 1 1 1 47) O 317 318 F RXA02654 GR00752 7405 8289 GLUCOSE 1 -DEHYDROGENASE II (EC 1 1 1 47) 319 320 RXN01049 W0079 9633 11114 GLUCONOKINASE (EC 2 7 1 12) 321 322 F RXA01049 GR00296 1502 492 GLUCONOKINASE (EC 2 7 1 12) 323 324 F RXA01050 GR00296 1972 1499 GLUCONOKINASE (EC 2 7 1 12) 325 326 RXA00202 GR00032 1216 275 D-RIBOSE-BINDING PERIPLASMIC PROTEIN PRECURSOR 327 328 RXN00872 W0127 6557 5604 FRUCTOKINASE (EC 2 7 1 4) 329 330 F RXA00872 GR00240 565 1086 FRUCTOKINASE (EC 2 7 1 4) 331 332 RXN00799 W0009 58477 56834 PERIPLASMIC BETA-GLUCOSIDASE/BETA-XYLOSIDASE PRECURSOR (EC 3 2 1 21 ) (EC 3 2 1 37) 333 334 F RXA00799 GR00214 1 1584 PERIPLASMIC BETA-GLUCOSIDASE/BETA-XYLOSIDASE PRECURSOR (EC 3 2 1 21) (EC 3 2 1 37) 335 336 RXA00032 GR00003 12028 10520 MANNITOL 2-DEHYDROGENASE (EC 1 1 1 67) 337 338 RXA02528 GR00725 6880 7854 FRUCTOSE REPRESSOR 339 340 RXN00316 W0006 7035 8180 Hypothetical Oxidoreductase (EC 1 1 1 -) 341 342 F RXA00309 GR00053 316 5 GLUCOSE-FRUCTOSE OXIDOREDUCTASE PRECURSOR (EC 1 1 99 28) 343 344 RXN00310 W0006 6616 7050 GLUCOSE-FRUCTOSE OXIDOREDUCTASE PRECURSOR (EC 1 1 99 28) 345 346 F RXA00310 GR00053 735 301 GLUCOSE-FRUCTOSE OXIDOREDUCTASE PRECURSOR (EC 1 1 99 28) 347 348 RXA00041 GR00007 1246 5 SUCROSE-6-PHOSPHATE HYDROLASE (EC 32126) 349 350 RXA02026 GR00615 725 6 SUCROSE-6-PHOSPHATE HYDROLASE (EC 32126) 351 352 RXA02061 GR00626 1842 349 SUCROSE-6-PHOSPHATE HYDROLASE (EC 32126) Table 1 (continued) Nucleic Acid Ammo Acid Identification Code Contig NT Start NT Stop SEQ ID NO SEQ ID NO 353 354 RXN01369 W0124 595 1776 MANNOSE-6-PHOSPHATE ISOMERASE (EC 5 3 1 8) 355 356 F RXA01369 GR00398 3 503 MANNOSE-6-PHOSPHATE ISOMERASE (EC 5 3 1 8) 357 358 F RXA01373 GR00399 595 1302 MANNOSE-6-PHOSPHATE ISOMERASE (EC 5 3 1 8) 359 360 RXA02611 GR00743 1 1752 1 ,4-ALPHA-GLUCAN BRANCHING ENZYME (EC 2 4 1 18) 361 362 RXA02612 GR00743 1793 3985 1 ,4-ALPHA-GLUCAN BRANCHING ENZYME (EC 2 4 1 18) 363 364 RXN01884 W0184 1 1890 GLYCOGEN DEBRANCHING ENZYME (EC 2 4 1 25) (EC 3 2 1 33) 365 366 F RXA01884 GR00539 3 1475 GLYCOGEN DEBRANCHING ENZYME (EC 2 4 1 25) (EC 3 2 1 33) 367 368 RXA01111 GR00306 16981 17427 GLYCOGEN OPERON PROTEIN GLGX (EC 3 2 1 -) 369 370 RXN01550 W0143 14749 16260 GLYCOGEN PHOSPHORYLASE (EC 2 4 1 1 ) 371 372 F RXA01550 GR00431 3 1346 GLYCOGEN PHOSPHORYLASE (EC 2 4 1 1) 373 374 RXN02100 W0318 2 2326 GLYCOGEN PHOSPHORYLASE (EC 2 4 1 1) 375 376 F RXA02100 GR00631 3 920 GLYCOGEN PHOSPHORYLASE (EC 2 4 1 1) 377 378 F RXA02113 GR00633 2 1207 GLYCOGEN PHOSPHORYLASE (EC 2 4 1 1 ) 379 380 RXA02147 GR00639 15516 16532 ALPHA-AMYLASE (EC 3 2 1 1 ) 381 382 RXA01478 GR00422 10517 12352 GLUCOAMYLASE G1 AND G2 PRECURSOR (EC 3 2 1 3) 383 384 RXA01888 GR00539 4366 4923 GLUCOSE-RESISTANCE AMYLASE REGULATOR 385 386 RXN01927 W0127 50623 49244 XYLULOSE KINASE (EC 2 7 1 17) 387 388 F RXA01927 GR00555 3 1118 XYLULOSE KINASE (EC 2 7 1 17) 389 390 RXA02729 GR00762 747 4 RIBOKINASE (EC 2 7 1 15) 391 392 RXA02797 GR00778 1739 2641 RIBOKINASE (EC 2 7 1 15) 393 394 RXA02730 GR00762 1768 731 RIBOSE OPERON REPRESSOR 395 396 RXA02551 GR00729 2193 2552 6-PHOSPHO-BETA-GLUCOSIDASE (EC 3 2 1 86) 397 398 RXA01325 GR00385 5676 5005 DEOXYRIBOSE-PHOSPHATE ALDOLASE (EC 4 1 2 4) 399 400 RXA00195 GR00030 543 1103 1-deoxy-D-xylulose 5-phosphate reductoisomerase (EC 1 1 1 -) 401 402 RXA00196 GR00030 1094 1708 1-deoxy-D-xylulose 5-phosphate reductoisomerase (EC 1 1 1 -) 403 404 RXN01562 W0191 1230 3137 1 -DEOX YX YLULOSE-5-PHOSPHATE SYNTHASE 405 406 F RXA01562 GR00436 2 1039 1-DEOXYXYLULOSE-5-PHOSPHATE SYNTHASE 407 408 F RXA01705 GR00480 971 1573 1-DEOXYXYLULOSE-5-PHOSPHATE SYNTHASE 409 410 RXN00879 W0099 8763 6646 4-ALPHA-GLUCANOTRANSFERASE (EC 2 4 1 25) 411 412 F RXA00879 GR00242 5927 3828 4-ALPHA-GLUCANOTRANSFERASE (EC 2 4 1 25), amylo altase 413 414 RXN00043 W0119 3244 2081 N-ACETYLGLUCOSAMINE-6-PHOSPHATE DEACETYLASE (EC 3 5 1 25) 415 416 F RXA00043 GR00007 3244 2081 N-ACETYLGLUCOSAMINE-6-PHOSPHATE DEACETYLASE (EC 3 5 1 25) 417 418 RXN01752 W0127 35265 33805 N-ACETYLGLUCOSAMINYLTRANSFERASE (EC 2 4 1 -) 419 420 F RXA01839 GR00520 1157 510 N-ACETYLGLUCOSAMINYLTRANSFERASE (EC 2 4 1 -) 421 422 RXA01859 GR00529 1473 547 N-ACETYLGLUCOSAMINYLTRANSFERASE (EC 2 4 1 -) 423 424 RXA00042 GR00007 2037 1279 GLUCOSAMINE-6-PHOSPHATE ISOMERASE (EC 5 3 1 10) 425 426 RXA01482 GR00422 17271 15397 GLUCOSAMINE-FRUCTOSE-6-PHOSPHATE AMINOTRANSFERASE (ISOMERIZING) (EC 2 6 1 16) 427 428 RXN03179 W0336 2 667 URONATE ISOMERASE (EC 5 3 1 12) 429 430 F RXA02872 GR10013 675 4 URONATE ISOMERASE, Glucuronate isomerase (EC 5 3 1 12) 431 432 RXN03180 W0337 672 163 URONATE ISOMERASE (EC 5 3 1 12) 433 434 F RXA02873 GR10014 672 163 URONATE ISOMERASE, Glucuronate isomerase (EC 5 3 1 12) 435 436 RXA02292 GR00662 1611 2285 GALACTOSIDE O-ACETYLTRANSFERASE (EC 2 3 1 18) 437 438 RXA02666 GR00753 7260 6493 D-RIBITOL-5-PHOSPHATE CYTIDYLYLTRANSFERASE (EC 2 7 7 40) 439 440 RXA00202 GR00032 1216 275 D-RIBOSE-BINDING PERIPLASMIC PROTEIN PRECURSOR 441 442 RXA02440 GR00709 5097 4258 D-RIBOSE-BINDING PERIPLASMIC PROTEIN PRECURSOR Table 1 (continued) Nucleic Acid Ammo Acid Identification Code Contig NT Start NT Stop Function SEQ ID NO SEQ ID NO 443 444 RXN01569 W0009 41086 42444 dTDP-4-DEHYDRORHAMNOSE REDUCTASE (EC 1 1 1 133) 445 446 F RXA01569 GR00438 2 427 DTDP-4-DEHYDRORHAMNOSE REDUCTASE (EC 1 1 1 133) 447 448 F RXA02055 GR00624 7122 8042 DTDP-4-DEHYDRORHAMNOSE REDUCTASE (EC 1 1 1 133) 449 450 RXA00825 GR00222 222 1154 DTDP-GLUCOSE 4,6-DEHYDRATASE (EC 4 2 1 46) 451 452 RXA02054 GR00624 6103 7119 DTDP-GLUCOSE 4,6-DEHYDRATASE (EC 4 2 1 46) 453 454 RXN00427 W0112 7004 6219 dTDP-RHAMNOSYL TRANSFERASE RFBF (EC 2 - - -) 455 456 F RXA00427 GR00098 1591 2022 DTDP-RHAMNOSYL TRANSFERASE RFBF (EC 2 - - -) 457 458 RXA00327 GR00057 10263 9880 PROTEIN ARAJ 459 460 RXA00328 GR00057 11147 10656 PROTEIN ARAJ 461 462 RXA00329 GR00057 12390 11167 PROTEIN ARAJ 463 464 RXN01554 W0135 28686 26545 GLUCAN ENDO-1.3-BETA-GLUCOSIDASE A1 PRECURSOR (EC 3 2 1 39) 465 466 RXN03015 W0063 289 8 UDP-GLUCOSE 6-DEHYDROGENASE (EC 1 1 1 22) 467 468 RXN03056 W0028 6258 6935 PUTATIVE HEXULOSE-6-PHOSPHATE ISOMERASE (EC 5 - - -) 469 470 RXN03030 W0009 57006 56443 PERIPLASMIC BETA-GLUCOSIDASE/BETA-XYLOSIDASE PRECURSOR (EC 3 2 1 21) (EC 3 2 1 37) 471 472 RXN00401 W0025 12427 11489 5-DEHYDRO-4-DEOXYGLUCARATE DEHYDRATASE (EC 4 2 1 41) 473 474 RXN02125 W0102 23242 22442 ALDOSE REDUCTASE (EC 1 1 1 21) 475 476 RXN00200 W0181 1679 5116 arabmosyl transferase subunit B (EC 2 4 2 -) 477 478 RXN01175 W0017 39688 38303 PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE (EC 4 1 2 15) 479 480 RXN01376 W0091 5610 4750 PUTATIVE GLYCOSYL TRANSFERASE WBIF 481 482 RXN01631 W0050 47021 46143 PUTATIVE HEXULOSE-6-PHOSPHATE ISOMERASE (EC 5 - - -) 483 484 RXN01593 W0229 13274 12408 NAGD PROTEIN 485 486 RXN00337 W0197 20369 21418 GALACTOKINASE (EC 2 7 1 6) 487 488 RXS00584 W0323 5516 6640 PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE (EC 4 1 2 15) 489 490 RXS02574 BETA-HEXOSAMINIDASE A PRECURSOR (EC 3 2 1 52) 491 492 RXS03215 GLUCOSE-FRUCTOSE OXIDOREDUCTASE PRECURSOR (EC 1 1 99 28) 493 494 F RXA01915 GR00549 1 1008 GLUCOSE-FRUCTOSE OXIDOREDUCTASE PRECURSOR (EC 1 1 99 28) 495 496 RXS03224 CYCLOMALTODEXTRINASE (EC 32154) 497 498 F RXA00038 GR00006 1417 260 CYCLOMALTODEXTRINASE (EC 32154) 499 500 RXC00233 protein involved in sugar metabolism 501 502 RXC00236 Membrane Lipoprotem involved in sugar metabolism 503 504 RXC00271 Exported Protein involved in ribose metabolism 505 506 RXC00338 protein involved in sugar metabolism 507 508 RXC00362 Membrane Spanning Protein involved in metabolism of diols 509 510 RXC00412 Ammo Acid ABC Transporter ATP-Bindmg Protein involved in sugar metabolism 511 512 RXC00526 ABC Transporter ATP-Bindmg Protein involved in sugar metabolism 513 514 RXC01004 Membrane Spanning Protein involved in sugar metabolism 515 516 RXC01017 Cytosohc Protein involved in sugar metabolism 517 518 RXC01021 Cytosohc Kinase involved in metabolism of sugars and thiamin 519 520 RXC01212 ABC Transporter ATP-Bindmg Protein involved in sugar metabolism 521 522 RXC01306 Membrane Spanning Protein involved in sugar metabolism 523 524 RXC01366 Cytosohc Protein involved in sugar metabolism 525 526 RXC01372 Cytosohc Protein involved in sugar metabolism Table 1 (continued) Nucleic Acid Ammo Acid Identification Code Contig NT Start NT Stop Function SEQ ID NO SEQ ID NO 527 528 RXC01659 protein involved in sugar metabolism 529 530 RXC01663 protein involved in sugar metabolism 531 532 RXC01693 protein involved in sugar metabolism 533 534 RXC01703 Cytosohc Protein involved in sugar metabolism 535 536 RXC02254 Membrane Associated Protein involved in sugar metabolism 537 538 RXC02255 Cytosohc Protein involved in sugar metabolism 539 540 RXC02435 protein involved in sugar metabolism 541 542 F RXA02435 GR00709 825 268 Uncharactenzed protein involved in glycerol metabolism (homolog of Drosophila rhomboid) 543 544 RXC03216 protein involved in sugar metabolism TCA-cycle Nucleic Acid Ammo Acid Identification Code Contig NT Start NT Stop Function SEQ ID NO SEQ ID NO 545 546 RXA02175 GR00641 10710 9418 CITRATE SYNTHASE (EC 4 1 3 7) 547 548 RXA02621 GR00746 2647 1829 CITRATE LYASE BETA CHAIN (EC 4 1 3 6) 549 550 RXN00519 W0144 5585 3372 ISOCITRATE DEHYDROGENASE (NADP) (EC 1 1 1 42) 551 552 F RXA00521 GR00133 2 1060 ISOCITRATE DEHYDROGENASE [NADP] (EC 1 1 1 42) 553 554 RXN02209 W0304 1 1671 ACONITATE HYDRATASE (EC 4 2 1 3) 555 556 F RXA02209 GR00648 3 1661 ACONITATE HYDRATASE (EC 4 2 1 3) 557 558 RXN02213 W0305 1378 2151 ACONITATE HYDRATASE (EC 4 2 1 3) 559 560 F RXA02213 GR00649 1330 2046 ACONITATE HYDRATASE (EC 4 2 1 3) 561 562 RXA02056 GR00625 3 2870 2-OXOGLUTARATE DEHYDROGENASE E1 COMPONENT (EC 1 2 4 2) 563 564 RXA01745 GR00495 2 1495 DIHYDROLIPOAMIDE SUCCINYLTRANSFERASE COMPONENT (E2) OF 2-OXOGLUTARATE DEHYDROGENASE COMPLEX (EC 2 3 1 61) 565 566 RXA00782 GR00206 3984 3103 SUCCINYL-COA SYNTHETASE ALPHA CHAIN (EC 6 2 1 5) 567 568 RXA00783 GR00206 5280 4009 SUCCINYL-COA SYNTHETASE BETA CHAIN (EC 6 2 1 5) 569 570 RXN01695 W0139 11307 12806 L-MALATE DEHYDROGENASE (ACCEPTOR) (EC 1 1 99 16) 571 572 F RXA01615 GR00449 8608 9546 L-MALATE DEHYDROGENASE (ACCEPTOR) (EC 1 1 99 16) 573 574 F RXA01695 GR00474 4388 4179 L-MALATE DEHYDROGENASE (ACCEPTOR) (EC 1 1 99 16) 575 576 RXA00290 GR00046 4693 5655 MALIC ENZYME (EC 1 1 1 39) 577 578 RXN01048 W0079 12539 11316 MALIC ENZYME (EC 1 1 1 39) 579 580 F RXA01048 GR00296 3 290 MALIC ENZYME (EC 1 1 1 39) 581 582 F RXA00290 GR00046 4693 5655 MALIC ENZYME (EC 1 1 1 39) 583 584 RXN03101 W0066 2 583 DIHYDROLIPOAMIDE SUCCINYLTRANSFERASE COMPONENT (E2) OF 2-OXOGLUTARATE DEHYDROGENASE COMPLEX (EC 2 3 1 61) 585 586 RXN02046 W0025 15056 14640 DIHYDROLIPOAMIDE SUCCINYLTRANSFERASE COMPONENT OF 2- OXOGLUTARATE DEHYDROGENASE COMPLEX (EC 2 3 1 61) 587 588 RXN00389 W0025 11481 9922 oxoglutarate semialdehyde dehydrogenase (EC 1 2 1 -) Table 1 (continued) Glyoxylate bypass Nucleic Acid Ammo Acid Identification Code Contig NT Start NT Stop Function SEQ ID NO SEQ ID NO 589 590 RXN02399 W0176 19708 18365 ISOCITRATE LYASE (EC 4 1 3 1 ) 591 592 F RXA02399 GR00699 478 1773 ISOCITRATE LYASE (EC 4 1 3 1) 593 594 RXN02404 W0176 20259 22475 MALATE SYNTHASE (EC 4 1 3 2) 595 596 F RXA02404 GR00700 3798 1663 MALATE SYNTHASE (EC 4 1 3 2) 597 598 RXA01089 GR00304 3209 3958 GLYOXYLATE-INDUCED PROTEIN 599 600 RXA01886 GR00539 3203 2430 GLYOXYLATE-INDUCED PROTEIN Methylcitrate-pathway Nucleic Acid Ammo Acid Identification Code Contig NT Start NT Stop Function SEQ ID NO SEQ ID NO 600 602 RXN03117 W0092 3087 1576 2-methylιsocιtrate synthase (EC 5 3 3 -) 601 604 F RXA00406 GR00090 978 4 2-methyhsocιtrate synthase (EC 5 3 3 -) 603 606 F RXA00514 GR00130 1983 1576 2-methyhsocιtrate synthase (EC 5 3 3 -) 605 608 RXA00512 GR00130 621 4 2-methylcιtrate synthase (EC 4 1 3 31) 607 610 RXA00518 GR00131 3069 2773 2-methylcιtrate synthase (EC 4 1 3 31) o 609 612 RXA01077 GR00300 4647 6017 2-methyhsocιtrate synthase (EC 5 3 3 -) 611 614 RXN03144 W0141 2 901 2-methyhsocιtrate synthase (EC 5 3 3 -) 613 616 F RXA02322 GR00668 415 5 2-methyhsocιtrate synthase (EC 5 3 3 -) 615 618 RXA02329 GR00669 607 5 2-methyhsocιtrate synthase (EC 5 3 3 -) 617 620 RXA02332 GR00671 1906 764 2-methylcιtrate synthase (EC 4 1 3 31) 619 622 RXN02333 W0141 901 1815 methylisocitrate lyase (EC 4 1 3 30) 621 624 F RXA02333 GR00671 2120 1902 methylisocitrate lyase (EC 4 1 3 30) 623 626 RXA00030 GR00003 9590 9979 LACTOYLGLUTATHIONE LYASE (EC 44 1 5) Methyl-Malonyl-CoA-Mutases Nucleic Acid Ammo Acid Identification Code Contig NT Start NT Stop Function SEQ ID NO SEQ ID NO 625 628 RXN00148 W0167 9849 12059 METHYLMALONYL-COA MUTASE ALPHA-SUBUNIT (EC 5 4 99 2) 627 630 F RXA001 8 GR00023 2002 5 METHYLMALONYL-COA MUTASE ALPHA-SUBUNIT (EC 5 4 99 2) 629 632 RXA00149 GR00023 3856 2009 METHYLMALONYL-COA MUTASE BETA-SUBUNIT (EC 5 4 99 2) Table 1 (continued) Others Nucleic Acid Am o Acid Identification Code Contig NT Start NT Stop Function SEQ ID NO SEQ ID NO 631 634 RXN00317 W0197 26879 27532 PHOSPHOGLYCOLATE PHOSPHATASE (EC 31318) 635 636 F RXA00317 GR00055 344 6 PHOSPHOGLYCOLATE PHOSPHATASE (EC 31318) 637 638 RXA02196 GR00645 3956 3264 PHOSPHOGLYCOLATE PHOSPHATASE (EC 31318) 639 640 RXN02461 W0124 14236 14643 PHOSPHOGLYCOLATE PHOSPHATASE (EC 31318) Redox Chain Nucleic Acid Ammo Acid Identification Code Contig NT Start NT Stop Function SEQ ID NO SEQ ID NO 641 642 RXN01744 W0174 2350 812 CYTOCHROME D UBIQUINOL OXIDASE SUBUNIT I (EC 1 10 3 -) 643 644 F RXA00055 GR00008 11753 11890 CYTOCHROME D UBIQUINOL OXIDASE SUBUNIT I (EC 1 10 3 -) 645 646 F RXA01 44 GR00494 2113 812 CYTOCHROME D UBIQUINOL OXIDASE SUBUNIT I (EC 1 10 3 -) 647 648 RXA00379 GR00082 212 6 CYTOCHROME C-TYPE BIOGENESIS PROTEIN CCDA 649 650 RXA00385 GR00083 773 435 CYTOCHROME C-TYPE BIOGENESIS PROTEIN CCDA 651 652 RXA01743 GR00494 806 6 CYTOCHROME D UBIQUINOL OXIDASE SUBUNIT II (EC 1 10 3 -) 653 654 RXN02480 W0084 31222 29567 CYTOCHROME C OXIDASE POLYPEPTIDE I (EC 1 9 3 1) M 655 656 F RXA01919 GR00550 288 4 CYTOCHROME C OXIDASE SUBUNIT I (EC 1 9 3 1 ) 657 658 F RXA02480 GR00717 1449 601 CYTOCHROME C OXIDASE POLYPEPTIDE I (EC 1 9 3 1) 659 660 F RXA02481 GR00717 1945 1334 CYTOCHROME C OXIDASE POLYPEPTIDE I (EC 1 9 3 1) 661 662 RXA02140 GR00639 7339 8415 CYTOCHROME C OXIDASE POLYPEPTIDE II (EC 1 9 3 1) 663 664 RXA02142 GR00639 9413 10063 CYTOCHROME C OXIDASE POLYPEPTIDE I (EC 1 9 3 1) 665 666 RXA02144 GR00639 11025 12248 RIESKE IRON-SULFUR PROTEIN 667 668 RXA02740 GR00763 7613 8542 PROBABLE CYTOCHROME C OXIDASE ASSEMBLY FACTOR 669 670 RXA02743 GR00763 13534 12497 CYTOCHROME AA3 CONTROLLING PROTEIN 671 672 RXA01227 GR00355 1199 1519 FERREDOXIN 673 674 RXA01865 GR00532 436 122 FERREDOXIN 675 676 RXA00680 GR00179 2632 2315 FERREDOXIN VI 677 678 RXA00679 GR00179 2302 1037 FERREDOXIN-NAD(+) REDUCTASE (EC 1 18 1 3) 679 680 RXA00224 GR00032 24965 24015 ELECTRON TRANSFER FLAVOPROTEIN ALPHA-SUBUNIT 681 682 RXA00225 GR00032 25783 24998 ELECTRON TRANSFER FLAVOPROTEIN BETA-SUBUNIT 683 684 RXN00606 W0192 11299 9026 NADH DEHYDROGENASE I CHAIN L (EC 1 6 5 3) 685 686 F RXA00606 GR00160 121 1869 NADH DEHYDROGENASE I CHAIN L (EC 1 6 5 3) 687 688 RXN00595 W0192 8642 7113 NADH DEHYDROGENASE I CHAIN M (EC 1 6 5 3) 689 690 F RXA00608 GR00160 2253 3017 NADH DEHYDROGENASE I