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D2Y499 | MKLTTVLIVAVLVLAACQFTVTDNSGDDTENPSLRSAGENQNPDSTKTITARATRARTNMRRGLSRPSKGCIGGGDPCEFHRGYTCCSEHCIIWVCA | Function: Probable neurotoxin with unknown target. Possibly targets ion channels.
Sequence Mass (Da): 10448
Sequence Length: 97
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Subcellular Location: Secreted
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P0DQD4 | CKGKGASCRRTSYDCCTGSCRLGRC | Function: Omega-conotoxins act at presynaptic membranes, they bind and block voltage-gated calcium channels. This toxin blocks N-type calcium channels (Cav2.2/CACNA1B). It shows a higher potency when Cav2.2/CACNA1B is only expressed with the ancillary subunit CACNB3 (IC(50)=0.1 nM) than on Cav2.2/CACNA1B expressed with the ancillary subunits CACNA2D1 and CACNB3 (IC(50)=19.9 nM). The Cav2.2/CACNA1B block by this toxin is voltage-independent, whereas the recovery from toxin block is voltage-dependent . There is a low recovery at physiological membrane potential and a high recovery with hyperpolarized potential . This indicates that the toxin has a higher affinity for Cav2.2/CACNA1B in the inactivated state . It is noteworthy that ancillary subunits beta modulate recovery from this toxin block . Cav2.2/CACNA1B expressed with the ancillary subunit CACNB2a (isoform 2a) almost recover completely from this toxin block, whereas an expression with CACNB3 exhibits relatively weak recovery . Inhibition by this toxin of excitatory synaptic transmission is reversible . In vivo, when tested on rat model of persistent pain, this toxin blocks chronic pain behavior .
Sequence Mass (Da): 2672
Sequence Length: 25
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Subcellular Location: Secreted
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O06994 | MSEWWKEAVVYQIYPRSFYDANGDGFGDLQGVIQKLDYIKNLGADVIWLSPVFDSPQDDNGYDISDYKNMYEKFGTNEDMFQLIDEVHKRGMKIVMDLVVNHTSDEHAWFAESRKSKDNPYRDYYLWKDPKPDGSEPNNWGSIFSGSAWTYDEGTGQYYLHYFSKKQPDLNWENEAVRREVYDVMRFWMDRGVDGWRMDVIGSISKYTDFPDYETDHSRSYIVGRYHSNGPRLHEFIQEMNREVLSHYDCMTVGEANGSDIEEAKKYTDASRQELNMIFTFEHMDIDKEQNSPNGKWQIKPFDLIALKKTMTRWQTGLMNVGWNTLYFENHDQPRVISRWGNDRKLRKECAKAFATVLHGMKGTPFIYQGEEIGMVNSDMPLEMYDDLEIKNAYRELVVENKTMSEKEFVKAVMIKGRDHARTPMQWDAGKHAGFTAGDPWIPVNSRYQDINVKESLEDQDSIFFYYQKLIQLRKQYKIMIYGDYQLLQENDPQVFSYLREYRGEKLLVVVNLSEEKALFEAPPELIHERWKVLISNYPQERADLKSISLKPYEAVMGISI | Function: Hydrolyzes various disaccharides such as sucrose, maltose, and isomaltose with different efficiencies. Also hydrolyzes longer maltodextrins from maltotriose up to maltohexaose, but not maltoheptaose, palatinose, isomaltotriose, or isomaltotetraose.
Catalytic Activity: Hydrolysis of (1->6)-alpha-D-glucosidic linkages in some oligosaccharides produced from starch and glycogen by alpha-amylase, and in isomaltose.
Sequence Mass (Da): 66081
Sequence Length: 561
Subcellular Location: Cytoplasm
EC: 3.2.1.10
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O34364 | MKTDWWKDAVVYQIYPRSFQDSNGDGIGDLRGIISRLDYIKELGADVIWICPIYPSPNVDYGYDVTNHKAIMDSYGTMDDFHELLDQVHQRGLKLVMDFVLNHTSVEHPWFKEAELDKNSKYRSYYYWRPGTKNGPPTDWLSNYGCPVWQYEEHTGEYYLHMNAVKQADLNWENPEVRQAVYDMMKFWLDKGVDGLRIDQLHLISKKEYLPSYEDYINQQAEPKPFQPNGERIHDYLKEITDEVFSHYDVMSVGEVGSVTPEEGLKYTGTDKHELNMIFHFQHMELDQQPGKEHWDLKPLELSDLKSVLTKWQKKLEHQGWNTLFWCNHDQPRIVSRFGDDGEYRKASAKMLAAVIYFMKGTPYIYQGEEIGMTNAPFTRIEDYKDIQTINMYHKRVFEKGYDPNDVMRSILAKSRDHARTPMQWNSGKNAGFTDGTPWLKVNPNFTAINVEEAQGDPDSVLNYYKKLISLRKQYADLMKGSFDLLLPDDPQLFVYMRENSKQQLLSVNNFSKEQAVFQWPKNCGKAQASLLLSNYNNDDLDDEMVFRPYESRVYLLDKTN | Catalytic Activity: Hydrolysis of (1->6)-alpha-D-glucosidic linkages in some oligosaccharides produced from starch and glycogen by alpha-amylase, and in isomaltose.
Sequence Mass (Da): 65816
Sequence Length: 561
Subcellular Location: Cytoplasm
EC: 3.2.1.10
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O05242 | MKKAWWKEAVVYQIYPRSFKDSNGDGIGDIQGIRTKLSYIKELGADVIWICPLYDSPNADNGYDIRDYQNILSEFGTMEDFDELLGDIHDLDMKLIMDLVVNHTSDEHPWFIESRSSIHSEKRDWYIWKDGKNGKTPNNWESIFGGPAWEYDQKTSQYYLHLFDKKQPDLNWENEKVRNAVYDMINWWLDKGIDGFRVDAITHIKKKEGFPDMPNPKGLDYVPSFPYHMNADGIMDLLTELKENTFSRYPIMTVGEANGVAAKEAADWAGEKNGIFSMIFQFEHLGLWDVEINESIDIVAFKRILTDWQDSLEGIGWNALFMENHDQPRSVSVWGDDGVYLKESAKALSAVYFLMKGTPFIYQGQELGMTNVAFPSIEDYDDVALKRLYETKTAKGTSHEDVMKIVWKKGRDNSRTPMQWNAGPYAGFSEAKPWIGINENYKWLNAEAQKNDKTSVYHFYKSLIKLRQTYDVFINGTYELILPEDQQIFAYLRKNESHTALIAANLTGTPALFRHSGLPLSSDALVLSNIETEPHKHMTSVLLKPYEARIYLWC | Catalytic Activity: Hydrolysis of (1->6)-alpha-D-glucosidic linkages in some oligosaccharides produced from starch and glycogen by alpha-amylase, and in isomaltose.
Sequence Mass (Da): 63969
Sequence Length: 554
Subcellular Location: Cytoplasm
EC: 3.2.1.10
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P21332 | MEKQWWKESVVYQIYPRSFMDSNGDGIGDLRGIISKLDYLKELGIDVIWLSPVYESPNDDNGYDISDYCKIMNEFGTMEDWDELLHEMHERNMKLMMDLVVNHTSDEHNWFIESRKSKDNKYRDYYIWRPGKEGKEPNNWGAAFSGSAWQYDEMTDEYYLHLFSKKQPDLNWDNEKVRQDVYEMMKFWLEKGIDGFRMDVINFISKEEGLPTVETEEEGYVSGHKHFMNGPNIHKYLHEMNEEVLSHYDIMTVGEMPGVTTEEAKLYTGEERKELQMVFQFEHMDLDSGEGGKWDVKPCSLLTLKENLTKWQKALEHTGWNSLYWNNHDQPRVVSRFGNDGMYRIESAKMLATVLHMMKGTPYIYQGEEIGMTNVRFESIDEYRDIETLNMYKEKVMERGEDIEKVMQSIYIKGRDNARTPMQWDDQNHAGFTTGEPWITVNPNYKEINVKQAIQNKDSIFYYYKKLIELRKNNEIVVYGSYDLILENNPSIFAYVRTYGVEKLLVIANFTAEECIFELPEDISYSEVELLIHNYDVENGPIENITLRPYEAMVFKLK | Catalytic Activity: Hydrolysis of (1->6)-alpha-D-glucosidic linkages in some oligosaccharides produced from starch and glycogen by alpha-amylase, and in isomaltose.
Sequence Mass (Da): 66013
Sequence Length: 558
Subcellular Location: Cytoplasm
EC: 3.2.1.10
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Q60881 | MANKNNVTELIFTGLFQDPEVQKVCFVLFLPVYLATLLGNSLILVAVSISKTLHSPMYFFLSSLSLVEICYSSTIVPKFITDLLAKVKTISLKGCLTQIFFSHFFGVVEVILLVVMAYDRYVAICKPLHYMNIMSRQVCHMLVAGSWLGGFIHSIIQIIITIPLPFCGPNVIDHYFCDLQQLFKLACTDTFMEGFIVMANSGLISIVSLFILVSSYAVILISLRKRSAEGRRKALSTCASHITVVILFFVPGAFIYMRPSSTFTEDKLVSVFYTVITPMLNPIVYTLRNTEMKNAIRMSWKQKDS | Function: Odorant receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34312
Sequence Length: 305
Subcellular Location: Cell membrane
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Q60878 | MDSPRNVTEFFMLGLSQNPQVQRMLFGLFLLVFLVSVGGNMLIIITITFSPTLGSPMYFFLSYLSFIDTCYSSCMTPKLIADSLHEGRAISFEGCLAQFFVAHLLGGTEIILLTVMAYDRYVAICKPLHYTTTMTRHVCIVLVAVAWLGGILHSTAQLFLVLQLPFCGPNVINHFVCDLYPLLELACTDTYVIGLLVVANSGVICLLNFLMLAASYIVILRTLRSHSAEGRRKALSTCGAHFTVVALFFVPCIFIYMRPSSTLSIDKIVAVFYCILTPMFNPLIYTLRNAEVKNAMKNLWRK | Function: Odorant receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 33734
Sequence Length: 302
Subcellular Location: Cell membrane
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Q8NGJ6 | MSIINTSYVEITTFFLVGMPGLEYAHIWISIPICSMYLIAILGNGTILFIIKTEPSLHEPMYYFLSMLAMSDLGLSLSSLPTVLSIFLFNAPEISSNACFAQEFFIHGFSVLESSVLLIMSFDRFLAIHNPLRYTSILTTVRVAQIGIVFSFKSMLLVLPFPFTLRNLRYCKKNQLSHSYCLHQDVMKLACSDNRIDVIYGFFGALCLMVDFILIAVSYTLILKTVLGIASKKEQLKALNTCVSHICAVIIFYLPIINLAVVHRFARHVSPLINVLMANVLLLVPPLTNPIVYCVKTKQIRVRVVAKLCQRKI | Function: Odorant receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35256
Sequence Length: 313
Subcellular Location: Cell membrane
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Q9Y5P1 | MWPNITAAPFLLTGFPGLEAAHHWISIPFFAVYVCILLGNGMLLYLIKHDHSLHEPMYYFLTMLAGTDLMVTLTTMPTVMGILWVNHREISSVGCFLQAYFIHSLSVVESGSLLAMAYDCFIAIRNPLRYASILTNTRVIALGVGVFLRGFVSILPVILRLFSFSYCKSHVITRAFCLHQEIMRLACADITFNRLYPVILISLTIFLDCLIILFSYILILNTVIGIASGEERAKALNTCISHISCVLIFYVTVMGLTFIYRFGKNVPEVVHIIMSYIYFLFPPLMNPVIYSIKTKQIQYGIIRLLSKHRFSS | Function: Odorant receptor.
PTM: Ubiquitinated by the CRL2(FEM1A) and CRL2(FEM1C) complexes, which recognize the -Lys-Xaa-Xaa-Arg C-degron at the C-terminus, leading to its degradation.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35373
Sequence Length: 312
Subcellular Location: Cell membrane
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Q9Y5P0 | MWYNNSAGPFLLTGFLGSEAVHYRISMSFFVIYFSVLFGNGTLLVLIWNDHSLHEPMYYFLAMLADTDLGMTFTTMPTVLGVLLLDQREIAHAACFTQSFIHSLAIVESGILLVLAYDCFIAIRTPLRYNCILTNSRVMNIGLGVLMRGFMSILPIILSLYCYPYCGSRALLHTFCLHQDVIKLACADITFNHIYPIIQTSLTVFLDALIIIFSYILILKTVMGIASGQEEAKSLNTCVSHISCVLVFHITVMGLSFIHRFGKHAPHVVPITMSYVHFLFPPFVNPIIYSIKTKQIQRSIIRLFSGQSRA | Function: Odorant receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34912
Sequence Length: 310
Subcellular Location: Cell membrane
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Q9H339 | MSSSGSSHPFLLTGFPGLEEAHHWISVFFLFMYISILFGNGTLLLLIKEDHNLHEPMYFFLAMLAATDLGLALTTMPTVLGVLWLDHREIGSAACFSQAYFIHSLSFLESGILLAMAYDRFIAICNPLRYTSVLTNTRVVKIGLGVLMRGFVSVVPPIRPLYFFLYCHSHVLSHAFCLHQDVIKLACADTTFNRLYPAVLVVFIFVLDYLIIFISYVLILKTVLSIASREERAKALITCVSHICCVLVFYVTVIGLSLIHRFGKQVPHIVHLIMSYAYFLFPPLMNPITYSVKTKQIQNAILHLFTTHRIGT | Function: Odorant receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35241
Sequence Length: 312
Subcellular Location: Cell membrane
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Q9H340 | MGLNKSASTFQLTGFPGMEKAHHWIFIPLLAAYISILLGNGTLLFLIRNDHNLHEPMYYFLAMLAATDLGVTLTTMPTVLGVLWLDHREIGHGACFSQAYFIHTLSVMESGVLLAMAYDCFITIRSPLRYTSILTNTQVMKIGVRVLTRAGLSIMPIVVRLHWFPYCRSHVLSHAFCLHQDVIKLACADITFNRLYPVVVLFAMVLLDFLIIFFSYILILKTVMGIGSGGERAKALNTCVSHICCILVFYVTVVCLTFIHRFGKHVPHVVHITMSYIHFLFPPFMNPFIYSIKTKQIQSGILRLFSLPHSRA | Function: Odorant receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35269
Sequence Length: 312
Subcellular Location: Cell membrane
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Q8NGF3 | MQKPQLLVPIIATSNGNLVHAAYFLLVGIPGLGPTIHFWLAFPLCFMYALATLGNLTIVLIIRVERRLHEPMYLFLAMLSTIDLVLSSITMPKMASLFLMGIQEIEFNICLAQMFLIHALSAVESAVLLAMAFDRFVAICHPLRHASVLTGCTVAKIGLSALTRGFVFFFPLPFILKWLSYCQTHTVTHSFCLHQDIMKLSCTDTRVNVVYGLFIILSVMGVDSLFIGFSYILILWAVLELSSRRAALKAFNTCISHLCAVLVFYVPLIGLSVVHRLGGPTSLLHVVMANTYLLLPPVVNPLVYGAKTKEICSRVLCMFSQGGK | Function: Odorant receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35839
Sequence Length: 324
Subcellular Location: Cell membrane
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Q8TCB6 | MVDPNGNESSATYFILIGLPGLEEAQFWLAFPLCSLYLIAVLGNLTIIYIVRTEHSLHEPMYIFLCMLSGIDILISTSSMPKMLAIFWFNSTTIQFDACLLQMFAIHSLSGMESTVLLAMAFDRYVAICHPLRHATVLTLPRVTKIGVAAVVRGAALMAPLPVFIKQLPFCRSNILSHSYCLHQDVMKLACDDIRVNVVYGLIVIISAIGLDSLLISFSYLLILKTVLGLTREAQAKAFGTCVSHVCAVFIFYVPFIGLSMVHRFSKRRDSPLPVILANIYLLVPPVLNPIVYGVKTKEIRQRILRLFHVATHASEP | Function: Odorant receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35271
Sequence Length: 317
Subcellular Location: Cell membrane
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Q9H255 | MSSCNFTHATFVLIGIPGLEKAHFWVGFPLLSMYVVAMFGNCIVVFIVRTERSLHAPMYLFLCMLAAIDLALSTSTMPKILALFWFDSREISFEACLTQMFFIHALSAIESTILLAMAFDRYVAICHPLRHAAVLNNTVTAQIGIVAVVRGSLFFFPLPLLIKRLAFCHSNVLSHSYCVHQDVMKLAYADTLPNVVYGLTAILLVMGVDVMFISLSYFLIIRTVLQLPSKSERAKAFGTCVSHIGVVLAFYVPLIGLSVVHRFGNSLHPIVRVVMGDIYLLLPPVINPIIYGAKTKQIRTRVLAMFKISCDKDLQAVGGK | Function: Olfactory receptor . Activated by the odorant, beta-ionone, a synthetic terpenoid . The activity of this receptor is probably mediated by G-proteins leading to the elevation of intracellular Ca(2+), cAMP and activation of the protein kinases PKA and MAPK3/MAPK1 . Stimulation of OR51E2 by beta-ionone affects melanocyte proliferation, differentiation, and melanogenesis . Activation of OR51E2 by beta-ionone increases proliferation and migration of primary retinal pigment epithelial (RPE) cells . Activated also by the short-chain fatty acids (SCFA) acetate and propionate. In response to SCFA, may positively regulate renin secretion and increase blood pressure . May also be activated by steroid hormones and regulate cell proliferation . Activated by L-lactate in glomus cells (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35493
Sequence Length: 320
Subcellular Location: Cell membrane
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P14803 | DDIKLSQQYDVLDLFKYMHQ | Function: Putative receptor for octopamine. Octopamine (OA) is a neurotransmitter, neurohormone, and neuromodulator in invertebrates. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 2500
Sequence Length: 20
Subcellular Location: Cell membrane
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Q60856 | MEQDLRSIPASKLDKFIENHLPDTSFCADLREVIDALCALLKDRSFRGPVRRMRASKGVKGKGTTLKGRSDADLVVFLNNLTSFEDQLNQQGVLIKEIKKQLCEVQHERRCGVKFEVHSLRSPNSRALSFKLSAPDLLKEVKFDVLPAYDLLDHLNILKKPNQQFYANLISGRTPPGKEGKLSICFMGLRKYFLNCRPTKLKRLIRLVTHWYQLCKEKLGDPLPPQYALELLTVYAWEYGSRVTKFNTAQGFRTVLELVTKYKQLQIYWTVYYDFRHQEVSEYLHQQLKKDRPVILDPADPTRNIAGLNPKDWRRLAGEAAAWLQYPCFKYRDGSSVCSWEVPTEVGVPMKYLLCRIFWLLFWSLFHFIFGKTSSG | Function: Does not have 2'-5'-OAS activity, but can bind double-stranded RNA . The full-length protein displays antiviral activity against flaviviruses such as west Nile virus (WNV) via an alternative antiviral pathway independent of RNase L . The truncated form of the protein lacks antiviral activity .
