ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
A9KMC1 | MEQVYSVTQVNNYIKNMFVKDYVLNRIYMKGEVSNCKYHTSGHIYFTLKDETGQMACVLFAGYRTGLPFRLEEGQSVIVLGSISVYERDGKYQLYAKEIKLDGLGLLYERFELLKRKLNEEGLFDPSHKKTLVPYPRTVGIVTASTGAAIQDIINISKRRNPYVQLVLYPAKVQGEGAAKTIVAGIKALEAKGVDTIIVGRGGGSIEDLWAFNEEMVARAIFDCSIPIISAVGHETDITISDFVSDLRAPTPSAAAELAVPEIESLLSNLVDYHYSLVQCVMRKITMARSELEKKQLQLTHLSPVYALRQKRQYTIDLEN... | 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): 4492... |
Q88WM7 | MSESQQYLTVTALTQYLKRKFEVDPYLGKVYLTGEVSNYRPRPNTHQYFSLKDDHAKISAIMFKSAFAKVKFQPEEGMKVLVVGRIGLYEPSGSYQIYVERMEPDGVGALYQAYEQLKKKLAAEGLFSAPKKPLPRFPKRIAVVTSRSGAVIRDIITTTRRRFPIAQIVLFPSQVQGDAAAAEISRQIERANAQGDFDTLIIGRGGGSIEDLWPFNEEVVARAIAQSQLPVISSVGHETDTTIADLVADVRAATPTAAAELAVPVYNDVLLQLKQDQTRVFNAFQNFVQRDRQRLNKLQTSYVFTQPNRLYEGYLQKLDF... | 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): 5049... |
Q38XU8 | MVKPTDYLTVTALTQYLKAKFERDPYLDRVYLTGEISNFRLRPNAHQYFSLKDNKAKISAIMFKSAFEKVKFTPEEGMKVLIVGRISLYEASGNYQIYVERMEPDGLGALYQAYEQLKAKLATEGLFDAPKQPLVRFPKRIAVITSPSGAVIRDIITTTQRRYPIAQLVLFPAVVQGDGAADVLVERLKQVNEHGDFDTIIIGRGGGSIEDLWPFNEERVARAIVASQIPVISSVGHETDTTIADLVADVRAATPTAAAELATPVLTDEILKLQQQRLRLYQAFSKTVALNKKQLDHLQNSYVLKQPKRLYDGYLQNVDQ... | 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): 5069... |
Q5WY82 | MSSQLPILTVSQLNRQVKGFLENEIGLVHVEGEISNLSKPSSGHYYFTLKDSTAQIRCAFFKNRHSSSLLRNFNDGQQIVASGKLSLYEARGEYQLIVEEIVEAGMGILYQRFEELKIKLAREGLFNPERKKTLPRIPETIGIITSPTGAAIQDILSTLARRFPIARIIIYPSEVQGQAAPQQLVNALKLANTHKRCQVLILARGGGSIEDLWAFNDEYLARQIAISEIPVVSGIGHETDFTIADFVADYRAETPTAAATAVTPNCIELFNILDTAIYRLHDAIIRLVKGLQLKLNHLIDKIASPRQTISTYWQTLDYLE... | 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): 4965... |
Q6ADU9 | MRGTRVTETASAPRMAPGPPTLDDPWPVALLASKIRGWIERLGTAWVEGEITQWGVSGGNVYGKLKDLNEDATVGFTIWSSVKARIPADLKQGDRVIAAVKPNYWLKGGTLTMQVSDMRHVGLGDLLERLERLRAQLRAEGLFRPERKKRLPFLPHTIGLVTGKDSDAEKDVLRNAQLRWPQVRFRTVYAAVQGDRTVPEVTAALRELDADPEVEVIIVARGGGDFQNLLGFSDESLLRAAAGLSTPLVSAIGHEADRPLLDEVADLRASTPTDAAKRVVPDVAEELVRVHQARARIGTRLTHIIRHEIDRIGHLRTRPA... | 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): 4692... |
Q3AH76 | MSADRLPSYSVAELNTAIGSLLERGFAPRFLLEATVSRPQLKKGHLWLTLTDGSASISGVVWASKLAQLSYQPKDGDGVTVVGKLNFWAARASLTVQALDIRPSLSTVLRDFERVRQVLEQEGVIDPSRLRPLPSQPASIAVLTSVPSSALADMLRTAAERWPLTQLIVVPIPVQGSVAPTIINTLEAIAERTAELGLQALVLARGGGSREDLAVFDNEALCRLLANYPIPVVTGLGHEDDLTVADLVADHRAATPTAAIVALLPDREAERQGLTQRQSRLKDTLLGRILRERQRLQDRAVALQQQSPREKIMRKRQELI... | 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): 4218... |
Q0AZF4 | MKEILTVTELNSYIANLLDSDPFLGQLWLRGEISGFRLYQQSGHMYFTLKDEDSTISAVMFKSRARGLKFKPKDGMEVLLRASVSVFARQGKYQLYVEEMQPYGIGGLFLYLEELKKKLAAKGYFAPERKKAIPAFVQRVGIVTSQDGAALRDICRILKQRHPGVEVVLAHSSVQGSEAPGELAEGLRLLNSYAEVELIIIGRGGGSYEDLMAFNSELVVQAIYESNIPVISAVGHEVDFTLADLVADLRAATPSQAASLAVADMQALSRQLDNYQQRLLRAMQRKLLYYTEIIDRLMMKRIWKQPRSLLHMREELLSQL... | 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): 4603... |
Q47SR1 | MGMESSPESPQPVRVVLQAVGGWIGRLGRIWIEGQVAELHRRGGMAYITLRDPVANVSARVTCSIRVLRAADPPPEQGARVVVYAKPDFYVPRGTFSFQALEIRHVGLGELLARLERLRQALAAEGLFAESRKRKLPFLPGVVGLICGRDSAAERDVLENARRRWPAVRFEVREVAVQGDRAVPEVMAALEELDAHPEVDVIIIARGGGSLEDLLPFSDEALVRAVAAARTPVVSAIGHEQDTPLLDYVADLRASTPTDAAKKVVPDVGEQWELIRQLRDRARRVLEGGIAREEAWLASMRSRPVLANPVQEVERKIEQV... | 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): 4463... |
