ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q9NV66 | MDPSADTWDLFSPLISLWINRFYIYLGFAVSISLWICVQIVIKTQGKNLQEKSVPKAAQDLMTNGYVSLQEKDIFVSGVKIFYGSQTGTAKGFATVLAEAVTSLDLPVAIINLKEYDPDDHLIEEVTSKNVCVFLVATYTDGLPTESAEWFCKWLEEASIDFRFGKTYLKGMRYAVFGLGNSAYASHFNKVGKNVDKWLWMLGAHRVMSRGEGDCDVVKSKHGSIEADFRAWKTKFISQLQALQKGERKKSCGGHCKKGKCESHQHGSEEREEGSHEQDELHHRDTEEEEPFESSSEEEFGGEDHQSLNSIVDVEDLGKIMDHVKKEKREKEQQEEKSGLFRNMGRNEDGERRAMITPALREALTKQGYQLIGSHSGVKLCRWTKSMLRGRGGCYKHTFYGIESHRCMETTPSLACANKCVFCWRHHTNPVGTEWRWKMDQPEMILKEAIENHQNMIKQFKGVPGVKAERFEEGMTVKHCALSLVGEPIMYPEINRFLKLLHQCKISSFLVTNAQFPAEIRNLEPVTQLYVSVDASTKDSLKKIDRPLFKDFWQRFLDSLKALAVKQQRTVYRLTLVKAWNVDELQAYAQLVSLGNPDFIEVKGVTYCGESSASSLTMAHVPWHEEVVQFVHELVDLIPEYEIACEHEHSNCLLIAHRKFKIGGEWWTWIDYNRFQELIQEYEDSGGSKTFSAKDYMARTPHWALFGASERGFDPKDTRHQRKNKSKAISGC | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Probable component of the wybutosine biosynthesis pathway. Wybutosine is a hyper modified guanosine with a tricyclic base found at the 3'-position adjacent to the anticodon of eukaryotic phenylalanine tRNA. Catalyzes the condensation of N-methylguanine with 2 carbon atoms from pyruvate to form the tricyclic 4-demethylwyosine, an intermediate in wybutosine biosynthesis (By similarity).
Catalytic Activity: N(1)-methylguanosine(37) in tRNA(Phe) + pyruvate + S-adenosyl-L-methionine = 4-demethylwyosine(37) in tRNA(Phe) + 5'-deoxyadenosine + CO2 + H2O + L-methionine
Sequence Mass (Da): 83702
Sequence Length: 732
Pathway: tRNA modification; wybutosine-tRNA(Phe) biosynthesis.
EC: 4.1.3.44
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Q57705 | MIPEEIYKILRKQRYQIDGHTAVKLCGWVRKKMLEDKNCYKSKFYGIETHRCIQCTPSVIWCQQNCIFCWRVLPRDIGIDISQIKEPKWEEPEVVYEKILAMHKRIIMGYAGVLDRVGEKKFKEALEPKHVAISLSGEPTLYPYLDELIKIFHKNGFTTFVVSNGILTDVIEKIEPTQLYISLDAYDLDSYRRICGGKKEYWESILNTLDILKEKKRTCIRTTLIRGYNDDILKFVELYERADVHFIELKSYMHVGYSQKRLKKEDMLQHDEILKLAKMLDENSSYKLIDDSEDSRVALLQNENRKINPKL | Cofactor: Binds 2 [4Fe-4S] clusters. Binds 1 [4Fe-4S] cluster coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Component of the wyosine derivatives biosynthesis pathway that catalyzes the condensation of N-methylguanine with 2 carbon atoms from pyruvate to form the tricyclic 4-demethylwyosine (imG-14) on guanosine-37 of tRNA(Phe).
Catalytic Activity: N(1)-methylguanosine(37) in tRNA(Phe) + pyruvate + S-adenosyl-L-methionine = 4-demethylwyosine(37) in tRNA(Phe) + 5'-deoxyadenosine + CO2 + H2O + L-methionine
Sequence Mass (Da): 36712
Sequence Length: 311
Subcellular Location: Cytoplasm
EC: 4.1.3.44
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Q8BJM7 | MGPLDVWDLSPLLSLWMNRFYIYMGCALGLTLCICVQIIKKQVTRSQEKRVPGAPDSSLSPQKKQTHVSGVKIFYGSQTGTAKGFAVVLAKAVTSLDLPVAIINLKEYDPDDSLIGEITSKTVCAFLVATYTDGCPTESAEWFCKWLEESANDFRFGKTYLKGLRYAVFGLGDSAYRSHFNKVSTNVDKWLWMLGAQRVLTRGEGDCNAVQSKHGSIEADFTAWKTKFISRLQALQRGEKKACGGNCKRGKCESAQHGPGEARPHPQGELHPGDAEEEEPCESSSEDELGTQDYQSLTSVVDVEDLGNIMNPVKREKREKSHQDGKAAMQRNPEKTEDGEGRAMITPALREALTKQGYQLIGSHSGVKLCRWTKSMLRGRGGCYKHTFYGIESHRCMEATPSLACANKCVFCWRHHTNPVGTEWRWKMDQPELILKEAIENHQNMIKQFKGVPGLKAERFEEGMEVKHCALSLVGEPIMYPEINRLLKLLHQHGISSFLVTNAQFPEEIRKLTPVTQLYVSVDASTRDGLKKIDRPLFKDFWQRFLDSLKALSAKQQRTVYRLTLVKCWNVDELQAYAELVSLGNPDFIEVKGVTYCGESAASSLTMANVPWHEEVVRFVRELVDLLPDYEVACEHEHSNCLLIGHKKFKIDGEWWTWINYSRFQELVLQYEESGGSKTFSSRDYMARTPQWALFGARERGFDPKDTRYQRKNKTKDISGC | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Probable component of the wybutosine biosynthesis pathway. Wybutosine is a hyper modified guanosine with a tricyclic base found at the 3'-position adjacent to the anticodon of eukaryotic phenylalanine tRNA. Catalyzes the condensation of N-methylguanine with 2 carbon atoms from pyruvate to form the tricyclic 4-demethylwyosine, an intermediate in wybutosine biosynthesis (By similarity).
Catalytic Activity: N(1)-methylguanosine(37) in tRNA(Phe) + pyruvate + S-adenosyl-L-methionine = 4-demethylwyosine(37) in tRNA(Phe) + 5'-deoxyadenosine + CO2 + H2O + L-methionine
Sequence Mass (Da): 81599
Sequence Length: 721
Pathway: tRNA modification; wybutosine-tRNA(Phe) biosynthesis.
EC: 4.1.3.44
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Q8H8N3 | MPPPFPTATAAASTTSHLALLLLLSSSSVFFLYKSLRLRRNNPPSPPPGQGPAPTPTLLYASATGTSKALAAGLSRRLAEAGVTAHPADAAAFDPDDLPSLPLLLLVLPTHDGGAPPPAAAFLARWLEESAADFRAGAALLSGLRFAVFGVGSRAYGETFNAAARSFSRWLRALGAAEVVAVGEGDVDGGDLEVVFEEWCGRVVRVVKGEEIGEGHNGESDGFDELEEEESDDDDDEEEVDGGEVDMEDIAGKAPAARRRNGKVEGALSNGGENGVRDMVTPIIRTSLEKQGYKIIGSHSGVKICRWTKSQLRGRGGCYKHSFYGIESHRCMEATPSLACANKCVFCWRHHTNPVGKSWKWKMDDPLDIVNAAIDQHTKMVKQMKGVPGVKPERLAEGLSPRHCALSLVGEPIMYPEINVLIDELHRRHISTFLVTNAQFPDKIKTLKPITQLYVSVDAATKESLKAVDRPLFSDFWERFLDSLKSLHDKDQRTVYRLTLVKGWNAEEIDGYAKLLSLGQPDFIEIKGVTYCGSSATSKLTMENVPWHSDVKDFSEALALKSGGVYEVACEHAHSCCVLLAKVDKFKINGKWHTWIDYDRFHELVTSGKPFRSQDYMALTPSWAVYGAEEGGFDPDQSRYKKERRHGAAALKD | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Probable component of the wybutosine biosynthesis pathway. Wybutosine is a hyper modified guanosine with a tricyclic base found at the 3'-position adjacent to the anticodon of eukaryotic phenylalanine tRNA. Catalyzes the condensation of N-methylguanine with 2 carbon atoms from pyruvate to form the tricyclic 4-demethylwyosine, an intermediate in wybutosine biosynthesis (By similarity).
Catalytic Activity: N(1)-methylguanosine(37) in tRNA(Phe) + pyruvate + S-adenosyl-L-methionine = 4-demethylwyosine(37) in tRNA(Phe) + 5'-deoxyadenosine + CO2 + H2O + L-methionine
Sequence Mass (Da): 71423
Sequence Length: 653
Pathway: tRNA modification; wybutosine-tRNA(Phe) biosynthesis.
EC: 4.1.3.44
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O59412 | MMEMITIKPGKITVQANPNMPKEVAELFRKQHYEIVGRHSGVKLCHWLKKSLTEGRFCYKQKFYGIHSHRCLQMTPVLAWCTHNCIFCWRPMENFLGTELPQPWDDPAFIVEESIKAQRKLLIGYKGNPKVDKKKFEEAWNPTHAAISLSGEPMLYPYMGDLVEEFHKRGFTTFIVTNGTIPERLEEMIKEDKLPTQLYVSITAPDIETYNSVNIPMIPDGWERILRFLELMRDLPTRTVVRLTLVKGENMHSPEKYAKLILKARPMFVEAKAYMFVGYSRNRLTINNMPSHQDIREFAEALVKHLPGYHIEDEYEPSRVVLIMRDDVDPQGTGVEGRFIKH | Cofactor: Binds 1 [2Fe-2S] cluster.
Function: Component of the wyosine derivatives biosynthesis pathway that catalyzes the condensation of N-methylguanine with 2 carbon atoms from pyruvate to form the tricyclic 4-demethylwyosine (imG-14) on guanosine-37 of tRNA(Phe).
Catalytic Activity: N(1)-methylguanosine(37) in tRNA(Phe) + pyruvate + S-adenosyl-L-methionine = 4-demethylwyosine(37) in tRNA(Phe) + 5'-deoxyadenosine + CO2 + H2O + L-methionine
Sequence Mass (Da): 39840
Sequence Length: 342
Subcellular Location: Cytoplasm
EC: 4.1.3.44
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O59761 | MGYSLGYIGEHWEEYRAVLYIVLLLPVLIHFLIRRKTQLSNSDKSSEKKDEVKKQREVKRFKRVGKRGKIGSPSSSIRKQNDTIDWKNSPLCVFYSTLGGTAERYAKQVHEELSSLLQRDDIQLLNLDYVDLSEYFVSCPENAIYLVVLPSYEIESSIDYYLSSLQESFSDFRVPKDPLHGLSGYAVFGLGDMENYPGDKFCYQAIQADKWIKKLGARRLAPLGVVNTQLAPTAQIDALLQWTRSVAECLKNGTLLKIGNTDSLSSDVMDVEDMGSMMAKAKAEAALPVGTKEMVSTESPTYKALTKQGYSVVGSHSGVKICRWTKSAMRGRGFCYKYSFYGIRSHLCMEATPSLACANKCTFCWRHGTNPVGTSWRWKVDPPEMILQGILKAHYAKLKLMKGVPGVLPDRYEEASRVRHCALSLVGEPIFYPYINEFVSMLHEREISSFLVTNAQHPEALRNMGMVTQLYVSVDASTKQSLKSVDRPLFKDFWERMLTCLEILREKRQRTVYRMTLVKGFNMEQIKEYTELIRLGVPCFIEVKGVTYSGNSDQSPLTMKNVPYYEEVIDFVKKLIEYIDIHLQDLGVRYEIAAEHAHSCSILVAQTAFKKDGHWHTHIDYPKFFELIRTKKDFGPFDYMASTPDFAMFGNGGFSPEDTRFHRKKKTQTSKPISATISETATISEAAA | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Probable component of the wybutosine biosynthesis pathway. Wybutosine is a hyper modified guanosine with a tricyclic base found at the 3'-position adjacent to the anticodon of eukaryotic phenylalanine tRNA. Catalyzes the condensation of N-methylguanine with 2 carbon atoms from pyruvate to form the tricyclic 4-demethylwyosine, an intermediate in wybutosine biosynthesis (By similarity).
Catalytic Activity: N(1)-methylguanosine(37) in tRNA(Phe) + pyruvate + S-adenosyl-L-methionine = 4-demethylwyosine(37) in tRNA(Phe) + 5'-deoxyadenosine + CO2 + H2O + L-methionine
Sequence Mass (Da): 78188
Sequence Length: 688
Pathway: tRNA modification; wybutosine-tRNA(Phe) biosynthesis.
EC: 4.1.3.44
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O43818 | MSATAAARKRGKPASGAGAGAGAGKRRRKADSAGDRGKSKGGGKMNEEISSDSESESLAPRKPEEEEEEELEETAQEKKLRLAKLYLEQLRQQEEEKAEARAFEEDQVAGRLKEDVLEQRGRLQKLVAKEIQAPASADIRVLRGHQLSITCLVVTPDDSAIFSAAKDCSIIKWSVESGRKLHVIPRAKKGAEGKPPGHSSHVLCMAISSDGKYLASGDRSKLILIWEAQSCQHLYTFTGHRDAVSGLAFRRGTHQLYSTSHDRSVKVWNVAENSYVETLFGHQDAVAALDALSRECCVTAGGRDGTVRVWKIPEESQLVFYGHQGSIDCIHLINEEHMVSGADDGSVALWGLSKKRPLALQREAHGLRGEPGLEQPFWISSVAALLNTDLVATGSHSSCVRLWQCGEGFRQLDLLCDIPLVGFINSLKFSSSGDFLVAGVGQEHRLGRWWRIKEARNSVCIIPLRRVPVPPAAGS | Function: Component of a nucleolar small nuclear ribonucleoprotein particle (snoRNP) thought to participate in the processing and modification of pre-ribosomal RNA (pre-rRNA) . Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome .
PTM: Acetylation at Lys-12 and Lys-25 by KAT2B/PCAF under stress impairs pre-rRNA processing . Deacetylation by SIRT7 enhances RRP9-binding to U3 snoRNA, which is a prerequisite for pre-rRNA processing .
Sequence Mass (Da): 51841
Sequence Length: 475
Domain: The WD domains are required for nucleolar localization and U3 small nucleolar RNAs binding.
Subcellular Location: Nucleus
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O82383 | MRNVELIFIPTPTVGHLVPFLEFARRLIEQDDRIRITILLMKLQGQSHLDTYVKSIASSQPFVRFIDVPELEEKPTLGSTQSVEAYVYDVIERNIPLVRNIVMDILTSLALDGVKVKGLVVDFFCLPMIDVAKDISLPFYVFLTTNSGFLAMMQYLADRHSRDTSVFVRNSEEMLSIPGFVNPVPANVLPSALFVEDGYDAYVKLAILFTKANGILVNSSFDIEPYSVNHFLQEQNYPSVYAVGPIFDLKAQPHPEQDLTRRDELMKWLDDQPEASVVFLCFGSMARLRGSLVKEIAHGLELCQYRFLWSLRKEEVTKDDLPEGFLDRVDGRGMICGWSPQVEILAHKAVGGFVSHCGWNSIVESLWFGVPIVTWPMYAEQQLNAFLMVKELKLAVELKLDYRVHSDEIVNANEIETAIRYVMDTDNNVVRKRVMDISQMIQRATKNGGSSFAAIEKFIYDVIGIKP | Function: Possesses quercetin 3-O-glucosyltransferase activity in vitro.