Location Topology: Single-pass type IV membrane protein
Sequence Mass (Da): 43620
Sequence Length: 376
Subcellular Location: Endoplasmic reticulum membrane
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P00973 | MMDLRNTPAKSLDKFIEDYLLPDTCFRMQINHAIDIICGFLKERCFRGSSYPVCVSKVVKGGSSGKGTTLRGRSDADLVVFLSPLTTFQDQLNRRGEFIQEIRRQLEACQRERAFSVKFEVQAPRWGNPRALSFVLSSLQLGEGVEFDVLPAFDALGQLTGGYKPNPQIYVKLIEECTDLQKEGEFSTCFTELQRDFLKQRPTKLKSLIRLVKHWYQNCKKKLGKLPPQYALELLTVYAWERGSMKTHFNTAQGFRTVLELVINYQQLCIYWTKYYDFKNPIIEKYLRRQLTKPRPVILDPADPTGNLGGGDPKGWRQLAQEAEAWLNYPCFKNWDGSPVSSWILLAESNSADDETDDPRRYQKYGYIGTHEYPHFSHRPSTLQAASTPQAEEDWTCTIL | Function: Interferon-induced, dsRNA-activated antiviral enzyme which plays a critical role in cellular innate antiviral response . In addition, it may also play a role in other cellular processes such as apoptosis, cell growth, differentiation and gene regulation. Synthesizes higher oligomers of 2'-5'-oligoadenylates (2-5A) from ATP which then bind to the inactive monomeric form of ribonuclease L (RNase L) leading to its dimerization and subsequent activation. Activation of RNase L leads to degradation of cellular as well as viral RNA, resulting in the inhibition of protein synthesis, thus terminating viral replication . Can mediate the antiviral effect via the classical RNase L-dependent pathway or an alternative antiviral pathway independent of RNase L. The secreted form displays antiviral effect against vesicular stomatitis virus (VSV), herpes simplex virus type 2 (HSV-2), and encephalomyocarditis virus (EMCV) and stimulates the alternative antiviral pathway independent of RNase L.
PTM: Prenylated at C-terminal. C-terminal prenylation is necessary to initiate a block to SARS-CoV-2 and is associated with protection from severe COVID-1. The prenylated form is targeted to perinuclear structures rich in viral dsRNA, whereas the non-prenylated form is diffusely localized and unable to initiate a detectable block to SARS-CoV-2 replication (Probable). C-terminal prenylation is also necessary to initiate a block to cardiovirus EMCV (Probable).
Catalytic Activity: 3 ATP = 5'-triphosphoadenylyl-(2'->5')-adenylyl-(2'->5')-adenosine + 2 diphosphate
Sequence Mass (Da): 46029
Sequence Length: 400
Subcellular Location: Cytoplasm
EC: 2.7.7.84
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F1N3B8 | MGSRESHLYEKPSEKLEEFIQNHLRPSEDCQKDIDQSVDTICEVLQEPCPSLTVTGVAKGGSYGRRTVLRGNSDGILVVFFGDLEQFQDQEKRQYELLSKIWAQMKHCESTWKLAAKMELQNTNRSSRVTIQLSTKQQSITFNVLPAFNALGLSEKSSLWSYRELKRSLDMVKARPGEFSVCFTELQEKFFSNYPSKLKDLILLVKHWFQKCQEKLINSSLLPPYALELLTVYAWEQGCGAEDFDMAEGVRTVLRLIEKQEQLCVYWTVNYNFGDEIVRNILLSQLQAPRPVILDPTDPTNNVSMDNTCWLQLKHEAQNWLRSLRQNESPGPSWNVLPASLYITPGHLLDKFVKDFLQPNQTFQDQIKKALKIICSFLEENCFRHSTTKIQVIQGGSTVKGTALKTGSDASLVVFANSLKSYTSPKNERYNIIKEIHEQLEACRQEKDFEVKFEISKWKPPWVLSFTLKSKVLNESVDFDVLPAFNALGELKSGSTPSPRTYTELIHLYKPSDVFLEGEFSACFTKLQRNFVRSLPLKLKDLIRLLKHWYCGCEKKLKQKGSLPPKYALELLSIYAWEKGSGAQDFDMAEGFRTVLELVIQYQHLCVFWTVNYSFDDEILRNFLLGQIRRTRPVILDPADPTGDVGGGHRWCWHLLAKEATEWLSSLCFKDKSGCPIQPWNVPKKRVQTPGSCGAGIYSMVNEMHLLRSHRFLD | Function: Interferon-induced, dsRNA-activated antiviral enzyme which plays a critical role in cellular innate antiviral response. Activated by detection of double stranded RNA (dsRNA): polymerizes higher oligomers of 2'-5'-oligoadenylates (2-5A) from ATP which then bind to the inactive monomeric form of ribonuclease L (RNASEL) leading to its dimerization and subsequent activation. Activation of RNASEL leads to degradation of cellular as well as viral RNA, resulting in the inhibition of protein synthesis, thus terminating viral replication. Can mediate the antiviral effect via the classical RNASEL-dependent pathway or an alternative antiviral pathway independent of RNASEL. In addition, it may also play a role in other cellular processes such as apoptosis, cell growth, differentiation and gene regulation (By similarity). May act as a negative regulator of lactation, stopping lactation in virally infected mammary gland lobules, thereby preventing transmission of viruses to neonates (By similarity). Non-infected lobules would not be affected, allowing efficient pup feeding during infection (By similarity).
PTM: Myristoylation is not essential for its activity.
Catalytic Activity: 3 ATP = 5'-triphosphoadenylyl-(2'->5')-adenylyl-(2'->5')-adenosine + 2 diphosphate
Sequence Mass (Da): 81967
Sequence Length: 714
Subcellular Location: Cytoplasm
EC: 2.7.7.84
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P29728 | MGNGESQLSSVPAQKLGWFIQEYLKPYEECQTLIDEMVNTICDVLQEPEQFPLVQGVAIGGSYGRKTVLRGNSDGTLVLFFSDLKQFQDQKRSQRDILDKTGDKLKFCLFTKWLKNNFEIQKSLDGFTIQVFTKNQRISFEVLAAFNALSLNDNPSPWIYRELKRSLDKTNASPGEFAVCFTELQQKFFDNRPGKLKDLILLIKHWHQQCQKKIKDLPSLSPYALELLTVYAWEQGCRKDNFDIAEGVRTVLELIKCQEKLCIYWMVNYNFEDETIRNILLHQLQSARPVILDPVDPTNNVSGDKICWQWLKKEAQTWLTSPNLDNELPAPSWNVLPAPLFTTPGHLLDKFIKEFLQPNKCFLEQIDSAVNIIRTFLKENCFRQSTAKIQIVRGGSTAKGTALKTGSDADLVVFHNSLKSYTSQKNERHKIVKEIHEQLKAFWREKEEELEVSFEPPKWKAPRVLSFSLKSKVLNESVSFDVLPAFNALGQLSSGSTPSPEVYAGLIDLYKSSDLPGGEFSTCFTVLQRNFIRSRPTKLKDLIRLVKHWYKECERKLKPKGSLPPKYALELLTIYAWEQGSGVPDFDTAEGFRTVLELVTQYQQLCIFWKVNYNFEDETVRKFLLSQLQKTRPVILDPAEPTGDVGGGDRWCWHLLAKEAKEWLSSPCFKDGTGNPIPPWKVPTMQTPGSCGARIHPIVNEMFSSRSHRILNNNSKRNF | Function: Interferon-induced, dsRNA-activated antiviral enzyme which plays a critical role in cellular innate antiviral response . Activated by detection of double stranded RNA (dsRNA): polymerizes higher oligomers of 2'-5'-oligoadenylates (2-5A) from ATP which then bind to the inactive monomeric form of ribonuclease L (RNASEL) leading to its dimerization and subsequent activation . Activation of RNASEL leads to degradation of cellular as well as viral RNA, resulting in the inhibition of protein synthesis, thus terminating viral replication . Can mediate the antiviral effect via the classical RNASEL-dependent pathway or an alternative antiviral pathway independent of RNASEL . In addition, it may also play a role in other cellular processes such as apoptosis, cell growth, differentiation and gene regulation . May act as a negative regulator of lactation, stopping lactation in virally infected mammary gland lobules, thereby preventing transmission of viruses to neonates (By similarity). Non-infected lobules would not be affected, allowing efficient pup feeding during infection (By similarity).
PTM: Myristoylation is not essential for its activity.
Catalytic Activity: 3 ATP = 5'-triphosphoadenylyl-(2'->5')-adenylyl-(2'->5')-adenosine + 2 diphosphate
Sequence Mass (Da): 82431
Sequence Length: 719
Subcellular Location: Cytoplasm
EC: 2.7.7.84
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Q59327 | MSNVKKHVSTINPVGEVLDVGSADEVQWSDASDVVVVGWGGAGASAAIEAREQGAEVLVIERFSGGGASVLSGGVVYAGAVPATRRKPASRFTEAMTAYLKHEVNGVVSDETLARFSRDSVTNLNWLEKQGATFASTMPGYKTSYPADGMYLYYSGNEVVPAYGNPQLLKKPPPRGHRVVAKGQSGAMFFAALQKSTLAHGARTLTQARVQRLVREKDSGRVLGVEVMVLPEGDPRTERHKKLDELVAKSACIRRRVPRRVAVNVRRSRARSARSATSVPAKVWCCPLAAISSIRNCWSMRRYKPGWLTGAAGCDGSGLRLGQSVGGIAQDLNNISAWRFITPPSVWPKGLVVNIQGERFCNEQVYGAKLGYEMMEKQGGQAWLIIDSNVRRQAAWQCLFGGLWAFQSMPALALMYKVAIKGKSVDDLAKKLRMDAAVLQLQFDRANAPARGEIEDPLGKSQDMRHEFKGGSLFAIDISISQKMFPLAVLSLGGLKVNEDNGAVIDGAGYDIPGLYAAGVPPLVWLPRVT | Function: Involved in the degradation of steroids having an A:B ring fusion in a trans configuration. Catalyzes the elimination of hydrogens located at positions 4 and 5 and the introduction of double bonds into ring A.
Catalytic Activity: A + a 3-oxo-5alpha-steroid = a 3-oxo-Delta(4)-steroid + AH2
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 57289
Sequence Length: 530
Subcellular Location: Membrane
EC: 1.3.99.5
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Q3ZAJ2 | MFDRVEIRIKSGDGGSGKVSFRREKFVPYGGPDGGDGGDGGNVYLEADSGLYSLLNFKHKRVHKAANGENGMGSRCTGHNGADLVIKVPVGTVATIVEENGQKRVLADLAADGDRTLVARGGQGGLGNTHFVSSTNQAPMLAQKGQPGGEYELILELKLIADVAIIGYPNVGKSSLLSLLTAAKPRVANYPFTTLSPVMGVVERTEGTFVMAEVPGLIEDAHLGRGLGHDFLRHISRTRMVIHLLDGTSDNPIDDMIKVNSELYLYDASLSERPQVVAVNKIDDELVQLRREELTETFKEAGLEVFFISALTGEGVEVLLDKVAEKLAILKAADAPETETDQEIKVFRPAPKGKMGFHITRLEDGWQVEAPEIERIIEHSDIEDLEVRRQIMVLLKHRNVQQALIKAGAVIGQKIITGRLEWYL | Function: An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis control.
Sequence Mass (Da): 46209
Sequence Length: 424
Subcellular Location: Cytoplasm
EC: 3.6.5.-
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B1I5V8 | MFKDYAKIHVKAGDGGNGCVAFRREKYVPYGGPSGGDGGRGGHVILRADGGLRTLVDFRYRTHYKAGRGTHGQGKNMHGRKGEDLVLRVPVGTEVRRAGDATLMADLTVDGQEYRVARGGRGGRGNARFAAANRRAPSFAEKGEPGEELWLELELKLLADVGLVGFPNAGKSTIISKVSAARPKIADYPFTTLEPHLGVVRVGEGESFVLADIPGLIEGAHRGAGLGHRFLRHVERTRVLIHVVDVSGREGRDPVADFEAINRELAAYDPRLAARPQLVAANKTDLPGARDNARRLAEAAGGRYEVFEISALTGEGLDRLIYRTYRLLETIPVEPAPAPIVPDERETDVTLFLVAREGNTYVVEGEGIERRVAMTDLDNPEAVQHLQELLVRIGVEDALRAEGIRPGDNVRIGRFEFEYSENPTG | Function: An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis control.
Sequence Mass (Da): 46249
Sequence Length: 425
Subcellular Location: Cytoplasm
EC: 3.6.5.-
|
B8J4L3 | MRFVDEARIQVRAGKGGHGCLSFRREKFVPRGGPDGGNGGDGGSVYLRADNRLLSLYDFRLKRLYEAQNGRPGEGSQCDGRKGENLVLNLPVGTLVYAEGPEGEVLVADLSEPDAEVLVASGGRGGKGNEHFKSSTMRAPRFSQPGEPGEEFNLRLELKILADAGLIGLPNAGKSTFISQVSAARPKIAAYPFTTLTPNLGVMIDEVDPDRRMVIADIPGLIEGAHEGQGLGLRFLKHVERTRFLVHILSIEDVGDEDPWAGFSLVNEELRRFDAELGERRQIEVVNKIDLVSPERLEALKERARADGREVYFISARDDLGLEPLVQELWQVCESTARNEPIVRLEGLTDVEEEEFPEIEVIYTRE | Function: An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis control.
Sequence Mass (Da): 40419
Sequence Length: 366
Subcellular Location: Cytoplasm
EC: 3.6.5.-
|
A8ZRY1 | MKFIDEATITVSSGKGGRGCVSFRRERFVPRGGPDGGDGGSGGSLLFRVNPSKRTLYAFRSKKQFAAPNGAPGEGRQKTGKSGDDLVIEVPPGTLIFDADTGAIIRDMVSPEEDFVFLTGGRGGKGNKHFATSTHQTPRFAQPGEPAQTATVRLELKLLADVGLIGLPNAGKSTLLSVISAARPAIGAYPFTTLSPNLGMVTLAGAEPFAVADIPGLIEGAHTGAGLGIRFLKHIERTRLLVHLIDASAIDPADPVAPFRIINAELAMFSPALAERPQVVVLNKMDLTGAEALAQQFINAAGIKKCFLISAATRSGVEELKKHLFELLCSHDT | Function: An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis control.
Sequence Mass (Da): 35064
Sequence Length: 333
Subcellular Location: Cytoplasm
EC: 3.6.5.-
|
Q6AK07 | MAFVDEAKFFVKAGDGGNGCVSFRREKFVPKGGPNGGDGGKGGDVIMVASSKVQSLIDFRYRSHFKAERGVHGQGRDMHGRGGKDCYMDIPVGSVVKDSETGRVLADLSEEGEEFVVAQGGSGGMGNPHFSSGSNRTPRVATKGKLGEEKWLLIELKLMADVGLVGLPNAGKSTLLSKLSAANPKVADYPFTTLEPQLGMLHFPMRNSCIIADIPGLVEGAHQGVGLGHKFLRHVERTKILVHVIDASADDPFSDYDIIGNELRSYKEELADRAKILVLNKCDEFDFDKDLLPDFIEARGLEPKNVLFISAITGEGVDKLVKLIGDIIDDMEYQELKQKREEERLQDLKKQKEEERRQELKKQKEEEQAKDE | Function: An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis control.
Sequence Mass (Da): 41004
Sequence Length: 372
Subcellular Location: Cytoplasm
EC: 3.6.5.-
|
Q2GDW7 | MKFIDEVKVFLKAGNGGDGCSSFRREKFVEFGGPDGGCGGDGGNVIFITDENLNTLLDYRHRVHLKAENGKPGRKSNKRGESGSDLVCKVPIGTQILTQDRVLLSDLEQPKQSFISAFGGKGGRGNATFKNSLNRAATEFTCGEPGEEKTVILNLKILADIGLIGLPNAGKSTFLSRCSNAKPKIADYPFSTLEPIVGIAKINNHEIVIADIPGIIEGAHKNLGLGVKFLKHIERCKALIYLIDGTEKDIYSVYTLLSNELSLYSKKLEIKEHFILITKSDLLGKDEVQEKCQYIREKTGKLTLHTGIDQELASSLKAAQKLVELHQPGNKSRGKYNPLEV | Function: An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis control.
Sequence Mass (Da): 37285
Sequence Length: 341
Subcellular Location: Cytoplasm
EC: 3.6.5.-
|
Q30XW0 | MRFVDEAVIKAISGNGGHGCVSFRREKFIPRGGPDGGDGGNGGNVVFKASTRLLSLYDFRLKRVYQAENGRPGQGSQMHGRGGKDLVVEMPVGTLVFERGENGAESLIADLSEPDVEVVIAHGGRGGKGNEHFKSSTMQAPRFSQPGEPGEEKSLRLELKILADAGLLGLPNAGKSTFISQVSAAKPKIAAYPFTTLVPNLGVMMDEFDPDRRMVIADIPGLIEGAHEGQGLGHRFLKHVERTRFLVHILSIEDVDMENPWAGFDLINDELQRFDETLGSREQIQVVNKIDLLPPEEVDGLRARAEADGRRIFFISALEGEGLDAVVSEMWRMLAELDRNVPLDSSRQIEPEPEEEFDVEVVWVRE | Function: An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis control.
Sequence Mass (Da): 40223
Sequence Length: 366
Subcellular Location: Cytoplasm
EC: 3.6.5.-
|
B1ZZ37 | MFVDECVVKLQAGDGGRGCISFRREKYEPWGGPNGGDGGRGGDVILLGDDDTNNLVDYKYQPHWNAERGEHGLGKDQHGKDGAHRVLKMPLGTVVIDEATGKPVAEVVEDGQQIVLCKGGNGGWGNTHFKTATTRAPKRANDGHPGERGTYRLVLKSIADVGLVGFPNAGKSSLTCLITRARPRTAAYPFTTLHPQIGIIDYPPDRHGRRRLRLADVPGLIEGASENRGLGHRFLRHIERCALLLVLIDMAGTDGRDPREDYKHLLRELELYDPALLKKPRLVAANKMDVEAAAANLSKFKRRHRTVDVLPLSCLTSEGIELLKKELLKRVTALRGREKVSPRARD | Function: An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis control.