Q9X289 | MKDYTYSVTEINEYIKDLIEGDPYLTNVSVYGEISGVRPRKGHIFFSLVEENARLECVIFGGDNMGIRLQEGRMALVEGSVSVYIPHGTYRFICSNVRYLDQAGMYQIKFETTLKKLLEEGLLSRPKKTVPRFPRKIGIITSRDSAALQDVIRTARERKAPIEIYVFHTSVQGDSAREELIKALRKANEYDLDLVMIVRGGGSKEDLWVFNEEDVIREILRLRHPVVTGIGHEIDRVIADFVADVSMHTPTGAAEYVIPDASEIHEDLDSFFEKLITSLSNRFDMEERRLETLYFRLRMIGRRKLELNEFKIERVKELAA... | 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): 4535... |
B0K9E1 | MQLKALEVREITDYIKKMMDNDIILRNVRVKGEISNLKYHSTGIYFTLKDEIASLKCVMFNEYGKLLNFTLQDGMSVIVTGRISVYERNGTYQLYAQSIQSDGIGALYFAFNKLKEKLQKEGLFDSDKKKPIPKHPKKIAVVTSPTGAVIRDIITISRRRNPTVDILVVPVLVQGSSAADEICNALRILNKREDIDVIILARGGGSLEEIWPFNEEKVARCIYASRIPVVSAVGHETDFTISDFVADLRAPTPSAAAEIVVPDIKVYQRELFLLKTKLLTLMTAELNRKKKEFEGLKRALYLNSPTKKSEILRHKVENLT... | 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): 4548... |
B8GP32 | MAVTDRDIFTVTRLNQAVQGLLEGTFPLIWVEGELSSVSRPASGHLYFTLKDSGAQVRCALFRNRAQLMRFRPADGMQVLVRARVGLYAPRGDYQLIVEHMEEAGDGALRRAFEELKQRLEREGLFDAERKRPLPRFPRRLGVITSPTGAAIRDILSVLRRRFPGLPALIYPVPVQGAAAAPAIAEALRTASARKDCDVLILARGGGSLEDLWAFNEEIVARAIHDCEIPVVSGVGHEVDVTIADLAADLRAATPSAAAELVSPLRDEWLLHVERQRRLLVERMQRGLQHQALKLDNLERRLRQQHPERRLQNQAQRVDE... | 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): 5035... |
C4L8C6 | MAISQPVIYTVSRLNNVVRLLLEQEMGLVWLTAEISNLVQHSSGHWYFTLKDQQAQIRAAMFKGQNRRVSFRPQNGQQILVQGQLSLYEARGDYQLIVEKMQPAGDGLLQMKLEALKARLMAEGLFDPRRKRALPTQPKQIGIITSPTGAAIHDMLTILARRDPALPVILYPSAVQGESAVPALLNALETAWRRNECDLLIIGRGGGSLEDLWCFNDELVVRAIANSPIPIVSAVGHETDVTLSDFAADLRAPTPSAAAELVSRDQQQQLHRLAQYQHRLQQAIQLRLQQHQIAWQQQYARLNTQNPRYQLQQKIQKQDE... | 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): 5075... |
Q83HE6 | MDMQADEMYRQDPLGSCGNPRQVSHITGRLSSLLGELPATWIEGEVTQLSPRRIGVFLTLKDMNESKHLEFFLPFDAFKDEVEVGNRVKIHGKLEFWATSGQIKVKGFEIQSVGIGELIERIARLRVQLALEGLYEHKRPLPFIPKLIGLVTGQNSDAEKDVVTNVLLRWPAAKFCTIYASMQGASCVSETISAIQKLDANNDVDVIIVARGGGSFHDLIGFSDEQMIRAVFAIKTPLISAIGHEADRPILDEVADLRASTPTDAAKRVVPDIADEKRLIKSAMSFLKKSYEPVIDKIKCDTLSWSQAFSNPFETFIAPR... | 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): 4498... |
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... |
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... |
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... |
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... |
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... |
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... |
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... |
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... |
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 smoot... |
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, throug... |
G3XDA1 | MHIQSLQQSPSFAVELHQAASGRLGQIEARQVATPSEAQQLAQRQDAPKGEGLLARLGAALVRPFVAIMDWLGKLLGSHARTGPQPSQDAQPAVMSSAVVFKQMVLQQALPMTLKGLDKASELATLTPEGLAREHSRLASGDGALRSLSTALAGIRAGSQVEESRIQAGRLLERSIGGIALQQWGTTGGAASQLVLDASPELRREITDQLHQVMSEVALLRQAVESEVSRVSADKALADGLVKRFGADAEKYLGRQPGGIHSDAEVMALGLYTGIHYADLNRALRQGQELDAGQKLIDQGMSAAFEKSGQAEQVVKTFRG... | 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 ezr... |
