ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
A9KMC1 | MEQVYSVTQVNNYIKNMFVKDYVLNRIYMKGEVSNCKYHTSGHIYFTLKDETGQMACVLFAGYRTGLPFRLEEGQSVIVLGSISVYERDGKYQLYAKEIKLDGLGLLYERFELLKRKLNEEGLFDPSHKKTLVPYPRTVGIVTASTGAAIQDIINISKRRNPYVQLVLYPAKVQGEGAAKTIVAGIKALEAKGVDTIIVGRGGGSIEDLWAFNEEMVARAIFDCSIPIISAVGHETDITISDFVSDLRAPTPSAAAELAVPEIESLLSNLVDYHYSLVQCVMRKITMARSELEKKQLQLTHLSPVYALRQKRQYTIDLENKLRQRMNELIRYKRHLLDIQIERLKAASPLDKLKSGFSYVSDSSGKVVNSITKTKPGDELTIAVTDGMIKAKTIGVESIER | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 44927
Sequence Length: 401
Subcellular Location: Cytoplasm
EC: 3.1.11.6
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Q88WM7 | MSESQQYLTVTALTQYLKRKFEVDPYLGKVYLTGEVSNYRPRPNTHQYFSLKDDHAKISAIMFKSAFAKVKFQPEEGMKVLVVGRIGLYEPSGSYQIYVERMEPDGVGALYQAYEQLKKKLAAEGLFSAPKKPLPRFPKRIAVVTSRSGAVIRDIITTTRRRFPIAQIVLFPSQVQGDAAAAEISRQIERANAQGDFDTLIIGRGGGSIEDLWPFNEEVVARAIAQSQLPVISSVGHETDTTIADLVADVRAATPTAAAELAVPVYNDVLLQLKQDQTRVFNAFQNFVQRDRQRLNKLQTSYVFTQPNRLYEGYLQKLDFLNERLKQAGQNNFNLASQHYQRVFQQLRQQTPIHQVRQAQTQLLNLQQRLNRGTQLVVRQKRQQLTQTVQSLDLLSPLKIMTRGYAFVTADEQVVHGVKQLQPEQTVAIHMADGEAQAQITKIDGGK | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 50494
Sequence Length: 447
Subcellular Location: Cytoplasm
EC: 3.1.11.6
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Q38XU8 | MVKPTDYLTVTALTQYLKAKFERDPYLDRVYLTGEISNFRLRPNAHQYFSLKDNKAKISAIMFKSAFEKVKFTPEEGMKVLIVGRISLYEASGNYQIYVERMEPDGLGALYQAYEQLKAKLATEGLFDAPKQPLVRFPKRIAVITSPSGAVIRDIITTTQRRYPIAQLVLFPAVVQGDGAADVLVERLKQVNEHGDFDTIIIGRGGGSIEDLWPFNEERVARAIVASQIPVISSVGHETDTTIADLVADVRAATPTAAAELATPVLTDEILKLQQQRLRLYQAFSKTVALNKKQLDHLQNSYVLKQPKRLYDGYLQNVDQLQRRLLTAQQQLLKDRRQQVQLLQQRLMAQSPLMAVRQAQKDVTEQQRRLNQAMNRLMADRRQKAAQVIAALDLVSPLKILGRGFAYVTDDQQQMLKKVADFKTQQPIELHVQDGLVTAEVVATHKGEE | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 50698
Sequence Length: 449
Subcellular Location: Cytoplasm
EC: 3.1.11.6
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Q5WY82 | MSSQLPILTVSQLNRQVKGFLENEIGLVHVEGEISNLSKPSSGHYYFTLKDSTAQIRCAFFKNRHSSSLLRNFNDGQQIVASGKLSLYEARGEYQLIVEEIVEAGMGILYQRFEELKIKLAREGLFNPERKKTLPRIPETIGIITSPTGAAIQDILSTLARRFPIARIIIYPSEVQGQAAPQQLVNALKLANTHKRCQVLILARGGGSIEDLWAFNDEYLARQIAISEIPVVSGIGHETDFTIADFVADYRAETPTAAATAVTPNCIELFNILDTAIYRLHDAIIRLVKGLQLKLNHLIDKIASPRQTISTYWQTLDYLERQLISAMTQFINLNINKMNLFSTRLQANNPKTQIERTKIQLRQLILQLTQEIRIKVNQLKHQLSTNLSTLHAVSPLATLDRGYAIVSKNQRILFAAQQAQIGDTIDVRLAKGSLACEVTQIKD | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 49654
Sequence Length: 443
Subcellular Location: Cytoplasm
EC: 3.1.11.6
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Q6ADU9 | MRGTRVTETASAPRMAPGPPTLDDPWPVALLASKIRGWIERLGTAWVEGEITQWGVSGGNVYGKLKDLNEDATVGFTIWSSVKARIPADLKQGDRVIAAVKPNYWLKGGTLTMQVSDMRHVGLGDLLERLERLRAQLRAEGLFRPERKKRLPFLPHTIGLVTGKDSDAEKDVLRNAQLRWPQVRFRTVYAAVQGDRTVPEVTAALRELDADPEVEVIIVARGGGDFQNLLGFSDESLLRAAAGLSTPLVSAIGHEADRPLLDEVADLRASTPTDAAKRVVPDVAEELVRVHQARARIGTRLTHIIRHEIDRIGHLRTRPALASGSWIVDSRAQDLTRFVARGAELVERCVDREAARVAELRGQLRALSPQATLERGYAIVQNAAGRVVAAPGEAPAGTELRITVSGGSLAATAGKALPSPAQGATNGSLAAPRGK | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 46928
Sequence Length: 435
Subcellular Location: Cytoplasm
EC: 3.1.11.6
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Q3AH76 | MSADRLPSYSVAELNTAIGSLLERGFAPRFLLEATVSRPQLKKGHLWLTLTDGSASISGVVWASKLAQLSYQPKDGDGVTVVGKLNFWAARASLTVQALDIRPSLSTVLRDFERVRQVLEQEGVIDPSRLRPLPSQPASIAVLTSVPSSALADMLRTAAERWPLTQLIVVPIPVQGSVAPTIINTLEAIAERTAELGLQALVLARGGGSREDLAVFDNEALCRLLANYPIPVVTGLGHEDDLTVADLVADHRAATPTAAIVALLPDREAERQGLTQRQSRLKDTLLGRILRERQRLQDRAVALQQQSPREKIMRKRQELIQKHQLLKALSPERWLKRGLALISNKAGDPIPGLESVKIGDQLNIRMSDGSLEARVDQIQPSAPNTTS | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 42184
Sequence Length: 387
Subcellular Location: Cytoplasm
EC: 3.1.11.6
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Q0AZF4 | MKEILTVTELNSYIANLLDSDPFLGQLWLRGEISGFRLYQQSGHMYFTLKDEDSTISAVMFKSRARGLKFKPKDGMEVLLRASVSVFARQGKYQLYVEEMQPYGIGGLFLYLEELKKKLAAKGYFAPERKKAIPAFVQRVGIVTSQDGAALRDICRILKQRHPGVEVVLAHSSVQGSEAPGELAEGLRLLNSYAEVELIIIGRGGGSYEDLMAFNSELVVQAIYESNIPVISAVGHEVDFTLADLVADLRAATPSQAASLAVADMQALSRQLDNYQQRLLRAMQRKLLYYTEIIDRLMMKRIWKQPRSLLHMREELLSQLEKSLSRGMAEIFREKKMKLSMNMAALDSLSPLKIMERGYVLLQKEGRIIRDEQQVQIGDRLEVAMRHADLEIEVIKKERVKRWKS | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 46034
Sequence Length: 405
Subcellular Location: Cytoplasm
EC: 3.1.11.6
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Q47SR1 | MGMESSPESPQPVRVVLQAVGGWIGRLGRIWIEGQVAELHRRGGMAYITLRDPVANVSARVTCSIRVLRAADPPPEQGARVVVYAKPDFYVPRGTFSFQALEIRHVGLGELLARLERLRQALAAEGLFAESRKRKLPFLPGVVGLICGRDSAAERDVLENARRRWPAVRFEVREVAVQGDRAVPEVMAALEELDAHPEVDVIIIARGGGSLEDLLPFSDEALVRAVAAARTPVVSAIGHEQDTPLLDYVADLRASTPTDAAKKVVPDVGEQWELIRQLRDRARRVLEGGIAREEAWLASMRSRPVLANPVQEVERKIEQVFDLRDRGRRALTAALDRAGDNLAHIRARLHALSPATTLARGYAIVRRADGTVVRSAAEVAPGEELRLRFAEDGLVAIAQNREEDEL | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 44638
Sequence Length: 406
Subcellular Location: Cytoplasm
EC: 3.1.11.6
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Q9X289 | MKDYTYSVTEINEYIKDLIEGDPYLTNVSVYGEISGVRPRKGHIFFSLVEENARLECVIFGGDNMGIRLQEGRMALVEGSVSVYIPHGTYRFICSNVRYLDQAGMYQIKFETTLKKLLEEGLLSRPKKTVPRFPRKIGIITSRDSAALQDVIRTARERKAPIEIYVFHTSVQGDSAREELIKALRKANEYDLDLVMIVRGGGSKEDLWVFNEEDVIREILRLRHPVVTGIGHEIDRVIADFVADVSMHTPTGAAEYVIPDASEIHEDLDSFFEKLITSLSNRFDMEERRLETLYFRLRMIGRRKLELNEFKIERVKELAAKLRKKLMDYFEHNQKKLDSLGRMLESLNPLRPLERGFVLVKKDEKIVKESTDLKRGDVVSLVFKDGTKKAQVIG | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 45353
Sequence Length: 394
Subcellular Location: Cytoplasm
EC: 3.1.11.6
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B0K9E1 | MQLKALEVREITDYIKKMMDNDIILRNVRVKGEISNLKYHSTGIYFTLKDEIASLKCVMFNEYGKLLNFTLQDGMSVIVTGRISVYERNGTYQLYAQSIQSDGIGALYFAFNKLKEKLQKEGLFDSDKKKPIPKHPKKIAVVTSPTGAVIRDIITISRRRNPTVDILVVPVLVQGSSAADEICNALRILNKREDIDVIILARGGGSLEEIWPFNEEKVARCIYASRIPVVSAVGHETDFTISDFVADLRAPTPSAAAEIVVPDIKVYQRELFLLKTKLLTLMTAELNRKKKEFEGLKRALYLNSPTKKSEILRHKVENLTASLYNEMLSIYQHKRNDFLILAEKLNSLSPLKVLTRGYTIVLDKQEKVISSVKDIKPYDEIKILFKDGKAKAIVQEVKENE | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 45483
Sequence Length: 401
Subcellular Location: Cytoplasm
EC: 3.1.11.6
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B8GP32 | MAVTDRDIFTVTRLNQAVQGLLEGTFPLIWVEGELSSVSRPASGHLYFTLKDSGAQVRCALFRNRAQLMRFRPADGMQVLVRARVGLYAPRGDYQLIVEHMEEAGDGALRRAFEELKQRLEREGLFDAERKRPLPRFPRRLGVITSPTGAAIRDILSVLRRRFPGLPALIYPVPVQGAAAAPAIAEALRTASARKDCDVLILARGGGSLEDLWAFNEEIVARAIHDCEIPVVSGVGHEVDVTIADLAADLRAATPSAAAELVSPLRDEWLLHVERQRRLLVERMQRGLQHQALKLDNLERRLRQQHPERRLQNQAQRVDELERRLALAMQHRLRHRESRLARLQDRLQHRSPARALERLEAREAQLRLRLDSALRRRLDRFEARLAAAGRALHSVSPLATLGRGYSILTTAEGQVIRDASQVQVNDRVEARLGKGRLSCTVVTRYEG | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 50351
Sequence Length: 447
Subcellular Location: Cytoplasm
EC: 3.1.11.6
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C4L8C6 | MAISQPVIYTVSRLNNVVRLLLEQEMGLVWLTAEISNLVQHSSGHWYFTLKDQQAQIRAAMFKGQNRRVSFRPQNGQQILVQGQLSLYEARGDYQLIVEKMQPAGDGLLQMKLEALKARLMAEGLFDPRRKRALPTQPKQIGIITSPTGAAIHDMLTILARRDPALPVILYPSAVQGESAVPALLNALETAWRRNECDLLIIGRGGGSLEDLWCFNDELVVRAIANSPIPIVSAVGHETDVTLSDFAADLRAPTPSAAAELVSRDQQQQLHRLAQYQHRLQQAIQLRLQQHQIAWQQQYARLNTQNPRYQLQQKIQKQDELQFRLERVMTQTLVQANQQWMSQHQRLQQVSPKRQLPNLQKQHAYLYQRLLNAMQSKQQDSAQTLSRLSGQLHALSPLQVLARGYSVTTNAKGELIHSSQQVTTGEMLNVQLHQGTLKVRTEEVKSEN | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 50758
Sequence Length: 448
Subcellular Location: Cytoplasm
EC: 3.1.11.6
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Q83HE6 | MDMQADEMYRQDPLGSCGNPRQVSHITGRLSSLLGELPATWIEGEVTQLSPRRIGVFLTLKDMNESKHLEFFLPFDAFKDEVEVGNRVKIHGKLEFWATSGQIKVKGFEIQSVGIGELIERIARLRVQLALEGLYEHKRPLPFIPKLIGLVTGQNSDAEKDVVTNVLLRWPAAKFCTIYASMQGASCVSETISAIQKLDANNDVDVIIVARGGGSFHDLIGFSDEQMIRAVFAIKTPLISAIGHEADRPILDEVADLRASTPTDAAKRVVPDIADEKRLIKSAMSFLKKSYEPVIDKIKCDTLSWSQAFSNPFETFIAPRRREIDLFYQQMLTVVWANFSKTETEIAAIKKHLLAISPQNTLVRGYAMIEDETGRIISSADKLSAGDTVTLRLHDGLVRAEITQ | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 44985
Sequence Length: 404
Subcellular Location: Cytoplasm
EC: 3.1.11.6
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B2KAR1 | MKEQSFEANLKKLEKIVAQLEDEKTDLDKSAELFEEGSALAAELSAKLKTIKFKVSEIKEKQGDLFTEEINNDDE | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 8521
Sequence Length: 75
Subcellular Location: Cytoplasm
EC: 3.1.11.6
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B1GZX5 | MNKKQLNFEKSLKKLEEIVSEIENADPDLDKALALFAEGAELIKSCLAKLNETKKKIEVIISSGKTEFFKE | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 8028
Sequence Length: 71
Subcellular Location: Cytoplasm
EC: 3.1.11.6
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Q836W5 | MPAKEKTFEESLNALEEIVQRLERGDVPLEEALAAFQEGMALSKQCQDTLEKAEKTLTKMMTENNEEIVFEESEEA | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 8651
Sequence Length: 76
Subcellular Location: Cytoplasm
EC: 3.1.11.6
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B0S1L9 | MNEYREYDEGLKRLSEIVEKLEDRELSLEENIKLYEEGMKLHKRLSSILKEQEGKMTLIKDNKEEDFQINMLLSDDNE | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 9409
Sequence Length: 78
Subcellular Location: Cytoplasm
EC: 3.1.11.6
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Q4L6M3 | MSKDQQSFEEMMQELENIVQKLDNETVSLEESLELYQRGMKLSATCDATLKDAEKKVNQLIKDEAEDEENGKEVNE | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 8770
Sequence Length: 76
Subcellular Location: Cytoplasm
EC: 3.1.11.6
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Q3K2M3 | MSDKKTFEENLQELETIVSRLETGDVALEDAIAEFQKGMLISKELQRTLKEAEETLVKVMQADGTEVEMDT | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 8035
Sequence Length: 71
Subcellular Location: Cytoplasm
EC: 3.1.11.6
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Q9FBM4 | MTSEVEQPTAMSEALGYEQARDELIEVVRRLEAGGTTLEESLALWERGEELAEVCRRRLDGARARLDAALAEEADPEDGASGADGGGA | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 9376
Sequence Length: 88
Subcellular Location: Cytoplasm
EC: 3.1.11.6
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B2FP36 | MAKKSPENASPVAQFEQSLESLEQLVEQMETGELSLEASLSAYERGVGLYRQCQQALEQAELRVRLLSDPAQPEASEPFDPPSHDG | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 9474
Sequence Length: 86
Subcellular Location: Cytoplasm
EC: 3.1.11.6
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P0DJ94 | HSDATFTAEYSKLLAKLALQKYLESILGSSTSPRPPSS | Function: O-linked and free exendin-1 and exendin-1b have vasoactive intestinal peptide(VIP)/secretin-like biological activities. They interact with rat and human VIP receptors 1 (VIPR1) and 2 (VIPR2), with the highest affinity for the human VIPR2. They induce hypotension that is mediated by relaxation of cardiac smooth muscle.