CHAIN M (EC 1 6 5 3) 691 692 RXA00913 GR00249 3 2120 NADH DEHYDROGENASE I CHAIN L (EC 1 6 5 3) 693 694 RXA00909 GR00247 2552 3406 NADH DEHYDROGENASE I CHAIN L (EC 1 6 5 3) 695 696 RXA00700 GR00182 846 43 NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 2 697 698 RXN00483 W0086 44824 46287 NADH-UBIQUINONE OXIDOREDUCTASE 39 KD SUBUNIT PRECURSOR (EC 1 6 5 3) (EC 1 6 99 3) Table 1 (continued) Nucleic Acid Ammo Acid Identification Code Contig NT Start NT Stop Function SEQ ID NO SEQ ID NO 699 700 F RXA00483 GR00119 19106 20569 NADH-UBIQUINONE OXIDOREDUCTASE 39 KD SUBUNIT PRECURSOR (EC 1 6 5 3) (EC 1 6 99 3) 701 702 RXA01534 GR00427 1035 547 NADH-DEPENDENT FMN OXYDOREDUCTASE 703 704 RXA00288 GR00046 2646 1636 QUINONE OXIDOREDUCTASE (EC 1 6 5 5) 705 706 RXA02741 GR00763 9585 8620 QUINONE OXIDOREDUCTASE (EC 1 6 5 5) 707 708 RXN02560 W0101 9922 10788 NADPH-FLAVIN OXIDOREDUCTASE (EC 1 6 99 -) 709 710 F RXA02560 GR00731 6339 7160 NADPH-FLAVIN OXIDOREDUCTASE (EC 1 6 99 -) 711 712 RXA01311 GR00380 1611 865 SUCCINATE DEHYDROGENASE IRON-SULFUR PROTEIN (EC 1 3 99 1) 713 714 RXN03014 W0058 1273 368 NADH DEHYDROGENASE I CHAIN M (EC 1 6 5 3) 715 716 F RXA00910 GR00248 3 1259 Hydrogenase subunits 717 718 RXN01895 W0117 955 5 NADH DEHYDROGENASE (EC 16993) 719 720 F RXA01895 GR00543 2 817 DEHYDROGENASE 721 722 RXA00703 GR00183 2556 271 FORMATE DEHYDROGENASE ALPHA CHAIN (EC 1212) 723 724 RXN00705 W0005 6111 5197 FDHD PROTEIN 725 726 F RXA00705 GR00184 1291 407 FDHD PROTEIN 727 728 RXN00388 W0025 2081 3091 CYTOCHROME C BIOGENESIS PROTEIN CCSA 729 730 F RXA00388 GR00085 969 667 essential protein similar to cytochrome c 731 732 F RXA00386 GR00084 514 5 RESC PROTEIN, essential protein similar to cytochrome c biogenesis protein 733 734 RXA00945 GR00259 1876 2847 putative cytochrome oxidase 735 736 RXN02556 W0101 5602 6759 FLAVOHEMOPROTEIN / DIHYDROPTERIDINE REDUCTASE (EC 1 6 99 7) 737 738 F RXA02556 GR00731 2019 3176 FLAVOHEMOPROTEIN 739 740 RXA01392 GR00408 2297 3373 GLUTATHIONE S-TRANSFERASE (EC 2 5 1 18) 741 742 RXA00800 GR00214 2031 3134 GLUTATHIONE-DEPENDENT FORMALDEHYDE DEHYDROGENASE (EC 1 2 1 1) 743 744 RXA021 3 GR00639 10138 11025 QCRC PROTEIN, menaqumol cytochrome c oxidoreductase 745 746 RXN03096 W0058 405 4 NADH DEHYDROGENASE I CHAIN M (EC 1 6 5 3) 747 748 RXN02036 W0176 32683 33063 NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 4 (EC 1 6 5 3) 749 750 RXN02765 W0317 3552 2794 Hypothetical Oxidorductase 751 752 RXN02206 W0302 1784 849 Hypothetical Oxidoreductase 753 754 RXN02554 W0101 4633 4010 Hypothetical Oxidoreductase (EC 1 1 1 -) ATP-Synthase Nucleic Acid Ammo Acid Identification Code Contig NT Start NT Stop Function SEQ ID NO SEQ ID NO 755 756 RXN01204 W0121 1270 461 ATP SYNTHASE A CHAIN (EC 3 6 1 34) 757 758 F RXA01204 GR00345 394 1155 ATP SYNTHASE A CHAIN (EC 3 6 1 34) 759 760 RXA01201 GR00344 675 2315 ATP SYNTHASE ALPHA CHAIN (EC 3 6 1 34) 761 762 RXN01193 W0175 5280 3832 ATP SYNTHASE BETA CHAIN (EC 3 6 1 34) 763 764 F RXA01193 GR00343 15 755 ATP SYNTHASE BETA CHAIN (EC 3 6 1 34) 765 766 F RXA01203 GR00344 3355 3993 ATP SYNTHASE BETA CHAIN (EC 3 6 1 34) Table 1 (continued) Nucleic Acid Ammo Acid Identification Code Contig NT Start NT Stop Function SEQ ID NO SEQ ID NO 767 768 RXN02821 W0121 324 85 ATP SYNTHASE C CHAIN (EC 3 6 1 34) 769 770 F RXA02821 GR00802 139 318 ATP SYNTHASE C CHAIN (EC 3 6 1 34) 771 772 RXA01200 GR00344 2 610 ATP SYNTHASE DELTA CHAIN (EC 3 6 1 34) 773 774 RXA01194 GR00343 770 1141 ATP SYNTHASE EPSILON CHAIN (EC 3 6 1 34) 775 776 RXA01202 GR00344 2375 3349 ATP SYNTHASE GAMMA CHAIN (EC 3 6 1 34) 777 778 RXN02434 W0090 4923 3274 ATP-BINDING PROTEIN Cytochrome metabolism Nucleic Acid Ammo Acid Identification Code Contig NT Start NT Stop Function SEQ ID NO SEQ ID NO 779 780 RXN00684 W0005 29864 28581 CYTOCHROME P450 116 (EC 1 14 - -) 781 782 RXN00387 W0025 1150 2004 Hypothetical Cytochrome c Biogenesis Protein ^ t 4 0 o o o t o o TABLE 3 : Corynebacterium and Brevibacterium Strains Which May be Used in the Practice of the Invention 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 ID # length Genbank Hit Length Accession Name of Genbank Hit Source of Genbank Hit % homoloqv Date of (NT) (GAP) Deposit rxa00013 996 GB_GSS4 AQ713475 581 AQ713475 HS_5402_B2_A12_T7A RPCI-11 Human Male BAC Library Homo sapiens Homo sapiens 37,148 13-Jul-99 genomic clone Plate=978 Col=24 Row=B, genomic survey sequence GB HTG3 AC007420 130583 AC007420 Drosophila melanogaster chromosome 2 clone BACR07M10 (D630) RPCI-98 Drosophila melanogaster 34,568 20-Sep-9 07 M 10 map 24A-24D strain y, en bw sp, "* SEQUENCING IN PROGRESS *** , 83 unordered pieces GB HTG3 AC007420 130583 AC007420 Drosophila melanogaster chromosome 2 clone BACR07M10 (D630) RPCI-98 Drosophila melanogaster 34,568 20-Sep-9 07 M 10 map 24A-24D strain y, en bw sp, *** SEQUENCING IN PROGRESS *** , 83 unordered pieces rxa00014 903 GB_BA1 MTCY3A2 25830 Z83867 Mycobacterium tuberculosis H37Rv complete genome, segment 136/162 Mycobacterium 58,140 17-Jun-98 tuberculosis GB_BA1 LCB1779 43254 Z98271 Mycobacterium leprae cosmid B1779 Mycobacterium leprae 57,589 8-Aug-97 GB_BA1 SAPURCLUS 9120 X92429 S alboniger napH, pur7, pur10, purβ, pur4, pur5 and pur3 genes Streptomyces anulatus 55,667 28-Feb-9 rxa00030 513 GB EST21 C89713 767 C89713 C89713 Dictyostelium discoideum SS (H Urushihara) Dictyostehum discoideum Dictyostelium discoideum 45,283 20-Apr-98 cDNA clone SSG229, mRNA sequence GB EST28 AI497294 484 AI497294 fb63g03 y1 Zebrafish WashU MPIMG EST Danio reπo cDNA 5' similar to Danio reπo 42,991 11-MAR-1 SW AFP4_MYOOC P80961 ANTIFREEZE PROTEIN LS-12 „ mRNA sequence GB_EST21 C92167 637 C92167 C92167 Dictyostelium discoideum SS (H Urushihara) Dictyostelium discoideum Dictyostelium discoideum 44,444 12-Jul-99 cDNA clone SSD179, mRNA sequence rxa00032 1632 GB_BA2 AF010496 189370 AFO 10496 Rhodobacter capsulatus strain SB1003, partial genome Rhodobacter capsulatus 39,689 12-MAY-1 GB BA2 AF018073 9810 AF018073 Rhodobacter sphaeroides operon regulator (smoC), penplasmic sorbitol-binding Rhodobacter sphaeroides 48,045 22-OCT-1 protein (smoE), sorbitol/manmtol transport inner membrane protein (smoF), sorbitol/mannitol transport inner membrane protein (smoG), sorbitol/mannitol transport ATP-binding transport protein (smoK), sorbitol dehydrogenase (smoS), mannitol dehydrogenase (mtlK), and penplasmic mannitol-binding protein (smoM) genes, complete eds GB BA2 AF045245 5930 AF045245 Klebsiella pneumoniae D-arabinitol transporter (dalT), D-arabinitol kinase Klebsiella pneumoniae 38,514 16-Jul-98 (dalK), D-arabinitol dehydrogenase (dalD), and repressor (dalR) genes, complete eds rxa00041 1342 EM PAT E11760 6911 E11760 Base sequence of sucrase gene Corynebacterium 99,031 08-OCT-1 glutamicum (Rel 52, Created) GB_PAT 126124 6911 126124 Sequence 4 from patent US 5556776 Unknown 99,031 07-OCT-1 GBJN1 LMFL5883 31934 AL117384 Leishmania major Friedhn chromosome 23 cosmid L5883, complete sequence Leishmania major 43,663 21-OCT-1 rxa00042 882 EM PAT E11760 6911 E11760 Base sequence of sucrase gene Corynebacterium 94,767 08-OCT-1 glutamicum (Rel 52, Created) GB PAT 126124 6911 126124 Sequence 4 from patent US 5556776 Unknown 94,767 07-OCT-1 Table 4 (continued) GBJN1 CEU33051 4899 U33051 Caenorhabditis elegans sur-2 mRNA, complete eds Caenorhabditis elegans 40,276 23-Jan-96 rxa000431287 GB_PAT 126124 6911 126124 Sequence 4 from patent US 5556776 Unknown 97,591 07-OCT-1 EM PAT E11760 6911 E11760 Base sequence of sucrase gene Corynebacterium 97,591 08-OCT-1 glutamicum (Rel 52, Created) GB_PR3 AC005174 39769 AC005174 Homo sapiens clone UWGC g1564a012 from 7p14-15, complete sequence Homo sapiens 35,879 24-Jun-98 rxa000981743 GB_BA1 MSU88433 1928 U88433 Mycobacterium smegmatis phosphoglucose isomerase gene, complete eds Mycobacterium smegmatis 62,658 19-Apr-97 GB_BA1 SC5A7 40337 AL031107 Streptomyces coelicolor cosmid 5A7 Streptomyces coelicolor 37,638 27-Jul-98 GB_BA1 MTCY10D7 39800 Z79700 Mycobacterium tuberculosis H37Rv complete genome, segment 44/162 Mycobacterium 36,784 17-Jun-98 tuberculosis rxa001482334 GB_BA1 MTCY277 38300 Z79701 Mycobacterium tuberculosis H37Rv complete genome, segment 65/162 Mycobacterium 67,457 17-Jun-98 tuberculosis GB_BA1 MSGY456 37316 AD000001 Mycobacterium tuberculosis sequence from clone y456 Mycobacterium 40,883 03-DEC-1 tuberculosis GB_BA1 MSGY175 18106 AD000015 Mycobacterium tuberculosis sequence from clone y175 Mycobacterium 67,457 10-DEC-1 tuberculosis rxa00149 1971 GB_BA1 MSGY456 37316 AD000001 Mycobacterium tuberculosis sequence from clone y456 Mycobacterium 35,883 03-DEC-1 tuberculosis GB_BA1 MSGY175 18106 AD000015 Mycobacterium tuberculosis sequence from clone y175 Mycobacterium 51 ,001 10-DEC-1 tuberculosis GB_BA1 MTCY277 38300 Z79701 Mycobacterium tuberculosis H37Rv complete genome, segment 65/162 Mycobacterium 51 ,001 17-Jun-98 tuberculosis rxa00195 684 GB_BA1 MTCY274 39991 Z74024 Mycobacterium tuberculosis H37Rv complete genome, segment 126/162 Mycobacterium 35,735 19-Jun-98 tuberculosis GB_BA1 MSGB1529CS 36985 L78824 Mycobacterium leprae cosmid B1529 DNA sequence Mycobacterium leprae 57,014 15-Jun-96 GB_BA1 MTCY274 39991 Z74024 Mycobacterium tuberculosis H37Rv complete genome, segment 126/162 Mycobacterium 41 ,892 19-Jun-98 tuberculosis rxa00196 738 GB_BA1 MTCY274 39991 Z74024 Mycobacterium tuberculosis H37Rv complete genome, segment 126/162 Mycobacterium 41 ,841 19-Jun-98 tuberculosis GB_BA1 MTCY274 39991 Z74024 Mycobacterium tuberculosis H37Rv complete genome, segment 126/162 Mycobacterium 36,599 19-Jun-98 tuberculosis GB_RO RATCBRQ 10752 M55532 Rat carbohydrate binding receptor gene, complete eds Rattus norvegicus 36,212 27-Apr-93 rxa00202 1065 GB_EST11 AA253618 313 AA253618 mw95c10 r1 Soares mouse NML Mus musculus cDNA clone IMAGE 678450 5', Mus musculus 38,816 13-MAR-1 mRNA sequence GB_EST26 AI390284 490 AI390284 mw96a03 y1 Soares mouse NML Mus musculus cDNA clone IMAGE 678508 5' Mus musculus 42,239 2-Feb-99 similar to TR 009171 009171 BETAINE-HOMOCYSTEINE METHYLTRANSFERASE,, mRNA sequence GB_EST26 AI390280 467 AI390280 mw95c10 y1 Soares mouse NML Mus musculus cDNA clone IMAGE 678450 Mus musculus 37,307 2-Feb-99 5', mRNA sequence rxa00206 1161 GB_BA1 MLCB637 44882 Z99263 Mycobacterium leprae cosmid B637 Mycobacterium leprae 58,312 17-Sep-9 GB BA1 MTV012 70287 AL021287 Mycobacterium tuberculosis H37Rv complete genome, segment 132/162 Mycobacterium 36,632 23-Jun-99 tuberculosis Table 4 (continued) GB_BA1 SC6E10 23990 AL109661 Streptomyces coelicolor cosmid 6E 10 Streptomyces coelicolor 38,616 5-Aug-99 A3(2) rxa00224 1074 GB_BA1 BJU32230 1769 U32230 Bradyrhizobium japonicum electron transfer flavoprotein small subunit (etfS) nd Bradyrhizobium japonicum 48,038 25-MAY-1 large subunit (etfL) genes, complete cds GB_BA1 PDEETFAB 2440 L 14864 Paracoccus denitπficans electron transfer flavoprotein alpha and beta subunit Paracoccus denitnficans 48,351 27-OCT-1 genes, complete cds's GB_HTG3 AC009689 177954 AC009689 Homo sapiens chromosome 4 clone 104_F_7 map 4, LOW-PASS SEQUENCE Homo sapiens 38,756 28-Aug-99 SAMPLING rxa00225 909 GB_RO AF060178 2057 AF060178 Mus musculus heparan sulfate 2-sulfotransferase (Hs2st) mRNA, complete cds Mus musculus 39,506 18-Jun-98 GB_GSS11 AQ325043 734 AQ325043 mgxb0020J01 r CUGI Rice Blast BAC Library Magnaporthe grisea genomic Magnaporthe gnsea 38,333 8-Jan-99 clone mgxb0020J01r, genomic survey sequence GB_EST31 AI676413 551 AI676413 etmEST0167 EtH1 Eimeπa tenella cDNA clone etmc074 5', mRNA sequence Eimeria tenella 35,542 19-MAY-1 rxa00235 1398 GB_BA1 MTCY10G2 38970 Z92539 Mycobacterium tuberculosis H37Rv complete genome, segment 47/162 Mycobacterium 65,759 17-Jun-98 tuberculosis GB_BA2 AF061753 3721 AF061753 Nitrosomonas europaea CTP synthase (pyrG) gene, partial cds, and enolase Nitrosomonas europaea 58,941 31-Aug-98 (eno) gene, complete cds GB_BA2 AF086791 37867 AF086791 Zymomonas mobilis strain ZM4 clone 67E10 carbamoylphosphate synthetase Zymomonas mobilis 61 ,239 4-Nov-98 small subunit (carA), carbamoylphosphate synthetase large subunit (carB), transcription elongation factor (greA), enolase (eno), pyruvate dehydrogenase alpha subunit (pdhA), pyruvate dehydrogenase beta subunit (pdhB), ribonuclease H (rnh), homoserine kinase homolog, alcohol dehydrogenase II (adhB), and excinuclease ABC subunit A (uvrA) genes, complete cds, and unknown genes nca00246 1158 GB_BA2 AF012550 2690 AF012550 Acmetobacter sp BD413 ComP (comP) gene, complete cds Acmetobacter sp BD413 53,726 27-Sep-99 GB_PAT E03856 1506 E03856 gDNA encoding alcohol dehydrogenase Bacillus 51 ,688 29-Sep-97 stearothermophilus GB_BA1 BACADHT 1688 D90421 B stearothermophilus adhT gene for alcohol dehydrogenase Bacillus 51 ,602 7-Feb-99 stearothermophilus rxa00251 831 GB_BA1 MTCY20G9 37218 Z77162 Mycobacterium tuberculosis H37Rv complete genome, segment 25/162 Mycobacterium 42,875 17-Jun-98 tuberculosis GB_BA1 MTV004 69350 AL009198 Mycobacterium tuberculosis H37Rv complete genome, segment 144/162 Mycobacterium 40,380 18-Jun-98 tuberculosis GB_BA1 MTV004 69350 AL009198 Mycobacterium tuberculosis H37Rv complete genome, segment 144/162 Mycobacterium 41 ,789 18-Jun-98 tuberculosis rxa00288 1134 GB_BA2 AF050114 1038 AF050114 Pseudomonas sp W7 algmate lyase gene, complete cds Pseudomonas sp W7 49,898 03-MAR-1 GB_GSS3 B16984 469 B16984 344A14 TVC CIT978SKA1 Homo sapiens genomic clone A-344A14, genomic H Hoommoo ssaappiieennss 39,355 4-Jun-98 survey sequence GBJN2 AF144549 7887 AF 144549 Aedes albopictus nbosomal protein L34 (rpl34) gene, complete cds Aedes albopictus 36,509 3-Jun-99 rxa00293 1035 GB EST1 T28483 313 T28483 EST46182 Human Kidney Homo sapiens cDNA 3' end similar to flavin- Homo sapiens 42,997 6-Sep-95 containing monooxygenase 1 (HT 1956), mRNA sequence Table 4 (continued) GB_PR1 HUMFM01 2134 M64082 Human flavin-containing monooxygenase (FM01) mRNA, complete cds Homo sapiens 37,915 β-Nov-94 GB EST32 AI734238 512 AI734238 zb73c05 y5 Soares_fetal_lung_NbHL19W Homo sapiens cDNA clone Homo sapiens 41 ,502 14-Jun-99 IMAGE 309224 5' similar to gb M64082 DIMETHYLANILINE MONOOXYGENASE (HUMAN),, mRNA sequence rxa00296 2967 GBJHTG6 AC011069 168266 AC011069 Drosophila melanogaster chromosome X clone BACR11 H20 (D881 ) RPCI-98 Drosophila melanogaster 33,890 02-DEC-1 11 H 20 map 12B-12C strain y, en bw sp, *** SEQUENCING IN PROGRESS ***, 92 unordered pieces GB_EST15 AA531468 414 AA531468 nj63d12 s1 NCI_CGAP_Pr10 Homo sapiens cDNA clone IMAGE 997175, Homo sapiens 40,821 20-Aug-97 mRNA sequence GB HTG6 AC011069 168266 AC011069 Drosophila melanogaster chromosome X clone BACR11 H20 (D881 ) RPCI-98 Drosophila melanogaster 30,963 02-DEC-1 11 H 20 map 12B-12C strain y, en bw sp, *** SEQUENCING IN PROGRESS ***, 92 unordered pieces rxa00310 558 GB_VI VMVY16780 186986 Y 16780 variola minor virus complete genome variola minor virus 35,883 2-Sep-99 GB_VI VARCG 186103 L22579 Variola major virus (strain Bangladesh-1975) complete genome Variola major virus 34,664 12-Jan-95 GB_VI WCGAA 185578 X69198 Variola virus DNA complete genome Variola virus 36,000 13-DEC-1 rxa00317 777 GB_HTG3 AC009571 159648 AC009571 Homo sapiens chromosome 4 clone 57_A_22 map 4, *** SEQUENCING IN Homo sapiens 36,988 29-Sep-99 PROGRESS ***, 8 unordered pieces GB_HTG3 AC009571 159648 