Sequence Mass (Da): 38072
Sequence Length: 346
Subcellular Location: Cytoplasm
EC: 3.6.5.-
|
P95722 | MTTFVDRVELHVAAGNGGHGCASVHREKFKPLGGPDGGNGGRGGDVILTVDQSVTTLLDYHHSPHRKATNGKPGEGGNRSGKDGQDLVLPVPDGTVVLDGAGNVLADLVGHGTSYVAAQGGRGGLGNAALASARRKAPGFALLGEPGDLQDIHLELKTVADVALVGYPSAGKSSLISVLSAAKPKIADYPFTTLVPNLGVVTAGETVYTVADVPGLIPGASQGKGLGLEFLRHVERCSVLVHVLDTATLESERDPLSDLDVIETELREYGGLDNRPRIVVLNKIDVPDGKDLAEMVRPDLEARGYRVFEVSAVAHMGLRELSFALAELVATARAARPKEEATRIVIRPKAVDDAGFTVTREEDGLFRVRGEKPERWVRQTDFNNDEAVGYLSDRLNRLGVEDKLMKAGARNGDGVAIGPEDNAVVFDWEPSVTAGAEMLGRRGEDHRFEAPRPAAQRRRDRDAERDEAQQEFDGFEPF | Function: Plays an unknown essential role and a regulatory role in sporulation. Overexpression suppresses sporulation although cell growth rate was not reduced. Impaired differentiation was eliminated by addition of decoyinine, an inhibitor of GMP synthesis. Overexpression has no effect on undecylprodigiosin production, but decreases actinorhodin production.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 51073
Sequence Length: 478
Subcellular Location: Cytoplasm
EC: 3.6.5.-
|
B1VXD8 | MTTFVDRVELHAAAGNGGHGCASVHREKFKPLGGPDGGNGGRGGDVILVVEQSVTTLLDYHHSPHRKATNGQPGAGDNRSGKDGQDLVLPVPDGTVVLDKAGNVLADLVGQGTTFVAGQGGRGGLGNAALASARRKAPGFALLGEPGESRDIVLELKTVADVALVGYPSAGKSSLISVLSAAKPKIADYPFTTLVPNLGVVTAGSTVYTIADVPGLIPGASQGKGLGLEFLRHVERCSVLVHVLDTATLESDRDPVSDLDMIEEELRLYGGLENRPRIVALNKVDIPDGQDLADMIRPDLEARGYRVFEVSAIAHKGLKELSFALAGIIAEARATKPKEEATRIVIRPRAVDDAGFTVTLEDDGIYRVRGEKPERWVRQTDFNNDEAVGYLADRLNRLGVEDSLMKAGARAGDGVAIGPEENAVVFDWEPTVTAGAEMLGRRGEDHRLEEPRPAAQRRRERDAERDDAEKEYDEFDPF | Function: An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis control.
Sequence Mass (Da): 51024
Sequence Length: 478
Subcellular Location: Cytoplasm
EC: 3.6.5.-
|
B4SP14 | MKLVDEAEIEVFAGNGGNGCIGFRREKFIPLGGPDGGDGGAGGSVYIRADENLNTLVDFRHDRIFKAQRGENGMGRQAYGKGGEDLTITVPVGTVIINVATDEIIGDLTQHGDRLLVAQGGRGGLGNMHFKSSTNRSPRQALPGEPGEERTLKLELKLLADVGLLGFPNAGKSTLIRAVSAATPKVADYPFTTLYPNLGVVKVENYRSFVIADIPGLIEGAADGAGLGAQFLRHLQRTRLLLHLVDISPMEGGVEGISPVEQVRAIERELEKHDPELLQKPRWLVLNKADLMFEDEAKAAAEQIVAELGWKEPWFLVSALGREGTFPIMSRIMAFFDRQKEDELEARNAL | Function: An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis control.
Sequence Mass (Da): 38006
Sequence Length: 350
Subcellular Location: Cytoplasm
EC: 3.6.5.-
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Q561T9 | MAGIKALVALSFSGALGLTFLLLGCALEQFGQYWPMFVLIFYILSPIPNLIARRHADDTESSNACRELAYFLTTGIVVSAYGLPVVLARKAVIQWGAAGLVMAGNCVIFLTILGFFLIFGGGDDFSWEQW | Function: Involved in protein trafficking. May be involved in the down-regulation of membrane protein levels (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 14130
Sequence Length: 130
Subcellular Location: Golgi apparatus membrane
|
O15243 | MAGVKALVALSFSGAIGLTFLMLGCALEDYGVYWPLFVLIFHAISPIPHFIAKRVTYDSDATSSACRELAYFFTTGIVVSAFGFPVILARVAVIKWGACGLVLAGNAVIFLTIQGFFLIFGRGDDFSWEQW | Function: Negatively regulates leptin receptor (LEPR) cell surface expression, and thus decreases response to leptin. Negatively regulates growth hormone (GH) receptor cell surface expression in liver. May play a role in liver resistance to GH during periods of reduced nutrient availability.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 14254
Sequence Length: 131
Subcellular Location: Golgi apparatus membrane
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B9TRX0 | MAGVKALVALSFSGAIGLTFLMLGCALEDYGVYWPLFVLVFHALSPIPHFIAKRATYDSDATSSACRELAYFFTTGIVVSAFGFPVILARVAVIKWGACGLVLAGNAVIFLTIQGFFLVFGRGDDFSWEQW | Function: Negatively regulates leptin receptor (LEPR) cell surface expression, and thus decreases response to leptin/LEP. Negatively regulates growth hormone (GH) receptor cell surface expression in liver. May play a role in liver resistance to GH during periods of reduced nutrient availability (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 14198
Sequence Length: 131
Subcellular Location: Golgi apparatus membrane
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A6WXF0 | MARQEQANDVFALTSFLYGGNADYIEELYAKYEDDPNSVDPQWRDFFAKLGDNADDVKKNAEGASWTRKNWPIAANGELISALDGNWAEVEKHVTDKLKGKAAKGEAKGATGAALTSEEITQAARDSVRAIMMIRAYRMRGHLHANLDPLGLSEKPNDYNELEPENYGFTPADYNRKIFIDNVLGLEYATVPEMLDILKRTYCGTIGVEFMHISDPAEKAWIQERIEGPDKKVAFTPEGKKAILSKLIEAEGFEQFIDVKYKGTKRFGLDGGESLIPALEQIVKRGGAMGVKEIIFGMAHRGRLNVLSQVMGKPHRAIFHEFKGGSYAPDDVEGSGDVKYHLGASSDREFDGNKVHLSLTANPSHLEIVNPVVMGKARAKQDLLAGRTRDDMVPLATRAKVLPLLLHGDAAFAGQGVVAECLGLSGLKGHRVAGTLHFIINNQIGFTTNPAFSRSSPYPSDVAKMIEAPIFHVNGDDPEAVVFAAKVATEFRMTFHKPVVIDMFCYRRFGHNEGDEPSFTQPLMYKAIRAHKTTVQLYSDKLIAEGLIKQEEIDQMKAQWRENLETEFDAGQSYKPNKADWLDGAWAGLRTADNADEQRRGKTAVPMKTLKEIGKKLVEVPKDFHVHRTIQRFLDNRAKMMETGEGIDWATAESLAFGSLVAEGSPIRLSGQDVERGTFSQRHTVLYDQETQNRYIPLNNIQKGQAIYEAINSMLSEEAVLGYEYGYSLSDPRALVLWEAQFGDFANGAQVVFDQFISSGERKWLRMSGLVCLLPHGYEGQGPEHSSARLERWLQMCAEDNMQVANVTTPANYFHILRRQMKRDFRKPLIMMTPKSLLRHKRAVSTLNELSGESSFHRLLWDDAQYNKDEGIKLQKDAKIRRVVLCSGKVYYDLYEEREKRGIDDVYLLRVEQLYPFPAKALINELSRFRHAEMVWCQEEPKNMGAWSFIDPYLEWVLAHIDAKHQRVRYAGRPAAASPATGLMSKHLAQLAAFLEDALGN | Function: E1 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the decarboxylation of 2-oxoglutarate, the first step in the conversion of 2-oxoglutarate to succinyl-CoA and CO(2).
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue succinyltransferase] + 2-oxoglutarate + H(+) = (R)-N(6)-(S(8)-succinyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue succinyltransferase] + CO2
Sequence Mass (Da): 112439
Sequence Length: 1001
EC: 1.2.4.2
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P57388 | MDKNKIEYWLNSSWLSRENQNYIETIYKSFLTNAQSIDDMWHKAFLEFSEEQKNTYERNNTKNNKYLLIKKIDHMIHAFRSEGYQQSLIDPLKLKKRTKIHDLDLSFYNFTEEETRQTVEINFKNCTNFRTNIISLYKILYKKYCGSIGFEYMYVNNLLEKQWITNHIESFFNENVFTIEEKINFLKELTYAETLEKYIGKKFPGAKRFSLEGAETLIPVLHEVIRFSKKNNISKIVLGMAHRGRLNVLINVLNKSPKVLFDEFSNLNLFQKISGDVKYHMGGTAEIQYEKKIIFHMACNPSHLEIINPVVSGISRSYIDNMKNIDNEVLPISIHGDASVIGQGVVQETLNMSQTEGYKVGGTVHIIINNQIGFTTSNPKHLRSSEYCTDVAKIIQAPVFHVNADDLEASIFAIQLALHFRKIFKKDVFIDLVCYRRNGHNEVDEPSVTQPIMYQKIKNHPTSRTIYSDVLISKKIITSEKNQEIMNQYLSKLQKGHYIFSKSKNIHFKNEFFLEEKKIKKIKKDVNFSDLKNLACLINQIPDSVKMHQRVKKIYEERLEMAQRLKLFDWGAAETLAYATILNEGISCRISGEDVSRGTFFHRHAFIHNQINGSIYIPLNNISKKQGKFQIWDSVLSEEAVLAFEYGYSLSSPNTLTIWEAQFGDFINGAQIVIDQFISSGEQKWNKKSNLVVLLPHGYEGQGPEHSSSRIERFLQLCAEENMQICIPTTSSQIFHIFRKQIFDKILKPLIIFTPKSLLRNPMASSSFDDLVYGKFQKILDEVDNVNKKEIRLIFCSGKIYYDLLRNRREKKINSIILIRIEQLYPFPEGEILKILKNYFYIKDFIWCQEEPYNQGAWFYIKDCLSNILPLDASLKYIGRSSSASPAVGYISIHKKQQEKIIYNALNIN | Function: E1 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the decarboxylation of 2-oxoglutarate, the first step in the conversion of 2-oxoglutarate to succinyl-CoA and CO(2).
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue succinyltransferase] + 2-oxoglutarate + H(+) = (R)-N(6)-(S(8)-succinyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue succinyltransferase] + CO2
Sequence Mass (Da): 105807
Sequence Length: 909
EC: 1.2.4.2
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Q89AJ7 | MYKNEFNSSWMSSFNSSYIDNLYNKFLLDPTSIDNSWYIVFTELSKENYINSTNKYLNNKFQDSKDTIKLTIELLINIFRTLGYKFAHLNPLDTFKNDNSLSLKKFLKSSEAFRIQDSYLVKLSQYVLDDITTKNVYDDYKNIYCKRIGYQFMHIHNSNEMNWIKNYIETKHSNILKKKKKIQILKHLIISEMLEKYFSSKFPSIKRFSIEGAESLIPMLKEVIKYTKKFNLHKIIFGMSHRGRLNVLANILDKPIKTIFNEFCENNSNNFNSGDVKYHMGFCCTKTIGLRKIILDLKSNPSHLEVINPVVVGSSRAYIDSNDNLNDENILPIIIHGDAAISGQGVVQELLNMSQARGYKVGGTIHIVVNNQIGFTTSKVKDLRTSQYCTDIAKMIDSPIFHVNADDPESVIFVTHLALNYRFCFKKDVFINLVCYRRHGHNEIDDPSITQPVLYSKIKNHPTTATSYYNKLLLKNIINKSFLITYQKKIKKKLDVEYNLHNKKMSEKRLKCCSIVKADYINVSNTPINNISQSDLTILAKKIFSIPNNIEVHNRVFKIYKDRLKMANNEKLFDWGASELLAYASLLNEGISCRLSGEDVCRGTFFHRHAVIHDQKNDSKYIPLKNIKLKQGNFYIWDSVLSEEATLAFEYGYSIDQKNTLNVWEAQFGDFANGAQIIIDQFICSGEQKWNVTCNLVMLLPHGYEGQGPEHSSARIERYLQLSANNNIKIIIPTISSQIYHIIRKQAFSLIKKPLIIMSPKSLLRFPLAASSLSELSNGKFRTVIDEIDNLDTKKVQRIILCSGKIYYDLLTQRRINQQKNIVILRIEQIYPRPTKKLSAILYNYKDVHDYIWCQEEPCNQGAWLYHKSYLKKLLPKHSKLNYVGRSSSASPATGYMKIHKEQQKKIIYDALNISD | Function: E1 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the decarboxylation of 2-oxoglutarate, the first step in the conversion of 2-oxoglutarate to succinyl-CoA and CO(2).
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue succinyltransferase] + 2-oxoglutarate + H(+) = (R)-N(6)-(S(8)-succinyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue succinyltransferase] + CO2
Sequence Mass (Da): 106047
Sequence Length: 916
EC: 1.2.4.2
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P51056 | MPKITMQQFQKNSYLADNNAGYIETLYENFLKDPHSVNEEWRSYFRTLTNGASTPDISHATIREEFRELARKPRSISPTAITPAAEQAAVDLLIEGYRRFGHLNAKINPLGDNRPVDSRLELGHYNLTESDFNKTFATYGLLNKPKATLKEIYTRLREIYCGSIGVQYSTISDERERNWLRDYVEQRLPSIEFDKETKRNILQQLVTAESLEKYLDTKYVGQVRYSLEGGDSLIPLLDELTKRARHQKIEEIVICMAHRGRVNVLLNIMGQSAAELFQEFEGKKDYGLMSGDVKYHRGYSRDVKTDAGPIHLSLAFNPSHLEFICPVAMGSVRARQERQNGHKRDYAMTVMIHGDASFSGEGIVMEALSMSQTRAHHVGGSIHIILNNQVGFTTSNPHDARSSMYCSDIAKMLDAPVFHVNGDDPEAVVAVTQLALDYRMAFHKDVFIDLVCYRRHGHQEVDDPMPTQPAMYKVIQEHPTTRTLYAKNLIEKKLCTAEEVDQWIDDYRDRLDRGRQLVETLPEGLSAHYAANWTPYLGQDWTTLVDTTLPLKKLKALGKKFSTLPNTLHLHRKVEAIYKARLEMAEGKTPMDWGFAEMLAYASLLEEGFSVRLVGQDSRRGTFFHRHAVVFDQETGKEYEPLKHLSDKQAAPHIYDSLLCEAGALGFEYGYSTADPNSLVIWEAQFGDFANVAQVIVDQFISSGWQKWNRLSGIVLFLPHGYEGKGPEHSSARLERYLQLCAQNNMQVCAPTTPSQIFHLLRRQVLRPYRKPLVVLTPKSVLRNKLAVSSLEDLARGQLKLLIPEIEKHDPKKITRVILCSGKVYYDLLAKRREHKGKLNHIAMIRIEQLYPFPYDELKAELEKYPNAKQVIWCQEEPKNQGAWFCTRHRLIKCMRDDQTLEYVGRSAFAAPAAGYSALYVKLQEQLVNQALEI | Function: E1 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the decarboxylation of 2-oxoglutarate, the first step in the conversion of 2-oxoglutarate to succinyl-CoA and CO(2).
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue succinyltransferase] + 2-oxoglutarate + H(+) = (R)-N(6)-(S(8)-succinyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue succinyltransferase] + CO2
Sequence Mass (Da): 106723
Sequence Length: 934
EC: 1.2.4.2
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Q59106 | MMQQYQSNSYLFGGNAPYVEELYEAYLQNPASVPDNWRAYFDAMQNVPAVDGSNGRDIPHAPIVASFAERAKQGPIRTIVASADSDMGRKRVAATQLIAAYRNIGSHWADLDPLKRQERPPLPDLDPAFYGFSEADLDIVFNASNTYFGKESMSLRELLNNLRETYCGTIGFEFMYVSDQAQKRWWQERLETTRSKPVFTLEKKKHILDRLTAAEGLERFLHTKYVGQKRFSLEGGESFIAAMDELIQHAGSKGVQEIVIGMAHRGRLNVLVNTLGKMPADLFAEFEGKHVDDLPAGDVKYHKGFSSDVSTEGGPVHLSLAFNPSHLEIVNPVVEGSAKARQERRGEVGHKEVLPVQVHGDAAFAGQGVVMETLNLAQTRGYGTGGSMHIVINNQIGFTTSDPRDARSTLYCTDVVKMIEAPVLHVNGDDPEAVVYAMQLAVDFRMEFKKDVVVDIICFRKLGHNEQDTPAVTQPLMYKKIAQHPGTRKLYADKLAAQNLVPAEFGDEKVKAYRAAMDAGKHTADPVLSNFKNKFAVDWMPFLNRKWTDAADTAVPVTELKRLAERITTTPETLKLHPLVEKVVKDRANMGRGDQPLDWGMGEHLAFASLVSSGYPVRITGQDAGRGTFTHRHAVLHDQARERWDAGSYVPLQNVSENQAPFTVIDSVLSEEAVLGFEYGYSAAEPNALVIWEAQFGDFVNGAQVVIDQFISSGEVKWGRASGLTLMLPHGYEGQGPEHSSARIERFLQLCADHNMQVCQPTTPAQIFHLLRRQMIRLFRKPLVIMTPKSLLRNKDAVSPLSDLAKGHFETVIPDHEELNASKVKRVIMCSGKVYYDLVNTRKEREANDTAVIRLEQLYPFPHKAVAAELKKYPNATEIVWCQDEPQNQGAWFFVQHYIMENMTDGQKLGYAGRPASASPAVGYYAKHNEQQKALLEAAFAKLKGFVLTK | Function: E1 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the decarboxylation of 2-oxoglutarate, the first step in the conversion of 2-oxoglutarate to succinyl-CoA and CO(2).