PTM: O-linked glycan consists of Hex-HexNAc saccharide.
Sequence Mass (Da): 4096
Sequence Length: 38
Subcellular Location: Secreted
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P21760 | MRTLALSLALALLCLLHTEAAATVPDRSEVAGKWYIVALASNTDFFLREKGKMKMVMARISFLGEDELEVSYAAPSPKGCRKWETTFKKTSDDGELYYSEEAEKTVEVLDTDYKSYAVIFATRVKDGRTLHMMRLYSRSREVSPTAMAIFRKLARERNYTDEMVAVLPSQEECSVDEV | Function: Siderocalin-like lipocalin tightly binding a variety of bacterial ferric siderophores, also binds long-chain unsaturated fatty acids such as linoleic acid, oleic acid, arachidonic acid and, with a lower affinity, long chain saturated fatty acids such as steraic acid. May act as an antibacterial factor, through dual ligand specificity, both as a siderophore-sequestrating molecule and a lysophosphatidic acid (LPA) sensor.
PTM: Does not seem to be glycosylated.
Sequence Mass (Da): 20201
Sequence Length: 178
Subcellular Location: Secreted
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G3XDA1 | MHIQSLQQSPSFAVELHQAASGRLGQIEARQVATPSEAQQLAQRQDAPKGEGLLARLGAALVRPFVAIMDWLGKLLGSHARTGPQPSQDAQPAVMSSAVVFKQMVLQQALPMTLKGLDKASELATLTPEGLAREHSRLASGDGALRSLSTALAGIRAGSQVEESRIQAGRLLERSIGGIALQQWGTTGGAASQLVLDASPELRREITDQLHQVMSEVALLRQAVESEVSRVSADKALADGLVKRFGADAEKYLGRQPGGIHSDAEVMALGLYTGIHYADLNRALRQGQELDAGQKLIDQGMSAAFEKSGQAEQVVKTFRGTRGGDAFNAVEEGKVGHDDGYLSTSLNPGVARSFGQGTISTVFGRSGIDVSGISNYKNEKEILYNKETDMRVLLSASDEQGVTRRVLEEAALGEQSGHSQGLLDALDLASKPERSGEVQEQDVRLRMRGLDLA | Function: Bifunctional effector protein that is secreted and delivered by the type III secretion system into eukaryotic target cells . The N-terminus encodes a GTPase-activating protein activity, whereas the C-terminus encodes an ADP-ribosyltransferase activity. ADP-ribosylates several eukaryotic proteins including ezrin/radixin/moesin (ERM), cyclophilin A and several members of the Ras superfamily . Host Ras ADP-ribosylation blocks its activation by its guanine nucleotide exchange factor, thereby interfering with Ras-mediated signal transduction . For instance, prevents Ras from interacting with and activating phosphoinositol-3-kinase (PI3K), which is required to stimulate the phagocytic NADPH-oxidase that generates reactive oxygen species . The ADPRT domain contributes also to bacterial dissemination to the blood during pneumonia . In addition to this activity, acts via its N-terminal region as a GTPase-activating protein (GAP) for host Rho GTPases including RhoA, Rac1, Cdc42 and Ras . The GAP domain activity induces mitochondrial disruption in the target host cell by activating host caspases 3 and 9 that execute cellular death .
Catalytic Activity: L-arginyl-[protein] + NAD(+) = H(+) + N(omega)-(ADP-D-ribosyl)-L-arginyl-[protein] + nicotinamide
Sequence Mass (Da): 48302
Sequence Length: 453
Domain: The N-terminal contains a GTPase-activating protein (GAP) domain . The ADP-ribosyltransferase domain is located within the C-terminus region .
Subcellular Location: Secreted
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Q9I788 | MHIQSSQQNPSFVAELSQAVAGRLGQVEARQVATPREAQQLAQRQEAPKGEGLLSRLGAALARPFVAIIEWLGKLLGSRAHAATQAPLSRQDAPPAASLSAAEIKQMMLQKALPLTLGGLGKASELATLTAERLAKDHTRLASGDGALRSLATALVGIRDGSRIEASRTQAARLLEQSVGGIALQQWGTAGGAASQHVLSASPEQLREIAVQLHAVMDKVALLRHAVESEVKGEPVDKALADGLVEHFGLEAEQYLGEHPDGPYSDAEVMALGLYTNGEYQHLNRSLRQGRELDAGQALIDRGMSAAFEKSGPAEQVVKTFRGTQGRDAFEAVKEGQVGHDAGYLSTSRDPGVARSFAGQGTITTLFGRSGIDVSEISIEGDEQEILYDKGTDMRVLLSAKDGQGVTRRVLEEATLGERSGHGEGLLDALDLATGTDRSGKPQEQDLRLRMRGLDLA | Function: Bifunctional effector protein that is secreted and delivered by the type III secretion system into eukaryotic target cells. The N-terminus encodes a GTPase-activating protein activity, whereas the C-terminus encodes an ADP-ribosyltransferase activity . ADP-ribosylates several eukaryotic proteins including CT10 regulator of kinase (Crk) proteins . In turn, induces atypical anoikis apoptosis by transforming Crk adaptor protein into a cytotoxin . Affects host cell morphology by disrupting the actin cytoskeleton . In addition to this activity, acts via its N-terminal region as a GTPase-activating protein (GAP) for host Rho GTPases including RhoA, Rac1, Cdc42 and Ras . The GAP domain activity induces mitochondrial disruption in the target host cell by activating host caspases 3 and 9 that execute cellular death . This activity also causes stress fiber disassembly .
Catalytic Activity: L-arginyl-[protein] + NAD(+) = H(+) + N(omega)-(ADP-D-ribosyl)-L-arginyl-[protein] + nicotinamide
Sequence Mass (Da): 48515
Sequence Length: 457
Subcellular Location: Secreted
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P33699 | MTPTVNAKTVTRNVGWSVLSKTGTFGLKFVTVPILARILSPEEFGAVAVALTVVQFLAMIGGAGLTSALVIQQHEEMETVHSVFWANLAIALMMALGLFVFAEPLATLLGAPEAAYLLRIMSLLIPLQLGGDVAYSLLVRRMNFRKDAVWSMISESLGAVIAVLLALLGFGIWSLLAQLFVSALVRLSGLYAVSRYAPRFVFSLQRVLALSRFSFGMMGSEIANFITFQSPMVVISRYLGLSDAGAYSAANRFASIPNQVVLSAVMGVLFPTFGQMMHDRERRSQALMLSTQVTTVLLAPMMFGLWALAEPAMLVLFGSQWAYAWPVLGLLALSKGILTPCSTFIPYLKGVGQGAVLFWWALIRAVATTGAVAYGAIDGSLVEAMIWLCIVNAVTLVGYSWVVFRADSTPFLKGLFISSRPMIAALLMALVVRFLLEHFGAHVPNAVLQLIAGTAIGSVIYTVLILLTERSLLRRLLDMARARKPRAAPAGAAE | Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 53316
Sequence Length: 494
Pathway: Glycan metabolism; exopolysaccharide biosynthesis.
Subcellular Location: Cell membrane
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P33700 | MTAAAPTDVCIIISAKNAADTIARAVASALAEPEAAEVVVIDDGSTDDSASVARAADDGTGRLNVVRFEENRGPAAARNHAIAISHSPLIGVLDADDFFFPGRLGQLLSQDGWDFIADNIAFIDAAQAATAHGRIDRFAPTPRLIDLVGFVEGNISRRGVRRGEIGFLKPLMRRAFLDQHGLRYNETLRLGEDYDLYARALANGARYKIIHSCGYAAVVRGNSLSGSHRTIDLKRLYEADRAILAGSRLSSDAEAAVRRHERHIRDRYELRHFLDLKNQQGFGRAFGYALTHPAALPAIIGGILADKTERFRPSGSPAPVALGGKGDVRYLLETLAVDQPQK | Function: Glycosyltransferase required for the synthesis of succinoglycan (EPS I). Needed for the addition of the sixth sugar (glucose), catalyzes the formation of a beta-1,6 linkage between the fifth and sixth sugar.
Sequence Mass (Da): 37018
Sequence Length: 342
Pathway: Glycan metabolism; exopolysaccharide biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.4.-.-
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P33702 | MAKLTVVIPYYQKEPGILRRALASVFAQTLEDFHVLVIDDESPYPIADELAGLAQEERERITVIRQPNGGPGGARNTGLDNVPADSDFVAFLDSDDVWTPDHLLNAYQSMTRFDADCYWASITGGDAFYYHFGVADLEKSETVTRLSESPLVVELPELQDVMLKNWSFLHMSCMVIGRKLFEKVRFEATLKLAAEDVLFFCDCVLASKRVVLCDAAGAVRGEGLNIFHSIDNDSPQFLKQQFNTWVALDTLEGRYRNRPKAMEAIRSYKHTARRQALWSQARRIKRRKLPQFDLLARWLWRDPRLIGSAAELAVGKLSR | Function: Glycosyltransferase required for the synthesis of succinoglycan (EPS I). Needed for the addition of the seventh sugar (glucose), catalyzes the formation of a beta-1,3 linkage between the seventh and eighth sugar.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 36216
Sequence Length: 319
Pathway: Glycan metabolism; exopolysaccharide biosynthesis.
Subcellular Location: Cell membrane
EC: 2.4.-.-
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P14801 | MHQRCFGLRASLSIFKAFAVTLAASVFLQVVYFLSLLFMSFRPTRESDRSIHSGTRQADQPQKRDRDKTEQSNVPKLDPRRKRRTP | Function: Inhibition of exopolysaccharide synthesis (EPS) and nodulation ability (NOD).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 10026
Sequence Length: 86
Pathway: Glycan metabolism; exopolysaccharide biosynthesis.
Subcellular Location: Cell membrane
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Q02730 | MFAPRVFLSMIGALAAFAVATYYLNGSLASTAIQTLICAVLIQVGYFIAVLFLVWKEARERRRLSSQKQFMTAEAANDEKQPGKVSLRRLNRPHHLNS | Function: Inhibition of exopolysaccharide synthesis (EPS) and nodulation ability (NOD).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 10985
Sequence Length: 98
Pathway: Glycan metabolism; exopolysaccharide biosynthesis.
Subcellular Location: Cell membrane
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Q02731 | MKSATRSASSPFFIPEETGAVRPIGGMAKRSFDVLAASVALLLFSPLFLLIMALVKFSDGGSVFYGHRRIGHNGQSFKCLKFRTMMEKGDEVLEEFFRINPDAYEEWRATRKLQNDPRVTVVGAVLRKLSLDELPQLLNIIRGEMSVVGPRPVVEDELELYDSAAVFYLRSRPGLTGLWQISGRNDVSYATRVAFDTQYVQNWSLFADLVIVFKTIPAVCLSRGSY | Function: Needed for the addition of the first sugar (galactose) to the isoprenoid carrier. May function as a sugar transferase.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 25353
Sequence Length: 226
Pathway: Glycan metabolism; exopolysaccharide biosynthesis.
