ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q8NLN0 | MKETVGNKIVLIGAGDVGVAYAYALINQGMADHLAIIDIDEKKLEGNVMDLNHGVVWADSRTRVTKGTYADCEDAAMVVICAGAAQKPGETRLQLVDKNVKIMKSIVGDVMDSGFDGIFLVASNPVDILTYAVWKFSGLEWNRVIGSGTVLDSARFRYMLGELYEVAPSSVHAYIIGEHGDTELPVLSSATIAGVSLSRMLDKDPELEGRLEKIFEDTRDAAYHIIDAKGSTSYGIGMGLARITRAILQNQDVAVPVSALLHGEYGEEDIYIGTPAVVNRRGIRRVVELEITDHEMERFKHSANTLREIQKQFF | Function: Catalyzes the conversion of lactate to pyruvate.
Catalytic Activity: (S)-lactate + NAD(+) = H(+) + NADH + pyruvate
Sequence Mass (Da): 34405
Sequence Length: 314
Pathway: Fermentation; pyruvate fermentation to lactate; (S)-lactate from pyruvate: step 1/1.
Subcellular Location: Cytoplasm
EC: 1.1.1.27
|
Q4JY42 | MTAPQPHTITPPTPGSKIVLIGAGDVGIAYAYTLVNQGLTDHLAIIDLDERKTWGHVQDLNHAVPWSHHNTRVTVGTYEDCRDAAMVCICAGAAQKPGETRLDLVAKNTAIFKTIVGDVMSHGFNGIFLVASNPVDILSYATWKFSGMDSSRVIGSGTILDTARFRYALGRYFDLAPTSVHAYVIGEHGDTELPVLSAGSVAGTSIHHRLEMIGESADEDVDEIFVKTRDAAYEIIQAKGSTSFGIGMGLARITQAVFSNQDVVLPISTLLQGEYGFEDIYIGTPAVINRQGVRHAVELQLDSEEKERFDHSANVLRKVM... | Function: Catalyzes the conversion of lactate to pyruvate.
Catalytic Activity: (S)-lactate + NAD(+) = H(+) + NADH + pyruvate
Sequence Mass (Da): 35237
Sequence Length: 326
Pathway: Fermentation; pyruvate fermentation to lactate; (S)-lactate from pyruvate: step 1/1.
Subcellular Location: Cytoplasm
EC: 1.1.1.27
|
Q07251 | MKISLTSARQLARDILAAQQVPADIADDVAEHLVESDRCGYISHGLSILPNYRTALDGHSVNPQGRAKCVLDQGTLMVFDGDGGFGQHVGKSVMQAAIERVRQHGHCIVTLRRSHHLGRMGHYGEMAAAAGFVLLSFTNVINRAPVVAPFGGRVARLTTNPLCFAGPMPNGRPPLVVDIATSAIAINKARVLAEKGEPAPEGSIIGADGNPTTDASTMFGEHPGALLPFGGHKGYALGVVAELLAGVLSGGGTIQPDNPRGGVATNNLFAVLLNPALDLGLDWQSAEVEAFVRYLHDTPPAPGVDRVQYPGEYEAANRAQ... | Catalytic Activity: (S)-lactate + NAD(+) = H(+) + NADH + pyruvate
Sequence Mass (Da): 36756
Sequence Length: 349
Pathway: Fermentation; pyruvate fermentation to lactate; (S)-lactate from pyruvate: step 1/1.
Subcellular Location: Cytoplasm
EC: 1.1.1.27
|
Q6A9C3 | MSTFDATRRASKISVVGAGSVGSSLAYACLIRGSAGLVSLYDIAKDKVEAEVADLAHGTQFTPASVMGGADVHDTADSDVVFITAGARQKPGQTRLDLAGVNANILRSLMPQLVEQSPNALFVLVTNPCDVLTVVAQEATGLPANRVFSTGTMLDTSRLRWLIRQWANVEQRHVHATIVGEHGDSEFPLWSTANISGVPIRDWAVDGNRVFTEDVLADLAHEAAYAAYKIIEGKGATNYAIGLTGARLAEALLRPGRSVLPLSSVMTDMHGISGVALSMPCIVSRDGIEGVVPVAMDTEEIASLKASAERLHDTLSSIA | Function: Catalyzes the conversion of lactate to pyruvate.
Catalytic Activity: (S)-lactate + NAD(+) = H(+) + NADH + pyruvate
Sequence Mass (Da): 33663
Sequence Length: 319
Pathway: Fermentation; pyruvate fermentation to lactate; (S)-lactate from pyruvate: step 1/1.
Subcellular Location: Cytoplasm
EC: 1.1.1.27
|
P0CU49 | MFLARNVSRVALRSASLSPAAIPQQQHAGVAAVYAVRFASSSGSGRPADNWAESQKEKAKAGLKDAQAEVGKVAREVKDKAAGGIEQAKDAVKQGANDLKRSGSRTFENAKDDIQAKAQHAKSDLKGAKHQAEGVVENVKEAAENAWEKTKDVAENLKDKVQSPGGLADKAANAWETVKDRAQDAASEVKHKAGDLKDKAQQVIHDATTQSGDNRKQDQQQRRDSQGSQSGQNSRSRN | Function: Mitochondrial heat soluble protein acting as a molecular shield in water-deficient condition.
Sequence Mass (Da): 25461
Sequence Length: 238
Domain: Contiguous repeats of the 11-mer LEA motif is characteristic of group 3 LEA proteins and form an amphipathic helical structure under water-deficient conditions.
... |
A0A0E4AVP3 | MFLARNAGRAGYRGVVAYQQAASFSVSSAKAAGSRSSGGSDAGDYAREAAEHAKAGLKDLKNEASWKAKGVANQAAGAFERAKDTVKEGVHDMKRSGSRVFEQGQEEVEAGAQHAKAGYQSAKNAAQDTAATLKDKAGSAWNQAKHVVEDKGEDVVEAVKDTASKVWGKAKHVAEDVKENAQSPGGIADKASDVWSAAKDKAADVLSGAKHTAENLAHKAQAAIHDATASSGSQSQSQSQSQYRQGQQQGRQDQQQSKSQWGQTSPQSPDGFRPQAGQGPQGGKGPGQAGGRR | Function: Mitochondrial heat soluble protein acting as a molecular shield in water-deficient condition.
Sequence Mass (Da): 30485
Sequence Length: 293
Domain: Contiguous repeats of the 11-mer LEA motif is characteristic of group 3 LEA proteins and form an amphipathic helical structure under water-deficient conditions .... |
P38486 | MADSFSLNDALSGSGNPNPQGWPGPWGNQPAGAGGYPGASYPGAYPGQAPPGGYPGQAPPGGYPGQAPPGGYPGQAPPGGYPGQAPPGGYPGQAPPGGYPGQAPPGTYPGPTAPAYPGPTAPGTQPGQPSGPGAYPPPGQPSAPGAYPAAGPFGIPAGPLTVPYDLPLPGGVKPRMLITILGTVRPSANRLALDFKRGNDVAFHFNPRFNEDNKRVIVCNTKLDNIWGKEERQAAFPFESGKPFKIQVLVESDHFKVAVNDAHLLQYNHRMKNLPEISKLGISGDIDLTSASYAMI | Function: Galactose-specific lectin which binds IgE. May mediate with the alpha-3, beta-1 integrin the stimulation by CSPG4 of endothelial cells migration. Together with DMBT1, required for terminal differentiation of columnar epithelial cells during early embryogenesis. In the nucleus: acts as a pre-mRNA splicing fact... |
Q8EH83 | MKHIRNFSIIAHIDHGKSTLSDRLIQVCGGLSDREMDAQVLDSMDLERERGITIKAQSVTLEYKAKNGEIYQLNFIDTPGHVDFSYEVSRSLAACEGALLVVDAGQGVEAQTLANCYTALDMNLDVVPILNKIDLPQADPERVAAEIEDIVGIDAMNAVRCSAKTGVGIDDVLEVIVEQIPPPEGNPDAPLQALIIDSWFDSYLGVVSLVRIKHGVLKKGDKFKVMSTGQNHTADRVGIFTPKQTDKTELKTGEVGFVIAGIKEIHGAPVGDTLTLAKNGADKPLPGFKKVKPQVYAGVFPISTDEYENFRDALNKLSLN... | Function: Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex ... |
Q89AM6 | MSNYLSSFLLASSLITGTLWIINKILSHNLLDSKIPFNIKKSKIYYKSKQVVQTFASFFPILIIVFIIRTFICEPFQIPSESMMPTLLPGDFILVKKFSYGIKNPFSNNVIVFINTPKRGDIVVFKHPNNNAINYVKRIVGLPGDKINYNILTKRLTITPNNINEQHTKNISINYKYIKPNDFTKHFKLNNIILNNVHSLESSNNNLLQLEMYQEKIEKIAYNIFFKKKLIDQKDLYFKQFSQKQGTWIVPKHKYFVLGDNRDNSLDSRYWGFVPEKNLIGKVVFIWMHLIKKEGQWPTGIQFDRIGNIY | Catalytic Activity: Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 36313
Sequence Length: 310
Subcellular Location: Cell membrane
EC: 3.4.21.89
|
P00803 | MANMFALILVIATLVTGILWCVDKFFFAPKRRERQAAAQAAAGDSLDKATLKKVAPKPGWLETGASVFPVLAIVLIVRSFIYEPFQIPSGSMMPTLLIGDFILVEKFAYGIKDPIYQKTLIETGHPKRGDIVVFKYPEDPKLDYIKRAVGLPGDKVTYDPVSKELTIQPGCSSGQACENALPVTYSNVEPSDFVQTFSRRNGGEATSGFFEVPKNETKENGIRLSERKETLGDVTHRILTVPIAQDQVGMYYQQPGQQLATWIVPPGQYFMMGDNRDNSADSRYWGFVPEANLVGRATAIWMSFDKQEGEWPTGLRLSRI... | Catalytic Activity: Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35960
Sequence Length: 324
Subcellular Location: Cell inner membrane
EC: 3.4.21.89
|