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue succinyltransferase] + 2-oxoglutarate + H(+) = (R)-N(6)-(S(8)-succinyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue succinyltransferase] + CO2
Sequence Mass (Da): 105996
Sequence Length: 950
EC: 1.2.4.2
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Q54JE4 | MFTLKQVINKSIQTSMKNGVMSSAVKRSFSTVGGINQPKSRKELSESFLDGTSSTYVEDMFANWVKDPKSVHPSWASFFESSERGVPAGEAFMSPPTLGSSVATKATPSTYTSSGSPKQVSDSMRLLLLVRAYQVRGHALANLDPLGLEVKEEPAEFNPAKYGFTEADMDRPIFVGEGFISGFLTNKQPETTLRQVLKRLKETYCGDIGIEYMHIQDREMCDWIRDKFETSQPVEIPDKEKIKILERLSWADQFEGFLGLKYRATRRFGLDGCESLIPGMKAMIDTATEDGVESIVLGMPHRGRLNVLANVVRKPLPAIFNEFNGGVISIEGEYSATGDVKYHLGTSYDRVTSSGKKVHLSLVANPSHLEAVNPLVEGKVRAKQHYSKDTEQKKSMAVQLHGDASVAGQGVVYETLHLSNLDNYSTGGTVHIVVNNQIGFTTNPKYSRSSKYCTDVAKTIDIPVFHVNGDNVEAVVKVCKIAAEWRQKFKRDVFVDIVCYRKHGHNETDQPKFTQPIMYDKIGKQQPIIEKYSNKLIAEKVITQEQYLQMKNIIHESYEKGYQDGMKHVPNAEDWLESRWEGFKSPIELGNPGRTGIDQDLLQKIGKVLYTEPSGFEVHSTIKRLLKEKKDMFDKGTGFDWATAEALAFGSLLLDGNHVRLSGQDVERGTFSHRHAVWHDQKTDQTYAPLTKLATALGKKDAAEFVASNSSLSEFAVLGFELGYSLENPDALILWEAQFGDFSNGAQVIIDQFISSGEQKWMRQSGLTMLLPHGYDGAGPEHSSCRIERYLQLCDSDPNKIPPKEEAERKQSQHCNMQVLNCSTPVNYFHALRRQVHRDFRKPLVIATPKYLLRYEKSFSTAKEFSNDSFTRLYPEAFPDQINKPEKINRIVFCTGQVYYNLIASRESNNIKDVAIIRVEQLHPFPFDLVAEQLQHYPNAKAIWCQEEPMNMGYWNYIYPYFISTFKHINRPADITYTGRPSSASPAVASHTLHKLQLENFLSNALTGQVGSK | Function: The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity).
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue succinyltransferase] + 2-oxoglutarate + H(+) = (R)-N(6)-(S(8)-succinyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue succinyltransferase] + CO2
Sequence Mass (Da): 114068
Sequence Length: 1013
Subcellular Location: Mitochondrion matrix
EC: 1.2.4.2
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P0AFG5 | MQNSALKAWLDSSYLSGANQSWIEQLYEDFLTDPDSVDANWRSTFQQLPGTGVKPDQFHSQTREYFRRLAKDASRYSSTISDPDTNVKQVKVLQLINAYRFRGHQHANLDPLGLWQQDKVADLDPSFHDLTEADFQETFNVGSFASGKETMKLGELLEALKQTYCGPIGAEYMHITSTEEKRWIQQRIESGRATFNSEEKKRFLSELTAAEGLERYLGAKFPGAKRFSLEGGDALIPMLKEMIRHAGNSGTREVVLGMAHRGRLNVLVNVLGKKPQDLFDEFAGKHKEHLGTGDVKYHMGFSSDFQTDGGLVHLALAFNPSHLEIVSPVVIGSVRARLDRLDEPSSNKVLPITIHGDAAVTGQGVVQETLNMSKARGYEVGGTVRIVINNQVGFTTSNPLDARSTPYCTDIGKMVQAPIFHVNADDPEAVAFVTRLALDFRNTFKRDVFIDLVCYRRHGHNEADEPSATQPLMYQKIKKHPTPRKIYADKLEQEKVATLEDATEMVNLYRDALDAGDCVVAEWRPMNMHSFTWSPYLNHEWDEEYPNKVEMKRLQELAKRISTVPEAVEMQSRVAKIYGDRQAMAAGEKLFDWGGAENLAYATLVDEGIPVRLSGEDSGRGTFFHRHAVIHNQSNGSTYTPLQHIHNGQGAFRVWDSVLSEEAVLAFEYGYATAEPRTLTIWEAQFGDFANGAQVVIDQFISSGEQKWGRMCGLVMLLPHGYEGQGPEHSSARLERYLQLCAEQNMQVCVPSTPAQVYHMLRRQALRGMRRPLVVMSPKSLLRHPLAVSSLEELANGTFLPAIGEIDELDPKGVKRVVMCSGKVYYDLLEQRRKNNQHDVAIVRIEQLYPFPHKAMQEVLQQFAHVKDFVWCQEEPLNQGAWYCSQHHFREVIPFGASLRYAGRPASASPAVGYMSVHQKQQQDLVNDALNVE | Function: E1 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the decarboxylation of 2-oxoglutarate, the first step in the conversion of 2-oxoglutarate to succinyl-CoA and CO(2).
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue succinyltransferase] + 2-oxoglutarate + H(+) = (R)-N(6)-(S(8)-succinyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue succinyltransferase] + CO2
Sequence Mass (Da): 105062
Sequence Length: 933
EC: 1.2.4.2
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O24457 | MATAFAPTKLTATVPLHGSHENRLLLPIRLAPPSSFLGSTRSLSLRRLNHSNATRRSPVVSVQEVVKEKQSTNNTSLLITKEEGLELYEDMILGRSFEDMCAQMYYRGKMFGFVHLYNGQEAVSTGFIKLLTKSDSVVSTYRDHVHALSKGVSARAVMSELFGKVTGCCRGQGGSMHMFSKEHNMLGGFAFIGEGIPVATGAAFSSKYRREVLKQDCDDVTVAFFGDGTCNNGQFFECLNMAALYKLPIIFVVENNLWAIGMSHLRATSDPEIWKKGPAFGMPGVHVDGMDVLKVREVAKEAVTRARRGEGPTLVECETYRFRGHSLADPDELRDAAEKAKYAARDPIAALKKYLIENKLAKEAELKSIEKKIDELVEEAVEFADASPQPGRSQLLENVFADPKGFGIGPDGRYRCEDPKFTEGTAQV | Function: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity).
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase] + H(+) + pyruvate = (R)-N(6)-(S(8)-acetyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase] + CO2
Sequence Mass (Da): 47174
Sequence Length: 428
Subcellular Location: Plastid
EC: 1.2.4.1
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Q7XTJ3 | MAAASSFTAAAKFLAPVSARSAGDYKPPLPLPASASLRPGRKPAPRLRTALAVSSDVLPGNKAAPAAAAHSAVTREEALELYEDMVLGRIFEDMCAQMYYRGKMFGFVHLYNGQEAVSTGFIKLLNQADCVVSTYRDHVHALSKGVPARSVMAELFGKATGCCRGQGGSMHMFSEPHNLLGGFAFIGEGIPVATGAAFAAKYRHEVLKQSSPDGLDVTLAFFGDGTCNNGQFFECLNMAQLWKLPIVFVVENNLWAIGMSHLRATSDPEIYKKGPAFGMPGVHVDGMDVLKVREVAKEAIERARRGEGPTLVECETYRFRGHSLADPDELRRPDEKSHYAARDPITALKKYIIEQNLATESELKSIEKKIDDVVEEAVEFADASPLPPRSQLLENVFSDPKGFGIGPDGKYRCEDPLFTQGTAQV | Function: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity).
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase] + H(+) + pyruvate = (R)-N(6)-(S(8)-acetyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase] + CO2
Sequence Mass (Da): 46145
Sequence Length: 425
Subcellular Location: Plastid
EC: 1.2.4.1
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P29803 | MLAAFISRVLRRVAQKSARRVLVASRNSSNDATFEIKKCDLYLLEEGPPVTTVLTRAEGLKYYRMMLTVRRMELKADQLYKQKFIRGFCHLCDGQEACCVGLEAGINPSDHVITSYRAHGVCYTRGLSVRSILAELTGRRGGCAKGKGGSMHMYTKNFYGGNGIVGAQGPLGAGIALACKYKGNDEICLTLYGDGAANQGQIAEAFNMAALWKLPCVFICENNLYGMGTSTERAAASPDYYKRGNFIPGLKVDGMDVLCVREATKFAANYCRSGKGPILMELQTYRYHGHSMSDPGVSYRTREEIQEVRSKRDPIIILQDRMVNSKLATVEELKEIGAEVRKEIDDAAQFATTDPEPHLEELGHHIYSSDSSFEVRGANPWIKFKSVS | Function: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the glycolytic pathway to the tricarboxylic cycle.
PTM: Phosphorylation at Ser-291, Ser-293 and Ser-298 by PDK family kinases inactivates the enzyme; for this phosphorylation at a single site is sufficient. Phosphorylation at Ser-293 interferes with access to active site, and thereby inactivates the enzyme. Dephosphorylation at all three sites, i.e. at Ser-291, Ser-293 and Ser-298, is required for reactivation.
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase] + H(+) + pyruvate = (R)-N(6)-(S(8)-acetyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase] + CO2
Sequence Mass (Da): 42933
Sequence Length: 388
Subcellular Location: Mitochondrion matrix
EC: 1.2.4.1
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P35487 | MRKMLTAVLSHVFSGMVQKPALRGLLSSLKFSNDATCDIKKCDLYRLEEGPPTSTVLTRAEALKYYRTMQVIRRMELKADQLYKQKFIRGFCHLCDGQEACCVGLEAGINPTDHVITSYRAHGFCYTRGLSVKSILAELTGRKGGCAKGKGGSMHMYGKNFYGGNGIVGAQVPLGAGVAFACKYLKNGQVCLALYGDGAANQGQVFEAYNMSALWKLPCVFICENNLYGMGTSNERSAASTDYHKKGFIIPGLRVNGMDILCVREATKFAADHCRSGKGPIVMELQTYRYHGHSMSDPGISYRSREEVHNVRSKSDPIMLLRERIISNNLSNIEELKEIDADVKKEVEDAAQFATTDPEPAVEDIANYLYHQDPPFEVRGAHKWLKYKSHS | Function: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the glycolytic pathway to the tricarboxylic cycle.
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase] + H(+) + pyruvate = (R)-N(6)-(S(8)-acetyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase] + CO2
Sequence Mass (Da): 43413
Sequence Length: 391
Subcellular Location: Mitochondrion matrix
EC: 1.2.4.1
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P35485 | DQNGKVVNEKMEPKLPKETLLKMYKTAVLGRNADIKALQYQRQGRMLTYAPNMGQEAAQIGMAAAMEPQDWNSPMYRELNTLLYRGDKLENVFLYWYGNERGSIKPEGVKILPTNIIIGSQSNIAAGLAMASKIRKTNEVTAFTIGDGGTAHGEFYEGLNFAASFKAPVVAVIQNNQWAISTPVRKASNSETLAQKGVAFGIPYIQVDGNDMLAMYVASKEAMDRARKGDGPTLIEAFTYRMGPHTTSDDPCSIYRTKEEENEWAKKDQIARFKTYLINKGYWSEEEDKKLEEEVLAEINDTFKKVESYGANVELIEIFEHTYAEMTPQLKEQYEEHKKYLEGVK | Function: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase] + H(+) + pyruvate = (R)-N(6)-(S(8)-acetyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase] + CO2
Sequence Mass (Da): 38962
Sequence Length: 345
EC: 1.2.4.1
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P21881 | MAAKTKKAIVDSKKQFDAIKKQFETFQILNEKGEVVNEAAMPDLTDDQLKELMRRMVFTRVLDQRSISLNRQGRLGFYAPTAGQEASQIATHFALEKEDFVLPGYRDVPQLIWHGLPLYQAFLFSRGHFRGNQMPDDVNALSPQIIIGAQYIQTAGVALGLKKRGKKAVAITYTGDGGASQGDFYEGINFAGAYKAPAIFVVQNNRYAISTPVEKQSAAETIAQKAVAAGIVGVQVDGMDPLAVYAATAEARERAINGEGPTLIETLTFRYGPHTMAGDDPTKYRTKEIENEWEQKDPLVRFRAFLENKGLWSEEEEAKVIEDAKEEIKQAIKKADAEPKQKVTDLMKIMYEKMPHNLEEQFEIYTQKESK | Function: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase] + H(+) + pyruvate = (R)-N(6)-(S(8)-acetyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase] + CO2
Sequence Mass (Da): 41548
Sequence Length: 371
EC: 1.2.4.1
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P49823 | XXDATFEIKKXDL | Function: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the glycolytic pathway to the tricarboxylic cycle.
PTM: Phosphorylation by PDK family kinases inactivates the enzyme; it is reactivated by dephosphorylation.
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase] + H(+) + pyruvate = (R)-N(6)-(S(8)-acetyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase] + CO2
Sequence Mass (Da): 1513
Sequence Length: 13
Subcellular Location: Mitochondrion matrix
EC: 1.2.4.1
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Q54C70 | MLSNFLKVNSKALGHIRTFASKSGEIKHNFKKADTYLCDGPSDSTVTNKDELISFFTEMSRFRRLETVCDGLYKKKLIRGFCHLYTGQEAVCAGLESAITKDDHIITAYRDHTYMLSRGATPEEIFAELLMKETGCSKGKGGSMHMFTKNFYGGNGIVGAQCPLGAGIAFAQKYNKTGNVCLAMYGDGAANQGQLFEAFNMASLWKLPVIFICENNKYGMGTSQKRSTAGHDFYTRGHYVAGLKVDGMDVFAVKEAGKYAAEWCRAGNGPIILEMDTYRYVGHSMSDPGITYRTREEVNHVRQTRDPIENIRQIILDNKIATEDQLAAIEETVRDEMEKASEKAIAAPLPQARELFTNVYLQEVPVRGVEFVNSFKP | Function: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity).
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase] + H(+) + pyruvate = (R)-N(6)-(S(8)-acetyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase] + CO2
Sequence Mass (Da): 41988
Sequence Length: 377
Subcellular Location: Mitochondrion matrix
EC: 1.2.4.1
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P08559 | MRKMLAAVSRVLSGASQKPASRVLVASRNFANDATFEIKKCDLHRLEEGPPVTTVLTREDGLKYYRMMQTVRRMELKADQLYKQKIIRGFCHLCDGQEACCVGLEAGINPTDHLITAYRAHGFTFTRGLSVREILAELTGRKGGCAKGKGGSMHMYAKNFYGGNGIVGAQVPLGAGIALACKYNGKDEVCLTLYGDGAANQGQIFEAYNMAALWKLPCIFICENNRYGMGTSVERAAASTDYYKRGDFIPGLRVDGMDILCVREATRFAAAYCRSGKGPILMELQTYRYHGHSMSDPGVSYRTREEIQEVRSKSDPIMLLKDRMVNSNLASVEELKEIDVEVRKEIEDAAQFATADPEPPLEELGYHIYSSDPPFEVRGANQWIKFKSVS | Function: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the glycolytic pathway to the tricarboxylic cycle.
PTM: Phosphorylation at Ser-232, Ser-293 and Ser-300 by PDK family kinases inactivates the enzyme; for this phosphorylation at a single site is sufficient. Dephosphorylation at all three sites, i.e. at Ser-232, Ser-293 and Ser-300, is required for reactivation.
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase] + H(+) + pyruvate = (R)-N(6)-(S(8)-acetyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase] + CO2
Sequence Mass (Da): 43296
Sequence Length: 390
Subcellular Location: Mitochondrion matrix
EC: 1.2.4.1
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O13366 | MLSLKAQSSVVGKSSSLRLVRNFSKNVRALSQVADETKPGDDDLVQIDLPETSFEGYLLDVPELSYQTTKSNLLQMYKDMIIVRRMEMACDALYKAKKIRGFCHSSVGQEAIAVGIENAITKRDTVITSYRCHGFTYMRGAAVQAVLAELMGRRTGVSFGKGGSMHLYAPGFYGGNGIVGAQVPLGAGLAFAHQYKHEDACSFALYGDGASNQGQVFESFNMAKLWNLPAVFCCENNKYGMGTAAARSSAMTEYFKRGQYIPGLKVNGMDILAVYQASKFAKDWTVSGNGPIVLEYETYRYGGHSMSDPGTTYRTRDEIQHMRSKNDPIAGLKMHLLELGIATEDEIKAYDKAARKYVDEQVELADAAPAPEAKMSILFEDVYVPGSETPTLRGRLQEDTWDFAKKSFAFRD | Function: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase] + H(+) + pyruvate = (R)-N(6)-(S(8)-acetyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase] + CO2
Sequence Mass (Da): 45453
Sequence Length: 412
Subcellular Location: Mitochondrion matrix
EC: 1.2.4.1
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F4IAL1 | MGQERPNDEERPESRDLGVYGCSPPHSPRLGPTRFYVFAGDPNPKQTIKRCKRKRIQACNDQRTAKTAIGVMAILGFFCLVNWFMLSRLHEGRVWLRRGLSENPKHVSAQNEERKKFEKQKMKYNGTYGRMLSLATDALAEGMRDNRYCNGFDFEQNKLETKDLWQEPKEQASAWKPCADQRSLTPDDGKNGYIMVTANGGINQQRVAVCNIVVVARLLNAALVIPKFMLSDVWTDASQFGDIYQEEHFMEYLSPDIRIVKELPKELQSLNLEEIGSVVTDIEVMKEAKPDFYMTHILPILLKNRVIHFVGFGNRLAFDPLPFELQRLRCRCNFHALNFVPRIQETAALLVKRLRGSGSYYLALHLRFEIDMVAHSLCYFGGGETEQKELDSYRQKHFPSLSTLTRKKKFRSADVLRTEGLCPLTPEEAVLMLAALGFNRETRVFVAGANIYGGSKRLAVLTSLYPNLVTKEKLLTESELQPFKNFSSQLAALDFIACAAADAFAMTDSGSQLSSLVSGYRIYYGGGKLPTIRPNKRRLSDILLKNSTIEWNVFEKRVRKAIRQTKHVFARPNGRSVYRYPRCKECMCHA | Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 67314
Sequence Length: 590
Pathway: Glycan metabolism.
Subcellular Location: Membrane
EC: 2.4.1.-
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Q8WR51 | MHFFPIQLLVLFFAEKIAFAENSDQTVSRVDSNRYSVAAEKKFLLYDVNFGEGFNLRRDVYMRVANTVRSLRDSGENYILVLPPWGRLHHWKRMEVALSWRLFFDLESLNRFIPVIEFEDFLDENRPIDQVIYLQHYAEGWGTEYVRKFEKRSCLPPAESHYKQVEEFKWKGWFYSYEDVYSRNFQCVSIQGDSGTLKDLLKHSNFSESTSIMVDRAETILHEHYGEVDYWKARRSMRYSNDLVDVADAFRKKYLDSDDKRDKTKLVDDWTKEKPRRTAIGGPYLGIHWRRRDFLYARRAQLPTIPGTAKILQDLCKKLDLQKIYLATDAPDQEVDELKALLNGELEVYRFTDTQKLNDGQIAIIDQYLCAHAAYFIGSYESTFTFRIQEDREIIGFPISTTFNRLCPDTEPTCEQPAKWKIVY | Function: Catalyzes the reaction that attaches fucose through an O-glycosidic linkage to a conserved serine or threonine residue in the consensus sequence C1-X-X-S/T-C2 of thrombospondin type I repeats (TSRs) where C1 and C2 are the first and second cysteines of the repeat, respectively . O-fucosylates members of several protein families including the ADAMTS superfamily and the thrombospondin (TSP) and spondin families (By similarity).