Catalytic Activity: a flavonol + UDP-alpha-D-glucose = a flavonol 3-O-beta-D-glucoside + H(+) + UDP
Sequence Mass (Da): 53000
Sequence Length: 467
EC: 2.4.1.-
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P0DO49 | MKKAELVFIPAPGAGHLVSALQFGKRLLQRDDRISITVLAIKSAAPSSLGSYTEALVASESRLQLIDVPQAELPPLEFAKSPAKFFILNIENHVPNVREALTNYVSSKQDSVSIVGVVLDFFCVSMIHVVNEFNLPSYLFMTSNAGYLSFEFHFPAQDSRTGRPPKDSDPDWLVPGIVPPVPTKVLPVSLTDGSYYNYLGVASRFREAKGIIANTCVELETHAFNSFAEDQTTPPVYPVGPVLDLNDGQARSNLNQAQRDKIISWLDDQPEESVVFLCFGSMGSFTEAQVKEIALGLEQSGQRFLWSLRLTPPKGSKSLTPVDCSNLEEVLPDGFLERTREKGLICGWAPQVDVLSHKATGGFVSHCGWNSILESLWHGVPIVTWPMYAEQQLNAFRLVKEMGLGLEMRLDYKRGGDEVVKADEIGKAVASVMENSEVRKKVKEIGVVCRKAVEDGGSSSVSLGRFIEDVLRNHFGSE | Function: Glycosyltransferase that catalyzes the glucosylation of diverse hydroxycoumarins, naphthols, flavonoids, acylphloroglucinols, and pelargonidin . Involved in fruit ripening by synthesizing acylphloroglucinol glucosides and anthocyanin .
Catalytic Activity: a 2-acylphloroglucinol + UDP-alpha-D-glucose = a 2-acylphloroglucinol 1-O-beta-D-glucoside + UDP
Sequence Mass (Da): 52590
Sequence Length: 478
EC: 2.4.1.-
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Q9M156 | MEESKTPHVAIIPSPGMGHLIPLVEFAKRLVHLHGLTVTFVIAGEGPPSKAQRTVLDSLPSSISSVFLPPVDLTDLSSSTRIESRISLTVTRSNPELRKVFDSFVEGGRLPTALVVDLFGTDAFDVAVEFHVPPYIFYPTTANVLSFFLHLPKLDETVSCEFRELTEPLMLPGCVPVAGKDFLDPAQDRKDDAYKWLLHNTKRYKEAEGILVNTFFELEPNAIKALQEPGLDKPPVYPVGPLVNIGKQEAKQTEESECLKWLDNQPLGSVLYVSFGSGGTLTCEQLNELALGLADSEQRFLWVIRSPSGIANSSYFDSHSQTDPLTFLPPGFLERTKKRGFVIPFWAPQAQVLAHPSTGGFLTHCGWNSTLESVVSGIPLIAWPLYAEQKMNAVLLSEDIRAALRPRAGDDGLVRREEVARVVKGLMEGEEGKGVRNKMKELKEAACRVLKDDGTSTKALSLVALKWKAHKKELEQNGNH | Function: Bifunctional O-glycosyltransferase and N-glycosyltransferase that can detoxify xenobiotics. Possesses high activity to metabolize the persistent pollutants 2,4,5-trichlorophenol (TCP) and 3,4-dichloroaniline (DCA). Also active on benzoates and benzoate derivatives in vitro.
Catalytic Activity: hydroquinone + UDP-alpha-D-glucose = H(+) + hydroquinone O-beta-D-glucopyranoside + UDP
Sequence Mass (Da): 52930
Sequence Length: 480
EC: 2.4.1.-
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A0A0D1CFE5 | MVVKRILPLPRPAGLAPPTEVPLDGQDLAMPKMVMHCIWFFLASSQPSLESTSLQELEQAFTLGMQLFLARFPAAGARTRHDKDTARWYLEYNDQGADLEVIQLDRPLQDDWKALDGKCDSVFAPRPVMIFDDDASIFSIKVTRLSCGSVAISTSTHHWLVDFVGYIDLMEELSHCVSIFLNDPNAQINIDEGATKFDWSRDLLAYSKQLEPESIPSATWFTERGSPPQMTRAPSSCHYASLLFTQESLEKLKRSLAEWALETAPTTATDRIVPSKDNWIATNDALHALLWAAITDARGLDLNATTQLHTPLDGRRLLSSLSSADSQSRGKYIGNVHPGHVFPLPSSVVSAKDRSGLFNLAWLIRTQYLNVTPGQMSAIIRHHNYTDAETFGPGRLPKCTSMFGNDVTISNVARIPVRQRLDFGEKLGKPYTLTVVGMVPVTLNGLTLDSADGTCFIIQAPAEWTSKEAVLQHQPRSGDNQAPGGMLVYVGMRSEEMDKLLQNSLLQEFALVL | Function: Acyltransferase; part of the gene cluster that mediates the biosynthesis of the glycolipid biosurfactant ustilagic acid (UA) . UA is a secreted cellobiose glycolipid that is toxic for many microorganisms and confers biocontrol activity to U.maydis . UA consists of 15,16-dihydroxypalmitic or 2,15,16-trihydroxypalmitic acid, which is O-glycosidically linked to cellobiose at its terminal hydroxyl group . In addition, the cellobiose moiety is acetylated and acylated with a short-chain hydroxy fatty acid . UA biosynthesis starts with omega-hydroxylation of palmitic acid catalyzed by the cytochrome P450 monooxygenase cyp1 . Terminal hydroxylation of palmitic acid precedes subterminal hydroxylation catalyzed by the cytochrome P450 monooxygenase cyp2 . Sequential glucosylation of the hydroxy fatty acid is probably catalyzed by the glycosyltransferase ugt1 (Probable). The cellobiose lipid is further decorated by acetylation of the proximal glucose residue and by acylation with a short-chain beta-hydroxy fatty acid at the distal glucose residue (Probable). The acyltransferase uat1 may be a good candidate for catalyzing either acetylation or acylation of the cellobiose lipid (Probable). The fatty acid synthase fas2 may be involved in synthesis of the carbon backbone of the short-chain beta-hydroxy fatty acid esterified to the cellobiose disaccharide (Probable). The secreted UA consists of a mixture of both alpha-hydroxylated and non-hydroxylated glycolipids; therefore, alpha-hydroxylation of the long-chain fatty, catalyzed by the fatty acid hydroxylase ahd1, occurs late in UA biosynthesis and may be the last step before secretion .
Sequence Mass (Da): 56827
Sequence Length: 513
Pathway: Secondary metabolite biosynthesis.
EC: 2.3.1.-
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Q9ZU75 | MIGLFKVKEKQREESQSNNGRGASTVKKQSAGELRLHKDISELNLPKSCKISFPNGKNDLMNFEVTIKPDEGYYLSGNFVFSFQVSNMYPHEAPKVKCKTKVYHPNIDLEGNVCLNILREDWKPVLNINTVIYGLFHLFTEPNYEDPLNHEAAAVLRDNPKTFEYNVRRAMMGGQVGQTSFPRCM | Function: Accepts the ubiquitin-like protein NEDD8/RUB1 from the ECR1-AXR1 E1 complex and catalyzes its covalent attachment to other proteins.
Sequence Mass (Da): 21133
Sequence Length: 185
Pathway: Protein modification; protein neddylation.
EC: 2.3.2.-
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Q77J49 | MFTHLTRAFRKMNNLVNRSFIDVHRVVAELSYPEFEEDVKNPESSIYRTPISLFQNKDIVTIVGDYILSPKTDSFQVLYPIKKVIEHFPVIFHCTHNNAPLWVHLLDERHHRLLQSLLTYEIVNAKYRGIVVIPYYRRPINYQTGKSLLMSKLASVKVLDILMRCGSYKFISLMCMINKKNNTNFLHCCASKWGEVGSKMMLHIAEMFFANPTTSQHLSDASSFPDAAAEDDKGKTPAHLAIQEDNADALLFLISLYGAPWFQDNNSYMKSALELKSNKCVKVLSFAADKYEILPNINNNQLEPDTMCGVCATSVEEDENEGKTTSLSWYQMNCKHYIHCECLMGMCAAAGNVQCPMCREDVGDEVLERCPPTIFRWLKLAERSEHNRVLFEAKKQEFYKQMEAMKPPRVVVPPRRTFLTPARRGERAIRIAREIATNAIAEATAQGDVNSYFPVLIDGSGEEYEEEGEEFFNSEEEALAFGRPFLEDEEEARQIQMRQFAELSRRGVSVNIINNDNPHRHISTVNIVQPVYGVEKSPAASFIYNMLKNDVFESIRSRDTRVGGERVPVMNLSNDKRALFHAASSMLCDFATETNSQIVGLDFQAVYDPHHISNYIETFGSPLHAYPGAVTFLDGAQDYYAESIRYDNDIVSFSEMASELHITEALDVFEGSLLSPLFKKIRTGKSYSNWNDHLRRRNYARDIAEEFVRVCENSLASREHPPVHVHPFRDGAIPILIEYIVDFIHHCITWSMQVNALHCMRKYIEHENTNVHLLNLRPTDERVEVLRVSQLRWSRLFNEQYNTRMSLSTKRLSLMKIFNHDLGVSKFGVYKLLDIIEMYCFTLI | Function: Probable E3 ubiquitin-protein ligase which accepts ubiquitin from the E2 ubiquitin-conjugating enzyme UBE2E1/UBCH6 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Mediates ubiquitination of host tumor-suppressor-like protein (TSL) targeting it for degradation. Might function as an anti-apoptosis protein by counteracting TSL-induced apoptosis.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 97040
Sequence Length: 844
Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.27
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Q6DCJ1 | MSPAGCSHVNSFKVENWRQNLRVIYQCFVWSGTPETRKRKAKSCVCHMCGAHLNRLHSCLYCVYFGCFTKKHIHEHAKNKRHNLAIDLLYGGIYCFMCQDYIYDKDMEQVAKEEQRKAWKLQVFSPALVSPYQYTMTGVGEKYSTWEPTKRELELLQHNPKRRKITTNCTIGLRGLINLGNTCFMNCIVQALTHTPLLRDFFLSDRHKCEMQSPNSCLVCEMSTLFQEFYSGHRSPHIPYRLLHLVWTHARHLAGYEQQDAHEFLIAALDVLHRHCKGDDNGKKANNPNHCNCIIDQIFTGGLQSDVTCQVCHGVSTTIDPFWDISLDLPGSSTPFWPLSPGSDAGVVNGESHVSGTTTLTDCLRRFTRPEHLGSSAKIKCSGCHSYQESTKQLTMKKLPIVACFHLKRFEHSAKLRRKITTYVSFPLELDMMPFMASSKESRMNGQYQQPSDSLHNDNKYSLFAVVNHQGTLESGHYTSFIRQHKDQWFKCDDAIITKASIKDVIDSEGYLLFYHKQFLEYE | Function: Histone deubiquitinating component of the transcription regulatory histone acetylation (HAT) complex SAGA. Catalyzes the deubiquitination of both histones H2A and H2B, thereby acting as a coactivator. Recruited to specific gene promoters by activators, where it is required for transcription (By similarity).
Catalytic Activity: Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
Sequence Mass (Da): 60109
Sequence Length: 523
Subcellular Location: Nucleus
EC: 3.4.19.12
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P51668 | MALKRIQKELSDLQRDPPAHCSAGPVGDDLFHWQATIMGPPDSAYQGGVFFLTVHFPTDYPFKPPKIAFTTKIYHPNINSNGSICLDILRSQWSPALTVSKVLLSICSLLCDPNPDDPLVPDIAQIYKSDKEKYNRHAREWTQKYAM | Function: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins . In vitro catalyzes 'Lys-48'-linked polyubiquitination . Mediates the selective degradation of short-lived and abnormal proteins. Functions in the E6/E6-AP-induced ubiquitination of p53/TP53. Mediates ubiquitination of PEX5 and auto-ubiquitination of STUB1, TRAF6 and TRIM63/MURF1 . Ubiquitinates STUB1-associated HSP90AB1 in vitro . Lacks inherent specificity for any particular lysine residue of ubiquitin . Essential for viral activation of IRF3 . Mediates polyubiquitination of CYP3A4 .
PTM: Autoubiquitinated in vitro.
Catalytic Activity: S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine.
Sequence Mass (Da): 16602
Sequence Length: 147
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cytoplasm
EC: 2.3.2.23
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P62837 | MALKRIHKELNDLARDPPAQCSAGPVGDDMFHWQATIMGPNDSPYQGGVFFLTIHFPTDYPFKPPKVAFTTRIYHPNINSNGSICLDILRSQWSPALTISKVLLSICSLLCDPNPDDPLVPEIARIYKTDREKYNRIAREWTQKYAM | Function: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins . Catalyzes 'Lys-48'-linked polyubiquitination . Mediates the selective degradation of short-lived and abnormal proteins . Functions in the E6/E6-AP-induced ubiquitination of p53/TP53 . Mediates ubiquitination of PEX5 and autoubiquitination of STUB1 and TRAF6 . Involved in the signal-induced conjugation and subsequent degradation of NFKBIA, FBXW2-mediated GCM1 ubiquitination and degradation, MDM2-dependent degradation of p53/TP53 and the activation of MAVS in the mitochondria by RIGI in response to viral infection . Essential for viral activation of IRF3 .
Catalytic Activity: S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine.
Sequence Mass (Da): 16735
Sequence Length: 147
Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.23
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Q06AA9 | MALKRIHKELNDLARDPPAQCSAGPVGDDMFHWQATIMGPNDSPYQGGVFFLTIHFPTDYPFKPPKVAFTTRIYHPNINSNGSICLDILRSQWSPALTISKVLLSICSLLCDPNPDDPLVPEIARIYKTDRDKYNRISREWTQKYAM | Function: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-48'-linked polyubiquitination. Mediates the selective degradation of short-lived and abnormal proteins. Functions in the E6/E6-AP-induced ubiquitination of p53/TP53. Mediates ubiquitination of PEX5 and autoubiquitination of STUB1 and TRAF6. Involved in the signal-induced conjugation and subsequent degradation of NFKBIA, FBXW2-mediated GCM1 ubiquitination and degradation, MDM2-dependent degradation of p53/TP53 and the activation of MAVS in the mitochondria by RIGI in response to viral infection. Essential for viral activation of IRF3.
Catalytic Activity: S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine.
Sequence Mass (Da): 16737
Sequence Length: 147
Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.23
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P0CG53 | MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGC | Function: Exists either covalently attached to another protein, or free (unanchored) (By similarity). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains) . Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in proteotoxic stress response and cell cycle; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B (By similarity). Linear polymer chains formed via attachment by the initiator Met lead to cell signaling (By similarity). Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed (By similarity). When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling (By similarity).
PTM: Phosphorylated at Ser-65 by PINK1 during mitophagy . Phosphorylated ubiquitin specifically binds and activates parkin (PRKN), triggering mitophagy . Phosphorylation does not affect E1-mediated E2 charging of ubiquitin but affects discharging of E2 enzymes to form polyubiquitin chains (By similarity). It also affects deubiquitination by deubiquitinase enzymes such as USP30 (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 34308
Sequence Length: 305
Subcellular Location: Cytoplasm
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P0CG54 | MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGVYASPIF | Function: Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in proteotoxic stress response and cell cycle; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling.
