ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
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Q6CKY2 | MAFWRNRHESPAISQERSPSPDRFQNSEDIREDNNNYNEDEKLGWFASFMGMFSLPYDWYLSINEDIAVIDWDSKSNSVAWPLGNVLTFLFFSVRLLQDNVIAPNINKLTHSDDAFDFSKSKNLQKYDYFQQYGGSASSSENLYYKMLRQLHRLFYLLTVLLLITNISVTYRYLFAHFQTYSIFYWKTVPKSKNVTKKSLHDLNHTYVEDAKRDSLWGMIKYLLFNGSHDDETNRAHYYELRKWTPSRFLTSFFVSFSPIAFCFLWMTDVTFKTLIPIIIHQYVLWFIVIDRYEQKLKDEQILSMSSVAELNSKVIQPKMNVLKQDAMVDATPYNDGIVYFYPAYTTTRSHVFATHTLSGKLSKEKYNPRTDSFEDANSQRTENYVRFSYHHPKSINGAYVRESYPSRQHSPRLSPSRYSHLQSGNTPSAPSTPLLIPSQQPHFDHSMLANASRNHNISERRNSHSPIKQHFANRLLNYPDETNDSIPDVSDDRFRMDDRFRRGRQGYFNRSPDINSGTLHYDDGDDDDNRISKSPFRNSSSSPFR | Function: Member of a perinuclear network that controls recombination at multiple loci to maintain genome stability. Required for rDNA repeat stability (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 64087
Sequence Length: 546
Subcellular Location: Nucleus membrane
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C5E3S7 | MTFRLSRFESPLIEDDGESRASLLGYSPENELYTDVDENRESRFRRFMSFISSSPYDMFLAINEHVESIDWDSKASTIAGPLGNFFTCSLYTARLLQDSLIRPNQQKLDKKRDSFDLSRSEILRKFEYLSQVPKSGVVVTHLNWYWKFLTFLNVALQITVGFLILINLFVAYKFLIGHFQVYSLFYTKTSPRSKNVTKRSLSDLSFKSLEEVTNSSLWTMIRYMFVRKRLIIKDAPKGKYYYQLRKWTPGKFYTALFSAFSPISVIFLLVTEVSFKTALAVIGHQYILFLVLFKRYESRLDDEACLAKAHFEEINEKVIKPKTTIKTQDAMVDATTYGGGAAFFPSFTTTRSHIFQTHAVTGDIITERYNPETRNFEDVENTGRAKNYISQIQGVSHGQQVVSRSKAMNGATARPQFFSRQPSPSKIGTPSIILNYRTSPFSAPTTPTLKPVNGVQNGQSIFRNSPDPSKANSLNCDTSHLSRNNTLSRLRRNSVSPTKSGNYCSASGMRAIHKSNFGADSSVSYSMEAPSNELPFEEVARRGRHPFEITASRDLPAGRSSAVSSRHSSISPFKGNTSFAGRESLDSRPPFR | Function: Member of a perinuclear network that controls recombination at multiple loci to maintain genome stability. Required for rDNA repeat stability (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 67038
Sequence Length: 592
Subcellular Location: Nucleus membrane
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A7TH24 | MNGLDDENQIDERDHYTDDGDYEIDIDSMNMFKSLYYEMMAYFSDLQMHLGEHLMAIDWDMKCKSIAEPVGNCLTALFYIIRLLQDTLLSNYKDVYVSTEAFDLSKSTTLQEFPFLIRFVEVSKTKNLQNAKYIKKKTFMFYFDKLLLFLMILILSTNAYISWTFIWRNFKTYSLLYVVDRPNSKNVTKCSRTDLDQSYMENVSYGSYWTMLSYYIRNFRKKDDLEDEITTVKQKTPNVNEKDYYYQLKKWSPSKFLTSLFCSFSPTCLVFLILSDVSFTTSIAVILHQFIFKYVVFEGYESRINDESIIHSAMISEINQKFVEPRLSKKVQDAKIDATPEGKVYRTEFFPSLTNCKSNLFNRHDLKGRSITESYNDRIKEFEIVTNTNNETHNVIKVVKK | Function: Member of a perinuclear network that controls recombination at multiple loci to maintain genome stability. Required for rDNA repeat stability (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 47397
Sequence Length: 401
Subcellular Location: Nucleus membrane
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Q12066 | MGSNDLINEAYDDSEVVGEERESKSAWMKRWYQLLTSPLDLQLVINEKLEMINWDAYAKSLAKPLGNFLTILFFIIRLLQDNLIKPNYYKLNVKSGAFDLSKSNKLKEFDYLWEISSSFQNNNQFYAFQSWYFVTLRFLNNLFRFTIFILLSLNLYVSCKFMFGYFKTYNLFHLKKEFNSPNLTKHNLKDLSKEYYEDIYKQSLWSMLKHFFRGSRDDGPHVNQNEDEIFFQLRKWIPTNFMINLFVSFSPTAIVFLSFSDVSFTSAIAIVFHQYILDYIITKRFQRSVDDDLILSSAALQEYEDKHIMARINQCSNIDTLSSAMGTRSKTPRIFTTHSLCGEEIREVYNYEKREFEALPKMTESVPGSRETRIKDYGGISQVSDHQSHPIGFHYSPRMSPYYRDKVLDNNLAQSSSNENLEKGGAYLPNQDQNRPSKSLSPLRKTPLSARQKRFEGSEFNVLNKNDINSILRSPKKKKNYHKR | Function: Member of a perinuclear network that controls recombination at multiple loci to maintain genome stability. Required for rDNA repeat stability.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 56887
Sequence Length: 484
Subcellular Location: Nucleus membrane
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P97346 | MSGFLEELLGDKLVTGGGEEVDVHSLGARGIALLGLYFGCSLSAPCAQLSASLAAFYGRLRGDAAAGPGAGAGAGAAAEPEPRHRLEIVFVSSDQDQRQWQDFVRDMPWLALPYKEKHRKLKLWNKYRVSNIPSLIFLDATTGKVVCRNGLLVIRDDPEGLEFPWGPKPFREVIAGPLLRNNGQSLESSSLEGSHVGVYFSAHWCPPCRSLTRVLVESYRKIKEAGQEFEIIFVSADRSEESFKQYFSEMPWLAVPYTDEARRSRLNRLYGIQGIPTLIVLDPQGEVITRQGRVEVLNDEDCREFPWHPKPVLELSDSNAVQLNEGPCLVLFVDSEDDGESEAAKQLIQPIAEKIIAKYKAKEEEAPLLFFVAGEDDMTDSLRDYTNLPEAAPLLTILDMSARAKYVMDVEEITPAIVETFVNDFLAEKLKPEPI | Function: Functions as a redox-dependent negative regulator of the Wnt signaling pathway, possibly by preventing ubiquitination of DVL3 by the BCR(KLHL12) complex. May also function as a transcriptional regulator act as a regulator of protein phosphatase 2A (PP2A).
Catalytic Activity: [protein]-dithiol + NAD(+) = [protein]-disulfide + H(+) + NADH
Sequence Mass (Da): 48344
Sequence Length: 435
Subcellular Location: Cytoplasm
EC: 1.8.1.8
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Q5E9M6 | MQAACWYVLLLLQPTVYLVTCANLTNGGKSELLKSGGSKSTLKHIWTESSKDLSISRLLSQTFRGKENDTDLDLRYDTPEPYSEQDLWDWLRNSTDLQEPRPRAKRRPIVKTGKFKKMFGWGDFHSNIKTVKLNLLITGKIVDHGNGTFSVYFRHNSTGQGNVSVSLVPPTKIVEFDLAQQTVIDAKDSKSFNCRIEYEKVDKATKNTLCNYDPSKTCYQEQTQSHVSWLCSKPFKVICIYISFYSTDYKLVQKVCPDYNYHSDTPYFPSG | Function: May be signaling molecules that resemble neuropeptides. Ligand for alpha-neurexins (By similarity).
PTM: May be proteolytically processed at the boundary between the N-terminal non-conserved and the central conserved domain in neuron-like cells.
Sequence Mass (Da): 31018
Sequence Length: 271
Subcellular Location: Secreted
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Q61200 | MQAACWYVLLLLQPTVYLVTCANLTNGGKSELLKSGSSKSTLKHIWTESSKDLSISRLLSQTFRGKENDTDLDLRYDTPEPYSEQDLWDWLRNSTDLQEPRPRAKRRPIVKTGKFKKMFGWGDFHSNIKTVKLNLLITGKIVDHGNGTFSVYFRHNSTGQGNVSVSLVPPTKIVEFDLAQQTVIDAKDSKSFNCRIEYEKVDKATKNTLCNYDPSKTCYQEQTQSHVSWLCSKPFKVICIYISFYSTDYKLVQKVCPDYNYHSDTPYFPSG | Function: May be signaling molecules that resemble neuropeptides. Ligand for alpha-neurexins.
PTM: May be proteolytically processed at the boundary between the N-terminal non-conserved and the central conserved domain in neuron-like cells.
Sequence Mass (Da): 31048
Sequence Length: 271
Subcellular Location: Secreted
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P0DTY0 | MKLTYVLIVAMLVLVVCRADCFGRGGLCTWFDPSVCCSGICTFVDCW | Function: Probable neurotoxin.
PTM: May contain 3 disulfide bonds.
Sequence Mass (Da): 5196
Sequence Length: 47
Domain: The cysteine framework is C-C-C-CC-C-C.
Subcellular Location: Secreted
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D5KR58 | MKLTCVLIVAVLILTACQFTAADDMEYPKWLRGLSTDXSERGCWLCLGPNACCRGSVCHDYCPR | Function: Probable neurotoxin with unknown target. Possibly targets ion channels.
PTM: Five different peptides have been sequenced after total venom examination by HPLC-MS. cal6.4a-4c are identical in length but are differentially hydroxylated and brominated.
Sequence Mass (Da): 7111
Sequence Length: 64
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Subcellular Location: Secreted
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Q3YEE1 | MKLTCVLIITVLFLTACQLTAAGNSRDKQEDPVVRSSGEVQRSEDIKLAKRCLESGSLCFAGYGHSSCCSGACLDYGGLGVGACR | Function: Produces no obvious effect on ionic currents when tested on the mouse dorsal rooted ganglia (DRG).
Sequence Mass (Da): 8920
Sequence Length: 85
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Subcellular Location: Secreted
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Q8VG05 | MAFLQDGNHTAVTEFILLGLTDDPVLRVVLFTIILCIYLVTVFGNLSTILLIRVSSQLHHPMYFFLSHLASVDIGISSSVTPSMLVNFLLERSTISYLGCGIQLGSADFIASVECFLLAAMAYDRFMAVCNPLLYSTKMSTQVCVQLVVGSYIGGFLNASLIVTVYFFSFLFCGPNRIDHFFCDFAPLAELSCSDVSVSVLIISFSAGSVTMITVFVIVISYSYILITILKMHSTEGRHKAFSTCTSHLTAVTLYYGTITFIYVMPKSSFSTDQNKVVSVFYMVMIPMLNPLIYSLSNNEIKGALKRQLGMKTLS | Function: Potential odorant receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34774
Sequence Length: 315
Subcellular Location: Cell membrane
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Q8VFD3 | MAFLHNGNHTAVTEFILLGLTDDPVLRIVLFTIILCIYLVTVSGNLSTILLIRVSSQLHHPMYFFLSHLASADIGYSSSVTPNMLVNFLVKQNTISYIGCSIQFGSAAFFGGLECFLLAVMAYDRFVAICNPLLYSTKMSTQVCVQLVVGSYIGGFLNASFATVSFLFLFFCGPNIINHFFCDFAPLIELSCSDVRISVLVTSFSAGTVTMLTVLVIAISYTYILITILKMRSTEGRHKAFSTCTSHLTAVSLFYGTITFIYVMPKSRYSTDQNKVVSVFYMVVIPMLNPLIYSLRNNEIKGALRRHLGKKIFSQSNILFY | Function: Potential odorant receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35724
Sequence Length: 321
Subcellular Location: Cell membrane
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Q8VG02 | MAFLDNGNHTAVTEFILLGLTDDPFLRIVLFSIILCIYLVTVFGNLSTILLIRVSSQLHHPMYFFLSHLATVDLGISSSVTPSMLVNFLAERSTISYLGCGIQLSSAALFGTLECFLLAVMAYDRFMAICNPLLYSTKLSTRFCIQLVVGSYIGAFLNDSCYILSFAFFLFCGPNKVDHFFCDLSPMMELSCSDASVSGVVISFTAGSITMTTLIVIVISYFYILITILKMRSTEGRQKAFSTCTSHLTAVTLYYGTIIFIYVMPKSTYSRDQNKVVSLFYMVVIPMLNPLIYSLRNNEIKGALKKQFYRKTLL | Function: Potential odorant receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35125
Sequence Length: 314
Subcellular Location: Cell membrane
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Q8VEW5 | MAFLHNGNHTAVTEFILLGLTDDPVFRVILFTIILCIYLVTVSGNLSTILLIRVSSQLHHPMYFFLSHLASVDIGYSSSVTPNMLANFLVEKNTISYLGCTIQLSLAAFCGTVECFLLATMAYDRFMAICSPLLYSTKMSTQVCIQLIVGSYIGGFLNASSFTLFFLSFLFCGPNRINHFYCDFAPLVALSCSDVSVSEVVTSFFSGSVTMITMLVIAISYTYILITILKMRSTEGRHKAFSTCTSHLTAVTLFYGTITFIYVMPKSSFSTDQNKVVSVFYMVVIPMLNPLIYSLRNNEIKDALKRHLGKKIFS | Function: Potential odorant receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34953
Sequence Length: 314
Subcellular Location: Cell membrane
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Q8VEZ0 | MEPGNYTVVTEFILLGLTDDITVSVILFVMFLIVYSVTLMGNLNIIVLIRTSPQLHTPMYLFLSHLAFLDIGYSSSVTPIMLRGFLRKGTFIPVAGCVAQLCIVVAFGTSESFLLASMAYDRYVAICSPLLYSTQMSSTVCILLVGTSYLGGWVNAWIFTGCSLNLSFCGPNKINHFFCDYSPLLKLSCSHDFSFEVIPAISSGSIIVVTVFIIALSYVYILVSILKMRSTEGRQKAFSTCTSHLTAVTLFFGTITFIYVMPQSSYSTDQNKVVSVFYTVVIPMLNPLIYSFRNKEVKEAMKKLIAKTHWWS | Function: Probable odorant receptor, which recognizes only aliphatic alcohols, suggesting that it may convey a 'woody' or 'sweet' sour.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34729
Sequence Length: 312
Subcellular Location: Cell membrane
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Q98892 | MYHPACWIVFTATTALLFIPGVPVRSGDATFPKAMDNVTVRQGESATLRCTVDDRVRRVAWLNRSTILYAGNDKWSIDNRVVILSNTKTQYSIKIHNVDVYDEGPYTCSVQTDNHPKTSRVHLIVQVPPQIVNISSDITVNEGSSVTLMCLAFGRPEPTVTWRHLSGKGQGFVSEDEYLEITGITREQSGEYECSAVNDVAVPDVRKVKVTVNYPPYISNAKNTGASVGQKGILQCEASAVPVAEFQWFKEDTRLANGLEGVRIESKGRLSTLTFFNVSEKDYGNYTCVATNKLGNTNASIILYGPGAVHDSGNAASRAAAGLCLWATLLARLLLDF | Function: Inhibits neurite outgrowth.
