PharMolix/UniProtQA huggingface dataset:
Protein: TEBP_MACFA
Sequence: MQPASAKWYDRRDYVFIEFCVEDSKDVNVNFEKSKLTFSCLGGSDNFKHLNEIDLFHCIDPNDSKHKRTDRSILCCLRKGESGQSWPRLTKERAKLNWLSVDFNNWKDWEDDSDEDMSNFDRFSEMMNNMGGDEDVDLPEVDGADDDSQDSDDEKMPDLE
What is the function of this protein?
Cytosolic prostaglandin synthase that catalyzes the oxidoreduction of prostaglandin endoperoxide H2 (PGH2) to prostaglandin E2 (PGE2).  Molecular chaperone that localizes to genomic response elements in a hormone-dependent manner and disrupts receptor-mediated transcriptional activation, by promoting disassembly of transcriptional regulatory complexes.  Facilitates HIF alpha proteins hydroxylation via interaction with EGLN1/PHD2, leading to recruit EGLN1/PHD2 to the HSP90 pathway.
What are the official names of this protein?
Prostaglandin E synthase 3, Cytosolic prostaglandin E2 synthase, cPGES.
What is the protein family that this protein belongs to?
Belongs to the p23/wos2 family.
Protein: PDXT_STRPI
Sequence: MKIGILALQGAFAEHAKVLDQLGVESVELRNLDDFQQDQSDLSGLILPGGESTTMGKLLRDQNMLLPIREAILSGLPVFGTCAGLILLAKEITSQKESHLGTMDMVVERNAYGRQLGSFYTEAECKGVGKIPMTFIRGPIISSVGEGVEILATVNNQIVAAQEKNMLVSSFHPELTDDVRLHQYFINMCKEKS
What is the function of this protein?
Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate.  The resulting ammonia molecule is channeled to the active site of PdxS.
What are the official names of this protein?
Pyridoxal 5'-phosphate synthase subunit PdxT, Pdx2, Pyridoxal 5'-phosphate synthase glutaminase subunit.
What is the protein family that this protein belongs to?
Belongs to the glutaminase PdxT/SNO family.
Protein: AROC_ECOK1
Sequence: MAGNTIGQLFRVTTFGESHGLALGCIVDGVPPGIPLTEADLQHDLDRRRPGTSRYTTQRREPDQVKILSGVFEGVTTGTSIGLLIENTDQRSQDYSAIKDVFRPGHADYTYEQKYGLRDYRGGGRSSARETAMRVAAGAIAKKYLAEKFGIEIRGCLTQMGDIPLEIKDWSQVEQNPFFCPDPDKIDALDELMRALKKEGDSIGAKVTVVASGVPAGLGEPVFDRLDADIAHALMSINAVKGVEIGDGFDVVALRGSQNRDEITKDGFQSNHAGGILGGISSGQKIIAHMALKPTSSITVPGRTINRFGEEVEMITKGRHDPCVGIRAVPIAEAMLAIVLMDHLLRQRAQNADVKTDIPRW
What is the function of this protein?
Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis.  This reaction introduces a second double bond into the aromatic ring system.
What are the official names of this protein?
Chorismate synthase, CS, 5-enolpyruvylshikimate-3-phosphate phospholyase.
What is the protein family that this protein belongs to?
Belongs to the chorismate synthase family.
Protein: CRYD_ORYSJ
Sequence: MLHFLSSSSPLNPQFLLLPRQSARLRVLLSIPVSAMSSSSSSSSRGALAAAAVPSLSADEAGAAADEAFLRYTSPSMRRSGGGGVAIVWFRNDLRVLDNEAVVRAWAASDAVLPVYCVDPRISAGSTHYFGFPKTGALRAQFLIECLEDLKRNLTKQGLDLLIRHGKPEDILPSIAKAVTAHTVYAHKETCSEELLVEHLVRKGLEQVVIPQGGASNQKKPRNPKLQLIWGATLYHVDDLPFSVNNLPDVYTQFRKAVESKSSVRNCSKLPPSLGPPPGSGLDEIGGWGTVPTLESLGLSMTKAEKGMHFVGGESAALGRVHEYFWKKDQLKVYKETRNGMLGPDYSTKFSPWLASGSLSPRYICEEVKRYEKQRIANDSTYWVLFELIWRDYFRFISAKYGNSIFHLGGPRNVESKWSQDQALFESWRDGRTGYPLIDANMKELLATGFMSNRGRQIVCSFLVRDMGIDWRMGAEWFETCLLDYDPASNYGNWTYGAGVGNDPREDRYFSIPKQAKTYDPDGEYVAYWLPELRSIAKERRNFPGASYIKQVVPLKFDGGHQKRDQQFNRQRRPGHMYRRQK
What is the function of this protein?