PTM: Phosphorylated at Ser-65 by PINK1 during mitophagy. Phosphorylated ubiquitin specifically binds and activates parkin (PRKN), triggering mitophagy. Phosphorylation does not affect E1-mediated E2 charging of ubiquitin but affects discharging of E2 enzymes to form polyubiquitin chains. It also affects deubiquitination by deubiquitinase enzymes such as USP30.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 34983
Sequence Length: 311
Subcellular Location: Cytoplasm
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Q8MKD1 | MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRFIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGC | Function: Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in proteotoxic stress response and cell cycle; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling.
PTM: Phosphorylated at Ser-65 by PINK1 during mitophagy. Phosphorylated ubiquitin specifically binds and activates parkin (PRKN), triggering mitophagy. Phosphorylation does not affect E1-mediated E2 charging of ubiquitin but affects discharging of E2 enzymes to form polyubiquitin chains. It also affects deubiquitination by deubiquitinase enzymes such as USP30.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 34342
Sequence Length: 305
Subcellular Location: Cytoplasm
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P0CG47 | MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGC | Function: Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in proteotoxic stress response and cell cycle; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling.
PTM: Phosphorylated at Ser-65 by PINK1 during mitophagy . Phosphorylated ubiquitin specifically binds and activates parkin (PRKN), triggering mitophagy . Phosphorylation does not affect E1-mediated E2 charging of ubiquitin but affects discharging of E2 enzymes to form polyubiquitin chains. It also affects deubiquitination by deubiquitinase enzymes such as USP30 .
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 25762
Sequence Length: 229
Subcellular Location: Cytoplasm
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P0CG49 | MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGY | Function: Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in proteotoxic stress response and cell cycle; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling.
PTM: Phosphorylated at Ser-65 by PINK1 during mitophagy. Phosphorylated ubiquitin specifically binds and activates parkin (PRKN), triggering mitophagy. Phosphorylation does not affect E1-mediated E2 charging of ubiquitin but affects discharging of E2 enzymes to form polyubiquitin chains. It also affects deubiquitination by deubiquitinase enzymes such as USP30.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 34369
Sequence Length: 305
Subcellular Location: Cytoplasm
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P35133 | MASKRILKELKDLQKDPPTSCSAGPVAEDMFHWQATIMGPSESPYAGGVFLVTIHFPPDYPFKPPKVAFRTKVFHPNINSNGSICLDILKEQWSPALTISKVLLSICSLLTDPNPDDPLVPEIAHMYKTDKNKYESTARSWTQKYAMG | Function: Accepts the ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. Mediates the selective degradation of short-lived and abnormal proteins.
Catalytic Activity: S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine.
Sequence Mass (Da): 16537
Sequence Length: 148
Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.23
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P35134 | MASKRILKELKDLQKDPPSNCSAGPVAEDMFHWQATIMGPPESPYAGGVFLVSIHFPPDYPFKPPKVSFKTKVYHPNINSNGSICLDILKEQWSPALTISKVLLSICSLLTDPNPDDPLVPEIAHMYKTDRSKYESTARSWTQKYAMG | Function: Accepts the ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. Mediates the selective degradation of short-lived and abnormal proteins.
Catalytic Activity: S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine.
Sequence Mass (Da): 16551
Sequence Length: 148
Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.23
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O00103 | MDSDMQNQNPHTNSKNSSSAGMAVDGHSVTKRLRSELMSLMMSNTPGISAFPDSDSNLLHWAGTITGPSDTYYEGLKFKISMSFPANYPYSPPTIIFTSPMWHPNVDMSGNICLDILKDKWSAVYNVQTILLSLQSLLGEPNNASPLNAQAAELWSKDPIEYKRLLMQRYKEIDEI | Function: Catalyzes the covalent attachment of ubiquitin to other proteins.
Catalytic Activity: S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine.
Sequence Mass (Da): 19664
Sequence Length: 176
Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.23
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P52492 | MAVEEGGCVTKRLQNELLQLLSSTTESISAFPVDDNDLTYWVGYITGPKDTPYSGLKFKVSLKFPQNYPFHPPMIKFLSPMWHPNVDKSGNICLDILKEKWSAVYNVETILLSLQSLLGEPNNRSPLNAVAAELWDADMEEYRKKVLACYEEIDDY | Function: Catalyzes the covalent attachment of ubiquitin to other proteins.
Catalytic Activity: S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine.
Sequence Mass (Da): 17753
Sequence Length: 156
Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.23
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Q76MR7 | MAVLAKFISKNHPSVPIIIISNAPESAAASVAAIPSISYHRLPLPEIPPDMTTDRVELFFELPRLSNPNLLTALQQISQKTRIRAVILDFFCNAAFEVPTSLNIPTYYYFSAGTPTAILTLYFETIDETIPVDLQDLNDYVDIPGLPPIHCLDIPVALSPRKSLVYKSSVDISKNLRRSAGILVNGFDALEFRAIGSHSQRPMHFKGPTPPVYFIGPLVGDVDTKAGSEEHECLRWLDTQPSKSVVFLCFGRRGVFSAKQLKETAAALENSGHRFLWSVRNPPELKKATGSDEPDLDELLPEGFLERTKDRGFVIKSWAPQKEVLAHDSVGGFVTHCGRSSVSEGVWFGVPMIGWPVDAELRLNRAVMVDDLQVALPLEEEAGGFVTAAELEKRVRELMETKAGKAVRQRVTELKLSARAAVAENGSSLNDLKKFLHATRD | Function: Involved in the production of glucuronosylated baicalein, a flavonoid that shows antiallergic, anti-HIV and antitumor activities. Can use baicalein, scutellarein and wogonin as substrates, but not chrysin, apigenin, luteolin, quercetin, formononetin and daidzein. Highly specific for UDP-glucuronate (UDP-GlcUA) and no activity with UDP-glucose or UDP-galacturonic acid.
Catalytic Activity: baicalein + UDP-alpha-D-glucuronate = baicalin + UDP
Sequence Mass (Da): 48654
Sequence Length: 441
EC: 2.4.1.253
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Q09444 | MTDAGSWCLIESDPGVFTEMLRGFGVDGLQVEELYSLDDDKAMTRPTYGLIFLFKWRQGDETTGIPSDKQNIFFAHQTIQNACATQALINLLMNVEDTDVKLGNILNQYKEFAIDLDPNTRGHCLSNSEEIRTVHNSFSRQTLFELDIKGGESEDNYHFVTYVPIGNKVYELDGLRELPLEVAEFQKEQDWIEAIKPVIQQRMQKYSEGEITFNLMALVPNRKQKLQEMMENLIQANENNELEEQIADLNKAIADEDYKMEMYRKENNRRRHNYTPFVIELMKILAKEGKLVGLVDNAYQAAKEKSKLNTDITKLELKRKQ | Function: Ubiquitin-protein hydrolase involved both in the processing of ubiquitin precursors and of ubiquitinated proteins. This enzyme is a thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of ubiquitin.
Catalytic Activity: Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
Sequence Mass (Da): 37120
Sequence Length: 321
EC: 3.4.19.12
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Q5ZKS8 | MGPAELVQKISINAESPRGGERNDCGAGAERGPAGGWRQKCAAYVLALRPWSFSASLTPVALGSALAYRAEGALDPRLLVGSAVAVLAVHGAGNLVNTYYDFSKGIDHKKSDDRTLVDQILEPQDVVRFGVFLYTVGCICAAGLYAVSTLKLEHLALVYFGGLSSSFLYTGGIGFKYVALGDVVILITFGPLAVMFAHAVQVGYLSVSPLLYAVPLALSTEAILHSNNTRDMESDQQAGIVTLAIIIGPAFSYVLYTVLLFLPYLIFCVLATRYTISMALPLLTIPMAFSLERQFRSQNFNKIPQRTAKLNLLLGLFYVFGIMLAPAGALPKL | Function: Prenyltransferase that mediates the formation of menaquinone-4 (MK-4) and coenzyme Q10. MK-4 is a vitamin K2 isoform required for endothelial cell development. Mediates the conversion of phylloquinone (PK) into MK-4, probably by cleaving the side chain of phylloquinone (PK) to release 2-methyl-1,4-naphthoquinone (menadione; K3) and then prenylating it with geranylgeranyl pyrophosphate (GGPP) to form MK-4. Also plays a role in cardiovascular development independently of MK-4 biosynthesis, by acting as a coenzyme Q10 biosynthetic enzyme: coenzyme Q10, also named ubiquinone, plays an important antioxidant role in the cardiovascular system. Mediates biosynthesis of coenzyme Q10 in the Golgi membrane, leading to protect cardiovascular tissues from NOS3/eNOS-dependent oxidative stress.
Catalytic Activity: (2E,6E,10E)-geranylgeranyl diphosphate + menadiol = diphosphate + menaquinol-4
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35750
Sequence Length: 333
Pathway: Quinol/quinone metabolism; menaquinone biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.5.1.-
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E7FB98 | MQEMKPAALSGSNGLNGASGSSVRVPCSRLSRAGRMALDLQSKCAAYVLALRPWSFSASLTPVALGSALAYKLEGSVDLLLLLVCAVAVLLVHGAGNLVNTYYDFSKGIDHKKSDDRTLVDQILKPQDVVMFGAVLYSAGCLCATLLYFLSSLKLEHLALIYFGGLSSSFLYTGGIGLKYVALGDVVILITFGPLAVMFAHAVQVGYLSVLPLVYAVPLALNTEAILHSNNTRDMDSDKQAGIVTLAILLGPTLSYVIYNLLLFVPYLLFCILATRYTISMALPLLTLPMAFPLERQFRCRCYAKIPQKTAKLNLLMGLFYVFGIILAPQGSLPLL | Function: Prenyltransferase that mediates the formation of menaquinone-4 (MK-4) and coenzyme Q10 . MK-4 is a vitamin K2 isoform required for endothelial cell development (By similarity). Mediates the conversion of phylloquinone (PK) into MK-4, probably by cleaving the side chain of phylloquinone (PK) to release 2-methyl-1,4-naphthoquinone (menadione; K3) and then prenylating it with geranylgeranyl pyrophosphate (GGPP) to form MK-4 (By similarity). Also plays a role in cardiovascular development independently of MK-4 biosynthesis, by acting as a coenzyme Q10 biosynthetic enzyme: coenzyme Q10, also named ubiquinone, plays an important antioxidant role in the cardiovascular system . Mediates biosynthesis of coenzyme Q10 in the Golgi membrane, leading to protect cardiovascular tissues from nos3/eNOS-dependent oxidative stress .
Catalytic Activity: (2E,6E,10E)-geranylgeranyl diphosphate + menadiol = diphosphate + menaquinol-4
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 36214
Sequence Length: 336
Pathway: Quinol/quinone metabolism; menaquinone biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.5.1.-
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Q54K99 | MSTTINRNEKTKQVVNKTKEIKTESSQQQQQKPPISKLMGIILATRPWSLTISVTSVLVGSALAFREIREFDSIMLSIILVGAVSLQALGNVVNSFYDCKNGNDTKEKSADRTMFDFGLTEGNIINLIWYLLIQCAICLGLMIFRMDNIKCIVENILPLGAFGFILNISYTAAPIGLKYIGLGDLTIFLCFGPILVQSAFISQTHYHDSLAYFYSIPLALTIVAVLHVNNTRDIKADTEAGSITLASKLGFKNCYYIYAGLYLFAYIYLFKLSLDIDKYILNLPLILIPKIISLINQFKNKKLEDLTEKTGQLSFFFGGLNAIGVLLSMQ | Function: Prenyltransferase that mediates the formation of menaquinone-4 (MK-4), a vitamin K2 isoform.
Catalytic Activity: (2E,6E,10E)-geranylgeranyl diphosphate + menadiol = diphosphate + menaquinol-4
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 36794
Sequence Length: 330
Pathway: Quinol/quinone metabolism; menaquinone biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.5.1.-
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Q5P5M0 | MIAPATLSSRLPLYLRLMRLDKPIGILLLMWPTLWALWLAADGFPPLHLIVIFALGTVLMRSAGCVINDYADRDFDGHVERTRTRPLTTGAVTVREALLLAAGLSLVSFVLILPLDPLVRWLSLPALFLAASYPYTKRFLAIPQAYLGIAFGFGIPMGFAAVQGEVPAIAWLLLLANIFWAVAYDTEYAMVDRPDDLKIGIKTSAITFGRFDVAAVMLCYAVAFGLIAAVGIATGRGPWFFGGIAIAAAIAIYHYTLIRDRDRARCFRAFLHNNWVGAVLFVALVIDYVAFPAA | Function: Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of ubiquinone-8 (UQ-8) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB, generating the first membrane-bound Q intermediate 3-octaprenyl-4-hydroxybenzoate.
Catalytic Activity: 4-hydroxybenzoate + all-trans-octaprenyl diphosphate = 4-hydroxy-3-all-trans-octaprenylbenzoate + diphosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32191
Sequence Length: 294
Pathway: Cofactor biosynthesis; ubiquinone biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.5.1.39
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Q494A7 | MSNRLFFIKKCYNLAQLMRINQPIGFFLLLWPTLWGLWLSHKGIPDKVVLIVFVAGALCMRSAGCIINDYVDYDIDGHVQRTKTRPLPSGMIRKKEALVALSILLFIAFILVLSLNFITIFLSVVALILSWIYPYLKRYIYFPQVMLGLLFSWPILMAFTAINNPINSTAWLLFLMNTVWTIVYDTQYAMIDREDDIYVGIKSSAVLFGDMDKFLIGILQLCIVFILGIIGWKERFTVVFYFFSLFGVIILFMWQQILINKRKRIRYFQAFLSNNYVGMLVFIGIASSFH | Function: Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of ubiquinone-8 (UQ-8) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB, generating the first membrane-bound Q intermediate 3-octaprenyl-4-hydroxybenzoate.
Catalytic Activity: 4-hydroxybenzoate + all-trans-octaprenyl diphosphate = 4-hydroxy-3-all-trans-octaprenylbenzoate + diphosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 33678
Sequence Length: 290
Pathway: Cofactor biosynthesis; ubiquinone biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.5.1.39
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Q2SZ16 | MLARFPLYLRLIRMDKPIGSLLLLWPTLNALWIASDGHPAPSLVVIFVLGTLLMRSAGCAINDYADRDFDRHVKRTAERPLTSGKIRAWEAVAIAVGLALVSFLLILPLNALTKELSVVAVFVAATYPFMKRFFAIPQAYLGIAFGFGIPMAFAAVQDTVPALAWMLLAANVFWSVAYDTAYAMVDRDDDLKIGMRTSAITFGRYDVLAIMLCYAAMLGIYVWVGVTQHFGWPYWAGWAAAAGCSIYHYTLIKDRERMACFAAFRHNNWLGGALFAGIAAHYALSAL | Function: Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of ubiquinone-8 (UQ-8) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB, generating the first membrane-bound Q intermediate 3-octaprenyl-4-hydroxybenzoate.