Location Topology: Lipid-anchor
Sequence Mass (Da): 36887
Sequence Length: 337
Subcellular Location: Cell membrane
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B1ILY5 | MFIDTAKIFVKSGKGGDGSISFRREKYIAFGGPDGGDGGKGGNVVLVVDPNMTTLLDFTYKRKYKAEPGGNGAGSKCFGKNGKDLHIKVPMGTIVKDVETDKIMADLSKPEDSYVVAKGGRGGKGNCRFTTPTRQAPDFAEPGMPEEERWIKLELKLLADVGLIGFPNVGKSTLLSVVSKARPKIANYHFTTLKPNLGVVSIEGVNNFVIADIPGIIEGASEGVGLGLDFLRHVERTRVLIHVIDISSVEGRDPYDDFLKINEELKRYSVKLYDRPQIIAANKSDMLFDEEKFEEFKTKVEKHGYNKVFKISAATKQGVDDLMKEAARLLSTIPVTDLEISEEDRFIEEEKRFTYSIRKEDNTYIVEGSFVDRLLNAVNVNDPDDLRYFHKVLKNKGVMEELMEMGIEDGDIVRLNDFEFDFLL | 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): 47272
Sequence Length: 424
Subcellular Location: Cytoplasm
EC: 3.6.5.-
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Q18B27 | MFIDKARIFVKAGNGGNGSVAFRREKYVPAGGPDGGDGGRGASIIFEVDLGLRTLMDFKYQKKYQAQNGGDGSKGKRAGKNGENLVLKVPAGTVIRDEATGLVLADLKKEGDTAIVAKGGIGGKGNQHFANAVRQAPAFAKSGTDGEERWITLELKMIADVGLLGFPNVGKSTFLSVVTKAKPKIANYHFTTLTPNLGVVQTKFGDSFVLADIPGIIEGASEGIGLGHEFLRHVERTKVLIHIVDISGLEGRDPIEDFDKINDELKLYNEKLSKRPQVVVANKFDILEDESKFEKFKSELEGRGYTVFKMSAATRQGIDEVIAYVSKMLKEVEDVELVSEEEMYRPELDIGTEEELSIDIEDGVYVVTGKALRRIMYSVNFDDMESLQYFQKAMESQGVFDRLREMGIEDGDVVKIYELEFEFYN | 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): 46883
Sequence Length: 425
Subcellular Location: Cytoplasm
EC: 3.6.5.-
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B9E021 | MFVDRAEVFVKSGSGGNGSVSFRREKYVPRGGPDGGDGGKGGDVILVVDPEITTLLDFSYKKKYVAEKGENGSGSKCFGKNGENLYIKVPLGTVIRDVDTNKIMADLSHIGDKYIVAKGGKGGRGNVRFTTAVRQAPDFAEPGMPGEERYISLELKILADVGLLGFPNVGKSTLLSVVTKAAPKIANYHFTTLSPNLGVVNIPGIQSFVIADIPGIIEGAAEGVGLGIDFLRHIERTRLLIHIVDISGLEGRDPFGDFIKINEELKKYDVKLWDRPQIIAANKADMLYDDSIFQDFKKKVENLGYNKVFKISAATRQGVEELMKEAAAMLTNIPVTDMHISEEDKFIPEEKRFTYEIEKQGNVYVVKGSFVDRLLASINVNDANELRYFHKVLQNKGVMKQLIDMGIKDGDVVRLNDFEFDYIL | 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): 46780
Sequence Length: 424
Subcellular Location: Cytoplasm
EC: 3.6.5.-
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A0Q1T4 | MFIDTAKILVKSGNGGNGCISFRREKYVAMGGPNGGDGGNGGSVILVADRNLTTLLDFTYRRKYVADNGEDGGNSKCFGKKGEDLYIKVPIGTVVKDVETGKTMVDLAKEGDSYIVARGGKGGKGNYHFATPTRQAPNFAEPGMPGEERMINLEIKLLADVGLIGFPNVGKSTLLSMVSKAKPKIANYHFTTLKPNLGVVKIEGANAFVMADIPGIIEGASEGVGLGLDFLRHIERTRLLVHVVDISGVEGRNPIEDFKKINEELKNYSVKLWDRPQIVVANKIDMLYDEEVFETFKKEVNKLGFDKVFKISAATRDGVDDLIKEVTRQLSMIPITEMEIPEEERFMPEEKRFTYTIRVEDGVYVVEGSFVDRLLKSVNVNDPDSLRYFHKVLRNKGILDELKEMGIQDEDTVRLNDFEFDFLL | 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): 47136
Sequence Length: 424
Subcellular Location: Cytoplasm
EC: 3.6.5.-
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B5Y805 | MIFIDTAEIIVYGGKGGDGAASFRREKFIEKGGPDGGDGGKGGDVYLVTDPALLTLYDFKYQKEFRAEDGEPGRSQKQFGKDGKDLFIRIPVGVIVADLETQTVVDMDKPGMKLLVARGGRGGKGNARMATATRRAPRFRELGHEGEMRRLRLELKLVAHVGLVGLPNAGKSSLISVISKAKPEIAPYPFTTRSPVLGIVKKAEQSFVVSDVPGLIEGAHEGKGLGLTFLRHVERTKVLAIVIDAAAIDGYEPMQAYETIIGELRAYNPNLLEKPRVLVLNKIDLLQPEHIDQLKVQFADKESHVVLTSAATGEGTNQLVDVLFELISPTLSTEEPTAEFMTMELPPLPEDFSIRREDEYWVVEGRWARYISRYDTTQPWDFQYVQREIRRKKLEEMLRQMGAKEGETVVIHDKAFEIL | 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): 46625
Sequence Length: 419
Subcellular Location: Cytoplasm
EC: 3.6.5.-
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Q2VZU2 | MKFLDQAKIFVKSGDGGAGCCSFRREKHIEFGGPDGGDGGRGGDVILECVANLNTLIDYRYQQHFKAKIGNHGQGRNKTGGKGDDVILKVPVGTQVLDEEKETVLADLTSAGQTMVLLRGGDGGFGNMHYKSSTNQAPRRADEGWPGEERWIWLRLKMIADAGLVGLPNAGKSTFLAAVTRARPKIADYPFTTLHPNLGVVTLGEEEFVIADIPGLIEGAHEGAGIGDRFLGHIERCRVLLHLIDGTQDDVAEAYRVVRHELAAYGGGLDEKPEVVALNKCDSLTADDIELKLMELSEACGQEVLPLSGVSGVGLKPILARLFTHIREAREAEPAVPAASPIFGSSKRGAPTFQQRKRKLQAEDDEFAGGHWGADGEWIWHSADNDGDEVDEDYDDEDLEEVADDEEDDAEE | 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): 44644
Sequence Length: 412
Subcellular Location: Cytoplasm
EC: 3.6.5.-
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Q8EWL0 | MLIDKCTLFLRAGNGGNGVISWRKEAHYPEGGPWGGDGGKGGDVYIIGDHNLNSLIDLRYKKKIEAEDGENGKTKLATGKNGNDIYIKVPVGTTITNSITNEVIVDILVTGQKYLICKGGMGGKGNAYFKSSKNRIPNLCENGELGETIEAQFELKYIADVGLLGLPNAGKSTLVNSLSNTNLKTANYMFTTLSPSLGVVNFEDEHLVFADIPGIIEDASNGSGLGLDFLKHIERCHFLIHLISVANIDTENPFKDYLTIVEELKKYNKEILKRKIFIVLNKIDENDSKDNINLFLKEFKKISNKKVYQISGFFKENTNELLKDIFKDYKKHKEQWERELEEKINSYSLVKVEKEQEDIVTYEKDENRIWVVSSKRIAYWFNRIPFNTDENVTRFMQKIKMDEIEQTLKDKGAKIGDSFRIQDVMFEIN | 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): 48696
Sequence Length: 429
Subcellular Location: Cytoplasm
EC: 3.6.5.-
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Q0AKX2 | MKFLDQAKVYVRSGNGGGGCVSFRREAYVEYGGPDGGDGGKGGDVWVEAVEGLNTLIDYRYKQHFKADTGMHGMGRNRTGSGGEDVVLQVPAGTQLLDEDKEEILADLTEIGQRVLLARGGDGGKGNSHFKTSTNQAPRKTIPGWPGEERWIWLRLKLIADVGLVGLPNAGKSTFLSVVSKANPKIAAYPFTTLYPNLGVVDLGPGSRFIVADIPGLIEGAHEGAGIGDRFLGHIERCASLIHLIDGTQDDVVAAYKTVRGELEAYGDGLPEKQEILALNKIDAMDEAMVAEKRAELEAASGKTVMTLSGVSGDGVKALCGSAWDIVLQNRRAEKAAAEAAEKGEEGWAPS | 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): 37251
Sequence Length: 351
Subcellular Location: Cytoplasm
EC: 3.6.5.-
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A1TYY4 | MKFVDEATIIVEAGKGGHGCLSFRREKYVPKGGPDGGDGGDGGSVYLEADSALNTLIDYRFQRKYKAQNGEPGAGRNCTGTKGEDLVLPVPVGTTVVDMDTHEVLGDLTKEGQRLKVAQGGFHGLGNTRFKSSVNRAPRQTSKGSEGEARNLRLELKVLADVGLLGLPNAGKSTFIRSVSAARPKVADYPFTTLVPNLGVVSVQAHQSFVIADIPGLIEGAAEGAGLGIRFLKHLVRTRLLLHLVDVAPYDGSSPADAVRAIAHELEKFSETLASRPRWLVLNKVDMVAEEDREAHCQAIVDELGWEGPVFRISALSGEGTKPLVQAVMRWIEEQAEQEADNPDFAEQEAARRRRMDEEARQKIEADRQARRAARNADDDDDFDDDDYDVEVVYAPE | 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): 43231
Sequence Length: 397
Subcellular Location: Cytoplasm
EC: 3.6.5.-
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Q6F0U3 | MKFIDTAKFTIKAGNGGNGAVSFHTALFVPNGGPNGGDGGNGGSVIFEADGGKHSLLDLKLQKQLSAQDGFKGDIKNMHGAQGKDLIVRVPVGTLIIENKTGTILADMDEDKKQVLVAKGGKGGKGNARFANSRNKAPTIFEAGEIGQFYEVKAELKVLADVGFVGLPNAGKSTLLRAISNSKPEVADYAFTTLNPQLGVSRAKDGSTFVVADLPGLIEGASLGKGLGHQFLKHIERCRVICHVLDMSGNYGQEDVIKNYELIRSELVKYNYKLDERPEIIVANKMDTDEAQLNMMEEDIKKYFKDKKVVFVSGLLKDNVDELLLKIAKELETAKYVPLWEMEQDIYEGIKVYRLEEDEEDIQIINKGNGRWEVAGDTIYKIYQKFPITTDDNLLLFNEKLKKSGVYDMLRERGVGAGDIVKVFEYELEWMD | 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): 47699
Sequence Length: 432
Subcellular Location: Cytoplasm
EC: 3.6.5.-
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Q602A7 | MRFVDYVSIEVVAGKGGDGIISFRREAHVDKGGPDGGDGGWGGSIYFVGDSGMNTLLPFYQTKKIFGYNGENGRPKRQTGANGKDIFIKVPLGTQVFLKKSLICDIILEKKYLIAKGGRGGLGNFHFRNSKNKAPRISENGELGQNFYLDLQLKVMADIGLVGKPNAGKSTLLSLISNSKPKIANYEFTTLVPQLGVVKIYENSFVTADLPGLIQGASSGKGMGIIFLKHIERCRAIVHVIDFGSDNKNPIKDFIEIKSELEKFNKKLLDLNQIVIANKCDLPNFQFNLANFKRKFPKIKIIKSSLISAKQNEINIIKEKMFGLLEEKQKKLEIQEINTSKIEFNLKAPFLIKSRNNGFFEITGELIQKIIQKIPLNSQENILRFNAKVKKIGLWDELIKKGIKPGDLVRIYEFEFHWN | 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): 47002
Sequence Length: 419
Subcellular Location: Cytoplasm
EC: 3.6.5.-
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B3DVG9 | MFTDYVRILAKAGKGGNGCISFCREAFRPHGGPDGGDGGKGGDVILEVNPQLSDLSHFLFSPHQFAEDGQPGKGQKRKGRDGKNLKLEVPPGVVVYQLDPNRIFHSSRDLLPIPKPGEPLKKIGELIEPGMRFILCKGGKGGRGNFQFRSPINQSPRYCEEGEEGQSGQFLLELKTIADVGFVGLPNSGKSTLLRQVTDAKPKTAPYPFTTLKPHVGIVNFDDGYRMSCADIPGLIEGAHQGKGLGFYFLRHIERSHLLVYVLDLADPFLDPVQVFYTLRNELEKYNKELLKKPFLIVGNKVDLVAADSLNHKSLDFNKRTGLSFLPISALKAQGIELFLNSCRKSFESTKKLIPSSPKVLSPLT | 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): 40145
Sequence Length: 365
Subcellular Location: Cytoplasm
EC: 3.6.5.-
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A7NRU6 | MAGEFYDSARIFVQAGDGGDGAATFRREKYVPRGGPDGGDGGRGGHVYLVADPGLNTLLPFRERTRFIAERGGNGGRSRKHGRNGRDVFIRVPVGTVARTVIDGETYSVDLDAPGLRLLAARGGRGGLGNVHFATSSYQVPRIAELGEPGERREIELELKLLADVGLIGFPNAGKSTLLSVISAARPKIAPYPFTTLQPNLGVVEVGEYSFVVADIPGLIEGAHRGVGLGFSFLRHIERTRLLIHIIDAAGVDGRDPVNDFSAINEELRLYQPALAQRPQVVALNKADLPEAQANLKRLRAAIPVSEQDLFVISAATREGVDALLQRVAERLREMPAPHRAPRDETLTWPVPEVDERLYTIERTGDGWRVRGRRIERLISMTNFAQPDAIMRIQRVLEASGIGAALQEAGIQNGDVLYIEQAAFDWEDGAITYRMPGVS | 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): 47778
Sequence Length: 439
Subcellular Location: Cytoplasm
EC: 3.6.5.-
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Q165Y6 | MKFLDLCKVYIRSGAGGGGCVSFRREKYIEYGGPDGGDGGTGGSVWAEAVDGLNTLIDFRYQQHFFAKNGQPGMGRQRTGKDGDDIVLRVPVGTEILDEDQETVICDLTEVGQRVQLARGGNGGFGNLHFKSSTNQAPRRSNPGQDGVERTLWLRLKLIADVGLLGLPNAGKSTFLAATSNARPKIADYPFTTLHPNLGVVGVDNTEFVVADIPGLIEGASEGRGLGDLFLGHIERCAVLLHLFDGTSETLIEDYHTIIGELEAYGVGLADKPRITVLNKIDALDEERRAMALKQLNNVCGGGVMAMSGVAGDGVTDVLRKLRGEISDEPLRHKPVEEKEPWRP | 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): 37056
Sequence Length: 344
Subcellular Location: Cytoplasm
EC: 3.6.5.-
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Q1AVU3 | MQFIDEARFVVRGGRGGDGAVSFHREKYRPRGGPDGGRGGDGGSVILRATEDLQTLERYSRRKVISAGRGGHGSGNNRAGERGRDVVLDVPVGTLVYDESGLLADLAEPGQTFVAARGGEGGRGNASFATSRRQAPAFRELGLPGEEREIRLELRVLSDVGLVGLPNAGKSSLLRALSAARPRVGDYPFTTLTPQLGVVEERGYARPFVVADIPGLISGASEGRGLGNRFLRHVARARLLVLVLDASEDPEGAERTLRAELGAAGLSGRPSLVVLNKVDLLDAELRAYLGEAFPGAPQVSARTGEGVGELARLLERRLRELERSAEAAPRPGHRVFRPSWRGLRVERENGAYVVSGREVERLALKTDWDNPEGVEHFQRELERRGVMGALRRAGAGEGDEVRIGDVSFEFR | 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): 44319
Sequence Length: 411
Subcellular Location: Cytoplasm
EC: 3.6.5.-
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Q5LRY4 | MKFLDLAKVYIRSGSGGNGCVSFRREKFIEYGGPDGGDGGKGGSVWAEAVDGLNTLIDFRYQQHFFAQNGVPGKGQQRSGKDGEDIVLRVPVGTEILDEDEETVLADLTEVGQRVLLAKGGNGGFGNLHFKSATNQAPRRANPGQAGVDRTIWLRLKLIADVGLLGLPNAGKSTFLAATSNARPKIADYPFTTLHPNLGVVGVDNVEFVIADIPGLIAGAHEGRGIGDRFLGHVERCAVLLHLVDGTSGDLVEDYHTIIGELEAYGGDLAGKPRVTVLNKIDTLDDEERAFLVEELETASGGPVMMMSGASREGVTEVLRALRARIDANRLREKPVEESQPWQP | 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): 36883
Sequence Length: 344
Subcellular Location: Cytoplasm
EC: 3.6.5.-
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Q5W0B1 | MAQTVQNVTLSLTLPITCHICLGKVRQPVICINNHVFCSICIDLWLKNNSQCPACRVPITPENPCKEIIGGTSESEPMLSHTVRKHLRKTRLELLHKEYEDEIDCLQKEVEELKSKNLSLESQIKTILDPLTLVQGNQNEDKHLVTDNPSKINPETVAEWKKKLRTANEIYEKVKDDVDKLKEANKKLKLENGGLVRENLRLKAEVDNRSPQKFGRFAVAALQSKVEQYERETNRLKKALERSDKYIEELESQVAQLKNSSEEKEAMNSICQTALSADGKGSKGSEEDVVSKNQGDSARKQPGSSTSSSSHLAKPSSSRLCDTSSARQESTSKADLNCSKNKDLYQEQVEVMLDVTDTSMDTYLEREWGNKPSDCVPYKDEELYDLPAPCTPLSLSCLQLSTPENRESSVVQAGGSKKHSNHLRKLVFDDFCDSSNVSNKDSSEDDISRSENEKKSECFSSPKTGFWDCCSTSYAQNLDFESSEGNTIANSVGEISSKLSEKSGLCLSKRLNSIRSFEMNRTRTSSEASMDAAYLDKISELDSMMSESDNSKSPCNNGFKSLDLDGLSKSSQGSEFLEEPDKLEEKTELNLSKGSLTNDQLENGSEWKPTSFFLLSPSDQEMNEDFSLHSSSCPVTNEIKPPSCLFQTEFSQGILLSSSHRLFEDQRFGSSLFKMSSEMHSLHNHLQSPWSTSFVPEKRNKNVNQSTKRKIQSSLSSASPSKATKS | Function: E3 ubiquitin ligase essential for DNA replication origin activation during S phase . Acts as a replication origin selector which selects the origins to be fired and catalyzes the multi-mono-ubiquitination of a subset of chromatin-bound ORC3 and ORC5 during S-phase .