P44454 | MSNLFFVILLAVGFGVWKVLDYFQLPNTFSILLLILTALSGVLWCYHRFVVLPKRHRQVARAEQRSGKTLSEEEKAKIEPISEASEFLSSLFPVLAVVFLVRSFLFEPFQIPSGSMESTLRVGDFLVVNKYAYGVKDPIFQNTIIAGEKPQRGDVIVFKAPQQALIRTGLGATRAAFAENLALSSKDNMSGVDYIKRIVGKGGDRVIFDVEQKTLKVVYGKEGKPCEIDCETKAFEYTQNPTNPAFPNELELTEKGDVTHNVLISEYRRYSDLEFFPQEGMQTAEWLVPEGQYFVMGDHRDHSDDSRFWGFVPEKNIVGK... | Catalytic Activity: Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 39734
Sequence Length: 349
Subcellular Location: Cell inner membrane
EC: 3.4.21.89
|
O25300 | MKFLRSVYAFCSSWVGTIVIVLLVIFFIAQAFIIPSRSMVGTLYEGDMLFVKKFSYGIPIPKIPWIELPVMPDFKNNGHLIEGDRPKRGEVVVFIPPHEKKSYYVKRNFAIGGDEVLFTNEGFYLHPFESDTDKNYIAKHYPNAMTKEFMGKIFVLNPYKNEHPGIHYQKDNETFHLMEQLATQGAEANISMQLIQMEGEKVFYKKINDDEFFMIGDNRDNSSDSRFWGSVAYKNIVGSPWFVYFSLSLKNSLEMDAENNPKKRYLVRWERMFKSVGGLEKIIKKENATH | Catalytic Activity: Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 33710
Sequence Length: 290
Subcellular Location: Cell membrane
EC: 3.4.21.89
|
P9WKA0 | MTETTDSPSERQPGPAEPELSSRDPDIAGQVFDAAPFDAAPDADSEGDSKAAKTDEPRPAKRSTLREFAVLAVIAVVLYYVMLTFVARPYLIPSESMEPTLHGCSTCVGDRIMVDKLSYRFGSPQPGDVIVFRGPPSWNVGYKSIRSHNVAVRWVQNALSFIGFVPPDENDLVKRVIAVGGQTVQCRSDTGLTVNGRPLKEPYLDPATMMADPSIYPCLGSEFGPVTVPPGRVWVMGDNRTHSADSRAHCPLLCTDDPLPGTVPVANVIGKARLIVWPPSRWGVVRSVNPQQGR | Catalytic Activity: Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 31880
Sequence Length: 294
Subcellular Location: Cell membrane
EC: 3.4.21.89
|
B8E2W9 | MGKLYIFDTTLRDGEQTPGVNLNKEEKLEIAKQLAKLNVDIIEAGFPIASPGEFEAVKNIAEKVKGPIIAALARAIPMDIDRAWEAIKYSESPRIHTFIATSDIHIEKKLKKTRDEVLEQAVSAVKYAKRYCSDVEFSAEDAVRSDFNFLVKIFEAVIEAGATVINVPDTVGYALPWEFGELIRRLKENIRNIDKARVSVHCHNDLGLATANSLSAIVNGAEQVECTVNGLGERAGNAAMEEIVMAIKVRRLPFEVSIKTEEIYKTSKLVSNLTGIPIQPNKAIVGENAFAHESGIHQHGVIQDPSTYEIIDPKTIGIPE... | Function: Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-ketoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate).
Catalytic Activity: 3-methyl-2-oxobutanoate + acetyl-CoA + H2O = (2S)-2-isopropylmalate + CoA + H(+)
Sequence Mass (Da): 55320
Seque... |
Q8X9Z8 | MSQQVIIFDTTLRDGEQALQASLSVKEKLQIALALERMGVDVMEVGFPVSSPGDFESVQTIARQVKNSRVCALARCVEKDIDVAAESLKVAEAFRIHTFIATSPMHIATKLRSTLDEVIERAIYMVKRARNYTDDVEFSCEDAGRTPIADLARVVEAAINAGATTINIPDTVGYTMPFEFAGIISGLYERVPNIDKAIISVHTHDDLGLAVGNSLAAVHAGARQVEGAMNGIGERAGNCSLEEVIMAIKVRKDILNVHTAINHQEIWRTSQLVSQICNMPIPANKAIVGSGAFAHSSGIHQDGVLKNRENYEIMTPESIG... | Function: Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-ketoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate).
Catalytic Activity: 3-methyl-2-oxobutanoate + acetyl-CoA + H2O = (2S)-2-isopropylmalate + CoA + H(+)
Sequence Mass (Da): 57314
Seque... |
O31046 | MANRQQPSPMPTAKYRGYDQVDIADRTWPNQRITTAPRWLSTDLRDGNQALIDPMSPVRKRAMFDLLVKMGYKEIEVGFPASGQTDFDFVRSIIEEPGAIPDDVTISVLTQAREDLIERTVESLKGARRATVHLYNATAPVFRRVVFRGSRDDIKQIAVDGTRLVMEYAEKLLGPETEFGYQYSPEIFTDTELDFALEVCEAVMDTYQPGPGREIILNLPATVERSTPSTHADRFEWMGRNLSRREHVCLSVHPHNDRGTAVAAAELALMAGADRIEGCLFGQGERTGNVDLVTLGMNLFSQGVDPQIDFSDIDEIRRTW... | Function: Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-ketoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate).
Catalytic Activity: 3-methyl-2-oxobutanoate + acetyl-CoA + H2O = (2S)-2-isopropylmalate + CoA + H(+)
Sequence Mass (Da): 63323
Seque... |
B2FT78 | MTTIERITTPRIRIFDTTLRDGEQSPGCSMSPPQKLVMARALDELGVDIIETGFPASSQSDREAMALIGRELRRPSLSLAVLSRCLQADIETSARALEAAANPRLHVFLSTSPLHREHKLRMTREQVLESVRKHVSLARSYIDDVEFSAEDATRTELDYLIEVARVAIAAGATTINLPDTVGFTTPEEIRAMFQQVIAGVADVPNAANVIFSAHCHNDLGLAVANSLAAIEGGARQVECTVNGIGERAGNCSLEEIAMVLKVRQAFYEQDSSINTPRIVGTSQLLQRLVGMPVQRNKAIVGANAFAHESGIHQHGMLRHR... | Function: Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-ketoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate).
Catalytic Activity: 3-methyl-2-oxobutanoate + acetyl-CoA + H2O = (2S)-2-isopropylmalate + CoA + H(+)
Sequence Mass (Da): 57161
Seque... |
D2ATJ4 | MKTTTRQTGRYGAFTPVPLPGRTWPNNIIGSAPRWLSTDLRDGNQSLATPMSPDRKLAMFELLVSMGYKEIEVGFPVASQDDFDFLRVLIEQERIPEDVRISVLVQARDELIRRTVESLEGAPRATIHLYNATSPLFRRVVFGMSRNECKDLAVQGTRLMMKYAEKTLGDCDLGFQYSPELFSDTELDFSLEVCEAVMDVWQPEPGRGIILNFPTTVERSLPNVFADQIEWLSRNLSRREHVCLSIHPHNDRGTAVASAELALLAGAERIEGCLFGNGERAGNVCLVTLGLNMFTHGVDPGIDFSDINEIRRTVERCNGL... | Function: Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-ketoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate).
Catalytic Activity: 3-methyl-2-oxobutanoate + acetyl-CoA + H2O = (2S)-2-isopropylmalate + CoA + H(+)
Sequence Mass (Da): 63689
Seque... |
Q4JA78 | MGCLFSVNSKKVRIFDTTLRDGEQAPGIDLTVDQKIRVAKRLAELGVDVIEAGFPASSDGEFEATKKILSEIGDQVEVTGLSRSVKQDIDRTIDTGLSSIHIFIATSDIHLKYKLKMTREEVLNRIYESVRYAKDHGLIVEYSPEDATRSDEEFLLKAVKTAIDAGADRINIPDTVGVMHPFKFYDLISKIVKVTGDKIVSVHCHNDFGLATANSIAGVMAGARQVHVTVNGIGERAGNASLEEVVMSLKKLLGYDVGVRTYLLYEVSRYVAELTGVPVPYFKAIVGENAFGHEAGIHVHGVIENPMTYEPISPEEVGNF... | Function: Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate). Carries out the first step of the leucine biosynthesis pathway. Also displays a low citramalate synthase activity, using pyruvate as ... |
P34738 | MATHNIVVFGGDHCGPEVVLEAIKVLKAIETNSPSAGKFNLQNHLLGGASIDKHNDPLTDEALNAAKAADAVLLGAIGGPEWGTSSTVRPEQGLLKLRKELGTYGNLRPCNFASESLVDSSPLKAEVCRGTDFIVVRELTGGIYFGDRTEDDGSGYACDTEPYSRAEIVRIARLAGFLALAKNPPAKVWSLDKANVLATSRLWRKTVTDVISKEFPQLQLEHQLIDSAAMLLVKNPRALNGVVITSNLFGDIISDEASVIPGSIGLLPSASLGGIPDGKGKCNGIYEPIHGSAPDISGKGIVNPVGTILSVAMMLRYSLN... | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Function: Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate.
Catalytic Activity: (2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl-2-oxopentan... |
Q8EN68 | MEKHIILLPGDGIGREIIDSAKQVLTAIASEYNHRFTFEEHAIGGSAIDEYGTPLPDKTVDACSKADAILLGAVGGPKWDANPSHLRPEKGLLGIRKQLGLFANLRPVKTISSLLYASPLKEEIVSQADMLIIRELTGGIYFGTPSERTTNGVVDTLQYSREEIERIVERGFEAARIRKKHLTSVDKANVLESSKLWREIVEEKSKDYPDVAVNHLLVDAAAMKLVTQPSFFDVIVTENLFGDILSDEASVLTGSLGMLPSASLRADGLGLYEPVHGSAPDIAGKGIANPLAMILSAALMLEHSFGLVDEAKEIERAVND... | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Function: Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate.