Catalytic Activity: GDP-beta-L-fucose + L-seryl-[protein] = 3-O-(alpha-L-fucosyl)-L-seryl-[protein] + GDP + H(+)
Sequence Mass (Da): 50106
Sequence Length: 424
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Endoplasmic reticulum
EC: 2.4.1.221
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Q9W589 | MRGSWPRLGFPALLLLLHLLTGSDAAVRNGTAKREIGDSRGSSGTCVKGFLQEILPLPATCPPEVLGMRGAVYILYDVNISEGFNLRRDVYIRMAVFVRRLQRRRRFRHVRLVLPPWPRLYHWHSQGLQQSGLPWSHFFDLASLRRYAPVLDYEEFLAEQRLFGNPGAPLVHVGHAFRLQHYEVMLEQGIFRDKFERVTDKPCSEGSLSGGPLLQQAELRVGRFHCVRFQGSAGLLEKLLREAIDEDTAGPEDVDDMRTYALLSAETVLHDHWGDEHFWQARRSMRFARRLEQVAADFRRQALDTTDASAGVQRPAMWELERPKRNAKGGDYLCAHLRRGDFVRSRDATTPTLKAAAQQVKQLLRGFNMTTVFLATDATPYELMELKELFYRFRLVHFAPESNVQRRELKDGGVAVVDQLVCAYARYFVGTYESTFTYRIYEEREILGFTQASTFNTFCKALGGSCSRNAVWPIVWADGDSDSEEDSDPY | Function: Catalyzes the reaction that attaches fucose through an O-glycosidic linkage to a conserved serine or threonine residue in the consensus sequence C1-X-X-S/T-C2 of thrombospondin type I repeats (TSRs) where C1 and C2 are the first and second cysteines of the repeat, respectively. O-fucosylates members of several protein families including the ADAMTS, the thrombospondin (TSP) and spondin families.
Catalytic Activity: GDP-beta-L-fucose + L-seryl-[protein] = 3-O-(alpha-L-fucosyl)-L-seryl-[protein] + GDP + H(+)
Sequence Mass (Da): 56021
Sequence Length: 490
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Endoplasmic reticulum
EC: 2.4.1.221
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Q9Y2G5 | MATLSFVFLLLGAVSWPPASASGQEFWPGQSAADILSGAASRRRYLLYDVNPPEGFNLRRDVYIRIASLLKTLLKTEEWVLVLPPWGRLYHWQSPDIHQVRIPWSEFFDLPSLNKNIPVIEYEQFIAESGGPFIDQVYVLQSYAEGWKEGTWEEKVDERPCIDQLLYSQDKHEYYRGWFWGYEETRGLNVSCLSVQGSASIVAPLLLRNTSARSVMLDRAENLLHDHYGGKEYWDTRRSMVFARHLREVGDEFRSRHLNSTDDADRIPFQEDWMKMKVKLGSALGGPYLGVHLRRKDFIWGHRQDVPSLEGAVRKIRSLMKTHRLDKVFVATDAVRKEYEELKKLLPEMVRFEPTWEELELYKDGGVAIIDQWICAHARFFIGTSVSTFSFRIHEEREILGLDPKTTYNRFCGDQEKACEQPTHWKITY | Function: Catalyzes the reaction that attaches fucose through an O-glycosidic linkage to a conserved serine or threonine residue in the consensus sequence C1-X-X-S/T-C2 of thrombospondin type I repeats (TSRs) where C1 and C2 are the first and second cysteines of the repeat, respectively . O-fucosylates members of several protein families including the ADAMTS, the thrombospondin (TSP) and spondin families (Probable) . Required for the proper secretion of ADAMTS family members such as ADAMTSL1 and ADAMTS13 . The O-fucosylation of TSRs is also required for restricting epithelial to mesenchymal transition (EMT), maintaining the correct patterning of mesoderm and localization of the definite endoderm (By similarity).
Catalytic Activity: GDP-beta-L-fucose + L-seryl-[protein] = 3-O-(alpha-L-fucosyl)-L-seryl-[protein] + GDP + H(+)
Sequence Mass (Da): 49976
Sequence Length: 429
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Endoplasmic reticulum
EC: 2.4.1.221
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W7K6N5 | MKFIIVLLLFFFFKVIDRVICVTPQKLICLKEDVYLGDFFFFLKRKKYIMYDVNIGEGFNLQKEIFYRLSLVIYNLNKKDKINIYYLVLPPWCYVTHWNIRKGNNLRWEFFFNTDIMKKVIPIIEYEEYEKLYGNYSDIMINSKYILDNYKEKSFLILPFEECNINVNRFKQFCKKCEHKYNVLYSGYCTTINTKQSECYSYNMISNYFITSILENLFLYNITSVLIKQSTNILVPFVNELYQSNLEDILLFNNKLLSYGNNYISNILKTNHYISSHLRYTDFKYISRYNVPPIHIALLKLLYIMFINNCRIIFIASDEKVEIQKVINKDFHQYKKHFYFYNNQNNLHEGEFSIIEQWICTRSYIFIGNIFSRFTMNINWERHLINKGQINQNIDLCSYHINDDNDQDIKNSYKKIVHIFNHKALQKIKNIYDNYSDRDKKYINTICYNFLSHFPNNRSIYRKEYITNT | Function: Catalyzes the reaction that attaches fucose through an O-glycosidic linkage to a conserved serine or threonine residue in the consensus sequence C1-X-X-S/T-C2 of thrombospondin type I repeats (TSRs) where C1 and C2 are the first and second cysteines of the repeat, respectively (By similarity). O-fucosylates sporozoite proteins CSP and TRAP (By similarity). O-fucosylation regulates stability and intracellular trafficking of TRAP but not of CSP . Probably by regulating protein O-fucosylation, may play a role in parasite transmission to the mosquito vector and/or infection of the vertebrate host hepatocytes; however, POFUT2 involvement in transmission/infection is controversial .
Catalytic Activity: GDP-beta-L-fucose + L-seryl-[protein] = 3-O-(alpha-L-fucosyl)-L-seryl-[protein] + GDP + H(+)
Sequence Mass (Da): 57003
Sequence Length: 469
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Endoplasmic reticulum
EC: 2.4.1.221
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A5K6G1 | MKGRAHIWVALLLACLPPRFRNLDKDVSSPVCRTDDVYTGDAFYPFKKKKYVLYDVHIGEGFNLQKEVLYRVALAVYYLNQEERTHVHYLVLPPWCYVTHWGRERTNARIKWSIFFNLKALQNVIPVMEYAEYEGQFGPHTDYILSYRHIIGEWPKRGDKKSFQVLKLDKCQVKGYKLKKNLRKNCDHKYSVEYSGKCTNVKGKKMECLEFFFITSHFVSSTLLDIFQYDADSVLIKHGSNILVAFMNELVDANLEDVLPYSEDLINEGDQFVEKNFKSSKNYISCHLRYTDFRKISTYDVSPVGISLLKLLYIMFLRKSTLIFVSTDEKKEVKKVIDSQFPQFKHFFFFYENEKLHTGQVAIVDQWICARSGTFVGNIFSRFSMHIKWERSLIGKGGPDHNLDLCGYSISTNHELRKKYSDVQDAHLDEEALQKLRPLYMRLSQKDRDFLRTICYDFAHYYPQNVSIYRRGERREEGRLM | Function: Catalyzes the reaction that attaches fucose through an O-glycosidic linkage to a conserved serine or threonine residue in the consensus sequence C1-X-X-S/T-C2 of thrombospondin type I repeats (TSRs) where C1 and C2 are the first and second cysteines of the repeat, respectively . O-fucosylates sporozoite proteins CSP and TRAP . O-fucosylation regulates stability and intracellular trafficking of TRAP but not of CSP (By similarity). Probably by regulating protein O-fucosylation, may play a role in parasite transmission to the mosquito vector and/or infection of the vertebrate host hepatocytes; however, POFUT2 involvement in transmission/infection is controversial (By similarity).
Catalytic Activity: GDP-beta-L-fucose + L-seryl-[protein] = 3-O-(alpha-L-fucosyl)-L-seryl-[protein] + GDP + H(+)
Sequence Mass (Da): 56766
Sequence Length: 481
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Endoplasmic reticulum
EC: 2.4.1.221
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S7WCF5 | MHCQLGGQARALIFLMFESCRNSWHVSPWSSVPFLPSPCLFFSFSALPFLHPLSQLIACRGSSATWLFPVSSGTLVLRYALAASPPRGTMRPSTNPRTAEEGRPWLIHATQTGPQTASVLSLFPAVNAGFFSACRQHRGGRPPCLLNHRRLLLGLVSVLTVFLSCLPFTNATVSPAALQDVCYAFGNISRKLSSFLVPSRVTCPRGATPLSGVEAQDSLEHPEIPDFRFLVYDVKNGEGFHLQKEVIYRVALVISLLNARSAQQGRMTDVHTAEKAREDRGHPQASHMLCASSSFSHACSARSTFPFFPMWVLVLPPWCRLAHWHFSEETITAMAENSWLKHVRWGTFFDFQDLGERLPVMEYEDFLTYQLMRPDPWGERRQRKEKQTTPVELDVVLSVRFSSTPSSRSLPFCACLSSRASEIADEQAQRDDVCCNVNDLPGCPQIHAALTPQERQRAPAQRGGDPREEIDEQTGEFNEGHNPSGDGEREKRKPGRRSDTSRSRKEIQEEAKVSDTWSGVSLWLAGFCETVRALEMWCASLYIADAPRIADLLWRSVAERPPGAIQTVWLKFGENLLVPWPDVLLDAHLLDMLHVHPKLRQIGDLFINKFLSNRDKTETGKGERASTEGGTEGDENLAKHGYIAAHLRRTDFLYLKRSVPLQRAAAYLVSRMKEHGVFKAFICTDGSEDEKRELRDAVRRVGDAASSSPYTVVFFDLPTVRRLMIKTLEASSHVSDDGSFHDLKAVETPGYSGPNHISLLLHPGITALIEVWIAARAAYFIGTKDSRFSQAIRWERHLMGHPLDSSLEVFCVDSSPDQTGGQAQGKCFATKSHDPPEGRSRSELRRKYWPSLDPSSTL | Function: Catalyzes the reaction that attaches fucose through an O-glycosidic linkage to a conserved serine or threonine residue in the consensus sequence C1-X-X-S/T-C2 of thrombospondin type I repeats (TSRs) where C1 and C2 are the first and second cysteines of the repeat, respectively . O-fucosylates microneme protein MIC2 and may play a role in its stabilization . Probably by regulating protein O-fucosylation, may play a role in tachyzoite adhesion to and/or invasion of host cells; however, POFUT2 involvement in adhesion/invasion is controversial .
Catalytic Activity: GDP-beta-L-fucose + L-seryl-[protein] = 3-O-(alpha-L-fucosyl)-L-seryl-[protein] + GDP + H(+)
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 95964
Sequence Length: 858
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.4.1.221
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Q84WU0 | MVRNSSDEEEDHRNLIPQNDTRDNDLNLRPDARTVNMANGGGRSPRSALQIDEILSRARNRWKISVNKRYVVAAVSLTLFVGLLFLFTDTRTFFSSFKLDPMSSRVKESELQALNLLRQQQLALVSLLNRTNFNSSNAISSSVVIDNVKAALLKQISVNKEIEEVLLSPHRTGNYSITASGSDSFTGSYNADICRKVDQKLLDRKTIEWKPRPDKFLFAICLSGQMSNHLICLEKHMFFAALLDRVLVIPSSKFDYQYDKVIDIERINTCLGRTVVISFDQFKEIDKKNNAHIDRFICYVSSPQPCYVDEDHIKKLKGLGVSIGGKLEAPWSEDIKKPTKRTSQEVVEKFKSDDGVIAIGDVFYADMEQDLVMQPGGPINHKCKTLIEPSRLILVTAQRFIQTFLGKNFISLHLRRHGFLKFCNAKSPSCFYPIPQAADCISRMVERANAPVIYLSTDAAESETGLLQSLVVVDGKVVPLVKRPPQNSAEKWDSLLYRHGIEDDSQVYAMLDKTICAMSSVFIGASGSTFTEDILRLRKDWGTSSMCDEYLCRGEEPNFIAENE | Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 63622
Sequence Length: 564
Pathway: Glycan metabolism.
Subcellular Location: Membrane
EC: 2.4.1.-
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B7ZWR7 | MRRRRKTVVVAVVIRRVLIWAICVMTLLCFLTVHIYVAPFNRLPKLHLNHHNTRRGYIIDYNKSITEQSLTRNLSRPESNEIPLISNPKTNEIQYQSSISEHINNTELVPPHVSTSPSSSSKLNITSGIPDFDKLWKHPPNRNFVPCVSPNPSYTSPLESRGYLLVHTNGGLNQMRAGICDMVAIARIINATLVVPELDKRSFWQDTSKFSDVFDEDHFINALSKDIRVIKKLPKGIDGLTKVVKHFKSYSGLSYYQNEIASMWDEYKVIRAAKSDSRLANNNLPPDIQKLRCRACYEALRFSTKIRSMGELLVDRMRSYGLYIALHLRFEKEMLAFSGCNHGLSASEAAELRRIRKNTAYWKVKDIDGRVQRLKGYCPLTPKEVGILLTALGYSSDTPVYIAAGEIYGGESRLADLRSRFSMLMSKEKLATREELKTFMNHSTQMAALDYIVSIESDVFIPSYSGNMARAVEGHRRFLGHRKTISPDRKAIVRLVDRIGRGAEKDNRKVYERINEIHKTRQGSPRRRKGPASGTKGLERHRSEESFYENPLPDCLCQRDPSKAR | Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 64514
Sequence Length: 565
Pathway: Glycan metabolism.
Subcellular Location: Membrane
EC: 2.4.1.-
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F4HZX7 | MGKQGSPRSPRPETIDKEEKFGRRSLDSLSGNDLLLGRRIYASEVSKAQGSKHDQSSGSSNKFWKKQHSWLRRNFKSIVLMISVTGFIFCMDSIMVSIFHSDSRAVVQDISRLSNMTLHKNGAVDASPVQMYSRLLNLASDSLAKNEFKPDTPNFREERSSKSSQWKPCADNNKAAVALERSRELSNGYIMVSANGGLNQQRVAICNAVAVAALLNATLVLPRFLYSNVWKDPSQFGDIYQEDHFIEYLKDEVNIVKNLPQHLKSTDNKNLSLVTDTELVKEATPVDYIEHVLPLLKKYGMVHLFGYGNRLGFDPLPFDVQRLRCKCNFHALKFAPKIQEAGSLLVKRIRRFKTSRSRLEEALLGESMVKSTVKGEEEPLKYLALHLRFEEDMVAYSLCDFGGGEAERKELQAYREDHFPLLLKRLKKSKPVSPEELRKTGKCPLTPEEATLVLAGLGFKRKTYIYLAGSQIYGGSSRMLPLTRLYPNIATKETLLTPQELAPFKNFSSQLAALDFIACIASDVFAMTDSGSQLSSLVSGFRNYYGNGQAPTLRPNKKRLAAILSDSETIKWKIFEDRVRKMVEEGQKLRTRPYGRSIYRQPRCPECMCKF | Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 69119
Sequence Length: 611
Pathway: Glycan metabolism.
Subcellular Location: Membrane
EC: 2.4.1.-
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Q8H1E6 | MHGLSRLGNGSSNGRINIPSPSPPSSPRIRHTRGKSLAGGVYKQGLGERLVFLLFSIVFRRKGVLLLAPLLYIAGMLLFMGSFGFTVLDLGHGVEIVYRRGSPGSVYRSPKVFKRLWPVMEADVNGSSHNVLMEAWKPRVKSVWKPCISTNVSAAGSNSNGYFIIEANGGLNQQRLSICDAVAVAGLLNATLVIPIFHLNSVWRDSSKFGDIFDEDFFIYALSKNVNVVKELPKDVLERYNYNISSIVNLRLKAWSSPAYYLQKVLPQLLRLGAVRVAPFSNRLAHAVPAHIQGLRCLANFEALRFAEPIRLLAEKMVDRMVTKSVESGGKYVSVHLRFEMDMVAFSCCEYDFGQAEKLEMDMARERGWKGKFRRRGRVIRPGANRIDGKCPLTPLEVGMMLRGMGFNNSTLVYVAAGNIYKADKYMAPLRQMFPLLQTKDTLATPEELAPFKGHSSRLAALDYTVCLHSEVFVSTQGGNFPHFLIGHRRYLYKGHAETIKPDKRKLVQLLDKPSIRWDYFKKQMQDMLRHNDAKGVELRKPAASLYTFPMPDCMCKEPDPEPETDPA | Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 63766
Sequence Length: 568
Pathway: Glycan metabolism.
Subcellular Location: Membrane
EC: 2.4.1.-
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O42914 | MSVASKNLFDLLGEETPAATTTEKKTAASRDKKRSDSPPVPRELVAQSTTSRKRDPNQPTPRERTVNKKADQPRRRRQAPQGNEAFAREGKEARANNAAHPVDATGAPSNRRNARARRGREFDRHSQTGRVDTKKATERGWGDLVNSAANPDVAENEGNTPSGAQTPAAEEENVKTLDEYLSERKSAAKPVGRTVEKLENATKVEKSAPEELFASLKKSASQKKSAAKESKPKKVLLDIEQTFTARPARGGRPNRAPRRGPSETASKTQQAPPTLSETDFPALA | Function: Ribosome preservation factor that protect a small pool of nontranslating, vacant ribosomes in cells under nutrient starvation conditions. Under nutrient-limiting conditions, cells reduce ribosome biogenesis and degrade ribosomes via autophagy (ribophagy) or proteasomal degradation. To avoid excessive degradation during starvation, STM1 binds to and protects 80S ribosomes from proteasomal degradation. Under nutrient-sufficient conditions, TORC1 phosphorylates and inhibits STM1 to prevent formation of dormant 80S ribosomes. Acts as an inhibitor of mRNA translation by promoting ribosome hibernation: clamps the two ribosomal subunits, thereby preventing their dissociation, and inhibits translation by excluding mRNA-binding. Acts via its association with eEF2, promoting ribosome stabilization and storage in an inactive state. May also repress translation by preventing association of eEF3 with ribosomes (By similarity). Binds specifically G4 quadruplex (these are four-stranded right-handed helices, stabilized by guanine base quartets) and purine motif triplex (characterized by a third, antiparallel purine-rich DNA strand located within the major groove of a homopurine stretch of duplex DNA) nucleic acid structures. These structures may be present at telomeres or in rRNAs. Extends chronological lifespan when overexpressed .
PTM: Phosphorylation by TORC1 upon nutrient replenishment inhibits STM1 and causes its release from dormant ribosomes.