PTM: Auto-ubiquitinated.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 81116
Sequence Length: 726
Subcellular Location: Chromosome
EC: 2.3.2.27
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Q8K2Y0 | MAQTVQNVTLSLTLPITCHICLGKVRQPVVCTNNHVFCSICIDLWLKNNSQCPACRVPITPENPCKEIIGGTSESEPMLSHTVRKHLRKTRLELLHREYEDEIDCLQKEVEELKSKNLSLESQIKTILDPLALMQGSQNEDKHPLADNPSKMDPDSVVEWKKKLRTANEIYEKVKDDVDKLKEANKKLKLENGGLLRENLRLKAEVDNRSPQKFGRFTVAALQSKVEQYERETNRLKKALERSDKYIEELESQVAHLKHSEEAKEDVDALCQRAPSADSKGPNGSDELGPPKNQSDSARKQAGSASASHLASPSSSRLADSGSVRQESTSRTEPNCPQNKDRYPKPTEPRLGARETPMDTYLEREWGSKPSDCAPYKEDELYGIPASCTPLSLSCLQLNTPENRENPVIKAGSSKKHANHLRKLVFDDFCDSPNACNNNSSEDDRRENEKKSDCFASSKTGFWDCCSTSYAQSLEFDGSEGNAIANSVGEIPSKLSEKSGSCLSKRLSCIRSLEMNRTRTSSEASMDAAYLDKISELDSMMSESDNSKSPCNNGFKSVEVEGPSKSPQGREFLEEPDKLQEGSKLNLSKPALTADGLESGGEWKPSSFFLLSPADHEMSEDFSLHSTSHSGTSEVKPPNCLFQTEFSQGALLSSSQGLFEDQRFGSSLFKISSEMQSLHSPLQSPWSAAFVPEKRSKNGNQSTKRKIQSSLANASPSKATKS | Function: E3 ubiquitin ligase essential for DNA replication origin activation during S phase. Acts as a replication origin selector which selects the origins to be fired and catalyzes the multi-mono-ubiquitination of a subset of chromatin-bound ORC3 and ORC5 during S-phase.
PTM: Auto-ubiquitinated.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 79958
Sequence Length: 722
Subcellular Location: Chromosome
EC: 2.3.2.27
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F4JFU8 | MHKDNDSGSGSNPGQVSNYLIVRPHRGGYIDLFRYGVRDDQTSKAKFLEMPDNREWSTITIDEEAEDHRWVIVVSILVRKIIRLLRTPMEFTGFVVDFFLNLFSANGGFFGLLLRLIQAKVVIPERGSVTFVSTIGQLDGRISLYKEWNFVEHLEGIDSVDSGRVKIELGSRGLMDLCVMASKLAYENAKVVENVVDLHWKMNLVEFLDCWNDYQKQMSTQVFVFTDKQKDANLIVISFRGTEPFDADDWGTDFDYSWYEVPNVGKLHMGFLEAMGLGNRDDTTTFHYNLFEQTSSEEENSKKNLLDMVERSAYYAVRVILKRLLSEHENARFVVTGHSLGGALAILFPTLLVLNEETEIMKRLLGVYTFGQPRIGNREVGLFMKAQLNQPVDRYFRVVYCNDIVPRLPYDDKTFLYKHFGLCLFYDSFYNETKAEDEPDPNPYGLRYKILGHVIAVWELVRGLTMGYTHGPDYKEGWFRILFRLMGLVIPGLSDHCMTDYVNSVRLGPDNELQMSSL | Function: Acid lipase that can hydrolyze a range of triacylglycerols without a clear preference for acyl-chains . Can also cleave 1,2-diacylglycerol, 1,3-diacylglycerol and 1-monoacylglycerol, but not phosphatidylcholine, phosphatidylethanolamine, or sterol esters . Required for pollen tube growth . Triacylglycerol hydrolysis by OBL1 may provide acyl groups for the synthesis of membrane lipids in growing pollen tubes (Probable).
Catalytic Activity: (9Z)-octadecenoate + 1,2-di-(9Z-octadecenoyl)-glycerol + H(+) = 1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 59607
Sequence Length: 518
Subcellular Location: Lipid droplet
EC: 3.1.1.-
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Q5VKJ7 | MDDAGKITSTSHLIVSPDEGTFLDLFKHIVLSDLGSGAKFFRASDQRVPATAAYYSRWPVSVFICKILQLFQMPAAMLGHLTDFLLNFYYQNHGFLGILRNIFLIRLKIPKRGEADFISTIGYLDSRMDLHGTPMVSHQADEVISNADNPSLKEGHNSKIKGALGNRSLMDLCIMASKLAYENTKVVERVVAEHWKMHFVADYGGMNYFQDARNTHAFIFCDKPKDANLIVISFRGTGPFSIPNWCTDFDFSLVGLGDAGSVHVGFLEAMGLGHRNSISSFETSINTKSPGSITELRKESEMAPDHLVWAYDGVYFLAASTLKGLLKDHKNAKFVVTGHSLGGALAILFTCILEIQQETEVLDRLLNVYTFGQPRIGNYNLGYFMQNRLNFPERRYFRVVYCNDMVPRVPFDDVFFTFEHFGTCIYYDSRFFGYFTKEEPSRNPFGIENAISAHITAWWELWRSFILNHVYGAEYKETWESRMFRILGLFLPGVAAHSPVNYVNSVRLGRELAIPLMSLKMMAQGY | Function: Acid lipase that can hydrolyze a range of triacylglycerols but is not active on phospholipids . In vitro, hydrolyzes triolein, trilinolein, triricinolein, tripalmitin, trilaurin and tricaprin . May play a role in the regulation of lipolysis in germinating seeds .
Catalytic Activity: a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H(+)
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 59627
Sequence Length: 526
Subcellular Location: Membrane
EC: 3.1.1.3
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A0A1S3ZP85 | MASTKIDDKVSIPGPVTGTGNSRFLIVSHENGGIWDLVRFGVWGNKESGDKFLHYSAGGGLLEEHLVRSDDSGGGDDRGGEVPDHRWVIFVSIIVRKLIAIFGKPMEWTGYLVEFFLNLFSLNGNFLGLLYNILHGKVVMPHRGSETFISAIGHLDGRINLYKSETLTKEIGEPDFWQKIGIGHRDLMDLCMMASKLAYENEKVVRNVVNLHWKMHFVDFYNCWNDFEKEMSTQVFLLCDKPKDANLILVSFRGTEPFDADDWITDFDYSWYEIPKLGKVHMGFLEALGLGNRTNASTFHEQLFVNNLKFANLENVHATIPPSESSKSSTSFSDSDAHTGSDLSSDSERPTDTRKKKFRLEIPERTAYYVVRSKLKRLLKEHKNAKFVVTGHSLGGALAILFPAVLVLHEEVDVMERLLGIYTYGQPRVGNRQLGRFMEAHLEHPVPKYFRVVYCNDLVPRLPYDNKTFLFKHFGICQYYNSLYIEQNINEEPNPNYFGMRFLVPLYLNAGWELIRSFTMGYMYGSEYEECWESVMLRALGLFLPGISAHSPVDYVNSIRLGKARSTQMSSF | Function: Acid lipase that can hydrolyze a range of triacylglycerols without a clear preference for acyl-chains . Can also cleave 1,2-diacylglycerol, 1,3-diacylglycerol and 1-monoacylglycerol, but not phosphatidylcholine, phosphatidylethanolamine, or sterol esters . Required for pollen tube growth . Triacylglycerol hydrolysis by OBL1 may provide acyl groups for the synthesis of membrane lipids in growing pollen tubes (Probable).
Catalytic Activity: (9Z)-octadecenoate + 1,2-di-(9Z-octadecenoyl)-glycerol + H(+) = 1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 65270
Sequence Length: 572
Subcellular Location: Lipid droplet
EC: 3.1.1.-
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A1C8C3 | MACKYSTLIDSSLYDREGLCPGIDLRRHVAGELEEVGAFRAQEDWRRLVGPLPKPYAGLLGPDFSFITGAVPECHPDRMEIVAYALEFGFMHDDVIDTDVNHASLDEVGHTLDQSRTGKIEDKGSDGKRQMVTQIIREMMAIDPERAMTVAKSWASGVRHSSRRKEDTNFKALEQYIPYRALDVGYMLWHGLVTFGCAITIPNEEEEEAKRLIIPALVQASLLNDLFSFEKEKNDANVQNAVLIVMNEHGCSEEEARDILKKRIRLECANYLRNVKETNARADVSDELKRYINVMQYTLSGNAAWSTNCPRYNGPTKFNELQLLRSEHGLAKYPSRWSQENRTSGLVEGDCHESKPNELKRKRNGVSVDDEMRTNGTNGAKKPAHVSQPSTDSIVLEDMVQLARTCDLPDLSDTVILQPYRYLTSLPSKGFRDQAIDSINKWLKVPPKSVKMIKDVVKMLHSASLMLDDLEDNSPLRRGKPSTHSIYGMAQTVNSATYQYITATDITAQLQNSETFHIFVEELQQLHVGQSYDLYWTHNTLCPTIAEYLKMVDMKTGGLFRMLTRMMIAESPVVDKVPNSDMNLFSCLIGRFFQIRDDYQNLASADYAKAKGFAEDLDEGKYSFTLIHCIQTLESKPELAGEMMQLRAFLMKRRHEGKLSQEAKQEVLVTMKKTESLQYTLSVLRELHSELEKEVENLEAKFGEENFTLRVMLELLKV | Cofactor: Binds 4 Mg(2+) ions per subunit.
Function: Bifunctional sesterterpene synthase; part of the gene cluster that mediates the biosynthesis of the sesterterpenes ophiobolins, fungal phytotoxins with potential anti-cancer activities . The first step of the pathway is performed by the sesterterpene synthase oblA that possesses both prenyl transferase and terpene cyclase activity, converting isopentenyl diphosphate and dimethylallyl diphosphate into geranylfarnesyl diphosphate (GFPP) and further converting GFPP into ophiobolin F, respectively . Other sesterterpenoids (C(25) terpenoids) are found as minor products of oblA . It is expected that ophiobolin F is then oxidized to ophiobolin A via ophiobolin C and ophiobolin B intermediates by the combined action of the cytochrome P450 monooxygenase oblB and the FAD-dependent oxidoreductase oblC (Probable). Although oblB catalyzes multistep oxygenations at C5 and C21/C7 in a relatively efficient manner, it is unable to convert ophiobolin F to ophiobolin C and produces instead several unexpected derivatives .
Catalytic Activity: (2E,6E)-farnesyl diphosphate + isopentenyl diphosphate = (2E,6E,10E)-geranylgeranyl diphosphate + diphosphate
Sequence Mass (Da): 81603
Sequence Length: 718
Domain: The conserved DDXXD motifs as well as the NSE/DTE motif are important for the catalytic activity, presumably through binding to Mg(2+).
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
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A0A1V1FNM9 | MEAYFPQTTRDALAGLLPSQMSGRFPEMPAYLTQDVLLRAAGAVGAIYAIYISGLVIYRLFLSPLAKFPGPKIAAMTSYYELYYDVIHKGKYIFQIEKMHDKYGPIVRINPFELSIRDSEYYDELYVMGNIRKTDRYEAFVEGVVDFEGSHLATISHDLHRKRRKPLDPYFSRQGITRLEPMVAELTEKLVVNRLESYKGTGKVVRLDHAFTAFSGDVINRICVNRPSEVYVEDEDFAPWWFDMFHLGAVSLPLFMGMPWLIRLIRFMPASLASYLNTSMGSFSKFKLMCDEQLNEAKREKALKSKSQNSNQPTPGRLTLFRHLVDSDLPPAELSDTRLSREAQVLIGSGTMTTAGTMGFLCYYIMINPKIRARLSEELGSVMAEYPAKKPSLAELERLPYLQAVIKEGLRLSYGTMHRRARVSPSQPLLFKEWVIPPGTPVGMSAYFQHRDEKTFPRPMEFLPERWLGEITPAMYRNYIPFSKGSRHCLGMNLAYCELNFILAAMFRPGAAPFELYGTDESDVRPVHDLIVPMPRLDSLGVRVVYN | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of the sesterterpenes ophiobolins, fungal phytotoxins with potential anti-cancer activities . The first step of the pathway is performed by the sesterterpene synthase oblA that possesses both prenyl transferase and terpene cyclase activity, converting isopentenyl diphosphate and dimethylallyl diphosphate into geranylfarnesyl diphosphate (GFPP) and further converting GFPP into ophiobolin F, respectively (By similarity). Other sesterterpenoids (C(25) terpenoids) are found as minor products of oblA (By similarity). The cytochrome P450 monooxygenase oblB then catalyzes a four-step oxidative transformation of ophiobolin F to yield ophiobolin C . The function of the cytochrome P450 monooxygenase oblE has still to be determined (Probable).
Catalytic Activity: 4 O2 + ophiobolin F + 4 reduced [NADPH--hemoprotein reductase] = 4 H(+) + 6 H2O + ophiobolin C + 4 oxidized [NADPH--hemoprotein reductase]
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 62433
Sequence Length: 547
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
Subcellular Location: Membrane
EC: 1.-.-.-
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A1C8C5 | MHLSFGSLFACLLASSTAVASAPPSNFDVANFKSADIIKRDVAVIGGGSAGTYSAISLKDKGKSVILIEKKGRLGGHAETYIDPATGTPVDMGVLVFHNITVVKDYFKRFDIPLNRADDFMKSEFYFDFRTGRAVTPTFTPQAEEVSAAFAAYLAQYSKYPGLRNGTILPSPVPEELYMPFGKFVEKYGIQAAIPSMYYFNPGVGDILSNPVIEQFRYWSSDMVRSVATGFLGPVRRNVSELYTRAEAELFQSSSLLLSSEVVHALRADGESGVMLIVRTPAGRKLILAKKLLIAFPPKLDFLAPFDLSATEKSLFGKYIDAGYYVGLVKNSGLPNNTSISNAAQGHTDFTFPYLPAAYSFAPSAVPGLQLVTYATGQTTKSLPLSDEAVKADIINTIKRIQKQNPDKFTSTEPEFVTFASHAPYNLQVRAEDIRDGFYDKLYTLQGQRNTHWTGAAWKGEDSSLLWTYSEEIVVPQVIEGL | Function: FAD-dependent oxidoreductase; part of the gene cluster that mediates the biosynthesis of the sesterterpenes ophiobolins, fungal phytotoxins with potential anti-cancer activities . The first step of the pathway is performed by the sesterterpene synthase oblA that possesses both prenyl transferase and terpene cyclase activity, converting isopentenyl diphosphate and dimethylallyl diphosphate into geranylfarnesyl diphosphate (GFPP) and further converting GFPP into ophiobolin F, respectively . Other sesterterpenoids (C(25) terpenoids) are found as minor products of oblA . It is expected that ophiobolin F is then oxidized to ophiobolin A via ophiobolin C and ophiobolin B intermediates by the combined action of the cytochrome P450 monooxygenase oblB and the FAD-dependent oxidoreductase oblC (Probable). Although oblB catalyzes multistep oxygenations at C5 and C21/C7 in a relatively efficient manner, it is unable to convert ophiobolin F to ophiobolin C and produces instead several unexpected derivatives .