Catalytic Activity: (2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl-2-oxopentan... |
Q6FEW0 | MAGTTQGAKTLYDKLWDDHLVSQRDDGSCLIYIDRHLLHEVTSPQAFEGLQLAGRQPWRLNANIATPDHNVPTSKKEREQGIAGIEDDTSRIQVQTLDDNCKTFNIVEFGINDIRQGIVHVVGPEQGLTLPGMTVVCGDSHTATHGAFGCLAHGIGTSEVEHVLATQCLIQKKSKNMLIRVDGQLGKGVTPKDVVLAIIGKIGTAGGTGYAIEFGGQVFRDMSIEGRMTVCNMAIEAGARVGMVAVDDKTIEYVQSRHYAPKGEQWDQAVAYWNTLHSDDDAVFDEVVVLNGAEIEPQVSWGTSPEMVIPVSQAVPTLEQ... | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
Catalytic Activity: (2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate
Sequence Mass (Da): 51659
Sequence Length: 477
Pathway: Amino-acid biosyn... |
Q1IMI3 | MSGPRTLFEKIWSTHVVCVPDDQPPILYIDRHYVHEVTSPQAFDGLRAAGRKVRRTDLTFATVDHNVPTTSPRLVIKDDVAARQIDALRTNCAAFGVPLFDLTSEEQGIVHVIGPELGLTLPGMTIVCGDSHTSTHGAFGAFAFGIGTSEVEHVLATQCLPQRKPKTMKIEVSGTLPEGVTAKDLALGIIGKLGTDGATGHVIEYCGTAIRALSMEARMTLCNMSIEGGARAGLIGPDEITFAYIRNRQYAPKGAEWDTGVAEWAALNTDEGAKFDREIHINAADLQPQVTWGTNPGMVVSVGANVPDPKATSDDAQRQS... | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
Catalytic Activity: (2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate
Sequence Mass (Da): 50657
Sequence Length: 470
Pathway: Amino-acid biosyn... |
Q02142 | MSGKTIFDKLWDQHVIAGNEGEPQLLYIDLHVIHEVTSPQAFQGLREAGRRVRRKDLTYGTLDHNVPTQDIFNIQDLISKKQIDTFTKNVKEFDVPAETHGGKGQGIVHMVAPESGRTQPGKTIVCGDSHTATNGAFGAIAFGIGTSEVEHVLATQTIWQVKPKRMKIEFQGHPQKGIYSKDFILALIAKYGVDAGVGYAVEYSGDAISDLSMEERMTICNMSIEFGAKIGLMNPDEKTYDYVKGREHAPKNFDEAVSKWEKLVSDSDAQYDKILSLDVSQLKPMVTWGTNPGMGLEFGEKFPEINNDLNYERAYQYMDL... | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
Catalytic Activity: (2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate
Sequence Mass (Da): 50491
Sequence Length: 460
Pathway: Amino-acid biosyn... |
Q63DX5 | MEPFRIHKGTAAVLMNDNIDTDQIIPKQYLKRIERTGFGKFLFDEWRYDNERHENPNFPLNAPDRKGASILITGDNFGCGSSREHAPWALADYGFRVIIAGGFADIFYMNCMKNGMLPIVMDKDMRENLTKTDAREQIEVDLENEVITTSTHRFHFTIEKMWKEKLLNGLDEISITMQYEQEIREYERKVAVY | Function: Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
Catalytic Activity: (2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate
Sequence Mass (Da): 22594
Sequence Length: 193
Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3... |
A0ZZS8 | MEKLTTLTGVAVPLRRSNVDTDQIIPAVFLKRVKKSGFDDALFYAWRRDPEFVLNKPEYKQGKILVAGPDFGIGSSREHAVWALHDYGFRVVISSRFADIFYGNTAKNGVLAAIMPQESIELLWKLLDEEPGREMTVSLEDRTVTCGDVTLPFEVNDYTRWRLMNGYDDIDLTLQHEDDIIAYEKMRAEKFPFKPKTLPVKREPEQPIESAREGEYPDWQGPLADRGII | Function: Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
Catalytic Activity: (2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate
Sequence Mass (Da): 26240
Sequence Length: 229
Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3... |
Q89X27 | MDKFTTLEGVAAPLKIINVDTDMIIPKQYLKTIKRTGLGKGLFSEQRYKDDGSENPDFVLNQPAYRNTKVLVAGDNFGCGSSREHAPWALLDFGIRCVISTSFGDIFYNNCFKNGILPIRVSQEDLDKLFDDAERGANATLTIDLPNQEIRGPDGGKVKFEIDPFRKHCLINGLDDIGLTMEKKASIDTYEDKLKRERAWA | Function: Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
Catalytic Activity: (2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate
Sequence Mass (Da): 22567
Sequence Length: 201
Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3... |
Q50974 | VDRPFKEVEANEGYRLSIDLAEQTLTTPGGETFTFDITEHRKHCLLNGLDEIGLTLQHADKIKAFEEKRRQSQPWLFNG | Function: Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
Catalytic Activity: (2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate
Sequence Mass (Da): 9101
Sequence Length: 79
Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-m... |
P50181 | RQILLTRKNFGCGSSREHAPWALDDYGFRAIIAPSFADIFFNNCYKNGLLPIVLTEEQVDRLFKEVEANEGYRLSIDLAEQTLTTPSGETFTFDITEHRKHCLLNGLDEIGLTLQHADEIHAFEEKRRQSQPWLFNG | Function: Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
Catalytic Activity: (2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate
Sequence Mass (Da): 15758
Sequence Length: 137
Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3... |
Q9JZI6 | MKAFTKITAIVAPLDRSNVDTDAIIPKQFLKSIKRSGFGPNAFDEWRYLDHGEPGMDNSKRPLNPDFSLNQPRYQGAQILLTRKNFGCGSSREHAPWALDDYGFRAVIAPSFADIFFNNCYKNGLLPIVLTEERVDRLFKEVEANEGYQLSIDLAEQTLTTPSGETFTFDITEHRKHCLLNGLDEIGLTLQHADEIHAFEEKRRQSQPWLFNG | Function: Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
Catalytic Activity: (2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate
Sequence Mass (Da): 24264
Sequence Length: 213
Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3... |
A1SLW4 | MDKFTTHTGVGIPLRRSNVDTDQIIPAVYLKRVTRTGFEDGLFAAWRNDPSFVLNNEGYAGASVLVAGPDFGTGSSREHAVWALQNYGFKVVISPRFADIFRGNSGKAGLLAAQVDESVVQKIWDLLDEHPGTAVTVDLESRTVRAGEGVDAIEASFDIDDYTRWRLLEGLDDIGITLGHADAIASYEATRPSWRPATIHAH | Function: Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
Catalytic Activity: (2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate
Sequence Mass (Da): 22057
Sequence Length: 202
Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3... |
Q8YX03 | MVSEVREVTGRAIPLVGNDIDTDRIIPARYLKAITFDGLREGAFIDDRTALKGAHPFDQPQYQDANILIVNRNFGCGSSREHAPQALSKWGIQAVIGESFAEIFFGNCVAIGVPCVTADEAIVKQLQELVAANPQANVSINLETLQVQVGDFIAPISIGEGTRSTFITGAWDACGQLVANTEQVRVTAAKLPYVSWGKLAAS | Function: Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
Catalytic Activity: (2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate
Sequence Mass (Da): 21687
Sequence Length: 202
Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3... |
A8AHJ0 | MFAEYGVLNYWTYLVGAIFIVLVPGPNTIFVLKNSVGRGMKGGYLAASGVFIGDAVLMFLAYAGVATLIKTTPVLFNIVRYLGAFYLLYLGAKILYATLKSKGSEVAHDEVPFGAIFKRALILSLTNPKAILFYVSFFVQFIDVNAPHAGLSFFILATTLEVVSFFYLSFLIISGAFVTQYIRTKKKLAKVGNSLIGLIFVGFAARLATLQS | Function: Exporter of leucine.