Sequence Mass (Da): 30949
Sequence Length: 284
Subcellular Location: Cytoplasm
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Q89ZI2 | MKNNKIYLLGACLLCAVTTFAQNVSLQPPPQQLIVQNKTIDLPAVYQLNGGEEANPHAVKVLKELLSGKQSSKKGMLISIGEKGDKSVRKYSRQIPDHKEGYYLSVNEKEIVLAGNDERGTYYALQTFAQLLKDGKLPEVEIKDYPSVRYRGVVEGFYGTPWSHQARLSQLKFYGKNKMNTYIYGPKDDPYHSAPNWRLPYPDKEAAQLQELVAVANENEVDFVWAIHPGQDIKWNKEDRDLLLAKFEKMYQLGVRSFAVFFDDISGEGTNPQKQAELLNYIDEKFAQVKPDINQLVMCPTEYNKSWSNPNGNYLTTLGDKLNPSIQIMWTGDRVISDITRDGISWINERIKRPAYIWWNFPVSDYVRDHLLLGPVYGNDTTIAKEMSGFVTNPMEHAESSKIAIYSVASYAWNPAKYDTWQTWKDAIRTILPSAAEELECFAMHNSDLGPNGHGYRREESMDIQPAAERFLKAFKEGKNYDKADFETLQYTFERMKESADILLMNTENKPLIVEITPWVHQFKLTAEMGEEVLKMVEGRNESYFLRKYNHVKALQQQMFYIDQTSNQNPYQPGVKTATRVIKPLIDRTFATVVKFFNQKFNAHLDATTDYMPHKMISNVEQIKNLPLQVKANRVLISPANEVVKWAAGNSVEIELDAIYPGENIQINFGKDAPCTWGRLEISTDGKEWKTVDLKQKESRLSAGLQKAPVKFVRFTNVSDEEQQVYLRQFVLTIEKK | Function: Can hydrolyze the glycosidic link of O-GlcNAcylated proteins. Can use p-nitrophenyl-beta-GlcNAc and 4-methylumbelliferone-GlcNAc as substrates (in vitro).
Catalytic Activity: 3-O-(N-acetyl-beta-D-glucosaminyl)-L-seryl-[protein] + H2O = L-seryl-[protein] + N-acetyl-D-glucosamine
Sequence Mass (Da): 84485
Sequence Length: 737
EC: 3.2.1.169
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Q0TR53 | MKRKMLKRLLTSAFACMFIANGLITTTVRAVGPKTGEENQVLVPNLNPTPENLEVVGDGFKITSSINLVGEEEADENAVNALREFLTANNIEINSENDPNSTTLIIGEVDDDIPELDEALNGTTAENLKEEGYALVSNDGKIAIEGKDGDGTFYGVQTFKQLVKESNIPEVNITDYPTVSARGIVEGFYGTPWTHQDRLDQIKFYGENKLNTYIYAPKDDPYHREKWREPYPESEMQRMQELINASAENKVDFVFGISPGIDIRFDGDAGEEDFNHLITKAESLYDMGVRSFAIYWDDIQDKSAAKHAQVLNRFNEEFVKAKGDVKPLITVPTEYDTGAMVSNGQPRAYTRIFAETVDPSIEVMWTGPGVVTNEIPLSDAQLISGIYNRNMAVWWNYPVTDYFKGKLALGPMHGLDKGLNQYVDFFTVNPMEHAELSKISIHTAADYSWNMDNYDYDKAWNRAIDMLYGDLAEDMKVFANHSTRMDNKTWAKSGREDAPELRAKMDELWNKLSSKEDASALIEELYGEFARMEEACNNLKANLPEVALEECSRQLDELITLAQGDKASLDMIVAQLNEDTEAYESAKEIAQNKLNTALSSFAVISEKVAQSFIQEALSFDLTLINPRTVKITASSEETSGENAPASFASDGDMNTFWHSKWSSPAHEGPHHLTLELDNVYEINKVKYAPRQDSKNGRITGYKVSVSLDGENFTEVKTGTLEDNAAIKFIEFDSVDAKYVRLDVTDSVSDQANGRGKFATAAEVNVHGKLKENAEVTGSVSLEALEEVQVGENLEVGVGIDELVNAEAFAYDFTLNYDENAFEYVEAISDDGVFVNAKKIEDGKVRVLVSSLTGEPLPAKEVLAKVVLRAEAKAEGSNLSVTNSSVGDGEGLVHEIAGTEKTVNIIEGTSPEIVVNPVRDFKASEINKKNVTVTWTEPETTEGLEGYILYKDGKKVAEIGKDETSYTFKKLNRHTIYNFKIAAKYSNGEVSSKESLTLRTAR | Function: Binds carbohydrates . Capable of hydrolyzing the glycosidic link of O-GlcNAcylated proteins. Can bind and deglycosylate O-glycosylated peptides from mammals.
Catalytic Activity: 3-O-(N-acetyl-beta-D-glucosaminyl)-L-seryl-[protein] + H2O = L-seryl-[protein] + N-acetyl-D-glucosamine
Sequence Mass (Da): 111080
Sequence Length: 1001
EC: 3.2.1.169
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P9WEQ7 | MVTKCIDPCEQQNQKRPVGHLVWDLIRISRYDKYNSFLALFSGVWSTLLAGALKLRNEPESTSVSFVLSRVVLCSLASYIFSGAGMVWNDWVDRDIDAKVARTKDRPLASGRLHTMEAMAWLIIQVAASTGLLYWMMEGRHVWISLVPPAIGTLLYPYCKRPTAQKFGIYPQYVLGLTAACPAVFGRAAIYNHEDSFQDLINASFPLCLFVFVWTLYFNTAYSYQDVKDDSKMKINSSYVFAGQHIHLFLVLLTGLVLASIPWVLHPLQSGWLWVSWMGVWSVGCAEQLVRFNANDPHTGGLVWRRNILLALWTIFACLVEVLLVWIHQI | Function: Polyprenyl transferase; part of the gene cluster that mediates the biosynthesis of 15-deoxyoxalicine B . The first step of the pathway is the synthesis of nicotinyl-CoA from nicotinic acid by the nicotinic acid-CoA ligase olcI . Nicotinyl-CoA is then a substrate of polyketide synthase olcA to produce 4-hydroxy-6-(3-pyridinyl)-2H-pyran-2-one (HPPO) which is further prenylated by the polyprenyl transferase olcH to yield geranylgeranyl-HPPO . Geranylgeranyl pyrophosphate is provided by the cluster-specific geranylgeranyl pyrophosphate synthase olcC . The FAD-dependent monooxygenase olcE catalyzes the epoxidation of geranylgeranyl-HPPO and the terpene cyclase olcD catalyzes the cyclization of the terpenoid component, resulting in the formation of the tricyclic terpene moiety seen in predecaturin E . The cytochrome P450 monooxygenase then catalyzes the allylic oxidation of predecaturin E, which is followed by spirocylization with concomitant loss of one molecule of water to form decaturin E . Decaturin E is the substrate of the cytochrome P450 monooxygenase olcJ which hydroxylates it at the C-29 position to form decaturin F . The short-chain dehydrogenase/reductase olcF may catalyze the oxidation of decaturin F to generate the 29-hydroxyl-27-one intermediate, and subsequent hemiacetal formation probably leads to the formation of decaturin C (Probable). The dioxygenase olcK may be a peroxisomal enzyme that catalyzes the hydroxylation of decaturin C into decaturin A once decaturin C is shuttled into the peroxisome by the MFS transporter olcL (Probable). Finally the cytochrome P450 monooxygenase olcB catalyzes the oxidative rearrangement to yield 15-deoxyoxalicine B . In the absence of olcJ, decaturin E may be shunted to a pathway in which it is oxidized to a ketone, possibly by olcF, to form decaturin D, which undergoes further allylic oxidation to yield decaturin G . Moreover, in the absence of oclK or oclL, oclB can convert decaturin C into 15-deoxyoxalicine A .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 37469
Sequence Length: 330
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
Subcellular Location: Membrane
EC: 2.5.1.-
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P9WEQ8 | MDLVSFAFSGPATHADQAPLYIDAKRPSRSLSEAPFRRLVRSLVAGFKAYGVERGDTVLVQLDNLVIHSALLFGIVGAGGVYMGCSPSSPRHELDHFVSLVEPRLILTVASALSVVRDVCTNKGISWSQICLVDDQSVDHLVSFAQNQSYNPQATPPVRDEGVHFDLKDMVSFGESDWMRIYDEATARITPAAMFSTSGTSGLPKAAIRTHHTIISHHQTVHYDVPYPVTRLMALPMSHSFGDFWSNLFPIRYGHPLYVMPRFDLSTFLNVVHRYNITETYLVPAMVHILNQSTLPVRESLGSLFYIGVSGAPIDADSLQRCQKLLNPQACIGQLWGMTEVGVIFQNRYGDQRYPGSIGKLLENYDIRLVRLDDGTTIHGESTPGELYVRGPGIMLAYQGRDDGIDAQGWFRTGDIAYSEDEHYHIVGRTKELIKVRGYSVAPAEIEAVLLKDPRVHDTMVIGITLPDGSTEVPRAYVVCALGQARPTADEVSALALKNLASYKALDGGVIFVESLPRTGIGKPHRSKLSHLDAQRTKLAALLSPV | Function: Nicotinic acid-CoA ligase; part of the gene cluster that mediates the biosynthesis of 15-deoxyoxalicine B . The first step of the pathway is the synthesis of nicotinyl-CoA from nicotinic acid by the nicotinic acid-CoA ligase olcI . Nicotinyl-CoA is then a substrate of polyketide synthase olcA to produce 4-hydroxy-6-(3-pyridinyl)-2H-pyran-2-one (HPPO) which is further prenylated by the polyprenyl transferase olcH to yield geranylgeranyl-HPPO . Geranylgeranyl pyrophosphate is provided by the cluster-specific geranylgeranyl pyrophosphate synthase olcC . The FAD-dependent monooxygenase olcE catalyzes the epoxidation of geranylgeranyl-HPPO and the terpene cyclase olcD catalyzes the cyclization of the terpenoid component, resulting in the formation of the tricyclic terpene moiety seen in predecaturin E . The cytochrome P450 monooxygenase then catalyzes the allylic oxidation of predecaturin E, which is followed by spirocylization with concomitant loss of one molecule of water to form decaturin E . Decaturin E is the substrate of the cytochrome P450 monooxygenase olcJ which hydroxylates it at the C-29 position to form decaturin F . The short-chain dehydrogenase/reductase olcF may catalyze the oxidation of decaturin F to generate the 29-hydroxyl-27-one intermediate, and subsequent hemiacetal formation probably leads to the formation of decaturin C (Probable). The dioxygenase olcK may be a peroxisomal enzyme that catalyzes the hydroxylation of decaturin C into decaturin A once decaturin C is shuttled into the peroxisome by the MFS transporter olcL (Probable). Finally the cytochrome P450 monooxygenase olcB catalyzes the oxidative rearrangement to yield 15-deoxyoxalicine B . In the absence of olcJ, decaturin E may be shunted to a pathway in which it is oxidized to a ketone, possibly by olcF, to form decaturin D, which undergoes further allylic oxidation to yield decaturin G . Moreover, in the absence of oclK or oclL, oclB can convert decaturin C into 15-deoxyoxalicine A .
Catalytic Activity: ATP + CoA + nicotinate = AMP + diphosphate + nicotinyl-CoA
Sequence Mass (Da): 60082
Sequence Length: 546
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
EC: 6.2.1.-
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P9WEQ9 | MDPNTWSADLFQLASQWQEKGLLTRYNVFMAISITVTALYLIHKGISRARSFRAPLVGRRFSWEPKWLIGLRFSQYGLEHLMEGCKRFNDGIFKVARNDTDILVIPNRYVDELHSKPEEHISAIKAHMKNLLGKYSTIDILQEGNLHTHVLQTKLTPNLGSLMSTIEEELRFAMTEEIPSTHEDWKDVSIYDIILHLVARISARVFVGQPTCRNQEWLDTSIRFTEHAFLTLAILRRLPKFLHPIVAPLLPSYWAVHRDLQTAKRIISPIVKQRTADEASGEPGYKKPTDLLQWMIDVASPRDGQPDKLAHRQLVLSLAAIHTTTMAVAYAIYDLCQFPEYVEPLRQEITDSLEQDGKWAKTTLTKMHKLDSFIKESQRLSPPSLLSFQRIVMQEVTLSDGTALPKGTHISVPAAEVLQGKAFDSSFDGFRYSRRRQNSGEAHKYQFATTDKNSLHFGHGKYACPGRFFAAYEIKMIISHLLMDYDFRFPPGTSRPKVFSADEVLLPDPSTRVLMHRRTDSAHSNCH | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of 15-deoxyoxalicine B . The first step of the pathway is the synthesis of nicotinyl-CoA from nicotinic acid by the nicotinic acid-CoA ligase olcI . Nicotinyl-CoA is then a substrate of polyketide synthase olcA to produce 4-hydroxy-6-(3-pyridinyl)-2H-pyran-2-one (HPPO) which is further prenylated by the polyprenyl transferase olcH to yield geranylgeranyl-HPPO . Geranylgeranyl pyrophosphate is provided by the cluster-specific geranylgeranyl pyrophosphate synthase olcC . The FAD-dependent monooxygenase olcE catalyzes the epoxidation of geranylgeranyl-HPPO and the terpene cyclase olcD catalyzes the cyclization of the terpenoid component, resulting in the formation of the tricyclic terpene moiety seen in predecaturin E . The cytochrome P450 monooxygenase then catalyzes the allylic oxidation of predecaturin E, which is followed by spirocylization with concomitant loss of one molecule of water to form decaturin E . Decaturin E is the substrate of the cytochrome P450 monooxygenase olcJ which hydroxylates it at the C-29 position to form decaturin F . The short-chain dehydrogenase/reductase olcF may catalyze the oxidation of decaturin F to generate the 29-hydroxyl-27-one intermediate, and subsequent hemiacetal formation probably leads to the formation of decaturin C (Probable). The dioxygenase olcK may be a peroxisomal enzyme that catalyzes the hydroxylation of decaturin C into decaturin A once decaturin C is shuttled into the peroxisome by the MFS transporter olcL (Probable). Finally the cytochrome P450 monooxygenase olcB catalyzes the oxidative rearrangement to yield 15-deoxyoxalicine B . In the absence of olcJ, decaturin E may be shunted to a pathway in which it is oxidized to a ketone, possibly by olcF, to form decaturin D, which undergoes further allylic oxidation to yield decaturin G . Moreover, in the absence of oclK or oclL, oclB can convert decaturin C into 15-deoxyoxalicine A .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 60269
Sequence Length: 527
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
Subcellular Location: Membrane
EC: 1.-.-.-
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P9WEP3 | MTIVSPDKLPSARAVELTAPLDDIYQILNEDGAVIIKNFIPLELVDKINKEVDPYLAQHAAGPNHMSEIYKLTVGSKTKHMGNLTMASKSFRDEVLNHPSMHAISEKLFRANFGDYWLNRAAVLEVDSGEKAQGLHRDDSLYPWKAFLTKDSPELMVNFFIALTEFREENGATRLVLGSHKWEDSTRYPSPEQTIPAEMQAGDAIVYLASLFHGAGQNRSQKTRRGLSITTHPAHFTPMESHIDVPRAIIENMTPLAQKMIGWRTWSTNHGVPVWTVRDGRMEDELKLKSLESPKQIQAAVI | Function: Dioxygenase; part of the gene cluster that mediates the biosynthesis of 15-deoxyoxalicine B . The first step of the pathway is the synthesis of nicotinyl-CoA from nicotinic acid by the nicotinic acid-CoA ligase olcI . Nicotinyl-CoA is then a substrate of polyketide synthase olcA to produce 4-hydroxy-6-(3-pyridinyl)-2H-pyran-2-one (HPPO) which is further prenylated by the polyprenyl transferase olcH to yield geranylgeranyl-HPPO . Geranylgeranyl pyrophosphate is provided by the cluster-specific geranylgeranyl pyrophosphate synthase olcC . The FAD-dependent monooxygenase olcE catalyzes the epoxidation of geranylgeranyl-HPPO and the terpene cyclase olcD catalyzes the cyclization of the terpenoid component, resulting in the formation of the tricyclic terpene moiety seen in predecaturin E . The cytochrome P450 monooxygenase then catalyzes the allylic oxidation of predecaturin E, which is followed by spirocylization with concomitant loss of one molecule of water to form decaturin E . Decaturin E is the substrate of the cytochrome P450 monooxygenase olcJ which hydroxylates it at the C-29 position to form decaturin F . The short-chain dehydrogenase/reductase olcF may catalyze the oxidation of decaturin F to generate the 29-hydroxyl-27-one intermediate, and subsequent hemiacetal formation probably leads to the formation of decaturin C (Probable). The dioxygenase olcK may be a peroxisomal enzyme that catalyzes the hydroxylation of decaturin C into decaturin A once decaturin C is shuttled into the peroxisome by the MFS transporter olcL (Probable). Finally the cytochrome P450 monooxygenase olcB catalyzes the oxidative rearrangement to yield 15-deoxyoxalicine B . In the absence of olcJ, decaturin E may be shunted to a pathway in which it is oxidized to a ketone, possibly by olcF, to form decaturin D, which undergoes further allylic oxidation to yield decaturin G . Moreover, in the absence of oclK or oclL, oclB can convert decaturin C into 15-deoxyoxalicine A .