AC009571 Homo sapiens chromosome 4 clone 57_A_22 map 4, *** SEQUENCING IN Homo sapiens 36,988 29-Sep-99 PROGRESS ***, 8 unordered pieces GB_PR3 AC005697 174503 AC005697 Homo sapiens chromosome 17, clone hRPK 138_P_22, complete sequence Homo sapiens 36,340 09-OCT-1 rxa00327 507 GB_BA1 LCATPASEB 1514 X64542 L casei gene for ATPase beta-subunit Lactobacillus casei 34,664 1 1-DEC-1 GB_BA1 LCATPASEB 1514 X64542 L casei gene for ATPase beta-subunit Lactobacillus casei 39,308 11 -DEC- 1 rxa00328 615 GB_BA1 STYPUTPE 1887 L01138 Salmonella (S2980) proline permease (putP) gene, 5' end Salmonella sp 39,623 09-MAY-1 GB_BA1 STYPUTPF 1887 L01139 Salmonella (S2983) proline permease (putP) gene, 5' end Salmonella sp 39,623 09-MAY-1 GB_BA1 STYPUTPI 1889 L01142 Salmonella (S3015) proline permease (putP) gene, 5' end Salmonella sp 42,906 09-MAY-1 rxa00329 1347 GB_PR3 AC004691 141990 AC004691 Homo sapiens PAC clone DJ0740D02 from 7p14-p15, complete sequence Homo sapiens 38,142 16-MAY-1 GB_PR4 AC004916 129014 AC004916 Homo sapiens clone DJ0891 L14, complete sequence Homo sapiens 38,549 17-Jul-99 GB_PR3 AC004691 141990 AC004691 Homo sapiens PAC clone DJ0740D02 from 7p14-p15, complete sequence Homo sapiens 35,865 16-MAY-1 rxa00340 1269 GB_BA1 MTCY427 38110 Z70692 Mycobacterium tuberculosis H37Rv complete genome, segment 99/162 Mycobacterium 38,940 24-Jun-99 tuberculosis GB_GSS12 AQ412290 238 AQ412290 RPCI-11 -195H2 TV RPCI-11 Homo sapiens genomic clone RPCI-11 -195H2, Homo sapiens 36,555 23-MAR-1 genomic survey sequence GB_PL2 AF112871 2394 AF112871 Astasia longa small subunit ribosomal RNA gene, complete sequence Astasia longa 36,465 28-Jun-99 rxa00379 307 GB_HTG1 CEY56A3 224746 AL022280 Caenorhabditis elegans chromosome III clone Y56A3, *** SEQUENCING IN Caenorhabditis elegans 35,179 6-Sep-99 PROGRESS ***, in unordered pieces GB HTG1 CEY56A3 224746 AL022280 Caenorhabditis elegans chromosome III clone Y56A3, *** SEQUENCING IN Caenorhabditis elegans 35,179 6-Sep-99 PROGRESS ***, in unordered pieces Table 4 (continued) GB_PR2 HS134019 86897 AL034555 Human DNA sequence from clone 134019 on chromosome 1 p36 11-36 33 Homo sapiens 40,604 23-Nov-9 complete sequence rxa00381 729 GB_GSS4 AQ730532 416 AQ730532 HS_2149_A1_C06_T7C CIT Approved Human Genomic Sperm Library D Homo sapiens 35,766 15-Jul-99 Homo sapiens genomic clone Plate=2149 Col=11 Row=E, genomic survey sequence GB_EST23 AH 20939 561 AH 20939 ub74f05 r1 Soares mouse mammary gland NMLMG Mus musculus cDNA clone Mus musculus 41 ,113 2-Sep-98 IMAGE 1383489 5' similar to gb J04046 CALMODULIN (HUMAN), gb M19381 Mouse calmodulin (MOUSE),, mRNA sequence GB_EST23 AM 20939 561 AM 20939 ub74f05 r1 Soares mouse mammary gland NMLMG Mus musculus cDNA clone Mus musculus 41 ,1 13 2-Sep-98 IMAGE 1383489 5' similar to gb J04046 CALMODULIN (HUMAN), gb M19381 Mouse calmodulin (MOUSE),, mRNA sequence rxa00385 362 GB_EST32 AI726450 565 AI726450 BNLGHι5857 Six-day Cotton fiber Gossypium hirsutum cDNA 5' similar to Gossypium hirsutum 41 ,152 11-Jun-9 (AF015913) Skbl Hs [Homo sapiens], mRNA sequence GB_GSS4 AQ740856 768 AQ740856 HS_2274_A2_A07_T7C CIT Approved Human Genomic Sperm Library D Homo sapiens 41 ,360 16-Jul-99 Homo sapiens genomic clone Plate=2274 Col=14 Row=A, genomic survey sequence GB_PR1 HSPAIP 1587 X91809 H sapiens mRNA for GAIP protein Homo sapiens 36,792 29-MAR-1 rxa00388 1134 GB_BA1 MTY25D10 40838 Z95558 Mycobacterium tuberculosis H37Rv complete genome, segment 28/162 Mycobacterium 51 ,852 17-Jun-9 tuberculosis GB_BA1 MSGY224 40051 AD000004 Mycobacterium tuberculosis sequence from clone y224 Mycobacterium 51 ,852 03-DEC-1 tuberculosis GB_HTG1 AP000471 72466 AP000471 Homo sapiens chromosome 21 clone B2308H15 map 21q22 3, *** Homo sapiens 36,875 13-Sep-9 SEQUENCING IN PROGRESS * **, in unordered pieces rxa00427 909 GB_BA1 MSGY126 37164 AD000012 Mycobacterium tuberculosis sequence from clone y126 Mycobacterium 60,022 10-DEC-1 tuberculosis GB_BA1 MTY13D12 37085 Z80343 Mycobacterium tuberculosis H37Rv complete genome, segment 156/162 Mycobacterium 60,022 17-Jun-9 tuberculosis GB_HTG1 CEY48C3 270193 Z92855 Caenorhabditis elegans chromosome II clone Y48C3, ** * SEQUENCING IN Caenorhabditis elegans 28,013 29-MAY-1 PROGRESS *** , in unordered pieces rxa00483 1587 GB_PR2 HSAF001550 173882 AF001550 Homo sapiens chromosome 16 BAC clone CIT987SK-334D11 complete Homo sapiens 38,226 22-Aug-9 sequence GB_BA1 LLCPJW565 12828 Y12736 Lactococcus lactis cremons plasmid pJW565 DNA, abnM, abnR genes and Lactococcus lactis subsp 37,492 01-MAR- orfX cremoπs GB_HTG2 AC006754 206217 AC006754 Caenorhabditis elegans clone Y40B10, *** SEQUENCING IN PROGRESS " Caenorhabditis elegans 36,648 23-Feb-9 5 unordered pieces rxa00511 615 GB_PR3 HSE127C11 38423 Z74581 Human DNA sequence from cosmid E127C11 on chromosome 22q11 2-qter Homo sapiens 39,831 23-NOV-9 contains STS GB_PR3 HSE127C11 38423 Z74581 Human DNA sequence from cosmid E127C11 on chromosome 22q11 2-qter Homo sapiens 36,409 23-Nov-9 contains STS rxa00512 718 GB BA1 MTCY22G8 22550 Z95585 Mycobacterium tuberculosis H37Rv complete genome, segment 49/162 Mycobacterium 56,232 17-Jun-9 tuberculosis Table 4 (continued) GB_BA1 MSGLTA 1776 X60513 M smegmatis gltA gene for citrate synthase Mycobacterium smegmatis 56,143 20-Sep-91 GB_BA2 ECU73857 128824 U73857 Escherichia coli chromosome minutes 6-8 Escherichia coli 48,563 14-Jul-99 rxa00517 1164 GB_HTG2 AC006911 298804 AC006911 Caenorhabditis elegans clone Y94H6x, *** SEQUENCING IN PROGRESS *** , Caenorhabditis elegans 37,889 24-Feb-99 15 unordered pieces GBJHTG2 AC006911 298804 AC006911 Caenorhabditis elegans clone Y94H6x, *** SEQUENCING IN PROGRESS *** , Caenorhabditis elegans 37,889 24-Feb-99 15 unordered pieces GB_EST29 AI602158 481 AI602158 UI-R-AB0-vy-a-01-0-UI s2 UI-R-ABO Rattus norvegicus cDNA clone UI-R-ABO- Rattus norvegicus 40,833 21-Apr-99 vy-a-01-O-UI 3', mRNA sequence rxa00518 320 GB_BA2 ECU73857 128824 U73857 Escherichia coli chromosome minutes 6-8 Escherichia coli 49,688 14-Jul-99 GB_BA2 STU51879 8371 U51879 Salmonella typhimuπum propionate catabolism operon RpoN activator protein Salmonella typhimuπum 50,313 5-Aug-99 homolog (prpR), carboxyphosphonoenolpyruvate phosphonomutase homolog (prpB), citrate synthase homolog (prpC), prpD and prpE genes, complete cds GB_BA2 AE000140 12498 AE000140 Escherichia coli K-12 MG1655 section 30 of 400 of the complete genome Escherichia coli 49,688 12-NOV-9 rxa00606 2378 GB_EST32 AU068253 376 AU068253 AU068253 Rice callus Oryza sativa cDNA clone C12658_9A, mRNA sequence Oryza sativa 41 ,333 7-Jun-99 GB_EST13 AA363046 329 AA363046 EST72922 Ovary II Homo sapiens cDNA 5' end, mRNA sequence Homo sapiens 34,347 21-Apr-97 GB_EST32 AU068253 376 AU068253 AU068253 Rice callus Oryza sativa cDNA clone C12658_9A, mRNA sequence Oryza sativa 41 ,899 7-Jun-99 rxa00635 1860 GB_BA1 PAORF1 1440 X13378 Pseudomonas amyloderamosa DNA for ORF 1 Pseudomonas 53,912 14-Jul-95 amyloderamosa GB_BA1 PAORF1 1440 X13378 Pseudomonas amyloderamosa DNA for ORF 1 Pseudomonas 54,422 14-Jul-95 amyloderamosa rxa00679 1389 GB_PL2 AC010871 80381 AC010871 Arabidopsis thaliana chromosome III BAC T16011 genomic sequence, Arabidopsis thaliana 38,244 13-Nov-9 complete sequence GB_PL1 AT81 KBGEN 81493 X98130 A thaliana 81 kb genomic sequence Arabidopsis thaliana 36,091 12-MAR-1 GB_PL2 AC010871 80381 AC010871 Arabidopsis thaliana chromosome III BAC T16011 genomic sequence, Arabidopsis thaliana 37,135 13-NOV-9 complete sequence rxa00680 441 GB_PR3 AC004058 38400 AC004058 Homo sapiens chromosome 4 clone B241P19 map 4q25, complete sequence Homo sapiens 36,165 30-Sep-9 GB_PL1 AT81 KBGEN 81493 X98130 A thaliana 81 kb genomic sequence Arabidopsis thaliana 38,732 12-MAR-1 GB_PL1 AB026648 43481 AB026648 Arabidopsis thaliana genomic DNA, chromosome 3, P1 clone MLJ15, complete Arabidopsis thaliana 38,732 07-MAY-1 sequence rxa00682 2022 GB_HTG3 AC010325 197110 AC010325 Homo sapiens chromosome 19 clone CITB-E1_2568A17, " * SEQUENCING IN Homo sapiens 37,976 15-Sep-9 PROGRESS *** , 40 unordered pieces GB_HTG3 AC010325 197110 AC010325 Homo sapiens chromosome 19 clone CITB-E1_2568A17, * * * SEQUENCING IN Homo sapiens 37,976 15-Sep-9 PROGRESS *** , 40 unordered pieces GB_PR4 AC008179 181745 AC008179 Homo sapiens clone NH0576F01 , complete sequence Homo sapiens 37,143 28-Sep-99 Table 4 (continued) rxa00683 1215 GB_BA2 AE000896 10707 AE000896 Methanobacteriu thermoautotrophicum from bases 1189349 to 1200055 Methanobacteπum 38,429 15-Nov-97 (section 102 of 1 8) of the complete genome thermoautotrophicum GBJN1 DMBR7A4 212734 AL109630 Drosophila melanogaster clone BACR7A4 Drosophila melanogaster 36,454 30-Jul-99 GB_EST35 AV163010 273 AV163010 AV163010 Mus musculus head C57BL/6J 13-day embryo Mus musculus cDNA Mus musculus 41 ,758 8-Jul-99 clone 3110006J22, mRNA sequence rxa00686 927 GB_HTG2 HSDJ137K2 190223 AL049820 Homo sapiens chromosome 6 clone RP1-137K2 map q25 1-25 3, *** Homo sapiens 38,031 03-DEC-1 SEQUENCING IN PROGRESS *** , in unordered pieces GBJHTG2 HSDJ137K2 190223 AL049820 Homo sapiens chromosome 6 clone RP1-137K2 map q25 1-25 3, ** * Homo sapiens 38,031 03-DEC-1 SEQUENCING IN PROGRESS *** , in unordered pieces GB_EST12 AA284399 431 AA284399 zs57b04 r1 NCI_CGAP_GCB1 Homo sapiens cDNA clone IMAGE 701551 5', Homo sapiens 39,205 14-Aug-97 mRNA sequence rxa00700 927 GB_EST34 AI785570 454 AI785570 uj44d03 x1 Sugano mouse liver m a Mus musculus cDNA clone Mus musculus 41 ,943 2-Jul-99 IMAGE 1922789 3' similar to gb Z28407 60S RIBOSOMAL PROTEIN L8 (HUMAN),, mRNA sequence GB_EST25 AI256147 684 AI256147 uι95e12 x1 Sugano mouse liver m a Mus musculus cDNA clone Mus musculus 40,791 12-Nov-9 IMAGE 1890190 3' similar to gb Z28407 60S RIBOSOMAL PROTEIN L8 (HUMAN),, mRNA sequence GB_BA1 CARCG12 2079 X14979 C aurantiacus reaction center genes 1 and 2 Chloroflexus aurantiacus 37,721 23-Apr-91 rxa00703 2409 GB_BA1 SC7H2 42655 AL109732 Streptomyces coelicolor cosmid 7H2 Streptomyces coelicolor 56,646 2-Aug-99 A3(2) GB_BA1 MTCY274 39991 Z74024 Mycobacterium tuberculosis H37Rv complete genome, segment 126/162 Mycobacterium 37,369 19-Jun-98 tuberculosis GB_BA2 REU60056 2520 U60056 Ralstonia eutropha formate dehydrogenase-like protein (cbbBc) gene, complete Ralstonia eutropha 51 ,087 16-OCT-1 cds rxa00705 1038 GB_GSS15 AQ604477 505 AQ604477 HS_2116_B1_G07_MR CIT Approved Human Genomic Sperm Library D Homo Homo sapiens 39,617 10-Jun-99 sapiens genomic clone Plate=2116 Col=13 Row=N, genomic survey sequence GB_EST11 AA224340 443 AA224340 zr14e07 s1 Stratagene hNT neuron (#937233) Homo sapiens cDNA clone Homo sapiens 35,129 11-MAR-1 IMAGE 648804 3', mRNA sequence GB_EST5 N30648 291 N30648 yw77b02 s1 Soares_placenta_8to9weeks_2NbHP8to9W Homo sapiens cDNA Homo sapiens 43,986 5-Jan-96 clone IMAGE 258219 3', mRNA sequence rxa00782 1005 GB_BA1 MTCY10D7 39800 Z79700 Mycobacterium tuberculosis H37Rv complete genome, segment 44/162 Mycobacterium 63,327 17-Jun-98 tuberculosis GB_BA1 MLCL373 37304 AL035500 Mycobacterium leprae cosmid L373 Mycobacterium leprae 62,300 27-Aug-9 GB_BA2 AF 128399 2842 AF128399 Pseudomonas aeruginosa succinyl-CoA synthetase beta subunit (sucC) and Pseudomonas aeruginosa 53,698 25-MAR-1 succinyl-CoA synthetase alpha subunit (sucD) genes, complete cds rxa00783 1395 GBJHTG2 AC008158 118792 AC008158 Homo sapiens chromosome 17 clone hRPK 42_F_20 map 17, * ** Homo sapiens 35,135 28-Jul-99 SEQUENCING IN PROGRESS *** , 14 unordered pieces GB_HTG2 AC008158 118792 AC008158 Homo sapiens chromosome 17 clone hRPK 42_F_20 map 17, ** * Homo sapiens 35,135 28-Jul-99 SEQUENCING IN PROGRESS *** , 14 unordered pieces GB_PR3 AC005017 137176 AC005017 Homo sapiens BAC clone GS214N13 from 7p14-p15, complete sequence Homo sapiens 35,864 8-Aug-98 rxa00794 1128 GB_BA1 MTV017 67200 AL021897 Mycobacterium tuberculosis H37Rv complete genome, segment 48/162 Mycobacterium 40,331 24-Jun-99 tuberculosis Table 4 (continued) GB_BA1 MLCB1222 34714 AL049491 Mycobacterium leprae cosmid B1222 Mycobacterium leprae 61 ,170 27-Aug-99 GB PR2 HS151 B14 128942 Z82188 Human DNA sequence from clone 151 B14 on chromosome 22 Contains Homo sapiens 37,455 16-Jun-99 SOMATOSTATIN RECEPTOR TYPE 3 (SS3R) gene.pseudogene similar to πbosomal protein L39.RAC2 (RAS-RELATED C3 BOTULINUM TOXIN SUBSTRATE 2 (P21-RAC2)) gene ESTs, STSs, GSSs and CpG islands, complete sequence rxa00799 1767 GB PL2 AF016327 616 AF016327 Hordeum vulgare Barperml (perml ) mRNA, partial cds Hordeum vulgare 41 ,311 01-OCT-1 GB HTG2 HSDJ319M7 128208 AL079341 Homo sapiens chromosome 6 clone RP1-319M7 map p21 1-21 3, ** * Homo sapiens 36,845 30-Nov-99 SEQUENCING IN PROGRESS ***, in unordered pieces GB HTG2 HSDJ319M7 128208 AL079341 Homo sapiens chromosome 6 clone RP1-319M7 map p21 1-21 3, *** Homo sapiens 36,845 30-NOV-99 SEQUENCING IN PROGRESS ***, in unordered pieces rxa00800 1227 GB BA1 MTV022 13025 AL021925 Mycobacterium tuberculosis H37Rv complete genome, segment 100/162 Mycobacterium 63,101 17-Jun-98 tuberculosis GB_BA1 AB019513 4417 AB019513 Streptomyces coelicolor genes for alcohol dehydrogenase and ABC Streptomyces coelicolor 41 ,312 13-Nov-98 transporter, complete cds GB_PL1 SCSFAARP 7008 X68020 S cerevisiae SFA and ARP genes Saccharomyces cerevisiae 36,288 29-NOV-9 rxa00825 1056 GB_BA1 MTY15C10 33050 Z95436 Mycobacterium tuberculosis H37Rv complete genome, segment 154/162 Mycobacterium 39,980 17-Jun-98 tuberculosis GB_BA1 MLCB2548 38916 AL023093 Mycobacterium leprae cosmid B2548 Mycobacterium leprae 39,435 27-Aug-9 GB_BA2 AF169031 1141 AF169031 Xanthomonas oryzae pv oryzae putative sugar nucleotide Xanthomonas oryzae pv 46,232 14-Sep-9 epimerase/dehydratase gene, partial cds oryzae rxa00871 rxa00872 1077 GBJN1 CEF23H12 35564 Z74472 Caenorhabditis elegans cosmid F23H12, complete sequence Caenorhabditis elegans 34,502 08-OCT-1 GB HTG2 AC007263 167390 AC007263 Homo sapiens chromosome 14 clone BAC 79J20 map 14q31 , *** Homo sapiens 35,714 24-MAY-1 SEQUENCING IN PROGRESS ***, 5 ordered pieces GB_HTG2 AC007263 167390 AC007263 Homo sapiens chromosome 14 clone BAC 79J20 map 14q31 , *** Homo sapiens 35,714 24-MAY-1 SEQUENCING IN PROGRESS ***, 5 ordered pieces rxa00879 2241 GB BA1 MTV049 40360 AL022021 Mycobacterium tuberculosis H37Rv complete genome, segment 81/162 Mycobacterium 36,981 19-Jun-98 tuberculosis GB_PL2 CDU236897 1827 AJ236897 Candida dubliniensis ACT1 gene, exons 1-2 Candida dubliniensis 38,716 1-Sep-99 GB_PL1 CAACT1A 3206 X16377 Candida albicans actl gene for actin Candida albicans 36,610 10-Apr-93 rxa00909 955 GB_BA2 AF010496 189370 AF010496 Rhodobacter capsulatus strain SB1003, partial genome Rhodobacter capsulatus 51 ,586 12-MAY-1 GB_BA1 RMPHA 7888 X93358 Rhizobium meliloti pha[A,B,C,D E,F,G] genes Sinorhizobium meliloti 48,367 12-MAR-1 GB_EST16 C23528 317 C23528 C23528 Japanese flounder spleen Paralichthys ohvaceus cDNA clone HB5(2), P Paarraalicchhtthhyyss oolliivvaacceeuuss 41 ,640 28-Sep-9 mRNA sequence rxa00913 2118 GB HTG2 AC007734 188267 AC007734 Homo sapiens chromosome 18 clone hRPK 44_0_1 map 18, *** Homo sapiens 34,457 5-Jun-99 SEQUENCING IN PROGRESS ***, 18 unordered pieces Table 4 (continued) GB HTG2 AC007734 188267 AC007734 Homo sapiens chromosome 18 clone hRPK 44_0_1 map 18, *** Homo sapiens 34,457 5-Jun-99 SEQUENCING IN PROGRESS * ** , 18 unordered pieces GB EST18 