Catalytic Activity: 4-hydroxybenzoate + all-trans-octaprenyl diphosphate = 4-hydroxy-3-all-trans-octaprenylbenzoate + diphosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31700
Sequence Length: 287
Pathway: Cofactor biosynthesis; ubiquinone biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.5.1.39
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A1WKC0 | MSGTPRSRLSLYLDLIRWNRPAGWLVCLWPTLSALWVAADGFPGWHLLLVFVLGTCIMRSAGCCVNDVADRDFDRHVKRTAQRPVTTGAVGVKEALAVGAVLALLAFGLVLSTNAATIAWSVPALLVAIAYPYAKRLVSMPQTVLGIAFNFGIVLAFAAVQGRVPAVAWWLWLGTMFWVLAYDTEYAMVDRDDDLKIGIKTSAITLGRLDVAAIMLCYLLFLSLWVWALHSRALGALFYIAIAAALAQALWHWRLIRQRTRAGCFAAFRVNHWLGCTVFAGIAGSYLVRHLQSNG | Function: Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of ubiquinone-8 (UQ-8) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB, generating the first membrane-bound Q intermediate 3-octaprenyl-4-hydroxybenzoate.
Catalytic Activity: 4-hydroxybenzoate + all-trans-octaprenyl diphosphate = 4-hydroxy-3-all-trans-octaprenylbenzoate + diphosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32421
Sequence Length: 295
Pathway: Cofactor biosynthesis; ubiquinone biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.5.1.39
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A5CXV6 | MRLDNPIGIYLLLWPTLWALFLASEGFPDLKLLLIFVLGVVLMRSAGCVINDYADRYIDKLVERTKHRPITSGEIHHRSALKFFVLLIMLAFLLVLLTNWLTIQLAMIAVLLAILYPFTKRWTYFPQFVLGLAFAMSVLMAFSATLNEIPITAWYVFAATVIWTVIYDTMYAMADREEDLKIGIKSSAILFAKFDRLIIGILQIIFLLILIKISNVFNLTISYHITLLLVTLLMIYHQYLIKNNENYSYLHGFLHNNYIGMVIFIGIVLSVGL | Function: Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of ubiquinone-8 (UQ-8) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB, generating the first membrane-bound Q intermediate 3-octaprenyl-4-hydroxybenzoate.
Catalytic Activity: 4-hydroxybenzoate + all-trans-octaprenyl diphosphate = 4-hydroxy-3-all-trans-octaprenylbenzoate + diphosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31363
Sequence Length: 273
Pathway: Cofactor biosynthesis; ubiquinone biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.5.1.39
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Q0A5V8 | MYRNKEASWWPRRHPSRRRVPRGLEAWLDEPGSLTARLRRSVPGGLEVTVLVERWGRPSIDEARAVELSDGRHARIREVLLGSRDQAWIYARTIMPPEALAGDGRRLARLGRTPLGGALFRGRTVARGPLSIARLGPRDPLAARVPGGGAGCWARRSRLWYGNAGLLVTEVFLPPLLQSLED | Function: Removes the pyruvyl group from chorismate, with concomitant aromatization of the ring, to provide 4-hydroxybenzoate (4HB) for the ubiquinone pathway.
Catalytic Activity: chorismate = 4-hydroxybenzoate + pyruvate
Sequence Mass (Da): 20280
Sequence Length: 182
Pathway: Cofactor biosynthesis; ubiquinone biosynthesis.
Subcellular Location: Cytoplasm
EC: 4.1.3.40
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Q5P5L9 | MRIRPHSETWLKRPPRPRVPARLRPWLTDPGSLTARIRSRCSLFSVNVLAQRLAVPHPDEAALLGLRRGELAWLREVLLVADGVPVVFARSILPRHDVRGAWILFQGLGSRPLGAALFADPRIGRKPLACACLDRRDARYHRASAAAAPRRLPLALWARRSLFGLRGRTLLVSEVFLPTILELPT | Function: Removes the pyruvyl group from chorismate, with concomitant aromatization of the ring, to provide 4-hydroxybenzoate (4HB) for the ubiquinone pathway.
Catalytic Activity: chorismate = 4-hydroxybenzoate + pyruvate
Sequence Mass (Da): 20742
Sequence Length: 185
Pathway: Cofactor biosynthesis; ubiquinone biosynthesis.
Subcellular Location: Cytoplasm
EC: 4.1.3.40
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Q2L1H6 | MTTKYQAPLAAGWLIRAPSLLSPTQRHWLFRPGALTAGLRQLGKVQLRVVSEHAEGASLDEARAMLIAPGSPVWVREVLMSVDGIDSVPARSLTPLAASHGSWQGMRRLLTRPLADMLYHDRGVTRSPFVCRRLSSPLPFYRMALPPNHDGSAIWARRSVFWRHGQPLLVAECFLPDFWRKVTLGRAIPPLKAHDRRA | Function: Removes the pyruvyl group from chorismate, with concomitant aromatization of the ring, to provide 4-hydroxybenzoate (4HB) for the ubiquinone pathway.
Catalytic Activity: chorismate = 4-hydroxybenzoate + pyruvate
Sequence Mass (Da): 22167
Sequence Length: 198
Pathway: Cofactor biosynthesis; ubiquinone biosynthesis.
Subcellular Location: Cytoplasm
EC: 4.1.3.40
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Q1QSG3 | MSPDRFPGWPHWLPIAAQRPRMSPDWWPWVASRDSLTARLRIASPRPFSVRLLTQGVTRPRLDEAQALGLPHRTHVWHREVLLRLGNASWVAARSVAPLEGLSGARLCTLGERSLGSWLFRQPNLERGPIEAIRAPAMTGLDAWRGDAGPWGRRSLLRVGRTRILVQEFFLAAMAADLSLPSR | Function: Removes the pyruvyl group from chorismate, with concomitant aromatization of the ring, to provide 4-hydroxybenzoate (4HB) for the ubiquinone pathway.
Catalytic Activity: chorismate = 4-hydroxybenzoate + pyruvate
Sequence Mass (Da): 20588
Sequence Length: 183
Pathway: Cofactor biosynthesis; ubiquinone biosynthesis.
Subcellular Location: Cytoplasm
EC: 4.1.3.40
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Q9CKD6 | MTDQHAFATEQVQLDPTLSPTTEETTHFGFKTVAKSEKQKMVANVFHSVAGKYDLMNDLLSFGIHRVWKRFTIDCSGVRKGHKVLDLAGGTGDFTAKFSRLVGPSGEVILADINDSMLRVGREKLRNLGVVGNVNYVQANAEALPFPDNTFDCVIISFGLRNVTDKDKALRSMFRVLKPGGRLLVLEFSKPILDPLSKIYNFYSFNILPKIGEVVVNDSESYRYLAESIRMHPAQDVLKQMMIDAGFEQVNYYNLSAGIVALHRGYKF | Function: Methyltransferase required for the conversion of demethylmenaquinol (DMKH2) to menaquinol (MKH2) and the conversion of 2-polyprenyl-6-methoxy-1,4-benzoquinol (DDMQH2) to 2-polyprenyl-3-methyl-6-methoxy-1,4-benzoquinol (DMQH2).
Catalytic Activity: a 2-demethylmenaquinol + S-adenosyl-L-methionine = a menaquinol + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 30020
Sequence Length: 268
Pathway: Quinol/quinone metabolism; menaquinone biosynthesis; menaquinol from 1,4-dihydroxy-2-naphthoate: step 2/2.
EC: 2.1.1.163
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B4RC42 | MTGPSATFGFRDVDAREKPGLVRGVFDRVARRYDLMNDLMSAGVHRLWKDAVAARLNPQPGETILDVAGGTGDMARRFARMARRAQERRGGDDAKVFVIDYNAEMIAAGRERGFEPEICWTVGDAQRLPLPDACADAYVISFGIRNVTDIPAALREARRVLKPGGRFLCLEFSRPVTEPLQRAYDLYSFKVIPEIGERVAGDRESYQYLVESIRRFPDQKRFAGMIGEAGFSRVGYTNFTAGVAALHTGRAI | Function: Methyltransferase required for the conversion of demethylmenaquinol (DMKH2) to menaquinol (MKH2) and the conversion of 2-polyprenyl-6-methoxy-1,4-benzoquinol (DDMQH2) to 2-polyprenyl-3-methyl-6-methoxy-1,4-benzoquinol (DMQH2).
Catalytic Activity: a 2-demethylmenaquinol + S-adenosyl-L-methionine = a menaquinol + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 28025
Sequence Length: 252
Pathway: Quinol/quinone metabolism; menaquinone biosynthesis; menaquinol from 1,4-dihydroxy-2-naphthoate: step 2/2.
EC: 2.1.1.163
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Q9A9X1 | MTQAASAAPSWSIDPADVARFSAIAAEWWDPKGKFAPLHVFNPCRLAFIREQALARFDRDGAARAPFEGLTLLDIGCGGGLLSEPMARLGFAVTAIDASEKNIKTAATHAAEQGLDIGYRPATAEQLLAEGAGPFDVVLTMEVIEHVADPGEFLRTCAKLLKPGGIMFVATLNRTLKALALAKIGAEYVLRWVPPGTHDWKQFLKPEELRAFLAGEPVAMQGPFGVAYNPLTGRWSRSSDTDINYMMTVTKD | Function: O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway.
Catalytic Activity: a 3-demethylubiquinol + S-adenosyl-L-methionine = a ubiquinol + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 27245
Sequence Length: 252
Pathway: Cofactor biosynthesis; ubiquinone biosynthesis.
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Q9FIQ1 | MAEFSDPPPSNLSSSHKLTKPNQTLDESSPTAPIRDLVTNSLSLSSPIRQIQALSPAKPDGSSSSPPDKTLNFNPEENRDVNPDESSSSPSDKTLIAPPAQISPVSNNNHLRITNTSDSYLYRPPRRYIEYESDDDELNKMEPTKPLQLSWWYPRIEPTGVGAGLYNSGNTCFIASVLQCFTHTVPLIDSLRSFMYGNPCNCGNEKFCVMQALRDHIELALRSSGYGINIDRFRDNLTYFSSDFMINHQEDAHEFLQSFLDKLERCCLDPKNQLGSVSSQDLNIVDNVFGGGLMSTLCCCNCNSVSNTFEPSLGWSLEIEDVNTLWKALESFTCVEKLEDQLTCDNCKEKVTKEKQLRFDKLPPVATFHLKRFTNDGVTMEKIFDHIEFPLELDLSPFMSSNHDPEVSTRYHLYAFVEHIGIRATFGHYSSYVRSAPETWHNFDDSKVTRISEERVLSRPAYILFYAREGTPWFSSTFEQLKTVFEATPLHFSPVSVLDNSYESVDNSSKACNDSVGVSIPDVKWPDSCCQEPKEEVFHSAESSNNEDSSAMIDALGSPQSEKPFAETSQQTEPESCPTENKAYIDKSEKPFAETSQPKEPKPFADRASIDAPLLKVQNQDISPKRKAGERATLGGPKLKYQKPNSHQKRQGTFQIQRAHLQTKKQEESRKTKRPLFRSNVAASAPDPKYKNHALSYLNRAQTPRARKLANALSDSPTKKKKSSNMRRSIKL | Function: Recognizes and hydrolyzes the peptide bond at the C-terminal Gly of ubiquitin. Involved in the processing of poly-ubiquitin precursors as well as that of ubiquitinated proteins (By similarity).
Catalytic Activity: Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
Sequence Mass (Da): 82417
Sequence Length: 732
EC: 3.4.19.12
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Q9UK80 | MPQASEHRLGRTREPPVNIQPRVGSKLPFAPRARSKERRNPASGPNPMLRPLPPRPGLPDERLKKLELGRGRTSGPRPRGPLRADHGVPLPGSPPPTVALPLPSRTNLARSKSVSSGDLRPMGIALGGHRGTGELGAALSRLALRPEPPTLRRSTSLRRLGGFPGPPTLFSIRTEPPASHGSFHMISARSSEPFYSDDKMAHHTLLLGSGHVGLRNLGNTCFLNAVLQCLSSTRPLRDFCLRRDFRQEVPGGGRAQELTEAFADVIGALWHPDSCEAVNPTRFRAVFQKYVPSFSGYSQQDAQEFLKLLMERLHLEINRRGRRAPPILANGPVPSPPRRGGALLEEPELSDDDRANLMWKRYLEREDSKIVDLFVGQLKSCLKCQACGYRSTTFEVFCDLSLPIPKKGFAGGKVSLRDCFNLFTKEEELESENAPVCDRCRQKTRSTKKLTVQRFPRILVLHLNRFSASRGSIKKSSVGVDFPLQRLSLGDFASDKAGSPVYQLYALCNHSGSVHYGHYTALCRCQTGWHVYNDSRVSPVSENQVASSEGYVLFYQLMQEPPRCL | Function: Deubiquitinates histone H2A, a specific tag for epigenetic transcriptional repression, thereby acting as a coactivator (By similarity). Deubiquitination of histone H2A releaves the repression of di- and trimethylation of histone H3 at 'Lys-4', resulting in regulation of transcriptional initiation (By similarity). Regulates gene expression via histone H2A deubiquitination (By similarity). Deubiquitinates BAZ2A/TIP5 leading to its stabilization . Also capable of removing NEDD8 from NEDD8 conjugates but has no effect on Sentrin-1 conjugates . Also acts as a negative regulator of the ribosome quality control (RQC) by mediating deubiquitination of 40S ribosomal proteins RPS10/eS10 and RPS20/uS10, thereby antagonizing ZNF598-mediated 40S ubiquitination .
Catalytic Activity: Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
Sequence Mass (Da): 62656
Sequence Length: 565
Subcellular Location: Cytoplasm
EC: 3.4.19.12
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Q9LEW0 | MSARISFLKNPDPCNHLSDYKLRYGTDGYKSFNNLFRCFNDARIKIKLQGIDIPRCSYCSVYQKRLYICLICRSISCSSHILLHTQLNKGHDIAIDVERSELYCCACIDQVYDSEFDEVVVSKQLFGLGMSVKSGADVVAVRSNKKRRLDSQLIIGSNFLVSPRDRREKWTFPLGLRGLNNLGSTCFMNAVLQALVHAPPLRNFWLSGQHNRDLCPRRTMGLLCLPCDLDVIFSAMFSGDRTPYSPAHLLYSWWQHSTNLATYEQQDSHEFFISLLDRIHENEGKSKCLYQDNEECQCITHKAFSGLLRSDVTCTTCGSTSTTYDPFIDISLTLDSMNGFSPADCRKNRYSGGPSVNAIMPTLSGCLDFFTRSEKLGPDQKLNCQSCGEKRESSKQMSIRRLPLLLCLHVKRFEHSLTRKTSRKIDSYLQYPFRLNMSPYLSSSIIGKRFGNRIFAFDGEGEYDSSSSSSPSAEFEIFAVVTHKGMLESGHYVTYLRLKGLWYRCDDAWINEVEEEVVRGCECYMLFYAQETVIQKAHKELSYQVISMADAFPFADC | Function: Component of a deubiquitination module (DUB module) that specifically deubiquinates monoubiquinated histone H2B (H2Bub) . Does not seem to be a component of the TREX-2 complex . Seems to act independently of the SAGA multiprotein complex . The DUB module is responsible for the major H2Bub deubiquitinase activity in Arabidopsis .