Sequence Mass (Da): 33969
Sequence Length: 302
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
Subcellular Location: Peroxisome matrix
EC: 1.14.11.-
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P9WEP4 | MANIGGSNAVSSAQGSQISDSPTTVDDRLDEHKETSTQSIDHSENITQSPTSLQKPPDESNATPVGFGEDGCQSDSQEYPNSWRLAAIMIGVCLAVFSMALDNTILATAIPKITDQFTSLGDVGWYGSVYPLTNCCLTLVFGKLYTFYSTKWVYLSALAVFEIGSLICGATPSSLGLIIGRAIAGLGSSGIYLGSMIILSQSVPLQKRPLFTSLVGGLYGVAGVAGPLLGGAFTDYVSWRWCFYINPLFGAVTALFILLFFDGKEPIKSPGKIKEQISQFDLIGLFFFLPGMISLLLALQWGGQQYNWQSGRIIGLFVCSICLLSIFIMVQWRQKEKATVTLRMIKNKNVWGASLFNFCITGSFLVFSYYLPVWFQSIKNVSATKSGLMNLPMLLGVILCSIISGYGVGRIGYYTPFMYAAPIVSAIGAGLLSTFQANFGPSQWIGYQALYGIGLGLGLSQPIVVIQAAIPLIDIPSAIAIVTFIQSLGGSVSVSIAQNVFRNELLRGLAQNAPKVDAHKLITAGPTTLRYVVPAELLERVLVAYNSAITHAFYVGAAFSVLAMIGALPIQWISVKGRE | Function: MFS-type transporter; part of the gene cluster that mediates the biosynthesis of 15-deoxyoxalicine B . The first step of the pathway is the synthesis of nicotinyl-CoA from nicotinic acid by the nicotinic acid-CoA ligase olcI . Nicotinyl-CoA is then a substrate of polyketide synthase olcA to produce 4-hydroxy-6-(3-pyridinyl)-2H-pyran-2-one (HPPO) which is further prenylated by the polyprenyl transferase olcH to yield geranylgeranyl-HPPO . Geranylgeranyl pyrophosphate is provided by the cluster-specific geranylgeranyl pyrophosphate synthase olcC . The FAD-dependent monooxygenase olcE catalyzes the epoxidation of geranylgeranyl-HPPO and the terpene cyclase olcD catalyzes the cyclization of the terpenoid component, resulting in the formation of the tricyclic terpene moiety seen in predecaturin E . The cytochrome P450 monooxygenase then catalyzes the allylic oxidation of predecaturin E, which is followed by spirocylization with concomitant loss of one molecule of water to form decaturin E . Decaturin E is the substrate of the cytochrome P450 monooxygenase olcJ which hydroxylates it at the C-29 position to form decaturin F . The short-chain dehydrogenase/reductase olcF may catalyze the oxidation of decaturin F to generate the 29-hydroxyl-27-one intermediate, and subsequent hemiacetal formation probably leads to the formation of decaturin C (Probable). The dioxygenase olcK may be a peroxisomal enzyme that catalyzes the hydroxylation of decaturin C into decaturin A once decaturin C is shuttled into the peroxisome by the MFS transporter olcL (Probable). Finally the cytochrome P450 monooxygenase olcB catalyzes the oxidative rearrangement to yield 15-deoxyoxalicine B . In the absence of olcJ, decaturin E may be shunted to a pathway in which it is oxidized to a ketone, possibly by olcF, to form decaturin D, which undergoes further allylic oxidation to yield decaturin G . Moreover, in the absence of oclK or oclL, oclB can convert decaturin C into 15-deoxyoxalicine A .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 62278
Sequence Length: 579
Subcellular Location: Peroxisome membrane
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Q17833 | MKGTLIFVVFYSSYGFAHCNTILRSSSLSRNFEDSLRRIPRSTDKDETGFEDSNVQEVIFILLYCLFVALAILICGLIIFYNSRKRELRANRSRGDEYLLEPTSADHKRRNSSNIVPPEPTPYPITSGESDLRQTPSRLSNVECPPELELAPINEKIMYLHYYAEVEINEEDLDISKGRPLGSGEFGIIRKGFLRSKNSKNEEKESRLEVAVKLPLNEYNQIQQELIYDELKVMCAVGKHPNILALVGGITFGERKMIVSEFVENGDLLSFLRDNRIYFTNDQWTLETEQDSLSLVDLLSFAFQIAKGMEYLIHVPCVHRDLALRNVLIKKNRIIRIADFGLARRHKNKDYYKTQSVDTPLPIHWMAPESIDKLLFTQKSDVWSYGVCLYELFSLGKSPYENVIKYDQRDFYWKYVLSYLNEGKRLAQPAHADAEIYNVMKLCWDLDMNSRTTFLDCIEFFEKELKTTSNEYFLDLTRKLRSETNNQLRLSNWLSDEKHCDS | Function: Receptor tyrosine kinase which plays a role in promoting longevity and resistance to stresses including UV irradiation and high temperatures, probably downstream of daf-16.
Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 58385
Sequence Length: 502
Subcellular Location: Cell membrane
EC: 2.7.10.1
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P0DV58 | MTIESIRVKNLLSFDDVILRDFRDINCIIGRNNVGKSNLLKVIRYFYAKLENKKVIPLDFHTNYNAVGEITFTFDTTRIKKIVTSRKNNGRFHKHIYNTLFKSSSVKLNFEELIARKNSTNKSFFSLTLTICKDDSVMWSVDDPKVRSLLATLYPFLYIETRHIDLYDWNPIWKLISNLNSFNFDDVDHDELVNFLDEKISSRKGDYKKYIDRVVSVIDTKPYTYKEKVINYIKVAIKGDSFVNAGEELFTQSDGTNSNKFLETLLHLLITLTRTEFISPIVYIDEPEVGLHPKLAESFVSNLNKIYSKFKKTSELSGPGRYKTPYPNIFYSTHSPSILKQTIKLFGKDQQVLHFSKKKDGSTRVNKINSTYSDERFLNIFSDNEARLFFSEYIVFVEGATELELFRNLSLLNLYPAFSLADIYDANEVILANINPGYSKASIPFVIIKDIDTLIDYSIKTEKFSLRPLFEKMIKELTKEFDYYDTGFGRVRKEIDLFSDIQSSTKKHMDSGLFFKRFSLHNLSSRINKVSRKLNRYFMTTTIEGALINEQSLPYFFNWIGDVILTQMTINNPNPDKFIEAMRRRYNIKSQVVPLFKSVFCIGLNHPVYSSAVDKQALRIKLSFLNYLKRKVYSDFNNEKEIVLALRLAFGGKTETQYTLDKLRKDGEAELFREKIKNYKNNELFFLEPQMTKTSGWVTTFLNYTIEKITSEESDDDRIRQKLSFIFPEIISIIEQASSSIEAEESSLTG | Cofactor: Probably binds 2 metal cations.
Function: Probable nuclease member of antiviral defense system retron Eco8, composed of an reverse transcriptase (RT), this nuclease and a non-coding RNA (ncRNA) encoded between them. Expression of retron Eco8 confers protection against bacteriophages T4, T6, T7 and SECphi4, SECphi6 and SECphi18. At multiplicity of infection (MOI) of 0.02 cultures slow growth when infected with SECphi4 but do not collapse, at MOI 2 cultures collapse. When the retron is cloned in another E.coli strain synthesizes msDNA (a branched RNA linked by a 2',5'-phosphodiester bond to a single-stranded DNA). The retron transcript serves as primer and template to the reaction, and codes for the RT.
Sequence Mass (Da): 87256
Sequence Length: 750
EC: 3.1.-.-
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E8PLM2 | MLKRLQVKNFRCLEDIDLPLGPLTAIVGPNGAGKTTILRAIDLVLGDVWPSLRSFRIPQDFINFDTTRAIEITVHFDPPYTQGSFNITAFRLTCKGEDADFHVDLEPLDEGGNVPRYPSGNPLRVGTDMRNHARVLFLDHRRNLAQHLPSIRGSILGRLLQPVRREFKLQDNFKQVYEQAMDLLRTEQVKQIEKTIAETAKQMLGFLGKDAMKSMEIGFGFADPANPFNSLRLQYRESDLTLPGDELGLGIQSAIVVGIFEAFRQLGEKIGTVIIEEPEMYLHPQAQRYFYRLLCEMADKDQCQIIYSTHSPIFADVNRFEALRLVRKDRDDRVVVSYVREEDKSALDNVRNRFKLGGRFDTARNEVLFAKRALLVEGYGDRVAALQLFNQLEVDPDAECIAVVDCGGKAGIELIVGVCKALDIPFVVVHDEDVWPIDERADEETRRKQEQENKAEQEKNQRIQACAGAERVFVVQPSLEAALGIGRNASDKPYRIAEILKTVDVGQPPDALRPFVEAIRQVTRPMEE | Cofactor: Probably binds 2 metal cations. In vitro during a short incubation, Mn(2+) is most efficient on linear or supercoiled dsDNA, nicks but only poorly digests dsDNA with Co(2+), Ni(2+) or Zn(2+). When purified from E.coli Ca(2+) and Mg(2+) are the most abundant metals.
Function: An exodeoxyribonuclease that degrades linear or supercoiled dsDNA from 5'-3'. Nicks and linearizes circular DNA. Activity is not stimulated by ATP or AMP-PNP, although it has DNA-stimulated ATPase activity.
Catalytic Activity: Exonucleolytic cleavage in the 5'- to 3'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 59748
Sequence Length: 528
Domain: The ATPase domain dimerizes on its own via its dimerization region, the Toprim (topoisomerase/primase) domain does not. The Toprim domain has Mn(2+)-dependent nuclease activity on linear and supercoiled dsDNA. It faces away from the dimerization domain.
EC: 3.1.11.3
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Q84T21 | MADRPQQLQVHPQRGHGHYEGGIKNQRGGGPSAVKVMAVLAALPVGGTLLALAGLTLAGSVIGLLVTSPLFIIFSPVLVPAAIVVGLAVASFLSSGALGLTGLSSLSWVLNYLRCASQSLPREMDQAKRRMQDMAAFVGQKTREVGQEIQSRAQEGRRT | Function: May have a structural role to stabilize the lipid body during desiccation of the seed by preventing coalescence of the oil. Probably interacts with both lipid and phospholipid moieties of lipid bodies. May also provide recognition signals for specific lipase anchorage in lipolysis during seedling growth.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 16698
Sequence Length: 159
Subcellular Location: Lipid droplet
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Q647G3 | MSDQTRTGYGGGGSYGSSYGGGGTYGSSYGTSYDPSTNQPIRQAIKFMTASTIGVSFLILSGLILTGTVIGLIIATPLLVIFSPILVPAAITLALAAGGFLFSGGCGVAAIAALSWLYSYVTGKHPAGSDRLDYAKGVIADKARDVKDRAKDYAGAGRAQEGTPGY | Function: May have a structural role to stabilize the lipid body during desiccation of the seed by preventing coalescence of the oil. Probably interacts with both lipid and phospholipid moieties of lipid bodies. May also provide recognition signals for specific lipase anchorage in lipolysis during seedling growth.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 16875
Sequence Length: 166
Subcellular Location: Lipid droplet
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C0HM28 | MADYQHQQQHQRPADAFKGMFPEKGQAQVQGPSASKVIAVVTLLPLGGFLLLLAGLTFAGTLIGLALSTPLFVLCSPVLVPAAIVIGLAVTGFLTSGAFGITGISSLSWILKYLRGTSVPEQMEHAKRRAQDTAGHLGQKARETGQTVTGKGQEAGKTLEGGRGEEKKT | Function: May have a structural role to stabilize the lipid body during desiccation of the seed by preventing coalescence of the oil. Probably interacts with both lipid and phospholipid moieties of lipid bodies. May also provide recognition signals for specific lipase anchorage in lipolysis during seedling growth.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 17695
Sequence Length: 169
Domain: The proline-knot motif may be involved in the targeting to oil bodies.
Subcellular Location: Lipid droplet
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Q96543 | MADHHRDRGVLGGGALGERGSHGGYGYTGDHGGYGGDDEQHQQKQPVMMCALKAATAATAGGSMLVLSGLILAGTVIALTVATPVLVIFSPVLVPAAISMALMSAGFVTSGGLGVAAVSVFSWMYKYLAGKHPPGADQLDHAKARLASKARDIKDAAQIRVEQAQGA | Function: May have a structural role to stabilize the lipid body during desiccation of the seed by preventing coalescence of the oil. Probably interacts with both lipid and phospholipid moieties of lipid bodies. May also provide recognition signals for specific lipase anchorage in lipolysis during seedling growth (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 16996
Sequence Length: 167
Subcellular Location: Lipid droplet
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Q8EG66 | MKYSRVFINSLAYELAPVVVSSSELESRLAPLYQKFRIPMGQLAALTGITERRWWPKGHQLSDGAINAAHKAIAETGIDVAELGAVVYTGVCRDQHEPATACRIAAALGVSKDTAIYDISNACLGVLSGILDIANRIELGQIKAGMVVSCESARDIVDVTIDNMLADPTMQNFAQSLATLTGGSGAVAVILTDGSLPLTNVRKHQLLGASHLSAPQHHQLCQWGLQEVGHNIYREFMRTDAVTLLKEGVELAKHTWEHFLAQRNWLVEQVDKVICHQVGASNRKQVLSALNIPPEKEFPTYQLLGNMGTVSLPVTAAMAHDQGFLRPGDQVSFLGIGSGLNCMMLGIKW | Function: Involved in olefin biosynthesis . Catalyzes a non-decarboxylative head-to-head Claisen condensation of two acyl-CoA molecules, generating an (R)-2-alkyl-3-oxoalkanoate (By similarity). The S.oneidensis oleABCD genes produce 3,6,9,12,15,19,22,25,28-hentriacontanonaene, which may aid the cells in adapting to a sudden drop in temperature .
Catalytic Activity: a 1,2-saturated acyl-CoA + an acyl-CoA + H2O = an (R)-2-alkyl-3-oxoalkanoate + 2 CoA + H(+)
Sequence Mass (Da): 37831
Sequence Length: 349
EC: 2.3.3.20
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Q8PDX2 | MLFQNVSIAGLAHIDAPHTLTSKEINERLQPTYDRLGIKTDVLGDVAGIHARRLWDQDVQASDAATQAARKALIDANIGIEKIGLLINTSVSRDYLEPSTASIVSGNLGVSDHCMTFDVANACLAFINGMDIAARMLERGEIDYALVVDGETANLVYEKTLERMTSPDVTEEEFRNELAALTLGCGAAAMVMARSELVPDAPRYKGGVTRSATEWNKLCRGNLDRMVTDTRLLLIEGIKLAQKTFVAAKQVLGWAVEELDQFVIHQVSRPHTAAFVKSFGIDPAKVMTIFGEHGNIGPASVPIVLSKLKELGRLKKGDRIALLGIGSGLNCSMAEVVW | Function: Involved in olefin biosynthesis . Catalyzes a non-decarboxylative head-to-head Claisen condensation of two acyl-CoA molecules, generating an (R)-2-alkyl-3-oxoalkanoate . Is active with fatty acyl-CoA substrates that ranged from C(8) to C(16) in length, and is the most active with palmitoyl-CoA and myristoyl-CoA .
Catalytic Activity: a 1,2-saturated acyl-CoA + an acyl-CoA + H2O = an (R)-2-alkyl-3-oxoalkanoate + 2 CoA + H(+)
Sequence Mass (Da): 36629
Sequence Length: 338
Domain: Contains three extended channels that together form a T-shaped, three-channel nexus . Contains an active site base originating from the second monomer of the dimer .
Subcellular Location: Cytoplasm
EC: 2.3.3.20
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Q8EG65 | MLDTLLPFKRHFLSRNGNKLHYINEGQGEPVVMVHGNPSWSFYYRNLVSALKDTHQCIVPDHIGCGLSDKPDDSGYDYTLKNRIDDLEALLDSLNVKENITLVVHDWGGMIGMGYAARYPERIKRLVILNTGAFHLPDTKPLPLALWICRNTLLGTVLVRGFNAFSSIASYVGVKRQPMSKYIREAYVAPFNSWANRISTLRFVQDIPLKPGDRNYQLVSDIAASLPKFAKVPTLICWGLQDFVFDKHFLVKWREHMPHAQVHEFADCGHYILEDASDEVITHIKHFMTETETLATQVNPADSITEFESASQAPQAER | Function: Involved in olefin biosynthesis . Catalyzes the elimination of carbon dioxide from beta-lactones to form the final olefin product (By similarity). The S.oneidensis oleABCD genes produce 3,6,9,12,15,19,22,25,28-hentriacontanonaene, which may aid the cells in adapting to a sudden drop in temperature .
Catalytic Activity: a cis-3-alkyl-4-alkyloxetan-2-one = a cis-alkene + CO2
Sequence Mass (Da): 36114
Sequence Length: 318
EC: 4.1.1.114
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Q8PDW8 | MTYPGYSFTPKRLDVRPGIAMSYLDEGPSDGEVVVMLHGNPSWGYLWRHLVSGLSDRYRCIVPDHIGMGLSDKPDDAPDAQPRYDYTLQSRVDDLDRLLQHLGITGPITLAVHDWGGMIGFGWALSHHAQVKRLVITNTAAFPLPPEKPMPWQIAMGRHWRLGEWFIRTFNAFSSGASWLGVSRRMPAAVRRAYVAPYDNWKNRISTIRFMQDIPLSPADQAWSLLERSAQALPSFADRPAFIAWGLRDICFDKHFLAGFRRALPQAEVMAFDDANHYVLEDKHEVLVPAIRAFLERNPL | Function: Involved in olefin biosynthesis . Catalyzes the elimination of carbon dioxide from beta-lactones to form the final olefin product .
Catalytic Activity: a cis-3-alkyl-4-alkyloxetan-2-one = a cis-alkene + CO2
Sequence Mass (Da): 34080
Sequence Length: 300
Subcellular Location: Cytoplasm
EC: 4.1.1.114
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Q8EG64 | MTKVDDALFEHGASAVAVEQNNGRDNPTKPKDANICRHLKLAAHHIPHHLAVAVQQGKGKSFANLTYQELDFISLNKQSDAIAFALNAYGLTRGMKAVLMVTPSLDFFALTFALFKAGIIPVLVDPGMGIKNLKQCFIEAAPDAFIGIPKAHIARRLLGWGKASVKRLINVDANQSGVTDTLSRLLTGAPSLASMLSFTTKSSSAKLPEQVEYPMALLEHDEMAAILFTSGSTGTPKGVVYSHGMFEAQIQALKQDYGIAHGERDLATFPLFSLFGPALGMTSIVPEMDASKPITANPEFLFAAIEKYQCSNIFVNPALLERLGRAGEQTDSKNQHKLSSVKRVISAGAPATIASIARFSKMLSDGVPVLNSYGATESLPISMIASDELFTTTQVTDNGGGICVGRAIDGVKIEIIAITEADIPEWDNRLCLNAGEIGEIVVTGQMVSQSYYHREKATAASKIWDSERQTFRHRMGDLGYLDDSGRLWMCGRKAHRVDATQGGQFAKRYYSIPCERIFNTHPNVKRSALVGVTVKGQHGVGEIKPLICIELDQSLVCNKSAQLYQELMVIAEQYSQTQGIRRFLIHPDFPVDVRHNAKIFREKLAVWAQSQTKG | Function: Involved in olefin biosynthesis . Catalyzes the conversion of 2-alkyl-3-hydroxyalkanoic acids to beta-lactones in the presence of ATP (By similarity). The S.oneidensis oleABCD genes produce 3,6,9,12,15,19,22,25,28-hentriacontanonaene, which may aid the cells in adapting to a sudden drop in temperature .