Q9I788 | MHIQSSQQNPSFVAELSQAVAGRLGQVEARQVATPREAQQLAQRQEAPKGEGLLSRLGAALARPFVAIIEWLGKLLGSRAHAATQAPLSRQDAPPAASLSAAEIKQMMLQKALPLTLGGLGKASELATLTAERLAKDHTRLASGDGALRSLATALVGIRDGSRIEASRTQAARLLEQSVGGIALQQWGTAGGAASQHVLSASPEQLREIAVQLHAVMDKVALLRHAVESEVKGEPVDKALADGLVEHFGLEAEQYLGEHPDGPYSDAEVMALGLYTNGEYQHLNRSLRQGRELDAGQALIDRGMSAAFEKSGPAEQVVKT... | 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 CT1... |
P33699 | MTPTVNAKTVTRNVGWSVLSKTGTFGLKFVTVPILARILSPEEFGAVAVALTVVQFLAMIGGAGLTSALVIQQHEEMETVHSVFWANLAIALMMALGLFVFAEPLATLLGAPEAAYLLRIMSLLIPLQLGGDVAYSLLVRRMNFRKDAVWSMISESLGAVIAVLLALLGFGIWSLLAQLFVSALVRLSGLYAVSRYAPRFVFSLQRVLALSRFSFGMMGSEIANFITFQSPMVVISRYLGLSDAGAYSAANRFASIPNQVVLSAVMGVLFPTFGQMMHDRERRSQALMLSTQVTTVLLAPMMFGLWALAEPAMLVLFGSQ... | 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 | MTAAAPTDVCIIISAKNAADTIARAVASALAEPEAAEVVVIDDGSTDDSASVARAADDGTGRLNVVRFEENRGPAAARNHAIAISHSPLIGVLDADDFFFPGRLGQLLSQDGWDFIADNIAFIDAAQAATAHGRIDRFAPTPRLIDLVGFVEGNISRRGVRRGEIGFLKPLMRRAFLDQHGLRYNETLRLGEDYDLYARALANGARYKIIHSCGYAAVVRGNSLSGSHRTIDLKRLYEADRAILAGSRLSSDAEAAVRRHERHIRDRYELRHFLDLKNQQGFGRAFGYALTHPAALPAIIGGILADKTERFRPSGSPAPV... | 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 biosynthe... |
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
Pat... |
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... |
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 ... |
O34456 | MFSKDKLPVILFLFLAGVINYLDRSALSIAAPFIQDDLTLSATQMGLIFSSFSIGYAIFNFLGGVASDRYGAKLTLFVAMVVWSLFSGAVALAFGFVSLLIIRILFGMGEGPLSATINKMVNNWFPPTQRASVIGVTNSGTPLGGAISGPIVGMIAVAFSWKVSFVLIMIIGLIWAVLWFKFVKEKPQETIKEAPAIKAETSPGEKIPLTFYLKQKTVLFTAFAFFAYNYILFFFLTWFPSYLVDERGLSVESMSVITVIPWILGFIGLAAGGFVSDYVYKKTARKGVLFSRKVVLVTCLFSSAVLIGFAGLVATTAGAV... | 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 | MFKIKGLRWYMIGLVTIGTVLGYLTRNAIAAAAPTLQEQLHISTQQYSYIIAAYSACYTIMQPVAGYVLDVLGTKVGYAMFAILWALFCAGTALANSWGGLAVARGAVGMAEAAMIPAGLKASSEWFPAKERSVAVGYFNVGSSIGGMLAPPLVVWAIMAHSWQMAFLITGALSLVWALCWLYFYKHPKDQKKLSTEEREYILSGQEAQHQAGNAKRMSAWQILRNRQFWGIALPRFLAEPAWGTFNAWIPLFMFKAYGFNLKEIAMFAWMPMLFADLGCILGGYMPMLFQKYFKVNLIVSRKLVVTLGALLMIGPGTIG... | 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
Su... |
P0AA79 | MRKIKGLRWYMIALVTLGTVLGYLTRNTVAAAAPTLMEELNISTQQYSYIIAAYSAAYTVMQPVAGYVLDVLGTKIGYAMFAVLWAVFCGATALAGSWGGLAVARGAVGAAEAAMIPAGLKASSEWFPAKERSIAVGYFNVGSSIGAMIAPPLVVWAIVMHSWQMAFIISGALSFIWAMAWLIFYKHPRDQKHLTDEERDYIINGQEAQHQVSTAKKMSVGQILRNRQFWGIALPRFLAEPAWGTFNAWIPLFMFKVYGFNLKEIAMFAWMPMLFADLGCILGGYLPPLFQRWFGVNLIVSRKMVVTLGAVLMIGPGMIG... | 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 | MLPDSEGQKLKTFLLGTGTTLDPSLDPTGNSNFSMATTSDSSTIWTALPASQPGDKDIPTVDLAAISEAYGSTSSTTSLTSSVTSQYQYNSYPQYAMYTSANPANYYQQVTANLRAGTTAFPYSLTTPSYYGSYPVDYTSAAAAYQNPYYTNLRGGTAAPYYNPLNATTAAAYASVASSVLGTDAVNLGTSSDGSTGVPSTVTSFSLKEKKPKVSKKKKTGSCSPGDETYARVFIWDIDDIAVISRNYLASVTHTNEFYARAANSVSHLMERIALNNFADVNEFLEGDITNIEDAVVDETTMDSGPIDNLRGLDVMRRVA... | 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 ... |
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... |