Catalytic Activity: H(+)(out) + L-leucine(in) = H(+)(in) + L-leucine(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 23132
Sequence Length: 212
Subcellular Location: Cell inner membrane
|
B9E1Z5 | MTERSNNRQSQIYNFIKSQIKQKGYPPSVREICTAVGLKSTSTVHSYLEKLERRGFIKRDATKSRTIEVIEKSQKKEMIEVPIIGTITAGMPIIAVENIEDYFPLPMDYIKNKREIFMLRVKGESMVDAGILDGDLSLIEKVHSAENGDIVVALIENEATLKRFFKEENHIRLQPENKNMPPIIVDDCKIIGRLIGIYRQYE | Function: Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually ... |
Q8NP86 | MPNGKPDPASLSDRQRRILEVIRDAVVLRGYPPSIREIGDAAGLQSTSSVAYQLKELEKKGFLRRDPNKPRAVDVRHLPETESRSSKAATQAKSKAPQAGVHDPELAGQTSFVPVVGKIAAGSPITAEQNIEEYYPLPAEIVGDGDLFMLQVVGESMRDAGILTGDWVVVRSQPVAEQGEFVAAMIDGEATVKEFHKDSSGIWLLPHNDTFAPIPAENAEIMGKVVSVMRKL | Function: Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually ... |
Q4JV87 | MSIDESSDNPTPRPKLGRPPKSEADKRAEKEAQKDGKKPALSTRQRRILEVIRDSTIIRGYPPSIREIADAVGLHSTSSVSYHLTQLEKRGYLRRDGKRPRAVDVRAFDGGQLTNESTKKNAGSPQPTSAAIPEPTTEGETMPEATYVPVVGQIAAGAPILAEQNVEAHFPLPQELVGNGELFLLQVVGESMHDAGIFNGDWVVVRSQSVAEFGDFVAAMIDGEATVKEFQKDADGLWLIPHNPLFEPIPAEEATILGKVAAVLRKI | Function: Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually ... |
Q0K9E3 | MATLTPRQQQIFDLIRNTIRRTGFPPTRAEIAAEFGFSSPNAAEEHLRALARKGVIELTPGASRGIRLKVAHSDSEMPDQFSLPMAGVMQLTLPLVGRVAAGSPILAAEHIDRQYQVDASVFDERPDYLLRVRGLSMRDAGILDGDLLAVRRASEAANGKIVVARLGDDVTVKRLQRRGGHIELIAENPDFTNIIVEPGEEFSLEGIAVGLIRSSGF | Function: Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually ... |
Q5NR31 | MLTRKQHDLLLFIHNRLSVSGISPSFEEMKLALDLKSKSGIHRLIKALEERGFIRRLPNRARALEVIRLPEDKTEIQKKISRDYTPPKADNDVIEIPLHGRIAAGLPIEALEGQSHLAVPPSYLGSGAHYALEVAGDSMVDAGIFDGDYIIVRQTDEAHEGEIVVALIDNSDATLKYFHREGRMVRLDPANRAYAPMRYDASRIGIQGRLVGLLRRY | Function: Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually ... |
P19256 | MVAGSDAGRALGVLSVVCLLHCFGFISCFSQQIYGVVYGNVTFHVPSNVPLKEVLWKKQKDKVAELENSEFRAFSSFKNRVYLDTVSGSLTIYNLTSSDEDEYEMESPNITDTMKFFLYVLESLPSPTLTCALTNGSIEVQCMIPEHYNSHRGLIMYSWDCPMEQCKRNSTSIYFKMENDLPQKIQCTLSNPLFNTTSSIILTTCIPSSGHSRHRYALIPIPLAVITTCIVLYMNGILKCDRKPDRTNSN | Function: Ligand of the T-lymphocyte CD2 glycoprotein. This interaction is important in mediating thymocyte interactions with thymic epithelial cells, antigen-independent and -dependent interactions of T-lymphocytes with target cells and antigen-presenting cells and the T-lymphocyte rosetting with erythrocytes. In addi... |
F4JIE8 | MAKSDIETGGGNELYPGMKESSELRWAFIRKLYSILSLQLLVTVGVSAVVYFVRPIPEFITETHRGLAVFFVILLLPLLLLWPLLAFEKKHPINCIVLSIFTLSISFSVGICCSLSQGRIVLEAAILTAVMVFGLTIYTFWAVKRGHDFSFLGPFLFGALLIILVFTLLQIFHPLGKLSSMIFSGIASIVFCGYIIFDTNQLIKKLNYDEYITAAIRLYLDVMNLFLSLLGIISN | Function: (Microbial infection) Facilitates the development of the powdery mildew fungus E.cruciferarum.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 26272
Sequence Length: 235
Subcellular Location: Membrane
|
Q9K1E9 | MRIPLLAPDNYAFPDPAYALARCDGLVGVSGDLDAGRLLEAYRNGVFPWFSRDGWFFWYAVGPRAVVFPDRLHIPRSLAKTLRNGSYRVAVNGCFAEVVAHCAAAARPNQDGTWIAPEFQTAYLKLHEMGYAHSFECHYPDESGETRLAGGFYGVQIGRVFYGESMFALQPDASKIAFACAVPFLADLGVELIDCQQDTEHMRRFGSELLPFADFAERLRMLNAVPLKEEIGRREVACKGL | Function: Functions in the N-end rule pathway of protein degradation where it conjugates Leu, Phe and, less efficiently, Met from aminoacyl-tRNAs to the N-termini of proteins containing an N-terminal arginine or lysine.
Catalytic Activity: L-leucyl-tRNA(Leu) + N-terminal L-lysyl-[protein] = H(+) + N-terminal L-leucyl-L... |
Q0AIB2 | MIRTLFSDTPFPPLEQALIEPNGLLAAGGDLSPERLISAYQQGIFPWFNQGEVILWWSPNPRMVLFPQELKISRSLHKTLKKNHYQIRTDSAFTQVMQACAAPREKQTGTWIHPEMVAAYTTLHQRGIAHSVETWVDGELVGGLYGVAIGKAFFGESMFSRVPDASKIALVYLARQLERQGYGLIDCQMKTAHLMSMGAREIPRLQFSKLLGKLTDQPEQNRKWHFDFTWPKQQ | Function: Functions in the N-end rule pathway of protein degradation where it conjugates Leu, Phe and, less efficiently, Met from aminoacyl-tRNAs to the N-termini of proteins containing an N-terminal arginine or lysine.
Catalytic Activity: L-leucyl-tRNA(Leu) + N-terminal L-lysyl-[protein] = H(+) + N-terminal L-leucyl-L... |
Q82ST5 | MIRTLYSDTPFPPLEQALIEPNGLLAAGGDLSPERLISAYRQGIFPWFNPGEIILWWSPDPRMVLFPRELKISRSLHKTLKKNDYQIRTDSAFTEVMQACAAPREDQAGTWIHEEMIAAYTALHQMGVAHSVETWIEGELAGGLYGVAIGRAFFGESMFSRATDASKIALVHLARQLENWGYGLIDCQMKTAHLMSMGAREIPRSQFSKRLNQLNALPGQNRKWYFDFTYPGRSEQ | Function: Functions in the N-end rule pathway of protein degradation where it conjugates Leu, Phe and, less efficiently, Met from aminoacyl-tRNAs to the N-termini of proteins containing an N-terminal arginine or lysine.
Catalytic Activity: L-leucyl-tRNA(Leu) + N-terminal L-lysyl-[protein] = H(+) + N-terminal L-leucyl-L... |
Q2Y5H5 | MIPWLSSDSLFPPLHTALIQPNGLLAVGGDLSPRRLIEAYSQGIFPWFNDGDPILWWSPDPRMVLFPRELKVSRSLQKSLRKGNYEIRTDRNFTPVMRACAAPRRDSCGTWIQNKMIFAYSALHEMGFAHSVETWMDGELVGGLYGVALGRVFFGESMFSRVSNASKIAFVHLVRQLERWGFEMIDCQMKTAHLASLGAREIPREEFSQRLKELVNYMERGEKWCFDHEQVE | Function: Functions in the N-end rule pathway of protein degradation where it conjugates Leu, Phe and, less efficiently, Met from aminoacyl-tRNAs to the N-termini of proteins containing an N-terminal arginine or lysine.
Catalytic Activity: L-leucyl-tRNA(Leu) + N-terminal L-lysyl-[protein] = H(+) + N-terminal L-leucyl-L... |
Q3J7Z7 | MEEFHCIDSNRLANAFPHPRLALAEPNGLLAVGGDLSPERLIMAYRQGIFPWYNQGQPILWWSPDPRLILFPQQLHISRSLHKRLRRGIYQVTLDLDFPGVIQACASPRQDGEGTWITSEMKSAYNRLHEMGIAHSVETWEDKELIGGLYGVSIGRIFFGESMFSKRPDASKIAFVYLCRQLQRWGFPLIDCQIQSEHLQRLGAQTLPRNKFLHWLHEFSNSPSLKRPWHFDPDLLKNSL | Function: Functions in the N-end rule pathway of protein degradation where it conjugates Leu, Phe and, less efficiently, Met from aminoacyl-tRNAs to the N-termini of proteins containing an N-terminal arginine or lysine.
Catalytic Activity: L-leucyl-tRNA(Leu) + N-terminal L-lysyl-[protein] = H(+) + N-terminal L-leucyl-L... |
Q8YQ68 | MQYDIASIIQGYAQGYFLMADDNDCLGWYGSRDRTLIPLDERFRYPKSLQRVLNQERFTVAINRDFAAVVAGCANRESTWISQELQEIYRLLYQTGYAYSFETWQGEELAGGILGIVIGGAFIGESMFYRIPEGSKVAMVKLVERLRQREFVMFDAQMMNPHLERFGAYRIKDKEYKTLLEKALLSPSTLI | Function: Functions in the N-end rule pathway of protein degradation where it conjugates Leu, Phe and, less efficiently, Met from aminoacyl-tRNAs to the N-termini of proteins containing an N-terminal arginine or lysine.
Catalytic Activity: L-leucyl-tRNA(Leu) + N-terminal L-lysyl-[protein] = H(+) + N-terminal L-leucyl-L... |
Q2GA52 | MSRIEPHAIPPELLLKAYRAGIFPMADSRDDPEVFWVEPKMRAILPLEGFHLSRSLARTLRRGKFTVTCNAAFEAVIDACAAPRPGAEESWISARIRESYIGLHEHGHAHSIECWHNGRLVGGLYGVGFARVFCGESMFSREPDASKVALAWLVASLRKVGAELLDCQFTTPHLASLGAVEIPQSQYLQLLSKAQRPYSSGELAAARALADAVGDGLGIGGAGVVKGDAAALGLPAGFAALRAEGAGSSSPGNVIAQSLTHTS | Function: Functions in the N-end rule pathway of protein degradation where it conjugates Leu, Phe and, less efficiently, Met from aminoacyl-tRNAs to the N-termini of proteins containing an N-terminal arginine or lysine.
Catalytic Activity: L-leucyl-tRNA(Leu) + N-terminal L-lysyl-[protein] = H(+) + N-terminal L-leucyl-L... |
A1B1I1 | MSGGLTAERMLAAYAQGVFPMAESASAAQLYWFEPALRGILPVGGVHVSRSMRRFLRHCDWRATIDNDFAGVVAGCADREETWINAPLLALYQDLFRMGHAHSLEIRAGEDLIGGMFGLTLGGAFFAESMFSRRSNASKAALIWMSSHLARCGFTLWDTQYPNPHLASMGGRAIPRLEYRRRLAAALRIPADFTAHALPDVQALLQEITQTS | Function: Functions in the N-end rule pathway of protein degradation where it conjugates Leu, Phe and, less efficiently, Met from aminoacyl-tRNAs to the N-termini of proteins containing an N-terminal arginine or lysine.