Catalytic Activity: Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
Sequence Mass (Da): 63518
Sequence Length: 557
Subcellular Location: Nucleus
EC: 3.4.19.12
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P0C8Z3 | MDAELVVTPPGCAHLGSFKVDNWKQNLRAIYQCFVWSGSAEARKRKAKSCVCHVCGLHLNRLHSCLHCVFFGCFTKKHIHEHAKSKRHNLAIELMYGGIYCFLCQDYIYDKDIEIIAKEEQRKAWKMQGVGEKFSTWEPTKRELELLKHNPKRRKITSNCTIGLRGLINLGNTCFMNCIVQALTHTPLLRDFFLSDRHRCEMQSPSSCLVCEMSSLFQEFYSGHRSPHIPYKLLHLVWTHARHLAGYEQQDAHEFLIAALDVLHRHCKGDDNGKKANNPNHCNCIIDQIFTGGLQSDVTCQVCHGVSTTIDPFWDISLDLPGSSTPFWPLSPGSESSVVNGESHVSGTTTLTDCLRRFTRPEHLGSSAKIKCSGCHSYQESTKQLTMKKLPIVACFHLKRFEHSAKLRRKITTYVSFPLELDMTPFMASSKESRMNGQYQQPTDSLNNDNKYSLFAVVNHQGTLESGHYTSFIRQHKDQWFKCDDAIITKASIADVLDSEGYLLFYHKQFLEYE | Function: Histone deubiquitinating component of the transcription regulatory histone acetylation (HAT) complex SAGA. Catalyzes the deubiquitination of both histones H2A and H2B, thereby acting as a coactivator. Recruited to specific gene promoters by activators such as MYC, where it is required for transcription. Required for nuclear receptor-mediated transactivation and cell cycle progression (By similarity).
Catalytic Activity: Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
Sequence Mass (Da): 58737
Sequence Length: 514
Subcellular Location: Nucleus
EC: 3.4.19.12
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A6H8I0 | MSPAGCSHVNGFKVDNWKQNLRVIYQCFVWSGSAETRKRKAKSCICHMCGAHLNRLHSCLHCVFFGCFSKKHIHEHAKNKRHNLAIDLLYGGIYCFVCQDYIYDKDMEQIAKEEQRKAWKLQGIGEKYSMWEPTKRELELLRHNPKRRKITANCTIGLRGLINLGNTCFMNCIVQALTHTPLLRDFFLSDRHKCEMQSNSCLVCEMSQLFQEFYSGHRSPHIPFRLLHLVWTHARHLAGYEQQDAHEFLIAALDVLHRHCKDDNGKKANNPNHCNCIIDQIFTGGLQSDVTCQVCHGVSTTIDPFWDISLDLPGSSTPFWPLSPGSDGSVVNGDSHPSGATTLTDCLRRFTRPEHLGSSAKIKCSGCHSYQESTKQLTMKRLPIVACFHLKRFEHSAKLRRKITTYVSFPLELDMTPFMASSKESRMNGQYQQPVDSLNNDNKYSLFAVVNHQGTLESGHYTTFIRQHKDQWFKCDDAIITKASIKDVLDSEGYLLFYHKQFLEYE | Function: Histone deubiquitinating component of the transcription regulatory histone acetylation (HAT) complex SAGA. Catalyzes the deubiquitination of both histones H2A and H2B, thereby acting as a coactivator. Recruited to specific gene promoters by activators, where it is required for transcription (By similarity).
Catalytic Activity: Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
Sequence Mass (Da): 58120
Sequence Length: 506
Subcellular Location: Nucleus
EC: 3.4.19.12
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Q9UPT9 | MVSRPEPEGEAMDAELAVAPPGCSHLGSFKVDNWKQNLRAIYQCFVWSGTAEARKRKAKSCICHVCGVHLNRLHSCLYCVFFGCFTKKHIHEHAKAKRHNLAIDLMYGGIYCFLCQDYIYDKDMEIIAKEEQRKAWKMQGVGEKFSTWEPTKRELELLKHNPKRRKITSNCTIGLRGLINLGNTCFMNCIVQALTHTPLLRDFFLSDRHRCEMQSPSSCLVCEMSSLFQEFYSGHRSPHIPYKLLHLVWTHARHLAGYEQQDAHEFLIAALDVLHRHCKGDDNGKKANNPNHCNCIIDQIFTGGLQSDVTCQVCHGVSTTIDPFWDISLDLPGSSTPFWPLSPGSEGNVVNGESHVSGTTTLTDCLRRFTRPEHLGSSAKIKCSGCHSYQESTKQLTMKKLPIVACFHLKRFEHSAKLRRKITTYVSFPLELDMTPFMASSKESRMNGQYQQPTDSLNNDNKYSLFAVVNHQGTLESGHYTSFIRQHKDQWFKCDDAIITKASIKDVLDSEGYLLFYHKQFLEYE | Function: Histone deubiquitinating component of the transcription regulatory histone acetylation (HAT) complex SAGA. Catalyzes the deubiquitination of both histones H2A and H2B, thereby acting as a coactivator. Recruited to specific gene promoters by activators such as MYC, where it is required for transcription. Required for nuclear receptor-mediated transactivation and cell cycle progression.
Catalytic Activity: Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
Sequence Mass (Da): 59961
Sequence Length: 525
Subcellular Location: Nucleus
EC: 3.4.19.12
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Q9FPS4 | MEVATSSTEITIQTDRDPSSNNNGSCAVASSTASAVFRKIEFHPARKPFNGFSNGRSDFKIETLNPCSSNQRLLSAPSAKKPDSSDLLEHGFEPDLTFSITFRKIGAGLQNLGNTCFLNSVLQCLTYTEPLAATLQTAAHQKYCHVAGFCALCAIQKHVRTARQANGRILAPKDLVSNLRCISRNFRNCRQEDAHEYMINLLECMHKCSLPSGVPSESSDAYRRSLVHKIFGGSLRSQVKCEQCSHCSNKFDPFLDLSLDISKADSLQRALSRFTAVELLDNGAKVYQCERCKQKVKAKKQLTVSKAPYVLTVHLKRFEAHRSEKIDRKVDFTSAIDMKPFVSGPHEGNLKYTLYGVLVHYGRSSHSGHYACFVRTSSGMWYSLDDNRVVQVSEKTVFNQKAYMLFYVRDRQNAVPKNSVPVVKKESFATNRASLIVASNIKDQVNGSTVIKECGFGALVANGLAPLKSCGPSTPAVLTQKDLNAKETQNNAISNVEAKEILETENGSAPVKTCDLAAPTVLVQKDLNTKEIFQKEVPLPQANGEGSLVKEDSKAACLILPEKVSPHLDGSANAQTLVKLPTLGPKAENSVEEKNSLNNLNEPANSLKVINVSVGNPPVEKAVLIDQTMGHHLEESATSIESLKLTSERETLTTPKKTRKPKTKTLKVEFKFFKLALGLRKKKVQRRERLSTTVAGEIISEELLSKKRVKYQDTSLIAPSKMISSSDGAVTSDQQQPVGSSDLSEASQNAKRKRESVLLQKEAVNILTRGVPETVVAKWDEEISASQKRGSKSEGASSIGYVADEWDEEYDRGKKKKIRIKEESYRGPNPFQMLASKRQKETKKKWTQSITDAKTAYRI | Function: Recognizes and hydrolyzes the peptide bond at the C-terminal Gly of ubiquitin. Involved in the processing of poly-ubiquitin precursors as well as that of ubiquitinated proteins (By similarity).
Catalytic Activity: Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
Sequence Mass (Da): 94903
Sequence Length: 859
EC: 3.4.19.12
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Q9FPS3 | MSEKKVFVFGSFTEHETRSFFEQKPTKDPQNSKDKCVGSIQFGSLNLAAENSSVNTNGELKKGEADGTVKSAGSQERLDASRPASSDKNNDSDAKLPRKNSLRVPEHVVQNGIIKEISESNKSLNNGVAVKTDPIGLDNLSMSDGESDPVYKASSSKFQALDNEDFSSDSSSGSIQRKKNLKVPTESVPPVKDFTPRGLINAGNLCFLNATLQALLSCSPFVQLLQKIQLQDIPKADSPTLAAFSEFISELDVPSSSSIRNNVTVVEAGRPFRPAMFEGVLRNFTPDVLNNMSGRPRQEDAQEFLSFIMDQMHDELLKLKEQSPKVTASKSSVISSANDDGDEWETVGPKNKSAVTRTQSFVPSELSEIFGGQLKSVVKAKGTKASATVQPYLLLHLDIHPDGVQGIEDALHLFSAQEDLEGYRASVTGKTGVVSASKSIKIQKLSKIMILHLMRFSYGSQGSTKLRKGVKFPLELNLNRSHLVSLSNESLRYELVATITHHGWDPSKGHYTTDARRKNGQWLRFDDASVTPIGTKLVLHDQAYVLFYKQV | Function: Recognizes and hydrolyzes the peptide bond at the C-terminal Gly of ubiquitin. Involved in the processing of poly-ubiquitin precursors as well as that of ubiquitinated proteins (By similarity).
Catalytic Activity: Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
Sequence Mass (Da): 60440
Sequence Length: 551
EC: 3.4.19.12
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Q9FPS2 | MGFKLQMSWMPSLLSQKRRNGPPLGLRNLGNTCYLNSVLQCLTFTPPLANFCLTHKHSSHCDTYVDGERKRDCPFCIVEKRIARSLSVDLTTDAPNKISSCLKIFAEHFKLGRQEDAHEFLRYVIDACHNTSLRLKKLRYNGNEPFNGNSVVKEIFGGALQSQVKCLSCGAESNKADEIMDISLEILQSSSVKESLQKFFQSEILDGNNKYRCESCEKLVTARKQMSILQAPNILVIQLKRFGGIFGGKIDKAISFGEILVLSNFMSKASKDPQPEYKLFGIIVHSGFSPESGHYYAYVKDSLGRWYCCNDSFVSLSTLQEVLSEKAYILFFSRSNQRPASAKTLVTSNGTTSHEVNGCETSNPQKFIGPLNGFNMKPQAEQSFQKGNLASSKPHKFIRPKPRAEQAPLEDNLLSSKVEKAPLRPHAKVSISVNLGAKRVSPVNGRLSFHQDENIAPKANKENSVSVLPTKVNSGTERKFGTENGGNGVKENGSAPGSSNHKVALHPHERSNGSSNGGDHHKDNLHPCGSNGSQNGTAHPETERNGVSTTQSKGLCSSTKEDPCILLRKDESSRNELEAIKESLKKDALSHLRSCGWYDKVLISMHAKKRLRTEQSGGEDGSDLKRRLIEDVKSSLKSQIPEELKADLVNRIWEISKKKYS | Function: Recognizes and hydrolyzes the peptide bond at the C-terminal Gly of ubiquitin. Involved in the processing of poly-ubiquitin precursors as well as that of ubiquitinated proteins (By similarity).
Catalytic Activity: Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
Sequence Mass (Da): 73293
Sequence Length: 661
EC: 3.4.19.12
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Q9BXU7 | MAALFLRGFVQIGNCKTGISKSKEAFIEAVERKKKDRLVLYFKSGKYSTFRLSDNIQNVVLKSYRGNQNHLHLTLQNNNGLFIEGLSSTDAEQLKIFLDRVHQNEVQPPVRPGKGGSVFSSTTQKEINKTSFHKVDEKSSSKSFEIAKGSGTGVLQRMPLLTSKLTLTCGELSENQHKKRKRMLSSSSEMNEEFLKENNSVEYKKSKADCSRCVSYNREKQLKLKELEENKKLECESSCIMNATGNPYLDDIGLLQALTEKMVLVFLLQQGYSDGYTKWDKLKLFFELFPEKICHGLPNLGNTCYMNAVLQSLLSIPSFADDLLNQSFPWGKIPLNALTMCLARLLFFKDTYNIEIKEMLLLNLKKAISAAAEIFHGNAQNDAHEFLAHCLDQLKDNMEKLNTIWKPKSEFGEDNFPKQVFADDPDTSGFSCPVITNFELELLHSIACKACGQVILKTELNNYLSINLPQRIKAHPSSIQSTFDLFFGAEELEYKCAKCEHKTSVGVHSFSRLPRILIVHLKRYSLNEFCALKKNDQEVIISKYLKVSSHCNEGTRPPLPLSEDGEITDFQLLKVIRKMTSGNISVSWPATKESKDILAPHIGSDKESEQKKGQTVFKGASRRQQQKYLGKNSKPNELESVYSGDRAFIEKEPLAHLMTYLEDTSLCQFHKAGGKPASSPGTPLSKVDFQTVPENPKRKKYVKTSKFVAFDRIINPTKDLYEDKNIRIPERFQKVSEQTQQCDGMRICEQAPQQALPQSFPKPGTQGHTKNLLRPTKLNLQKSNRNSLLALGSNKNPRNKDILDKIKSKAKETKRNDDKGDHTYRLISVVSHLGKTLKSGHYICDAYDFEKQIWFTYDDMRVLGIQEAQMQEDRRCTGYIFFYMHNEIFEEMLKREENAQLNSKEVEETLQKE | Function: Deubiquitinase regulating several biological processes through the deubiquitination of components of these processes . Involved in somatic cell reprogramming through the 'Lys-48'-linked deubiquitination and stabilization of CBX4 and CBX6, two components of the polycomb-repressive complex 1 (PRC1) . Also deubiquitinates and probably stabilizes the androgen receptor (AR), regulating the androgen receptor signaling pathway . May play a role in spermatogenesis .
Catalytic Activity: Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
Sequence Mass (Da): 104047
Sequence Length: 913
Subcellular Location: Nucleus
EC: 3.4.19.12
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Q99MX1 | MEPILINAQVQMWSAKAGMSKSRNALIETCVGKREVKLILYFSTGKIKTLQLHDNIKSVVLQTYGEDQNYLHLTFKNNDFLFVEKLTTTDARRLKRFLDKTSQGSIRPARSDERCGEPSTSAQELNGSGSSCETNSECFESPKESEMCMFRELSLLPSSSTFLHNVGLLENQFIKRKRFFSDLAKNEKQSNLKDSIRDFEANLVVCISNEKGKERNVREVDISKPGFGFPFETNYPEDSGVDVRDLNDLITKLFSPVLLETHCIENGLEWHEYMKTYLLYPEKLWQGLPNVGNTCYINVVLQSLCSIPLFINDLFNQGFPWIKAPKDDFNMLLMQLLVLKDIYNARFRQKLLIGITKALPIFGEIFAVDRQNDAHEFLSLCLVQLKETFQRVTMMWQSENDSGDFYLLKDIFADYATINKMPVCPVTNNFEFELLSSIFCKACGLTLFKGEPSRYLSINIPQGGKDMSIQSTLDLFFSAEELEHRCEKCLYNKSVSFHRFGRLPRVIIVHLKRYHFNESWVMKKDERPILVSKYLRLSCHCSKSTKPPPPLRPGEHVKNLDLLKPLEVLGSEILKLPFNSVRTSRSKGFETINITSNRESEAQSGKRVSEVLSGKVQQENSGKGDTAHIVGSELTKETEKLKKHEEEHRPSDLDSGSIREAQKYQQAEKCNEGRSDKQISLEALTQSRPKPISQEQTENLGKTTLSHTQDSSQSSQSSSDSSKSSRCSDDLDKKAKPTRKVDPTKLNKKEDNVYRLVNIINHIGNSPNGGHYINDAFDFKRQSWFTYSDLHVTRTQEDFVYRGRSSTGYVFFYMHNDIFEELLAKETQSTSTSKG | Function: Deubiquitinase regulating several biological processes through the deubiquitination of components of these processes . Involved in somatic cell reprogramming through the 'Lys-48'-linked deubiquitination and stabilization of CBX4 and CBX6, two components of the polycomb-repressive complex 1 (PRC1) (By similarity). Also deubiquitinates and probably stabilizes the androgen receptor (AR), regulating the androgen receptor signaling pathway (By similarity). May play a role in spermatogenesis (By similarity).