P97767 | MEMQDLTSPHSRLSGSSESPSGPKLDSSHINSTSMTPNGTEVKTEPMSSSEIASTAADGSLDSFSGSALGSSSFSPRPAHPFSPPQIYPSKSYPHILPTPSSQTMAAYGQTQFTTGMQQATAYATYPQPGQPYGISSYGALWAGIKTESGLSQSQSPGQTGFLSYGTSFGTPQPGQAPYSYQMQGSSFTTSSGLYSGNNSLTNSSGFNSSQQDYPSYPGFGQGQYAQYYNSSPYPAHYMTSSNTSPTTPSTNATYQLQEPPSGVTSQAVTDPTAEYSTIHSPSTPIKETDSERLRRGSDGKSRGRGRRNNNPSPPPDSDL... | 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 DN... |
Q58DB6 | MLELLVSASLTVNSDRPGKLKPSRADADVWTLSDREGITTSARSVSQLFARPCPRVPPGQPPSAMAAYSQTQYSAGIQQATPYTAYPPPAQAYGIPSYSIKTEDSLNHSPGQSGFLSYGSSFSTPASGQSPYTYQMHGTAGIYQGANGLTNAAGFGTVHQDYPSYPGFPQSQYSQYYSSSYNPPYVPASSICPSPLSTSTYVLQEASHNIPSQSSESLGGEYNTHNGPSTPAKEGDTDRPPRASDGKLRGRSKRSSDPSPAGDNEIERVFVWDLDETIIIFHSLLTGTFASRYGKDTTASVRIGLMMEEMIFNLADTHLF... | 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... |
O00167 | MVELVISPSLTVNSDCLDKLKFNRADAAVWTLSDRQGITKSAPLRVSQLFSRSCPRVLPRQPSTAMAAYGQTQYSAGIQQATPYTAYPPPAQAYGIPSYSIKTEDSLNHSPGQSGFLSYGSSFSTSPTGQSPYTYQMHGTTGFYQGGNGLGNAAGFGSVHQDYPSYPGFPQSQYPQYYGSSYNPPYVPASSICPSPLSTSTYVLQEASHNVPNQSSESLAGEYNTHNGPSTPAKEGDTDRPHRASDGKLRGRSKRSSDPSPAGDNEIERVFVWDLDETIIIFHSLLTGTFASRYGKDTTTSVRIGLMMEEMIFNLADTHL... | 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 DN... |
O08575 | MLEVVTSPSLATSSDWSEHGAAVGTLSDREGIAKSAALSVPQLFVKSHPRVPPGQSSTAMAAYGQTQYSTGIQQAPPYTAYPTPAQAYGIPPYSIKTEDSLNHSPSQSGFLSYGPSFSTAPAGQSPYTYPVHSTAGLYQGANGLTNTAGFGSVHQDYPSYPSFSQNQYPQYFSPSYNPPYVPASSLCSSPLSTSTYVLQEAPHNVPSQSSESLAGDYNTHNGPSTPAKEGDTERPHRASDGKLRGRSKRNSDPSPAGDNEIERVFVWDLDETIIIFHSLLTGTFASRYGKDTTTSVRIGLMMEEMIFNLADTHLFFNDLE... | 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 DN... |
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 i... |
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... |
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... |
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 i... |
Q9A8G9 | MGRSAFGSRTRMTAFVDLAARLAAEPADAALKDVVLTIAETCAQISRVVASGALSGSLGAAGSTNVQDEEQKKLDVITNDMLSDALKACGPVAGLASEELEEVEPTGRVGGYLVTFDPLDGSSNIDVNVSVGTIFSVLPAPAGHAPTEGDFLQPGRNQVAAGYAVYGPQTMLVVTLSGGVNGFTLSADGRWLLTHPDLAIKPDTAEFAINMSNQRHWAPAVRRYIDGCLQGKDGARGKNFNMRWVASMVADVHRIMMRGGVFMYPWDAREPDKPGKLRLMYEANPMSLLAERAGGKSIEGLNEILDINPAKLHQRVPVVL... | 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 | MNKLTTIESHFLQLQKRYPEINSEVTDLLNDVAFAAKLVRREVVRAGLADILGLAGSTNVQGEEVKKLDLFANERLINAIGQHGRFAIMGSEENEEIIKPPKFESGEYVLLFDPLDGSSNIDVNVSVGTIFSIYRLKSGEPSQASLEDCLQKGADQIAAGYVIYGSSVMMVYTTGHGVHGFTYDQTVGEFLLSHENITTPEHGKYYSVNEGSWQEFNDGTKRFLDYLKEEDKATGRPYSTRYIGSFVADFHRNLLTGGVFVYPATKKHKNGKLRLMYEANPMAFICEQAGGRATDGYRRILDIEPKELHQRTPLYIGSKN... | 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 | MKTLGEFIVEKQHEFSHATGELTALLSAIKLGAKIIHRDINKAGLVDILGASGAENVQGEVQQKLDLFANEKLKAALKARDIVAGIASEEEDEIVVFEGCEHAKYVVLMDPLDGSSNIDVNVSVGTIFSIYRRVTPVGTPVTEEDFLQPGNKQVAAGYVVYGSSTMLVYTTGCGVHAFTYDPSLGVFCLCQERMRFPEKGNTYSINEGNYIKFPNGVKKYIKFCQEEDKSTNRPYTSRYIGSLVADFHRNLLKGGIYLYPSTASHPEGKLRLLYECNPMAFLAEQAGGKASDGKERILDITPESLHQRRPFFVGTDHMVE... | 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 | MKTLGEFIVEKQHEFSHATGELTALLSAIKLGAKIIHRDINKAGLVDILGASGVENVQGETQQKLDLFANEKLKAALKARDIVAGIASEEEDEIVVFEGCEHAKYVVLMDPLDGSSNIDVNVSVGTIFSIYRRVTPVGTPVTMEDFLQPGSQQVAAGYVVYGSSTMLVYTTGCGVHAFTYDPSLGVFCLCQERMRFPQSGNTYSINEGNYIKFPMGVKKYIKYCQEEDKATQRPYTSRYIGSLVADFHRNLLKGGIYLYPSTASHPEGKLRLLYECNPMAFLAEQAGGKASDGKQRILDIKPDSLHQRRPFFVGTEQMVN... | 