May have a photoreceptor function.  Binds ss- and ds-DNA in a sequence non-specific manner, lacks photolyase activity (By similarity).
What are the official names of this protein?
Cryptochrome DASH, chloroplastic/mitochondrial.
What is the protein family that this protein belongs to?
Belongs to the DNA photolyase class-1 family.
What are the subcellular locations of this protein?
Plastid, chloroplast. Mitochondrion.
Protein: RPOTF_PRRSL
Sequence: MSGTFSRCMCTPAARVFWNAGQVFCTRCLSARSLLSPELQDTDLGAVGLFYKPRDKLHWKVPIGIPQVECTPSGCCWLSAVFPLARMTSGNHNFLQRLVKVADVLYRDGCLAPRHLRELQVYERGCNWYPITGPVPGMGLFANSMHVSDQPFPGATHVLTNSPLPQQACRQPFCPFEEAHSSVYRWKKFVVFTDSSLNGRSRMMWTPESDDSAALEVLPPELERQVEILIRSFPAHHPVDLADWELTESPENGFSFNTSHSCGHLVQNPDVFDGKCWLSCFLGQSVEVRCHEEHLADAFGYQTKWGVHGKYLQRRLQVRGIRAVVDPDGPIHVEALSCPQSWIRHLTLDDDVTPGFVRLTSLRIVPNTEPTTSRIFRFGAHKWYGAAGKRARAKRAAKSEKDSAPTPKVALPVPTCGITTYSPPTDGSCGWHVLAAIMNRMINGDFTSPLTQYNRPEDDWASDYDLVQAIQCLRLPATVVRNRACPNAKYLIKLNGVHWEVEVRSGMAPRSLSRECVVGVCSEGCVAPPYPADGLPKRALEALASAYRLPSDCVSSGIADFLANPPPQEFWTLDKMLTSPSPERSGFSSLYKLLLEVVPQKCGATEGAFIYAVERMLKDCPSSKQAMALLAKIKVPSSKAPSVSLDECFPTDVLADFEPASQERPQSSGAAVVLCSPDAKEFEEAAPEEVQESGHKAVHSALLAEGPNNEQVQVVAGEQLKLGGCGLAVGNAHEGALVSAGLINLVGGNLSPSDPMKENMLNSREDEPLDLSQPAPASTTTLVREQTPDNPGSDAGALPVTVREFVPTGPILCHVEHCGTESGDSSSPLDLSDAQTLDQPLNLSLAAWPVRATASDPGWVHGRREPVFVKPRNAFSDGDSALQFGELSESSSVIEFDRTKDAPVVDAPVDLTTSNEALSVVDPFEFAELKRPRFSAQALIDRGGPLADVHAKIKNRVYEQCLQACEPGSRATPATREWLDKMWDRVDMKTWRCTSQFQAGRILASLKFLPDMIQDTPPPVPRKNRASDNAGLKQLVAQWDRKLSVTPPPKPVGPVLDQIVPPPTDIQQEDVTPSDGPPHAPDFPSRVSTGGSWKGLMLSGTRLAGSISQRLMTWVFLKFSPTSQLLCSHFSRRGALWLQVIGCLQVSFYLLSCSVVLTRYSDAFPYWVSFLVLCGVFVWVFLVLGWLLLYFYSRLHPTQSVLLVTTIRRSVMLSFWLLSSANFGNLCAALWSAPQASYVSFLASYSVGHVISGMFSYVYACLQIWPFLLFMWCPRGVVTSVGESV
What is the function of this protein?
Plays a role in viral replication.
What are the official names of this protein?
Replicase polyprotein 1TF, ORF1ab polyprotein.
What are the subcellular locations of this protein?