Subcellular Location: Cell membrane
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P26502 | MLFHAAEKTGHHFTIGAAGVDVFFVISGFIMWVISDRRSVTPVEFIADRARRIVPVYWLATGVMVAGALAGLFPNLVLTLEHVLASLFFVPARSPSSGEIWPVLVQGWTLNFEMLFYAVFAGSLFMPRNWRLPVVSGLFLALVIAGRVVAFDDAVMLTYTRPVILEFVAGMIIGEFWLKGRVPPLAVGSALFACSLGGFALIGVLGLPFDELTTGPLAVLLVIGVLSLEANGCVRALSLPGLLGDASYSIYLWHTFAISVVAKAGLAIGLGAPATMFAAVLSGTLIGIAAYMMLERPLLRRGRARRVTAGLAGRAAE | Function: Required for the acetyl modification of the third sugar (glucose) of the octasaccharide subunit of succinoglycan (EPS I).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 33821
Sequence Length: 317
Subcellular Location: Cell membrane
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P03697 | MTPDIILQRTGIDVRAVEQGDDAWHKLRLGVITASEVHNVIAKPRSGKKWPDMKMSYFHTLLAEVCTGVAPEVNAKALAWGKQYENDARTLFEFTSGVNVTESPIIYRDESMRTACSPDGLCSDGNGLELKCPFTSRDFMKFRLGGFEAIKSAYMAQVQYSMWVTRKNAWYFANYDPRMKREGLHYVVIERDEKYMASFDEIVPEFIEKMDEALAEIGFVFGEQWR | Function: Facilitates phage DNA recombination through the double-strand break repair (DSBR) and single-strand annealing pathways. Also important for the late, rolling-circle mode of lambda DNA replication.
Catalytic Activity: Exonucleolytic cleavage in the 5'- to 3'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 25909
Sequence Length: 226
EC: 3.1.11.3
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Q7XUD0 | MAPCLLLVLFLLPALATGHQHPSTLGSSALSEWRSAKASYYAADPEDAIGGACGFGDLGKHGYGMATVGLSTALFERGAACGGCYEVKCVDDLKYCLPGTSIVVTATNFCAPNFGLPADAGGVCNPPNHHFLLPIQSFEKIALWKAGVMPIQYRRVNCLRDGGVRFAVAGRSFFLTVLISNVGGAGDVRSVKIKGTESGWLSMGRNWGQIWHINSDFRGQPLSFELTSSDGKTLTNYNVVPKEWDFGKTYTGKQFLL | Function: May cause loosening and extension of plant cell walls by disrupting non-covalent bonding between cellulose microfibrils and matrix glucans. No enzymatic activity has been found. May be required for rapid internodal elongation in deepwater rice during submergence (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 27551
Sequence Length: 257
Subcellular Location: Secreted
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O34456 | MFSKDKLPVILFLFLAGVINYLDRSALSIAAPFIQDDLTLSATQMGLIFSSFSIGYAIFNFLGGVASDRYGAKLTLFVAMVVWSLFSGAVALAFGFVSLLIIRILFGMGEGPLSATINKMVNNWFPPTQRASVIGVTNSGTPLGGAISGPIVGMIAVAFSWKVSFVLIMIIGLIWAVLWFKFVKEKPQETIKEAPAIKAETSPGEKIPLTFYLKQKTVLFTAFAFFAYNYILFFFLTWFPSYLVDERGLSVESMSVITVIPWILGFIGLAAGGFVSDYVYKKTARKGVLFSRKVVLVTCLFSSAVLIGFAGLVATTAGAVTLVALSVFFLYLTGAIYWAVIQDVVDQNNVGSVGGFMHFLANTAGIIGPALTGFIVDQTGTFSGAFLLAGGLAVFASLAVIRFVRPIIGKPAGTEAENPVSY | Function: Transport of aldohexuronates such as D-glucuronate and D-galacturonate.
Catalytic Activity: aldehydo-D-glucuronate(in) + H(+)(in) = aldehydo-D-glucuronate(out) + H(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 45314
Sequence Length: 422
Subcellular Location: Cell membrane
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P94774 | MFKIKGLRWYMIGLVTIGTVLGYLTRNAIAAAAPTLQEQLHISTQQYSYIIAAYSACYTIMQPVAGYVLDVLGTKVGYAMFAILWALFCAGTALANSWGGLAVARGAVGMAEAAMIPAGLKASSEWFPAKERSVAVGYFNVGSSIGGMLAPPLVVWAIMAHSWQMAFLITGALSLVWALCWLYFYKHPKDQKKLSTEEREYILSGQEAQHQAGNAKRMSAWQILRNRQFWGIALPRFLAEPAWGTFNAWIPLFMFKAYGFNLKEIAMFAWMPMLFADLGCILGGYMPMLFQKYFKVNLIVSRKLVVTLGALLMIGPGTIGLFTSPYVAIACCASAALPTSPCPVR | Function: Transport of D-galacturonate . Cannot transport the dimer digalacturonic acid . Uptake is an active process .
Catalytic Activity: aldehydo-D-galacturonate(out) + H(+)(out) = aldehydo-D-galacturonate(in) + H(+)(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 37870
Sequence Length: 345
Subcellular Location: Cell inner membrane
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P0AA79 | MRKIKGLRWYMIALVTLGTVLGYLTRNTVAAAAPTLMEELNISTQQYSYIIAAYSAAYTVMQPVAGYVLDVLGTKIGYAMFAVLWAVFCGATALAGSWGGLAVARGAVGAAEAAMIPAGLKASSEWFPAKERSIAVGYFNVGSSIGAMIAPPLVVWAIVMHSWQMAFIISGALSFIWAMAWLIFYKHPRDQKHLTDEERDYIINGQEAQHQVSTAKKMSVGQILRNRQFWGIALPRFLAEPAWGTFNAWIPLFMFKVYGFNLKEIAMFAWMPMLFADLGCILGGYLPPLFQRWFGVNLIVSRKMVVTLGAVLMIGPGMIGLFTNPYVAIMLLCIGGFAHQALSGALITLSSDVFGRNEVATANGLTGMSAWLASTLFALVVGALADTIGFSPLFAVLAVFDLLGALVIWTVLQNKPAIEVAQETHNDPAPQH | Function: Transport of aldohexuronates such as D-glucuronate and D-galacturonate.
Catalytic Activity: aldehydo-D-glucuronate(in) + H(+)(in) = aldehydo-D-glucuronate(out) + H(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 46892
Sequence Length: 432
Subcellular Location: Cell inner membrane
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O17670 | MLPDSEGQKLKTFLLGTGTTLDPSLDPTGNSNFSMATTSDSSTIWTALPASQPGDKDIPTVDLAAISEAYGSTSSTTSLTSSVTSQYQYNSYPQYAMYTSANPANYYQQVTANLRAGTTAFPYSLTTPSYYGSYPVDYTSAAAAYQNPYYTNLRGGTAAPYYNPLNATTAAAYASVASSVLGTDAVNLGTSSDGSTGVPSTVTSFSLKEKKPKVSKKKKTGSCSPGDETYARVFIWDIDDIAVISRNYLASVTHTNEFYARAANSVSHLMERIALNNFADVNEFLEGDITNIEDAVVDETTMDSGPIDNLRGLDVMRRVAPKYSAFRQFYTENSTKNDVAGFKQEQNGFNFELLERVGFGAREATELYQSAIQLQTLPNFGQRWPCAQRCMDLVVEKSKLSAEKYANVVLSNDGLVLGAAQLMISGLNSSVPVENIYSISKQGKESVFEKIQSRFGKKCSFICITSGDTANSAKRLNIPVWPLNSNTDLDKLYSALDNFLLGG | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Tyrosine protein phosphatase (By similarity). Acts probably as a transcription regulator in the embryonic and postembryonic development of several tissues including pharynx, vulva and gonads . Required for the development of anterior tissues during late embryogenesis . Together with ceh-34, required to specify the coelomocyte fate in embryonic and postembryonic precursors . In the anterior part of the embryo, prevents apoptosis in cells that are not fated to die . Together with ceh-34 activates proapoptotic factor egl-1 expression to promote motor neuron M4 sister cell apoptosis . Also promotes apoptosis of I1 pharyngeal neuron sister cell . Plays a role in locomotion and fertility . May play a role in resistance to heat and oxidative stresses . May cooperate with the transcription factors vab-3 and ceh-32 to repress transcription factor ets-5 expression in non BAG neuronal cells .
Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Sequence Mass (Da): 54522
Sequence Length: 503
Subcellular Location: Nucleus
EC: 3.1.3.48
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Q9YHA0 | RKLAFRYRRVKEIYNTYKNNVGGLLGPAKREAWLQLRAEIEALTDSWLTLALKALTLIHSRTNCVNILVTTTQLIPALAKVLLYGLGVVFPIENIYSATKIGKESCFERIIQRFGRKVV | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Functions both as protein phosphatase and as transcriptional coactivator for SIX1, and probably also for other transcription factors of this family. Tyrosine phosphatase that dephosphorylates 'Tyr-142' of histone H2AX (H2AXY142ph) and promotes efficient DNA repair via the recruitment of DNA repair complexes containing MDC1. 'Tyr-142' phosphorylation of histone H2AX plays a central role in DNA repair and acts as a mark that distinguishes between apoptotic and repair responses to genotoxic stress. Its function as histone phosphatase may contribute to its function in transcription regulation during organogenesis. Has also phosphatase activity with proteins phosphorylated on Ser and Thr residues (in vitro). Required for normal embryonic development of the skeleton, kidneys and ears (By similarity).
Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Sequence Mass (Da): 13549
Sequence Length: 119
Subcellular Location: Cytoplasm
EC: 3.1.3.16
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P97767 | MEMQDLTSPHSRLSGSSESPSGPKLDSSHINSTSMTPNGTEVKTEPMSSSEIASTAADGSLDSFSGSALGSSSFSPRPAHPFSPPQIYPSKSYPHILPTPSSQTMAAYGQTQFTTGMQQATAYATYPQPGQPYGISSYGALWAGIKTESGLSQSQSPGQTGFLSYGTSFGTPQPGQAPYSYQMQGSSFTTSSGLYSGNNSLTNSSGFNSSQQDYPSYPGFGQGQYAQYYNSSPYPAHYMTSSNTSPTTPSTNATYQLQEPPSGVTSQAVTDPTAEYSTIHSPSTPIKETDSERLRRGSDGKSRGRGRRNNNPSPPPDSDLERVFIWDLDETIIVFHSLLTGSYANRYGRDPPTSVSLGLRMEEMIFNLADTHLFFNDLEECDQVHIDDVSSDDNGQDLSTYNFGTDGFPAAATSANLCLATGVRGGVDWMRKLAFRYRRVKEIYNTYKNNVGGLLGPAKREAWLQLRAEIEALTDSWLTLALKALSLIHSRTNCVNILVTTTQLIPALAKVLLYGLGIVFPIENIYSATKIGKESCFERIIQRFGRKVVYVVIGDGVEEEQGAKKHAMPFWRVSSHSDLMALHHALELEYL | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Functions both as protein phosphatase and as transcriptional coactivator for SIX1, and probably also for SIX2, SIX4 and SIX5 . Tyrosine phosphatase that dephosphorylates 'Tyr-142' of histone H2AX (H2AXY142ph) and promotes efficient DNA repair via the recruitment of DNA repair complexes containing MDC1. 'Tyr-142' phosphorylation of histone H2AX plays a central role in DNA repair and acts as a mark that distinguishes between apoptotic and repair responses to genotoxic stress . Its function as histone phosphatase may contribute to its function in transcription regulation during organogenesis . Has also phosphatase activity with proteins phosphorylated on Ser and Thr residues (in vitro). Required for normal embryonic development of the craniofacial and trunk skeleton, kidneys and ears . Together with SIX1, it plays an important role in hypaxial muscle development; in this it is functionally redundant with EYA2 .
PTM: Sumoylated with SUMO1.
Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Sequence Mass (Da): 64324
Sequence Length: 591
Subcellular Location: Cytoplasm
EC: 3.1.3.16
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Q58DB6 | MLELLVSASLTVNSDRPGKLKPSRADADVWTLSDREGITTSARSVSQLFARPCPRVPPGQPPSAMAAYSQTQYSAGIQQATPYTAYPPPAQAYGIPSYSIKTEDSLNHSPGQSGFLSYGSSFSTPASGQSPYTYQMHGTAGIYQGANGLTNAAGFGTVHQDYPSYPGFPQSQYSQYYSSSYNPPYVPASSICPSPLSTSTYVLQEASHNIPSQSSESLGGEYNTHNGPSTPAKEGDTDRPPRASDGKLRGRSKRSSDPSPAGDNEIERVFVWDLDETIIIFHSLLTGTFASRYGKDTTASVRIGLMMEEMIFNLADTHLFFNDLEDCDQIHVDDVSSDDNGQDLSTYNFSADGFHSSAPGANLCLGSGVHGGVDWMRKLAFRYRRVKEMYNTYKNNVGGLIGAPKRETWLQLRAELEALTDLWLTHSLKALNLINSRPNCVNVLVTTTQLIPALAKVLLYGLGSVFPIENIYSATKTGKESCFERIMQRFGRKAVYIVIGDGVEEEQGAKKHNMPFWRISCHADLEALRHALELEYL | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Functions both as protein phosphatase and as transcriptional coactivator for SIX1, and probably also for SIX2, SIX4 and SIX5. Tyrosine phosphatase that dephosphorylates 'Tyr-142' of histone H2AX (H2AXY142ph) and promotes efficient DNA repair via the recruitment of DNA repair complexes containing MDC1. 'Tyr-142' phosphorylation of histone H2AX plays a central role in DNA repair and acts as a mark that distinguishes between apoptotic and repair responses to genotoxic stress. Its function as histone phosphatase may contribute to its function in transcription regulation during organogenesis. Plays an important role in hypaxial muscle development together with SIX1 and DACH2; in this it is functionally redundant with EYA1.
Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Sequence Mass (Da): 58807
Sequence Length: 537
Subcellular Location: Cytoplasm
EC: 3.1.3.48
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O00167 | MVELVISPSLTVNSDCLDKLKFNRADAAVWTLSDRQGITKSAPLRVSQLFSRSCPRVLPRQPSTAMAAYGQTQYSAGIQQATPYTAYPPPAQAYGIPSYSIKTEDSLNHSPGQSGFLSYGSSFSTSPTGQSPYTYQMHGTTGFYQGGNGLGNAAGFGSVHQDYPSYPGFPQSQYPQYYGSSYNPPYVPASSICPSPLSTSTYVLQEASHNVPNQSSESLAGEYNTHNGPSTPAKEGDTDRPHRASDGKLRGRSKRSSDPSPAGDNEIERVFVWDLDETIIIFHSLLTGTFASRYGKDTTTSVRIGLMMEEMIFNLADTHLFFNDLEDCDQIHVDDVSSDDNGQDLSTYNFSADGFHSSAPGANLCLGSGVHGGVDWMRKLAFRYRRVKEMYNTYKNNVGGLIGTPKRETWLQLRAELEALTDLWLTHSLKALNLINSRPNCVNVLVTTTQLIPALAKVLLYGLGSVFPIENIYSATKTGKESCFERIMQRFGRKAVYVVIGDGVEEEQGAKKHNMPFWRISCHADLEALRHALELEYL | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Functions both as protein phosphatase and as transcriptional coactivator for SIX1, and probably also for SIX2, SIX4 and SIX5 . Tyrosine phosphatase that dephosphorylates 'Tyr-142' of histone H2AX (H2AXY142ph) and promotes efficient DNA repair via the recruitment of DNA repair complexes containing MDC1. 'Tyr-142' phosphorylation of histone H2AX plays a central role in DNA repair and acts as a mark that distinguishes between apoptotic and repair responses to genotoxic stress . Its function as histone phosphatase may contribute to its function in transcription regulation during organogenesis. Plays an important role in hypaxial muscle development together with SIX1 and DACH2; in this it is functionally redundant with EYA1 .
Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Sequence Mass (Da): 59232
Sequence Length: 538
Subcellular Location: Cytoplasm
EC: 3.1.3.48
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O08575 | MLEVVTSPSLATSSDWSEHGAAVGTLSDREGIAKSAALSVPQLFVKSHPRVPPGQSSTAMAAYGQTQYSTGIQQAPPYTAYPTPAQAYGIPPYSIKTEDSLNHSPSQSGFLSYGPSFSTAPAGQSPYTYPVHSTAGLYQGANGLTNTAGFGSVHQDYPSYPSFSQNQYPQYFSPSYNPPYVPASSLCSSPLSTSTYVLQEAPHNVPSQSSESLAGDYNTHNGPSTPAKEGDTERPHRASDGKLRGRSKRNSDPSPAGDNEIERVFVWDLDETIIIFHSLLTGTFASRYGKDTTTSVRIGLMMEEMIFNLADTHLFFNDLEDCDQIHVDDVSSDDNGQDLSTYNFSTDGFHSTAPGASLCLGTGVHGGVDWMRKLAFRYRRVKEMYNTYRNNVGGLIGAPKRETWLQLRAELEALTDLWLTHSLKALNLINSRPNCVNVLVTTTQLIPALAKVLLYGLGSVFPIENIYSATKTGKESCFERIMQRFGRKAVYIVIGDGVEEEQGAKKHNMPFWRISCHADLEALRHALELEYL | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Functions both as protein phosphatase and as transcriptional coactivator for SIX1, and probably also for SIX2, SIX4 and SIX5 . Tyrosine phosphatase that dephosphorylates 'Tyr-142' of histone H2AX (H2AXY142ph) and promotes efficient DNA repair via the recruitment of DNA repair complexes containing MDC1. 'Tyr-142' phosphorylation of histone H2AX plays a central role in DNA repair and acts as a mark that distinguishes between apoptotic and repair responses to genotoxic stress. Its function as histone phosphatase may contribute to its function in transcription regulation during organogenesis (By similarity). Plays an important role in hypaxial muscle development together with SIX1 and DACH2; in this it is functionally redundant with EYA1 (By similarity).
Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Sequence Mass (Da): 58246
Sequence Length: 532
Subcellular Location: Cytoplasm
EC: 3.1.3.48
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Q2NKR7 | MGSLRGLRLVAGSCFRSCERDAFSSLRLTRNSDLKRTNGFCSKPQESPKPPDQHTYSHRVPLHKPTDWEKKILIWSGRFKKEDEIPETVSFEMLDAAKNKVRVKISYVMIALTVAGCVLMVIEGKKAARRNETLTSLNLEKKARLREEAAMKAKTE | Function: Proposed to be involved in regulation of apoptosis; the exact mechanism may differ between cell types/tissues. May be involved in hypoxia-induced cell death of transformed cells implicating cytochrome C release and caspase activation (such as CASP9) and inducing mitochondrial permeability transition. May be involved in hypoxia-induced cell death of neuronal cells probably by promoting release of AIFM1 from mitochondria to cytoplasm and its translocation to the nucleus; however, the involvement of caspases has been reported conflictingly.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 17737
Sequence Length: 156
Subcellular Location: Mitochondrion membrane
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Q96A26 | MGSLSGLRLAAGSCFRLCERDVSSSLRLTRSSDLKRINGFCTKPQESPGAPSRTYNRVPLHKPTDWQKKILIWSGRFKKEDEIPETVSLEMLDAAKNKMRVKISYLMIALTVVGCIFMVIEGKKAAQRHETLTSLNLEKKARLKEEAAMKAKTE | Function: Proposed to be involved in regulation of apoptosis; the exact mechanism may differ between cell types/tissues . May be involved in hypoxia-induced cell death of transformed cells implicating cytochrome C release and caspase activation (such as CASP9) and inducing mitochondrial permeability transition . May be involved in hypoxia-induced cell death of neuronal cells probably by promoting release of AIFM1 from mitochondria to cytoplasm and its translocation to the nucleus; however, the involvement of caspases has been reported conflictingly (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 17342
Sequence Length: 154
Subcellular Location: Mitochondrion membrane
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Q9D6U8 | MWSLGGLRLAAGHCLRLYERNASSSLRFTRNTDLKRINGFCTKPQESPKTPTQSYRHGVPLHKPTDFEKKILLWSGRFKKEEEIPETISFEMLDAAKNKLRVKVSYLMIALTVAGCIYMVIEGKKAAKRHESLTSLNLERKARLREEAAMKAKTD | Function: Proposed to be involved in regulation of apoptosis; the exact mechanism may differ between cell types/tissues . May be involved in hypoxia-induced cell death of transformed cells implicating cytochrome C release and caspase activation (such as CASP9) and inducing mitochondrial permeability transition . May be involved in hypoxia-induced cell death of neuronal cells probably by promoting release of AIFM1 from mitochondria to cytoplasm and its translocation to the nucleus; however, the involvement of caspases has been reported conflictingly .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 17725
Sequence Length: 155
Subcellular Location: Mitochondrion membrane
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Q4QQV3 | MWSLRGLRLAAGHCFRLCERNVSSPLRLTRNTDLKRINGFCTKPQESPKAPTQSYRHRVPLHKPTDFEKKILLWSGRFKKEEEIPETISFEMLDAAKNKIRVKVSYLMIALTVAGCVYMVIEGKKAAKRHESLTSLNLERKARLREEAAMKAKAD | Function: Proposed to be involved in regulation of apoptosis; the exact mechanism may differ between cell types/tissues. May be involved in hypoxia-induced cell death of transformed cells implicating cytochrome C release and caspase activation (such as CASP9) and inducing mitochondrial permeability transition. May be involved in hypoxia-induced cell death of neuronal cells probably by promoting release of AIFM1 from mitochondria to cytoplasm and its translocation to the nucleus; however, the involvement of caspases has been reported conflictingly.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 17827
Sequence Length: 155
Subcellular Location: Mitochondrion membrane
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Q9A8G9 | MGRSAFGSRTRMTAFVDLAARLAAEPADAALKDVVLTIAETCAQISRVVASGALSGSLGAAGSTNVQDEEQKKLDVITNDMLSDALKACGPVAGLASEELEEVEPTGRVGGYLVTFDPLDGSSNIDVNVSVGTIFSVLPAPAGHAPTEGDFLQPGRNQVAAGYAVYGPQTMLVVTLSGGVNGFTLSADGRWLLTHPDLAIKPDTAEFAINMSNQRHWAPAVRRYIDGCLQGKDGARGKNFNMRWVASMVADVHRIMMRGGVFMYPWDAREPDKPGKLRLMYEANPMSLLAERAGGKSIEGLNEILDINPAKLHQRVPVVLGSANEVEVIRAEMRAG | Cofactor: Binds 2 magnesium ions per subunit.
Catalytic Activity: beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-phosphate + phosphate
Sequence Mass (Da): 35734
Sequence Length: 336
Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Subcellular Location: Cytoplasm
EC: 3.1.3.11
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Q8KFG8 | MNKLTTIESHFLQLQKRYPEINSEVTDLLNDVAFAAKLVRREVVRAGLADILGLAGSTNVQGEEVKKLDLFANERLINAIGQHGRFAIMGSEENEEIIKPPKFESGEYVLLFDPLDGSSNIDVNVSVGTIFSIYRLKSGEPSQASLEDCLQKGADQIAAGYVIYGSSVMMVYTTGHGVHGFTYDQTVGEFLLSHENITTPEHGKYYSVNEGSWQEFNDGTKRFLDYLKEEDKATGRPYSTRYIGSFVADFHRNLLTGGVFVYPATKKHKNGKLRLMYEANPMAFICEQAGGRATDGYRRILDIEPKELHQRTPLYIGSKNDVLIAEEFEQGKR | Cofactor: Binds 2 magnesium ions per subunit.
Catalytic Activity: beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-phosphate + phosphate
Sequence Mass (Da): 37311
Sequence Length: 333
Pathway: Carbohydrate biosynthesis; Calvin cycle.
Subcellular Location: Cytoplasm
EC: 3.1.3.11
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A8AMG4 | MKTLGEFIVEKQHEFSHATGELTALLSAIKLGAKIIHRDINKAGLVDILGASGAENVQGEVQQKLDLFANEKLKAALKARDIVAGIASEEEDEIVVFEGCEHAKYVVLMDPLDGSSNIDVNVSVGTIFSIYRRVTPVGTPVTEEDFLQPGNKQVAAGYVVYGSSTMLVYTTGCGVHAFTYDPSLGVFCLCQERMRFPEKGNTYSINEGNYIKFPNGVKKYIKFCQEEDKSTNRPYTSRYIGSLVADFHRNLLKGGIYLYPSTASHPEGKLRLLYECNPMAFLAEQAGGKASDGKERILDITPESLHQRRPFFVGTDHMVEDVERFIREFPDA | Cofactor: Binds 2 magnesium ions per subunit.
Catalytic Activity: beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-phosphate + phosphate
Sequence Mass (Da): 36805
Sequence Length: 332
Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Subcellular Location: Cytoplasm
EC: 3.1.3.11
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A7MM48 | MKTLGEFIVEKQHEFSHATGELTALLSAIKLGAKIIHRDINKAGLVDILGASGVENVQGETQQKLDLFANEKLKAALKARDIVAGIASEEEDEIVVFEGCEHAKYVVLMDPLDGSSNIDVNVSVGTIFSIYRRVTPVGTPVTMEDFLQPGSQQVAAGYVVYGSSTMLVYTTGCGVHAFTYDPSLGVFCLCQERMRFPQSGNTYSINEGNYIKFPMGVKKYIKYCQEEDKATQRPYTSRYIGSLVADFHRNLLKGGIYLYPSTASHPEGKLRLLYECNPMAFLAEQAGGKASDGKQRILDIKPDSLHQRRPFFVGTEQMVNDVERFIREFPDA | Cofactor: Binds 2 magnesium ions per subunit.
Catalytic Activity: beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-phosphate + phosphate
Sequence Mass (Da): 36801
Sequence Length: 332
Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Subcellular Location: Cytoplasm
EC: 3.1.3.11
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B2FU10 | MSRTSLTRFLIQEQHAGRINADLRQLIAVVARACTSISIAVSKGALGGVLGDAGTGNVQGEAQKKLDVISNEILLEANAWGGHLAACASEEMDHSQPVPDIYPRGDFLLLFDPLDGSSNIDVNVSVGTIFSVLRCPTNVELPGDDAFLQPGSKQIAAGYCIYGPSTQLVLTVGHGTHAFTLDREKGEFVLTTENMQIPAATQEFAINMSNQRHWEAPMQAYVGDLLAGKEGTRGKNFNMRWIASMVADVHRILTRGGIFIYPWDKKDPSKAGKLRLMYEANPMGLLVEQAGGAAWTGRERILDIQPDQLHQRVPVFLGSREEVAEAVRYHHAHDNAQG | Cofactor: Binds 2 magnesium ions per subunit.
Catalytic Activity: beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-phosphate + phosphate
Sequence Mass (Da): 36797
Sequence Length: 338
Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Subcellular Location: Cytoplasm
EC: 3.1.3.11
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Q9I8L5 | MAFSGTWQVYAQENYEEFLRAISLPEEVIKLAKDVKPVTEIQQNGSDFTITSKTPGKTVTNSFTIGKEAEITTMDGKKLKCIVKLDGGKLVCRTDRFSHIQEIKAGEMVETLTVGGTTMIRKSKKI | Function: Binds hydrophobic ligands, such as cholate, in the cytoplasm. May be involved in intracellular lipid transport (By similarity). Binds one cholate per subunit.
Sequence Mass (Da): 14004
Sequence Length: 126
Domain: Forms a beta-barrel structure that accommodates hydrophobic ligands in its interior.
Subcellular Location: Cytoplasm
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P00743 | MAGLLHLVLLSTALGGLLRPAGSVFLPRDQAHRVLQRARRANSFLEEVKQGNLERECLEEACSLEEAREVFEDAEQTDEFWSKYKDGDQCEGHPCLNQGHCKDGIGDYTCTCAEGFEGKNCEFSTREICSLDNGGCDQFCREERSEVRCSCAHGYVLGDDSKSCVSTERFPCGKFTQGRSRRWAIHTSEDALDASELEHYDPADLSPTESSLDLLGLNRTEPSAGEDGSQVVRIVGGRDCAEGECPWQALLVNEENEGFCGGTILNEFYVLTAAHCLHQAKRFTVRVGDRNTEQEEGNEMAHEVEMTVKHSRFVKETYDFDIAVLRLKTPIRFRRNVAPACLPEKDWAEATLMTQKTGIVSGFGRTHEKGRLSSTLKMLEVPYVDRSTCKLSSSFTITPNMFCAGYDTQPEDACQGDSGGPHVTRFKDTYFVTGIVSWGEGCARKGKFGVYTKVSNFLKWIDKIMKARAGAAGSRGHSEAPATWTVPPPLPL | Function: Factor Xa is a vitamin K-dependent glycoprotein that converts prothrombin to thrombin in the presence of factor Va, calcium and phospholipid during blood clotting.
PTM: The vitamin K-dependent, enzymatic carboxylation of some glutamate residues allows the modified protein to bind calcium.
Catalytic Activity: Selective cleavage of Arg-|-Thr and then Arg-|-Ile bonds in prothrombin to form thrombin.