Catalytic Activity: L-leucyl-tRNA(Leu) + N-terminal L-lysyl-[protein] = H(+) + N-terminal L-leucyl-L... |
Q6D3U2 | MRLYQLSPQSLQFPDPNHALDNPNGLLAVGGDLSVARLKVAYRQGIFPWFSPGEPILWWSPNPRAVLLPGELHLSRSMKKFLKRHTFHATLNQAFDDVIHACAQEHHDGTWITPDIISAYRQLHQVGKAHSVEVWHNGALVGGLYGIEQGRLFCGESMFSRMDNASKYALLAFQQHFIRHGGHLIDCQVLNSHTASLGVSEIPRVRFLQQLSQWQDIAVEEGCWLPQQLAEPAF | Function: Functions in the N-end rule pathway of protein degradation where it conjugates Leu, Phe and, less efficiently, Met from aminoacyl-tRNAs to the N-termini of proteins containing an N-terminal arginine or lysine.
Catalytic Activity: L-leucyl-tRNA(Leu) + N-terminal L-lysyl-[protein] = H(+) + N-terminal L-leucyl-L... |
Q95Y52 | MQYLQFLSLVVLLLMCHARKSVYRRNSPSLRRLTRNYDWEVDEHGGLKPIINPAKVERATKNCANDSFILGTIMSNYNRHKIPGGQVDVEVEVWVQEITTISDITSDFQLDIYIYETWYDPALNYAFMNPCKYNLSLNSVLLEKLWTPNSCFINSKTADIHKSPFPNIFLMIYANGTVWTNYRLKLQGPCIMDLTKFPFDNVTCSLTFESFNYNTDEVKMDWSVNGVQKMRDKMELADYELVDIHKIRTTEEYPAGYWHELTMSFEFKRRAGWYILQAYLPTYLTICISWISFALGSKAIPARTMLGVNSLLAMTFQFGN... | Function: Probable component of a ligand-gated anion channel. Negatively regulates synaptic transmission and synaptic vesicle release in response to acetylcholine in cholinergic motor neurons. Role in synaptic vesicle release kinetics may be in association with the ligand-gated ion channel protein acc-4.
Location Topol... |
P54245 | MIICYSCLTVSILLTIKFVPCRFAGIEHQNTKSRVHFSLLDSRQENDTNHFEIAEAKFQKPHNEENTIGTITKFAPSVQEQHSSAVIPMPHFDQNRLEQALRIKGSIDGTEEALYRSLLDHTVYEKDVRPCIHHSQPTNVTFGFLLNQIVEMDERNQALTTRSWLNINWMDPRLSWNESLWSEIKAIYIPHARIWKPDIILVNNAIREYYASLVSTDVMVTSDGNVTWLFSALFRSSCPIRVRYYPFDDQQCDLKFASWSHDITEINLGLNTDKGDLSSYMNNSEFDLVDMTAVREVVTFPSDTNSDWPIIVIRIHMHRR... | Function: Possible acetylcholine receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 72916
Sequence Length: 635
Subcellular Location: Postsynaptic cell membrane
|
Q0QWS4 | MSEVTITGFRSRDVRFPTSLDKTGSDAMNAAGDYSAAYCILETDSAHSGHGMTFTIGRGNDIVCAAINHVADRLKGKKLSSLVADWGKTWRYLVNDSQLRWIGPEKGVIHLALGAVVNAVWDLWAKTLNKPVWRIVADMTPEEYVRCIDFRYITDAITPEEAVAMLREQEAGKAKRIEEALQNRAVPAYTTSAGWLGYGEDKMKQLLRETLAAGYRHFKVKVGGSVEEDRRRLGIAREILGFDKGNVLMVDANQVWSVPEAIDYMKQLSEYKPWFIEEPTSPDDIMGHKAIRDALKPYGIGVATGEMCQNRVMFKQLIMT... | Cofactor: Divalent metal ions. Magnesium seems to be the preferred ion.
Function: Mediates the conversion of L-galactonate to 2-dehydro-3-deoxy-L-galactonate, the second step in D-galacturonate catabolic process.
Catalytic Activity: L-galactonate = 2-dehydro-3-deoxy-L-galactonate + H2O
Sequence Mass (Da): 50124
Sequenc... |
F0M433 | MQNLNVGLIGGGFMGKAHSLAYAAMPMFFWPAPALPVRKVIAEANPELAAEAARRFGFENSTSDWRSIIDDPDIHVVDIATPNHLHAEIAIAAAEAGKHIICEKPLARTGEESKAMYDAVKDKNIVHMVAFNYRRTPAVALAKKYIEEGAIGRILSFRGTYLQDWSADPNSPLSWRFQKSIAGSGALGDIATHVIDMARYLVGEFSAVNAVLSTWIPERPLQSGGADALGTVRGGEGPKGPVDVDDEVMTMIRFANGAVGSVEATRNAHGRNNYITFEIHGTEGSIVFNYERRDELQVAFASDQADRRGFRTVYTGPAHP... | Function: Catalyzes the oxidation of levoglucosan (1,6-anhydro-beta-D-glucose, LG) to 3-dehydrolevoglucosan (3-keto-LG) . Exhibits high substrate specificity toward levoglucosan and NAD(+) for the oxidative reaction . Exhibits weak activities (about 4% compared with that of LG) toward L-sorbose and 1,5-anhydro-D-glucit... |
Q21389 | MQSNYSISYFLLILFTGTSSYFTIWNFVDHTRVGAFPEEDYIRLAYIIGGNFMTRLMFMQHFKSVLKYSDHFFRLHLITDENHRSDIHELMTSWNISNCEWFFHNLTEFEKRVAWIPNSHYSKYYGLSKLLIPEIIGNDIGKIMFMDVDIIFQTNIFDLWKQFRNFNNSQVFGMVENLSDWYLNKDGKKSVWPALGRGFNTGIIMFDLDKLRKNGWASKWRVVANKYLRIHGKTAMSDQDIFNAYIHDYPTEIIQIPCAYNYQLGALTKSKELCPETPLALHFNSQNKTVGKNYAFFDKIRKAFDEMDGSDLKRRRRSFK... | Function: Probable glycosyltransferase.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 74525
Sequence Length: 631
Subcellular Location: Golgi apparatus membrane
EC: 2.4.-.-
|
Q8R980 | MDIPSLSPYAFKFGPIAVHWYGIFMAISIAVGGYYLYKQATKLNYDEDFLLNLLMIVVIFGVIGARLMFVLANYPEWFVKDPVQVFKIYEGGLSWHGAVLGGFLAGLYYCRKKGVRINPLEDFAVVGLALGNMLVRVGNIFNHEVLGRPTEFFFGRWPAQLVGVAIGAFLLIRYFYVQKKHMPDGYQFWSFIFYYQLLRGVFEETVKDVPLVWPVYLNEEWGIGLFTMTQVATPFILILAYWMIKRVLNDPNRQYYD | Function: Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins.
Catalytic Activity: 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + L-cysteinyl-[prolipoprotein] = H(+... |
A7GZR7 | MSTWNDIYNHFDPVAFTLFGFSVHWYGIMYILALLSALGAAKYFVKKDNIPITDALLDNYFFWVEIGVILGARLGYIAIYSGEAVYFFTHPWQIFNPFHNGEFVGIRGMSYHGAVVGFLLATILFCKKYKQNLWQLLDLCALCIPFGYIFGRIGNFLNQELFGRATDVSWGINVFGILRHPSQLYEAALEGLAVFLILFFYRKFKKFDGELIALYAVLYTLARFVCEFFREPDAGIGFIIFGLSMGQILSILMFFGGILAYFFLKKNYIK | Function: Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins.
Catalytic Activity: 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + L-cysteinyl-[prolipoprotein] = H(+... |
Q9JZF9 | MITHPQFDPVLISIGPLAVRWYALSYILGFILFTFLGRRRIAQGLSVFTKESLDDFLTWGILGVILGGRLGYVLFYKFSDYLAHPLDIFKVWEGGMSFHGGFLGVVIAIRLFGRKHGIGFLKLMDTVAPLVPLGLASGRIGNFINGELWGRVTDINAFWAMGFPQARYEDAEAAAHNPLWAEWLQQYGMLPRHPSQLYQFALEGICLFTVIWLFSKKQRSTGQVASLFLGGYGIFRFIAEFARQPDDYLGLLTLGLSMGQWLSVPMIVLGIVGFVRFGMKKQH | Function: Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins.
Catalytic Activity: 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + L-cysteinyl-[prolipoprotein] = H(+... |
Q5YYN2 | MTLRSDVLAYIPSPPQGVWHIGPIPLRAYALCIILGIVVAIWWGERRWQQRGGREGTVLDVAMFAVPFGLIGGRAYHVATDWRKYFGEGGNPVEALYIWQGGLGIWGAVFLGGIGAWIACRIYRIPLPAFGDAIAPPILLAQAIGRLGNWFNQELYGRETTLPWGLEIYPRFDAAGDPDPMNGISNGVVEKIVHPTFLYELLWNVLVVIALVQLDKRFRIGHGRLFALYVAGYSFGRFFVELMRDDEATLVAGIRINNFTSALVFLAAIAYFVFATKGREAPERLQPGGTTRPWPWQLAALRAAGVAANGPAEPGATAST... | Function: Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins.