Sequence Mass (Da): 52840
Sequence Length: 482
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
EC: 1.21.-.-
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M2URK9 | MRSVTSLVSFSACLLASSVTAADTPLTVNGKKFYSQDIITRDVVVVGGGSSGCHIAVRLQDAGKSVVVVEKSARLGGHVATYTDPATRKTAEQGLVTFHNTTHVTDYLTRLDIPLAPISFSPSTNFDYDLRTGKPVNRTYNPTQEEFAAGFAGYSAQLAKYPQLNDGTFLPYPVPEDLTMPFGKFLEKYNLTGALMQMYNFNWGTGNFLTNPTVEQMRYWGANTVAAVTTGKFLVTARHNSSEIYTKVGNVLGATSSVLLNSEVTYTRRSEGKTGVQLIVKTPEGSKLLVAKKLVIAIPPKLDFVAPLDLSKTEKDLFGKYIDAGYYVGMVRNTGIPARTLITNSAQDTPYNLPVLPAVNIMNPTAIDGVWTVFSSSLQSKASFPWADDAVKADIIRSIKALQTANPDKFQQTEPEIIEWHSHAPYFLQVSSEEIKNGFYAKLYALQGLRNTHFTGAAWRVHDSSQIWKYTDTQVLPKLLAGL | Function: FAD-dependent oxidoreductase; part of the gene cluster that mediates the biosynthesis of the sesterterpenes ophiobolins, fungal phytotoxins with potential anti-cancer activities . The first step of the pathway is performed by the sesterterpene synthase oblA that possesses both prenyl transferase and terpene cyclase activity, converting isopentenyl diphosphate and dimethylallyl diphosphate into geranylfarnesyl diphosphate (GFPP) and further converting GFPP into ophiobolin F, respectively (By similarity). Other sesterterpenoids (C(25) terpenoids) are found as minor products of oblA (By similarity). The cytochrome P450 monooxygenase oblB then catalyzes a four-step oxidative transformation of ophiobolin F to yield ophiobolin C . The FAD-dependent oxidoreductase oblC might be involved in a later oxidation step that produces ophiobolin A (Probable).
Sequence Mass (Da): 52924
Sequence Length: 483
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
EC: 1.21.-.-
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A1E959 | MKIIILLGFLGATLSAPLIPQRLMSASNSNELLLNLNNGQLLPLQLQGPLNSWIPPFSGILQQQQQAQIPGLSQFSLSALDQFAGLLPNQIPLTGEASFAQGAQAGQVDPLQLQTPPQTQPGPSHVMPYVFSFKMPQEQGQMFQYYPVYMVLPWEQPQQTVPRSPQQTRQQQYEEQIPFYAQFGYIPQLAEPAISGGQQQLAFDPQLGTAPEIAVMSTGEEIPYLQKEAINFRHDSAGVFMPSTSPKPSTTNVFTSAVDQTITPELPEEKDKTDSLREP | Function: Tooth-associated epithelia protein that probably plays a role in odontogenesis, the complex process that results in the initiation and generation of the tooth. May be incorporated in the enamel matrix at the end of mineralization process. Involved in the induction of RHOA activity via interaction with ARHGEF and expression of downstream factors such as ROCK. Plays a role in attachment of the junctional epithelium to the tooth surface.
PTM: O-glycosylated.
Sequence Mass (Da): 30777
Sequence Length: 279
Subcellular Location: Secreted
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A1E960 | MKIIILLGLIGASSSAPLISQRLLSASNSHELLLNLNNGQLLPLQFQGAFNSWIPPFPGFLQQQQAQVSGRPQFTLSTLESFAGLFPNQIPLSRQVGLAQGGQAGQPDLSQQQTPPQTQQSASPMSYVVPVKVPQDQTQMFQYYPVYMLLPWEQPQTVTSSPQHTGQQLFEEQIPFYNQFGFAPPQAEPGVPGGQQHLAFDSFVGTAPETPGMPVEGSLLYPQKEPISFKHDNAGVFMPTTSPKPSTDNFFTSGIDPTIAPEQKVKTDSLREP | Function: Tooth-associated epithelia protein that probably plays a role in odontogenesis, the complex process that results in the initiation and generation of the tooth. May be incorporated in the enamel matrix at the end of mineralization process. Involved in the induction of RHOA activity via interaction with ARHGEF and expression of downstream factors such as ROCK. Plays a role in attachment of the junctional epithelium to the tooth surface.
PTM: O-glycosylated.
Sequence Mass (Da): 29820
Sequence Length: 273
Subcellular Location: Secreted
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Q3HS83 | MKIIILLGLIGATSSAPLITQRLLSASNSHELLLNLNNGQLLPLQFQSAFNSWIPPFPGLLQQQQQQAQVSGHPQFPLSTLESFAGLFPNQIPFSRQVGFAQGGQAGQPDFSQQQTPSQTQQASPMSYVVPVKVPQDQTQMFQYYPVYMLLPWEQPQQTVTSSPQQTGQQLYEEQIPFYNQFGFVPQQAEPGVPGGQQHLVLDSFVGTAPETPGMPAVEGPLYPQKEPIGFKQDNVGVSTPSTSPKPDTGNFFTSEINPTIAPLLPEQKVNADSLREP | Function: Tooth-associated epithelia protein that probably plays a role in odontogenesis, the complex process that results in the initiation and generation of the tooth. May be incorporated in the enamel matrix at the end of mineralization process. Involved in the induction of RHOA activity via interaction with ARHGEF and expression of downstream factors such as ROCK. Plays a role in attachment of the junctional epithelium to the tooth surface.
PTM: O-glycosylated.
Sequence Mass (Da): 30443
Sequence Length: 278
Subcellular Location: Secreted
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Q9M7Z1 | MIARRIWRSHRFLRPFSSSSVCSPPFRVPEYLSQSSSSPASRPFFVHPPTLMKWGGGSRSWFSNEAMATDSNSGLIDVPLAQTGEGIAECELLKWFVKEGDSVEEFQPLCEVQSDKATIEITSRFKGKVALISHSPGDIIKVGETLVRLAVEDSQDSLLTTDSSEIVTLGGSKQGTENLLGALSTPAVRNLAKDLGIDINVITGTGKDGRVLKEDVLRFSDQKGFVTDSVSSEHAVIGGDSVSTKASSNFEDKTVPLRGFSRAMVKTMTMATSVPHFHFVEEINCDSLVELKQFFKENNTDSTIKHTFLPTLIKSLSMALTKYPFVNSCFNAESLEIILKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQHLAANNKLNPEDVTGGTITLSNIGAIGGKFGSPLLNLPEVAIIALGRIEKVPKFSKEGTVYPASIMMVNIAADHRVLDGATVARFCCQWKEYVEKPELLMLQMR | Cofactor: Binds 1 lipoyl cofactor covalently.
Function: The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3). Within this complex, the catalytic function of this enzyme is to accept, and to transfer to coenzyme A, acyl groups that are generated by the branched-chain alpha-keto acid decarboxylase component (By similarity). Required during sugar starvation and acts under the control of a sugar-sensing mechanism involving Ser/Thr kinases and phosphatases.
Catalytic Activity: (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + 2-methylpropanoyl-CoA = (R)-N(6)-(S(8)-2-methylpropanoyldihydrolipoyl)-L-lysyl-[protein] + CoA
Sequence Mass (Da): 52706
Sequence Length: 483
Subcellular Location: Mitochondrion matrix
EC: 2.3.1.168
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P37942 | MAIEQMTMPQLGESVTEGTISKWLVAPGDKVNKYDPIAEVMTDKVNAEVPSSFTGTITELVGEEGQTLQVGEMICKIETEGANPAEQKQEQPAASEAAENPVAKSAGAADQPNKKRYSPAVLRLAGEHGIDLDQVTGTGAGGRITRKDIQRLIETGGVQEQNPEELKTAAPAPKSASKPEPKEETSYPASAAGDKEIPVTGVRKAIASNMKRSKTEIPHAWTMMEVDVTNMVAYRNSIKDSFKKTEGFNLTFFAFFVKAVAQALKEFPQMNSMWAGDKIIQKKDINISIAVATEDSLFVPVIKNADEKTIKGIAKDITGLAKKVRDGKLTADDMQGGTFTVNNTGSFGSVQSMGIINYPQAAILQVESIVKRPVVMDNGMIAVRDMVNLCLSLDHRVLDGLVCGRFLGRVKQILESIDEKTSVY | Cofactor: Binds 1 lipoyl cofactor covalently.
Function: The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3).
Catalytic Activity: (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + 2-methylpropanoyl-CoA = (R)-N(6)-(S(8)-2-methylpropanoyldihydrolipoyl)-L-lysyl-[protein] + CoA
Sequence Mass (Da): 45837
Sequence Length: 424
EC: 2.3.1.168
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P11181 | MAAALVLRTWSRAAGQLICVRYFQTCGNVHVLKPKYVCFFGYPPFKYSHPYQWLKTTAALQGQIVQFKLSDIGEGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDTAYVGKPLVDIETEALKDSEEDVVETPAVSHDEHTHQEIKGQKTLATPAVRRLAMENNIKLSEVIGSGKDGRILKEDILNYLEKQTGAILPPSPKAEIMPPPPKPKDRTIPIPISKPPVFIGKDRTEPVKGFHKAMVKTMSAALKIPHFGYCDEVDLTELVKLREELKPIAFARGIKLSFMPFFLKAASLGLLQFPILNASVDENCQNITYKASHNIGIAMDTEQGLIVPNVKNVQIRSIFEIATELNRLQKLGSAGQLSTNDLIGGTFTLSNIGSIGGTYAKPVILPPEVAIGALGTIKALPRFNEKGEVCKAQIMNVSWSADHRIIDGATVSRFSNLWKSYLENPAFMLLDLK | Cofactor: Binds 1 lipoyl cofactor covalently.
Function: The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3). Within this complex, the catalytic function of this enzyme is to accept, and to transfer to coenzyme A, acyl groups that are generated by the branched-chain alpha-keto acid decarboxylase component.
Catalytic Activity: (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + 2-methylpropanoyl-CoA = (R)-N(6)-(S(8)-2-methylpropanoyldihydrolipoyl)-L-lysyl-[protein] + CoA
Sequence Mass (Da): 53410
Sequence Length: 482
Subcellular Location: Mitochondrion matrix
EC: 2.3.1.168
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Q23571 | MMAARLLGTSSRIFKLNKHLHTSKVAFMPVVQFKLSDIGEGIAEVQVKEWYVKEGDTISQFDKVCEVQSDKAAVTISCRYDGIVKKLYHEVDGMARVGQALIDVEIEGNVEEPEQPKKEAASSSPEAPKSSAPKAPESAHSEGKVLATPAVRRIAIENKIKLAEVRGTGKDGRVLKEDVLKFLGQVPADHTSGSTNIRTTHQAPQPSSKSYEPLKEDVAVPIRGYTRAMVKTMTEALKIPHFGYNDEINVDSLVKYRAELKEFAKERHIKLSYMPFFIKAASLALLEYPSLNSTTDEKMENVIHKASHNICLAMDTPGGLVVPNIKNCEQRSIFEIAQELNRLLEAGKKQQIKREDLIDGTFSLSNIGNIGGTYASPVVFPPQVAIGAIGKIEKLPRFDKHDNVIPVNIMKVSWCADHRVVDGATMARFSNRWKFYLEHPSAMLAQLK | Cofactor: Binds 1 lipoyl cofactor covalently.
Function: The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2) (By similarity). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity). Within this complex, the catalytic function of this enzyme is to accept, and to transfer to coenzyme A, acyl groups that are generated by the branched-chain alpha-keto acid decarboxylase component (By similarity). Required for the catabolism of branched-chain amino acids and the subsequent synthesis of monomethyl branched-chain fatty acids, which are important for regulating postembryonic growth .
Catalytic Activity: (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + 2-methylpropanoyl-CoA = (R)-N(6)-(S(8)-2-methylpropanoyldihydrolipoyl)-L-lysyl-[protein] + CoA
Sequence Mass (Da): 49691
Sequence Length: 448
Subcellular Location: Mitochondrion matrix
EC: 2.3.1.168
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P11182 | MAAVRMLRTWSRNAGKLICVRYFQTCGNVHVLKPNYVCFFGYPSFKYSHPHHFLKTTAALRGQVVQFKLSDIGEGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDIETEALKDSEEDVVETPAVSHDEHTHQEIKGRKTLATPAVRRLAMENNIKLSEVVGSGKDGRILKEDILNYLEKQTGAILPPSPKVEIMPPPPKPKDMTVPILVSKPPVFTGKDKTEPIKGFQKAMVKTMSAALKIPHFGYCDEIDLTELVKLREELKPIAFARGIKLSFMPFFLKAASLGLLQFPILNASVDENCQNITYKASHNIGIAMDTEQGLIVPNVKNVQICSIFDIATELNRLQKLGSVGQLSTTDLTGGTFTLSNIGSIGGTFAKPVIMPPEVAIGALGSIKAIPRFNQKGEVYKAQIMNVSWSADHRVIDGATMSRFSNLWKSYLENPAFMLLDLK | Cofactor: Binds 1 lipoyl cofactor covalently.
Function: The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3). Within this complex, the catalytic function of this enzyme is to accept, and to transfer to coenzyme A, acyl groups that are generated by the branched-chain alpha-keto acid decarboxylase component.
Catalytic Activity: (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + 2-methylpropanoyl-CoA = (R)-N(6)-(S(8)-2-methylpropanoyldihydrolipoyl)-L-lysyl-[protein] + CoA
Sequence Mass (Da): 53487
Sequence Length: 482
Subcellular Location: Mitochondrion matrix
EC: 2.3.1.168
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Q9I1M0 | MGTHVIKMPDIGEGIAEVELVEWHVQVGDSVNEDQVLAEVMTDKATVEIPSPVAGRILALGGQPGQVMAVGGELIRLEVEGAGNLAESPAAATPAAPVAATPEKPKEAPVAAPKAAAEAPRALRDSEAPRQRRQPGERPLASPAVRQRARDLGIELQFVQGSGPAGRVLHEDLDAYLTQDGSVARSGGAAQGYAERHDEQAVPVIGLRRKIAQKMQDAKRRIPHFSYVEEIDVTDLEALRAHLNQKWGGQRGKLTLLPFLVRAMVVALRDFPQLNARYDDEAEVVTRYGAVHVGIATQSDNGLMVPVLRHAESRDLWGNASEVARLAEAARSGKAQRQELSGSTITLSSLGVLGGIVSTPVINHPEVAIVGVNRIVERPMVVGGNIVVRKMMNLSSSFDHRVVDGMDAAAFIQAVRGLLEHPATLFLE | Cofactor: Binds 1 lipoyl cofactor covalently.
Function: The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity).
Catalytic Activity: (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + 2-methylpropanoyl-CoA = (R)-N(6)-(S(8)-2-methylpropanoyldihydrolipoyl)-L-lysyl-[protein] + CoA
Sequence Mass (Da): 45774
Sequence Length: 428
EC: 2.3.1.168
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P09062 | MGTHVIKMPDIGEGIAQVELVEWFVKVGDIIAEDQVVADVMTDKATVEIPSPVSGKVLALGGQPGEVMAVGSELIRIEVEGSGNHVDVPQAKPAEVPAAPVAAKPEPQKDVKPAAYQASASHEAAPIVPRQPGDKPLASPAVRKRALDAGIELRYVHGSGPAGRILHEDLDAFMSKPQSAAGQTPNGYARRTDSEQVPVIGLRRKIAQRMQDAKRRVAHFSYVEEIDVTALEALRQQLNSKHGDSRGKLTLLPFLVRALVVALRDFPQINATYDDEAQIITRHGAVHVGIATQGDNGLMVPVLRHAEAGSLWANAGEISRLANAARNNKASREELSGSTITLTSLGALGGIVSTPVVNTPEVAIVGVNRMVERPVVIDGQIVVRKMMNLSSSFDHRVVDGMDAALFIQAVRGLLEQPACLFVE | Cofactor: Binds 1 lipoyl cofactor covalently.
Function: The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3).