Sequence Mass (Da): 54510
Sequence Length: 492
Subcellular Location: Secreted
EC: 3.4.21.6
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P25155 | MAGRLLLLLLCAALPDELRAEGGVFIKKESADKFLERTKRANSFLEEMKQGNIERECNEERCSKEEAREAFEDNEKTEEFWNIYVDGDQCSSNPCHYGGQCKDGLGSYTCSCLDGYQGKNCEFVIPKYCKINNGDCEQFCSIKKSVQKDVVCSCTSGYELAEDGKQCVSKVKYPCGKVLMKRIKRSVILPTNSNTNATSDQDVPSTNGSILEEVFTTTTESPTPPPRNGSSITDPNVDTRIVGGDECRPGECPWQAVLINEKGEEFCGGTILNEDFILTAAHCINQSKEIKVVVGEVDREKEEHSETTHTAEKIFVHSKYIAETYDNDIALIKLKEPIQFSEYVVPACLPQADFANEVLMNQKSGMVSGFGREFEAGRLSKRLKVLEVPYVDRSTCKQSTNFAITENMFCAGYETEQKDACQGDSGGPHVTRYKDTYFVTGIVSWGEGCARKGKYGVYTKLSRFLRWVRTVMRQK | Function: Factor Xa is a vitamin K-dependent glycoprotein that converts prothrombin to thrombin in the presence of factor Va, calcium and phospholipid during blood clotting. VAP cleaves the fusion proteins of Sendai virus, NDV, and influenza virus a at a specific single arginine-containing site, and plays a key role in the viral spreading in the allantoic sac.
PTM: The vitamin K-dependent, enzymatic carboxylation of some glutamate residues allows the modified protein to bind calcium.
Catalytic Activity: Selective cleavage of Arg-|-Thr and then Arg-|-Ile bonds in prothrombin to form thrombin.
Sequence Mass (Da): 53142
Sequence Length: 475
Subcellular Location: Secreted
EC: 3.4.21.6
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P00742 | MGRPLHLVLLSASLAGLLLLGESLFIRREQANNILARVTRANSFLEEMKKGHLERECMEETCSYEEAREVFEDSDKTNEFWNKYKDGDQCETSPCQNQGKCKDGLGEYTCTCLEGFEGKNCELFTRKLCSLDNGDCDQFCHEEQNSVVCSCARGYTLADNGKACIPTGPYPCGKQTLERRKRSVAQATSSSGEAPDSITWKPYDAADLDPTENPFDLLDFNQTQPERGDNNLTRIVGGQECKDGECPWQALLINEENEGFCGGTILSEFYILTAAHCLYQAKRFKVRVGDRNTEQEEGGEAVHEVEVVIKHNRFTKETYDFDIAVLRLKTPITFRMNVAPACLPERDWAESTLMTQKTGIVSGFGRTHEKGRQSTRLKMLEVPYVDRNSCKLSSSFIITQNMFCAGYDTKQEDACQGDSGGPHVTRFKDTYFVTGIVSWGEGCARKGKYGIYTKVTAFLKWIDRSMKTRGLPKAKSHAPEVITSSPLK | Function: Factor Xa is a vitamin K-dependent glycoprotein that converts prothrombin to thrombin in the presence of factor Va, calcium and phospholipid during blood clotting.
PTM: The vitamin K-dependent, enzymatic carboxylation of some glutamate residues allows the modified protein to bind calcium.
Catalytic Activity: Selective cleavage of Arg-|-Thr and then Arg-|-Ile bonds in prothrombin to form thrombin.
Sequence Mass (Da): 54732
Sequence Length: 488
Subcellular Location: Secreted
EC: 3.4.21.6
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P16930 | MSFIPVAEDSDFPIHNLPYGVFSTRGDPRPRIGVAIGDQILDLSIIKHLFTGPVLSKHQDVFNQPTLNSFMGLGQAAWKEARVFLQNLLSVSQARLRDDTELRKCAFISQASATMHLPATIGDYTDFYSSRQHATNVGIMFRDKENALMPNWLHLPVGYHGRASSVVVSGTPIRRPMGQMKPDDSKPPVYGACKLLDMELEMAFFVGPGNRLGEPIPISKAHEHIFGMVLMNDWSARDIQKWEYVPLGPFLGKSFGTTVSPWVVPMDALMPFAVPNPKQDPRPLPYLCHDEPYTFDINLSVNLKGEGMSQAATICKSNFKYMYWTMLQQLTHHSVNGCNLRPGDLLASGTISGPEPENFGSMLELSWKGTKPIDLGNGQTRKFLLDGDEVIITGYCQGDGYRIGFGQCAGKVLPALLPS | Catalytic Activity: 4-fumarylacetoacetate + H2O = acetoacetate + fumarate + H(+)
Sequence Mass (Da): 46374
Sequence Length: 419
Pathway: Amino-acid degradation; L-phenylalanine degradation; acetoacetate and fumarate from L-phenylalanine: step 6/6.
EC: 3.7.1.2
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Q17449 | MIFYLVLLVLGAIAFYVHFSNNRKKLIERLEIVAQRRRDDLSKNVEQARKAADKLDTQRRDWIGSLDFEQLRDELQRGHVTCVEAIRAYFHKAILAHEKTNAVTCFILDAERQAEELDEQAKLPYYVKPPLFGVPLSLKECLKVKGYDTTRGFVQDAYHPATEDSIQVEHYKKLGLIPFCQTNVPQSLLSYNCSNPLFGTTTNPYDSTRTCGGSSGGEGALIGAGGSLIGIGTDVGGSVRIPCHFTGTAGIKPSKMRFAHRGGGASVPGKPLIDANDGPMAKDVKTNVEFLRNVWGDIDFQSDRDPYCPPVHWNESVYSSEKKLRVGYYIDDGWFTPTPALQRAVLESKKHLEAAGHTVIPFYPPRLPSVMQLYFRAVCLDGGQYVLNKLLKDIIEPTIRFQVTLWMVPVWIQRILSYPVSLVFPRMGMLMQSLTRDTFELREAYADIEAYREEFVGLMMKDNLDVILCPASIMPAPQHDIPSKVVSGVSYTCLYNLLDFGAGVVPVTAVSKSDEEKLINEYPETDKWYQITKKATLGAVGMPIGVQVAAPPYREEAVLRTMREIEIAVTGK | Function: Catalyzes the hydrolysis of endogenous amidated lipids like anandamide (AEA or N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine) and eicosapentaneoyl ethanolamide (EPEA or (5Z,8Z,11Z,14Z,17Z-eicosapentaenoyl) ethanolamine), as well as other fatty amides, to their corresponding fatty acids, thereby regulating the signaling functions of these molecules . EPEA promotes dauer formation and may constitute a signal of high nutrient availability . Breakdown of EPEA may promote lifespan extension when nutrient availability is high . Facilitates axon regeneration after injury by degradating inhibitory compounds such as AEA . FAAH cooperates with PM20D1 in the hydrolysis of amino acid-conjugated fatty acids such as N-fatty acyl glycine and N-fatty acyl-L-serine, thereby acting as a physiological regulator of specific subsets of intracellular, but not of extracellular, N-fatty acyl amino acids (By similarity).
Catalytic Activity: H2O + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine = (5Z,8Z,11Z,14Z)-eicosatetraenoate + ethanolamine
Sequence Mass (Da): 64001
Sequence Length: 572
EC: 3.5.1.99
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O00519 | MVQYELWAALPGASGVALACCFVAAAVALRWSGRRTARGAVVRARQRQRAGLENMDRAAQRFRLQNPDLDSEALLALPLPQLVQKLHSRELAPEAVLFTYVGKAWEVNKGTNCVTSYLADCETQLSQAPRQGLLYGVPVSLKECFTYKGQDSTLGLSLNEGVPAECDSVVVHVLKLQGAVPFVHTNVPQSMFSYDCSNPLFGQTVNPWKSSKSPGGSSGGEGALIGSGGSPLGLGTDIGGSIRFPSSFCGICGLKPTGNRLSKSGLKGCVYGQEAVRLSVGPMARDVESLALCLRALLCEDMFRLDPTVPPLPFREEVYTSSQPLRVGYYETDNYTMPSPAMRRAVLETKQSLEAAGHTLVPFLPSNIPHALETLSTGGLFSDGGHTFLQNFKGDFVDPCLGDLVSILKLPQWLKGLLAFLVKPLLPRLSAFLSNMKSRSAGKLWELQHEIEVYRKTVIAQWRALDLDVVLTPMLAPALDLNAPGRATGAVSYTMLYNCLDFPAGVVPVTTVTAEDEAQMEHYRGYFGDIWDKMLQKGMKKSVGLPVAVQCVALPWQEELCLRFMREVERLMTPEKQSS | Function: Catalyzes the hydrolysis of endogenous amidated lipids like the sleep-inducing lipid oleamide ((9Z)-octadecenamide), the endocannabinoid anandamide (N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine), as well as other fatty amides, to their corresponding fatty acids, thereby regulating the signaling functions of these molecules . Hydrolyzes polyunsaturated substrate anandamide preferentially as compared to monounsaturated substrates . It can also catalyze the hydrolysis of the endocannabinoid 2-arachidonoylglycerol (2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol) . FAAH cooperates with PM20D1 in the hydrolysis of amino acid-conjugated fatty acids such as N-fatty acyl glycine and N-fatty acyl-L-serine, thereby acting as a physiological regulator of specific subsets of intracellular, but not of extracellular, N-fatty acyl amino acids (By similarity).
Catalytic Activity: H2O + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine = (5Z,8Z,11Z,14Z)-eicosatetraenoate + ethanolamine
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 63066
Sequence Length: 579
Subcellular Location: Endomembrane system
EC: 3.5.1.99
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O08914 | MVLSEVWTALSGLSGVCLACSLLSAAVVLRWTRSQTARGAVTRARQKQRAGLETMDKAVQRFRLQNPDLDSEALLALPLLQLVQKLQSGELSPEAVLFTYLGKAWEVNKGTNCVTSYLTDCETQLSQAPRQGLLYGVPVSLKECFSYKGHASTLGLSLNEGVTSESDCVVVQVLKLQGAVPFVHTNVPQSMLSYDCSNPLFGQTMNPWKPSKSPGGSSGGEGALIGSGGSPLGLGTDIGGSIRFPSAFCGICGLKPTGNRLSKSGLKSCVYGQTAVQLSVGPMARDVDSLALCMKALLCEDLFRLDSTIPPLPFREEIYRSSRPLRVGYYETDNYTMPTPAMRRAVMETKQSLEAAGHTLVPFLPNNIPYALEVLSAGGLFSDGGCSFLQNFKGDFVDPCLGDLVLVLKLPRWFKKLLSFLLKPLFPRLAAFLNSMCPRSAEKLWELQHEIEMYRQSVIAQWKAMNLDVVLTPMLGPALDLNTPGRATGAISYTVLYNCLDFPAGVVPVTTVTAEDDAQMEHYKGYFGDMWDNILKKGMKKGIGLPVAVQCVALPWQEELCLRFMREVERLMTPEKRPS | Function: Catalyzes the hydrolysis of endogenous amidated lipids like the endocannabinoid anandamide (N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine), as well as other fatty amides such as the taurine-conjugated fatty acids (a structural class of central nervous system (CNS) metabolites), to their corresponding fatty acids, thereby regulating the signaling functions of these molecules . FAAH cooperates with PM20D1 in the hydrolysis of amino acid-conjugated fatty acids such as N-fatty acyl glycine and N-fatty acyl-L-serine, thereby acting as a physiological regulator of specific subsets of intracellular, but not of extracellular, N-fatty acyl amino acids . It can also catalyze the hydrolysis of the endocannabinoid 2-arachidonoylglycerol (2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol) (By similarity).
Catalytic Activity: H2O + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine = (5Z,8Z,11Z,14Z)-eicosatetraenoate + ethanolamine
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 63221
Sequence Length: 579
Subcellular Location: Endoplasmic reticulum membrane
EC: 3.5.1.99
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P97612 | MVLSEVWTTLSGVSGVCLACSLLSAAVVLRWTGRQKARGAATRARQKQRASLETMDKAVQRFRLQNPDLDSEALLTLPLLQLVQKLQSGELSPEAVFFTYLGKAWEVNKGTNCVTSYLTDCETQLSQAPRQGLLYGVPVSLKECFSYKGHDSTLGLSLNEGMPSESDCVVVQVLKLQGAVPFVHTNVPQSMLSFDCSNPLFGQTMNPWKSSKSPGGSSGGEGALIGSGGSPLGLGTDIGGSIRFPSAFCGICGLKPTGNRLSKSGLKGCVYGQTAVQLSLGPMARDVESLALCLKALLCEHLFTLDPTVPPLPFREEVYRSSRPLRVGYYETDNYTMPSPAMRRALIETKQRLEAAGHTLIPFLPNNIPYALEVLSAGGLFSDGGRSFLQNFKGDFVDPCLGDLILILRLPSWFKRLLSLLLKPLFPRLAAFLNSMRPRSAEKLWKLQHEIEMYRQSVIAQWKAMNLDVLLTPMLGPALDLNTPGRATGAISYTVLYNCLDFPAGVVPVTTVTAEDDAQMELYKGYFGDIWDIILKKAMKNSVGLPVAVQCVALPWQEELCLRFMREVEQLMTPQKQPS | Function: Catalyzes the hydrolysis of endogenous amidated lipids like the sleep-inducing lipid oleamide ((9Z)-octadecenamide), the endocannabinoid anandamide (N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine), as well as other fatty amides, to their corresponding fatty acids, thereby regulating the signaling functions of these molecules . Hydrolyzes polyunsaturated substrate anandamide preferentially as compared to monounsaturated substrates . It can also catalyze the hydrolysis of the endocannabinoid 2-arachidonoylglycerol (2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol) . FAAH cooperates with PM20D1 in the hydrolysis of amino acid-conjugated fatty acids such as N-fatty acyl glycine and N-fatty acyl-L-serine, thereby acting as a physiological regulator of specific subsets of intracellular, but not of extracellular, N-fatty acyl amino acids (By similarity).