AA709478 406 AA709478 vv34a05 Stratagene mouse heart (#937316) Mus musculus cDNA clone Mus musculus 42,065 24-DEC-1 IMAGE 1224272 5', mRNA sequence rxa00945 1095 GB HTG4 AC010351 220710 AC010351 Homo sapiens chromosome 5 clone CITB-H1_2022B6, *** SEQUENCING IN Homo sapiens 36,448 31-OCT-1 PROGRESS ** * , 68 unordered pieces GB HTG4 AC010351 220710 AC010351 Homo sapiens chromosome 5 clone CITB-H1_2022B6, * ** SEQUENCING IN Homo sapiens 36,448 31-OCT-1 PROGRESS * ** , 68 unordered pieces GB BA1 MTCY05A6 38631 Z96072 Mycobacterium tuberculosis H37Rv complete genome, segment 120/162 Mycobacterium 36,218 17-Jun-98 tuberculosis rxa00965 rxa00999 1575 GB_PAT E13660 1916 E13660 gDNA encoding 6-phosphogluconate dehydrogenase Corynebacterium 98,349 24-Jun-98 glutamicum GB BA1 MTCY359 36021 Z83859 Mycobacterium tuberculosis H37Rv complete genome, segment 84/162 Mycobacterium 38,520 17-Jun-98 tuberculosis GB_BA1 MLCB1788 39228 AL008609 Mycobacterium leprae cosmid B1788 Mycobacterium leprae 64,355 27-Aug-9 rxa01015 442 GB_BA1 MTV008 63033 AL021246 Mycobacterium tuberculosis H37Rv complete genome, segment 108/162 Mycobacterium 39,860 17-Jun-98 tuberculosis GB BA1 MTV008 63033 AL021246 Mycobacterium tuberculosis H37Rv complete genome, segment 108/162 Mycobacterium 39,120 17-Jun-98 tuberculosis rxa01025 1119 GB_BA1 SC7A1 32039 AL034447 Streptomyces coelicolor cosmid 7A1 Streptomyces coelicolor 55,287 15-DEC- GB_BA1 MSGB1723CS 38477 L78825 Mycobacterium leprae cosmid B1723 DNA sequence Mycobacterium leprae 56,847 15-Jun-96 GB_BA1 MLCB637 44882 Z99263 Mycobacterium leprae cosmid B637 Mycobacterium leprae 56,676 17-Sep-9 rxa01048 1347 GB_BA2 AF017444 3067 AF017444 Sinorhizobium meliloti NADP-dependent malic enzyme (tme) gene, complete Sinorhizobium meliloti 53,660 2-Nov-97 cds GB_BA1 BSUB0013 218470 Z99116 Bacillus subtihs complete genome (section 13 of 21 ) from 2395261 to Bacillus subtihs 37,255 26-Nov-9 2613730 GB_VI HSV2HG52 154746 Z86099 Herpes simplex virus type 2 (strain HG52), complete genome human herpesvirus 2 38,081 04-DEC-1 rxa01049 1605 GB_HTG2 AC002518 131855 AC002518 Homo sapiens chromosome X clone bWXD20, *** SEQUENCING IN Homo sapiens 35,647 2-Sep-97 PROGRESS "*, 11 unordered pieces GB_HTG2 AC002518 131855 AC002518 Homo sapiens chromosome X clone bWXD20, *** SEQUENCING IN Homo sapiens 35,647 2-Sep-97 PROGRESS ** * , 11 unordered pieces GB_HTG2 AC002518 131855 AC002518 Homo sapiens chromosome X clone bWXD20, *** SEQUENCING IN Homo sapiens 26,180 2-Sep-97 PROGRESS ** *, 11 unordered pieces rxa01077 1494 GB_PR3 HSDJ653C5 85237 AL049743 Human DNA sequence from clone 653C5 on chromosome 1p21 3-22 3 Homo sapiens 36,462 23-Nov-9 Contains CA repeat(D1S435), STSs and GSSs, complete sequence GB_BA1 ECU29579 72221 U29579 Escherichia coli K-12 genome, approximately 61 to 62 minutes Escherichia coli 41 ,808 l-Jul-95 GB_BA1 ECU29579 72221 U29579 Escherichia coli K-12 genome, approximately 61 to 62 minutes Escherichia coli 36,130 l-Jul-95 rxa01089 873 GB GSS8 AQ044021 387 AQ044021 CIT-HSP-2318C18 TR CIT-HSP Homo sapiens genomic clone 2318C18, Homo sapiens 36,528 14-Jul-98 genomic survey sequence Table 4 (continued) GB_GSS8 AQ042907 392 AQ042907 CIT-HSP-2318D17 TR CIT-HSP Homo sapiens genomic clone 2318D17, Homo sapiens 35,969 14-Jul-98 genomic survey sequence GB_GSS8 AQ044021 387 AQ044021 CIT-HSP-2318C18 TR CIT-HSP Homo sapiens genomic clone 2318C18, Homo sapiens 44,545 14-Jul-98 genomic survey sequence rxa01093 1554 GB_BA1 CORPYKI 2795 L27126 Corynebacterium pyruvate kinase gene, complete cds Corynebacterium 100,000 07-DEC-1 glutamicum GB_BA1 MTCY01 B2 35938 Z95554 Mycobacterium tuberculosis H37Rv complete genome, segment 72/162 Mycobacterium 63,771 17-Jun-98 tuberculosis GB_BA1 MIU65430 1439 U65430 Mycobacterium intracellulare pyruvate kinase (pykF) gene, complete cds Mycobacterium 67,061 23-DEC-1 intracellulare rxa01099 948 GB_BA2 AF045998 780 AF045998 Corynebacterium glutamicum inositol monophosphate phosphatase (impA) Corynebacterium 99,615 19-Feb-9 gene, complete cds glutamicum GB BA2 AF051846 738 AF051846 Corynebacteπum glutamicum phosphoπbosylformιmιno-5-amιno-1- Corynebacterium 100,000 12-MAR-1 phosphorιbosyl-4- imidazolecarboxamide isomerase (hisA) gene, complete glutamicum cds GB GSS1 FR0005503 619 Z89313 F rubnpes GSS sequence, clone 079B16aE8, genomic survey sequence Fugu rubnpes 37,785 01-MAR-1 rxa01111 541 GB_PR3 AC004063 177014 AC004063 Homo sapiens chromosome 4 clone B32I8, complete sequence Homo sapiens 35,835 IO-Jul-98 GB_PR3 HS1178121 62268 AL109852 Human DNA sequence from clone RP5-1178121 on chromosome X, complete Homo sapiens 37,873 01-DEC-1 sequence GB_HTG3 AC009301 163369 AC009301 Homo sapiens clone NH0062F14, *** SEQUENCING IN PROGRESS ***, 5 Homo sapiens 37,240 13-Aug-9 unordered pieces rxa01130 687 GB_HTG3 AC009444 164587 AC009444 Homo sapiens clone 1_0_3, * ** SEQUENCING IN PROGRESS *** , 8 Homo sapiens 38,416 22-Aug-9 unordered pieces GB_HTG3 AC009444 164587 AC009444 Homo sapiens clone 1_0_3, ** * SEQUENCING IN PROGRESS ***, 8 Homo sapiens 38,416 22-Aug-9 unordered pieces GBJN1 DMC66A1 34127 AL031227 Drosophila melanogaster cosmid 66A1 Drosophila melanogaster 38,416 05-OCT-1 rxa01193 1572 GB_BA1 CGAS019 1452 X76875 C glutamicum (ASO 19) ATPase beta-subunit gene Corynebacterium 99,931 27-OCT-1 glutamicum EM_PAT E09634 1452 E09634 Brevibacterium flavum UncD gene whose gene product is involved in Corynebacterium 99,242 07-OCT-1 glutamicum (Rel 52, Created) GB_BA1 MLU15186 36241 U15186 Mycobacterium leprae cosmid L471 Mycobacterium leprae 39,153 09-MAR-1 rxa01194 495 EM_PAT E09634 1452 E09634 Brevibacterium flavum UncD gene whose gene product is involved in Corynebacterium 100,000 07-OCT-1 glutamicum (Rel 52, Created) GB_BA1 CGAS019 1452 X76875 C glutamicum (ASO 19) ATPase beta-subunit gene Corynebacterium 100,000 27-OCT-1 glutamicum GB VI HEPCRE4B 414 X60570 Hepatitis C genomic RNA for putative envelope protein (RE4B isolate) Hepatitis C virus 36,769 5-Apr-92 rxa01200 Table 4 (continued) rxa01201 1764 GB_BA1 SLATPSYNA 8560 Z22606 S lividans i protein and ATP synthase genes Streptomyces lividans 66,269 01-MAY-1 GB_BA1 MTCY373 35516 Z73419 Mycobacterium tuberculosis H37Rv complete genome, segment 57/162 Mycobacterium 65,437 17-Jun-98 tuberculosis GB_BA1 MLU15186 36241 U15186 Mycobacterium leprae cosmid L471 Mycobacterium leprae 39,302 09-MAR-1 rxa01202 1098 GB_BA1 SLATPSYNA 8560 Z22606 S lividans i protein and ATP synthase genes Streptomyces lividans 57,087 01-MAY-1 GB_BA1 SLATPSYNA 8560 Z22606 S lividans i protein and ATP synthase genes Streptomyces lividans 38,298 01-MAY-1 GB_BA1 MCSQSSHC 5538 Y09978 M capsulatus orfx, orfy, orfz, sqs and she genes Methylococcus capsulatus 37,626 26-MAY-1 rxa01204 933 GB_PL1 AP000423 154478 AP000423 Arabidopsis thaliana chloroplast genomic DNA, complete sequence, Chloroplast Arabidopsis 38,395 15-Sep-99 strain Columbia thaliana GB_HTG6 AC009762 164070 AC009762 Homo sapiens clone RP11-114116, * " SEQUENCING IN PROGRESS " 39 Homo sapiens 35,459 04-DEC-1 unordered pieces GB_HTG6 AC009762 164070 AC009762 Homo sapiens clone RP11-114116, ** * SEQUENCING IN PROGRESS ** 39 Homo sapiens 36,117 04-DEC-1 unordered pieces rxa01216 1124 GB_BA1 MTCY10G2 38970 Z92539 Mycobacterium tuberculosis H37Rv complete genome, segment 47/162 Mycobacterium 39,064 17-Jun-98 tuberculosis GB_BA2 AF017435 4301 AFO 17435 Methylobacteπum extorquens methanol oxidation genes, glmU-like gene Methylobacteπum 42,671 10-MAR-1 partial cds, and orfL2, orfL1 , orfR genes, complete cds extorquens GB_BA1 CCRFLBDBA 4424 M69228 C crescentus flagellar gene promoter region Caulobacter crescentus 41 ,054 26-Apr-93 rxa01225 1563 GB_BA2 AF058302 25306 AF058302 Streptomyces roseofulvus frenolicin biosynthetic gene cluster, complete Streptomyces roseofulvus 36,205 2-Jun-98 sequence GB HTG3 AC007301 165741 AC007301 Drosophila melanogaster chromosome 2 clone BACR04B09 (D576) RPCI-98 Drosophila melanogaster 39,922 17-Aug-99 04 B 9 map 43E12-44F1 strain y, en bw sp, ** * SEQUENCING IN PROGRESS ** *, 150 unordered pieces GBJHTG3 AC007301 165741 AC007301 Drosophila melanogaster chromosome 2 clone BACR04B09 (D576) RPCI-98 Drosophila melanogaster 39,922 17-Aug-99 04 B 9 map 43E12-44F1 strain y, en bw sp, ** * SEQUENCING IN PROGRESS *** , 150 unordered pieces rxa01227 444 GB_BA1 SERFDXA 3869 M61119 Saccharopolyspora erythraea ferredoxin (fdxA) gene, complete cds Saccharopolyspora 64,908 13-MAR-1 erythraea GB_BA1 MTV005 37840 AL010186 Mycobacterium tuberculosis H37Rv complete genome, segment 51/162 Mycobacterium 62,838 17-Jun-98 tuberculosis GB_BA1 MSGY348 40056 AD000020 Mycobacterium tuberculosis sequence from clone y348 Mycobacterium 61 ,712 10-DEC-1 tuberculosis rxa01242 900 GB_PR3 AC005697 174503 AC005697 Homo sapiens chromosome 17, clone hRPK 138_P_22, complete sequence Homo sapiens 35,373 09-OCT-1 GB_HTG3 AC010722 160723 AC010722 Homo sapiens clone NH0122L09, *** SEQUENCING IN PROGRESS ***, 2 Homo sapiens 39,863 25-Sep-99 unordered pieces GB HTG3 AC010722 160723 AC010722 Homo sapiens clone NH0122L09, *** SEQUENCING IN PROGRESS *** , 2 Homo sapiens 39,863 25-Sep-99 unordered pieces Table 4 (continued) rxa01243 1083 GB GSS10 AQ255057 583 AQ255057 mgxb0008N01r CUGI Rice Blast BAC Library Magnaporthe gπsea genomic Magnaporthe grisea 38,722 23-OCT-1 clone mgxb0008N01 r, genomic survey sequence GBJN1 CEK05D4 19000 Z92804 Caenorhabditis elegans cosmid K05D4, complete sequence Caenorhabditis elegans 35,448 23-NOV-98 GBJN1 CEK05D4 19000 Z92804 Caenorhabditis elegans cosmid K05D4, complete sequence Caenorhabditis elegans 35,694 23-Nov-98 rxa01259 981 GB BA1 CGLPD 1800 Y16642 Corynebacterium glutamicum Ipd gene, complete CDS Corynebacterium 100,000 1-Feb-99 glutamicum GB_HTG4 AC010567 143287 AC010567 Drosophila melanogaster chromosome 3L/69C1 clone RPCI98-11 N6, ** * Drosophila melanogaster 37,178 16-OCT-1 SEQUENCING IN PROGRESS ***, 70 unordered pieces GB_HTG4 AC010567 143287 AC010567 Drosophila melanogaster chromosome 3L/69C1 clone RPCI98-11N6, Drosophila melanogaster 37,178 16-OCT-1 ♦ "SEQUENCING IN PROGRESS *** , 70 unordered pieces rxa01262 1284 GB BA2 AF172324 14263 AF172324 Eschenchia coli GalF (galF) gene, partial cds, 0-antιgen repeat unit transporter Eschenchia coli 59,719 29-OCT-1 Wzx (wzx), WbnA (wbnA), 0-antιgen polymerase Wzy (wzy), WbnB (wbnB), WbnC (wbnC), WbnD (wbnD), WbnE (wbnE), UDP-Glc-4-epιmerase GalE (galE), 6-phosphogluconate dehydrogenase Gnd (gnd), UDP-Glc-6- dehydrogenase Ugd (ugd), and WbnF (wbnF) genes, complete cds, and chain length determinant Wzz (wzz) gene, partial cds GB_BA2 ECU78086 4759 U78086 Eschenchia coli hypothetical urιdιne-5'-dιphosphoglucose dehydrogenase (ugd) Eschenchia coli 59,735 5-Nov-97 and O-chain length regulator (wzz) genes, complete cds GB BA1 D90841 20226 D90841 E coli genomic DNA, Kohara clone #351 (45 1-45 5 mm ) Eschenchia coli 37,904 21-MAR-1 rxa01311 870 GB_PR3 AC004103 144368 AC004103 Homo sapiens Xp22 BAC GS-619J3 (Genome Systems Human BAC library) Homo sapiens 37,340 18-Apr-98 complete sequence GB_HTG3 AC007383 215529 AC007383 Homo sapiens clone NH0310K15, * * * SEQUENCING IN PROGRESS *** , 4 Homo sapiens 36,385 25-Sep-9 unordered pieces GB_HTG3 AC007383 215529 AC007383 Homo sapiens clone NH0310K15, *** SEQUENCING IN PROGRESS ***, 4 Homo sapiens 36,385 25-Sep-9 unordered pieces rxa01312 2142 GB_BA2 AE000487 13889 AE000487 Eschenchia coli K-12 MG1655 section 377 of 400 of the complete genome Eschenchia coli 39,494 12-Nov-9 GB_BA1 MTV016 53662 AL021841 Mycobacterium tuberculosis H37Rv complete genome, segment 143/162 Mycobacterium 46,252 23-Jun-99 tuberculosis GB_BA1 U00022 36411 U00022 Mycobacterium leprae cosmid L308 Mycobacterium leprae 46,368 01-MAR-1 rxa01325 795 GB_HTG4 AC009245 215767 AC009245 Homo sapiens chromosome 7, *" SEQUENCING IN PROGRESS ***, 24 Homo sapiens 36,016 2-NOV-99 unordered pieces GB_HTG4 AC009245 215767 AC009245 Homo sapiens chromosome 7, *** SEQUENCING IN PROGRESS ***, 24 Homo sapiens 36,016 2-NOV-99 unordered pieces GB_HTG4 AC009245 215767 AC009245 Homo sapiens chromosome 7, *** SEQUENCING IN PROGRESS ***, 24 Homo sapiens 39,618 2-NOV-99 unordered pieces rxa01332 576 GB HTG6 AC007186 225851 AC007186 Drosophila melanogaster chromosome 2 clone BACR03D06 (D569) RPCI-98 Drosophila melanogaster 35,366 07-DEC-1 03 D 6 map 32A-32A strain y, en bw sp, *** SEQUENCING IN PROGRESS 91 unordered pieces GB HTG6 AC007147 202291 AC007147 Drosophila melanogaster chromosome 2 clone BACR19N18 (D572) RPCI-98 Drosophila melanogaster 35,366 07-DEC-1 19 N 18 map 32A-32A strain y, en bw sp, *** SEQUENCING IN PROGRESS *** , 22 unordered pieces Table 4 (continued) GBJHTG3 AC010207 207890 AC010207 Homo sapiens clone RPCI11-375120, *** SEQUENCING IN PROGRESS 25 Homo sapiens 34,821 16-Sep-99 unordered pieces rxa01350 1107 GB_BA2 AF109682 990 AF109682 Aquaspiπllum arcticum malate dehydrogenase (MDH) gene, complete cds Aquaspiπllum arcticum 58,487 19-OCT-1 GB_HTG2 AC006759 103725 AC006759 Caenorhabditis elegans clone Y40G12, *** SEQUENCING IN PROGRESS ** Caenorhabditis elegans 37,963 25-Feb-99 8 unordered pieces GB_HTG2 AC006759 103725 AC006759 Caenorhabditis elegans clone Y40G12, " * SEQUENCING IN PROGRESS ** Caenorhabditis elegans 37,963 25-Feb-99 8 unordered pieces rxa01365 1497 GB_BA1 MTY20B11 36330 Z95121 Mycobacterium tuberculosis H37Rv complete genome, segment 139/162 Mycobacterium 38,011 17-Jun-98 tuberculosis GB_BA1 XANXANAB 3410 M83231 Xanthomonas campestns phosphoglucomutase and phosphomannomutase Xanthomonas campestns 47,726 26-Apr-93 (xanA) and phosphomannose isomerase and GDP-mannose pyrophosphorylase (xanB) genes, complete cds GB_GSS10 AQ194038 697 AQ194038 RPCI11-47D24 TJ RPCI-11 Homo sapiens genomic clone RPCI-11-47D24, Homo sapiens 36,599 20-Apr-99 genomic survey sequence rxa01369 1305 GB_BA1 MTY20B11 36330 Z95121 Mycobacterium tuberculosis H37Rv complete genome, segment 139/162 Mycobacterium 36,940 17-Jun-98 tuberculosis GB_GSS3 B10037 974 B10037 T27A19-T7 TAMU Arabidopsis thaliana genomic clone T27A19, genomic Arabidopsis thaliana 35,284 14-MAY-1 survey sequence GB_GSS3 B09549 1097 B09549 T21A19-T7 1 TAMU Arabidopsis thaliana genomic clone T21A19, genomic Arabidopsis thaliana 38,324 14-MAY-1 survey sequence rxa01377 1209 GB_BA1 MTCY71 42729 Z92771 Mycobacterium tuberculosis H37Rv complete genome, segment 141/162 Mycobacterium 39,778 10-Feb-99 tuberculosis GB_HTG5 AC007547 262181 AC007547 Homo sapiens clone RP11-252018, WORKING DRAFT SEQUENCE, 121 Homo sapiens 32,658 16-Nov-9 unordered pieces GB_HTG5 AC007547 262181 AC007547 Homo sapiens clone RP11-252018, WORKING DRAFT SEQUENCE, 121 Homo sapiens 38,395 16-Nov-9 unordered pieces rxa01392 1200 GB BA2 AF072709 8366 AF072709 Streptomyces lividans amphfiable element AUD4 putative Streptomyces lividans 55,221 δ-Jul-98 transcriptional regulator, putative ferredoxin, putative cytochrome P450 oxidoreductase, and putative oxidoreductase genes, complete cds, and unknown genes GB_BA1 CGLYSEG 2374 X96471 C glutamicum lysE and lysG genes Corynebacterium 100,000 24-Feb-97 glutamicum GB_PR4 AC005906 185952 AC005906 Homo sapiens 12p13 3 BAC RPCI11-429A20 (Roswell Park Cancer Homo sapiens 36,756 30-Jan-99 Institute Human BAC Library) complete sequence rxa01436 1314 GB_BA1 CGPTAACKA 3657 X89084 C glutamicum