Catalytic Activity: a (2R,3S)-2-alkyl-3-hydroxyalkanoate + ATP = a cis-3-alkyl-4-alkyloxetan-2-one + AMP + diphosphate
Sequence Mass (Da): 66991
Sequence Length: 614
EC: 6.1.3.1
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B2FI28 | MNRPCNIAARLPELARERPDQIAIRCPGRRGAGNGMAAYDVTLDYRQLDARSDAMAAGLAGYGIGRGVRTVVMVRPSPEFFLLMFALFKLGAVPVLVDPGIDRRALKQCLDEAQPEAFIGIPLAHVARLVLRWAPSAARLVTVGRRLGWGGTTLAALERAGAKGGPMLAATDGEDMAAILFTSGSTGVPKGVVYRHRHFVGQIQLLGSAFGMEAGGVDLPTFPPFALFDPALGLTSVIPDMDPTRPAQADPVRLHDAIQRFGVTQLFGSPALMRVLAKHGRPLPTVTRVTSAGAPVPPDVVATIRSLLPADAQFWTPYGATECLPVAVVEGRELERTRAATEAGAGTCVGSVVAPNEVRIIAIDDAPLADWSQARVLAVGEVGEITVAGPTATDSYFNRPQATAAAKIRETLADGSTRVVHRMGDVGYFDAQGRLWFCGRKTQRVETARGPLYTEQVEPVFNTVAGVARTALVGVGAAGAQVPVLCVELLRGQSDSPALQEALRAHAAARTPEAGLQHFLVHPAFPVDIRHNAKIGREKLAVWASAELEKRA | Function: Involved in olefin biosynthesis . Catalyzes the conversion of beta-hydroxy acid substrates to beta-lactones in the presence of ATP . Can use all four stereoisomers of 2-hexyl-3-hydroxydecanoic acid .
Catalytic Activity: a (2R,3S)-2-alkyl-3-hydroxyalkanoate + ATP = a cis-3-alkyl-4-alkyloxetan-2-one + AMP + diphosphate
Sequence Mass (Da): 58578
Sequence Length: 552
EC: 6.1.3.1
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Q74A86 | MKKGMKVSLSVAAAALLMSAPAAFAFHSGGVAECEGCHTMHNSLGGAVMNSATAQFTTGPMLLQGATQSSSCLNCHQHAGDTGPSSYHISTAEADMPAGTAPLQMTPGGDFGWVKKTYTWNVRGLNTSEGERKGHNIVAGDYNYVADTTLTTAPGGTYPANQLHCSSCHDPHGKYRRFVDGSIATTGLPIKNSGSYQNSNDPTAWGAVGAYRILGGTGYQPKSLSGSYAFANQVPAAVAPSTYNRTEATTQTRVAYGQGMSEWCANCHTDIHNSAYPTNLRHPAGNGAKFGATIAGLYNSYKKSGDLTGTQASAYLSLAPFEEGTADYTVLKGHAKIDDTALTGADATSNVNCLSCHRAHASGFDSMTRFNLAYEFTTIADASGNSIYGTDPNTSSLQGRSVNEMTAAYYGRTADKFAPYQRALCNKCHAKD | Cofactor: Binds 6 low-spin heme groups per subunit.
Function: Plays an important role in extracellular electron transfer. Can transfer electrons to insoluble Fe(3+) oxides as well as other extracellular electron acceptors, including Mn(4+) oxide and humic substances . Essential for direct interspecies electron transfer (DIET) in cocultures with G. metallireducens .
Sequence Mass (Da): 45389
Sequence Length: 432
Subcellular Location: Cell outer membrane
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Q99983 | MGFLSPIYVIFFFFGVKVHCQYETYQWDEDYDQEPDDDYQTGFPFRQNVDYGVPFHQYTLGCVSECFCPTNFPSSMYCDNRKLKTIPNIPMHIQQLYLQFNEIEAVTANSFINATHLKEINLSHNKIKSQKIDYGVFAKLPNLLQLHLEHNNLEEFPFPLPKSLERLLLGYNEISKLQTNAMDGLVNLTMLDLCYNYLHDSLLKDKIFAKMEKLMQLNLCSNRLESMPPGLPSSLMYLSLENNSISSIPEKYFDKLPKLHTLRMSHNKLQDIPYNIFNLPNIVELSVGHNKLKQAFYIPRNLEHLYLQNNEIEKMNLTVMCPSIDPLHYHHLTYIRVDQNKLKEPISSYIFFCFPHIHTIYYGEQRSTNGQTIQLKTQVFRRFPDDDDESEDHDDPDNAHESPEQEGAEGHFDLHYYENQE | Function: May be implicated in biomineralization processes. Has a function in binding of osteoblasts via the alpha(V)beta(3)-integrin.
PTM: Glycosylated; contains keratan sulfate.
Sequence Mass (Da): 49492
Sequence Length: 421
Subcellular Location: Secreted
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O35103 | MGFLSPIYVLFFCFGVRVYCQYEAYRWDDDYDQEPNEDYDPEFQFHQNIEYGVPFYNNILGCAKECFCPTNFPTSMYCDNRKLKTIPIIPMHIQQLNLQFNDIEAVTANSFINATHLKEINLSHNKIKSQKIDYGVFAKLSNLQQLHLEHNNLEEFPFPLPKSLERLLLGYNEISILPTNAMDGLVNVTMLDLCYNHLSDSMLKEKTLSKMEKLMQLNLCNNRLESMPLGLPSSLMYLSLENNSISSIPDNYFDKLPKLHALRISHNKLEDIPYDIFNLSNLIELNVGHNKLKQAFYIPRNLEHLYLQNNEIESINVTMICPSPDPVHHHHLTYLRVDQNKLKEPISSYIFFCFPRIHSIYYGEQRSTNGETIQLKTQVFRSYQEEEEEDDHDSQDNTLEGQEVSDEHYNSHYYEMQEWQDTI | Function: May be implicated in biomineralization processes. Has a function in binding of osteoblasts via the alpha(V)beta(3)-integrin.
PTM: Glycosylated; contains keratan sulfate.
Sequence Mass (Da): 49745
Sequence Length: 423
Subcellular Location: Secreted
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P02931 | MMKRNILAVIVPALLVAGTANAAEIYNKDGNKVDLYGKAVGLHYFSKGNGENSYGGNGDMTYARLGFKGETQINSDLTGYGQWEYNFQGNNSEGADAQTGNKTRLAFAGLKYADVGSFDYGRNYGVVYDALGYTDMLPEFGGDTAYSDDFFVGRVGGVATYRNSNFFGLVDGLNFAVQYLGKNERDTARRSNGDGVGGSISYEYEGFGIVGAYGAADRTNLQEAQPLGNGKKAEQWATGLKYDANNIYLAANYGETRNATPITNKFTNTSGFANKTQDVLLVAQYQFDFGLRPSIAYTKSKAKDVEGIGDVDLVNYFEVGATYYFNKNMSTYVDYIINQIDSDNKLGVGSDDTVAVGIVYQF | Function: Forms pores that allow passive diffusion of small molecules across the outer membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 39333
Sequence Length: 362
Subcellular Location: Cell outer membrane
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Q56113 | MMKRKILAAVIPALLAAATANAAEIYNKDGNKLDLYGKAVGRHVWTTTGDSKNADQTYAQIGFKGETQINTDLTGFGQWEYRTKADRAEGEQQNSNLVRLAFAGLKYAEVGSIDYGRNYGIVYDVESYTDMAPYFSGETWGGAYTDNYMTSRAGGLLTYRNSDFFGLVDGLSFGIQYQGKNQDNHSINSQNGDGVGYTMAYEFDGFGVTAAYSNSKRTNDQQDRDGNGDRAESWAVGAKYDANNVYLAAVYAETRNMSIVENTVTDTVEMANKTQNLEVVAQYQFDFGLRPAISYVQSKGKQLNGADGSADLAKYIQAGATYYFNKNMNVWVDYRFNLLDENDYSSSYVGTDDQAAVGITYQF | Function: Forms pores that allow passive diffusion of small molecules across the outer membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 40106
Sequence Length: 363
Subcellular Location: Cell outer membrane
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Q8XB59 | MSELLSFALFLASVLIYAWKAGRNTWWFAATLTVLGLFVVLNITLFASDYFTGDGINDAVLYTLTNSLTGAGVSKYILPGIGIVLGLTAVFGALGWILRRRRHHPHHFGYSLLALLLALGSVDASPAFRQITELVKSQSRDGDPDFAAYYKEPSKTIPDPKLNLVYIYGESLERTYFDNEAFPDLTPELGALKNEGLDFSHTQQLPGTDYTIAGMVASQCGIPLFAPFEGNASASVSSFFPQNICLGDILKNSGYQNYFVQGANLRFAGKDVFLKSHGFDHLYGSEELKSVVADPHYRNDWGFYDDTVLDEAWKKFEELSRSGQRFSLFTLTVDTHHPDGFISRTCNRKKYDFDGKPNQSFSAVSCSQENIATFINKIKASPWFKDTVIVVSSDHLAMNNTAWKYLNKQDRNNLFFVIRGDKPQQETLAVKRNTMDNGATVLDILGGDNYLGLGRSSLSGQSMSEIFLNIKEKTLAWKPDIIRLWKFPKEMKEFTIDQQKNMIAFSGSHFRLPLLLRVSDKRVEPLPESEYSAPLRFQLADFAPRDNFVWVDRCYKMAQLWAPELALSTDWCVSQGQLGGQQIVQHVDKTTWKSKTAFKDTVIDMARYKGNVDTLKIVDNDIRYKADSFIFNVAGAPEEVKQFSGISRPESWGRWSNAQLGDEVKIEYKHPLPKKFDLVITAKAYGNNASRPIPVRVGNEEQTLVLGNEVTTTTLHFDNPTDADTLVIVPPEPVSTNEGNILGHSPRKLGIGMVEIKVVEREG | Function: Transfers a phosphoglycerol residue from phosphatidylglycerol to the membrane-bound nascent glucan backbones.
Catalytic Activity: phosphatidylglycerol + membrane-derived-oligosaccharide D-glucose = 1,2-diacyl-sn-glycerol + membrane-derived-oligosaccharide 6-(glycerophospho)-D-glucose.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 85524
Sequence Length: 763
Pathway: Glycan metabolism; osmoregulated periplasmic glucan (OPG) biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.7.8.20
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Q8XVC3 | MRLAVGLLALASAQAALAFGLNDVAARAKQLAAKPYQAPPDTLPHELRELRYDQYREIRFKSDQAYWRRDKLPFELGFFHEGSYYDQPVKINEVSPAGAREIRFDPRLFDYGPVKLDPKHLRNLGFAGFRIHYPMNTPKYKDEVIVFLGASYFRGIGKGQVYGLSARGLAIDTALNSGEEFPRFTEFWIERPAANAKELTIYALLNSRRATGAYRFVIKPGTDTEVDVKAQLYMRENVSKLGIAPLTSMFFFGENQPASALDFRPEVHDSDGLSMLSGTGEWIWRPLTNPKRLLVSSFSTTNPGGFGLMQRDRAFSSYQEIGDRYELRPSAWVEPVGKWGAGRVELVQIPTPDETNDNVVAYWVPETPPKPQQPFNLEYRLLWQKEGDKKPGLSWVTQTRRSHGWTTKRPDERKPDDTIALVVDFEGPALAKLPPNAPVEPVFTADANGKIESIFGQPNTATGGWRVTVRLKRVDDDKPIELRGYLRSGGTGLSETWSYLLPPG | Function: Involved in the biosynthesis of osmoregulated periplasmic glucans (OPGs).
Sequence Mass (Da): 56761
Sequence Length: 504
Pathway: Glycan metabolism; osmoregulated periplasmic glucan (OPG) biosynthesis.
Subcellular Location: Periplasm
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Q6N5U4 | MNRRQVLTGLAALPLLQAKPDPAAADRSSSIDFDPWMVRKLARELASKPYEAPDSSLPASLNDLSYDAYRSLRFRPERALWRAENLPFQVQFFHRGFLYKNRVTIFEVADGKARHVPYRADDFSFGDVAPPPDSDLGFAGFRIHAPLQRADYYDEVSAFLGAAYFRAVTKGERYGLSARGLSIDTGQSSGEEFPLFKTFWLERPAPGASSMVVHALLDSKSVAGAYRFTIRPGDTTVFDVEMALYPRVDLQHAGLAPMTSMFLFGPNDPADTPDFRAAVHDSDGLAIFNGSGEELWRPLCNPKDLQISSFGDRNPRGFGLMQRERSFANYQDLESRYELRPSLWAEPIGDWTDGAVKLIEIPTREEVHDNIASFWEPKQPLRAKGEHIYTYRLHWGPDTPKPKGLARFVRTGVSARGDNDRLFVLDLAGDRLKTVDAAAVRGVVTADKGEIRNIVTQPNPAMGGWRLSFDLAQARAPVELRAVVCEGDAAVSEVWLYRWTP | Function: Involved in the biosynthesis of osmoregulated periplasmic glucans (OPGs).
Sequence Mass (Da): 56032
Sequence Length: 501
Pathway: Glycan metabolism; osmoregulated periplasmic glucan (OPG) biosynthesis.
Subcellular Location: Periplasm
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P24138 | MLKYIGRRLVYMIITLFVIVTVTFFLMQAAPGGPFSGEKKLPPEIEANLNAHYGLDKPLFVQYVSYLKSVAMWDFGPSFKYKGQSVNDLISSGFPVSFTLGAEAILLALALGVLFGVIAALYHNKWQDYTVAILTIFGISVPSFIMAAVLQYVFSMKLGLFPVAGWDSWAYTFLPSIALASMPMAFIARLSRSSMIEVLNSDYIRTAKAKGLSRPAVTVRHAIRNALLPVVTYMGPMAAQVLTGSFIIETIFGIPGLGAHFVNSITNRDYTVIMGVTVFFSVILLLCVLIVDVLYGIIDPRIKLSKAKKGA | Function: Part of the binding-protein-dependent transport system for oligopeptides; probably responsible for the translocation of the substrate across the membrane. Also required for sporulation and competence.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34075
Sequence Length: 311
Subcellular Location: Cell membrane
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P0A4N7 | MWKVIIRRILLMIPQLFILSILVFFFAKLMPGDPFSGLIGPHTDPHEVEALRRAAGLYDPWWEQYLRWLGNAIHGNLGMSYNLKEPVMTVIGHRAINTFWMSLLSVILTYLFAIPMSIVAARNEGKWQDQLWLTYNSITFGIPPYVFYLLIIFIFGYSLNWFPTGGTVSPDAMGIIPVFFSKIYHMILPAFSLAVFGTVGIFTYFRSGILDEQTQDYVRTARAKGVKEKVIFRRHILRNASLPIASNFGFVITGLLGGAIFAETIFGYPGLGQLFITSISGRDYSMITALILLNGFLGLLGALLSDIIMAMVDPRIRIQ | Function: Part of the binding-protein-dependent transport system for oligopeptides; probably responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35962
Sequence Length: 319
Subcellular Location: Cell membrane
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P75554 | MFIVMTIVFFLVNSTGQTPLSATSSKDLEAVKTQLDAFGFNDPLIVRYGRYWQTLFSGSLGTYYSSPNQTIDQIVFGRVPNTLYVVLISFFIGSLLGIIFGMISGLFRGKLIDAVINVLVVLFVSIPSFVVGLGLLKAAGLFRLPPRFINFDDANFNFGNFLLASIIPILSLVFYTSAAFTYRVRNEVVEVMNQDYIKTARSKGLSTFAVALYHIFRNSIIPSVPLFVFGISGAFSGGFIIESLFGVQGVSRILIDSVQSNETNLVMFNIMFIQGIPLLASVFIELIYVLVDPRIRIASAGGVSLWTKLKFVYLRQAWLRKWRRINHTNSHNVLFNSPQHRQLLELKAIDYKHNTISLTEQQKTTLKIEPTANFVLLGTKCLKIITIHG | Function: Part of the binding-protein-dependent transport system for oligopeptides; probably responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 43538
Sequence Length: 389
Subcellular Location: Cell membrane
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P08005 | MLKFILRRCLEAIPTLFILITISFFMMRLAPGSPFTGERALPPEVLANIEAKYHLNDPIMTQYFSYLKQLAHGDFGPSFKYKDYTVNDLVAASFPVSAKLGAAAFLLAVIIGVSAGVIAALKQNTRWDYTVMGFAMTGVVIPSFVVAPLLVMVFAITLQWLPGGGWNGGALKFMILPMVALSLAYIASIARITRGSMIEVLHSNFIRTARAKGLPMRRIIFRHALKPALLPVLSYMGPAFVGIITGSMVIETIYGLPGIGQLFVNGALNRDYSLVLSLTILVGALTILFNAIVDVLYAVIDPKIRY | Function: Part of the binding-protein-dependent transport system for oligopeptides; probably responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 33420
Sequence Length: 306
Subcellular Location: Cell inner membrane
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P24139 | MQNIPKNMFEPAAANAGDAEKISKKSLSLWKDAMLRFRSNKLAMVGLIIIVLIILMAIFAPMFSRYDYSTTNLLNADKPPSKDHWFGTDDLGRDIFVRTWVGARISIFIGVAAAVLDLLIGVIWGSISGFRGGRTDEIMMRIADILWAVPSLLMVILLMVVLPKGLFTIIIAMTITGWINMARIVRGQVLQLKNQEYVLASQTLGAKTSRLLFKHIVPNAMGSILVTMTLTVPTAIFTEAFLSYLGLGVPAPLASWGTMASDGLPALTYYPWRLFFPAGFICITMFGFNVVGDGLRDALDPKLRK | Function: Part of the binding-protein-dependent transport system for oligopeptides; probably responsible for the translocation of the substrate across the membrane. Also required for sporulation and competence.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 33621
Sequence Length: 305
Subcellular Location: Cell membrane
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P0AFH7 | MMLSKKNSETLENFSEKLEVEGRSLWQDARRRFMHNRAAVASLIVLVLIALFVILAPMLSQFAYDDTDWAMMSSAPDMESGHYFGTDSSGRDLLVRVAIGGRISLMVGVAAALVAVVVGTLYGSLSGYLGGKVDSVMMRLLEILNSFPFMFFVILLVTFFGQNILLIFVAIGMVSWLDMARIVRGQTLSLKRKEFIEAAQVGGVSTSGIVIRHIVPNVLGVVVVYASLLVPSMILFESFLSFLGLGTQEPLSSWGALLSDGANSMEVSPWLLLFPAGFLVVTLFCFNFIGDGLRDALDPKDR | Function: Part of the binding-protein-dependent transport system for oligopeptides; probably responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 33022
Sequence Length: 302
Subcellular Location: Cell inner membrane
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P0A4N9 | MTEKKHKNSLSLVHSIKEELKKDKLAMISTIFLVAVFLIVYIYSMFLKQSNYVDVNIMDQYLAPLTNGHLLGTDNGGRDIIMMLMISARNSFNIAFAVTLITLVVGNILGVITGYFGGRFDLIFMRFTDFVMILPSMMIIIVFVTIIPRFNSWSLIGIISIFSWIGTTRLIRARTMTEVNRDYVRASKTSGTSDFKIMFREIWPNLSTLVIAEATLVFAGNIGLETGLSFLGFGLPAGTPSLGTMINEATNPETMTDKPWTWVPATVVILIVVLAIIFIGNALRRVADQRQATR | Function: Part of the binding-protein-dependent transport system for oligopeptides; probably responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32835
Sequence Length: 294
Subcellular Location: Cell membrane
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