[Nsp1]: Host nucleus. Host cytoplasm. SUBCELLULAR LOCATION: [Nsp1-alpha papain-like cysteine proteinase]: Host nucleus. Host cytoplasm. SUBCELLULAR LOCATION: [Nsp1-beta papain-like cysteine proteinase]: Host nucleus. SUBCELLULAR LOCATION: [Nsp2TF]: Host cytoplasm. Host membrane; Multi-pass membrane protein. Note=Nsp2 and nsp2TF localize to different intracellular compartments.
Protein: SDCS_STAAB
Sequence: MAYFNQHQSMISKRYLTFFSKSKKKKPFSAGQLIGLILGPLLFLLTLLFFHPQDLPWEGVYVLAITLWIATWWITEAIPIAATSLLPIVLLPLGHILTPEQVSSEYGNDIIFLFLGGFILAIAMERWNLHTRVALTIINLIGASTSKILLGFMVATGFLSMFVSNTAAVMIMIPIGLAIIKEAHDLQEANTNQTSIQKFEKSLVLAIGYAGTIGGLGTLIGTPPLIILKGQYMQHFGHEISFAKWMIVGIPTVIVLLGITWLYLRYVAFRHDLKYLPGGQTLIKQKLDELGKMKYEEKVVQTIFVLASLLWITREFLLKKWEVTSSVADGTIAIFISILLFVIPAKNTEKHRRIIDWEVAKELPWGVLILFGGGLALAKGISESGLAKWLGEQLKSLNGVSPILIVIVITIFVLFLTEVTSNTATATMILPILATLSVAVGVHPLLLMAPAAMAANCAYMLPVGTPPNAIIFGSGKISIKQMASVGFWVNLISAIIIILVVYYVMPIVLGIDINQPLPLK
What is the function of this protein?
Mediates the transport of the dicarboxylates fumarate, malate, and succinate across the cytoplasmic membrane via a Na(+)-electrochemical gradient.
What are the official names of this protein?
Sodium-dependent dicarboxylate transporter SdcS, Na(+)/dicarboxylate symporter.
What is the protein family that this protein belongs to?
Belongs to the SLC13A/DASS transporter (TC 2.A.47) family. NADC subfamily.
What are the subcellular locations of this protein?
Cell membrane; Multi-pass membrane protein.
Protein: UVRC_DEIGD
Sequence: MHFDDLPVLPASPGVYIFRRGGTPIYIGKAVNLRSRVAQHFKAGGKSGKFTALADSLDFITTRNEVEALILEANLIKQHRPHYNVLLKDDKHYPFLKLTNEAFPMLVVTRRVLKDGASYYGPYPDASAVRRVKHLIDTMFPLRKNSGLPMQKKPRPCLNYHMGRCLGPCVDAADPQAYAQVVEDVKALLEGRAAPVIARLKADMQAAARAQDFEQAARLRDRVQAVEKLFGTEQHAYVSEETDLDFLGVAQAGEYAMVQLFRLRGGRVVGRDKRFLVGAEGGADVGEVLGAFVQDYYTQATHVPPLILLPAEFEDAPVWSAFLSERAGRRVEMRTPKRGDKAELVEMAQRNAAAGLESELALLERRGDHPGLDALREVLALPDRPWRIEGYDNSNLFGSNIVSGMVVFEGGRARRSEHRRFKVRGLDHPDDYAAMHQTITRRLTGSLADKLPLPDLILIDGGRGQVHAALDALRAADVRVPLVGLAKREERIILPGRFGAQWWLETGTEVGVGGELLLPHTHPALRVLIGVRDEVHHYAVSYHRTLRGEQMLRSVFDDLPGIGQKRRDALLEHFTSLEDLAAAPVERIAAVPGMNLRAAQSVKKFLAERTANGTPT
What is the function of this protein?
The UvrABC repair system catalyzes the recognition and processing of DNA lesions.  UvrC both incises the 5' and 3' sides of the lesion.  The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision.
What are the official names of this protein?
UvrABC system protein C, Protein UvrC, Excinuclease ABC subunit C.
What is the protein family that this protein belongs to?
Belongs to the UvrC family.
What are the subcellular locations of this protein?
Cytoplasm.