Catalytic Activity: (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + 2-methylpropanoyl-CoA = (R)-N(6)-(S(8)-2-methylpropanoyldihydrolipoyl)-L-lysyl-[protein] + CoA
Sequence Mass (Da): 45129
Sequence Length: 423
EC: 2.3.1.168
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Q9LPL5 | MAIWFARSKTLVSSLRHNLNLSTILIKRDYSHRPIFYTTSQLSSTAYLSPFGSLRHESTAVETQADHLVQQIDEVDAQELDFPGGKVGYTSEMKFIPESSSRRIPCYRVLDEDGRIIPDSDFIPVSEKLAVRMYEQMATLQVMDHIFYEAQRQGRISFYLTSVGEEAINIASAAALSPDDVVLPQYREPGVLLWRGFTLEEFANQCFGNKADYGKGRQMPIHYGSNRLNYFTISSPIATQLPQAAGVGYSLKMDKKNACTVTFIGDGGTSEGDFHAGLNFAAVMEAPVVFICRNNGWAISTHISEQFRSDGIVVKGQAYGIRSIRVDGNDALAVYSAVRSAREMAVTEQRPVLIEMMTYRVGHHSTSDDSTKYRAADEIQYWKMSRNPVNRFRKWVEDNGWWSEEDESKLRSNARKQLLQAIQAAEKWEKQPLTELFNDVYDVKPKNLEEQELGLKELVKKQPQDYPPGFHV | Function: The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity). Required during sugar starvation.
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] + 3-methyl-2-oxobutanoate + H(+) = (R)-N(6)-(S(8)-2-methylpropanoyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] + CO2
Sequence Mass (Da): 53488
Sequence Length: 472
Subcellular Location: Mitochondrion matrix
EC: 1.2.4.4
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Q84JL2 | MALHLRSSFSSKSTLLNILRHNLGFGSRSHVTRHIRQILPHDPPLRGSQNPISRLCNTMAEPETLSSFVQHEYANNHQVMDFPGGKVAFTPEIQFISESDKERVPCYRVLDDNGQLITNSQFVQVSEEVAVKIYSDMVTLQIMDNIFYEAQRQGRLSFYATAIGEEAINIASAAALTPQDVIFPQYREPGVLLWRGFTLQEFANQCFGNKSDYGKGRQMPVHYGSNKLNYFTVSATIATQLPNAVGAAYSLKMDKKDACAVTYFGDGGTSEGDFHAALNIAAVMEAPVLFICRNNGWAISTPTSDQFRSDGVVVKGRAYGIRSIRVDGNDALAMYSAVHTAREMAIREQRPILIEALTYRVGHHSTSDDSTRYRSAGEIEWWNKARNPLSRFRTWIESNGWWSDKTESDLRSRIKKEMLEALRVAEKTEKPNLQNMFSDVYDVPPSNLREQELLVRQTINSHPQDYPSDVPL | Function: The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity).
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] + 3-methyl-2-oxobutanoate + H(+) = (R)-N(6)-(S(8)-2-methylpropanoyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] + CO2
Sequence Mass (Da): 53214
Sequence Length: 472
Subcellular Location: Mitochondrion matrix
EC: 1.2.4.4
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O74378 | MLRFIPSSAKARALRRSAVTAYRLNRLTCLSSLQQNRTFATQPTDDFLTGGAADYVDEMYDAWKKDPNSVHASWQAYFKNVQERGVSPSKAFQAPPLLDYADSYTALDSSLINGNNYADIDVGIYMKVQLLVRAYQSRGHHLAKLDPLGINVNHNRPSELTLEHYGFTESDLNRTIHLGPGILPNFREAGRKTMTLREIVETCEKIYCGSFAVEFTHISSRKRSNWILSHLETPTPFRYSHDQKIMIFDRLSWADSFERFLFTKFPNDKRFGLEGCEAMVPGMKALIDRSVDEGISNIVIGMAHRGRLNLLHNIVRKPAQAIFSEFRGTQDPDDEGSGDVKYHLGMNYQRPTPSGKRVSLSLVANPSHLEAEDPVVLGKVRAIQHYTSDEASHEQSMGILIHGDAAFAAQGVVYETFGLHALPGYSTGGTVHIVINNQIGFTTDPRFARSTPYCTDIAKSMEAPIFHVNGDDVEAVTFICQLAADWRKAFKTDVVVDIVCYRRHGHNETDQPSFTQPRMYKAIAKHPPTFKIYTQQLLQEKTVSKAEVDAQEKRVWDILESSFESSKNYKSDHREWLSNPWVGFASPKDLMTKILPSYPTGVNIDTLKQIGKALYTLPEGFDAHRNLKRILNNRNKSISSGEGIDMPTAEALAFGTLLEEGHHVRVSGQDVERGTFSQRHAVLHDQSSENVYIPLNHLSPNQASFVIRNSSLSEYGVLGFEYGYSLSSPNALVVWEAQFGDFANNAQCIIDQFIAAGETKWLQRTGIVLSLPHGYDGQGPEHSSARMERYLQLCNEDPREFPSEEKLQRQHQDCNIQAIYVTKPSQYFHALRRNIHRQFRKPLVIFFSKSLLRHPAARSTIDEFDEKHGFKLILEEEEHGKSILPPEKIEKLIICSGQVWVALSKAREENKIDNIAITRVEQLHPFGWKQMAANISQYPNLKEIIWCQEEPLNAGAWTYMEPRIYTILKHLGRDLPVRYAGRPPSASVAAGNKQQHLAEQEQFLNDALL | 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): 114164
Sequence Length: 1009
Subcellular Location: Mitochondrion matrix
EC: 1.2.4.2
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P81895 | AQAAPVPRPVXLSKKTDSF | 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).
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): 2024
Sequence Length: 19
Subcellular Location: Mitochondrion membrane
EC: 1.2.4.2
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P0C601 | MTNERKEVSEAPVNFGANLGLMLDLYDDFLQDPSSVPEDLQVLFSIIKNDDSIVPALKSTSSQNSDGTIKRVMRLIDNIRQYGHLKADIYPVNPPKRKHVPKLEIEDFDLDQQTLEGISAGIVSDHFADIYDNAYEAILRMEKRYKGPIAFEYTHINNNTERGWLKRRIETPYKVTLNNNEKRALFKQLAYVEGFEKYLHKNFVGAKRFSIEGVDALVPMLQRTITIAAKEGIKNIQIGMAHRGRLNVLTHVLEKPYEMMISEFMHTDPMKFLPEDGSLQLTAGWTGDVKYHLGGIKTTDSYGTMQRIALANNPSHLEIVAPVVEGRTRAAQDDTQRAGAPTTDHHKAMPIIIHGDAAYPGQGINFETMNLGNLKGYSTGGSLHIITNNRIGFTTEPIDARSTTYSTDVAKGYDVPIFHVNADDVEATIEAIDIAMEFRKEFHKDVVIDLVGYRRFGHNEMDEPSITNPVPYQNIRKHDSVEYVFGKKLVNEGVISEDEMHSFIEQVQKELRQAHDKINKADKMDNPDMEKPAELALPLQADEQSFTFDHLKEINDALLTYPDGFNILKKLNKVLEKRHEPFNKEDGLVDWAQAEQLAFATILQDGTPIRLTGQDSERGTFSHRHAVLHDEQTGETYTPLHHVPDQKATFDIHNSPLSEAAVVGFEYGYNVENKKSFNIWEAQYGDFANMSQMIFDNFLFSSRSKWGERSGLTLFLPHAYEGQGPEHSSARLERFLQLAAENNCTVVNLSSSSNYFHLLRAQAASLDSEQMRPLVVMSPKSLLRNKTVAKPIDEFTSGGFEPILTESYQADKVTKVILATGKMFIDLKEALAKNPDESVLLVAIERLYPFPEEEIEALLAQLPKLEEVSWVQEEPKNQGAWLYVYPYVKVLVADKYDLSYHGRIQRAAPAEGDGEIHKLVQNKIIENALKNN | 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): 105383
Sequence Length: 932
EC: 1.2.4.2
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G0RYE0 | MSRFLRPAFRLATTATRASTIRPTPSSLITKAAAVPTTRLLQKRSYAAEATGVKEYTVREALNEALAEELESNPKVFILGEEVAQYNGAYKVTKGLLDRFGEKRVIDTPITEMGFAGLAVGAALAGLQPVCEFMTFNFAMQAIDHIVNSAAKTLYMSGGIQPCNITFRGPNGFAAGVAAQHSQDYAAWYGSIPGLKVVSPWSAEDAKGLLKAAIRDPNPVVVLENELMYGVSFPMSEAAQKDDFVLPFGKAKIERAGKDLTIVSLSRCVGQSLVAAENLKKKYGIEAEVINLRSIKPLDVEAIVKSVKKTHRLLAVESGFPAFGVGAEILALTMEYAFDYLDTPAQRITGADVPTPYAQKLEEMSFPTEQLIEDYAAKMLRV | Function: The 10-megadalton pyruvate dehydrogenase complex contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3) and catalyzes the overall oxidative decarboxylation of pyruvate to form acetyl-CoA and CO(2) . Within the complex, pyruvate and thiamine pyrophosphate (TPP or vitamin B1) are bound by pyruvate dehydrogenase E1 subunits alpha and beta and pyruvate is decarboxylated leading to the 2-carbon hydrohyethyl bound to TPP. The E2 component contains covalently-bound lipoyl cofactors and transfers the hydroxyethyl group from TPP to an oxidized form of covalently bound lipoamide, and the resulting acetyl group is then transferred to free coenzyme A to form acetyl-CoA and reduced dihydrolipoamide-E2. Finally, the flavoprotein dihydrolipoamide dehydrogenase (E3) re-oxidizes the lipoyl group of dihydrolipoamide-E2 to form lipoamide-E2 and NADH. A fourth subunit, E3BP, is responsible for tethering E3 in proximity to the core, forming the entire metabolon (Probable).
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): 41425
Sequence Length: 382
Subcellular Location: Mitochondrion
EC: 1.2.4.1
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A2CI50 | MAVRFLFEALQKAIDEEMEREKRVVLIGEDIGHYGGSYKVTQGLYGKYGKHRVIDTPIAEYSFVGAAVGAAATGLIPVVEGMNMAFILLAYSQISNNMGMLCATSGGHFQVPMVLRGPGGIGKQLGAEHSQRLESYFQSVPGLQIVTCSTPYNAKGLLKSAIRSKNPILFIEHVLLYNLKGEVPDNDYLLPLEKAELVREGSDITVLTYSRQRYNVIQAVKVLVEEGYDPEVIDLISLKPFDMETIGKSIQKTHKVLIVEECMMTGGISNVLQSLIIDNFFDALDAAPLILSSPNVPTPYTGPLEEATVVQTIDIIESIEYGITGKPPKPRTAKK | 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): 36680
Sequence Length: 335
Subcellular Location: Plastid
EC: 1.2.4.1
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Q85FX1 | MLHKLFMYEALREAIDEEMARDKRVFVLGEDVGHYGGSYKVTKQLHTKYGDLRVLDTPIAENSFTGMAIGAAMTGLKPVVEGMNLSFLLLAFNQISNNAGMLHYTSGGNWSIPLVIRGPGGIGKQLSAEHSQRIEAYFQAVPGLKIVACSTPYNAKGLLKAAIRDNNPVLFLEHVLLYNLKQEIPKQEYVLPLDKAQVVREGSDVTIITYSRMLHHVMQAVKQLVAQGMNPEVIDLISLKPIDLETLVTSVSKTHKAIIVEECMQTGGIAAEVMAQIYSHAFDELDAPIRRLSSKDVPTPYNGYLEQACLVQPTQIVEAVKTLMST | 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): 35983
Sequence Length: 326
Subcellular Location: Plastid
EC: 1.2.4.1
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Q86HX0 | MLSSILKKIQPSLLVNFRIITRTYATKEVTVRDAINSALDEELARDEKVFIMGEEVAQYNGAYKITKGLFDKYGGDRIIDTPITEAGFAGIGVGAAMAGTRPIIEFMTFNFAMQAIDHIINSSAKTHYMSGGKVFNPIVWRGPNGPPTAVGAQHSQCFAAWYGSVPGLKVVAPWSAADHRGLLKSAIRDDNPVVYLESELLYNYKFDLSDQEQDKEYLVPIGKAKVEREGKDVTIVGFSRIVSNCMEAAEILAKEGISAEVINLRTIRPIDAETIVNSLKKTNKLVTVEEGWAQSGIGAEISALMMEHAFDYLDAPIERICGADVPMPYASNLENAAMVQTQNIVNAAKRVTQRNK | 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): 39068
Sequence Length: 356
Subcellular Location: Mitochondrion matrix
EC: 1.2.4.1
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Q7K5K3 | MLRTRLIQAASSAQRAFSTSQKALAAKQMTVRDALNSALDDELARDDRVFILGEEVAQYDGAYKVSRGLWKKYGDKRVIDTPITEMGFAGIAVGAAMAGLRPVCEFMTWNFSMQAIDHIINSAAKTFYMSAGAVNVPIVFRGPNGAASGVAAQHSQCFAAWYAHCPGLKVLSPYDAEDARGLLKSAIRDPDPVVFLENELVYGTAFPVADNVADKDFLVPIGKAKVMRPGKDITLVAHSKAVETSLLAAAELAKKGIEAEVINLRSIRPLDTATIFASVRKTHHLVTVENGWPQHGVGAEICARIMEDQTFFELDAPVWRCAGVDVPMPYAKTLEAHALPRVQDLVEATLKVLGGKVGKAAAANK | Function: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2) (By similarity). Might play a role in regulating synapse structure formation at neuromuscular junctions . Might play a role in maintenance of mitochondrial morphology .
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): 39351
Sequence Length: 365
Subcellular Location: Mitochondrion matrix
EC: 1.2.4.1
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P11177 | MAAVSGLVRRPLREVSGLLKRRFHWTAPAALQVTVRDAINQGMDEELERDEKVFLLGEEVAQYDGAYKVSRGLWKKYGDKRIIDTPISEMGFAGIAVGAAMAGLRPICEFMTFNFSMQAIDQVINSAAKTYYMSGGLQPVPIVFRGPNGASAGVAAQHSQCFAAWYGHCPGLKVVSPWNSEDAKGLIKSAIRDNNPVVVLENELMYGVPFEFPPEAQSKDFLIPIGKAKIERQGTHITVVSHSRPVGHCLEAAAVLSKEGVECEVINMRTIRPMDMETIEASVMKTNHLVTVEGGWPQFGVGAEICARIMEGPAFNFLDAPAVRVTGADVPMPYAKILEDNSIPQVKDIIFAIKKTLNI | 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): 39233
Sequence Length: 359
Subcellular Location: Mitochondrion matrix
EC: 1.2.4.1
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Q6ABX8 | MERAPALAEPEPRVQSLPMVKALNAGLRQALVADPKVLILGEDVGPLGGVFRVTEGLQSEFGASRVVDTPLAEAGIVGTAIGLAMRGYRPVVEIQFNGFVFPGFDQITTQLAKMANRHSGAVSMPVVIRIPHGGHIGAVEHHQEAPEAYFAHTAGLRIVAPSTPHDAYWMIQEAIASDDPVIFFEPMSRYWPKGEVDTLENPLPLHASRIVRSGTDATIVAWAGMVPVALRAAEIAAEEGRSLEVVDLRSLAPIDYAPVLRSVQKTGRLVVAQEAPGIVSVGSEVAAVVGEKAFYSLEAPVLRVAGFDTPFPPAKLESLYLPDADRILEVVDRSLAY | 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): 36087
Sequence Length: 337
EC: 1.2.4.1
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P86222 | EAINQGMDEELERDEKVFLLGEEVAQYDGAYKVSRTYYMSAGLQPVPIVFRGPNGASAGVAAQHSQCFAAWYGHCPGLKVVSPWNSEDAKGLIKSAIRDDNPVVMLENELMYGVAFELPTEAQSKDFLIPIGKEGIECEVINLRTIRPMDIEAIEASVMKTNHLVTVEGGWPQFGVGAEICARIMEGPAFNFLDAPAVRVTGADVPMPYAK | 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): 23010
Sequence Length: 211
Subcellular Location: Mitochondrion matrix
EC: 1.2.4.1
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P75391 | MSKTIQANNIEALGNAMDLALERDPNVVLYGQDAGFEGGVFRATKGLQKKYGEERVWDCPIAEAAMAGIGVGAAIGGLKPIVEIQFSGFSFPAMFQIFTHAARIRNRSRGVYTCPIIVRMPMGGGIKALEHHSETLEAIYGQIAGLKTVMPSNPYDTKGLFLAAVESPDPVVFFEPKKLYRAFRQEIPADYYTVPIGQANLISQGNNLTIVSYGPTMFDLINMVYGGELKDKGIELIDLRTISPWDKETVFNSVKKTGRLLVVTEAAKTFTTSGEIIASVTEELFSYLKAAPQRVTGWDIVVPLARGEHYQFNLNARILEAVNQLLK | 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): 35914
Sequence Length: 327
EC: 1.2.4.1
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P52904 | MLGVIRNKTIRPSFSAFRFFSSAKQMTVRDALNSALDVEMSADSKVFLMGEEVGEYQGAYKVTKGLLEKYGPERVLDTPITEAGFTGIGVGAAYYGLKPVVEFMTFNFSMQAIDHIINSAAKSNYMSAGQISVPIVFRGLNGDAAGVGAQHSHCYASWYGSCPGLKVLVPHSAEDARGLLKAAIRDPDPVVFLENELLYGESFPVSAEVLDSSFWLPIGKAKIEREGKDVTITAFSKMVGFALKAAEILEKEGISAEVINLRSIRPLDRPTINASVRKTNRLVTVEEGFPQHGVGAEICTSVIEESFGYLDATVERIGGADVPMPYAGNLERLVVPHVEDIVRAAKRACHRSVPLAAAA | 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): 38793
Sequence Length: 359
Subcellular Location: Mitochondrion matrix
EC: 1.2.4.1
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Q9D136 | MAPQRRGPPRIPEGSSAAERRRATSTKKDRLPREAQRTWLRIVAFGVGLALVTCLLWSSVGIDDDVAEVVARRGEVLEGRFIEVPCSEDYDGHRRFEGCTPRKCGRGVTDIVITREEAEQIRRIAEKGLSLGGSDGGASILDLHSGALSVGKHFVNLYRYFGDKIQNIFSEEDFQLYRDIRQKVQLTIAEAFGISASLLYLTKPTFFSRINSTEARTAHDEYWHAHVDKVTYGSFDYTSLLYLSDYLEDFGGGRFVFMEEGSNKTVEPRAGRVSFFTSGSENLHRVEKVLWGTRYAITIAFTCNPDHGIEDPVLT | Cofactor: Binds 1 Fe(2+) ion per subunit.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 35385
Sequence Length: 315
Subcellular Location: Membrane
EC: 1.14.11.-
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Q9FNY7 | MKRPRPTSQPSISSTVKPPLSPPVTPILKQKLHRTGTPKWFPLKLTHTELTLPLTFPTGQTFRWKKTGAIQYSGTIGPHLVSLRQRPGDDAVSYCVHCSTSPKSAELALLDFLNAEISLAELWSDFSKKDPRFGELARHLRGARVLRQDPLECLIQFLCSSNNNIARITKMVDFVSSLGLHLGDIDGFEFHQFPSLDRLSRVSEEEFRKAGFGYRAKYITGTVNALQAKPGGGNEWLLSLRKVELQEAVAALCTLPGVGPKVAACIALFSLDQHSAIPVDTHVWQIATNYLLPDLAGAKLTPKLHGRVAEAFVSKYGEYAGWAQTLLFIAELPAQKTLLQSFSQPINKLDESAEVNETSCDTLKP | Function: Involved in repair of DNA damaged by oxidation by incising DNA at 8-oxoG residues. Excises 7,8-dihydro-8-oxoguanine and 2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine (Fapy) from damaged DNA. Has a beta-lyase activity that nicks DNA 3' to the lesion.