pta gene and ackA gene Corynebacterium 100,000 23-MAR-1 glutamicum GB_BA1 D90861 14839 D90861 E coli genomic DNA, Kohara clone #405(52 0-52 3 mm ) Eschenchia coli 53,041 29-MAY-1 GB_PAT E02087 1200 E02087 DNA encoding acetate kinase protein form Eschenchia coli Eschenchia coli 54,461 29-Sep-97 rxa01468 948 GB_GSS1 HPU60627 280 U60627 Hehcobacter pylori feoB- ke DNA sequence, genomic survey sequence Helicobacter pylori 39,286 9-Apr-97 GB ^ EST31 AI701691 349 AI701691 we81c04 x1 Soares_NFL_T_GBC_S1 Homo sapiens cDNA clone Homo sapiens 39,412 3-Jun-99 IMAGE 2347494 3' similar to gb L19686_rna1 MACROPHAGE MIGRATION INHIBITORY FACTOR (HUMAN),, mRNA sequence Table 4 (continued) GB EST15 AA480256 389 AA480256 ne31f04 s1 NCI_CGAP_Co3 Homo sapiens cDNA clone IMAGE 898975 3' Homo sapiens 39,574 14-Aug-97 similar to gb L19686_rna1 MACROPHAGE MIGRATION INHIBITORY FACTOR (HUMAN),, mRNA sequence rxa01478 1959 GB_BA1 SCI51 40745 AL109848 Streptomyces coelicolor cosmid 151 Streptomyces coelicolor 54,141 16-Aug-99 A3(2) GB_BA1 SCE36 12581 AL049763 Streptomyces coelicolor cosmid E36 Streptomyces coelicolor 38,126 05-MAY-1 GB BA1 CGU43535 2531 U43535 Corynebacterium glutamicum multidrug resistance protein (cmr) gene, Corynebacterium 41 ,852 9-Apr-97 complete cds glutamicum rxa01482 1998 GB_BA1 SC6G4 41055 AL031317 Streptomyces coelicolor cosmid 6G4 Streptomyces coelicolor 62,149 20-Aug-98 GB BA1 U00020 36947 U00020 Mycobacterium leprae cosmid B229 Mycobacterium leprae 38,303 01-MAR-1 GB BA1 MTCY77 22255 Z95389 Mycobacterium tuberculosis H37Rv complete genome, segment 146/162 Mycobacterium 38,179 18-Jun-98 tuberculosis rxa01534 rxa01535 1530 GB_BA1 MLCB1222 34714 AL049491 Mycobacterium leprae cosmid B1222 Mycobacterium leprae 66,208 27-Aug-99 GB_BA1 MTV017 67200 AL021897 Mycobacterium tuberculosis H37Rv complete genome, segment 48/162 Mycobacterium 38,553 24-Jun-99 tuberculosis GB_BA1 PAU72494 4368 U72494 Pseudomonas aeruginosa fumarase (fumC) and Mn superoxide dismutase Pseudomonas aeruginosa 52,690 23-OCT-1 (sodA) genes, complete cds rxa01550 1635 GB_BA1 D90907 132419 D90907 Synechocystis sp PCC6803 complete genome, 9/27, 1056467-1188885 Synechocystis sp 56,487 7-Feb-99 GB IN2 AF073177 9534 AF073177 Drosophila melanogaster glycogen phosphorylase (GlyP) gene, complete cds Drosophila melanogaster 55,100 1-Jul-99 GBJN2 AF073179 3159 AF073179 Drosophila melanogaster glycogen phosphorylase (Glp1) mRNA, complete cds Drosophila melanogaster 56,708 27-Apr-99 rxa01562 rxa01569 1482 GB_BA1 D78182 7836 D78182 Streptococcus mutans DNA for dTDP-rhamnose synthesis pathway, complete Streptococcus mutans 44,050 5-Feb-99 cds GB_BA2 AF079139 4342 AF079139 Streptomyces venezuelae pikCD operon, complete sequence Streptomyces venezuelae 38,587 28-OCT-1 GB_BA2 AF087022 1470 AF087022 Streptomyces venezuelae cytochrome P450 monooxygenase (picK) gene, Streptomyces venezuelae 38,621 15-OCT-1 complete cds rxa01570 978 GB_BA1 MTCY63 38900 Z96800 Mycobacterium tuberculosis H37Rv complete genome, segment 16/162 Mycobacterium 59,035 17-Jun-98 tuberculosis GB BA2 AF097519 4594 AF097519 Klebsiella pneumoniae dTDP-D-glucose 4,6 dehydratase (r lB), glucose-1- Klebsiella pneumoniae 59,714 4-Nov-98 phosphate thymidylyl transferase (rmlA), dTDP-4-keto-L-rhamnose reductase (rmlD), dTDP-4-keto-6-deoxy-D-glucose 3,5-epιmerase (rmlC), and rhamnosyl transferase (wbbL) genes, complete cds Table 4 (continued) GB_BA2 NGOCPSPS 8905 L09189 Neisseπa menmgitidis dTDP-D-glucose 4,6-dehydratase (rfbB), glucose-1- Neisseπa meningitidis 58,384 30-Jul-96 phosphate thymidyl transferase (rfbA) and rfbC genes, complete cds and UPD- glucose-4-epιmerase (galE) pseudogene rxa01571 723 GB_BA1 AB01 1413 12070 AB011413 Streptomyces gπseus genes for Orf2, Orf3, Orf4, Orf5, AfsA, Orf8, partial and Streptomyces gπseus 57,500 7-Aug-98 complete cds GB_BA1 AB01 1413 12070 AB011413 Streptomyces gnseus genes for Orf2, Orf3, Orf4, Orf5, AfsA, Orf8, partial and Streptomyces gπseus 35,655 7-Aug-98 complete cds rxa01572 615 GB_BA1 AB011413 12070 AB011413 Streptomyces gnseus genes for Orf2, Orf3, Orf4, Orf5, AfsA, Orf8, partial and Streptomyces gnseus 57,843 7-Aug-98 complete cds GB_BA1 AB011413 12070 AB011413 Streptomyces gnseus genes for Orf2, Orf3, Orf4, Orf5, AfsA, Orfβ, partial and Streptomyces gnseus 38,119 7-Aug-98 complete cds rxa01606 2799 GB_VI CFU72240 4783 U72240 Choπstoneura fumiferana nuclear polyhedrosis virus ETM protein homolog, 79 Cho stoneura fumiferana 3377,,111155 29-Jan-9 kDa protein homolog, 15 kDa protein homolog and GTA protein homolog nucleopolyhedrovirus genes, complete cds GB_GSS10 AQ213248 408 AQ213248 HS_3249_B1_A02_MR CIT Approved Human Genomic Sperm Library D Homo Homo sapiens 34,559 18-Sep-9 sapiens genomic clone Plate=3249 Col=3 Row=B, genomic survey sequence GB_GSS8 AQ070145 285 AQ070145 HS_3027_B1_H02_MR CIT Approved Human Genomic Sperm Library D Homo Homo sapiens 40,351 5-Aug-98 sapiens genomic clone Plate=3027 Col=3 Row=P, genomic survey sequence rxa01626 468 GB_PR4 AF152510 2490 AF152510 Homo sapiens protocadheπn gamma A3 short form protein (PCDH-gamma-A3) Homo sapiens 34,298 14-Jul-99 variable region sequence, complete cds GB_PR4 AF152323 4605 AF152323 Homo sapiens protocadheπn gamma A3 (PCDH-gamma-A3) mRNA, complete Homo sapiens 34,298 22-Jul-99 cds GB_PR4 AF152509 2712 AF152509 Homo sapiens PCDH-gamma-A3 gene, aberrantly spliced, mRNA sequence Homo sapiens 34,298 14-Jul-99 rxa01632 1128 GBJHTG4 AC006590 127171 AC006590 Drosophila melanogaster chromosome 2 clone BACR13N02 (D543) RPCI-98 Drosophila melanogaster 3 333,,881122 19-OCT-1 13 N 2 map 36E-36E strain y, en bw sp, *** SEQUENCING IN PROGRESS***, 101 unordered pieces GB_HTG4 AC006590 127171 AC006590 Drosophila melanogaster chromosome 2 clone BACR13N02 (D543) RPCI-98 Drosophila melanogaster 3 333,,881122 19-OCT-1 13 N 2 map 36E-36E strain y, en bw sp, *** SEQUENCING IN PROGRESS***, 101 unordered pieces GB_GSS8 B99182 415 B99182 CIT-HSP-2280113 TR CIT-HSP Homo sapiens genomic clone 2280113, Homo sapiens 36,111 26-Jun-9 genomic survey sequence rxa01633 1206 GB_BA1 BSUB0009 208780 Z99112 Bacillus subtihs complete genome (section 9 of 21) from 1598421 to 1807200 Bacillus subtihs 36,591 26-Nov-9 GB_BA1 BSUB0009 208780 Z99112 Bacillus subtihs complete genome (section 9 of 21) from 1598421 to 1807200 Bacillus subtihs 34,941 26-NOV-9 GB_HTG2 AC006247 174368 AC006247 Drosophila melanogaster chromosome 2 clone BACR48110 (D505) RPCI-98 Drosophila melanogaster 37,037 2-Aug-99 48 I 10 map 49E6-49F8 strain y, en bw sp, *** SEQUENCING IN PROGRESS ***, 17 unordered pieces Table 4 (continued) rxa01695 1623 GB_BA1 CGA224946 2408 AJ224946 Corynebacterium glutamicum DNA for L-Malate quinone oxidoreductase Corynebacterium 100,000 11-Aug-98 glutamicum GB_BA1 MTCY24A1 20270 Z95207 Mycobacterium tuberculosis H37Rv complete genome, segment 124/162 Mycobacterium 38,626 17-Juπ-98 tuberculosis GBJN1 DMU15974 2994 U 15974 Drosophila melanogaster kinesin-hke protein (klp68d) mRNA, complete cds Drosophila melanogaster 36,783 18-Jul-95 rxa01702 1155 GB BA1 CGFDA 3371 X17313 Corynebacterium glutamicum fda gene for fructose-bisphosphate aldolase (EC Corynebacteπum 99,913 12-Sep-93 4 1 2 13) glutamicum GB BA1 MTY13E10 35019 Z95324 Mycobacterium tuberculosis H37Rv complete genome, segment 18/162 Mycobacterium 38,786 17-Jun-98 tuberculosis GB_BA1 MLCB4 36310 AL023514 Mycobacterium leprae cosmid B4 Mycobacterium leprae 38,238 27-Aug-99 rxa01743 901 GBJN2 CELC27H5 35840 U14635 Caenorhabditis elegans cosmid C27H5 Caenorhabditis elegans 35,334 13-Jul-95 GB_EST24 AI167112 579 AI167112 xylem est 878 Poplar xylem Lambda ZAPll library Populus balsamifera subsp Populus balsamifera 39,222 03-DEC-1 tπchocarpa cDNA 5', mRNA sequence subsp tπchocarpa GB_GSS9 AQ102635 347 AQ102635 HS_3048_B1_F08_MF CIT Approved Human Genomic Sperm Library D Homo Homo sapiens 40,653 27-Aug-98 sapiens genomic clone Plate=3048 Col=15 Row=L, genomic survey sequence rxa01744 1662 GB_BA1 MTCY01 B2 35938 Z95554 Mycobacterium tuberculosis H37Rv complete genome, segment 72/162 Mycobacterium 36,650 17-Jun-98 tuberculosis GB_GSS1 AF009226 665 AF009226 Mycobacterium tuberculosis cytochrome D oxidase subunit I (appC) gene, Mycobacterium 63,438 31-Jul-97 partial sequence, genomic survey sequence tuberculosis GB_BA1 SCD78 36224 AL034355 Streptomyces coelicolor cosmid D78 Streptomyces coelicolor 53,088 26-Nov-98 rxa01745 836 GB_BA1 MTCY190 34150 Z70283 Mycobacterium tuberculosis H37Rv complete genome, segment 98/162 Mycobacterium 62,081 17-Jun-98 tuberculosis GB_BA1 MLCB22 40281 Z98741 Mycobacterium leprae cosmid B22 Mycobacterium leprae 61 ,364 22-Aug-97 GB_BA2 AE000175 15067 AE000175 Eschenchia coli K-12 MG1655 section 65 of 400 of the complete genome Eschenchia coli 52,323 12-NOV-98 rxa01758 1140 GB_PR3 HS57G9 113872 Z95116 Human DNA sequence from BAC 57G9 on chromosome 22q12 1 Contains Homo sapiens 39,209 23-Nov-99 ESTs, CA repeat, GSS GB_PL2 YSCH9666 39057 U 10397 Saccharomyces cerevisiae chromosome VIII cosmid 9666 Saccharomyces cerevisiae 40,021 5-Sep-97 GB_PL2 YSCH9986 41664 U00027 Saccharomyces cerevisiae chromosome VIII cosmid 9986 Saccharomyces cerevisiae 34,375 29-Aug-9 rxa01814 1785 GB_BA1 ABCCELB 2058 L24077 Acetobacter xyhnum phosphoglucomutase (celB) gene, complete cds Acetobacter xyhnus 62,173 21-Sep-9 GB_BA1 MTCY22D7 31859 Z83866 Mycobacterium tuberculosis H37Rv complete genome, segment 133/162 Mycobacterium 39,749 17-Jun-98 tuberculosis GB_BA1 MTCY22D7 31859 Z83866 Mycobacterium tuberculosis H37Rv complete genome, segment 133/162 Mycobacterium 40,034 17-Jun-98 tuberculosis rxa01851 1809 GB_GSS9 AQ142579 529 AQ142579 HS_2222_B1_H03_MR CIT Approved Human Genomic Sperm Library D Homo H Hoommoo ssaappiieennss 38,068 24-Sep-98 sapiens genomic clone Plate=2222 Col=5 Row=P, genomic survey sequence GBJN2 AC005889 108924 AC005889 Drosophila melanogaster, chromosome 2L, region 30A3- 30A6, P1 clones Drosophila melanogaster 36,557 30-OCT-1 DS06958 and DS03097, complete sequence GB GSS1 AG008814 637 AG008814 Homo sapiens genomic DNA, 21q region, clone B137B7BB68, genomic survey H Hoommoo ssaappiieennss 35,316 7-Feb-99 sequence Table 4 (continued) rxa01859 1050 GB BA2 AF183408 63626 AF183408 Microcystis aeruginosa DNA polymerase III beta subunit (dnaN) gene, partial Microcystis aeruginosa 36,364 03-OCT-1 cds, microcystin synthetase gene cluster, complete sequence, Uma1 (umal), Uma2 (uma2), Uma3 (uma3), Uma4 (uma4), and Uma5 (umaδ) genes, complete cds, and Uma6 (umaδ) gene, partial cds GB_HTG5 AC008031 158889 AC008031 Trypanosoma brucei chromosome II clone RPCI93-25N14, * ** SEQUENCING Trypanosoma brucei 35,334 15-NOV-9 IN PROGRESS * * * , 2 unordered pieces GB_BA2 AF183408 63626 AF183408 Microcystis aeruginosa DNA polymerase III beta subunit (dnaN) gene, partial Microcystis aeruginosa 36,529 03-OCT-1 cds, microcystin synthetase gene cluster, complete sequence, Uma1 (umal ), Uma2 (uma2), Uma3 (uma3), Uma4 (uma4), and Uma5 (uma5) genes, complete cds, and Uma6 (uma6) gene, partial cds rxa01865 438 GB_BA1 SERFDXA 3869 M61119 Saccharopolyspora erythraea ferredoxm (fdxA) gene, complete cds Saccharopolyspora 59,862 13-MAR-1 erythraea GB_BA1 MTV005 37840 AL010186 Mycobacterium tuberculosis H37Rv complete genome, segment 51/162 Mycobacterium 61 ,949 17-Jun-98 tuberculosis GB_BA1 MSGY348 40056 AD000020 Mycobacterium tuberculosis sequence from clone y348 Mycobacterium 59,908 10-DEC-1 tuberculosis rxa01882 1113 GB_PR1 HUMADRA2C 1491 J03853 Human kidney alpha-2-adrenergιc receptor mRNA, complete cds Homo sapiens 36,899 27-Apr-93 GB_PR4 HSU72648 4850 U72648 Homo sapiens alpha2-C4-adrenergιc receptor gene, complete cds Homo sapiens 36,899 23-Nov-9 GB GSS3 B42200 387 B42200 HS-1055-B1-A03-MR abi CIT Human Genomic Sperm Library C Homo sapiens Homo sapiens 34,805 18-OCT-1 genomic clone Plate=CT 777 Col=5 Row=B, genomic survey sequence rxa01884 1913 GB_BA1 MTCY48 35377 Z74020 Mycobacterium tuberculosis H37Rv complete genome, segment 69/162 Mycobacterium 37,892 17-Jun-9 tuberculosis GB_BA1 SCO001206 9184 AJ001206 Streptomyces coelicolor A3(2), glycogen metabolism cluster II Streptomyces coelicolor 40,413 29-MAR-1 GB_BA1 D90908 122349 D90908 Synechocystis sp PCC6803 complete genome, 10/27, 1188886-1311234 Synechocystis sp 47,792 7-Feb-99 rxa01886 897 GB_GSS9 AQ116291 572 AQ116291 RPCI11-49P6 TK 1 RPCI-11 Homo sapiens genomic clone RPCI-11-49P6, Homo sapiens 43,231 20-Apr-9 genomic survey sequence GB_BA2 AE001721 17632 AE001721 Thermotoga maπtima section 33 of 136 of the complete genome Thermotoga maπtima 39,306 2-Jun-99 GB_EST16 AA567090 596 AA567090 GM01044 5prιme GM Drosophila melanogaster ovary BlueScnpt Drosophila Drosophila melanogaster 42,807 28-Nov-9 melanogaster cDNA clone GM01044 5prιme, mRNA sequence rxa01887 1134 GB_HTG6 AC008147 303147 AC008147 Homo sapiens clone RP3-405J10, *** SEQUENCING IN PROGRESS ***, 102 Homo sapiens 36,417 03-DEC-1 unordered pieces GB_HTG6 AC008147 303147 AC008147 Homo sapiens clone RP3-405J10, *** SEQUENCING IN PROGRESS ** * , 102 Homo sapiens 37,667 03-DEC-1 unordered pieces GB BA2 ALW243431 26953 AJ243431 Acmetobacter Iwoffn wzc, wzb, wza, weeA, weeB, wceC, wzx, wzy, weeD, Acmetobacter Iwoffii 39,640 01-OCT-1 weeE, weeF, weeG, weeH, weel, weeJ, weeK, galU, ugd, pgi, galE, pgm (partial) and mip (partial) genes (emulsan biosynthetic gene cluster), strain RAG-1 rxa01888 658 GB HTG2 AC008197 125235 AC008197 Drosophila melanogaster chromosome 3 clone BACR02L12 (D753) RPCI-98 Drosophila melanogaster 32,969 2-Aug-99 02 L 12 map 94B-94C strain y, en bw sp, *** SEQUENCING IN PROGRESS 113 unordered pieces Table 4 (continued) GB_HTG2 AC008197 125235 AC008197 Drosophila melanogaster chromosome 3 clone BACR02L12 (D753) RPCI-98 Drosophila melanogaster 32,969 2-Aug-99 02 L 12 map 94B-94C strain y, en bw sp, "* SEQUENCING IN PROGRESS *** , 113 unordered pieces GB_EST36 AI881527 598 AI881527 606070C09 y1 606 - Ear tissue cDNA library from Schmidt lab Zea mays cDNA. Zea mays 43,617 21-Jul-99 mRNA sequence n<a01891 887 GB_VI HIV232971 621 AJ232971 Human immunodeficiency virus type 1 subtype C nef gene, patient MP83 Human immunodeficiency 40,040 05-MAR-1 virus type 1 GB_PL1 AFCHSE 6158 Y09542 A fumigatus chsE gene Aspergillus fumigatus 37,844 1-Apr-97 GB_PR3 AF064858 193387 AF064858 Homo sapiens chromosome 21q22 3 BAC 28F9, complete sequence Homo sapiens 37,136 2-Jun-98 rxa01895 1051 GB_BA1 CGL238250 1593 AJ238250 Corynebacterium glutamicum ndh gene Corynebacterium 100,000 24-Apr-99 glutamicum GB_BA2 AF038423 1376 AF038423 Mycobacterium smegmatis NADH dehydrogenase (ndh) gene, complete cds Mycobacterium smegmatis 65,254 05-MAY-1 GB_BA1 MTCY359 36021 Z83859 Mycobacterium tuberculosis H37Rv complete genome, segment 84/162 Mycobacterium 40,058 17-Jun-9 tuberculosis rxa01901 1383 GB_BA1 MSGB38COS 37114 L01095 M leprae genomic DNA sequence, cosmid B38 bfr gene, complete cds Mycobacterium leprae 59,551 6-Sep-94 GB_BA1 SCE63 37200 AL035640 Streptomyces coelicolor cosmid E63 Streptomyces coelicolor 39,468 17-MAR-1 GB_PR3 AF093117 147216 AF093117 Homo sapiens chromosome 7qtelo BAC E3, complete sequence Homo sapiens 39,291 02-OCT-1 rxa01927 1503 GB_BA1 CGPAN 2164 X96580 C glutamicum panB, panC & xylB genes Corynebacterium 38,384 11-MAY-1 glutamicum GB_BA1 ASXYLA 1905 X59466 