Protein: PLSY_JANMA
Sequence: MNTVLFALGAYLIGSISFAVVVSKCFRLADPRSYGSKNPGATNVLRSGNKKAAILTLLGDGAKGFLAVWLVKHFGPGYGVHENGVALVAIAVFLGHLWPVFFRFVGGKGVATALGVLLALNGWLGLATLVTWLVIAYAFRYSSLAALIAAIFAPFYYGLLFGPDVILLAVLAMSILLVYRHSKNIGNLLAGKESRLGSKKK
What is the function of this protein?
Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA).  This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
What are the official names of this protein?
Glycerol-3-phosphate acyltransferase, Acyl-PO4 G3P acyltransferase, Acyl-phosphate--glycerol-3-phosphate acyltransferase, G3P acyltransferase, GPAT, Lysophosphatidic acid synthase, LPA synthase.
What is the protein family that this protein belongs to?
Belongs to the PlsY family.
What are the subcellular locations of this protein?
Cell inner membrane; Multi-pass membrane protein.
Protein: YIHI_SHISS
Sequence: MKPSSSNSRSKGHAKARRKTREELDQEARDRKRQKKRRGHAPGSRAAGGNTTSGSKGQNAPKDPRIGSKTPIPLGVAEKVTKQHKPKSEKPMLSPQAELELLETDERLDALLERLEAGETLSAEEQSWVDAKLDRIDELMQKLGLSYDDDEEEEEDEKQEDMMRLLRGN
What is the function of this protein?
A GTPase-activating protein (GAP) that modifies Der/EngA GTPase function.  May play a role in ribosome biogenesis.
What are the official names of this protein?
Der GTPase-activating protein YihI.
What is the protein family that this protein belongs to?
Belongs to the YihI family.
Protein: ANDC_EMEVA
Sequence: MGFLQDKVVIITGAAAGIGLATATAALDEGARVFGIDLAPAPTSLQENPNFEFLRADLTDHDCPKRAVQACIAAFGQRIDGLLNVAGIADNYGSADSVTDEVWDRCLAVNLAAPVKLMREVIPIMREAGKGSIVNTSSKAGLSGASSGVAYTASKHGLIGVTKNVAWRFKTEGIRCNAISVATEMGMTGDFSLWDQAAMEAMRPIHAAHMDMGIGATIKAEEVAQTLLFLVSDLSRRVNGAVIPVDDAWSTI
What is the function of this protein?
Short chain dehydrogenase; part of the gene cluster that mediates the biosynthesis of anditomin, a fungal meroterpenoid (PubMed:25216349).  The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid (DMOA) by the polyketide synthase andM (PubMed:25216349).  DMOA is then converted to the phthalide compound 5,7-dihydroxy-4,6-dimethylphthalide (DHDMP) by the cytochrome P450 monooxygenase andK, which is further prenylated by the prenyltransferase andD to yield farnesyl-DHDMP (PubMed:25216349).  Further epoxidation by the FAD-dependent monooxygenase andE leads to epoxyfarnesyl-DHDMP (PubMed:25216349).  The next step involves the terpene cyclase andB that converts epoxyfarnesyl-DHDMP into preandiloid A through opening of the epoxide ring followed by the cyclization of the farnesyl moiety (PubMed:25216349).  Preandiloid A is in turn oxidized at the C-3 hydroxyl group to yield preandiloid B by the dehydrogenase andC (PubMed:25216349).  The dioxygenase andA is solely responsible for the dehydrogenation of preandiloid B leading to the enone preandiloid C, as well as for the intriguing structural rearrangement to generate the bicyclo[2. 2. 2]octane core, transforming preandiloid C into andiconin (PubMed:25216349).  FAD-binding monooxygenase andJ then produces andilesin D which is reduced by dehydrogenase andI to yield andilesin A (PubMed:25216349).  Action of acetyltransferase andG followed by a spontaneous acetate elimination leads then to andilesin B, which is in turn substrate of the short chain dehydrogenase andH to yield andilesin C (PubMed:25216349).  Finally, the dioxygenase andF catalyzes the transformation of andilesin C to anditomin (PubMed:25216349).
What are the official names of this protein?
Short chain dehydrogenase andC, Anditomin synthesis protein C.
What is the protein family that this protein belongs to?