Catalytic Activity: 2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-monophospho-2'-deoxyribonucleoside-DNA + H(+)
Sequence Mass (Da): 40283
Sequence Length: 365
Subcellular Location: Nucleus
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Q9V3I8 | MLAHNLGFHKKRLFSNMKAVLQDRGVIGLSLEECDLERTLLGGQSFRWRSICDGNRTKYGGVVFNTYWVLQQEESFITYEAYGTSSPLATKDYSSLISDYLRVDFDLKVNQKDWLSKDDNFVKFLSKPVRLLSQEPFENIFSFLCSQNNNIKRISSMIEWFCATFGTKIGHFNGADAYTFPTINRFHDIPCEDLNAQLRAAKFGYRAKFIAQTLQEIQKKGGQNWFISLKSMPFEKAREELTLLPGIGYKVADCICLMSMGHLESVPVDIHIYRIAQNYYLPHLTGQKNVTKKIYEEVSKHFQKLHGKYAGWAQAILFSADLSQFQNTSTVACKKKSNKKPKK | Function: DNA repair enzyme that incises DNA at 8-oxoG residues. Excises 7,8-dihydro-8-oxoguanine and 2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine (FAPY) from damaged DNA. Has a beta-lyase activity that nicks DNA 3' to the lesion. Efficiently incises DNA duplexes containing 8-hydroxyguanine (8-OH-Gua), 8-hydroxyadenine (8-OH-Ade) and abasic (AP) sites placed opposite to a cytosine.
Catalytic Activity: 2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-monophospho-2'-deoxyribonucleoside-DNA + H(+)
Sequence Mass (Da): 39406
Sequence Length: 343
Subcellular Location: Nucleus
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O15527 | MPARALLPRRMGHRTLASTPALWASIPCPRSELRLDLVLPSGQSFRWREQSPAHWSGVLADQVWTLTQTEEQLHCTVYRGDKSQASRPTPDELEAVRKYFQLDVTLAQLYHHWGSVDSHFQEVAQKFQGVRLLRQDPIECLFSFICSSNNNIARITGMVERLCQAFGPRLIQLDDVTYHGFPSLQALAGPEVEAHLRKLGLGYRARYVSASARAILEEQGGLAWLQQLRESSYEEAHKALCILPGVGTKVADCICLMALDKPQAVPVDVHMWHIAQRDYSWHPTTSQAKGPSPQTNKELGNFFRSLWGPYAGWAQAVLFSADLRQSRHAQEPPAKRRKGSKGPEG | Function: DNA repair enzyme that incises DNA at 8-oxoG residues. Excises 7,8-dihydro-8-oxoguanine and 2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine (FAPY) from damaged DNA. Has a beta-lyase activity that nicks DNA 3' to the lesion.
Catalytic Activity: 2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-monophospho-2'-deoxyribonucleoside-DNA + H(+)
Sequence Mass (Da): 38782
Sequence Length: 345
Subcellular Location: Nucleus
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Q58134 | MMLIKKIEELKNSEIKDIIDKRIQEFKSFKNKSNEEWFKELCFCILTANFTAEGGIRIQKEIGDGFLTLPREELEEKLKNLGHRFYRKRAEYIVLARRFKNIKDIVESFENEKVAREFLVRNIKGIGYKEASHFLRNVGYDDVAIIDRHILRELYENNYIDEIPKTLSRRKYLEIENILRDIGEEVNLKLSELDLYIWYLRTGKVLK | Function: Catalyzes the excision of an oxidatively damaged form of guanine (7,8-dihydro-8-oxoguanine = 8-oxoG) from DNA . Also cleaves the DNA backbone at apurinic/apyrimidinic sites (AP sites) . Has little specificity for the base opposite oxoG .
Catalytic Activity: 2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-monophospho-2'-deoxyribonucleoside-DNA + H(+)
Sequence Mass (Da): 24827
Sequence Length: 207
Domain: Contains two domains separated by the central HhH motif. The C-terminal domain undergoes a conformational change upon DNA binding.
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P23272 | MTRRNQTAISQFFLLGLPFPPEYQHLFYALFLAMYLTTLLGNLIIIILILLDSHLHTPMYLFLSNLSFADLCFSSVTMPKLLQNMQSQVPSIPYAGCLAQIYFFLFFGDLGNFLLVAMAYDRYVAICFPLHYMSIMSPKLCVSLVVLSWVLTTFHAMLHTLLMARLSFCEDSVIPHYFCDMSTLLKVACSDTHDNELAIFILGGPIVVLPFLLIIVSYARIVSSIFKVPSSQSIHKAFSTCGSHLSVVSLFYGTVIGLYLCPSANNSTVKETVMSLMYTMVTPMLNPFIYSLRNRDIKDALEKIMCKKQIPSFL | Function: Odorant receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35455
Sequence Length: 314
Subcellular Location: Cell membrane
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Q6UX06 | MRPGLSFLLALLFFLGQAAGDLGDVGPPIPSPGFSSFPGVDSSSSFSSSSRSGSSSSRSLGSGGSVSQLFSNFTGSVDDRGTCQCSVSLPDTTFPVDRVERLEFTAHVLSQKFEKELSKVREYVQLISVYEKKLLNLTVRIDIMEKDTISYTELDFELIKVEVKEMEKLVIQLKESFGGSSEIVDQLEVEIRNMTLLVEKLETLDKNNVLAIRREIVALKTKLKECEASKDQNTPVVHPPPTPGSCGHGGVVNISKPSVVQLNWRGFSYLYGAWGRDYSPQHPNKGLYWVAPLNTDGRLLEYYRLYNTLDDLLLYINARELRITYGQGSGTAVYNNNMYVNMYNTGNIARVNLTTNTIAVTQTLPNAAYNNRFSYANVAWQDIDFAVDENGLWVIYSTEASTGNMVISKLNDTTLQVLNTWYTKQYKPSASNAFMVCGVLYATRTMNTRTEEIFYYYDTNTGKEGKLDIVMHKMQEKVQSINYNPFDQKLYVYNDGYLLNYDLSVLQKPQ | Function: May promote proliferation of pancreatic cancer cells by favoring the transition from the S to G2/M phase. In myeloid leukemic cell lines, inhibits cell growth and induces cell differentiation and apoptosis. May play a role in the inhibition of EIF4EBP1 phosphorylation/deactivation. Facilitates cell adhesion, most probably through interaction with cell surface lectins and cadherin.
PTM: N-glycosylated.
Sequence Mass (Da): 57280
Sequence Length: 510
Domain: The olfactomedin-like domain is involved in the interaction with cadherin.
Subcellular Location: Secreted
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Q07081 | MYICLLTLVLIHAAAAFVAQNATGILAGKDHCVCEVLLPDSSFPAKRVGALEDETIRLSNRVEDEMQKLEEQDIILDTYSEKIINLTRRVEYLEKLHPESLVEISFEVLKREIRELEMYISAMRVKPNGNSVQVETLYNEVKNMSKTVGQLETLDKNNVLQAKREIVNLKKRLVDCEKNLKAKPSLMVPLGSCQHQGLAHISKPNLMQLNWKGNAYKSGAWGKDAAWNTTKKSLYWVAPLNTDGRVLESIRIYPSMSDLQMYKNPIDLPLSMLIKNKLNNTFAGQGAGVVVHNNNLYYNCFNSHDMCRASLTSGVYQKKPLLNALFNNRFSYAGTMFQDMDFSSDEKGLWVIFTTEKSAGKIVVGKVNVATFTVDNIWITTQNKSDASNAFMICGVLYVTRSLGPKMEEVFYMFDTKTGKEGHLSIMMEKMAEKVHSLSYNSNDRKLYMFSEGYLLHYDIALKP | Function: May influence the maintenance, growth, or differentiation of chemosensory cilia on the apical dendrites of olfactory neurons. Major component of the extracellular matrix of the olfactory neuroepithelium.
PTM: Most, if not all, of the six potential sites for N-glycosylation carry carbohydrate moieties of 8-10 sugar residues.
Sequence Mass (Da): 52572
Sequence Length: 464
Subcellular Location: Secreted
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C7DLJ6 | MNPITSKFDKVLNASSEYGHVNHEPDSSKEQQRNTPQKSMPFSDQIGNYQRNKGIPVQSYDNSKIYIIGSGIAGMSAAYYFIRDGHVPAKNITFLEQLHIDGGSLDGAGNPTDGYIIRGGREMDMTYENLWDMFQDIPALEMPAPYSVLDEYRLINDNDSNYSKARLINNKGEIKDFSKFGLNKMDQLAIIRLLLKNKEELDDLTIEDYFSESFLKSNFWTFWRTMFAFENWHSLLELKLYMHRFLHAIDGLNDLSSLVFPKYNQYDTFVTPLRKFLQEKGVNIHLNTLVKDLDIHINTEGKVVEGIITEQDGKEVKIPVGKNDYVIVTTGSMTEDTFYGNNKTAPIIGIDNSTSGQSAGWKLWKNLAAKSEIFGKPEKFCSNIEKSAWESATLTCKPSALIDKLKEYSVNDPYSGKTVTGGIITITDSNWLMSFTCNRQPHFPEQPDDVLVLWVYALFMDKEGNYIKKTMLECTGDEILAELCYHLGIEDQLENVQKNTIVRTAFMPYITSMFMPRAKGDRPRVVPEGCKNLGLVGQFVETNNDVVFTMESSVRTARIAVYKLLNLNKQVPDINPLQYDIRHLLKAAKTLNDDKPFVGEGLLRKVLKGTYFEHVLPAGAAEEEEHESFIAEHVNKFREWVKGIRG | Cofactor: Binds 1 FAD per subunit. FAD does not seem to be involved in catalysis but rather in the structural stabilization of the enzyme.
Function: Catalyzes the hydration of oleate at its cis-9-double bond to yield 10-hydroxyoctadecanoate. The hydration of unsaturated fatty acids is suggested to be a detoxification mechanism and a survival strategy for living in fatty acid-rich environments.
Catalytic Activity: (R)-10-hydroxyoctadecanoate = (9Z)-octadecenoate + H2O
Sequence Mass (Da): 73488
Sequence Length: 646
Pathway: Lipid metabolism; fatty acid metabolism.
EC: 4.2.1.53
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B9E972 | MYYSNGNYEAFARPKKPEGVDNKSAYLVGSGLASLAAASFLIRDGQMKGENIHILEELDLPGGSLDGILNPERGYIMRGGREMENHFECLWDLFRSVPSLEVEDASVLDEFYWLNKEDPNYSKCRVIENRGQRLESDGKMTLTKKANKEIIQLCLMKEEQLNDVKISDVFSKDFLDSNFWIYWKTMFAFEPWHSAMEMRRYLMRFIHHIGGLADFSALKFTKFNQFESLVMPLIEHLKAKNVTFEYGVTVKNIQVECSKESKVAKAIDIVRRGNEESIPLTENDLVFVTNGSITESTTYGDNDTPAPPTSKPGGAWQLWENLSTQCEEFGNPAKFYKDLPEKSWFVSATATTNNKEVIDYIQKICKRDPLSGRTVTGGIVTVDDSNWQLSFTLNRQQQFKNQPDDQVSVWIYALYSDERGERTNKTIVECSGKEICEEWLYHMGVPEEKISALAAECNTIPSYMPYITAYFMPRKEGDRPLVVPHGSKNIAFIGNFAETERDTVFTTEYSVRTAMEAVYKLLEVDRGVPEVFASVYDVRILLHALSVLNDGKKLDEIDMPFYERLVEKRLLKKASGTFIEELLEEANLI | Cofactor: Binds 1 FAD per subunit. FAD does not seem to be involved in catalysis but rather in the structural stabilization of the enzyme.
Function: Catalyzes the hydration of oleate at its cis-9-double bond to yield 10-hydroxyoctadecanoate. Cannot catalyze the reverse reaction. Is not active with saturated fatty acids and trans-, cis-5-, cis-6-, cis-8-, cis-11-, cis-13-, cis-14-, and cis-15-double bond unsaturated fatty acids as substrate; is only active on cis-9- and/or cis-12-double bond of unsaturated fatty acids without any trans-configurations, producing 10-hydroxy and 10,13-dihydroxy fatty acids. The hydration of unsaturated fatty acids is suggested to be a detoxification mechanism and a survival strategy for living in fatty acid-rich environments.
Catalytic Activity: (R)-10-hydroxyoctadecanoate = (9Z)-octadecenoate + H2O
Sequence Mass (Da): 67309
Sequence Length: 589
Pathway: Lipid metabolism; fatty acid metabolism.
EC: 4.2.1.53
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B5XK69 | MYYTSGNYEAFATPRKPEGVDQKSAYIVGTGLAGLAAAVFLIRDGHMAGERIHLFEELPLAGGSLDGIEKPHLGFVTRGGREMENHFECMWDMYRSIPSLEIPGASYLDEFYWLDKDDPNSSNCRLIHKRGNRVDDDGQYTLGKQSKELIHLIMKTEESLGDQTIEEFFSEDFFKSNFWVYWATMFAFEKWHSAVEMRRYAMRFIHHIDGLPDFTSLKFNKYNQYDSMVKPIIAYLESHDVDIQFDTKVTDIQVEQTAGKKVAKTIHMTVSGEAKAIELTPDDLVFVTNGSITESSTYGSHHEVAKPTKALGGSWNLWENLAAQSDDFGHPKVFYQDLPAESWFVSATATIKHPAIEPYIERLTHRDLHDGKVNTGGIITITDSNWMMSFAIHRQPHFKEQKENETTVWIYGLYSNSEGNYVHKKIEECTGQEITEEWLYHLGVPVDKIKDLASQEYINTVPVYMPYITSYFMPRVKGDRPKVIPDGSVNLAFIGNFAESPSRDTVFTTEYSIRTAMEAVYSFLNGERGIPQGFNSAYDIRELLKAFYYLNDKKAIKDMDLPIPALIEKIGHKKIKDTFIEELLKDANLM | Cofactor: Binds 1 FAD per subunit. FAD does not seem to be involved in catalysis but rather in the structural stabilization of the enzyme.