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 | MSRTSLTRFLIQEQHAGRINADLRQLIAVVARACTSISIAVSKGALGGVLGDAGTGNVQGEAQKKLDVISNEILLEANAWGGHLAACASEEMDHSQPVPDIYPRGDFLLLFDPLDGSSNIDVNVSVGTIFSVLRCPTNVELPGDDAFLQPGSKQIAAGYCIYGPSTQLVLTVGHGTHAFTLDREKGEFVLTTENMQIPAATQEFAINMSNQRHWEAPMQAYVGDLLAGKEGTRGKNFNMRWIASMVADVHRILTRGGIFIYPWDKKDPSKAGKLRLMYEANPMGLLVEQAGGAAWTGRERILDIQPDQLHQRVPVFLGSR... | 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... |
P00743 | MAGLLHLVLLSTALGGLLRPAGSVFLPRDQAHRVLQRARRANSFLEEVKQGNLERECLEEACSLEEAREVFEDAEQTDEFWSKYKDGDQCEGHPCLNQGHCKDGIGDYTCTCAEGFEGKNCEFSTREICSLDNGGCDQFCREERSEVRCSCAHGYVLGDDSKSCVSTERFPCGKFTQGRSRRWAIHTSEDALDASELEHYDPADLSPTESSLDLLGLNRTEPSAGEDGSQVVRIVGGRDCAEGECPWQALLVNEENEGFCGGTILNEFYVLTAAHCLHQAKRFTVRVGDRNTEQEEGNEMAHEVEMTVKHSRFVKETYDF... | 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: ... |
P25155 | MAGRLLLLLLCAALPDELRAEGGVFIKKESADKFLERTKRANSFLEEMKQGNIERECNEERCSKEEAREAFEDNEKTEEFWNIYVDGDQCSSNPCHYGGQCKDGLGSYTCSCLDGYQGKNCEFVIPKYCKINNGDCEQFCSIKKSVQKDVVCSCTSGYELAEDGKQCVSKVKYPCGKVLMKRIKRSVILPTNSNTNATSDQDVPSTNGSILEEVFTTTTESPTPPPRNGSSITDPNVDTRIVGGDECRPGECPWQAVLINEKGEEFCGGTILNEDFILTAAHCINQSKEIKVVVGEVDREKEEHSETTHTAEKIFVHSKY... | 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... |
P00742 | MGRPLHLVLLSASLAGLLLLGESLFIRREQANNILARVTRANSFLEEMKKGHLERECMEETCSYEEAREVFEDSDKTNEFWNKYKDGDQCETSPCQNQGKCKDGLGEYTCTCLEGFEGKNCELFTRKLCSLDNGDCDQFCHEEQNSVVCSCARGYTLADNGKACIPTGPYPCGKQTLERRKRSVAQATSSSGEAPDSITWKPYDAADLDPTENPFDLLDFNQTQPERGDNNLTRIVGGQECKDGECPWQALLINEENEGFCGGTILSEFYILTAAHCLYQAKRFKVRVGDRNTEQEEGGEAVHEVEVVIKHNRFTKETYD... | 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: ... |
P16930 | MSFIPVAEDSDFPIHNLPYGVFSTRGDPRPRIGVAIGDQILDLSIIKHLFTGPVLSKHQDVFNQPTLNSFMGLGQAAWKEARVFLQNLLSVSQARLRDDTELRKCAFISQASATMHLPATIGDYTDFYSSRQHATNVGIMFRDKENALMPNWLHLPVGYHGRASSVVVSGTPIRRPMGQMKPDDSKPPVYGACKLLDMELEMAFFVGPGNRLGEPIPISKAHEHIFGMVLMNDWSARDIQKWEYVPLGPFLGKSFGTTVSPWVVPMDALMPFAVPNPKQDPRPLPYLCHDEPYTFDINLSVNLKGEGMSQAATICKSNFK... | 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 | MIFYLVLLVLGAIAFYVHFSNNRKKLIERLEIVAQRRRDDLSKNVEQARKAADKLDTQRRDWIGSLDFEQLRDELQRGHVTCVEAIRAYFHKAILAHEKTNAVTCFILDAERQAEELDEQAKLPYYVKPPLFGVPLSLKECLKVKGYDTTRGFVQDAYHPATEDSIQVEHYKKLGLIPFCQTNVPQSLLSYNCSNPLFGTTTNPYDSTRTCGGSSGGEGALIGAGGSLIGIGTDVGGSVRIPCHFTGTAGIKPSKMRFAHRGGGASVPGKPLIDANDGPMAKDVKTNVEFLRNVWGDIDFQSDRDPYCPPVHWNESVYSS... | 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 t... |
O00519 | MVQYELWAALPGASGVALACCFVAAAVALRWSGRRTARGAVVRARQRQRAGLENMDRAAQRFRLQNPDLDSEALLALPLPQLVQKLHSRELAPEAVLFTYVGKAWEVNKGTNCVTSYLADCETQLSQAPRQGLLYGVPVSLKECFTYKGQDSTLGLSLNEGVPAECDSVVVHVLKLQGAVPFVHTNVPQSMFSYDCSNPLFGQTVNPWKSSKSPGGSSGGEGALIGSGGSPLGLGTDIGGSIRFPSSFCGICGLKPTGNRLSKSGLKGCVYGQEAVRLSVGPMARDVESLALCLRALLCEDMFRLDPTVPPLPFREEVYT... | 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 o... |
O08914 | MVLSEVWTALSGLSGVCLACSLLSAAVVLRWTRSQTARGAVTRARQKQRAGLETMDKAVQRFRLQNPDLDSEALLALPLLQLVQKLQSGELSPEAVLFTYLGKAWEVNKGTNCVTSYLTDCETQLSQAPRQGLLYGVPVSLKECFSYKGHASTLGLSLNEGVTSESDCVVVQVLKLQGAVPFVHTNVPQSMLSYDCSNPLFGQTMNPWKPSKSPGGSSGGEGALIGSGGSPLGLGTDIGGSIRFPSAFCGICGLKPTGNRLSKSGLKSCVYGQTAVQLSVGPMARDVDSLALCMKALLCEDLFRLDSTIPPLPFREEIYR... | 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 ... |