Belongs to the short-chain dehydrogenases/reductases (SDR) family.
Protein: TIGAR_BOVIN
Sequence: MTRFALTVVRHGETRLNKEKIIQGQGIDEPLSETGFKQAAAAGIFLKDVKFTHVFSSDLTRTKQTVHGILEKSKFCKDMTVKYDSRLRERKYGVAEGRPLSELRAMAKAAGEECPAFTPPGGETLDQLKRRGKDFFEFLCQLILKEAGQNEQFSQEAPSSCLESSLAEIFPLGKNCASTFNSDSGTPGLAASVLVVSHGAYIRSLLDYFLTDLKCSFPATLSRSELTSVSPNTGMTVFILNFEKGGKGRPTAQCVCVNLQGHLAGVNKTP
What is the function of this protein?
Fructose-bisphosphatase hydrolyzing fructose-2,6-bisphosphate as well as fructose-1,6-bisphosphate (By similarity).  Acts as a negative regulator of glycolysis by lowering intracellular levels of fructose-2,6-bisphosphate in a p53/TP53-dependent manner, resulting in the pentose phosphate pathway (PPP) activation and NADPH production.  Contributes to the generation of reduced glutathione to cause a decrease in intracellular reactive oxygen species (ROS) content, correlating with its ability to protect cells from oxidative or metabolic stress-induced cell death.  Plays a role in promoting protection against cell death during hypoxia by decreasing mitochondria ROS levels in a HK2-dependent manner through a mechanism that is independent of its fructose-bisphosphatase activity.  In response to cardiac damage stress, mediates p53-induced inhibition of myocyte mitophagy through ROS levels reduction and the subsequent inactivation of BNIP3.  Reduced mitophagy results in an enhanced apoptotic myocyte cell death, and exacerbates cardiac damage.  Plays a role in adult intestinal regeneration; contributes to the growth, proliferation and survival of intestinal crypts following tissue ablation.  Plays a neuroprotective role against ischemic brain damage by enhancing PPP flux and preserving mitochondria functions.  Protects glioma cells from hypoxia- and ROS-induced cell death by inhibiting glycolysis and activating mitochondrial energy metabolism and oxygen consumption in a TKTL1-dependent and p53/TP53-independent manner.  Plays a role in cancer cell survival by promoting DNA repair through activating PPP flux in a CDK5-ATM-dependent signaling pathway during hypoxia and/or genome stress-induced DNA damage responses.  Involved in intestinal tumor progression.
What are the official names of this protein?
Fructose-2,6-bisphosphatase TIGAR, TP53-induced glycolysis and apoptosis regulator, TP53-induced glycolysis regulatory phosphatase.
What is the protein family that this protein belongs to?
Belongs to the phosphoglycerate mutase family.
What are the subcellular locations of this protein?
Cytoplasm. Nucleus. Mitochondrion. Note=Translocated to the mitochondria during hypoxia in a HIF1A-dependent manner. Colocalizes with HK2 in the mitochondria during hypoxia. Translocated to the nucleus during hypoxia and/or genome stress-induced DNA damage responses in cancer cells. Translocation to the mitochondria is enhanced in ischemic cortex after reperfusion and/or during oxygen and glucose deprivation (OGD)/reoxygenation insult in primary neurons.
Protein: FBXW5_MOUSE
Sequence: MDEGGLPLLPDSLVYQIFLSLGPADVLAAGLVCRQWQAVSRDEFLWKEQFYRYYQVARDVPRHPAATSWYEEFRRLYDMVPCVEVQTLKEHTDQVLHLSFSHSGYQFASCSKDCTVKIWNNDLTISLLHSADMRPYNWSYTQFSQFNQDDSLLLASGVFLGPHNSSSGEIAVISLDSFALLSRVRNKPYDVFGCWLTETSLISGNLHRIGDITSCSVLWLNNAFQDVESENVNVVKRLFKIQNLNASTIRTVMVADCSRFDSPDLLLDASDQAGLPCRVFDLGGDTEEEATDPGLHTSGSDHVKKGLRRVFDSVLDGHGQLSDCALETKVAELLAQGHTKPPECNDADTRNKYLIFTTGCLTYSPHQIGIKQILPHQMTTAGPVLGEGRGSDAFFDALDHVIDVHGHIIGMGLSPDNRYLYVNSRAWPPGSVVADPMQPPPIAEEIDLLVFDLKTMREVKRALRAHRAYTPNDECFFIFLDVSRDFVASGAEDRHGYIWDRHYNICLAKLRHEDVVNSVAFSPQEQELLLTASDDATIKAWRSPRIVRVLQAPRPRPRPRPRPFFSWFASHRR
What is the function of this protein?