Catalytic Activity: 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + L-cysteinyl-[prolipoprotein] = H(+... |
Q8CX97 | MLHTAAPIDRVAIEIGPLSIYWYGIIIAFGAILAIYLASKEADRLGLTKDLMLDFVMFAVPIAIIFARIYYVFFEFDQYANGPWWKVFAIWEGGIAIHGAVIGGVITAIVFAKVRKVSFWQIADIVAPSLILGQAIGRWGNFVNQEAHGGPISQATYESFHQYLPDFIMNQMTINGVMYHPTFLYESVWNILIFVGLLLLRKYNPVRGEVFLTYAITYSIGRYFIEGLRTDSLYMFDIIRTAQFISILIIIVSIIFIIYRRKTVSERYLDAPPSNKKKNKKSTKKKK | Function: Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins.
Catalytic Activity: 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + L-cysteinyl-[prolipoprotein] = H(+... |
P60966 | MQPLVLPGFFIPSPTVSAVEIGPLTIRFYALCILAGIVIGAWLTARRFRARGGTTAQAMDIIMWAVPFGIVGGRLYHVITDNQLYFGPGKDPWGAFRIWEGGLGIWGAVAVGLAGAAIGARRTGVRLATFADAAAPGLLLAQAMGRWGNWFNNELYGEPTNLPWKLQIHNMNPATGQAVLTADGTPETLGYFQPTFLYESLWCLAAAALLVFLDRRYKLGAGSVFALYVVLYTAGRFIFELMRSDYANTILGLRVNTWVSALLFLAALAVFLILRSRPRSASTAQSACSIDGFDTRANGHDPEKHDETDGKGNRHHVP | Function: Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins.
Catalytic Activity: 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + L-cysteinyl-[prolipoprotein] = H(+... |
Q6MC92 | MLTEHWLAWLYWNPPREAFTLPFIDHPVMWYGICFITGFILGYFIIVPIIALFVNQSKHLSSMDIQDWRSLVNQLKTSSSPLIQKCQNALNRQERQKLNSEIQPLNISSDLKNALLIKLNTILKENSIQRKDLEQAFQGAITSAKQISYFLADRLCWFIVFGTLIGARLGAVFFYDWNYFKSHPLEIFEVWKGGLASHGGALGVMLALFFYTSYIKKWTPTLSFLRVLDFVAIPSALTAVFIRIGNFFNQEIIGTPSAYPWAVLFAQPADGSLPIPRHPVQLYEAFAYLMTFFLLFTLWKKCNTCLAAGTYAGFLFIFNF... | Function: Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins.
Catalytic Activity: 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + L-cysteinyl-[prolipoprotein] = H(+... |
I0HUL8 | MAERKGSISGLTDDEAQEFHKFWVQGFVGFTAVAVVAHFLVWVWRPWL | Function: Antenna complexes are light-harvesting systems, which transfer the excitation energy to the reaction centers.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 5550
Sequence Length: 48
Subcellular Location: Cell inner membrane
|
Q3J145 | MTDDLNKVWPSGLTVAEAEEVHKQLILGTRVFGGMALIAHFLAAAATPWLG | Function: Antenna complexes are light-harvesting systems, which transfer the excitation energy to the reaction centers.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 5448
Sequence Length: 51
Subcellular Location: Cell inner membrane
|
P11696 | TDIRTGLTDEECQEIHEMNMLGMHAYWSIGLIANALAYAWRPFHQGRAGNRLEDHAPDYVRSALT | Function: Antenna complexes are light-harvesting systems, which transfer the excitation energy to the reaction centers.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 7415
Sequence Length: 65
Subcellular Location: Cell inner membrane
|
P35095 | MADKPLTADQAEELHKYVIDGARAFVAIAAFAHVLAYSLTPWLH | Function: Antenna complexes are light-harvesting systems, which transfer the excitation energy to the reaction centers.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 4853
Sequence Length: 44
Subcellular Location: Cell inner membrane
|
P07368 | MTDDKAGPSGLSLKEAEEIHSYLIDGTRVFGAMALVAHILSAIATPWLG | Function: Antenna complexes are light-harvesting systems, which transfer the excitation energy to the reaction centers.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 5155
Sequence Length: 49
Subcellular Location: Cell inner membrane
|
P35107 | MADDPNKVWPTGLTIAESEELHKHVIDGTRIFGAIAIVAHFLAYVYSPWLH | Function: Antenna complexes are light-harvesting systems, which transfer the excitation energy to the reaction centers.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 5732
Sequence Length: 51
Subcellular Location: Cell inner membrane
|
P95654 | MTDDMDKVWPTGLTLAEAEEVHKQLIDGTRVFGAIALFAHFLAAIATPWLG | Function: Antenna complexes are light-harvesting systems, which transfer the excitation energy to the reaction centers.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 5569
Sequence Length: 51
Subcellular Location: Cell inner membrane
|
P80591 | AEDRKSLSGLTEQEAQEFGTLYTQGVAFVAVIAIVAHALVWAWRPWLQ | Function: Antenna complexes are light-harvesting systems, which transfer the excitation energy to the reaction centers.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 5358
Sequence Length: 48
Subcellular Location: Cell inner membrane
|
P35096 | AVLSPEQSEELHKYVIDGARAFLGIALVAHFLAFSATPWLH | Function: Antenna complexes are light-harvesting systems, which transfer the excitation energy to the reaction centers.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 4506
Sequence Length: 41
Subcellular Location: Cell inner membrane
|
P35097 | ADDVKGLTGLTAAESEELHKHVIDGTRVFFVIAIFAHVLAFAFSPWLH | Function: Antenna complexes are light-harvesting systems, which transfer the excitation energy to the reaction centers.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 5278
Sequence Length: 48
Subcellular Location: Cell inner membrane
|
P26790 | ATLTAEQSEELHKYVIDGTRVFLGLALVAHFLAFSATPWLH | Function: Antenna complexes are light-harvesting systems, which transfer the excitation energy to the reaction centers.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 4554
Sequence Length: 41
Subcellular Location: Cell inner membrane
|
P35098 | AEDRSSLSGVSDAEAKEFHALFVSSFMGFMVVAVLAHVLAWAWRPWIPGPKGWA | Function: Antenna complexes are light-harvesting systems, which transfer the excitation energy to the reaction centers.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 5917
Sequence Length: 54
Subcellular Location: Cell inner membrane
|
P35099 | AEDRSSLSGVSDAEAKEFHALFVSSFTAFIVIAVLAHVLAWAWRPWIPGPKGWA | Function: Antenna complexes are light-harvesting systems, which transfer the excitation energy to the reaction centers.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 5897
Sequence Length: 54
Subcellular Location: Cell inner membrane
|
P80260 | AEIDRPVSLSGLTEGEAREFHGVFMTSFMVFIAVAIVAHILAWMWRPWIPGPEGYA | Function: Antenna complexes are light-harvesting systems, which transfer the excitation energy to the reaction centers.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 6261
Sequence Length: 56
Subcellular Location: Cell inner membrane
|
Q16W22 | MSQISSNLLRNTVQNGKFGCLKNSIQCKHTAANPLEKIRERLESGPSFQDFVQNPSYNRDDWTDYEGKLRREKGENDRLRLPPWLKTKIPMGKNFSRIKDQLRELKLATVCEEAKCPNIGECWGGGEHGTQTATIMLMGDTCTRGCRFCSVKTARVPPPLDPAEPTNTASAIASWGLDYIVLTSVDRDDLPDGGSNHIAATIREIKRQNPRIFVECLAPDFRGDLECVKVVAQSGLDVYAHNIETVEALTPFVRDRRARYRQSLDVLRSIKEINPSMITKTSIMLGLGETDEQIEQTMKDLRSVGVDCLTLGQYMQPTKR... | Cofactor: Binds 2 [4Fe-4S] clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes,... |
Q9ZWT1 | MHSRSALLYRFLRPASRCFSSSSAVTPVTVTQSPKSLEALRARLANESPSLTDFIHGDTYSVEVGTKKKPLPKPKWMKESIPGGERYVQIKKKLRDLKLHTVCEEAKCPNLGECWSGGETGTATATIMILGDTCTRGCRFCNVKTSRTPPPPDPNEPNNVAEAIASWGVDYVVITSVDRDDLPDQGSGHFAETVQRLKFLKPEMLIEALVPDFRGDGGCVEKVSKSGLDVLAHNIETVEELQSFVRDHRANFKQSLDVLRMAKEYAPAGTLTKTSVMLGCGETPDQVVKTMEKVRAAGVDVMTFGQYMRPSKRHMPVAEY... | Cofactor: Binds 2 [4Fe-4S] clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes,... |