P97612 | MVLSEVWTTLSGVSGVCLACSLLSAAVVLRWTGRQKARGAATRARQKQRASLETMDKAVQRFRLQNPDLDSEALLTLPLLQLVQKLQSGELSPEAVFFTYLGKAWEVNKGTNCVTSYLTDCETQLSQAPRQGLLYGVPVSLKECFSYKGHDSTLGLSLNEGMPSESDCVVVQVLKLQGAVPFVHTNVPQSMLSFDCSNPLFGQTMNPWKSSKSPGGSSGGEGALIGSGGSPLGLGTDIGGSIRFPSAFCGICGLKPTGNRLSKSGLKGCVYGQTAVQLSLGPMARDVESLALCLKALLCEHLFTLDPTVPPLPFREEVYR... | 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 o... |
Q6GMR7 | MAPSFTARIQLFLLRALGFLIGLVGRAALVLGGPKFASKTPRPVTEPLLLLSGMQLAKLIRQRKVKCIDVVQAYINRIKDVNPMINGIVKYRFEEAMKEAHAVDQKLAEKQEDEATLENKWPFLGVPLTVKEAFQLQGMPNSSGLMNRRDAIAKTDATVVALLKGAGAIPLGITNCSELCMWYESSNKIYGRSNNPYDLQHIVGGSSGGEGCTLAAACSVIGVGSDIGGSIRMPAFFNGIFGHKPSPGVVPNKGQFPLAVGAQELFLCTGPMCRYAEDLAPMLKVMAGPGIKRLKLDTKVHLKDLKFYWMEHDGGSFLMS... | 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 o... |
Q9U217 | MGNNFWSTWSPSQRIFSLIWPATILYLIMKLLIEKMWGKNRGAVERFQTRREALFDDFKSRSAPASLVNNPRIVKGNETAEQIETTFNEILKLDLIALKSALQTDKYNAYTVLCAFVWRAIDVNSEINCITEVIREAFNTAEALDDNYAQTGEKGQLFGLPFSVKSNFYMENYDVTVGLAKLLEQPKTTTCPMVQFLSDQGAVPFCLTNVPQGLLSYVSSNPIYGTTKNPWDFSRTPGGSSGGEAALLAAGGAAFGIGSDLAGSLRIPAAFCGLVTLKPTQDRLCVTDTHGGLPGRGRLGLSFGFYTRSVKEQEFLLGLI... | 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 r... |
Q7XJJ7 | MGKYQVMKRASEVDLSTVKYKAETMKAPHLTGLSFKLFVNLLEAPLIGSLIVDYLKKDNGMTKIFRNTVIPEEPMFRPEFPSQEPEHDVVIVGEDESPIDRLETALKCLPQYDPSRSLHADPVSSFRYWKIRDYAYAYRSKLTTPLQVAKRIISIIEEFGYDKPPTPFLIRFDANEVIKQAEASTRRFEQGNPISVLDGIFVTIKDDIDCLPHPTNGGTTWLHEDRSVEKDSAVVSKLRSCGAILLGKANMHELGMGTTGNNSNYGTTRNPHDPKRYTGGSSSGSAAIVAAGLCSAALGTDGGGSVRIPSALCGITGLKT... | 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 f... |
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 i... |
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... |
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 Le... |
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 Le... |
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 ace... |
Q8ABI8 | MDKINAVITGVGGYVPDYVLTNDEISKMVDTTDEWIMGRIGIKERHILNEEGLGTSYMARKAAKQLMQRTKSRPDDIDLVIVATTTSDYRFPSTASILCERLGLKNAFAFDMQAVCSGFLYAMETGANFIRSGKYKKIIIVGADKMSSVIDYTDRATCPIFGDGAAAFMLEPTTEEVGIMDSVLRTDGKGLPFLHIKAGGSVCPPSYYSLDHHLHYIYQEGRTVFKYAVANMSDSCEAIIARNHLTKEEVDWVIPHQANQRIITAVAQRLEVPSEKVMVNIERYGNTSAGTLPLCIWDFEKKLKKGDNLIFTAFGAGFAW... | 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 ace... |
Q88YZ4 | MPTYTKLTAMGQYVPGRVVDNDELAAIMDTSDEWIQAHTGIKTRHYAMNDENTSDLATQVAQQLLQKSGLAASAIDLILVTTITPDALTPATACLVQANIGADNAFAFDLSAACAGFTFGLATADKFIRSGQYQNVMVISAEVNSKMMDFQDRTAAVFFGDGAGGALLQATDNPDENSLIAEKLESQGNATVIHSGRVRPITEVAATNYPQTDAFYQVGRDVFQFATTVVPEQMRGLIASAQLTPSDLQYVICHQANLRIIEKIAANLALPMTKFPHNVDHYGNTSSAGVAMALANVFDTLTGPVLLTAFGGGLAYGSVL... | 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 ace... |
P72392 | MSKIKPSKGAPYARILGVGGYRPTRVVPNEVILEKIDSSDEWIRSRSGIETRHWAGPEETVAAMSVEASGKALADAGIDASRIGAVVVSTVSHFSQTPAIATEIADRLGTDKAAAFDISAGCAGFGYGLTLAKGMVVEGSAEYVLVIGVERLSDLTDLEDRATAFLFGDGAGAVVVGPSQEPAIGPTVWGSEGDKAETIKQTVSWDRFRIGDVSELPLDSEGNVKFPAITQEGQAVFRWAVFEMAKVAQQALDAAGISPDDLDVFIPHQANVRIIDSMVKTLKLPEHVTVARDIRTTGNTSAASIPLAMERLLATGDARS... | 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 producti... |