Function: Catalyzes the hydration of oleate at its cis-9-double bond to yield 10-hydroxyoctadecanoate, and of linoleate at its cis-9- and cis-12-double bond to yield 10-hydroxy-12-octadecenoate and 10,13-dihydroxyoctadecanoate. Is not active on trans-double bonds and esterified fatty acids as substrate; is only active on cis-9- and/or cis-12-double bond of C16 and C18 fatty acids without any trans-configurations, producing 10-hydroxy and 10,13-dihydroxy derivatives. Appears to play a role in oleic acid detoxification and bacterial virulence.
Catalytic Activity: (R)-10-hydroxyoctadecanoate = (9Z)-octadecenoate + H2O
Sequence Mass (Da): 67408
Sequence Length: 590
Pathway: Lipid metabolism; fatty acid metabolism.
EC: 4.2.1.53
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I6WU39 | MAVKHLIVLKFKDEITEAQKEEFFKTYVNLVNIIPAMKDVYWGKDVTQKNKEEGYTHIVEVTFESVETIQDYIIHPAHVGFGDVYRSFWEKLLIFDYTPRK | Function: Involved in the biosynthesis of cannabinoids-related terpenophenolic natural products, which have pharmacological activity . Polyketide cyclase which functions in concert with OLS/TKS to form olivetolic acid . Has no intrinsic polyketide synthase activity and requires the presence of OLS to produce olivetolic acid .
Catalytic Activity: 3,5,7-trioxododecanoyl-CoA = CoA + H(+) + olivetolate
Sequence Mass (Da): 12002
Sequence Length: 101
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
Subcellular Location: Cytoplasm
EC: 4.4.1.26
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P0DH58 | MRKKLTALVLSALPLAAVADVSLYGEIKAGVEGRNYQLQLTEAQAANGGASGQVKVTKVTKAKSRIRTKISDFGSFIGFKGSEDLGDGLKAVWQLEQDVSVAGGGATQWGNRESFIGLAGEFGTLRAGRVANQFDDASQAIDPWDSNNDVASQLGIFKRHDDMPVSVRYDSPEFSGFSGSVQFVPIQNSKSAYTPAYYTKNTNNNLTLVPAVVGKPGSDVYYAGLNYKNGGFAGNYAFKYARHANVGRNAFELFLIGSGSDQAKGTDPLKNHQVHRLTGGYEEGGLNLALAAQLDLSENGDKTKNSTTEIAATASYRFGNAVPRISYAHGFDFIERGKKGENTSYDQIIAGVDYDFSKRTSAIVSGAWLKRNTGIGNYTQINAASVGLRHKF | Function: Serves as a slightly cation selective porin. Major antigen on the gonococcal cell surface and it may have pathogenic properties in addition to its porin activity.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 42078
Sequence Length: 392
Subcellular Location: Cell outer membrane
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P0DJO6 | LTAKLSYPIYDDLDIYTRLGGMVWRADAKNNVGGGDRSNHDTGVSPVFAGGVEYAWTPSIATRLEYQWINNIGDAGTVGTRPDNGMLSVGVSYRFGQDEAAPVVAPAPAPAPQVQTKHFTLKSDVLFNFNKSTLKPEGQQALDQLYTQLSNLDPKDGAVVVLGYTDRIGSDAYNQRLSQQRAQSVVDYLVSKGIPAGKITAQGQGESNPVTGSTCDNVKQRAALIDCLAPDRRVEIEVKGV | Function: With TolR probably plays a role in maintaining the position of the peptidoglycan cell wall in the periplasm. Acts as a porin with low permeability that allows slow penetration of small solutes; an internal gate slows down solute passage.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 25917
Sequence Length: 241
Domain: The extracellular loops are most variable in sequence, and in some bacteria confer sensitivity to phage and/or colicins.
Subcellular Location: Cell outer membrane
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A0A2S4N3N0 | MKKTAIAIAVALAGFATVAQAAPKDNTWYTGAKLGWSQYHDTGFIPNNGPTHENQLGAGAFGGYQVNPYVGFEMGYDWLGRMPYKGDNINGAYKAQGVQLTAKLGYPITDDLDIYTRLGGMVWRADTKANVPGGASFKDHDTGVSPVFAGGVEYAITPEIATRLEYQWTNNIGDANTIGTRPDNGLLSLGVSYRFGQGEAAPVVAPAPAPEVQTKHFTLKSDVLFNFNKATLKPEGQAALDQLYSQLSNLDPKDGSVVVLGYTDRIGSDAYNQGLSERRAQSVVDYLISKGIPADKISARGMGESNPVTGNTCDNVKQRAALIDCLAPDRRVEIEVKGIKDVVTQPQA | Function: With TolR probably plays a role in maintaining the position of the peptidoglycan cell wall in the periplasm. Acts as a porin with low permeability that allows slow penetration of small solutes; an internal gate slows down solute passage.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 37283
Sequence Length: 348
Domain: The extracellular loops are most variable in sequence, and in some bacteria confer sensitivity to phage and/or colicins.
Subcellular Location: Extracellular vesicle
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P18195 | MKKSLIALTLAALPVAATADVTLYGAIKAGVQTYRSVEHTDGKVSKVETGSEIADFGSKIGFKGQEDLGNGLKAVWQLEQGASVAGTNTGWGNKQSFVGLKGGFGTIRAGSLNSPLKNTDANVNAWESGKFTGNVLEISGMAKREHRYLSVRYDSPEFAGFSGSVQYAPKDNSGSNGESYHVGLNYQNSGFFAQYAGLFQRYGEGTKKIEYEHQVYSIPSLFVEKLQVHRLVGGYDNNALYVSVAAQQQDAKLYGARRANSHNSQTEVAATAAYRFGNVTPRVSYAHGFKGTVDSADHDNTYDQVVVGAEYDFSKRTSALVSAGWLQEGKGADKIVSTASAVVLRHKF | Function: Serves as a slightly cation selective porin. Major antigen on the gonococcal cell surface and it may have pathogenic properties in addition to its porin activity.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 37417
Sequence Length: 348
Subcellular Location: Cell outer membrane
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P30690 | MKKSLIALTLAALPVAAMADVTLYGTIKAGVETSRSVFHQNGQVTEVTTATGIVDLGSKIGFKGQEDLGNGLKAIWQVEQKASIAGTDSGWGNRQSFIGLKGGFGKLRVGRLNSVLKDTGDINPWDSKSDYLGVNKIAEPEARLISVRYDSPEFAGLSGSVQYALNDNAGRHNSESYHAGFNYKNGGFFVQYGGAYKRHHQVQEGLNIEKYQIHRLVSGYDNDALYASVAVQQQDAKLTDASNSHNSQTEVAATLAYRFGNVTPRVSYAHGFKGLVDDADIGNEYDQVVVGAEYDFSKRTSALVSAGWLQEGKGENKFVATAGGVGLRHKF | Function: Serves as a slightly cation selective porin.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35682
Sequence Length: 331
Subcellular Location: Cell outer membrane
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Q94AM1 | MLMATPTSRASLNLLRRSPKPKYFSSSSCHFRPSTFRKSYPCPIWSSSFSFCLPPPRSTTSTSLSSSSFRPFSSPPSMSSAAAAAVESVVSDETLSSNPLLQDFDFPPFDSVDASHVRPGIRALLQHLEAELEELEKSVEPTWPKLVEPLEKIVDRLTVVWGMINHLKAVKDTPELRAAIEDVQPEKVKFQLRLGQSKPIYNAFKAIRESPDWSSLSEARQRLVEAQIKEAVLIGIALDDEKREEFNKIEQELEKLSHKFSENVLDATKKFEKLITDKKEIEGLPPSALGLFAQAAVSKGHENATAENGPWIITLDAPSYLPVMQHAKNRALREEVYRAYLSRASSGDLDNTAIIDQILKLRLEKAKLLGYNNYAEVSMAMKMATVEKAAELLEKLRSASWDAAVQDMEDLKSFAKNQGAAESDSMTHWDTTFWSERLRESKYDINEEELRPYFSLPKVMDGLFSLAKTLFGIDIEPADGLAPVWNNDVRFYRVKDSSGNPIAYFYFDPYSRPSEKRGGAWMDEVVSRSRVMAQKGSSVRLPVAHMVCNQTPPVGDKPSLMTFREVETVFHEFGHALQHMLTKQDEGLVAGIRNIEWDAVELPSQFMENWCYHRDTLMSIAKHYETGETLPEEVYKKLLAARTFRAGSFSLRQLKFASVDLELHTKYVPGGPESIYDVDQRVSVKTQVIPPLPEDRFLCSFSHIFAGGYAAGYYSYKWAEVLSADAFSAFEDAGLDDIKAVKETGQRFRNTILALGGGKAPLKVFVEFRGREPSPEPLLRHNGLLAASASA | Cofactor: Binds 1 zinc ion.
Function: Oligopeptidase degrading short peptides from 8 to 23 amino acid residues. Plays a role in the degradation of transit peptides and of peptides derived from other proteolytic events. Does not exhibit a strict cleavage pattern. Binds salicylic acid.
Catalytic Activity: Hydrolysis of oligopeptides, with broad specificity. Gly or Ala commonly occur as P1 or P1' residues, but more distant residues are also important, as is shown by the fact that Z-Gly-Pro-Gly-|-Gly-Pro-Ala is cleaved, but not Z-(Gly)(5).
Sequence Mass (Da): 88757
Sequence Length: 791
Subcellular Location: Mitochondrion matrix
EC: 3.4.24.70
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Q2RI41 | MGKVRNISGCVAVAHGVRLADVDVICSYPIRPYTGIMSELARMVADGELDAEFVHGEGEHAQLSVVYGASAAGARVFTGSSGVGVTYAMEVYSPISGERLPVQMAIADRTLDPPGDFGEEHTDAECCRDQGWIQGWASTPQEALDNTLIYYRVGEDQRVLLPQYACLDGYFVSHILGPVDIPDEAQVKEFLPPYKNHHVLDPRKPQIIGPQIEPAMGPPLQYQRYQAVKGVHKVLEEACDEFARIFGRKYDPYLDEYLTDDAEVIIFGQGAHMETAKAVARRLRNLGEKVGVARLRTFRPFPTEQIKERLSKFKAIGVLDVSANFGISCSGGVLLSELRAALYDYGDKVKTVGFVAGLGGEVVTHDEFYRMFQKLKEIAKTGKVEQTSYWIPFEL | Function: Catalyzes the anaerobic oxidation of oxalate using a broad range of electron acceptors, including ferredoxin and the nickel-dependent carbon monoxide dehydrogenase. Does not require coenzyme A as cosubstrate. Enables anaerobic growth on oxalate which is used as energy source by the bacteria.
Catalytic Activity: oxalate + oxidized 2[4Fe-4S]-[ferredoxin] = 2 CO2 + reduced 2[4Fe-4S]-[ferredoxin]
Sequence Mass (Da): 43687
Sequence Length: 395
EC: 1.2.7.10
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Q2RI42 | MLDRIASIKKAPDEEYYVPGHRTCAGCGPALTYRLVAKAAGPNTIFIGPTGCMYVANTSYGCGPWRVPWIHAQITNGGAVASGIEAAYKAMIRKKKTDAEFPNIIVMAGDGGAVDIGLQALSAMLYRGHDVLFICYDNESYANTGIQTSPTTPYGANTTFTPPGEVVPEGKKLFPKDNPKVIAHGHPELKYVATASIGWPVDLMNKVRKGLNQEGPAYIHIHAPCPKGWQFPADKTIEMAKLAVQTGMFQLYEYENGEYKLSVKVDKRKPVSEYMKLQKRFAHLKPEHIAKMQAFVDARCAEVGITVPVVASNA | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the anaerobic oxidation of oxalate using a broad range of electron acceptors, including ferredoxin and the nickel-dependent carbon monoxide dehydrogenase. Does not require coenzyme A as cosubstrate. Enables anaerobic growth on oxalate which is used as energy source by the bacteria.
Catalytic Activity: oxalate + oxidized 2[4Fe-4S]-[ferredoxin] = 2 CO2 + reduced 2[4Fe-4S]-[ferredoxin]
Sequence Mass (Da): 34234
Sequence Length: 314
EC: 1.2.7.10
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Q2RI40 | MSTKDLFAEPNLKQITVWARGVVMNKDARDIVVALTEAAAKEGKYVQAWENYVDLPDRIYVPVRAYARISSDPIESKYIYENETPDIVVLVEESLIKGVPILKGIRPGSTLVVNTKRSIDTILEFLGDTGNLAQIVTVDANSMAEAVMTLSGAEGATDATGIGAGIAAPIAGAVVKATGIVDVENLAAVVKNPAAMRRGYAEAQVRQLPPHEAVEEAAVSATELLRQMPFAGTVPSPVTENEGMVTGNWRIQRPIIDREACTECYTCWIYCPDSCITRTEEGPVFNMKYCKGCGLCTAVCPSGALTNVPELDFKD | Cofactor: Binds 2 [4Fe-4S] clusters per subunit.
Function: Catalyzes the anaerobic oxidation of oxalate using a broad range of electron acceptors, including ferredoxin and the nickel-dependent carbon monoxide dehydrogenase. Does not require coenzyme A as cosubstrate. Enables anaerobic growth on oxalate which is used as energy source by the bacteria.
Catalytic Activity: oxalate + oxidized 2[4Fe-4S]-[ferredoxin] = 2 CO2 + reduced 2[4Fe-4S]-[ferredoxin]
Sequence Mass (Da): 33931
Sequence Length: 315
EC: 1.2.7.10
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Q59160 | MTLREVSVATDLSDFYDLLVIGAGPAGMAAAVEASASGARVAVLDENPRPGGQIYREITRNSPDRRTYLGPDYWKGQPLAEAFCLSNVDYASRATVWSLETRDKTAGQARNVVGVTVAGSARMVETNAVVLATGAQERPMPVPGWTLPGVMTAGAAQIALKAAGAMPAGPVVLIGCGPLLYLLASQLVDAGVPDLTVLDTAQSPFRGAVLRHMPEFLLSPYVLKGIGLLLKVRRHAQVVYGVRSIAIIGSQHAESVRYAVGQGERSIPAKSVLLHQGVIPSTSLSNAAGCELQWNDEQRAFQPVTDHDGRTTKAGIYVAGDGAGIAGAQAAEVSGRLAALAALADLKLVSTQTSSTSIKSRHAQARRFLRGRAFLDALYTPRQSFLAPSAPETIVCRCEEITVRKLREAIALGPPGPNQLKTFVRCGMGQCQGRLCAATVTEIMVAEERKVSPADVGTYRLRSPVKPVRLAELAHLPHTARALKAVTGRDPVDHDTTETGHIL | Function: Oxidative cleavage of octopine into L-arginine and pyruvate.
Sequence Mass (Da): 53268
Sequence Length: 503
Pathway: Opine metabolism; octopine degradation.
EC: 1.-.-.-
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Q92XP4 | MSLWDAIVIGAGPAGIGASGLLAENGAKVLVIDEAPGPGGQIWRGVEDVSDARARILGSDYLAGRDEVRRLRASGAELSFETQAWRVEPEGTVWLKDSHGIRRERGRRLLIATGAMERPCPLDGWTLPGVTTVGGLQILLKREGMLPGGPLVLIGTGPLFYLFAAQCLAAGMRDLSLIDTAAAGAIVSALRHVPAALTGKGPSYLIKGLKLLWMLRRAGVDIYNHSGDLRIKSAADGLEVHFRMREVEHRLSASHVGLHEGVIPETHLPRALGCRMHWSEAGGAFHPHRDIHLQSSVAGVYIAGDAGGIGGATVALLEGRLAAMGILASLGRPIDELLLRATRRDRAAHLAARPLLDHLYQPSPAILTPADGVLACRCEEVTCGEIRAALRAGCAGPNQVKAFLRCGMGPCQGRMCGMTLTSLAASTHDISMGDAGFLTIRPPLRPISLGEVADLVEP | Function: Oxidative cleavage of octopine into L-arginine and pyruvate.
Sequence Mass (Da): 48410
Sequence Length: 458
Pathway: Opine metabolism; octopine degradation.