Substrate recognition component of both SCF (SKP1-CUL1-F-box protein) and DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes.  Substrate-specific adapter of the DCX(FBXW5) E3 ubiquitin-protein ligase complex which mediates the polyubiquitination and subsequent degradation of TSC2.  May also act as a negative regulator of MAP3K7/TAK1 signaling in the interleukin-1B (IL1B) signaling pathway.  Substrate recognition component of the SCF(FBXW5) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of SASS6 during S phase, leading to prevent centriole reduplication (By similarity).  The SCF(FBXW5) complex also mediates ubiquitination and degradation of actin-regulator EPS8 during G2 phase, leading to the transient degradation of EPS8 and subsequent cell shape changes required to allow mitotic progression.
What are the official names of this protein?
F-box/WD repeat-containing protein 5, F-box and WD-40 domain-containing protein 5.
What is the protein family that this protein belongs to?
Belongs to the FBXW5 family.
What are the subcellular locations of this protein?
Cytoplasm.
Protein: EASC_CLAFS
Sequence: MASQVSLTAQGSGLSAPLNGPEHLTSTTVENDPRLLDILSRFNREKIPERAVHARGAGAYGEFEVTHDVSDICDIDMLLGIGKKTPCAVRFSTTALERGSAESVRDVKGMAIKLFTGDGEWDWVCLNIPMFFIRDPSKFPDLVHAQRPDPATNLANPAAWWEFVCNNHESLHMAVFLFTDFGTMFDYRSMSGYVSHAYKWVMPDGTWKYVHWFLASDQGPNFEQGNQTREAAPNDSESATRDLYQSLERGECPSWTVKVQVIDPEDAPRLAFNILDVSKHWNLGNYPPDIPVIPERCVGKLTLKKGPENYFEEIEKLAFSPSHLVHGVEPSEDPMLQARLFAYPDAQEHRLGPQFSDMAAKRTGHAANDAPKTKKPAVPLQKQSREHAEWVSQVTSSSWSQPNETDYKFPRELWAALPRLRGEEFQNRLVVNMAESVSQIPEDLRQKVYKTLALVAEDLASRVESLTEEMVVPEQRPRL
What is the function of this protein?
Catalase; part of the gene cluster that mediates the biosynthesis of fungal ergot alkaloid (PubMed:17720822).  DmaW catalyzes the first step of ergot alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4-dimethylallyl-L-tryptophan (By similarity).  The second step is catalyzed by the methyltransferase easF that methylates 4-dimethylallyl-L-tryptophan in the presence of S-adenosyl-L-methionine, resulting in the formation of 4-dimethylallyl-L-abrine (By similarity).  The catalase easC and the FAD-dependent oxidoreductase easE then transform 4-dimethylallyl-L-abrine to chanoclavine-I which is further oxidized by easD in the presence of NAD(+), resulting in the formation of chanoclavine-I aldehyde (By similarity).  Agroclavine dehydrogenase easG then mediates the conversion of chanoclavine-I aldehyde to agroclavine via a non-enzymatic adduct reaction: the substrate is an iminium intermediate that is formed spontaneously from chanoclavine-I aldehyde in the presence of glutathione (By similarity).  Further conversion of agroclavine to paspalic acid is a two-step process involving oxidation of agroclavine to elymoclavine and of elymoclavine to paspalic acid, the second step being performed by the elymoclavine oxidase cloA (PubMed:17720822).  However, cloA does not encode a functional enzyme indicating that C. fusiformis terminates its ergot alkaloid pathway at elymoclavine (PubMed:17720822).
What are the official names of this protein?
Catalase easC, Ergot alkaloid synthesis protein C.
What is the protein family that this protein belongs to?
Belongs to the catalase family.