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 ace... |
Q24U40 | MVSVGIVGTGSYVPDKVLTNFDLEQMVDTNDQWIVSRTGIKERHIAEPETPVSELCYQAAVRALEDAKLAPEELDLVIVATITPDFVFPATACLVAERLGAKKAAGFDLQAACTGFLYGVATAAQFIATGIYKNALVIGGETLSKILNWEDRGTCILFGDGAGAAVLQQVEEGYGFLGYDLGMDGAGGSLLTMPGGGSMHPASAETVAKKMHTIQMAGSEVFKFAVRIMGETALKALDKAGLGIGDVDCLIPHQANTRIVDAAVKRLGIDAGKVVVNLDRYGNMSAASIPVALDEAARSGRLNYGDIMVMVGFGGGLTWG... | 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 ace... |
Q6AJF8 | MSVVILGTGSCLPEKIVTNKDLEKIVETNDEWIRTRTGICERRIAGPGEQAYILASRAAKNALDAAGLVAEDLDMIVVGTISAHMVMPSCACMIQQEIGAKKAFAFDVNAACSGFLYAMEVGSKYVATNPAMKVLCIGTETLSARTNQQDRNTSIIFADGAGAAVIGYEEGDRGILASKLFSDGSFGDILFLSGSESTNTDLRLGEYEGSHIHMEGREVFKHAVRAMEGAVNTIMEEVGVSPHEIKLLIPHQANIRIIKNLGERLGLSSEQVFVNIANYGNTSAASVPIALDEAVRGGKIESGDLVLLCSFGGGFTWGAS... | 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 ace... |
Q72CS6 | MTSPSLLRGFGAYAPERILTNADIESMVETTDEWITTRTGIRQRHVVAPGQTTSDLAVEAARAALADAALDTADITHVLVATCTPDASCPNTACIVARKLGMTGVMALDCNAACSGFLYGLELAQGIVAARPASRVLLVAAEALSLRCNWKDRTTCVLFGDGAGATVVTADVDATQGTAVLEDSIVTSDGSLGDLLTIGGGTANPYAIGDSVGEEYFVRMQGRDVFKHAVRSMTQVCNDLLARNGFTTEDVDLVIPHQANLRIIEAVGDRLGFASEKVFVNVHDFGNTSAASIPLALADARAQGRIRPGMRVLLTTFGGG... | 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 ace... |
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 ace... |
B9DVE9 | MTYSKISQAAHHLPEQVISNDDLSLILETNDQWISSRTGIKERRISRSENTSDLASRVAEKLLEKANIDATEIDFIIVATITGDSIMPSVAAKVQGTIGATHAFAFDMTAACSGFVFALAMADKLIRSASYQKGLVIGAEVLSKYLDWEDRSTAVLFGDGAGGVLVEACSEQHFMAESLHTDGSRGQNLTSGNNPLRSPFSDSEEASPFIKMDGRAIFDFAIRDVSKSIISLLEESSVTAEEIDYFLLHQANRRILDKMARKIGCPRDKFLENMMTYGNTSAASIPILLSESVEKGLILLDGSQKVLLSGFGGGLTWGSL... | 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 ace... |
Q31N84 | MTRPGVGVAITGSGSAVPSTTLSNDQLSQLVETSDEWIRSRTGIGQRRVAQPQIESLSSLAAAAGQSALEAAGLEATSVDLILLATSTPDDLFGSACQVQAALGATQAVAFDLTAACSGFLFALVTGAQFIRSGAYRTVLVIGADVLSRWTDWSDRRTCVLFGDGAGAVVLQASEIDQLLGFEMRSDGSLNGCLTLAYQADNQSLLSDIEIAQGTYQPVAMNGQEVYRFAVKRVPEILEKTLFHAGIDRQEVDWLLLHQANQRILDAVADRLDISRDRVLSNLVNYGNTSSATIPLVLDEAVKAGKIQSGDLIAASGFGA... | 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 ace... |
A5GP11 | MAGQSPPVLGVGLIGSGSAQAAQVISNDQLSQRVDTNDEWIRTRTGIGRRRVSTADQTLVDLAAEAGRSALTMAGRSPQDLDLILLATSTPDDLFGSAPRVQAELGATNAVAFDLTAACSGFLFALVTAAQYLRTGAMRRALVIGADQLSRFVDWDDRRSCVLFGDGAGAVVLEASDEDGLLGFLLHSDGARGAVLNLPANDTSAPLIAGAEHRAGGYRPIVMNGQEVYKFAVREVPAVLQSLLKRCDVSADQLDWLLLHQANQRILDAVADRLSVPGAKVLSNLAAYGNTSAATIPLMLDEAVRDGRVSSGDLLASSGF... | 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 ace... |
P73951 | MNTLGSGLKIIGSGTAIADQSLTNQDLSNIVETSDEWIQSRTGMRQRYICSAQENLASLGVKAGQKALAMAGLQPEDLDLIILATSTPDDLFGTAAQIQGGLGATRAFAFDITAACSGFVVGLNVAAQFLRTGVYQRVLIVGGDVLSRWVDWSDRTTCVLFGDGAGAVVLQRQAQDNLLAFEMYTDGTGNGCLNLSYQANPQPLTAEKTVAQGTYQAITMNGREVYRFAVAKVPEIIEKVLFKAQLTTSDLDWVILHQANQRIMDAVGDRLGIPSEKIISNVGEYGNTSAASIPLALDQAVREGKIKEGDLIALAGFGAG... | 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 ace... |