Catalytic Activity: Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
Sequence Mass (Da): 95452
Sequence Length: 835
Subcellular Location: Nucleus
EC: 3.4.19.12
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Q9VC99 | MQDLRNADTLRLPNGDGAAANDEVKSPFLIGVAGGTASGKSTVCKKIMEQLGQAEMDHTQRQVVSISQDSFYRELTPAEKAKAQKGLFNFDHPDAFNEELMYSTLQNILKGHKVEIPSYDYRTNSLDFENVLVIYPADVVLFEGILVFYFPKIRELFHMKLFVDTDSDTRLARRVPRDINERGRDLDAVLTQYMTFVKPAFEEFCSPTKKFADVIIPRGADNTVAIDLIVHHIGEILATTNSAQHSNTVRVAASSMKRDH | Function: (Microbial infection) Required for optimal replication of E.chaffeensis in the immune tissues, hemocytes, and fat body.
Catalytic Activity: ATP + uridine = ADP + H(+) + UMP
Sequence Mass (Da): 29213
Sequence Length: 260
Pathway: Pyrimidine metabolism; CTP biosynthesis via salvage pathway; CTP from cytidine: step 1/3.
EC: 2.7.1.48
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B9TQX1 | MNWNQIIFISLIATVLILAIANEAESAAVRTDKSDIKREDGENMKKRIFMQESEATAFLKRRGRRSTKSKDEVNAENRQRLAADERRREYYEEQRNEFENYVEEERDEQQERNREKTEQWREYHYDGLYPSYQYNRHHI | Function: May be involved in the negative control of osteogenic differentiation of osteochondrogenic precursor cells in peripheral zones of fetal cartilage and at the cartilage-bone interface.
PTM: Proteolytically cleaved by a furin-like convertase to generate a persistent C-terminal fragment found in almost the entire cartilage matrix, and affecting osteoblast differentiation.
Sequence Mass (Da): 16998
Sequence Length: 139
Subcellular Location: Secreted
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Q6NWB6 | MSWTQPALLTCLLVLSAITLFDGADSAVSDKRDAVNPQGALRKIFMPEADAASFFKRRSRRAVKTQDEINAEQRQRLAADERRREYHEEQRNKYENYAEEENDEQDERTREKTEQWREFHYDGLDPSYEYNRHTI | Function: May be involved in the negative control of osteogenic differentiation of osteochondrogenic precursor cells in peripheral zones of fetal cartilage and at the cartilage-bone interface.
PTM: Proteolytically cleaved by a furin-like convertase to generate a persistent C-terminal fragment found in almost the entire cartilage matrix, and affecting osteoblast differentiation.
Sequence Mass (Da): 16061
Sequence Length: 135
Subcellular Location: Secreted
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B9TQX3 | MSWTRVVVLSSLTTLLILTFSSVVKSAAVRDDSKAGDPKGAARHVFMPESDASNFFKHRSRRSPRYYSERQAEQRVRLSANERRREYNEEQRNEFENYVEEERDEQNERSREKNEQVREYHYDGLYPRYHWFH | Function: May be involved in the negative control of osteogenic differentiation of osteochondrogenic precursor cells in peripheral zones of fetal cartilage and at the cartilage-bone interface.
PTM: Proteolytically cleaved by a furin-like convertase to generate a persistent C-terminal fragment found in almost the entire cartilage matrix, and affecting osteoblast differentiation.
Sequence Mass (Da): 16109
Sequence Length: 133
Subcellular Location: Secreted
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Q14BU0 | MSWRRVILLSSLLALVLLCMLQEGTSASVGSRQAAAEGVQEGVKQKIFMQESDASNFLKRRGKRSPKSRDEVNAENRQRLRDDELRREYYEEQRNEFENFVEEQRDEQEERTREAVEQWRQWHYDGLYPSYLYNRQNI | Function: May be involved in the negative control of osteogenic differentiation of osteochondrogenic precursor cells in peripheral zones of fetal cartilage and at the cartilage-bone interface.
PTM: Proteolytically cleaved by a furin-like convertase to generate a persistent C-terminal fragment found in almost the entire cartilage matrix, and affecting osteoblast differentiation.
Sequence Mass (Da): 16579
Sequence Length: 138
Subcellular Location: Secreted
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Q96RP3 | MTRCALLLLMVLMLGRVLVVPVTPIPTFQLRPQNSPQTTPRPAASESPSAAPTWPWAAQSHCSPTRHPGSRIVLSLDVPIGLLQILLEQARARAAREQATTNARILARVGHC | Function: Suppresses food intake, delays gastric emptying and decreases heat-induced edema. Might represent an endogenous ligand for maintaining homeostasis after stress.
PTM: Glycosylated.
Sequence Mass (Da): 12146
Sequence Length: 112
Subcellular Location: Secreted
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P08067 | MLGIRSSVKTCFKPMSLTSKRLISQSLLASKSTYRTPNFDDVLKENNDADKGRSYAYFMVGAMGLLSSAGAKSTVETFISSMTATADVLAMAKVEVNLAAIPLGKNVVVKWQGKPVFIRHRTPHEIQEANSVDMSALKDPQTDADRVKDPQWLIMLGICTHLGCVPIGEAGDFGGWFCPCHGSHYDISGRIRKGPAPLNLEIPAYEFDGDKVIVG | Cofactor: Binds 1 [2Fe-2S] cluster per subunit.
Function: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c (Probable). The Rieske protein is a catalytic core subunit containing a [2Fe-2S] iron-sulfur cluster . It cycles between 2 conformational states during catalysis to transfer electrons from the quinol bound in the Q(0) site in cytochrome b (COB) to cytochrome c1 (CYT1) (Probable).
Catalytic Activity: a quinol + 2 Fe(III)-[cytochrome c](out) = a quinone + 2 Fe(II)-[cytochrome c](out) + 2 H(+)(out)
PTM: Processed by both the mitochondrial processing peptidase (MPP) and the mitochondrial intermediate protease (MIP). Initially, MPP removes 22 amino acids from the newly imported precursor in the mitochondrial matrix. This proteolytic processing is then followed by a second proteolytic cleavage by MIP, which removes an octapeptide to generate mature-sized RIP1.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 23365
Sequence Length: 215
Subcellular Location: Mitochondrion inner membrane
EC: 7.1.1.8
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Q9SG91 | MGKQPVKLKAVVYALSPFQQKIMTGLWKDLPEKIHHKVSENWISATLLVTPVVGTYWYAQYFKEQEKLEHRF | Function: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 8505
Sequence Length: 72
Subcellular Location: Mitochondrion inner membrane
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Q9FLB7 | MGKQPVKLKAVVYALSPFQQKIMTGLWKDLPEKIHHKVSENWISTILLVAPVVGTYSYAQYFKEQEKLEHRF | Function: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 8418
Sequence Length: 72
Subcellular Location: Mitochondrion inner membrane
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Q94K78 | MAGTSGLLNAVKPKIQTIDIQAAAGWGIAAAAGAIWVVQPFGWIKKTFIDPPPTEEK | Function: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 5976
Sequence Length: 57
Subcellular Location: Mitochondrion inner membrane
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A0A411KUP5 | MIIQGNQLDSLPKAEDWEAFAESYKRIAEVAVMKPVQALLQCLDDRLPLSGAVGILDNGSGPGIIMSSLIERYGPQLPPDCVLTCVDYAPAMIDQVDKARIKAVEEDADSAWGRVEGKVLDALDLHSIADESQSHIAAGLLYNLTTDPAKCLSECKRTLQPGGVLAVSAWEGNDWIEMLRVVPLIKPDLKTAIQPKWSTVDAVRWDLELAGFREVHVQRIPIKIPFTSHALFVDTLMRYQPRMVAMLRTFTEDEKTELRRLLMNEMKVICPSQPGMMSGAVMVGAGVR | Function: Methyltransferase; part of the gene cluster that mediates the biosynthesis of UCS1025A, a member of the pyrrolizidinone family that acts as a strong telomerase inhibitor and displays potent antibacterial and antitumor properties . These compounds share a hemiaminal-containing pyrrolizidinone core fused with a gamma-lactone, giving a furopyrrolizidine that is connected to a decalin fragment . The polyketide synthase module (PKS) of the PKS-NRPS ucsA is responsible for the synthesis of the polyketide backbone via the condensation of an acetyl-CoA starter unit with 6 malonyl-CoA units . The downstream nonribosomal peptide synthetase (NRPS) module then amidates the carboxyl end of the polyketide with a 2S,3S-methylproline derived from L-isoleucine by the 2-oxoglutarate-dependent dioxygenase ucsF which converts L-isoleucine to (4S,5S)-4-methylpyrroline-5-carboxylate that is further converted to 2S,3S-methylproline by the pyrroline-5-carboxylate reductase ucsG . Reductive release of the completed aminoacyl polyketide from the assembly line can form the 3-pyrrolin-2-one structure via an intramolecular Knoevenagel reaction . Because ucsA lacks a designated enoylreductase (ER) domain, the required activity is provided the enoyl reductase ucsL . This keto acyclic precursor is the substrate of the Diels-Alderase ucsH, that catalyzes the Diels-Alder cycloaddition . Oxidation of the 3S-methyl group to a carboxylate by the cytochrome P450 monooxygenase ucsK allows an oxa-Michael cyclization that might involve the reductase/dehydrogenase ucsI and which furnishes the furopyrrolizidine . The oxidase ucsJ likely plays a critical role in stereoselective reduction of the C5-C6 double bond to afford the required R-configured carboxylate group (Probable). Further enolization and oxidation at C5 by an unidentified enzyme affords the last intermediate that can undergo oxa-Michael cyclization to yield UCS1025A (Probable).
Sequence Mass (Da): 31826
Sequence Length: 288
Pathway: Mycotoxin biosynthesis.
EC: 2.1.1.-
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A0A411KUP9 | MYPFFTYSPGRHYFEYKWYNLELLRLIGSAPYGGCDAAEFLELVASLKPNDADEWHHKFLALAERTQAKGEQMSEAGHEAVARGAYLRASNYFRCAQYMFPIMPAARQGEFLKLYHRSIRSFEQAAELMEHRVERVSIPFQPPEYRAPAVELPGWLHLPAAHQRLSGRKTPLLICVGGADSTQEELYFLSAAEGPGLGYAILTFDGPGQGLTLRESGVPLRPDGEVVIEAVLDFIESYAAEHPEADLDVDAISITGQSLGGYLALRGAADPRIKACVAVDPIYDFYDLAMSRMPRWFMWPWERNYMGDGFVDFAVIEHSKLDVATKYTFAQGGQMFGSASPAQMIRDMKQYTFRLDKTITASKRHGNNRDYLEWVTCPVFVTGAAGDEKLFLPEMSTSAIMRNLANVPDEHKELWIPKEWSEGGAQAKSGAWPLLQHRCFKFLDEKLGISRGAKPVQLKTGFVKGVNGHGLTNGGLNGALNGATNGITNGVH | Function: Alpha/beta hydrolase; part of the gene cluster that mediates the biosynthesis of UCS1025A, a member of the pyrrolizidinone family that acts as a strong telomerase inhibitor and displays potent antibacterial and antitumor properties . These compounds share a hemiaminal-containing pyrrolizidinone core fused with a gamma-lactone, giving a furopyrrolizidine that is connected to a decalin fragment . The polyketide synthase module (PKS) of the PKS-NRPS ucsA is responsible for the synthesis of the polyketide backbone via the condensation of an acetyl-CoA starter unit with 6 malonyl-CoA units . The downstream nonribosomal peptide synthetase (NRPS) module then amidates the carboxyl end of the polyketide with a 2S,3S-methylproline derived from L-isoleucine by the 2-oxoglutarate-dependent dioxygenase ucsF which converts L-isoleucine to (4S,5S)-4-methylpyrroline-5-carboxylate that is further converted to 2S,3S-methylproline by the pyrroline-5-carboxylate reductase ucsG . Reductive release of the completed aminoacyl polyketide from the assembly line can form the 3-pyrrolin-2-one structure via an intramolecular Knoevenagel reaction . Because ucsA lacks a designated enoylreductase (ER) domain, the required activity is provided the enoyl reductase ucsL . This keto acyclic precursor is the substrate of the Diels-Alderase ucsH, that catalyzes the Diels-Alder cycloaddition . Oxidation of the 3S-methyl group to a carboxylate by the cytochrome P450 monooxygenase ucsK allows an oxa-Michael cyclization that might involve the reductase/dehydrogenase ucsI and which furnishes the furopyrrolizidine . The oxidase ucsJ likely plays a critical role in stereoselective reduction of the C5-C6 double bond to afford the required R-configured carboxylate group (Probable). Further enolization and oxidation at C5 by an unidentified enzyme affords the last intermediate that can undergo oxa-Michael cyclization to yield UCS1025A (Probable).
Sequence Mass (Da): 54716
Sequence Length: 492
Pathway: Mycotoxin biosynthesis.
EC: 3.7.1.-
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A0A411KUX1 | MSRNSGTTLEDGPLHADPTTEAPNNATVTTNVTANDENTEKEVDADAAAAAPAEAPKPNQGFRFWAIVAALAFTALLSSLEGTIITSALPKITADLGGGNSFIWVPNGYFLATIVMLPLMAQASNLFGRRWLTLISVATFTLGSGICGGANSQAMLIGGRVVQGFGGGGIALMINIILTDLVPLRERGKYMGIVQMVSAVGAALGPFLGGLLTSKSTWRWVFYINLPIGGTSLVALFFFLRVAKPPPTTLAEKISRIDFSGNAIFIASTVSVLIGVTWGGAVYPWSSFRVIVPLVLGFFGLGLFVVYEWTVAKNPSLPKDIILNRTAATVLGVTFLHTVATYWSFYFMPIYFQAVKGETSFWSGVDTLPLFAGIFPFAILGGMLLAKFGRYKPMHLIGMAIITLSFGLFSLLDQGSSKAAWACFQLLFAVGAGLMIAILLPAMQAPLPESLVALSTGVWTFVRGFGTVWGVTIPSAIFNNQCRLKAADLSDQGVASHLNSGKAYQYATKDFLDSIHDDATRRQVVELFTSSLRTVWYVGVALAGFGWLLIWLEKEVTLRSKLNTKFGLEEKKKAAKADEDVESASA | Function: MFS-type transporter; part of the gene cluster that mediates the biosynthesis of UCS1025A, a member of the pyrrolizidinone family that acts as a strong telomerase inhibitor and displays potent antibacterial and antitumor properties . These compounds share a hemiaminal-containing pyrrolizidinone core fused with a gamma-lactone, giving a furopyrrolizidine that is connected to a decalin fragment .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 62810
Sequence Length: 586
Subcellular Location: Membrane
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A0A411KUU9 | MATRTADKLEKKLVVVVGGTSGLGFAVAQAAVDRKANVVVASSKQASVDDALSRLQAGLASDDDVARVRGLTLDLAAANVEEQIVALYDFASKNGQQKIDHIAVTAGDSLYPKALDQVKAEDFINASQVRVIGALLLAKHAAKYLAKSAASSFTLTSGVRDVRPAANFAPVAPVSAAVKSLAKTLAHDLAPIRVNSISPGAVRTEFFTKIAGEHADAVLQGLAEQTLTKSNGVAEDIAEIYLVVMTSAYIDGADLVADGGSLIA | Function: Short-chain dehydrogenase/reductase; part of the gene cluster that mediates the biosynthesis of UCS1025A, a member of the pyrrolizidinone family that acts as a strong telomerase inhibitor and displays potent antibacterial and antitumor properties . These compounds share a hemiaminal-containing pyrrolizidinone core fused with a gamma-lactone, giving a furopyrrolizidine that is connected to a decalin fragment . The polyketide synthase module (PKS) of the PKS-NRPS ucsA is responsible for the synthesis of the polyketide backbone via the condensation of an acetyl-CoA starter unit with 6 malonyl-CoA units . The downstream nonribosomal peptide synthetase (NRPS) module then amidates the carboxyl end of the polyketide with a 2S,3S-methylproline derived from L-isoleucine by the 2-oxoglutarate-dependent dioxygenase ucsF which converts L-isoleucine to (4S,5S)-4-methylpyrroline-5-carboxylate that is further converted to 2S,3S-methylproline by the pyrroline-5-carboxylate reductase ucsG . Reductive release of the completed aminoacyl polyketide from the assembly line can form the 3-pyrrolin-2-one structure via an intramolecular Knoevenagel reaction . Because ucsA lacks a designated enoylreductase (ER) domain, the required activity is provided the enoyl reductase ucsL . This keto acyclic precursor is the substrate of the Diels-Alderase ucsH, that catalyzes the Diels-Alder cycloaddition . Oxidation of the 3S-methyl group to a carboxylate by the cytochrome P450 monooxygenase ucsK allows an oxa-Michael cyclization that might involve the reductase/dehydrogenase ucsI and which furnishes the furopyrrolizidine . The oxidase ucsJ likely plays a critical role in stereoselective reduction of the C5-C6 double bond to afford the required R-configured carboxylate group (Probable). Further enolization and oxidation at C5 by an unidentified enzyme affords the last intermediate that can undergo oxa-Michael cyclization to yield UCS1025A (Probable).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 27268
Sequence Length: 264
Pathway: Mycotoxin biosynthesis.