O32198 | MRKKMLASLQWRAIRMTTGISLLLFVCLISFMMFYYRLDPLVLLSSSWFGIPFILILLLISVTVGFASGYMYGNRLKTRIDTLIESILTFENGNFAYRIPPLGDDEIGLAADQLNEMAKRVELQVASLQKLSNERAEWQAQMKKSVISEERQRLARDLHDAVSQQLFAISMMTSAVLEHVKDADDKTVKRIRMVEHMAGEAQNEMRALLLHLRPVTLEGKGLKEGLTELLDEFRKKQPIDIEWDIQDTAISKGVEDHLFRIVQEALSNVFRHSKASKVTVILGIKNSQLRLKVIDNGKGFKMDQVKASSYGLNSMKERAS... | Function: Member of the two-component regulatory system LiaS/LiaR probably involved in response to a subset of cell wall-active antibiotics that interfere with the lipid II cycle in the cytoplasmic membrane (bacitracin, nisin, ramoplanin and vancomycin). Seems also involved in response to cationic antimicrobial peptide... |
Q21452 | MLARVWVRGLAATKKKPQVLVKDGPSLQDFISSASVAEAVEKYEGKLKLEKGDRRLRLPPWLKKEKILPSENENVSRLKKQLKHLKLATVCQEARCPNLGECWGGSDDSLATATIMLMGDTCTRGCKFCSVKTARAPPPLDPMEPENTSTAVASWGVEYIVLTSVDRDDLPDGGADHLRKTVQLMKLKKPELLIECLLPDFAGDKISVEKMATSGLDVYAHNIETVERLTPWVRDPRAKYRQSLDALRYAKEVSPKLITKTSIMLGLGEAEDEIKQCLADLRASNVDVVTFGQYMQPTKRHLLVKEWVTPEKFDQWAEYS... | Cofactor: Binds 2 [4Fe-4S] clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes,... |
A8JGF7 | MKRNKLPGGDKYTEIKAKLRELKLSTVCEEARCPNLGECWGGGDGHTATATIMLMGDTCTRGCKFCAVKTSKAPPPLDPHEPENVSKAIAAWGLDYVVLTSVDRDDLPDGGAAHIASTIRLLKQKTEGRLLVEALVPDFQGDMGGVQTIVEAGLDVYAHNIETVERLQGQVRDRRAGWAQSLATLSAAKRVSGGRLLTKSSIMLGCGESREEVVDTLKALRANGVDVVTLGQYMRPTKKHMAVAEFVTPEAFAAYEQIAKDLGFLYVASGPMVRSSYRAGELYITNVLKGRRGGEGEGGEGQQQQQGQQQQQARAATA | Cofactor: Binds 2 [4Fe-4S] clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes,... |
Q6PHG4 | MALISRSCGAASRYSSSHLFLPSKGAEAANVYCNRLSTAASTSSSSSPSPSTHNDRKKDLREDGLNLQDFISGELSEKSKWEEYRGNLKREKGERLRLPPWLKTEIPIGKNYNKLKNTLRELNLHTVCEEARCPNIGECWGGGEYATATATIMLMGDTCTRGCRFCSVKTARRPPPLDPDEPYNTAKAIAAWGLDYVVLTSVDRDDIPDGGAEHFAKTVSNIKERNSKILVECLTPDFRGDLAAVEKIALSGLDVYAHNVETVRELQRHVRDPRANFDQSLSVLRHAKKVKSSVLTKTSIMLGLGETDAQIQATLTELRD... | Cofactor: Binds 2 [4Fe-4S] clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes,... |
Q0KJL4 | MPRRDRNMDSAPCMWMRGGTSKGGYFLRADLPADTAARDAFLLAVMGSPDPRQIDGMGGADPLTSKVAVVSKSERPGIDVDYLFLQVFVDQAIVTDAQNCGNILAGVGPFAIERGLVAASGDETRVAIFMENTGQVAVATVRTPGGSVTYAGDAAIDGVPGTHAPIPTEFRDTAGSSCGALLPSGNAVDVVNGLPVTLIDNGMPCVVMKAADVGITGYEDRDSLDANAELKAKIEAIRLAVGELMNLGDVTEKSVPKMMLVAPPRDGGAVCVRSFIPHRAHATIGVLGAVSVATACLIPGSPAAEVAVVPEGARKTLSIE... | Function: Contributes to the degradation of lignin at the level of the protocatechuate 4,5-cleavage pathway. Catalyzes the isomerization of the double bond between C4 and C5 in (4E)-oxalomesaconate (OMA) to (3Z)-2-keto-4-carboxy-3-hexenedioate (KCH), where the double bond has migrated between C3 and C4 via a 1,3-allyli... |
G2IN04 | MLSAEQNDKLARVGPGTPMGELLRRYWHPIGGESEFETKATRPVRLMGEDLVLYKDLSGNYGLMDRHCPHRRADMACGMVEADGLRCSYHGWMFDAQGACTEQPFEDTANPKGRYKDKVRIKAYPVRALGGLLWAYMGPLPAPELPDWEPFSWKNGFRQIVISVLPCNWLQGQENSMDPIHFEWMHANWSKRLRGETGPYGPKHLKIDFREYDYGFTYNRIREDTDETNPLWTIGRACLWPNAMFTGDHFEYRVPIDDETMMSVGWFFTRVPRDAEPYVQESIPVWHGPIKDAQGEWITSHVMNQDFVAWIGQGTISDRT... | Cofactor: Binds 1 [2Fe-2S] cluster per subunit.
Function: Involved in the catabolism of 5,5'-dehydrodivanillate (DDVA), an intermediate in the biodegradation of lignin. Part of a three-component monooxygenase that catalyzes the O-demethylation of DDVA, leading to the formation of 2,2',3-trihydroxy-3'-methoxy-5,5'-dicar... |
G2IN77 | MAQLKVVTRDGSLHEFEAPDGYTVMEAIRDQGIDELLAICGGCCSCATCHVFVEEAFLDKLPPLKGDEDDLLDSSDHRQANSRLSCQLPIGPELGGMTVTIAPED | Cofactor: Binds 1 [2Fe-2S] cluster.
Function: Involved in the catabolism of 5,5'-dehydrodivanillate (DDVA), an intermediate in the biodegradation of lignin. Part of a three-component monooxygenase that catalyzes the O-demethylation of DDVA, leading to the formation of 2,2',3-trihydroxy-3'-methoxy-5,5'-dicarboxybiphenyl... |
G2ITT5 | MPHFDCLIVGGGHAGAQAAILLRQLKFEGTVGLISGETEYPYERPPLSKDYLAGEKIFDRILLRPRNFWGDQGIELFLGERVKALQPAEHSLTTASGAEFTYGKLIWAGGGVARRLSCPGGTAKGLFTVRTRADVDAVMAVLPQAERFAIVGGGYIGLEAAAVLSKLGKQVTLIEALDRVLARVAGPELSAFFEDEHRAHGVDVRLACGVEAIEADEQDRATGVRLADGTIIPTDAVIVGIGIVPETGPLLLAGASGGNGVDVDEYCLTSLPDVYAIGDCAAHENRFAEGRRVRVESVQNANDQARTAVQHIIGTPAPYD... | Cofactor: Binds 1 FAD per monomer.
Function: Involved in the catabolism of 5,5'-dehydrodivanillate (DDVA), an intermediate in the biodegradation of lignin. Part of a three-component monooxygenase that catalyzes the O-demethylation of DDVA, leading to the formation of 2,2',3-trihydroxy-3'-methoxy-5,5'-dicarboxybiphenyl ... |
P47145 | MPVVHCSSNLPITPYIYERLVYFIKASSISSCISDNLLLVNKTFNDGGCPPHINFCNDEIINPTAGQTVVELVLNAKKGELGSGYLAVDHGKKVVILAFRGSTTRQDWFSDFEIYPVNYSPLCVKEYRKLIEEGKIRECEGCKMHRGFLRFTETLGMDVFKKMESILESFPEYRIVVTGHSLGAALASLAGIELKIRGFDPLVLTFATPKIFNSEMKQWVDELFETDAIEKESILKDEIQFRKGYFRVVHTGDYIPMVPPFYHPAGLEMFINKVGLPQNAEDIEYRGKNNRLTLKDGFREGMSGLVEDWLHVYEHRAYFI... | Function: Lipases catalyze the hydrolysis of the ester bond of tri-, di- and monoglycerides of long-chain fatty acids into fatty acids and glycerol.
Catalytic Activity: a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H(+)
Sequence Mass (Da): 37205
Sequence Length: 328
EC: 3.1.1.3
|
D4Z909 | MSADTETLARKVREEVIKPEQSTLISPDRQSPSLLRREATVEPRFELFHFVFSVCSQKVRGTLMEKGVTFGSNELTILPPQNENYCPQYVRLRLRSEAAAKHRPVSSFTGQSSVDSEGFDPLVVPTLVDHETGRILADSKAICLYLCDALSGGTDLLPADIREAVLKQVQLADTTPHVALLYGADPDGDRRPESMQAVMPGIHAHKIDAVRRNIPLADGDPLLLEAYQHKIVKEEAAASFVINEPQMRTAISKAEQLVTDLDRDLGASTGPWLFGDRFTLADLFWAVSLYRFLWLGYSGFWKDGAGKPRVEAYANRLFAR... | Function: Catalyzes the degradation of 2,5-dichlorohydroquinone (2,5-DCHQ) into hydroquinone (HQ) via chlorohydroquinone (CHQ). Is involved in the degradation pathway that allows S.japonicum UT26 to grow on gamma-hexachlorocyclohexane (gamma-HCH or lindane) as the sole source of carbon and energy. However, the conversi... |
Q9WXE6 | MMQLPERVEGLHHITVATGSAQGDVDLLVKTLGQRLVKKTMFYDGARPVYHLYFGNELGEPGTLYTTFPVRQAGYTGKRGAGQISAVSYNAPVGTLSWWQEHLIKRAVTVSEVRERFGQKYLSFEHPDCGVGFEIIEQDTDGQFEPWDSPYVPKEVALRGFHSWTATLNRNEEMDSFMRNAWNLKPQGRDGNYQRYAFGNGGAAKVLDVYIDEDERPGTWALGEGQVHHAAFEVADLDVQAALKFDVEGLGYTDFSDRKHRGYFESIYVRTPGGVLFEASVTLGFTHDESPEKLGSEVKVAPQLEGVKDELLRTMNDPIV... | Cofactor: Binds 1 Fe(2+) ion.
Function: Cleaves aromatic rings with two hydroxyl groups at para positions with consumption of O(2). Catalyzes the cleavage of chlorohydroquinone (CHQ), as part of the gamma-hexachlorocyclohexane (gamma-HCH or lindane) degradation pathway, producing 5-chlorocarbonyl-4-hydroxy-penta-2,4-di... |
Q5W9E3 | MQFVYDPLPYRVIFGAGSVRRVADELSHVGSRALVLSTPEQAGSAQELAATLGDKAVGLFSKAVMHVPVATVDAAAAVARELDADCTVAIGGGSTVGLAKALSLRLDLPSLVVPTTYAGSEVTPIWGLTEDGIKTTGRDKKVLPKVVVYDPDLTLSLPAEMSIASGLNAIAHAMEGLYAFDGNPIVSLMAEESIRALARSLPLIKADPTDAKARGDALYGCWLAGSVLGAASVALHHKLCHTLGGTFDMPHAQTHTAVLPHAIAYNAPSVPEAMERASRALGGGDPATKLYELAVGLGAEMSLAKLGMPKDGIAKAAALA... | Cofactor: The maleylacetate reductase family of enzymes does not require any metal ion for activity, despite being related to the family III metal-dependent polyol dehydrogenases.