Catalytic Activity: H2O + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine = (5Z,8Z,11Z,14Z)-eicosatetraenoate + ethanolamine
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 63357
Sequence Length: 579
Subcellular Location: Endoplasmic reticulum membrane
EC: 3.5.1.99
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Q6GMR7 | MAPSFTARIQLFLLRALGFLIGLVGRAALVLGGPKFASKTPRPVTEPLLLLSGMQLAKLIRQRKVKCIDVVQAYINRIKDVNPMINGIVKYRFEEAMKEAHAVDQKLAEKQEDEATLENKWPFLGVPLTVKEAFQLQGMPNSSGLMNRRDAIAKTDATVVALLKGAGAIPLGITNCSELCMWYESSNKIYGRSNNPYDLQHIVGGSSGGEGCTLAAACSVIGVGSDIGGSIRMPAFFNGIFGHKPSPGVVPNKGQFPLAVGAQELFLCTGPMCRYAEDLAPMLKVMAGPGIKRLKLDTKVHLKDLKFYWMEHDGGSFLMSKVDQDLIMTQKKVVVHLETILGASVQHVKLKKMKYSFQLWIAMMSAKGHDGKEPVKFVDLLGDHGKHVSPLWELIKWCLGLSVYTIPSIGLALLEEKLRYSNEKYQKFKAVEESLRKELVDMLGDDGVFLYPSHPTVAPKHHVPLTRPFNFAYTGVFSALGLPVTQCPLGLNAKGLPLGIQVVAGPFNDHLTLAVAQYLEKTFGGWVCPGKF | Function: Catalyzes the hydrolysis of endogenous amidated lipids like the sleep-inducing lipid oleamide ((9Z)-octadecenamide), the endocannabinoid anandamide (N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine), as well as other fatty amides, to their corresponding fatty acids, thereby regulating the signaling functions of these molecules . Hydrolyzes monounsaturated substrate anandamide preferentially as compared to polyunsaturated substrates.
Catalytic Activity: H2O + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine = (5Z,8Z,11Z,14Z)-eicosatetraenoate + ethanolamine
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 58304
Sequence Length: 532
Subcellular Location: Membrane
EC: 3.5.1.99
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Q9U217 | MGNNFWSTWSPSQRIFSLIWPATILYLIMKLLIEKMWGKNRGAVERFQTRREALFDDFKSRSAPASLVNNPRIVKGNETAEQIETTFNEILKLDLIALKSALQTDKYNAYTVLCAFVWRAIDVNSEINCITEVIREAFNTAEALDDNYAQTGEKGQLFGLPFSVKSNFYMENYDVTVGLAKLLEQPKTTTCPMVQFLSDQGAVPFCLTNVPQGLLSYVSSNPIYGTTKNPWDFSRTPGGSSGGEAALLAAGGAAFGIGSDLAGSLRIPAAFCGLVTLKPTQDRLCVTDTHGGLPGRGRLGLSFGFYTRSVKEQEFLLGLIVGRSEYLELCPMSSPAKLEKHIEKDQKLVIGWFVDDGFNPVVPSNRRAVEETVKSLQAKGHQVVELKLADVSEEFPPFAVADMLFRNVMPDNGAYMSEMYAGEQYDEHMKLFIRLVCLKQNFLVSFLLRYGVMPFAKLALSKRLACIGSAYNSDLAACRQNQENTDSYKLQWIRYWKSKKIDALICPSFITPAQPFEYPAQLSNGAFITGLFNMLDVPAGVVPVSPVNQKDVDQLIDGFSTEGDLLLKKQREAARGTTGLPNAVQVVTLPNCEEMCLRVMRLVEESAEGVQRLQWRVGASAAPIDVENTPAGVVSSLEHFERVNLLH | Function: Converts monoacylglycerides to free fatty acids and glycerol . Hydrolyzes the endocannabinoid 2-arachidonoylglycerol (2-AG), and thereby regulates the degradation of endocannabinoid-related monoacylglycerides . Also hydrolyzes arachidonoyl ethanolamide (anandamide, or AEA), but with low efficiency . Plays a role in the regulation of longevity and resistance to oxidative stress .
Catalytic Activity: Hydrolyzes glycerol monoesters of long-chain fatty acids.
Sequence Mass (Da): 71729
Sequence Length: 647
EC: 3.1.1.23
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Q7XJJ7 | MGKYQVMKRASEVDLSTVKYKAETMKAPHLTGLSFKLFVNLLEAPLIGSLIVDYLKKDNGMTKIFRNTVIPEEPMFRPEFPSQEPEHDVVIVGEDESPIDRLETALKCLPQYDPSRSLHADPVSSFRYWKIRDYAYAYRSKLTTPLQVAKRIISIIEEFGYDKPPTPFLIRFDANEVIKQAEASTRRFEQGNPISVLDGIFVTIKDDIDCLPHPTNGGTTWLHEDRSVEKDSAVVSKLRSCGAILLGKANMHELGMGTTGNNSNYGTTRNPHDPKRYTGGSSSGSAAIVAAGLCSAALGTDGGGSVRIPSALCGITGLKTTYGRTDMTGSLCEGGTVEIIGPLASSLEDAFLVYAAILGSSSADRYNLKPSPPCFPKLLSHNGSNAIGSLRLGKYTKWFNDVSSSDISDKCEDILKLLSNNHGCKVVEIVVPELEEMRAAHVISIGSPTLSSLTPYCEAGKNSKLSYDTRTSFAIFRSFSASDYIAAQCLRRRLMEYHLNIFKDVDVIVTPTTGMTAPVIPPDALKNGETNIQVTTDLMRFVLAANLLGFPAISVPVGYDKEGLPIGLQIMGRPWAEATVLGLAAAVEELAPVTKKPAIFYDILNTN | Function: Catalyzes the hydrolysis of bioactive endogenous fatty acid amides to their corresponding acids . The hydrolysis of endogenous amidated lipids terminates their participation as lipid mediators in various signaling systems (Probable). Converts a wide range of N-acylethanolamines (NAEs) to their corresponding free fatty acids and ethanolamine . Can use oleamide as substrate, but not indole-3-acetamide, 1-naphtalene-acetamide, nicotinic acid amide or L-asparagine . Can use 2-arachidonylglycerol as substrate . Participates in the regulation of plant growth . Hydrolyzes N-dodecanoylethanolamine, which is has a growth inhibitory effect on seedling growth . Involved in plant defense signaling . Involved in abscisic acid (ABA) signaling through mechanisms that are independent of the catalytic activity . Involved in the regulation of flowering time . Catalyzes the hydrolysis of N-acyl L-homoserine lactones (AHLs), which are a class of signaling molecules produced by bacteria for quorum sensing . Accumulation of L-homoserine appears to encourage plant growth at low concentrations by stimulating transpiration, but higher concentrations inhibit growth by stimulating ethylene production .
Catalytic Activity: H2O + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine = (5Z,8Z,11Z,14Z)-eicosatetraenoate + ethanolamine
Sequence Mass (Da): 66079
Sequence Length: 607
Subcellular Location: Endoplasmic reticulum membrane
EC: 3.5.1.99
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Q1AMT3 | MAFTGKYQLESHENFEAFMKAVGVPDDEVEKGKDIKSISEIHQDGKDFKVTVTAGTKVILYSFTVGEECELETFTGDRAKTVVQMDGNKLTAFVKGIESVTELDGDTISNTLSFNGIVYKRISRRIS | Function: Binds free fatty acids and their coenzyme A derivatives, bilirubin, and some other small molecules in the cytoplasm. May be involved in intracellular lipid transport (By similarity).
Sequence Mass (Da): 14080
Sequence Length: 127
Domain: Forms a beta-barrel structure that accommodates hydrophobic ligands in its interior.
Subcellular Location: Cytoplasm
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P73574 | MTALTAQVALVTGASRGIGKATALALAATGMKVVVNYAQSSTAADAVVAEIIANGGEAIAVQANVANADEVDQLIKTTLDKFSRIDVLVNNAGITRDTLLLRMKLEDWQAVIDLNLTGVFLCTKAVSKLMLKQKSGRIINITSVAGMMGNPGQANYSAAKAGVIGFTKTVAKELASRGVTVNAVAPGFIATDMTENLNAEPILQFIPLARYGQPEEVAGTIRFLATDPAAAYITGQTFNVDGGMVMF | Function: Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP substrates to beta-hydroxyacyl-ACP products, the first reductive step in the elongation cycle of fatty acid biosynthesis (Probable). Is capable of reducing acetoacetyl-CoA, but less well than its paralog PhaB .
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] + NADP(+) = a 3-oxoacyl-[ACP] + H(+) + NADPH
Sequence Mass (Da): 25724
Sequence Length: 247
Pathway: Lipid metabolism; fatty acid biosynthesis.
EC: 1.1.1.100
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Q9X248 | MRLEGKVCLITGAASGIGKATTLLFAQEGATVIAGDISKENLDSLVKEAEGLPGKVDPYVLNVTDRDQIKEVVEKVVQKYGRIDVLVNNAGITRDALLVRMKEEDWDAVINVNLKGVFNVTQMVVPYMIKQRNGSIVNVSSVVGIYGNPGQTNYAASKAGVIGMTKTWAKELAGRNIRVNAVAPGFIETPMTEKLPEKARETALSRIPLGRFGKPEEVAQVILFLASDESSYVTGQVIGIDGGLVI | Function: Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP substrates to beta-hydroxyacyl-ACP products, the first reductive step in the elongation cycle of fatty acid biosynthesis.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] + NADP(+) = a 3-oxoacyl-[ACP] + H(+) + NADPH
Sequence Mass (Da): 26402
Sequence Length: 246
Pathway: Lipid metabolism; fatty acid biosynthesis.
EC: 1.1.1.100
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P55336 | MNLEGKIALVTGASRGIGRAIAELLVERGATVIGTATSEGGAAAISEYLGENGKGLALNVTDVESIEATLKTINDECGAIDILVNNAGITRDNLLMRMKDDEWNDIINTNLTPIYRMSKAVLRGMMKKRAGRIINVGSVVGTMGNAGQTNYAAAKAGVIGFTKSMAREVASRGVTVNTVAPGFIETDMTKALNDDQRAATLSNVPAGRLGDPREIASAVVFLASPEAAYITGETLHVNGGMYMV | Function: Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP substrates to beta-hydroxyacyl-ACP products, the first reductive step in the elongation cycle of fatty acid biosynthesis.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] + NADP(+) = a 3-oxoacyl-[ACP] + H(+) + NADPH
Sequence Mass (Da): 25519
Sequence Length: 244
Pathway: Lipid metabolism; fatty acid biosynthesis.
EC: 1.1.1.100
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P35731 | MHYLPVAIVTGATRGIGKAICQKLFQKGLSCIILGSTKESIERTAIDRGQLQSGLSYQRQCAIAIDFKKWPHWLDYESYDGIEYFKDRPPLKQKYSTLFDPCNKWSNNERRYYVNLLINCAGLTQESLSVRTTASQIQDIMNVNFMSPVTMTNICIKYMMKSQRRWPELSGQSARPTIVNISSILHSGKMKVPGTSVYSASKAALSRFTEVLAAEMEPRNIRCFTISPGLVKGTDMIQNLPVEAKEMLERTIGASGTSAPAEIAEEVWSLYSRTALET | Function: Involved in biosynthesis of fatty acids in mitochondria.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] + NADP(+) = a 3-oxoacyl-[ACP] + H(+) + NADPH
Sequence Mass (Da): 31184
Sequence Length: 278
Pathway: Lipid metabolism; fatty acid biosynthesis.
Subcellular Location: Mitochondrion
EC: 1.1.1.100
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O34746 | MKAGILGVGRYIPEKVLTNHDLEKMVETSDEWIRTRTGIEERRIAADDVFSSHMAVAAAKNALEQAEVAAEDLDMILVATVTPDQSFPTVSCMIQEQLGAKKACAMDISAACAGFMYGVVTGKQFIESGTYKHVLVVGVEKLSSITDWEDRNTAVLFGDGAGAAVVGPVSDDRGILSFELGADGTGGQHLYLNEKRHTIMNGREVFKFAVRQMGESCVNVIEKAGLSKEDVDFLIPHQANIRIMEAARERLELPVEKMSKTVHKYGNTSAASIPISLVEELEAGKIKDGDVVVMVGFGGGLTWGAIAIRWGR | Function: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Has some substrate specificity for branched chain acyl-CoA, determining the biosynthesis of branched-chain of fatty acids instead of straight-chain.
Catalytic Activity: (2S)-2-methylbutanoyl-CoA + H(+) + malonyl-[ACP] = (4S)-4-methyl-3-oxohexanoyl-[ACP] + CO2 + CoA
Sequence Mass (Da): 33732
Sequence Length: 312
Domain: The last Arg residue of the ACP-binding site is essential for the weak association between ACP/AcpP and FabH.
Pathway: Lipid metabolism; fatty acid biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.3.1.180
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Q8ABI8 | MDKINAVITGVGGYVPDYVLTNDEISKMVDTTDEWIMGRIGIKERHILNEEGLGTSYMARKAAKQLMQRTKSRPDDIDLVIVATTTSDYRFPSTASILCERLGLKNAFAFDMQAVCSGFLYAMETGANFIRSGKYKKIIIVGADKMSSVIDYTDRATCPIFGDGAAAFMLEPTTEEVGIMDSVLRTDGKGLPFLHIKAGGSVCPPSYYSLDHHLHYIYQEGRTVFKYAVANMSDSCEAIIARNHLTKEEVDWVIPHQANQRIITAVAQRLEVPSEKVMVNIERYGNTSAGTLPLCIWDFEKKLKKGDNLIFTAFGAGFAWGAVYVKWGYDPKEDA | Function: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids.
Catalytic Activity: acetyl-CoA + H(+) + malonyl-[ACP] = 3-oxobutanoyl-[ACP] + CO2 + CoA
Sequence Mass (Da): 37220
Sequence Length: 335
Domain: The last Arg residue of the ACP-binding site is essential for the weak association between ACP/AcpP and FabH.
Pathway: Lipid metabolism; fatty acid biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.3.1.180
|
Q88YZ4 | MPTYTKLTAMGQYVPGRVVDNDELAAIMDTSDEWIQAHTGIKTRHYAMNDENTSDLATQVAQQLLQKSGLAASAIDLILVTTITPDALTPATACLVQANIGADNAFAFDLSAACAGFTFGLATADKFIRSGQYQNVMVISAEVNSKMMDFQDRTAAVFFGDGAGGALLQATDNPDENSLIAEKLESQGNATVIHSGRVRPITEVAATNYPQTDAFYQVGRDVFQFATTVVPEQMRGLIASAQLTPSDLQYVICHQANLRIIEKIAANLALPMTKFPHNVDHYGNTSSAGVAMALANVFDTLTGPVLLTAFGGGLAYGSVLIKK | Function: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids.