Subcellular Location: Membrane
EC: 1.1.-.-
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A0A411KUQ7 | MGVPLLDVSQLQAGPEARKQYLQALVQSFRDYGFVRLTKHDVPAKRVQRIFDLSTQMFNLDIDSKLEFANIADGSPQRGYSAVGVEKTASLHGNLIGRRVDEKLTDAREHFDCGSPLDKSFANRWPEKLQGFQQELESFYFELEQVTAGILGSLEEALNCPPGTLNNMITKENNASELRLNHYPPVPAGTLRNGNVARIWPHFDLGVITLLFTSAVGGLEVEDRNAPGPQTFIPVEPETEAELIVNISETLQRWTDDHLPAGLHRVTIPKDLDTEIQNDANVEIPGRYSIAYLCKADREADVGTLPVFQTGEAPRYKAMTASEYHRSRLLTAY | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: 2-oxoglutarate-dependent dioxygenase; part of the gene cluster that mediates the biosynthesis of UCS1025A, a member of the pyrrolizidinone family that acts as a strong telomerase inhibitor and displays potent antibacterial and antitumor properties . These compounds share a hemiaminal-containing pyrrolizidinone core fused with a gamma-lactone, giving a furopyrrolizidine that is connected to a decalin fragment . The polyketide synthase module (PKS) of the PKS-NRPS ucsA is responsible for the synthesis of the polyketide backbone via the condensation of an acetyl-CoA starter unit with 6 malonyl-CoA units . The downstream nonribosomal peptide synthetase (NRPS) module then amidates the carboxyl end of the polyketide with a 2S,3S-methylproline derived from L-isoleucine by the 2-oxoglutarate-dependent dioxygenase ucsF which converts L-isoleucine to (4S,5S)-4-methylpyrroline-5-carboxylate that is further converted to 2S,3S-methylproline by the pyrroline-5-carboxylate reductase ucsG . Reductive release of the completed aminoacyl polyketide from the assembly line can form the 3-pyrrolin-2-one structure via an intramolecular Knoevenagel reaction . Because ucsA lacks a designated enoylreductase (ER) domain, the required activity is provided the enoyl reductase ucsL . This keto acyclic precursor is the substrate of the Diels-Alderase ucsH, that catalyzes the Diels-Alder cycloaddition . Oxidation of the 3S-methyl group to a carboxylate by the cytochrome P450 monooxygenase ucsK allows an oxa-Michael cyclization that might involve the reductase/dehydrogenase ucsI and which furnishes the furopyrrolizidine . The oxidase ucsJ likely plays a critical role in stereoselective reduction of the C5-C6 double bond to afford the required R-configured carboxylate group (Probable). Further enolization and oxidation at C5 by an unidentified enzyme affords the last intermediate that can undergo oxa-Michael cyclization to yield UCS1025A (Probable).
Sequence Mass (Da): 37179
Sequence Length: 333
Pathway: Mycotoxin biosynthesis.
EC: 1.14.11.-
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A0A411KUQ8 | MRNGAHRCESAMPGVTMTVLGCGKLGTAIIQGLLRSCPKASEAAPQKYLYPISTVIAAVRSKDRLESLIKSLVAEINDHTCPLDFVIANNVEAVRRADVVFLACHPNQATECLGGIGMQDAISGKLVISVLGGVSVATLEQAVYSSTRRPASGQAPCHIVQAIANTAAARQQSVTVVAEEETANSHEKGSLCEDVLRRLGQVSYVSPDLMPAVTALCASGTAFFTTYLDAMIQGAVSEGLGEDVATRLAALTMAGAANAVISGEHPAAVTSRVTTPGGVTAEGLKVLREGDLRTLTAKAISATTRRLRLVDEKSRKQS | Function: Pyrroline-5-carboxylate reductase; part of the gene cluster that mediates the biosynthesis of UCS1025A, a member of the pyrrolizidinone family that acts as a strong telomerase inhibitor and displays potent antibacterial and antitumor properties . These compounds share a hemiaminal-containing pyrrolizidinone core fused with a gamma-lactone, giving a furopyrrolizidine that is connected to a decalin fragment . The polyketide synthase module (PKS) of the PKS-NRPS ucsA is responsible for the synthesis of the polyketide backbone via the condensation of an acetyl-CoA starter unit with 6 malonyl-CoA units . The downstream nonribosomal peptide synthetase (NRPS) module then amidates the carboxyl end of the polyketide with a 2S,3S-methylproline derived from L-isoleucine by the 2-oxoglutarate-dependent dioxygenase ucsF which converts L-isoleucine to (4S,5S)-4-methylpyrroline-5-carboxylate that is further converted to 2S,3S-methylproline by the pyrroline-5-carboxylate reductase ucsG . Reductive release of the completed aminoacyl polyketide from the assembly line can form the 3-pyrrolin-2-one structure via an intramolecular Knoevenagel reaction . Because ucsA lacks a designated enoylreductase (ER) domain, the required activity is provided the enoyl reductase ucsL . This keto acyclic precursor is the substrate of the Diels-Alderase ucsH, that catalyzes the Diels-Alder cycloaddition . Oxidation of the 3S-methyl group to a carboxylate by the cytochrome P450 monooxygenase ucsK allows an oxa-Michael cyclization that might involve the reductase/dehydrogenase ucsI and which furnishes the furopyrrolizidine . The oxidase ucsJ likely plays a critical role in stereoselective reduction of the C5-C6 double bond to afford the required R-configured carboxylate group (Probable). Further enolization and oxidation at C5 by an unidentified enzyme affords the last intermediate that can undergo oxa-Michael cyclization to yield UCS1025A (Probable).
Sequence Mass (Da): 33213
Sequence Length: 318
Pathway: Mycotoxin biosynthesis.
EC: 1.5.1.-
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A0A411KUQ1 | MARINRQTAYQKAQEIEFSTSSADPLAAWRISGIKGTAWEQWYFDSIADDGKSGIVLTMARDASYTVLGRGVLRVELDVTFEDGSHHNHVDWMNEAIVEDRSSPKSTGTIDGVWTAPGKSIRFQIAADGSAAKVEVDTPETKGHFTLAALSPPMYPNGETQNELESQGKVASTELLPKIHLVQVIPTATFEGDLMVNGRLLRFRGIGGHMHAWAQGAWFDTTLGWKVARGVAGPFSVTLMEYTDMEGIVHSSGYVVEDGVKRFGGLETYATPRSSATSQQVLKYRDEDRKGKQTVRWTPTYNTGFAGRFGDSSTGAILQFSSADSGETYRFELTHRRKAFEFLFGSSDSGLTAFLGEIKGGKIGSEVYEGVQASNVCVLPQGWTKIYFFICMLLAVVTFGYINILETNT | Function: Diels-Alderase; part of the gene cluster that mediates the biosynthesis of UCS1025A, a member of the pyrrolizidinone family that acts as a strong telomerase inhibitor and displays potent antibacterial and antitumor properties . These compounds share a hemiaminal-containing pyrrolizidinone core fused with a gamma-lactone, giving a furopyrrolizidine that is connected to a decalin fragment . The polyketide synthase module (PKS) of the PKS-NRPS ucsA is responsible for the synthesis of the polyketide backbone via the condensation of an acetyl-CoA starter unit with 6 malonyl-CoA units . The downstream nonribosomal peptide synthetase (NRPS) module then amidates the carboxyl end of the polyketide with a 2S,3S-methylproline derived from L-isoleucine by the 2-oxoglutarate-dependent dioxygenase ucsF which converts L-isoleucine to (4S,5S)-4-methylpyrroline-5-carboxylate that is further converted to 2S,3S-methylproline by the pyrroline-5-carboxylate reductase ucsG . Reductive release of the completed aminoacyl polyketide from the assembly line can form the 3-pyrrolin-2-one structure via an intramolecular Knoevenagel reaction . Because ucsA lacks a designated enoylreductase (ER) domain, the required activity is provided the enoyl reductase ucsL . This keto acyclic precursor is the substrate of the Diels-Alderase ucsH, that catalyzes the Diels-Alder cycloaddition . Oxidation of the 3S-methyl group to a carboxylate by the cytochrome P450 monooxygenase ucsK allows an oxa-Michael cyclization that might involve the reductase/dehydrogenase ucsI and which furnishes the furopyrrolizidine . The oxidase ucsJ likely plays a critical role in stereoselective reduction of the C5-C6 double bond to afford the required R-configured carboxylate group (Probable). Further enolization and oxidation at C5 by an unidentified enzyme affords the last intermediate that can undergo oxa-Michael cyclization to yield UCS1025A (Probable).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 44901
Sequence Length: 409
Pathway: Mycotoxin biosynthesis.
Subcellular Location: Membrane
EC: 5.5.1.-
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A0A411KUQ9 | MSPTDMKAVVFYGPHSIAIESRPIPKVQHDKDIVVKVSASGLCGSDLHYFRGHEVVDSAGFIMGHEFVGEVVEAGRAVTTVRPGDKVVSPFTVSCGDCFYCKLQNSSRCVHCQVFGSNGLDGAQAEYVRVPLADSTVVRAPPGLSDDALILMADIFPTGFFGARNAMAGLGAQDPTEAVVVVIGCGPVGLCAIVSALEYRPRVVFAIDSVDSRLGLAEKLGARPLDLKKGVPSIISAVQEVTEGRGADAVVEVVGQGPALRTAYDIIRPFGSISSIGAHHSAMPFSATDGYE | Cofactor: Binds 1 zinc ion per subunit.
Function: Medium chain reductase/dehydrogenase; part of the gene cluster that mediates the biosynthesis of UCS1025A, a member of the pyrrolizidinone family that acts as a strong telomerase inhibitor and displays potent antibacterial and antitumor properties . These compounds share a hemiaminal-containing pyrrolizidinone core fused with a gamma-lactone, giving a furopyrrolizidine that is connected to a decalin fragment . The polyketide synthase module (PKS) of the PKS-NRPS ucsA is responsible for the synthesis of the polyketide backbone via the condensation of an acetyl-CoA starter unit with 6 malonyl-CoA units . The downstream nonribosomal peptide synthetase (NRPS) module then amidates the carboxyl end of the polyketide with a 2S,3S-methylproline derived from L-isoleucine by the 2-oxoglutarate-dependent dioxygenase ucsF which converts L-isoleucine to (4S,5S)-4-methylpyrroline-5-carboxylate that is further converted to 2S,3S-methylproline by the pyrroline-5-carboxylate reductase ucsG . Reductive release of the completed aminoacyl polyketide from the assembly line can form the 3-pyrrolin-2-one structure via an intramolecular Knoevenagel reaction . Because ucsA lacks a designated enoylreductase (ER) domain, the required activity is provided the enoyl reductase ucsL . This keto acyclic precursor is the substrate of the Diels-Alderase ucsH, that catalyzes the Diels-Alder cycloaddition . Oxidation of the 3S-methyl group to a carboxylate by the cytochrome P450 monooxygenase ucsK allows an oxa-Michael cyclization that might involve the reductase/dehydrogenase ucsI and which furnishes the furopyrrolizidine . The oxidase ucsJ likely plays a critical role in stereoselective reduction of the C5-C6 double bond to afford the required R-configured carboxylate group (Probable). Further enolization and oxidation at C5 by an unidentified enzyme affords the last intermediate that can undergo oxa-Michael cyclization to yield UCS1025A (Probable).
Sequence Mass (Da): 30635
Sequence Length: 292
Pathway: Mycotoxin biosynthesis.
EC: 1.-.-.-
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A0A411KUU5 | MTKKIFATGATGYIGGDAIYALLSASPEYEVSCLVRSGAKATELVARHPSVRIVDGTLDDLELLEEAAANADIVCNFAHATHEPSVSALAKGLARRQRPGHGYLIHTMGSGTMIYDDVIQRRFGEHSDKVFNDVEGLPEVLAVPDFAKARGAENAVRDVGVKNPDRVRTAVVCTGSAYGPGRGLVEYRTSAIHELVRCTLSRGHALQVGAGKSAWRNVYIRDLSDVFVKLITHATNDEQDSDNTDESVWGGSGGYYFVENGEHVWGELARAISDEAVAQGLIQGGDIESIDAAEAASLAPMCNFFWGCNARVEGRRAARGLNWKPVGPPLVKELEVIVQKEAEKLGLS | Function: Oxidase; part of the gene cluster that mediates the biosynthesis of UCS1025A, a member of the pyrrolizidinone family that acts as a strong telomerase inhibitor and displays potent antibacterial and antitumor properties . These compounds share a hemiaminal-containing pyrrolizidinone core fused with a gamma-lactone, giving a furopyrrolizidine that is connected to a decalin fragment . The polyketide synthase module (PKS) of the PKS-NRPS ucsA is responsible for the synthesis of the polyketide backbone via the condensation of an acetyl-CoA starter unit with 6 malonyl-CoA units . The downstream nonribosomal peptide synthetase (NRPS) module then amidates the carboxyl end of the polyketide with a 2S,3S-methylproline derived from L-isoleucine by the 2-oxoglutarate-dependent dioxygenase ucsF which converts L-isoleucine to (4S,5S)-4-methylpyrroline-5-carboxylate that is further converted to 2S,3S-methylproline by the pyrroline-5-carboxylate reductase ucsG . Reductive release of the completed aminoacyl polyketide from the assembly line can form the 3-pyrrolin-2-one structure via an intramolecular Knoevenagel reaction . Because ucsA lacks a designated enoylreductase (ER) domain, the required activity is provided the enoyl reductase ucsL . This keto acyclic precursor is the substrate of the Diels-Alderase ucsH, that catalyzes the Diels-Alder cycloaddition . Oxidation of the 3S-methyl group to a carboxylate by the cytochrome P450 monooxygenase ucsK allows an oxa-Michael cyclization that might involve the reductase/dehydrogenase ucsI and which furnishes the furopyrrolizidine . The oxidase ucsJ likely plays a critical role in stereoselective reduction of the C5-C6 double bond to afford the required R-configured carboxylate group (Probable). Further enolization and oxidation at C5 by an unidentified enzyme affords the last intermediate that can undergo oxa-Michael cyclization to yield UCS1025A (Probable).