Arthrobacter Sp N R R L B3728 xylA gene for D-xylose(D-glucose) isomerase Arthrobacter sp 56,283 04-MAY-1 GB_HTG3 AC009500 176060 AC009500 Homo sapiens clone NH0511A20, *** SEQUENCING IN PROGRESS ** * , 6 Homo sapiens 37,593 24-Aug-9 unordered pieces rxa01952 1836 GB_BA2 AE000739 13335 AE000739 Aquifex aeolicus section 71 of 109 of the complete genome Aquifex aeolicus 36,309 25-MAR- GB_EST28 AI519629 612 AI519629 LD39282 5prιme LD Drosophila melanogaster embryo pOT2 Drosophila Drosophila melanogaster 41 ,941 16-MAR- melanogaster cDNA clone LD39282 5prιme, mRNA sequence GB_EST21 AA949396 767 AA949396 LD28277 5pπme LD Drosophila melanogaster embryo pOT2 Drosophila Drosophila melanogaster 39,855 25-N0V-9 melanogaster cDNA clone LD28277 5pπme, mRNA sequence rxa01989 630 GB_BA1 BSPGIA 1822 X16639 Bacillus stearothermophilus pgiA gene for phosphoglucoisomerase isoenzyme Bacillus 66,292 20-Apr-9 A (EC 5 3 1 9) stearothermophilus GB_BA1 BSUB001 217420 Z99120 Bacillus subtihs complete genome (section 17 of 21) from 3197001 to Bacillus subtihs 37,255 26-Nov-9 3414420 GB_BA2 AF132127 8452 AF132127 Streptococcus mutans sorbitol phosphoenolpyruvate sugar phosphotransferase Streptococcus mutans 63,607 28-Sep-9 operon, complete sequence and unknown gene rxa02026 720 GB_BA1 SXSCRBA 3161 X67744 S xylosus scrB and scrR genes Staphylococcus xylosus 67,778 28-Nov-9 GB_BA1 BSUB0020 212150 Z99123 Bacillus subtihs complete genome (section 20 of 21) from 3798401 to Bacillus subtihs 35,574 26-Nov-9 4010550 GB_BA1 BSGENR 97015 X73124 B subtihs genomic region (325 to 333) Bacillus subtihs 51 ,826 2-Nov-93 rxa02028 526 GB_BA1 MTCI237 27030 Z94752 Mycobacterium tuberculosis H37Rv complete genome, segment 46/162 Mycobacterium 54,476 17-Jun-9 tuberculosis Table 4 (continued) GB_PL2 SCE9537 66030 U18778 Saccharomyces cerevisiae chromosome V cosmids 9537, 9581 , 9495, 9867, Saccharomyces cerevisiae 36,100 1-Aug-97 and lambda clone 5898 GB_GSS13 AQ501177 767 AQ501177 V26G9 mTn-3xHA/lacZ Insertion Library Saccharomyces cerevisiae genomic 5', Saccharomyces cerevisiae 32,039 29-Apr-9 genomic survey sequence rxa02054 1140 GB_BA1 MLCB1222 34714 AL049491 Mycobacterium leprae cosmid B1222 Mycobacterium leprae 61 ,896 27-Aug-9 GB_BA1 MTY13E12 43401 Z95390 Mycobacterium tuberculosis H37Rv complete genome, segment 147/162 Mycobacterium 59,964 17-Jun-9 tuberculosis GB_BA1 MTU43540 3453 U43540 Mycobacterium tuberculosis rfbA, rhamnose biosynthesis protein (rfbA), and Mycobacterium 59,659 14-Aug-9 rmlC genes, complete cds tuberculosis rxa02056 2891 GB_PAT E14601 4394 E14601 Brevibacterium lactofermentum gene for alpha-ketoglutaπc acid Corynebacterium 98,928 28-Jul-99 dehydrogenase glutamicum GB_BA1 D84102 4394 D84102 Corynebacterium glutamicum DNA for 2-oxoglutarate dehydrogenase, complete Corynebacterium 98,928 6-Feb-99 cds glutamicum GB_BA1 MTV006 22440 AL021006 Mycobacterium tuberculosis H37Rv complete genome, segment 54/162 Mycobacterium 39,265 18-Jun-9 tuberculosis rxa02061 1617 GBJHTG7 AC005883 211682 AC005883 Homo sapiens chromosome 17 clone RP11-958E11 map 17, *** Homo sapiens 37,453 08-DEC-1 SEQUENCING IN PROGRESS *** , 2 ordered pieces GB_PL2 ATAC003033 84254 AC003033 Arabidopsis thaliana chromosome II BAC T21 L14 genomic sequence, complete Arabidopsis thaliana 37,711 19-DEC-1 sequence GB_PL2 ATAC002334 75050 AC002334 Arabidopsis thaliana chromosome II BAC F25I18 genomic sequence, complete Arabidopsis thaliana 37,711 04-MAR- sequence rxa02063 1350 GB_BA1 SCGLGC 1518 X89733 S coelicolor DNA for glgC gene Streptomyces coelicolor 5 566,,997722 12-Jul-99 GB_GSS4 AQ687350 786 AQ687350 nbxb0074H11 r CUGI Rice BAC Library Oryza sativa genomic clone Oryza sativa 40,696 1-Jul-99 nbxb0074H11 r, genomic survey sequence GB_EST38 AW028530 444 AW028530 wv27f10 x1 NCI_CGAP_Kιd11 Homo sapiens cDNA clone IMAGE 2530795 3' Homo sapiens 36,795 27-OCT-1 similar to WP T03G11 6 CE04874 ,, mRNA sequence rxa02100 2348 GB_BA1 MSGY151 37036 AD000018 Mycobacterium tuberculosis sequence from clone y 151 Mycobacterium 40,156 10-DEC-1 tuberculosis GB_BA1 MTCY130 32514 Z73902 Mycobacterium tuberculosis H37Rv complete genome, segment 59/162 Mycobacterium 55,218 17-Jun-9 tuberculosis GB_BA1 SCO001205 9589 AJ001205 Streptomyces coelicolor A3(2) glycogen metabolism clusterl Streptomyces coelicolor 3 388,,447755 29-MAR- rxa02122 822 GB_BA1 D90858 13548 D90858 E coli genomic DNA, Kohara clone #401(51 3-51 6 mm ) Eschenchia coli 38,586 29-MAY- GB_EST37 AI948595 469 AI948595 wq07d12 x1 NCI_CGAP_Kιd12 Homo sapiens cDNA clone IMAGE 2470583 3', Homo sapiens 37,259 6-Sep-99 mRNA sequence GB_HTG3 AC010387 220665 AC010387 Homo sapiens chromosome 5 clone CITB-H1_2074D8, *** SEQUENCING IN Homo sapiens 38,868 15-Sep-9 PROGRESS * **, 77 unordered pieces rxa02140 1200 GB_BA1 MSGB1551CS 36548 L78813 Mycobacterium leprae cosmid B1551 DNA sequence Mycobacterium leprae 51 ,399 15-Jun-9 GB_BA1 MSGB1554CS 36548 L78814 Mycobacterium leprae cosmid B1554 DNA sequence Mycobacterium leprae 51 ,399 15-Jun-9 GB_RO AF093099 2482 AF093099 Mus musculus transcription factor TBLYM (Tblym) mRNA, complete cds Mus musculus 36,683 01-OCT-1 rxa02142 774 GB_BA1 MTCY190 34150 Z70283 Mycobacterium tuberculosis H37Rv complete genome, segment 98/162 Mycobacterium 57,292 17-Jun-9 tuberculosis Table 4 (continued) GB_BA1 SC6G10 36734 AL049497 Streptomyces coelicolor cosmid 6G10 Streptomyces coelicolor 35,058 24-MAR-1 GB_BA1 AB016787 5550 AB016787 Pseudomonas putida genes for cytochrome o ubiquinol oxidase A-E and 2 Pseudomonas putida 47,403 5-Aug-99 ORFs, complete cds rxa02143 1011 GB BA1 MTCY190 34150 Z70283 Mycobacterium tuberculosis H37Rv complete genome, segment 98/162 Mycobacterium 57,317 17-Jun-98 tuberculosis GB_BA1 MSGB1551 CS 36548 L78813 Mycobacterium leprae cosmid B1551 DNA sequence Mycobacterium leprae 38,159 15-Jun-96 GB_BA1 MSGB1554CS 36548 L78814 Mycobacterium leprae cosmid B1554 DNA sequence Mycobacterium leprae 38,159 15-Jun-96 rxa02144 1347 GB BA1 MTCY190 34150 Z70283 Mycobacterium tuberculosis H37Rv complete genome, segment 98/162 Mycobacterium 55,530 17-Jun-98 tuberculosis GB_HTG3 AC011500_0 300851 AC011500 Homo sapiens chromosome 19 clone CIT978SKB_60E11 , *** SEQUENCING Homo sapiens 39,659 18-Feb-0 IN PROGRESS *** , 246 unordered pieces GB_HTG3 AC011500_0 300851 AC011500 Homo sapiens chromosome 19 clone CIT978SKB_60E11 , *** SEQUENCING Homo sapiens 39,659 18-Feb-0 IN PROGRESS ***, 246 unordered pieces rxa02147 1140 GB_EST28 AI492095 485 AI492095 tg07a01 x1 NCI_CGAP_CLL1 Homo sapiens cDNA clone IMAGE 2108040 3', Homo sapiens 39,798 30-MAR-1 mRNA sequence GB_EST10 AA157467 376 AA157467 zo50e01 r1 Stratagene endothehal cell 937223 Homo sapiens cDNA clone Homo sapiens 36,436 11-DEC-1 IMAGE 590328 5', mRNA sequence GB_EST10 AA157467 376 AA157467 zo50e01 r1 Stratagene endothehal cell 937223 Homo sapiens cDNA clone Homo sapiens 36,436 1 1-DEC-1 IMAGE 590328 5', mRNA sequence rxa02149 1092 GB_PR3 HSBK277P6 61698 AL117347 Human DNA sequence from clone 277P6 on chromosome 1q25 3-31 2, Homo sapiens 36,872 23-NOV-9 complete sequence GB_BA2 EMB065R075 360 AF116423 Rhizobium eth mutant MB045 RosR-transcnptionally regulated sequence Rhizobium etli 43,175 06-DEC-1 GB_EST34 AI789323 574 AI789323 uk53g05 y1 Sugano mouse kidney kia Mus musculus cDNA clone Mus musculus 39,715 2-Jul-99 IMAGE 1972760 5' similar to WP K11 H12 8 CE12160 „ mRNA sequence rxa02175 1416 GB_BA1 CGGLTG 3013 X66112 C glutamicum git gene for citrate synthase and ORF Corynebacterium 100,000 17-Feb-9 glutamicum GB BA1 MTCY31 37630 Z73101 Mycobacterium tuberculosis H37Rv complete genome, segment 41/162 Mycobacterium 64,331 17-Jun-9 tuberculosis GB_BA1 MLCB57 38029 Z99494 Mycobacterium leprae cosmid B57 Mycobacterium leprae 62,491 10-Feb-9 rxa02196 816 GB RO RATDAPRP 2819 M76426 Rattus norvegicus dipeptidyl aminopeptidase-related protein (dpp6) mRNA, Rattus norvegicus 38,791 31 -MAY- 1 complete cds GB_GSS8 AQ012162 763 AQ012162 127PB037070197 Cosmid library of chromosome II Rhodobacter sphaeroides Rhodobacter sphaeroides 40,044 4-Jun-98 genomic clone 127PB037070197, genomic survey sequence GB_RO RATDAPRP 2819 M76426 Rattus norvegicus dipeptidyl aminopeptidase-related protein (dppθ) mRNA, Rattus norvegicus 37,312 31-MAY-1 complete cds rxa02209 1694 GB_BA1 AB025424 2995 AB025424 Corynebacterium glutamicum gene for aconitase, partial cds Corynebacterium 99,173 glutamicum GB BA2 AF002133 15437 AF002133 Mycobacterium avium strain GIR10 transcriptional regulator (mav81) gene, Mycobacterium avium 40,219 26-MAR-1 partial cds, aconitase (acn), invas 1 (ιnv1), invasin 2 (ιnv2), transcriptional regulator (moxR), ketoacyl-reductase (fabG), enoyl-reductase (inhA) and ferrochelatase (mav272) genes, complete cds Table 4 (continued) GB BA1 MTV007 32806 AL021184 Mycobacterium tuberculosis H37Rv complete genome, segment 64/162 Mycobacterium 38,253 17-Jun-98 tuberculosis rxa02213 874 GB_BA1 AB025424 2995 AB025424 Corynebacterium glutamicum gene for aconitase, partial cds Corynebacteπum 99,096 3-Apr-99 glutamicum GB BA1 MTV007 32806 AL021184 Mycobacterium tuberculosis H37Rv complete genome, segment 64/162 Mycobacterium 34,937 17-Jun-9 tuberculosis GB BA2 AF002133 15437 AF002133 Mycobacterium avium strain GIR10 transcriptional regulator (mav81) gene, Mycobacterium avium 36,885 26-MAR-1 partial cds, aconitase (acn), mvasin 1 (ιnv1), invasm 2 (ιnv2), transcriptional regulator (moxR), ketoacyl-reductase (fabG), enoyl-reductase (inhA) and ferrochelatase (mav272) genes, complete cds rxa02245 780 GB BA2 RCU23145 5960 U23145 Rhodobacter capsulatus Calvin cycle carbon dioxide fixation operon fructose- Rhodobacter capsulatus 48,701 28-OCT-1 1 ,6-/sedoheptulose-1 ,7-bιsphosphate aldolase (cbbA) gene, partial cds, Form II rιbulose-1 ,5-bιsphosphate carboxylase/oxygenase (cbbM) gene, complete cds, and Calvin cycle operon pentose-5-phosphate-3-epιmerase (cbbE), phosphoglycolate phosphatase (cbbZ), and cbbY genes, complete cds GB_BA1 ECU82664 139818 U82664 Eschenchia coli minutes 9 to 11 genomic sequence Eschenchia coli 39,119 11-Jan-9 GB_HTG2 AC007922 158858 AC007922 Homo sapiens chromosome 18 clone hRPK 178_F_10 map 18, * * * Homo sapiens 33,118 26-Jun-9 SEQUENCING IN PROGRESS *** , 11 unordered pieces rxa02256 1125 GB_BA1 CGGAPPGK 3804 X59403 C glutamicum gap, pgk and tpi genes for glyceraldehyde-3-phosphate, Corynebacterium 99,289 05-OCT-1 phosphoglycerate kinase and triosephosphate isomerase glutamicum GB_BA1 SCC54 30753 AL035591 Streptomyces coelicolor cosmid C54 Streptomyces coelicolor 36,951 11-Jun-9 GB_BA1 MTCY493 40790 Z95844 Mycobacterium tuberculosis H37Rv complete genome, segment 63/162 Mycobacterium 64,196 19-Jun-9 tuberculosis rxa02257 1338 GB_BA1 CGGAPPGK 3804 X59403 C glutamicum gap, pgk and tpi genes for glyceraldehyde-3-phosphate, Corynebacteπum 98,873 05-OCT-1 phosphoglycerate kinase and triosephosphate isomerase glutamicum GB_BA1 MTCY493 40790 Z95844 Mycobacterium tuberculosis H37Rv complete genome, segment 63/162 Mycobacterium 61 ,273 19-Jun-9 tuberculosis GB_BA2 MAU82749 2530 U82749 Mycobacterium avium glyceraldehyde-3-phosphate dehydrogenase homolog Mycobacterium avium 61 ,772 6-Jan-98 (gapdh) gene, complete cds, and phosphoglycerate kinase gene, partial cds rxa02258 900 GB_BA1 CGGAPPGK 3804 X59403 C glutamicum gap, pgk and tpi genes for glyceraldehyde-3-phosphate, Corynebacterium 99,667 05-OCT-1 phosphoglycerate kinase and triosephosphate isomerase glutamicum GB_BA1 CORPEPC 4885 M25819 C glutamicum phosphoenolpyruvate carboxylase gene, complete cds Corynebacterium 100,000 15-DEC-1 glutamicum GB_PAT A09073 4885 A09073 C glutamicum ppg gene for phosphoenol pyruvate carboxylase Corynebacterium 100,000 25-Aug-9 glutamicum rxa02259 2895 GB_BA1 CORPEPC 4885 M25819 C glutamicum phosphoenolpyruvate carboxylase gene, complete cds Corynebacterium 100,000 15-DEC-1 glutamicum GB_PAT A09073 4885 A09073 C glutamicum ppg gene for phosphoenol pyruvate carboxylase Corynebacterium 100,000 25-Aug-9 glutamicum GB BA1 CGPPC 3292 X14234 Corynebacterium glutamicum phosphoenolpyruvate carboxylase gene (EC Corynebacterium 99,827 12-Sep-9 4 1 1 31 ) glutamicum Table 4 (continued) rxa02288 969 GB_PR3 HSDJ94E24 243145 AL05031 Human DNA sequence from clone RP1-94E24 on chromosome 20q12, Homo sapiens 36,039 03-DEC-1 complete sequence GB_HTG3 AC010091 159526 AC010091 Homo sapiens clone NH0295A01 , *** SEQUENCING IN PROGRESS "*, 4 Homo sapiens 35,331 11-Sep-9 unordered pieces GB_HTG3 AC010091 159526 AC010091 Homo sapiens clone NH0295A01 , *** SEQUENCING IN PROGRESS *** , 4 Homo sapiens 35,331 11-Sep-9 unordered pieces rxa02292 798 GB_BA2 AF125164 26443 AF125164 Bacteroides fragihs 638R polysacchaπde B (PS B2) biosynthesis locus, Bacteroides fragihs 39,747 01-DEC-1 complete sequence, and unknown genes GB GSS5 AQ744695 827 AQ744695 HS_5505_A2_C06_SP6 RPCI-11 Human Male BAC Library Homo sapiens Homo sapiens 39,185 16-Jul-99 genomic clone Plate=1081 Col=12 Row=E, genomic survey sequence GB_EST14 AA381925 309 AA381925 EST95058 Activated T-cells I Homo sapiens cDNA 5' end, mRNA sequence Homo sapiens 35,922 21-Apr-97 rxa02322 511 GB_BA1 MTCY22G8 22550 Z95585 Mycobacterium tuberculosis H37Rv complete genome, segment 49/162 Mycobacteπum 57,677 17-Jun-98 tuberculosis GB_BA1 MTCY22G8 22550 Z95585 Mycobacterium tuberculosis H37Rv complete genome, segment 49/162 Mycobacterium 37,143 17-Jun-98 tuberculosis rxa02326 939 GB_BA1 CGPYC 3728 Y09548 Corynebacterium glutamicum pyc gene Corynebacterium 100,000 08-MAY-1 glutamicum GB_BA2 AF038548 3637 AF038548 Corynebacterium glutamicum pyruvate carboxylase (pyc) gene, complete cds Corynebacterium 100,000 24-DEC-1 glutamicum GB_BA1 MTCY349 43523 Z83018 Mycobacterium tuberculosis H37Rv complete genome, segment 131/162 Mycobacterium 37,363 17-Jun-9 tuberculosis rxa02327 1083 GB_BA1 CGPYC 3728 Y09548 Corynebacterium glutamicum pyc gene Corynebacterium 99,259 08-MAY-1 glutamicum GB_BA2 AF038548 3637 AF038548 Corynebacterium glutamicum pyruvate carboxylase (pyc) gene, complete cds Corynebacterium 99,259 24-DEC-1 glutamicum GB_BA1 MTCY349 43523 Z83018 Mycobacterium tuberculosis H37Rv complete genome, segment 131/162 Mycobacterium 41 ,317 17-Jun-9 tuberculosis rxa02328 1719 GB_BA1 CGPYC 3728 Y09548 Corynebacterium glutamicum pyc gene Corynebacterium 100,000 08-MAY-1 glutamicum GB_BA2 AF038548 3637 AF038548 Corynebacterium glutamicum pyruvate carboxylase (pyc) gene, complete cds Corynebacterium 100,000 24-DEC-1 glutamicum GB_PL2 AF097728 3916 AF097728 Aspergillus terreus pyruvate carboxylase (Pyc) mRNA, complete cds Aspergillus terreus 52,248 29-OCT-1 rxa02332 1266 GB_BA1 MSGLTA 1776 X60513 M smegmatis gltA gene for citrate synthase Mycobacterium smegmatis 58,460 20-Sep-9 GB_BA2 ABU85944 1334 U85944 Antarctic bacterium DS2-3R citrate synthase (cisy) gene, complete cds Antarctic bacterium DS2- 57,154 23-Sep-9 3R GB. .BA2 AE000175 15067 AE000175 Eschenchia coli K-12 MG1655 section 65 of 400 of the complete genome Eschenchia coli 38,164 12-Nov-9 rxa02333 1038 GB. _BA1 MSGLTA 1776 X60513 M smegmatis gltA gene for citrate synthase Mycobacterium smegmatis 58,929 20-Sep-9 GB PR4 HUAC002299 171681 AC002299 Homo sapiens Chromosome 16 BAC clone CIT987-SKA-113A6 -complete Homo sapiens 33,070 23-Nov-9 genomic sequence, complete sequence Table 4 (continued) GB HTG2 AC007889 