Protein: SYP_THEYD
Sequence: MRYSKLFIPTMREIPSGINAISHILMLKAGYVRQLAAGLFIFLPLGWRVLNKINMILKEEMERIGAQEISMPILHPAEIWQETGRWYTIKEEMFRLKDRTGRDMCLGMTHEEIMTWIASKEIKSYRQLPQIWYQIQTKLRDEARPRGGVLRTREFIMKDSYSFDIDWEGLDKSYNLHAEAYHRIFTKCGLKYYQVESDPGIMGDMESHEFMAPTPAGEDEIVLCDSCGYSANIEVAKSELPTLPSLNFEYKEIYTPEKKSVKEVSDFLGLSEKYFIKTLIVISEKNGPVLVMLRGDQELNEKKLARIIGEFSFATSEQALEILGVELGFVGPVGHKIKKIADFSIQKEISYISGANKKNYHLQGIIPGIHFDAQWADIRRVKEEDRCPKCGNSLKIEKAIEVGNIFKLGTKYTEPLHAYFLDKDGKEKPIIMGSYGIGPARVAAAAIEQNHDSDGIIWPKSISPFDIEIIPLNMDDEKTVSIAEELYEKVTEIYNSFADRHMEVLIDDRDERPGVKFKDADLIGIPIQIVIGKKGLKENKVEIKKRRTKETKKVSVNKAVVEIVNSYYETY
What is the function of this protein?
Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro).  As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine.  One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP.  The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Ala-tRNA(Pro).  The misacylated Cys-tRNA(Pro) is not edited by ProRS.
What are the official names of this protein?
Proline--tRNA ligase, Prolyl-tRNA synthetase, ProRS.
What is the protein family that this protein belongs to?
Belongs to the class-II aminoacyl-tRNA synthetase family. ProS type 1 subfamily.
What are the subcellular locations of this protein?
Cytoplasm.
Protein: IMB3_YEAST
Sequence: MSALPEEVNRTLLQIVQAFASPDNQIRSVAEKALSEEWITENNIEYLLTFLAEQAAFSQDTTVAALSAVLFRKLALKAPPSSKLMIMSKNITHIRKEVLAQIRSSLLKGFLSERADSIRHKLSDAIAECVQDDLPAWPELLQALIESLKSGNPNFRESSFRILTTVPYLITAVDINSILPIFQSGFTDASDNVKIAAVTAFVGYFKQLPKSEWSKLGILLPSLLNSLPRFLDDGKDDALASVFESLIELVELAPKLFKDMFDQIIQFTDMVIKNKDLEPPARTTALELLTVFSENAPQMCKSNQNYGQTLVMVTLIMMTEVSIDDDDAAEWIESDDTDDEEEVTYDHARQALDRVALKLGGEYLAAPLFQYLQQMITSTEWRERFAAMMALSSAAEGCADVLIGEIPKILDMVIPLINDPHPRVQYGCCNVLGQISTDFSPFIQRTAHDRILPALISKLTSECTSRVQTHAAAALVNFSEFASKDILEPYLDSLLTNLLVLLQSNKLYVQEQALTTIAFIAEAAKNKFIKYYDTLMPLLLNVLKVNNKDNSVLKGKCMECATLIGFAVGKEKFHEHSQELISILVALQNSDIDEDDALRSYLEQSWSRICRILGDDFVPLLPIVIPPLLITAKATQDVGLIEEEEAANFQQYPDWDVVQVQGKHIAIHTSVLDDKVSAMELLQSYATLLRGQFAVYVKEVMEEIALPSLDFYLHDGVRAAGATLIPILLSCLLAATGTQNEELVLLWHKASSKLIGGLMSEPMPEITQVYHNSLVNGIKVMGDNCLSEDQLAAFTKGVSANLTDTYERMQDRHGDGDEYNENIDEEEDFTDEDLLDEINKSIAAVLKTTNGHYLKNLENIWPMINTFLLDNEPILVIFALVVIGDLIQYGGEQTASMKNAFIPKVTECLISPDARIRQAASYIIGVCAQYAPSTYADVCIPTLDTLVQIVDFPGSKLEENRSSTENASAAIAKILYAYNSNIPNVDTYTANWFKTLPTITDKEAASFNYQFLSQLIENNSPIVCAQSNISAVVDSVIQALNERSLTEREGQTVISSVKKLLGFLPSSDAMAIFNRYPADIMEKVHKWFA
What is the function of this protein?