EC: 1.-.-.-
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Q59159 | MYEVDMTIIGGGLVGASIAWGLARSGTKPLVLDGADLDLRASRANFALVWVQGKGLHAPHYALWSDASARRWPTMANTLLDDSGIDVGLQQDGAFTFALSEEELEANRQDMESIELETNGRAPQFEVLDRQQTLDRVLGIGPEVVGSIYCAADGHVNALRLFHALHAAMERQGATYRPNHPVQSIEPTTGGFILKGEAFSILSRRIVLAAGLDNKRLAPMVGLSCPLKRSKGQILVTEKTQTALPCLSAGMRQADEGGIMIGDSEETDNTRISSSPDISAVLASRALRIFPALSDLNVVRSWTGFRVKTADGVPIYDHSERYPGAFLVACHSGVTLAANHALIVAQQIAAGQLEDELSVFSARRFHAQQAV | Function: Oxidative cleavage of octopine into L-arginine and pyruvate.
Sequence Mass (Da): 39939
Sequence Length: 371
Pathway: Opine metabolism; octopine degradation.
EC: 1.-.-.-
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Q92XP5 | MSDRCELLVIGGGLIGSAIAWGAARKGARVTLLDEGDIAYRASRANFGLVWLQGKGLGHPDYMHWSIRAGQLWPELSTILLKETGIDIGWRGGGGLHFCLSESEMAARRALIARSSAEGAAIRIQLLDRDALHEIVPDIGPEVRGASLSDLDGEANPLLTLNALQLAFQQNGGRLVVQFAARNIRSEPARGFVVSDANGDEISGRRVVLAAGLGNNELARQVGLKLGLTPERGQIVVTDRIAPFLRYPSNAIRQTREGTVLLGSSHEDAGFSTGTDVETIARLCRIGTRVFPALRAARLIRAWGALRIMSPDGLPIYEEAPEMPGAYVVTCHSGVTLASLHALELGPALAEGHLGPAPRSMRSTRFAL | Function: Oxidative cleavage of octopine into L-arginine and pyruvate.
Sequence Mass (Da): 39325
Sequence Length: 368
Pathway: Opine metabolism; octopine degradation.
EC: 1.-.-.-
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Q588Z2 | MFKPVVKSRSSRSFCYLAGCLAMVAATLSSTAQAKSEWACPEGFTPKAGLNTDFPSDGKKRAFVVVPPKDSAGGAPVWVPMVGTVEATNWNLNVPRSGNNAKLAEHGYMVISPVRQCAEQDPNLGAGACNGVGKDGWTWNPWNDGRAPDASGDKYKTDAGDDVRFLEAMVRCVGTKWKLDRKRLFLGGISAGGTMTNRALLFDSEFWAGGMPISGEWYSTKDDGSTVPFQETRKMVAAAPAKIWQGRVGPYPLPSKLDPMVVITVWGGEKDLWDCGPPLGLCSDYRPTTQASSNYFSSISNVVHVACSATHGHMWPQVNTDAFNLWALNTMASHPKGSSPKDFKLTAPPEGYSCKIGRFTDHYK | Function: Catalyzes the hydrolysis of 4,6-nonanedione, a beta-diketone compound. Also mediates hydrolysis of oxidized polyvinyl alcohol (PVA) in the second step in the degradation of polyvinyl alcohol. Not active toward the monoketone structure.
Catalytic Activity: H2O + nonane-4,6-dione = butanoate + H(+) + pentan-2-one
Sequence Mass (Da): 39401
Sequence Length: 364
Subcellular Location: Periplasm
EC: 3.7.1.7
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P21957 | MSENQRLGLSEEEVEAAEVLGVLKQSCRQKSQPSEDVSQADKMPASESSTTPLNILDRVSNKIISNVVTFYDEINTNKRPLKSIGRLLDDDDDEHDDYDYNDDEFFTNKRQKLSRAIAKGKDNLKEYKLNMSIESKKRLVTCLHLLKLANKQLSDKISCLQDLVEKEQVHPLHKQDGNARTTTGAGEDETSSDEDDDDEEFFDASEQVNASEQSIVVKMEVVGTVKKVYSLISKFTANSLPEPARSQVRESLLNLPTNWFDSVHSTSLPHHASFHYANCEEQKVEQQQQQQQQQQQQQLLQQQLLQQQQQKRNKDGDDSASPSSSVTANGKVLILAKESLEMVRNVMGVVDSTLGKAEEWVKQKQEVKEMIRERFLQQQQQYRQQQQKDGNYVKPSQDNVDSKD | Function: Negative regulator of the transcriptional complex INO2-INO4 in response to phospholipid precursor availability. When precursors become limiting, OPI1 is retained at the endoplasmic reticulum (ER) and INO2-INO4 activates INO1 and other genes required for phospholipid biosynthesis, whereas abundant precursor availability results in targeting of OPI1 to the nucleus to repress transcription of these genes. Binds directly to phosphatidic acid, which is required for ER targeting and may act as sensing mechanism for precursor availability, as phosphatidic acid becomes rapidly depleted upon phospholipid biosynthesis.
Sequence Mass (Da): 46065
Sequence Length: 404
Domain: The FFAT motif is required for interaction with SCS2 and proper localization of the protein.
Subcellular Location: Endoplasmic reticulum
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P35372 | MDSSAAPTNASNCTDALAYSSCSPAPSPGSWVNLSHLDGNLSDPCGPNRTDLGGRDSLCPPTGSPSMITAITIMALYSIVCVVGLFGNFLVMYVIVRYTKMKTATNIYIFNLALADALATSTLPFQSVNYLMGTWPFGTILCKIVISIDYYNMFTSIFTLCTMSVDRYIAVCHPVKALDFRTPRNAKIINVCNWILSSAIGLPVMFMATTKYRQGSIDCTLTFSHPTWYWENLLKICVFIFAFIMPVLIITVCYGLMILRLKSVRMLSGSKEKDRNLRRITRMVLVVVAVFIVCWTPIHIYVIIKALVTIPETTFQTVSWHFCIALGYTNSCLNPVLYAFLDENFKRCFREFCIPTSSNIEQQNSTRIRQNTRDHPSTANTVDRTNHQLENLEAETAPLP | Function: Receptor for endogenous opioids such as beta-endorphin and endomorphin . Receptor for natural and synthetic opioids including morphine, heroin, DAMGO, fentanyl, etorphine, buprenorphin and methadone . Also activated by enkephalin peptides, such as Met-enkephalin or Met-enkephalin-Arg-Phe, with higher affinity for Met-enkephalin-Arg-Phe (By similarity). Agonist binding to the receptor induces coupling to an inactive GDP-bound heterotrimeric G-protein complex and subsequent exchange of GDP for GTP in the G-protein alpha subunit leading to dissociation of the G-protein complex with the free GTP-bound G-protein alpha and the G-protein beta-gamma dimer activating downstream cellular effectors . The agonist- and cell type-specific activity is predominantly coupled to pertussis toxin-sensitive G(i) and G(o) G alpha proteins, GNAI1, GNAI2, GNAI3 and GNAO1 isoforms Alpha-1 and Alpha-2, and to a lesser extent to pertussis toxin-insensitive G alpha proteins GNAZ and GNA15 . They mediate an array of downstream cellular responses, including inhibition of adenylate cyclase activity and both N-type and L-type calcium channels, activation of inward rectifying potassium channels, mitogen-activated protein kinase (MAPK), phospholipase C (PLC), phosphoinositide/protein kinase (PKC), phosphoinositide 3-kinase (PI3K) and regulation of NF-kappa-B (By similarity). Also couples to adenylate cyclase stimulatory G alpha proteins (By similarity). The selective temporal coupling to G-proteins and subsequent signaling can be regulated by RGSZ proteins, such as RGS9, RGS17 and RGS4 (By similarity). Phosphorylation by members of the GPRK subfamily of Ser/Thr protein kinases and association with beta-arrestins is involved in short-term receptor desensitization (By similarity). Beta-arrestins associate with the GPRK-phosphorylated receptor and uncouple it from the G-protein thus terminating signal transduction (By similarity). The phosphorylated receptor is internalized through endocytosis via clathrin-coated pits which involves beta-arrestins (By similarity). The activation of the ERK pathway occurs either in a G-protein-dependent or a beta-arrestin-dependent manner and is regulated by agonist-specific receptor phosphorylation (By similarity). Acts as a class A G-protein coupled receptor (GPCR) which dissociates from beta-arrestin at or near the plasma membrane and undergoes rapid recycling (By similarity). Receptor down-regulation pathways are varying with the agonist and occur dependent or independent of G-protein coupling (By similarity). Endogenous ligands induce rapid desensitization, endocytosis and recycling (By similarity). Heterooligomerization with other GPCRs can modulate agonist binding, signaling and trafficking properties (By similarity).
PTM: Phosphorylated. Differentially phosphorylated in basal and agonist-induced conditions. Agonist-mediated phosphorylation modulates receptor internalization. Phosphorylated by GRK2 in a agonist-dependent manner. Phosphorylation at Tyr-168 requires receptor activation, is dependent on non-receptor protein tyrosine kinase Src and results in a decrease in agonist efficacy by reducing G-protein coupling efficiency. Phosphorylated on tyrosine residues; the phosphorylation is involved in agonist-induced G-protein-independent receptor down-regulation. Phosphorylation at Ser-377 is involved in G-protein-dependent but not beta-arrestin-dependent activation of the ERK pathway (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 44779
Sequence Length: 400
Subcellular Location: Cell membrane
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Q51487 | MKRSFLSLAVAAVVLSGCSLIPDYQRPEAPVAAAYPQGQAYGQNTGAAAVPAADIGWREFFRDPQLQQLIGVALENNRDLRVAALNVEAFRAQYRIQRADLFPRIGVDGSGTRQRLPGDLSTTGSPAISSQYGVTLGTTAWELDLFGRLRSLRDQALEQYLATEQAQRSAQTTLVASVATAYLTLKADQAQLQLTKDTLGTYQKSFDLTQRSYDVGVASALDLRQAQTAVEGARATLAQYTRLVAQDQNALVLLLGSGIPANLPQGLGLDQTLLTEVPAGLPSDLLQRRPDILEAEHQLMAANASIGAARAAFFPSISLTANAGTMSRQLSGLFDAGSGSWLFQPSINLPIFTAGSLRASLDYAKIQKDINVAQYEKAIQTAFQEVADGLAARGTFTEQLQAQRDLVKASDEYYQLADKRYRTGVDNYLTLLDAQRSLFTAQQQLITDRLNQLTSEVNLYKALGGGWNQQTVTQQQTAKKEDPQA | Function: The outer membrane component of the MexAB-OprM efflux system that confers multidrug resistance . Functions as the major efflux pump for n-hexane and p-xylene efflux . Has been shown in one study to be involved in the active efflux of the autoinducer N-(3-oxododecanoyl) homoserine lactone, thereby playing an indirect role in quorum-sensing; but has been shown in another study not to be involved in efflux of this autoinducer . Over-expression of the pump increases antibiotic and solvent efflux capacities . Can replace the OprJ outer membrane component of the MexCD-OprJ pump; the antibiotics exported are those exported by the intact MexCD pump, showing that efflux substrate specificity is not conferred by this component . Serves as the outer membrane component for the MexXY efflux system . Implicated in the secretion of the siderophore pyoverdine . OprM is probably involved in the efflux of the siderophore across the outer membrane .
Location Topology: Lipid-anchor
Sequence Mass (Da): 52598
Sequence Length: 485
Subcellular Location: Cell outer membrane
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P41146 | MEPLFPAPFWEVIYGSHLQGNLSLLSPNHSLLPPHLLLNASHGAFLPLGLKVTIVGLYLAVCVGGLLGNCLVMYVILRHTKMKTATNIYIFNLALADTLVLLTLPFQGTDILLGFWPFGNALCKTVIAIDYYNMFTSTFTLTAMSVDRYVAICHPIRALDVRTSSKAQAVNVAIWALASVVGVPVAIMGSAQVEDEEIECLVEIPTPQDYWGPVFAICIFLFSFIVPVLVISVCYSLMIRRLRGVRLLSGSREKDRNLRRITRLVLVVVAVFVGCWTPVQVFVLAQGLGVQPSSETAVAILRFCTALGYVNSCLNPILYAFLDENFKACFRKFCCASALRRDVQVSDRVRSIAKDVALACKTSETVPRPA | Function: G-protein coupled opioid receptor that functions as receptor for the endogenous neuropeptide nociceptin. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors. Signaling via G proteins mediates inhibition of adenylate cyclase activity and calcium channel activity. Arrestins modulate signaling via G proteins and mediate the activation of alternative signaling pathways that lead to the activation of MAP kinases. Plays a role in modulating nociception and the perception of pain. Plays a role in the regulation of locomotor activity by the neuropeptide nociceptin.
PTM: Phosphorylation at Ser-363 requires GRK3.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 40693
Sequence Length: 370
Subcellular Location: Cell membrane
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Q5W9T5 | MENFTEENLHPWITTTTRVYNNVTIFPQYDDELGKFEIMVLCILCFMALFGNAVVLIVLRIKKTTLTRMQLLIVYLSVTDISVALFHILPTIILKINVYFLGDISACRVYQFITVAELYASSFVLIVTALDRYISICHPLAAHMWTNRRVHMTTALALFLALMCSLPQLDAVLVDFHGGKLCRPNLTTELANIAYSWWAFCSVFFVPLLLLIFFYGRICFVVWQSMRGRECTQSVGSSASRYVRKPIKCRISSQTSSENRVKNYSDARDKDSSRNPRAICRGVSKSKIKTIKLTFSVVACFIICYTPFFTVLMARTYDAELSSAQTPALVILSLLPSLNSCTNPWIYLAFSGKVWCRQQSQNFPRTWTQTTNTYLVELEAKKRTSFGAEHVTFASNSTARKTLNVDDTNTTALMSSSPC | Function: Acts as a receptor for octopressin.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 47505
Sequence Length: 419
Subcellular Location: Cell membrane
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P06002 | MESFAVAAAQLGPHFAPLSNGSVVDKVTPDMAHLISPYWNQFPAMDPIWAKILTAYMIMIGMISWCGNGVVIYIFATTKSLRTPANLLVINLAISDFGIMITNTPMMGINLYFETWVLGPMMCDIYAGLGSAFGCSSIWSMCMISLDRYQVIVKGMAGRPMTIPLALGKIAYIWFMSSIWCLAPAFGWSRYVPEGNLTSCGIDYLERDWNPRSYLIFYSIFVYYIPLFLICYSYWFIIAAVSAHEKAMREQAKKMNVKSLRSSEDAEKSAEGKLAKVALVTITLWFMAWTPYLVINCMGLFKFEGLTPLNTIWGACFAKSAACYNPIVYGISHPKYRLALKEKCPCCVFGKVDDGKSSDAQSQATASEAESKA | Function: Visual pigments are the light-absorbing molecules that mediate vision. They consist of an apoprotein, opsin, covalently linked to cis-retinal.
PTM: Phosphorylated on some or all of the serine and threonine residues present in the C-terminal region.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 41495
Sequence Length: 373
Subcellular Location: Membrane
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Q8NGN0 | MNPANHSQVAGFVLLGLSQVWELRFVFFTVFSAVYFMTVVGNLLIVVIVTSDPHLHTTMYFLLGNLSFLDFCYSSITAPRMLVDLLSGNPTISFGGCLTQLFFFHFIGGIKIFLLTVMAYDRYIAISQPLHYTLIMNQTVCALLMAASWVGGFIHSIVQIALTIQLPFCGPDKLDNFYCDVPQLIKLACTDTFVLELLMVSNNGLVTLMCFLVLLGSYTALLVMLRSHSREGRSKALSTCASHIAVVTLIFVPCIYVYTRPFRTFPMDKAVSVLYTIVTPMLNPAIYTLRNKEVIMAMKKLWRRKKDPIGPLEHRPLH | Function: Odorant receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35771
Sequence Length: 318
Subcellular Location: Cell membrane
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P0C645 | MEEAILLNQTSLVTYFRLRGLSVNHKARIAMFSMFLIFYVLTLIGNVLIVITIIYDHRLHTPMYFFLSNLSFIDVCHSTVTVPKMLRDVWSEEKLISFDACVTQMFFLHLFACTEIFLLTVMAYDRYVAICKPLQYMIVMNWKVCVLLAVALWTGGTIHSIALTSLTIKLPYCGPDEIDNFFCDVPQVIKLACIDTHVIEILIVSNSGLISVVCFVVLVVSYAVILVSLRQQISKGKRKALSTCAAHLTVVTLFLGHCIFIYSRPSTSLPEDKVVSVFFTAVTPLLNPIIYTLRNEEMKSALNKLVGRKERKEEK | Function: Odorant receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35737
Sequence Length: 315
Subcellular Location: Cell membrane
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