127840 AC007889 Drosophila melanogaster chromosome 3 clone BACR48E12 (D695) RPCI-98 Drosophila melanogaster 34,897 2-Aug-99 48 E 12 map 87A-87B strain y, cn bw sp, * ** SEQUENCING IN PROGRESS *** , 86 unordered pieces rxa02399 1467 GB_BA1 CGACEA 2427 X75504 C glutamicum aceA gene and thiX genes (partial) Corynebacteπum 100,000 9-Sep-94 glutamicum GB_BA1 CORACEA 1905 L28760 Corynebactenum glutamicum isocitrate lyase (aceA) gene Corynebacterium 100,000 10-Feb-9 glutamicum GB_PAT 113693 2135 113693 Sequence 3 from patent US 5439822 Unknown 99,795 26-Sep-9 rxa02404 2340 GB_BA1 CGACEB 3024 X78491 C glutamicum (ATCC 13032) aceB gene Corynebacterium 99,914 13-Jan-95 glutamicum GB_BA1 CORACEB 2725 L27123 Corynebacterium glutamicum malate synthase (aceB) gene, complete cds Corynebacterium 99,786 8-Jun-95 glutamicum GB_BA1 PFFC2 5588 Y11998 P fluorescens FC2 1 , FC2 2, FC2 3c, FC2 4 and FC2 5c open reading frames Pseudomonas fluorescens 63,539 11-Jul-97 rxa02414 870 GB_PR4 AC007102 176258 AC007102 Homo sapiens chromosome 4 clone C0162P16 map 4p16, complete sequence Homo sapiens 35,069 2-Jun-99 GB_HTG3 AC011214 183414 AC011214 Homo sapiens clone 5_C_3, LOW-PASS SEQUENCE SAMPLING Homo sapiens 36,885 03-OCT-1 GB_HTG3 AC011214 183414 AC011214 Homo sapiens clone 5_C_3, LOW-PASS SEQUENCE SAMPLING Homo sapiens 36,885 03-OCT-1 rxa02435 681 GB_BA2 AF101055 7457 AF101055 Clostridium acetobutylicum atp operon, complete sequence Clostridium acetobutylicum 39,605 03-MAR-1 GB_OM RABPKA 4441 J03247 Rabbit phosphorylase kinase (alpha subunit) mRNA, complete cds Oryctolagus cuniculus 36,061 27-Apr-93 GB_OM RABPLASISM 4458 M64656 Oryctolagus cuniculus phosphorylase kinase alpha subunit mRNA, complete Oryctolagus cuniculus 36,000 22-Jun-9 cds rxa02440 963 GB_EST14 AA417723 374 AA417723 zv01b12 s1 NCI_CGAP_GCB1 Homo sapiens cDNA clone IMAGE 746207 3' Homo sapiens 38,770 16-OCT-1 similar to contains Alu repetitive element.contains element L1 repetitive element ,, mRNA sequence GB_EST11 AA215428 303 AA215428 zr95a07 s1 NCI_CGAP_GCB1 Homo sapiens cDNA clone IMAGE 683412 3' Homo sapiens 39,934 13-Aug-9 similar to contains Alu repetitive element,, mRNA sequence GB_BA1 MTCY77 22255 Z95389 Mycobacterium tuberculosis H37Rv complete genome, segment 146/162 Mycobacterium 38,889 18-Jun-9 tuberculosis rxa02453 876 GB_EST14 AA426336 375 AA426336 zv53g02 s1 Soares_testιs_NHT Homo sapiens cDNA clone IMAGE 757394 3', Homo sapiens 38,043 16-OCT-1 mRNA sequence GB_BA1 STMAACC8 1353 M55426 S fradiae ammoglycoside acetyltransferase (aacCδ) gene, complete cds Streptomyces fradiae 37,097 05-MAY-1 GB_PR3 AC004500 77538 AC004500 Homo sapiens chromosome 5, P1 clone 1076B9 (LBNL H14), complete Homo sapiens 33,256 30-MAR-1 sequence rxa02474 897 GB_BA1 AB009078 2686 AB009078 Brevibacterium saccharolyticum gene for L-2 3-butanedιol dehydrogenase, Brevibacterium 96,990 13-Feb-9 complete cds saccharolyticum GB_OM BTU71200 877 U71200 Bos taurus acetom reductase mRNA, complete cds Bos taurus 51 ,659 8-Oct-97 GB_EST2 F12685 287 F12685 HSC3DA031 normalized infant brain cDNA Homo sapiens cDNA clone c- Homo sapiens 41 ,509 14-Mar-9 3da03, mRNA sequence rxa02480 1779 GB BA1 MTV012 70287 AL021287 Mycobacterium tuberculosis H37Rv complete genome, segment 132/162 Mycobacterium 36,737 23-Jun-99 tuberculosis Table 4 (continued) GB_BA1 SC6G10 36734 AL049497 Streptomyces coelicolor cosmid 6G10 Streptomyces coelicolor 35,511 24-MAR-1 GB_BA1 AP000060 347800 AP000060 Aeropyrum pernix genomic DNA, section 3/7 Aeropyrum pernix 48,014 22-Jun-9 rxa02485 rxa02492 840 GB_BA1 STMPGM 921 M83661 Streptomyces coelicolor phosphoglycerate mutase (PGM) gene, complete cds Streptomyces coelicolor 65,672 26-Apr-93 GB_BA1 MTCY20G9 37218 Z77162 Mycobacterium tuberculosis H37Rv complete genome, segment 25/162 Mycobacterium 61 ,436 17-Jun-9 tuberculosis GB_BA1 U00018 42991 U00018 Mycobacterium leprae cosmid B2168 Mycobacterium leprae 37,893 01-MAR-1 rxa02528 1098 GB_PR2 HS161 N10 56075 AL008707 Human DNA sequence from PAC 161 N10 on chromosome Xq25 Contains Homo sapiens 37,051 23-Nov-9 EST GB_HTG2 AC008235 136017 AC008235 Drosophila melanogaster chromosome 3 clone BACR15B19 (D995) RPCI-98 Drosophila melanogaster 36,822 2-Aug-99 15 B 19 map 94F-95A strain y, cn bw sp, *** SEQUENCING IN PROGRESS ***, 125 unordered pieces GBJHTG2 AC008235 136017 AC008235 Drosophila melanogaster chromosome 3 clone BACR15B19 (D995) RPCI-98 Drosophila melanogaster 36,822 2-Aug-99 15 B 19 map 94F-95A strain y, cn bw sp, *** SEQUENCING IN PROGRESS * * * , 125 unordered pieces rxa02539 1641 GB_BA2 RSU17129 17425 U17129 Rhodococcus erythropohs ThcA (thcA) gene, complete cds, and unknown Rhodococcus erythropohs 66,117 16-Jul-99 genes GB_BA1 MTV038 16094 AL021933 Mycobacterium tuberculosis H37Rv complete genome, segment 24/162 Mycobacterium 65,174 17-Jun-9 tuberculosis GB_BA2 AF068264 3152 AF068264 Pseudomonas aeruginosa quinoprotem ethanol dehydrogenase (exaA)gene, Pseudomonas aeruginosa 65,448 18-MAR-1 partial cds, cytochrome c550 precursor (exaB), NAD+ dependent acetaldehyde dehydrogenase (exaC), and pyrroloquinohne quinone synthesis A (pqqA) genes, complete cds, and pyrroloquinohne quinone synthesis B (pqqB) gene, partial cds rxa02551 483 GB_BA1 BACHYPTP 17057 D29985 Bacillus subtihs wapA and orf genes for wall-associated protein and Bacillus subtihs 53,602 7-Feb-99 hypothetical proteins GB_BA1 BACHUTWAPA28954 D31856 Bacillus subtihs genome containing the hut and wapA loci Bacillus subtihs 53,602 7-Feb-99 GB_BA1 BSGBGLUC 4290 Z34526 B subtihs (Marburg 168) genes for beta-glucoside permease and beta- Bacillus subtihs 53,602 3-Jul-95 glucosidase rxa02556 1281 GBJHTG3 AC008128 335761 AC008128 Homo sapiens, *** SEQUENCING IN PROGRESS *** , 106 unordered pieces Homo sapiens 34,022 22-Aug-9 GB_HTG3 AC008128 335761 AC008128 Homo sapiens, ** * SEQUENCING IN PROGRESS *** , 106 unordered pieces Homo sapiens 34,022 22-Aug-9 GB_PL2 AC005292 99053 AC005292 Genomic sequence for Arabidopsis thaliana BAC F26F24, complete sequence Arabidopsis thaliana 33,858 16-Apr-9 rxa02560 990 GBJN1 CEF07A11 35692 Z66511 Caenorhabditis elegans cosmid F07A11 , complete sequence Caenorhabditis elegans 3 366,,442200 2-Sep-99 GB_EST32 AI731605 566 AI731605 BNLGH 0201 Six-day Cotton fiber Gossypium hirsutum cDNA 5' similar to Gossypium hirsutum 38,095 11-Jun-9 (AC004684) hypothetical protein [Arabidopsis thaliana], mRNA sequence GBJN1 CEF07A11 35692 Z66511 Caenorhabditis elegans cosmid F07A11 , complete sequence Caenorhabditis elegans 33,707 2-Sep-99 Table 4 (continued) rxa02572 668 GB_BA1 MTCY63 38900 Z96800 Mycobacterium tuberculosis H37Rv complete genome, segment 16/162 Mycobacterium 61 ,677 17-Jun-98 tuberculosis GB_BA1 MTCY63 38900 Z96800 Mycobacterium tuberculosis H37Rv complete genome, segment 16/162 Mycobacterium 37,170 17-Jun-98 tuberculosis GBJHTG1 HS24H01 46989 AL121632 Homo sapiens chromosome 21 clone LLNLc116H0124 map 21q21 , *** Homo sapiens 19,820 29-Sep-9 SEQUENCING IN PROGRESS ***, in unordered pieces rxa02596 1326 GB_BA1 MTV026 23740 AL022076 Mycobacterium tuberculosis H37Rv complete genome, segment 157/162 Mycobacterium 36,957 24-Jun-99 tuberculosis GB_BA2 AF026540 1778 AF026540 Mycobacterium tuberculosis UDP-galactopyranose mutase (glf) gene, complete Mycobacterium 67,627 30-OCT-1 cds tuberculosis GB_BA2 MTU96128 1200 U96128 Mycobacterium tuberculosis UDP-galactopyranose mutase (glf) gene, complete Mycobacterium 70,417 25-MAR-1 cds tuberculosis rxa02611 1775 GB_BA1 MTCY130 32514 Z73902 Mycobacterium tuberculosis H37Rv complete genome, segment 59/162 Mycobacteπum 38,532 17-Jun-98 tuberculosis GB_BA1 MSGY151 37036 AD000018 Mycobacteπum tuberculosis sequence from clone y151 Mycobacterium 60,575 10-DEC-1 tuberculosis GB_BA1 U00014 36470 U00014 Mycobacterium leprae cosmid B1549 Mycobacterium leprae 57,486 29-Sep-9 rxa02612 2316 GB_BA1 MTCY130 32514 Z73902 Mycobacterium tuberculosis H37Rv complete genome, segment 59/162 Mycobacterium 38,018 17-Jun-98 tuberculosis GB_BA1 MSGY151 37036 AD000018 Mycobacterium tuberculosis sequence from clone y151 Mycobacterium 58,510 10-DEC-1 tuberculosis GB_BA1 STMGLGEN 2557 L11647 Streptomyces aureofaciens glycogen branching enzyme (glgB) gene, complete Streptomyces 57,193 25-MAY-1 cds aureofaciens rxa02621 942 GB_BA1 CGL133719 1839 AJ 133719 Corynebacterium glutamicum yjcc gene, amtR gene and citE gene, partial Corynebacterium 36,858 12-Aug-9 glutamicum GBJN1 CEM106 39973 Z46935 Caenorhabditis elegans cosmid M106, complete sequence Caenorhabditis elegans 37,608 2-Sep-99 GB_EST29 AI547662 377 AI547662 UI-R-C3-sz-h-03-0-UI s1 UI-R-C3 Rattus norvegicus cDNA clone UI-R-C3-sz-h- Rattus norvegicus 50,667 3-Jul-99 03-0-UI 3', mRNA sequence rxa02640 1650 GB_BA1 MTV025 121125 AL022121 Mycobacterium tuberculosis H37Rv complete genome, segment 155/162 Mycobacterium 39,187 24-Jun-9 tuberculosis GB_BA1 PAU49666 4495 U49666 Pseudomonas aeruginosa (orfX), glycerol dflffusion facilitator (glpF), glycerol Pseudomonas aeruginosa 59,273 18-MAY-1 kinase (glpK), and Glp repressor (glpR) genes, complete cds, and (orfK) gene, partial cds GB_BA1 AB015974 1641 AB015974 Pseudomonas tolaasu glpK gene for glycerol kinase, complete cds Pseudomonas tolaasu 58,339 28-Aug-9 rxa02654 1008 GB_EST6 N65787 512 N65787 20827 Lambda-PRL2 Arabidopsis thaliana cDNA clone 232B7T7, mRNA Arabidopsis thaliana 39,637 5-Jan-98 sequence GB_PL2 T17H3 65839 AC005916 Arabidopsis thaliana chromosome 1 BAC T17H3 sequence, complete Arabidopsis thaliana 33,735 5-Aug-99 sequence GB_RO MMU58105 88871 U58105 Mus musculus Btk locus, alpha-D-galactosidase A (Ags), πbosomal protein Mus musculus 35,431 13-Feb-9 (L44L), and Bruton's tyrosine kinase (Btk) genes, complete cds rxa02666 891 GB PR3 AC004643 43411 AC004643 Homo sapiens chromosome 16, cosmid clone 363E3 (LANL), complete Homo sapiens 38,851 01-MA -1 sequence Table 4 (continued) GB_PR3 AC004643 43411 AC004643 Homo sapiens chromosome 16, cosmid clone 363E3 (LANL), complete Homo sapiens 41 ,599 01-MAY-1 sequence GB_BA2 AF049897 9196 AF049897 Corynebactenum glutamicum N-acetylglutamylphosphate reductase (argC), Corynebacterium 40,413 l-Jul-98 ornithine acetyltransferase (argJ), N-acetylglutamate kinase (argB), glutamicum acetylornithine traπsaminase (argD), ornithine carbamoyltransferase (argF), arginine repressor (argR), argininosuccinate synthase (argG), and argininosuccinate lyase (argH) genes, complete cds rxa02675 1980 GB BA1 PDENQOURF 10425 L02354 Paracoccus denitnficans NADH dehydrogenase (URF4), (NQ08), (NQ09), Paracoccus denitnficans 40,735 20-MAY-1 (URF5), (URF6), (NQO10), (NQ011 ), (NQ012), (NQ013), and (NQ014) genes, complete cds's, biotin [acetyl-CoA carboxyl] hgase (birA) gene, complete cds GB BA1 MTCY339 42861 Z77163 Mycobacterium tuberculosis H37Rv complete genome, segment 101/162 Mycobacterium 36,471 17-Jun-98 tuberculosis GB_BA1 MXADEVRS 2452 L19029 Myxococcus xanthus devR and devS genes, complete cds's Myxococcus xanthus 38,477 27-Jan-94 rxa02694 1065 GB_BA1 BACLDH 1147 19394 B caldolyticus lactate dehydrogenase (LDH) gene, complete cds Bacillus caldolyticus 57,371 26-Apr-93 GB_BA1 BACLDHL 1361 M14788 B stearothermophilus let gene encoding L-lactate dehydrogenase, complete Bacillus 57,277 26-Apr-93 cds stearothermophilus GB_PAT A06664 1350 A06664 B stearothermophilus let gene Bacillus 57,277 29-Jul-93 stearothermophilus rxa02729 844 GB_EST15 AA494626 121 AA494626 fa09d04 r1 Zebrafish ICRFzfls Danio reno cDNA clone 11A22 5' similar to Danio reno 50,746 27-Jun-97 TR G1171163 G1171163 G/T-MISMATCH BINDING PROTEIN „ mRNA sequence GB EST15 AA494626 121 AA494626 fa09d04 r1 Zebrafish ICRFzfls Danio reno cDNA clone 11 A22 5' similar to Danio reno 36,364 27-Jun-97 TR G1171163 G1171163 G/T-MISMATCH BINDING PROTEIN „ mRNA sequence rxa02730 1161 GB_EST19 AA758660 233 AA758660 ah67d06 s1 Soares_testιs_NHT Homo sapiens cDNA clone 1320683 3', mRNA Homo sapiens 37,059 29-DEC-1 sequence GB EST15 AA494626 121 AA494626 fa09d04 Zebrafish ICRFzfls Danio reno cDNA clone 11A22 5' similar to Danio reno 42,149 27-Jun-9 TR G1171163 G1171163 G T-MISMATCH BINDING PROTEIN „ mRNA sequence GB_PR4 AC006285 150172 AC006285 Homo sapiens, complete sequence Homo sapiens 37,655 15-Nov-9 rxa02737 1665 GB PAT E13655 2260 E13655 gDNA encoding glucose-6-phosphate dehydrogenase Corynebactenum 99,580 24-Jun-9 glutamicum GB_BA1 MTCY493 40790 Z95844 Mycobacteπum tuberculosis H37Rv complete genome, segment 63/162 Mycobacterium 38,363 19-Jun-9 tuberculosis GB_BA1 SC5A7 40337 AL031107 Streptomyces coelicolor cosmid 5A7 Streptomyces coelicolor 39,444 27-Jul-98 rxa02738 1203 GB_PAT E 13655 2260 E 13655 gDNA encoding glucose-6-phosphate dehydrogenase Corynebacterium 98,226 24-Jun-98 glutamicum GB_BA1 SCC22 22115 AL096839 Streptomyces coelicolor cosmid C22 Streptomyces coelicolor 60,399 12-Jul-99 GB_BA1 SC5A7 40337 AL031107 Streptomyces coelicolor cosmid 5A7 Streptomyces coelicolor 36,426 27-Jul-98 rxa02739 2223 GB BA1 AB023377 2572 AB023377 Corynebacterium glutamicum tkt gene for transketolase, complete cds Corynebacterium 99,640 20-Feb-9 glutamicum Table 4 (continued) GB_BA1 MLCL536 36224 Z99125 Mycobacterium leprae cosmid L536 Mycobacterium leprae 61 ,573 04-DEC-1 GB BA1 U00013 35881 U00013 Mycobacterium leprae cosmid B1496 Mycobacterium leprae 61 ,573 01-MAR-1 rxa02740 1053 GBJHTG2 AC006247 174368 AC006247 Drosophila melanogaster chromosome 2 clone BACR48I10 (D505) RPCI-98 Drosophila melanogaster 37,105 2-Aug-99 48 1 10 map 49E6-49F8 strain y, cn bw sp, * * * SEQUENCING IN PROGRESS *** , 17 unordered pieces GB_HTG2 AC006247 174368 AC006247 Drosophila melanogaster chromosome 2 clone BACR48I10 (D505) RPCI-98 Drosophila melanogaster 37,105 2-Aug-99 48 I 10 map 49E6^19F8 strain y, cn bw sp, *** SEQUENCING IN PROGRESS ** *, 17 unordered pieces GB_HTG3 AC007150 121474 AC007150 Drosophila melanogaster chromosome 2 clone BACR16P13 (D597) RPCI-98 Drosophila melanogaster 38,728 20-Sep-9 16 P 13 map 49E-49F strain y, cn bw sp, *** SEQUENCING IN PROGRESS *** , 87 unordered pieces rxa02741 1089 GB_HTG2 AC004951 129429 AC004951 Homo sapiens clone DJ1022I14, *** SEQUENCING IN PROGRESS *** , 14 Homo sapiens 33,116 12-Jun-98 unordered pieces GB_HTG2 AC004951 129429 AC004951 Homo sapiens clone DJ1022I14, *** SEQUENCING IN PROGRESS ***, 14 Homo sapiens 33,116 12-Jun-9 unordered pieces GBJN1 AB006546 931 AB006546 Ephydatia fluviatihs mRNA for G protein a subunit 4, partial cds Ephydatia fluviatihs 36,379 23-Jun-9 rxa02743 1161 GB_BA1 MLCL536 36224 Z99125 Mycobacterium leprae cosmid L536 Mycobacterium leprae 48,401 04-DEC-1 GB_BA1 U00013 35881 U00013 Mycobacterium leprae cosmid B1496 Mycobacterium leprae 48,401 01-MAR-1 GB_HTG2 AC007401 83657 AC007401 Homo sapiens clone NH0501O07, ' SEQUENCING IN PROGRESS ' Homo sapiens 37,128 26-Jun-9 unordered pieces rxa02797 1026 GB_BA1 CGBETPGEN 2339 X93514 C glutamicum betP gene Corynebacterium 38,889 8-Sep-97 glutamicum GB_GSS9 AQ148714 405 AQ148714 HS_3136_A1_A03_MR CIT Approved Human Genomic Sperm Library D Homo Homo sapiens 34,321 08-OCT-1 sapiens genomic clone Plate=3136 Col=5 Row=A, genomic survey sequence GB_BA1 BFU64514 3837 U64514 Bacillus firmus dppABC operon, dipeptide transporter protein dppA gene, Bacillus firmus 38,072 1-Feb-97 partial cds, and dipeptide transporter proteins dppB and dppC genes, complete