Plays a role in protein secretion.
What are the official names of this protein?
Importin subunit beta-3, Karyopherin subunit beta-3, Karyopherin-121, Protein secretion enhancer 1.
What is the protein family that this protein belongs to?
Belongs to the importin beta family. Importin beta-3 subfamily.
What are the subcellular locations of this protein?
Cytoplasm. Nucleus.
Protein: DENR_YEAST
Sequence: MLREVIYCGICSYPPEYCEFSGKLKRCKVWLSENHADLYAKLYGTDDNTQEVEAVTNKLAESSIGEAREEKLEKDLLKIQKKQENREQRELAKKLSSKVIIKREARTKRKFIVAISGLEVFDIDMKKLAKTFASRFATGCSVSKNAEKKEEVVIQGDVMDEVETYIHSLLEEKGLKDVKVETIDAKKKKKPAAEGAAK
What are the official names of this protein?
Translation machinery-associated protein 22, Density-regulated protein homolog.
What is the protein family that this protein belongs to?
Belongs to the DENR family.
What are the subcellular locations of this protein?
Cytoplasm.
Protein: DAPB_GEOSM
Sequence: MVKIAVCGAAGRMGGRIIAAVKEAEGVEICGALERPGHPMVGQDAGYNAGLGAIGVAISDDLNAVVQACDVLIDFTAPKVSLKNLEVCALYGKSIVIGSTGFTPEERALAAELARDIPVIIAPNMSVGVNVCFKVLADVAKILGEDFDVEIVESHHRLKKDSPSGTAVRMGEVVAGALGRDYNKVANYHREGICGERTHDEIGMQTVRGGDIVGEHTVYFIGMGERIEITHRAHTRDMFSRGSVRAAKWVVTAKQGVYDMQDVLGLR
What is the function of this protein?
Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.
What are the official names of this protein?
4-hydroxy-tetrahydrodipicolinate reductase, HTPA reductase.
What is the protein family that this protein belongs to?
Belongs to the DapB family.
What are the subcellular locations of this protein?
Cytoplasm.
Protein: KN14N_ARATH
Sequence: MVGAMANNGRIRSAFPVTNGSKDLTPNSAPASTTGSEYGPVEFTREDVETLLNERIKYKSKFNYKERCENMMDYIKRLRLCIRWFQELELDYAFEQEKLKNALELNEKHCVDMEVSLKNKEEELNMIIEELRKNFESVQVQLAREQTEKLAANDSLGKEKEARLSVEKAQAGLTEELGKAQGDLQTANQRIQSVNDMYKLLQEYNSSLQLYNSKLQGDLDEAHETIKRGEKERTAIIENIGNLKGQFSALQEQLAASKASQEDIMKQKGELVNEIASLKVELQQVKDDRDRHLVEVKTLQTEATKYNDFKDAITELETTCSSQSTQIRQLQDRLVNSERRLQVSDLSTFEKMNEYEDQKQSIIDLKSRVEEAELKLVEGEKLRKKLHNTILELKGNIRVFCRVRPLLPGENNGDEGKTISYPTSLEALGRGIDLMQNAQKHAFTFDKVFAPTASQEDVFTEISQLVQSALDGYKVCIFAYGQTGSGKTYTMMGRPGNVEEKGLIPRCLEQIFETRQSLRSQGWKYELQVSMLEIYNETIRDLLSTNKEAVRTDSGVSPQKHAIKHDASGNTHVAELTILDVKSSREVSFLLDHAARNRSVGKTQMNEQSSRSHFVFTLRISGVNESTEQQVQGVLNLIDLAGSERLSKSGSTGDRLKETQAINKSLSSLGDVIFALAKKEDHVPFRNSKLTYLLQPCLGGDAKTLMFVNIAPESSSTGESLCSLRFAARVNACEIGTPRRQTNIKPLENRLSLG
What are the official names of this protein?
Kinesin-like protein KIN-14N, AtKIN14d, Kinesin-like protein KatC.
What is the protein family that this protein belongs to?
Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Kinesin family. KIN-14 subfamily.
What are the subcellular locations of this protein?
Cytoplasm, cytoskeleton.