Catalytic Activity: acetyl-CoA + H(+) + malonyl-[ACP] = 3-oxobutanoyl-[ACP] + CO2 + CoA
Sequence Mass (Da): 34391
Sequence Length: 323
Domain: The last Arg residue of the ACP-binding site is essential for the weak association between ACP/AcpP and FabH.
Pathway: Lipid metabolism; fatty acid biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.3.1.180
|
P72392 | MSKIKPSKGAPYARILGVGGYRPTRVVPNEVILEKIDSSDEWIRSRSGIETRHWAGPEETVAAMSVEASGKALADAGIDASRIGAVVVSTVSHFSQTPAIATEIADRLGTDKAAAFDISAGCAGFGYGLTLAKGMVVEGSAEYVLVIGVERLSDLTDLEDRATAFLFGDGAGAVVVGPSQEPAIGPTVWGSEGDKAETIKQTVSWDRFRIGDVSELPLDSEGNVKFPAITQEGQAVFRWAVFEMAKVAQQALDAAGISPDDLDVFIPHQANVRIIDSMVKTLKLPEHVTVARDIRTTGNTSAASIPLAMERLLATGDARSGDTALVIGFGAGLVYAATVVTLP | Function: Essential enzyme that catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain of fatty acids.
Catalytic Activity: acetyl-CoA + H(+) + malonyl-[ACP] = 3-oxobutanoyl-[ACP] + CO2 + CoA
Sequence Mass (Da): 35982
Sequence Length: 343
Domain: The last Arg residue of the ACP-binding site is essential for the weak association between ACP/AcpP and FabH.
Pathway: Lipid metabolism; fatty acid biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.3.1.180
|
Q9KQH5 | MYSKILGTGSYLPSQVRTNADLEKMVETSDEWIVARTGIRERRIAADNETVADMAFFAAQNAINMAGIDKHDIDMIIVATTSASHTFPSAACQVQGKLGIKGCPAFDLAAACSGFMYALSIADQHVKSGMCKHVLVIGADALSKTCDPTDRSTIILFGDGAGAVVVGASNEPGILSTHIHADGEFGDLLSLEVPVRGGDSDKWLHMAGNEVFKVAVTQLSKLVVDTLKANNMHKSELDWLVPHQANYRIISATAKKLSMSLDQVVITLDRHGNTSAATVPTALDEAVRDGRIQRGQMLLLEAFGGGFTWGSALVKF | Function: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids.
Catalytic Activity: acetyl-CoA + H(+) + malonyl-[ACP] = 3-oxobutanoyl-[ACP] + CO2 + CoA
Sequence Mass (Da): 33749
Sequence Length: 316
Domain: The last Arg residue of the ACP-binding site is essential for the weak association between ACP/AcpP and FabH.
Pathway: Lipid metabolism; fatty acid biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.3.1.180
|
Q24U40 | MVSVGIVGTGSYVPDKVLTNFDLEQMVDTNDQWIVSRTGIKERHIAEPETPVSELCYQAAVRALEDAKLAPEELDLVIVATITPDFVFPATACLVAERLGAKKAAGFDLQAACTGFLYGVATAAQFIATGIYKNALVIGGETLSKILNWEDRGTCILFGDGAGAAVLQQVEEGYGFLGYDLGMDGAGGSLLTMPGGGSMHPASAETVAKKMHTIQMAGSEVFKFAVRIMGETALKALDKAGLGIGDVDCLIPHQANTRIVDAAVKRLGIDAGKVVVNLDRYGNMSAASIPVALDEAARSGRLNYGDIMVMVGFGGGLTWGAAVVKWSKRGV | Function: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids.
Catalytic Activity: acetyl-CoA + H(+) + malonyl-[ACP] = 3-oxobutanoyl-[ACP] + CO2 + CoA
Sequence Mass (Da): 34706
Sequence Length: 331
Domain: The last Arg residue of the ACP-binding site is essential for the weak association between ACP/AcpP and FabH.
Pathway: Lipid metabolism; fatty acid biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.3.1.180
|
Q6AJF8 | MSVVILGTGSCLPEKIVTNKDLEKIVETNDEWIRTRTGICERRIAGPGEQAYILASRAAKNALDAAGLVAEDLDMIVVGTISAHMVMPSCACMIQQEIGAKKAFAFDVNAACSGFLYAMEVGSKYVATNPAMKVLCIGTETLSARTNQQDRNTSIIFADGAGAAVIGYEEGDRGILASKLFSDGSFGDILFLSGSESTNTDLRLGEYEGSHIHMEGREVFKHAVRAMEGAVNTIMEEVGVSPHEIKLLIPHQANIRIIKNLGERLGLSSEQVFVNIANYGNTSAASVPIALDEAVRGGKIESGDLVLLCSFGGGFTWGASLIRW | Function: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids.
Catalytic Activity: acetyl-CoA + H(+) + malonyl-[ACP] = 3-oxobutanoyl-[ACP] + CO2 + CoA
Sequence Mass (Da): 34580
Sequence Length: 324
Domain: The last Arg residue of the ACP-binding site is essential for the weak association between ACP/AcpP and FabH.
Pathway: Lipid metabolism; fatty acid biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.3.1.180
|
Q72CS6 | MTSPSLLRGFGAYAPERILTNADIESMVETTDEWITTRTGIRQRHVVAPGQTTSDLAVEAARAALADAALDTADITHVLVATCTPDASCPNTACIVARKLGMTGVMALDCNAACSGFLYGLELAQGIVAARPASRVLLVAAEALSLRCNWKDRTTCVLFGDGAGATVVTADVDATQGTAVLEDSIVTSDGSLGDLLTIGGGTANPYAIGDSVGEEYFVRMQGRDVFKHAVRSMTQVCNDLLARNGFTTEDVDLVIPHQANLRIIEAVGDRLGFASEKVFVNVHDFGNTSAASIPLALADARAQGRIRPGMRVLLTTFGGGFTWGAALLRF | Function: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids.
Catalytic Activity: acetyl-CoA + H(+) + malonyl-[ACP] = 3-oxobutanoyl-[ACP] + CO2 + CoA
Sequence Mass (Da): 34666
Sequence Length: 330
Domain: The last Arg residue of the ACP-binding site is essential for the weak association between ACP/AcpP and FabH.
Pathway: Lipid metabolism; fatty acid biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.3.1.180
|
Q2GH17 | MKRSTILGIGSYLPKKIVTNDELALTVETSDEWIVKRTGIKQRHIAENNEMTSDMAANAARLALTDACVHKDDIGLIIVATTTPDRTFPSCATIVQDKLECKNAFAFDIQAVCSGFVYAISIADNFIKSGQVNTALVIGAEIMSRILDWQDRSTCVLFGDGAGAVVLGNNSEKDSGIISTILHSDGAFCDLLYTTGGTAYNGHAGTICMNGTIVFEHAIEKLSASILEILDQNDLEINDVDWFVLHQANIRIIELVARRLKIPYEKMVVSVNWHGNTSAASIPLALSYAKSSGKLKKHDIAILAAIGGGFTWGTCLVRI | Function: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids.
Catalytic Activity: acetyl-CoA + H(+) + malonyl-[ACP] = 3-oxobutanoyl-[ACP] + CO2 + CoA
Sequence Mass (Da): 34493
Sequence Length: 319
Domain: The last Arg residue of the ACP-binding site is essential for the weak association between ACP/AcpP and FabH.
Pathway: Lipid metabolism; fatty acid biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.3.1.180
|
B9DVE9 | MTYSKISQAAHHLPEQVISNDDLSLILETNDQWISSRTGIKERRISRSENTSDLASRVAEKLLEKANIDATEIDFIIVATITGDSIMPSVAAKVQGTIGATHAFAFDMTAACSGFVFALAMADKLIRSASYQKGLVIGAEVLSKYLDWEDRSTAVLFGDGAGGVLVEACSEQHFMAESLHTDGSRGQNLTSGNNPLRSPFSDSEEASPFIKMDGRAIFDFAIRDVSKSIISLLEESSVTAEEIDYFLLHQANRRILDKMARKIGCPRDKFLENMMTYGNTSAASIPILLSESVEKGLILLDGSQKVLLSGFGGGLTWGSLIVKI | Function: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids.
Catalytic Activity: acetyl-CoA + H(+) + malonyl-[ACP] = 3-oxobutanoyl-[ACP] + CO2 + CoA
Sequence Mass (Da): 35151
Sequence Length: 324
Domain: The last Arg residue of the ACP-binding site is essential for the weak association between ACP/AcpP and FabH.
Pathway: Lipid metabolism; fatty acid biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.3.1.180
|
Q31N84 | MTRPGVGVAITGSGSAVPSTTLSNDQLSQLVETSDEWIRSRTGIGQRRVAQPQIESLSSLAAAAGQSALEAAGLEATSVDLILLATSTPDDLFGSACQVQAALGATQAVAFDLTAACSGFLFALVTGAQFIRSGAYRTVLVIGADVLSRWTDWSDRRTCVLFGDGAGAVVLQASEIDQLLGFEMRSDGSLNGCLTLAYQADNQSLLSDIEIAQGTYQPVAMNGQEVYRFAVKRVPEILEKTLFHAGIDRQEVDWLLLHQANQRILDAVADRLDISRDRVLSNLVNYGNTSSATIPLVLDEAVKAGKIQSGDLIAASGFGAGLSWGAALFRWGTVV | Function: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids.
Catalytic Activity: acetyl-CoA + H(+) + malonyl-[ACP] = 3-oxobutanoyl-[ACP] + CO2 + CoA
Sequence Mass (Da): 35383
Sequence Length: 335
Domain: The last Arg residue of the ACP-binding site is essential for the weak association between ACP/AcpP and FabH.
Pathway: Lipid metabolism; fatty acid biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.3.1.180
|
A5GP11 | MAGQSPPVLGVGLIGSGSAQAAQVISNDQLSQRVDTNDEWIRTRTGIGRRRVSTADQTLVDLAAEAGRSALTMAGRSPQDLDLILLATSTPDDLFGSAPRVQAELGATNAVAFDLTAACSGFLFALVTAAQYLRTGAMRRALVIGADQLSRFVDWDDRRSCVLFGDGAGAVVLEASDEDGLLGFLLHSDGARGAVLNLPANDTSAPLIAGAEHRAGGYRPIVMNGQEVYKFAVREVPAVLQSLLKRCDVSADQLDWLLLHQANQRILDAVADRLSVPGAKVLSNLAAYGNTSAATIPLMLDEAVRDGRVSSGDLLASSGFGAGLSWGAALLRWQGPT | Function: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids.
Catalytic Activity: acetyl-CoA + H(+) + malonyl-[ACP] = 3-oxobutanoyl-[ACP] + CO2 + CoA
Sequence Mass (Da): 35281
Sequence Length: 337
Domain: The last Arg residue of the ACP-binding site is essential for the weak association between ACP/AcpP and FabH.
Pathway: Lipid metabolism; fatty acid biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.3.1.180
|
P73951 | MNTLGSGLKIIGSGTAIADQSLTNQDLSNIVETSDEWIQSRTGMRQRYICSAQENLASLGVKAGQKALAMAGLQPEDLDLIILATSTPDDLFGTAAQIQGGLGATRAFAFDITAACSGFVVGLNVAAQFLRTGVYQRVLIVGGDVLSRWVDWSDRTTCVLFGDGAGAVVLQRQAQDNLLAFEMYTDGTGNGCLNLSYQANPQPLTAEKTVAQGTYQAITMNGREVYRFAVAKVPEIIEKVLFKAQLTTSDLDWVILHQANQRIMDAVGDRLGIPSEKIISNVGEYGNTSAASIPLALDQAVREGKIKEGDLIALAGFGAGLTWAASIVRW | Function: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids.
Catalytic Activity: acetyl-CoA + H(+) + malonyl-[ACP] = 3-oxobutanoyl-[ACP] + CO2 + CoA
Sequence Mass (Da): 35166
Sequence Length: 330
Domain: The last Arg residue of the ACP-binding site is essential for the weak association between ACP/AcpP and FabH.
Pathway: Lipid metabolism; fatty acid biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.3.1.180
|
C0QVH0 | MVVEPKILNNICITAHPLGCAKEVENHINYVKSQPKVKSNVKNALILGASGGYGLASRIAIAYGLGAKTMSVSFEKGATARRTATPGWYNNEAFSAFAKKDGIEDKNLILDAFLNASKEEVIKEAKTFFNGEKIDLLIYSLAAPVRMDESTGTLYRSSLKPIGKKYNGIGVDFLTEELLEVSIDPANEDDIKSTVKVMGGEDWKLWTDALLNADLLAENAINVAYSYIGPEMTKAVYREGTIGKAKDHLEATAHELDKEMQEKIKGHAYVSVNKAVVTRSSAVIPTVPLYIGILFKVMKNKGLHEGCIEQMYRLLNEKLYNGGEVPVDSDNRIRLDDWELREDVQKEVLDSWNKLTKDNLKEIADLALFRKDYMNMHGFDEEGIDYSQDVQI | Function: Involved in the fatty acid synthesis (FAS II). Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to a coenzyme A (CoA).
Catalytic Activity: a 2,3-saturated acyl-CoA + NAD(+) = a (2E)-enoyl-CoA + H(+) + NADH
Sequence Mass (Da): 43652
Sequence Length: 392
Pathway: Lipid metabolism; fatty acid biosynthesis.