C0QVH0 | MVVEPKILNNICITAHPLGCAKEVENHINYVKSQPKVKSNVKNALILGASGGYGLASRIAIAYGLGAKTMSVSFEKGATARRTATPGWYNNEAFSAFAKKDGIEDKNLILDAFLNASKEEVIKEAKTFFNGEKIDLLIYSLAAPVRMDESTGTLYRSSLKPIGKKYNGIGVDFLTEELLEVSIDPANEDDIKSTVKVMGGEDWKLWTDALLNADLLAENAINVAYSYIGPEMTKAVYREGTIGKAKDHLEATAHELDKEMQEKIKGHAYVSVNKAVVTRSSAVIPTVPLYIGILFKVMKNKGLHEGCIEQMYRLLNEKLY... | 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
Pathwa... |
Q62L02 | MIIKPRVRGFICVTTHPAGCAASVREQIAYVARRGPIERGPKKVLVIGASTGYGLAARIAAAFGVGAATLGVFFERAPADAKPGTAGWYNSAAFHDEAAARGLQATSVNGDAFSDEIKHKTIDAIRRDLGQVDLVVYSVAAPRRTHPKTGVTHQSTLKPIGHAVRLRGIDTDNEAIKETLLQPATPDEIADTVAVMGGEDWRMWIDALDAAGVLADGAKTTAFTYLGEQVTHDIYWNGSIGEAKKDLDRTVLALRGKLAARGGDARVSVLKAVVTQASSAIPMMPLYLSLLFKVMKARGTHEGCIEQVDGLLRDSLYSAQ... | 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... |
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 Lo... |
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 Lo... |
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 Lo... |
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 Lo... |
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 Lo... |
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 Lo... |
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 Lo... |
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 Lo... |
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 Lo... |
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 Lo... |
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 Lo... |
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 Lo... |
O32177 | MKEAVIVSGARTPVGKAKKGSLATVRPDDLGAICVKETLKRAGGYEGNIDDLIIGCATPEAEQGLNMARNIGALAGLPYTVPAITVNRYCSSGLQSIAYAAEKIMLGAYDTAIAGGAESMSQVPMMGHVTRPNLALAEKAPEYYMSMGHTAEQVAKKYGVSREDQDAFAVRSHQNAAKALAEGKFKDEIVPVEVTVTEIGEDHKPMEKQFVFSQDEGVRPQTTADILSTLRPAFSVDGTVTAGNSSQTSDGAAAVMLMDREKADALGLAPLVKFRSFAVGGVPPEVMGIGPVEAIPRALKLAGLQLQDIGLFELNEAFAS... | 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
|
P28793 | MIYEGKAITVTALESGIVELKFDLKGESVNKFNRLTLNELRQAVDAIKADASVKGVIVSSGKDVFIVGADITEFVENFKLPDAELIAGNLEANKIFSDFEDLNVPTVAAINGIALGGGLEMCLAADFRVMADSAKIGLPEVKLGIYPGFGGTVRLPRLIGVDNAVEWIASGKENRAEDALKVSAVDAVVTADKLGAAALDLIKRAISGELDYKAKRQPKLEKLKLNAIEQMMAFETAKGFVAGQAGPNYPAPVEAIKTIQKAANFGRDKALEVEAAGFAKLAKTSASNCLIGLFLNDQELKKKAKVYDKIAKDVKQAAVL... | 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... |
Q87ZB2 | MIYEGKAITVKALESGIVELNFDLKGESVNKFNRLTLNELRQAVDAVKADASVKGVIVTSGKDVFIVGADITEFVDNFKLPEAELVAGNLEANRIFSDFEDLGVPTVVAINGIALGGGLEMCLAADYRVISSSARVGLPEVKLGLYPGFGGTVRLPRIIGADNAIEWIASGKENSAEDALKVGVVDAIVAPEKLQAAALDLIQRAISGEFDYKAKRQPKLDKLKLNAIEQMMAFETAKGFVAGQAGPNYPAPVEAIKTIQKAAIFGRDKALEIEAAGFVKMAKTSAAQSLIGLFLNDQELKKKAKGYDEVARDVKQAAVL... | 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... |
Q9KT58 | MDNNNAFQLSFDEQHYAWLAIDVPGEKMNTLQAAFAEEMQAVFATLNEKRGQIKGLIIHSLKPDNFIAGADVRMLEACQSVHEAQALASQGQQMFQQLADLPFPVVAAIHGPCLGGGLELALACDYRVCTEDEVTRLGLPEVMLGLLPGSGGTQRLPRLIGLLPALDLILTGKQLRAKKAKKLGVVDACVPHSVLLDVAKRLLEEKGHKKRAQVTLPIKEKLLANTDLGRKLIFDQAAKKTQQKTRGNYPAAQAILEVIQYGLEKGMHAGLEYEAKRFAELVMTRESKALRSIFFATTEMKKDLGADAKPAPVAAVGVLG... | 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 metaboli... |
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