cds rxa02803 680 GB_BA1 U00020 36947 U00020 Mycobacterium leprae cosmid B229 Mycobacterium leprae 34,462 01 -MAR- GB BA2 PSU85643 4032 U85643 Pseudomonas syπngae pv syπngae putative dihydropteroate synthase gene, Pseudomonas syπngae pv 5 500,,444455 9-Apr-97 partial cds, regulatory protein MrsA (mrsA), tπose phosphate isomerase (tpiA) synngae transport protein SecG (secG), tRNA-Leu, tRNA-Met, and 15 kDa protein genes, complete cds GB_BA1 SC6G4 41055 AL031317 Streptomyces coelicolor cosmid 6G4 Streptomyces coelicolor 59,314 20-Aug-9 rxa02821 363 GB_HTG2 AC008105 91421 AC008105 Homo sapiens chromosome 17 clone 2020_K_17 map 17, *** SEQUENCING Homo sapiens 37,607 22-Jul-99 IN PROGRESS *** , 12 unordered pieces GB_HTG2 AC008105 91421 AC008105 Homo sapiens chromosome 17 clone 2020_K_17 map 17, *** SEQUENCING Homo sapiens 37,607 22-Jul-99 IN PROGRESS ***, 12 unordered pieces GB EST33 AV117143 222 AV117143 AV117143 Mus musculus C57BL/6J 10-day embryo Mus musculus cDNA clone Mus musculus 40,157 30-Jun-99 2610200J17, mRNA sequence Table 4 (continued) rxa02829 373 GB_HTG1 HSU9G8 48735 AL008714 Homo sapiens chromosome X clone LL0XNC01-9G8, ** * SEQUENCING IN Homo sapiens 41 ,595 23-Nov-9 PROGRESS * **, in unordered pieces GB_HTG1 HSU9G8 48735 AL008714 Homo sapiens chromosome X clone LL0XNC01-9G8, *** SEQUENCING IN Homo sapiens 41 ,595 23-NOV-9 PROGRESS * ** , in unordered pieces GB_PR3 HSU85B5 39550 Z69724 Human DNA sequence from cosmid U85B5, between markers DXS366 and Homo sapiens 41 ,595 23-NOV-9 DXS87 on chromosome X rxc03216 1141 GB HTG3 AC008184 151720 AC008184 Drosophila melanogaster chromosome 2 clone BACR04D05 (D540) RPCI-98 Drosophila melanogaster 39,600 2-Aug-99 04 D 5 map 36E5-36F2 strain y, cn bw sp, *** SEQUENCING IN PROGRESS ***, 27 unordered pieces GB EST15 AA477537 411 AA477537 zu36g12 r1 Soares ovary tumor NbHOT Homo sapiens cDNA clone Homo sapiens 37,260 9-Nov-97 IMAGE 740134 5' similar to contains Alu repetitive element, contains element HGR repetitive element ,, mRNA sequence GB_EST26 Al 330662 412 AI330662 fa91d08 y1 zebrafish fin dayl regeneration Danio reno cDNA 5', mRNA Danio reno 37,805 28-DEC-1 sequence rxs03215 1038 GB_BA1 SC3F9 19830 AL023862 Streptomyces coelicolor cosmid 3F9 Streptomyces coelicolor 48,657 10-Feb-9 A3(2) GB_BA1 SLLINC 36270 X79146 S hncolnensis (78-11) Lincomycin production genes Streptomyces hncolnensis 39,430 15-MAY-1 GB_HTG5 AC009660 204320 AC009660 Homo sapiens chromosome 15 clone RP11-424J10 map 15, *** SEQUENCING H Hoommoo ssaappiieennss 35,151 04-DEC-1 IN PROGRESS * * *, 41 unordered pieces rxs03224 1288 GB_PR3 AC004076 41322 AC004076 Homo sapiens chromosome 19, cosmid R30217, complete sequence Homo sapiens 37,788 29-Jan-98 GB_PL2 SPAC926 23193 AL110469 S pombe chromosome I cosmid c926 Schizosaccharomyces 38,474 2-Sep-99 pombe GB BA2 AE001081 11473 AE001081 Archaeoglobus fulgidus section 26 of 172 of the complete genome Archaeoglobus fulgidus 35,871 15-DEC-1 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/1 sucrose, 2.46 g/1 MgSO 4 x 7H 2 O, 10 ml/1 KH 2 PO 4 solution (100 g/1, adjusted to pH 6.7 with KOH), 50 ml/1 M12 concentrate (10 g/1 (NH 4 ) 2 SO 4 , 1 g/1 NaCl, 2 g/1 MgSO 4 x 7H 2 O, 0.2 g/1 CaCl 2 , 0.5 g/1 yeast extract (Difco), 10 ml/1 trace-elements-mix (200 mg/1 FeSO 4 x H 2 O, 10 mg/1 ZnSO 4 x 7 H 2 O, 3 mg/1 MnCl 2 x 4 H 2 O, 30 mg/1 H 3 BO 3 20 mg/1 CoCl, x 6 H 2 O, 1 mg/1 NiCl 2 x 6 H 2 O, 3 mg/1 Na 2 MoO 4 x 2 H 2 O, 500 mg/1 complexing agent (EDTA or critic acid), 100 ml/1 vitamins-mix (0.2 mg/1 biotin, 0.2 mg/1 folic acid, 20 mg/1 p-amino benzoic acid, 20 mg/1 riboflavin, 40 mg/1 ca-panthothenate, 140 mg/1 nicotinic acid, 40 mg/1 pyridoxole hydrochloride, 200 mg/1 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 R aseA 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 oi 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 & 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 & Cohen (1978) J. Bacteriol 134:1 141-1156), plasmids of the pBS series (pBSSK+, pBSSK- and others; Stratagene, LaJolla, USA), or cosmids as SuperCosl (Stratagene, LaJolla, USA) or Loristό (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 pBLl) 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 & 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. 159306-31 1), 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 & Murray (1983) J. Mol. Biol. 166:1-19). Genes may be overexpressed in C. glutamicum strains using plasmids which comprise pCGl (U.S. Patent No. 4,617,267) or fragments thereof, and optionally the gene for kanamycin resistance from TN903 (Grindley, N.D. and Joyce, CM. (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 α/. (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, raffmose, 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 C1 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 0 o of O.5 - 1.5 using cells grown on agar plates, such as CM plates (10 g/1 glucose, 2,5 g/1 NaCl, 2 g/1 urea, 10 g/1 polypeptone, 5 g/1 yeast extract, 5 g/1 meat extract, 22 g/1 NaCl, 2 g/1 urea, 10 g/1 polypeptone, 5 g/1 yeast extract, 5 g/1 meat extract, 22 g/1 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 r ed. Academic Press: New York; Bisswanger, H., (1994) Enzymkinetik, 2 nd ed. VCH: Weinheim (ISBN 3527300325); Bergmeyer, H.U., Bergmeyer, J., GraBl, M., eds. (1983-1986) Methods of Enzymatic Analysis, 3 r ed., vol. I-XII, Verlag Chemie: Weinheim; and Ullmann'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'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. & 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'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 SMP 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 SMP 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: 1 1- 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 αl (1995) Science 270: 467-470; Wodicka, L. et αl. (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: 1 193-1202; 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, 5 S-cysteine, 14 C-labelled amino acids, 15 N-amino acids, 15 NO 3 or 15 NH + 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.

Claims: What is claimed: 1. An isolated nucleic acid molecule from Corynebacterium glutamicum encoding an SMP protein, or a portion thereof, provided that the nucleic acid molecule does not consist of any of the F-designated genes set forth in Table 1. 2. The isolated nucleic acid molecule of claim 1, wherein said nucleic acid molecule encodes an SMP protein involved in the production of a fine chemical. 3. An isolated Corynebacterium glutamicum nucleic acid molecule selected from the group consisting of those sequences set forth as odd-numbered SEQ ID NOs of the Sequence Listing, or a portion thereof, provided that the nucleic acid molecule does not consist of any of the F-designated genes set forth in Table 1. 4. An isolated nucleic acid molecule which ' encodes a polypeptide sequence selected from the group consisting of those sequences set forth as even-numbered SEQ ID NOs of the Sequence Listing,, provided that the nucleic acid molecule does not consist of any of the F-designated genes set forth in Table 1. 5. An isolated nucleic acid molecule which encodes a naturally occurring allelic variant of a polypeptide selected from the group of amino acid sequences consisting of those sequences set forth in as even-numbered SEQ ID NOs of the Sequence Listing, provided that the nucleic acid molecule does not consist of any of the F-designated genes set forth in Table 1. 6. An isolated nucleic acid molecule comprising a nucleotide sequence which is at least 50% homologous to a nucleotide sequence selected from the group consisting of those sequences set forth as odd-numbered SEQ ID NOs of the Sequence Listing, or a portion thereof, provided that the nucleic acid molecule does not consist of any of the F-designated genes set forth in Table 1. 7. An isolated nucleic acid molecule comprising a fragment of at least 15 nucleotides of a nucleic acid comprising a nucleotide sequence selected from the group consisting of those sequences set forth as odd-numbered SEQ ID NOs of the Sequence Listing, provided that the nucleic acid molecule does not consist of any of the F-designated genes set forth in Table 1. 8. An isolated nucleic acid molecule which hybridizes to the nucleic acid molecule of any one of claims 1-7 under stringent conditions. 9. An isolated nucleic acid molecule comprising the nucleic acid molecule of any one of claims 1-8 or a portion thereof and a nucleotide sequence encoding a heterologous polypeptide. 10. A vector comprising the nucleic acid molecule of any one of claims 1-9. 11. The vector of claim 10, which is an expression vector. 12. A host cell transfected with the expression vector of claim 11. 13. The host cell of claim 12, wherein said cell is a microorganism. 14. The host cell of claim 13, wherein said cell belongs to the genus Corynebacterium or Brevibacterium. 15. The host cell of claim 12, wherein the expression of said nucleic acid molecule results in the modulation in production of a fine chemical from said cell. 16. The host cell of claim 15, wherein said fine chemical is selected from the group consisting of: organic acids, proteinogenic and nonproteinogenic amino acids, purine and pyrimidine bases, nucleosides, nucleotides, lipids, saturated and unsaturated fatty acids, diols, carbohydrates, aromatic compounds, vitamins, cofactors, polyketides, and enzymes. 17. A method of producing a polypeptide comprising culturing the host cell of claim 12 in an appropriate culture medium to, thereby, produce the polypeptide. 18. An isolated SMP polypeptide from Corynebacterium glutamicum, or a portion thereof. 19. The polypeptide of claim 18, wherein said polypeptide is involved in the production of a fine chemical. 20. An isolated polypeptide comprising an amino acid sequence selected from the group consisting of those sequences set forth as even-numbered SEQ ID NOs of the Sequence Listing, provided that the amino acid sequence is not encoded by any of the F-designated genes set forth in Table 1. 21. An isolated polypeptide comprising a naturally occurring allelic variant of a polypeptide comprising an amino acid sequence selected from the group consisting of those sequences set forth as even-numbered SEQ ID NOs of the Sequence Listing, or a portion thereof, provided that the amino acid sequence is not encoded by any of the F-designated genes set forth in Table 1. 22. The isolated polypeptide of any of claims 18-21, further comprising heterologous amino acid sequences. 23. An isolated polypeptide which is encoded by a nucleic acid molecule comprising a nucleotide sequence which is at least 50% homologous to a nucleic acid selected from the group consisting of those sequences set forth as odd-numbered SEQ ID NOs of the Sequence Listing, provided that the nucleic acid molecule does not consist of any of the F-designated nucleic acid molecules set forth in Table 1. 24. An isolated polypeptide comprising an amino acid sequence which is at least 50% homologous to an amino acid sequence selected from the group consisting of those sequences as even-numbered SEQ ID NOs of the Sequence Listing, provided that the amino acid sequence is not encoded by any of the F-designated genes set forth in Table 1. 25. A method for producing a fine chemical, comprising culturing a cell containing a vector of claim 12 such that the fine chemical is produced. 26. The method of claim 25, wherein said method further comprises the step of recovering the fine chemical from said culture. 27. The method of claim 25, wherein said method further comprises the step of transfecting said cell with the vector of claim 1 1 to result in a cell containing said vector. 28. The method of claim 25, wherein said cell belongs to the genus Corynebacterium or Brevibacterium. 29. The method of claim 25, wherein said cell is selected from the group consisting of: Corynebacterium glutamicum, Corynebacterium herculis, Corynebacterium, lilium, Corynebacterium acetoacidophilum, Corynebacterium acetoglutamicum, Corynebacterium acetophilum, Corynebacterium ammoniagenes, Corynebacterium fujiokense, Corynebacterium nitrilophilus, Brevibacterium ammoniagenes, Brevibacterium butanicum, Brevibacterium divaricatum, Brevibacterium flavum, Brevibacterium healii, Brevibacterium ketoglutamicum, Brevibacterium ketosoreductum, Brevibacterium lactofermentum, Brevibacterium linens, Brevibacterium paraffinolyticum, and those strains set forth in Table 3. 30. The method of claim 25, wherein expression of the nucleic acid molecule from said vector results in modulation of production of said fine chemical. 31. The method of claim 25, wherein said fine chemical is selected from the group consisting of: organic acids, proteinogenic and nonproteinogenic amino acids, purine and pyrimidine bases, nucleosides, nucleotides, lipids, saturated and unsaturated fatty acids, diols, carbohydrates, aromatic compounds, vitamins, cofactors, polyketides, and enzymes. 32. The method of claim 25, wherein said fine chemical is an amino acid. 33. The method of claim 32, wherein said amino acid is drawn from the group consisting of: lysine, glutamate, glutamine, alanine, aspartate, glycine, serine, threonine, methionine, cysteine, valine, leucine, isoleucine, arginine, proline, histidine, tyrosine, phenylalanine, and tryptophan. 34. A method for producing a fine chemical, comprising culturing a cell whose genomic DNA has been altered by the inclusion of a nucleic acid molecule of any one of claims 1-9. 35. A method for diagnosing the presence or activity of Corynebacterium diphtheriae in a subject, comprising detecting the presence of one or more of SEQ ID NOs 1 through 782 of the Sequence Listing in the subject, provided that the sequences are not or are not encoded by any of the F-designated sequences set forth in Table 1, thereby diagnosing the presence or activity of Corynebacterium diphtheriae in the subject. 36. A host cell comprising a nucleic acid molecule selected from the group consisting of the nucleic acid molecules set forth as odd-numbered SEQ ID NOs of the Sequence Listing, wherein the nucleic acid molecule is disrupted. 35. 37. A host cell comprising a nucleic acid molecule selected from the group consisting of the nucleic acid molecules set forth as odd-numbered SEQ ID NOs in the Sequence Listing, wherein the nucleic acid molecule comprises one or more nucleic acid modifications from the sequence set forth as odd-numbered SEQ ID NOs of the Sequence Listing s. 38. A host cell comprising a nucleic acid molecule selected from the group consisting of the nucleic acid molecules set forth as odd-numbered SEQ ID NOs of the Sequence Listing, wherein the regulatory region of the nucleic acid molecule is modified relative to the wild-type regulatory region of the molecule.

Inventors: HABERHAUER GREGOR, KROEGER BURKHARD, POMPEJUS MARKUS, SCHROEDER HARTWIG, ZELDER OSKAR, HABERHAUER, GREGOR, KROEGER, BURKHARD, POMPEJUS, MARKUS, SCHROEDER, HARTWIG, ZELDER, OSKAR
Applicants: BASF AG, BASF AKTIENGESELLSCHAFT
Application year: 2000
Main classification: C12N15
IPC codes: C07K14, C12N1, C12N5, C12N9, C12N15, C12P13, C12P21, C12Q1, C12R1, G01N33