EC: 1.3.1.44
|
Q62L02 | MIIKPRVRGFICVTTHPAGCAASVREQIAYVARRGPIERGPKKVLVIGASTGYGLAARIAAAFGVGAATLGVFFERAPADAKPGTAGWYNSAAFHDEAAARGLQATSVNGDAFSDEIKHKTIDAIRRDLGQVDLVVYSVAAPRRTHPKTGVTHQSTLKPIGHAVRLRGIDTDNEAIKETLLQPATPDEIADTVAVMGGEDWRMWIDALDAAGVLADGAKTTAFTYLGEQVTHDIYWNGSIGEAKKDLDRTVLALRGKLAARGGDARVSVLKAVVTQASSAIPMMPLYLSLLFKVMKARGTHEGCIEQVDGLLRDSLYSAQPHVDAEGRLRADRLELDPAVQARVLELWDQVTDDNLYTLTDFAGYKAEFLRLFGFGIDGVDYDAPVEPNVRIPNLIE | Function: Involved in the final reduction of the elongation cycle of fatty acid synthesis (FAS II). Catalyzes the NADH-dependent reduction of the carbon-carbon double bond in the enoyl moiety that is covalently linked to an acyl carrier protein (ACP). It is also able to reduce trans-2-dodecenoyl-CoA (DD-CoA).
Catalytic Activity: a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] + H(+) + NADH
Sequence Mass (Da): 42802
Sequence Length: 397
Pathway: Lipid metabolism; fatty acid biosynthesis.
EC: 1.3.1.9
|
Q8RD71 | MENKDIRKILPHRYPFLLVDRIIELEEGKRAVGIKNVTSNEPFFQGHFPDNPIMPGVLIVEALAQVAGIAVMNVEEFKGKLGLFAGIDKCRFKKVVRPGDQLILEVSIDSIRMGLVKAKGVAKVGEEIAATAELMFVMAEE | Function: Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O
Sequence Mass (Da): 15604
Sequence Length: 141
Subcellular Location: Cytoplasm
EC: 4.2.1.59
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A4XJ81 | MYDVTSILQILPHRYPFLLVDRIIEIEEGKKAKGIKNVTINEPFFQGHFPGNPVMPGVLIVEAMAQVGAVAILSKEEFKGKTPFFAGIDKVRFKKVVRPGDVLLIETELISLKGYIGKAKATAYVEGEVVCEGELLFAIK | Function: Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O
Sequence Mass (Da): 15476
Sequence Length: 140
Subcellular Location: Cytoplasm
EC: 4.2.1.59
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A0RMT3 | MIDVVEIQKILPHRYPFLLIDRVCELETGKSVYAYKNITIAEQIFEGHFPGHPIYPGVMIIEGMAQAGGILAFKSAEDPSGLSIENKVVYFMSIDRAKFRNPVKPGDKLEYRLEVLKHKGNVWVLDGKAYVDDKLVAEAELKAMIVDK | Function: Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O
Sequence Mass (Da): 16693
Sequence Length: 148
Subcellular Location: Cytoplasm
EC: 4.2.1.59
|
A1KRL1 | MDVQLPIEAKDIQKLIPHRYPFLQLDRITAFEPMKTLTAIKNVSINEPQFQGHFPDLPVMPGVLIIEAMAQACGTLAILSEGGRKENEFFFFAGIDEARFKRQVIPGDQLVFEVELLTSRRGIGKFNAVAKVDGQVAVEAIIMCAKRVV | Function: Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O
Sequence Mass (Da): 16613
Sequence Length: 149
Subcellular Location: Cytoplasm
EC: 4.2.1.59
|
Q3JCW5 | MDTLDIHEILKHLPHRYPFLLIDRVIECIPGKSLVAIKNVSYNEPYFQGHFPGLPIMPGVLILESLAQATGILAFKTTETMPSEEAIYYFAGIDRARFKRPVGPGDQMRLEVELVRSLRRLWKFTGRVTVDGSLVASAEVMCSYQETYK | Function: Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O
Sequence Mass (Da): 16931
Sequence Length: 149
Subcellular Location: Cytoplasm
EC: 4.2.1.59
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Q3SRI2 | MESPVRFEHVDIATILKTLPHRYPFLLIDRVLNIRADHSGIGVKNVTFNEPAFQGHFPERPVYPGVLMIEGMAQTAGVIGIMSVEGTEKPRAVYFLTIDKCKFRKPVMPGDIVEYHMRSIGRRKTMWWFHGDAKVNGTIVAEADVGAMLTD | Function: Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O
Sequence Mass (Da): 17011
Sequence Length: 151
Subcellular Location: Cytoplasm
EC: 4.2.1.59
|
Q04DN4 | MTATEIQKVLPHRYPMLMVDRVLELVSGERILAQKNVTINEEFFQGHFPGNPVMPGVLIVEALAQAGAIALLKMDRFAGKTPYFGGVDKVKFRRMVRPGDTLTLNVTLDKLKDNIGSAHALATVDGEKACSADLLFLIK | Function: Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O
Sequence Mass (Da): 15265
Sequence Length: 139
Subcellular Location: Cytoplasm
EC: 4.2.1.59
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Q67T91 | MEIIPHRHPFLLIDRVLELEPGRRVVAVKNVSMNEPVFQGHYPGNPIFPGVLILEAMAQAGAVAVLSQPEFAGKVPLFAGIDDARFRRPVLPGDQLRLEVEMVAMRRGLGVGKGMAYVGDELKAEATLKFALVDAATPEPAR | Function: Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O
Sequence Mass (Da): 15449
Sequence Length: 142
Subcellular Location: Cytoplasm
EC: 4.2.1.59
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Q3A554 | MTLEILDIMKLLPHRYPFLLVDRIEDLEPGKRAVGIKNVTINEPFFQGHYPGHPIMPGVLIIEAMAQVGGAVAAITAGDKDDQVPYFTGINKARFRRPVGPGDVLQLQLELLSSRRGLFVFSGKAYVDGNLVAEAELKAVFAPRSQD | Function: Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O
Sequence Mass (Da): 16156
Sequence Length: 147
Subcellular Location: Cytoplasm
EC: 4.2.1.59
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A0LPR6 | MDIAKIMGYLPHRYPFLLVDRILELTSEEIVGLKNVTINEPFFQGHFPGEPIMPGVLIIEALAQTGGVLAFTLVSDFRGKPIYFMGMDKVRFRKPVRPGDQLILKLKILKRRGPTFKMSAEAFVEEQLVAEAELLATIGAAKSEREA | Function: Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O
Sequence Mass (Da): 16459
Sequence Length: 147
Subcellular Location: Cytoplasm
EC: 4.2.1.59
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Q0AVV9 | MKKLELNTEEIMKILPHRYPFLLVDRIIELLPGERAVGIKNLSVNEPFFPGHFPGHPVMPGVLMIEAMAQVGACAILCDEKYQGRLGYLAGVDRIRFKRMAVPGDSLLITTEFTAIKGNIGKGKGQIKINEEMVCGGEFLFALG | Function: Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O
Sequence Mass (Da): 15900
Sequence Length: 144
Subcellular Location: Cytoplasm
EC: 4.2.1.59
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Q9WZQ8 | MNIDYVKSILPHRYPFLLVDGVIEESEDRIVAFKNISISDPVFQGHFPEYPIYPGVLIVEGLAQTAGILLLKSVEGIPLFLGIDEARFKKEVRPGDRLIYEVRKLGEKLGTVQVEGVAKVDDKIVAKARLLLGVKKK | Function: Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O
Sequence Mass (Da): 15300
Sequence Length: 137
Subcellular Location: Cytoplasm
EC: 4.2.1.59
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O32177 | MKEAVIVSGARTPVGKAKKGSLATVRPDDLGAICVKETLKRAGGYEGNIDDLIIGCATPEAEQGLNMARNIGALAGLPYTVPAITVNRYCSSGLQSIAYAAEKIMLGAYDTAIAGGAESMSQVPMMGHVTRPNLALAEKAPEYYMSMGHTAEQVAKKYGVSREDQDAFAVRSHQNAAKALAEGKFKDEIVPVEVTVTEIGEDHKPMEKQFVFSQDEGVRPQTTADILSTLRPAFSVDGTVTAGNSSQTSDGAAAVMLMDREKADALGLAPLVKFRSFAVGGVPPEVMGIGPVEAIPRALKLAGLQLQDIGLFELNEAFASQAIQVIRELGIDEEKVNVNGGAIALGHPLGCTGTKLTLSLIHEMKRRNEQFGVVTMCIGGGMGAAGVFELC | Function: Involved in the degradation of long-chain fatty acids.
Catalytic Activity: acetyl-CoA + an acyl-CoA = a 3-oxoacyl-CoA + CoA
Sequence Mass (Da): 41123
Sequence Length: 391
Pathway: Lipid metabolism; fatty acid beta-oxidation.
EC: 2.3.1.16
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P28793 | MIYEGKAITVTALESGIVELKFDLKGESVNKFNRLTLNELRQAVDAIKADASVKGVIVSSGKDVFIVGADITEFVENFKLPDAELIAGNLEANKIFSDFEDLNVPTVAAINGIALGGGLEMCLAADFRVMADSAKIGLPEVKLGIYPGFGGTVRLPRLIGVDNAVEWIASGKENRAEDALKVSAVDAVVTADKLGAAALDLIKRAISGELDYKAKRQPKLEKLKLNAIEQMMAFETAKGFVAGQAGPNYPAPVEAIKTIQKAANFGRDKALEVEAAGFAKLAKTSASNCLIGLFLNDQELKKKAKVYDKIAKDVKQAAVLGAGIMGGGIAYQSASKGTPILMKDINEHGIEQGLAEAAKLLVGRVDKGRMTPAKMAEVLNGIRPTLSYGDFGNVDLVVEAVVENPKVKQAVLAEVENHVREDAILASNTSTISISLLAKALKRPENFVGMHFFNPVHMMPLVEVIRGEKSSDLAVATTVAYAKKMGKNPIVVNDCPGFLVNRVLFPYFGGFAKLVSAGVDFVRIDKVMEKFGWPMGPAYLMDVVGIDTGHHGRDVMAEGFPDRMKDDRRSAIDALYEAKRLGQKNGKGFYAYEADKKGKQKKLVDSSVLEVLKPIVYEQRDVTDEDIINWMMIPLCLETVRCLEDGIVETAAEADMGLVYGIGFPLFRGGALRYIDSIGVAEFVALADQYAELGALYHPTAKLREMAKNGQSFFG | Function: Involved in the aerobic and anaerobic degradation of long-chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate.
Catalytic Activity: a (3S)-3-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + H(+) + NADH
Sequence Mass (Da): 77137
Sequence Length: 715
Pathway: Lipid metabolism; fatty acid beta-oxidation.
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Q87ZB2 | MIYEGKAITVKALESGIVELNFDLKGESVNKFNRLTLNELRQAVDAVKADASVKGVIVTSGKDVFIVGADITEFVDNFKLPEAELVAGNLEANRIFSDFEDLGVPTVVAINGIALGGGLEMCLAADYRVISSSARVGLPEVKLGLYPGFGGTVRLPRIIGADNAIEWIASGKENSAEDALKVGVVDAIVAPEKLQAAALDLIQRAISGEFDYKAKRQPKLDKLKLNAIEQMMAFETAKGFVAGQAGPNYPAPVEAIKTIQKAAIFGRDKALEIEAAGFVKMAKTSAAQSLIGLFLNDQELKKKAKGYDEVARDVKQAAVLGAGIMGGGIAYQSAVKGTPILMKDIREEAIQLGLNEASKLLGGRLEKGRLTAAKMAEALNAIRPTLSYGDFGNVDLVVEAVVENPKVKQAVLAEVEANVGENTILASNTSTISISLLAQALKRPENFVGMHFFNPVHMMPLVEVIRGEKSSEEAVATTVAYAKKMGKNPIVVNDCPGFLVNRVLFPYFGGFARLVSAGVDFVRIDKVMEKFGWPMGPAYLMDVVGIDTGHHGRDVMAEGFPDRMKDDRRSAVDALYEANRLGQKNGKGFYVYETDKKGKPKKVNDPAVLDVLKPIVYEQREVSDEDIINWMMIPLCLETVRCLEDGIVETAAEADMGLIYGIGFPPFRGGALRYIDSIGVAEFVALADRYAELGALYQPTAKLREMAANGQSFFGQASSEV | Function: Involved in the aerobic and anaerobic degradation of long-chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate.
Catalytic Activity: a (3S)-3-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + H(+) + NADH
Sequence Mass (Da): 77674
Sequence Length: 721
Pathway: Lipid metabolism; fatty acid beta-oxidation.
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Q9KT58 | MDNNNAFQLSFDEQHYAWLAIDVPGEKMNTLQAAFAEEMQAVFATLNEKRGQIKGLIIHSLKPDNFIAGADVRMLEACQSVHEAQALASQGQQMFQQLADLPFPVVAAIHGPCLGGGLELALACDYRVCTEDEVTRLGLPEVMLGLLPGSGGTQRLPRLIGLLPALDLILTGKQLRAKKAKKLGVVDACVPHSVLLDVAKRLLEEKGHKKRAQVTLPIKEKLLANTDLGRKLIFDQAAKKTQQKTRGNYPAAQAILEVIQYGLEKGMHAGLEYEAKRFAELVMTRESKALRSIFFATTEMKKDLGADAKPAPVAAVGVLGGGLMGAGISHVTVAKAKTSVRIKDVANDGVLNALNYNYKLFDKQRQRKILTKAQLQAQMSQLSGGTGFVGFDRCDVVIEAVFEDLKLKQQMVADIEANAKPTTIFATNTSSLPIHQIASQAQRPQNIVGLHYFSPVEKMPLVEVIPHATTSDETIATVVTLARKQGKTPIVVKDCAGFYVNRILAPYMNEAAQVLMAGEPIEKLDAALLDFGFPVGPITLLDEVGVDIGAKIMPILVKELGPRFQGPDVFDVLLKDNRKGRKSGKGFYTYKGSKKKEVDKSVYKLLKLTPESKLNDKEIAMRCLLPMLNEAVRCLDEGIIRSARDGDMGAIFGIGFPPFLGGPFRYMDTLGLTKVVEMMNQHTEKYGERFAPCDGLLTRAGLGEKFYP | Function: Catalyzes the formation of a hydroxyacyl-CoA by addition of water on enoyl-CoA. Also exhibits 3-hydroxyacyl-CoA epimerase and 3-hydroxyacyl-CoA dehydrogenase activities.
Catalytic Activity: a (3S)-3-hydroxyacyl-CoA = a (2E)-enoyl-CoA + H2O
Sequence Mass (Da): 77357
Sequence Length: 708
Pathway: Lipid metabolism; fatty acid beta-oxidation.
Subcellular Location: Cytoplasm
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