Function: Catalyzes the NADH-dependent reduction of maleylacetate to beta-ketoadipate, a step in the degradation of gamma-hexachlorocyclohex... |
Q84UV0 | MALIATKISSRSCFVSAYPNNSPTFLISKFPNTVDSLSPANTAKRSILRNVHASVSNPSKQFHNKTSLEYLHELNIKKIKNILSANVDVPSENLEMIDVIQSLGIDLHFRQEIEQTLHMIYKEGLQFNGDLHEIALRFRLLRQEGHYVQEIIFKNILDKKGGFKDVVKNDVKGLTELFEASELRVEGEETLDGAREFTYSRLNELCSGRESHQKQEIMKSLAQPRHKTVRGLTSKRFTSMIKIAGQEDPEWLQSLLRVAEIDSIRLKSLTQGEMSQTFKWWTELGLEKDVEKARSQPLKWHTWSMKILQDPTLTEQRLDL... | Cofactor: Binds 3 Mg(2+) or Mn(2+) ions per subunit.
Function: Involved in monoterpene (C10) biosynthesis. The major product is (S)-linalool.
Catalytic Activity: (2E)-geranyl diphosphate + H2O = (S)-linalool + diphosphate
Sequence Mass (Da): 65401
Sequence Length: 569
Domain: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif... |
A0A1L5BU05 | MANRLAGKVALITGGASGLGAAQAKRFAEEGAKVVIGDLNEEMAKGVVAEIRAAGGDALFIRLDVTDAASWNNAIAAAVEAFGGLTTLSNTAGIIHPGGFEEESIEGWNKMVAVNQTAIFLGIKAAIPELVKSGNGSIINISSLIGMFPTAGNASYCATKAAVRIMSKAAALEFVDRGVRVNTIVPGGMNTPITANVPPDVLKQQTSQIPMGKLGDPIDIANGALFLASDEAKYITGVDLPIDGGWSVGV | Function: Catalyzes the degradation of 2,5-dichloro-2,5-cyclohexadiene-1,4-diol (2,5-DDOL) into 2,5-dichlorohydroquinone (2,5-DCHQ) in vitro. LinX appears not to be involved in gamma-hexachlorocyclohexane (gamma-HCH) degradation pathway, in contrast to LinC which has the same enzymatic activity.
Catalytic Activity: 2,5... |
P0DV83 | MQIKNFPFLFLLNSLIIFSCSTIASLPEEPSSPQESTLKALSLYEAHLSSYIMYLQTFLVKTKQKVNNKNYPEFTLFDTSKLKKDQTLKSIKTNIAALKNHIDKIKPIAMQIYKKYSKNIP | Function: Outer membrane lipoprotein that could act as a component of a potential toxin-antitoxin system in B.burgdorferi which could serve as a plasmid stabilization mechanism in a growing bacterial population.
Location Topology: Lipid-anchor
Sequence Mass (Da): 13950
Sequence Length: 121
Subcellular Location: Cell ou... |
Q71DJ5 | MKWLLVAVLTSLTIFSALTQSHLLHGSPVNSLCADLIHPANYSCTEHSIQTKDGYILALQRVASLGPRLQSGPPVLLQHGLFMAGDVWFLNSPKESLGFILADHGFDVWVGNVRGTRYSYGHVTLSDTDKEFWDWSWQDLAMYDLAEMIQYLYSISNSKIFLVGHSQGTIMSFAALTQPHVAEMVEAAALLCPISYLDHVTAPLVERMVFMHLDQMVVALGLHQINFRSDMLVKLVDSLCEGHMDCTDFLTSITGTNCCFNASKIEYYLDYEPHPSSVKNIRHLFQMIRKGTFAQYDYGYFKNLRTYGLSKPPEFILSHI... | Function: Triacylglycerol (TAG) lipase active on triolein, trioctanoin, tributyrin and 1,3-Diolein, but not on phospho- and galactolipids . Involved but dispensable for TAG storage breakdown during seed germination .
Catalytic Activity: a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H(+)
Sequence Mass (Da)... |
D4ASH1 | MAKYDFVMLWILTLTAAIAAARPMVVDKGRQITYTGLDRNGIEVFLGIPFGHDTGGKNRFKPPVAVVPPRGSHINATVYGPICPQELRAGSRGKLVISENCLNLNIGRPKNMTSHDKLAVMVTIYGGGYWVGHNQDPRWHADNMVKESVANGRPIIHVAMNYRLGVFGFAQTTALRTERSENAALRDQRLALEWVRDNIAAFGGDPKRVTIFGQSSGGVSVGMQMLAYGGKQPVPYQQGICQSQVLEPGITGNFTSTAMELVTDKANCTSGDFNSEAALACLRELDTETLLAAAIATYQNGVDHNIGDIWLPSVDGDFLP... | Catalytic Activity: a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H(+)
Sequence Mass (Da): 61599
Sequence Length: 563
Subcellular Location: Secreted
EC: 3.1.1.3
|
Q751M6 | MAIGRYGTLVFYILAGLAFVWSLEYFKHYTKNNYERFHCTAVVEPVQGTATVEKLSAVGGPPCDKRAELKLITQKLTQHFDPNKQPALFCIVENTSVESVHYPVSRTNKGPAGYIAYAGYEADRAAVHKYCEAHGAAVLHM | Function: Component of the ceramide synthase complex required for synthesis of ceramides.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 15669
Sequence Length: 141
Subcellular Location: Endoplasmic reticulum membrane
|
Q9XTR8 | MPKNLRFSVFLLFLLCINSVFGEFGPEDAQYNETEARMLLSLSAAAYSLDVTPCIGRTFSPAENQTLLSTFSVRCDFVGNPCAGYIVVSDVLQQITVVFRGTKTSSQLLLEGWTTLKPSSDFYGMGLVNTYFRSGHEKTWQYVQDALSISQYRNYDVYVTGHSLGGALAGLCAPRIVHDGLRQSQKIKVVTFGEPRVGNIEFSRAYDQLVPYSFRVVHSGDVVPHLPGCVKDLSYTPPAGSDGSMPCDPVSTNGGYHHAIEIWYPGNMTQGDPFMVCTGLPRDEDFGCSDSLKVNLGDTNQGVWDHRNYFGVEVPDFGKG... | Function: Probable lipase.
Sequence Mass (Da): 38743
Sequence Length: 353
Subcellular Location: Secreted
EC: 3.1.1.-
|
O32129 | MAKKDEHLRKPEWLKIKLNTNENYTGLKKLMRENNLHTVCEEAKCPNIHECWAVRRTATFMILGSVCTRACRFCAVKTGLPTELDLQEPERVADSVALMNLKHAVITAVARDDQKDGGAGIFAETVRAIRRKSPFTTIEVLPSDMGGNYDNLKTLMDTRPDILNHNIETVRRLTPRVRARATYDRSLEFLRRAKEMQPDIPTKSSIMIGLGETKEEIIEVMDDLLANNVDIMAIGQYLQPTKKHLKVQKYYHPDEFAELKEIAMQKGFSHCEAGPLVRSSYHADEQVNEASKKRQAQA | Cofactor: Binds 2 [4Fe-4S] clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes,... |
Q8A029 | MADRVRKPEWLKINIGANDRYTETKRIVDSHCLHTICSSGRCPNMGECWGKGTATFMIGGDICTRSCKFCNTQTGRPHPLDANEPTHVAESIALMKLDHAVVTSVDRDDLPDLGAGHWAHTIREIKRLNPQTTIEVLIPDFQGRMELVDLVIEANPDIISHNMETVRRISPLVRSAANYDTSLQVIGHIARSGTKSKSGIMVGLGETPQEVETIMDDLLAVGCQILTIGQYLQPTHRHYPVAEYVTPQQFATYKTIGLEKGFSIVESAPLVRSSYHAEKHIR | Cofactor: Binds 2 [4Fe-4S] clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes,... |
A6GZL9 | METVLDSNILPVGKPKWLKVKLPIGQKYTELRGLVDKYKLNTICTSGSCPNMGECWGEGTATFMILGNICTRSCGFCGVKTGRPETVDWDEPEKVARSIKIMNIKHAVITSVDRDDLKDMGSIIWIETVKAIRRMNPETTLETLIPDFQGVERNLDRIVAANPEVVSHNVETVRRLTREVRIQAKYDKSLEVLRYLKAKGIKRTKSGIMLGLGETEEEVIQTMRDLREANVDIVTIGQYLQPSKKHLPVKEFITPEQFEKYELLGKEMGFRHVESGPLVRSSYHAQKHIL | Cofactor: Binds 2 [4Fe-4S] clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes,... |
Q0RFE8 | MSAVAPEGRPLLRLEARNAQTPIERKPPWIRTRMRTGPEYSDVKGLVRAAGLHTVCEEAGCPNIYECWEDREATFLIGGDVCTRRCDFCQIDSGRPTPLDRDEPRRVAESVRTMGLRYATVTGVARDDLADGGSWLYGETVRQIHALSAGTGVEVLIPDFGGRADQLDEVFGAAPEVLAHNLETVPRIFKRIRPAFRYERSLDVLRQARAAGLVTKSNLILGLGETAEEIHAAMRDLHAAGCELLTVTQYLRPTPRHHPVERWVRPEEFLDWERVGAELGFSGVMSGPLVRSSYRAGRLYQQAITARGEGHTAASDLPKS... | Cofactor: Binds 2 [4Fe-4S] clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes,... |
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.