Sequence Mass (Da): 37406
Sequence Length: 348
Pathway: Mycotoxin biosynthesis.
EC: 1.-.-.-
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A0A411KUQ5 | MALLNTPVLAAATAVSFGFYLAGLFVYRVFYHRLSHIPGPRLAAFTVYYQSYYDFFPHQGQFLWKLVELHKAYGPIIRIGPDEVHVNDARFYKEMYGSSVHKRNKSPIWYWMDGLGAVGDQSMFITLDHDHHRLRKAGLGTYFSKRKVQELEPRVKEKVLLLRQRLLERAGRGAINLKDAFGGMALDIITQYCFNQCMGALDRDDLGREWNQLMAAGVKINPFARTFPTVARTLLRLPKWVLGVSGMVSTTGEFLDLADRLSANARNEAIRDLQEGKYTLTDDADSRTVLHSMMRSDVLPEHEKGERRLQADGMTLIAAGFDTTSRTLTVVFYHLLAKPAMRARVLEEIRTLMPTPSSPLPTVAQLEQLPYLTCVIHEGTRLAHGVAGRLVRIAPEEDLVYHNSSDDTEYTIPRGATFGQSSYLVHTDESIYPNPHDFIPERYWSDDGKPTDAERYLVAFGKGTRMCSGINLAFAELYLTIAALLGAVDMKLAPGTTEHDVSLVAELFVGVLPESPGVRVNVVGSL | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of UCS1025A, a member of the pyrrolizidinone family that acts as a strong telomerase inhibitor and displays potent antibacterial and antitumor properties . These compounds share a hemiaminal-containing pyrrolizidinone core fused with a gamma-lactone, giving a furopyrrolizidine that is connected to a decalin fragment . The polyketide synthase module (PKS) of the PKS-NRPS ucsA is responsible for the synthesis of the polyketide backbone via the condensation of an acetyl-CoA starter unit with 6 malonyl-CoA units . The downstream nonribosomal peptide synthetase (NRPS) module then amidates the carboxyl end of the polyketide with a 2S,3S-methylproline derived from L-isoleucine by the 2-oxoglutarate-dependent dioxygenase ucsF which converts L-isoleucine to (4S,5S)-4-methylpyrroline-5-carboxylate that is further converted to 2S,3S-methylproline by the pyrroline-5-carboxylate reductase ucsG . Reductive release of the completed aminoacyl polyketide from the assembly line can form the 3-pyrrolin-2-one structure via an intramolecular Knoevenagel reaction . Because ucsA lacks a designated enoylreductase (ER) domain, the required activity is provided the enoyl reductase ucsL . This keto acyclic precursor is the substrate of the Diels-Alderase ucsH, that catalyzes the Diels-Alder cycloaddition . Oxidation of the 3S-methyl group to a carboxylate by the cytochrome P450 monooxygenase ucsK allows an oxa-Michael cyclization that might involve the reductase/dehydrogenase ucsI and which furnishes the furopyrrolizidine . The oxidase ucsJ likely plays a critical role in stereoselective reduction of the C5-C6 double bond to afford the required R-configured carboxylate group (Probable). Further enolization and oxidation at C5 by an unidentified enzyme affords the last intermediate that can undergo oxa-Michael cyclization to yield UCS1025A (Probable).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 58960
Sequence Length: 526
Pathway: Mycotoxin biosynthesis.
Subcellular Location: Membrane
EC: 1.-.-.-
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A0A411KUQ4 | MGSLIQTPSTQTAVVTTAEGRHQVAHGRRVPSCGPRSVLVRIKAVALNATDHKMPARVKREGLTSGCDFAGEVVAVGEQANDEPRRCELPRSWAPGDRVFGVVYGSNPGQPEWGAFAEYVEADPIMLCHVPDGWDWETAASVGGSVHGSVALCLFGDGNLALDYSNLKAQADSSSADAVTNQSPKPESFTKEELRKVVLVYGGSTACGTMALQLLRLAGYTPITTCSPRNFGLVESYGAVAAFDYHSETCATEMKTYTRSSLVAALDCLGNTQSAALCYAALGRAGGRYVALEKYPDSVSATRKLVKPSWVMGPVMFGRELQLADGYSQPADLAARAFACDWYPLAERLVHQERLRAHPVTIAGPSPPVGDKWADAILCGLQELRDGSVSASKLVVPVAA | Function: Trans-enoyl reductase; part of the gene cluster that mediates the biosynthesis of UCS1025A, a member of the pyrrolizidinone family that acts as a strong telomerase inhibitor and displays potent antibacterial and antitumor properties . These compounds share a hemiaminal-containing pyrrolizidinone core fused with a gamma-lactone, giving a furopyrrolizidine that is connected to a decalin fragment . The polyketide synthase module (PKS) of the PKS-NRPS ucsA is responsible for the synthesis of the polyketide backbone via the condensation of an acetyl-CoA starter unit with 6 malonyl-CoA units . The downstream nonribosomal peptide synthetase (NRPS) module then amidates the carboxyl end of the polyketide with a 2S,3S-methylproline derived from L-isoleucine by the 2-oxoglutarate-dependent dioxygenase ucsF which converts L-isoleucine to (4S,5S)-4-methylpyrroline-5-carboxylate that is further converted to 2S,3S-methylproline by the pyrroline-5-carboxylate reductase ucsG . Reductive release of the completed aminoacyl polyketide from the assembly line can form the 3-pyrrolin-2-one structure via an intramolecular Knoevenagel reaction . Because ucsA lacks a designated enoylreductase (ER) domain, the required activity is provided the enoyl reductase ucsL . This keto acyclic precursor is the substrate of the Diels-Alderase ucsH, that catalyzes the Diels-Alder cycloaddition . Oxidation of the 3S-methyl group to a carboxylate by the cytochrome P450 monooxygenase ucsK allows an oxa-Michael cyclization that might involve the reductase/dehydrogenase ucsI and which furnishes the furopyrrolizidine . The oxidase ucsJ likely plays a critical role in stereoselective reduction of the C5-C6 double bond to afford the required R-configured carboxylate group (Probable). Further enolization and oxidation at C5 by an unidentified enzyme affords the last intermediate that can undergo oxa-Michael cyclization to yield UCS1025A (Probable).
Sequence Mass (Da): 42535
Sequence Length: 400
Pathway: Mycotoxin biosynthesis.
EC: 1.-.-.-
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A0A411KUQ2 | MKHADPLRADTLGTAPLSQAIEAHHHGKEREAHRQSLSSVPGDTVVEAPEKVVDLEINSVDNDKEHHRAPTRDEIQTLRKVPGSIPATAYLLCFVDFAERASWFGARSVSSNFMQFPLPEGGNGAGAPPSGSELPAGALGHGQRFSVALGLVFSFLSYVIPIFGAWLAEAKVGRYRTILIGVLIGGVAHIIMIAGAVPSILQAGKGTAPFLVSLFLLALGAGLFRPNVSPTVLDQHRHYQPFVKELPSGENVIIDPEATMQRIMLIFYALINVGAFYSLATVYSEKLVGYWLAFLLPGIIYLLLPLMLWYLNDKLIKVPPDGGALTKFWKILTVSLVENKGMVWKKGFFDRVQPGALLQKYPSSGPVKWTSKDVEDVKRTLVACEIFLYFPIYHLNDGGVGTILPSQGAAMLKKGVPNDLLGNFNPITIMITVPVLTYIVYPALRKSNIKFGRISRITLGFWLAVISGLVSSLVQWRIYKTSPCGYHATTCPEVAPVSIWWQLPSYVLGALSECFSNVTGYELAYARSPPGMRSLVVSLFLFSTALSSALGLILTPAIVDPHLVWVWAGPTIALAVQTVIFWVRHRKYNDDEFMIEGDE | Function: MFS-type transporter; part of the gene cluster that mediates the biosynthesis of UCS1025A, a member of the pyrrolizidinone family that acts as a strong telomerase inhibitor and displays potent antibacterial and antitumor properties . These compounds share a hemiaminal-containing pyrrolizidinone core fused with a gamma-lactone, giving a furopyrrolizidine that is connected to a decalin fragment .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 65669
Sequence Length: 599
Subcellular Location: Membrane
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P22309 | MAVESQGGRPLVLGLLLCVLGPVVSHAGKILLIPVDGSHWLSMLGAIQQLQQRGHEIVVLAPDASLYIRDGAFYTLKTYPVPFQREDVKESFVSLGHNVFENDSFLQRVIKTYKKIKKDSAMLLSGCSHLLHNKELMASLAESSFDVMLTDPFLPCSPIVAQYLSLPTVFFLHALPCSLEFEATQCPNPFSYVPRPLSSHSDHMTFLQRVKNMLIAFSQNFLCDVVYSPYATLASEFLQREVTVQDLLSSASVWLFRSDFVKDYPRPIMPNMVFVGGINCLHQNPLSQEFEAYINASGEHGIVVFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQNDLLGHPMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMTSEDLENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAHDLTWYQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH | Function: UDP-glucuronosyltransferase (UGT) that catalyzes phase II biotransformation reactions in which lipophilic substrates are conjugated with glucuronic acid to increase the metabolite's water solubility, thereby facilitating excretion into either the urine or bile . Essential for the elimination and detoxification of drugs, xenobiotics and endogenous compounds . Catalyzes the glucuronidation of endogenous estrogen hormones such as estradiol, estrone and estriol . Involved in the glucuronidation of bilirubin, a degradation product occurring in the normal catabolic pathway that breaks down heme in vertebrates . Also catalyzes the glucuronidation the isoflavones genistein, daidzein, glycitein, formononetin, biochanin A and prunetin, which are phytoestrogens with anticancer and cardiovascular properties . Involved in the glucuronidation of the AGTR1 angiotensin receptor antagonist losartan, a drug which can inhibit the effect of angiotensin II . Involved in the biotransformation of 7-ethyl-10-hydroxycamptothecin (SN-38), the pharmacologically active metabolite of the anticancer drug irinotecan .
Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 59591
Sequence Length: 533
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.4.1.17
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A8MRY9 | MRNNPVLPVSDPPLAGENDSDGKGVDDRLFKGSAMTKRGAYAALSYMACAVMLVLFNKAALSSYDFPCVNVITLFQMVSSSLFLYALRRRKIISFTAADSFSIDSASTFVPVKTLFHTLPLAIAYLLYMLASMASVRGVNVPMYTTLRRTTVAFTMVIEYMLTGQRYTRSIIGSVGIILLGAFFAGARDLSFDFYGYGVVFLANISTAVYLATIARTGKSSGLNSFGLMWSNGIICGPILMIWTFICGDLEKTINFPHLLTPGFMVVLLCSCVLAFVLNYCIFLNTTLNSALTQTICGNMKDLFTVGLGWMLFGGLPFDLMNVIGQLFGFFGSGLYAYYKIIGR | Function: Mediates the transport of UDP-N-acetylglucosamine (UDP-GlcNAc) across the Golgi apparatus membrane . Delivers an essential substrate for the maturation of N-glycans and the GlcNAc-containing glycosyl inositol phosphorylceramide (GIPC) class of sphingolipids in the Golgi apparatus .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 37640
Sequence Length: 344
Subcellular Location: Golgi apparatus membrane
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Q9UTF8 | MNPYRPYVVVNNVEPTFSITPEPTFETQPTISKSEIFETLRSILVTKYLTTFFVQPLEVAKTVCQVEEYLPKRTKIERDGKQTKEPYDEDIPDGTEQEGLSDDEHEIYAYFETPTTEKAVTEQLAEKLCVDASGYVTDPSNLIERSYTIHSKRFSIKSIISELWEKEGARGLWKGHTISFLHNLLYSGLQSWLSATLSGALAIADPNIISPIDSVRPLLSLFIKSITSAISALILSPLDIARTKIILFPISSSSYLSSASETSGNSHKKFKPLTIRQCLKALPFYCPSSLILPTVCYVSLPPFVSSVLPLTFRNFLGSSPTLDAMVGLGTSAVQFLLKCPLEMVLRRAQAQYECNLPPQTIVPVGKYTGIVGTIWCLLSEEDPGKFGIEGLYRGWRVGIWGMSSTLALNYISSNLREEVEF | Function: Required for mitochondrial fusion as well as normal mitochondrial morphology. May coordinate fusion of inner and outer membranes during mitochondrial fusion (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 46910
Sequence Length: 421
Subcellular Location: Mitochondrion outer membrane
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Q03327 | MNNNNVTEATSRAQIRPYYDPDSFNAGYSAVFKPDEGVVDPHGYTIASKLNVINSSPTTKRMANALFKSSPMKKLSNSVNDGLSLEGSNGEITGLNNFEWAELVNIQKWRKIFEQLLDMFFRKYFQLLIQQPFDVARLLIQVGEFKIFKTTVDTNKPQAPIILRDEEGDGAAREGEEDAYDEEEIDFFPIERKIAEANSTAPIMAEETDHSHHEPTDISLTIAPQSLHTIDVINALFDQEGIRGLWKANNTTFIYNFLSLSIDTWFTGLLSSFLGVPDPYFMEVINSPDISKSFILALGAGVFTSIILLPVDLIRTRLIVTSFKKKKNVKTDGKNMVTNTRSLRQLIRCWSWRKNGVSIPLDMWSLTILQSINNSFFNKLFDLVIYNQFHIEKYSQTVMYNTMKFFSKSLELFIKLPLENLLRRCQLNYLLNDQRLSFKVDSTELIVKPKKYNGIWDVIRNNSNTNRGQLWNGWKVGVISLICGYGLQMMNKVDINMEQEKF | Function: Required for mitochondrial fusion as well as normal mitochondrial morphology by bridging the essential interaction between FZO1 and MGM1. May coordinate fusion of inner and outer membranes during mitochondrial fusion.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 57543
Sequence Length: 502
Subcellular Location: Mitochondrion outer membrane
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P08800 | MTDTATSKATVERPKLQSTGSLHSLFKNVDLFSENDEELYPPLQHGARFAAPIEDSTLLALGMKPDELKAFQKQRHAYINKDQIYTDEIKIPNKTEMVDYHQLHLVSPIDQSNASRLLNKLVVIKLNGGLGNSMGCKTAKSTMEIAPGVTFLDMAVAHIEQINQDYNVDVPLVIMNSYKTHNETNKVIEKYKTHKVSIKTFQQSMFPKMYKDTLNLVPKPNTPMNPKEWYPPGSGDIFRSLQRSGLIDEFLAAGKEYIFISNVENLGSIIDLQVLNHIHLQKIEFGLEVTNRINTDSTGGILMSYKDKLHLLELSQVKPEKLKIFKDFKLWNTNNIWVNLKSVSNLIKEDKLDLDWIVNYPLENHKAMVQLETPAGMGIQNFKNSVAIFVPRDRYRPIKSTSQLLVAQSNIFQFDHGQVKLNSKREGQDVPLVKLGEEFSTVSDYEKRFKSIPDLLELDHLTVSGDVYFGSRITLKGTVIIVANHGERVDIPDGVVLENKVLSGTLRILDH | Function: Plays a central role as a glucosyl donor in cellular metabolic pathways. During development the lack of the enzyme activity leads to cell death and lysis. Strains which lack UDPG pyrophosphorylase accomplish early developmental events but are unable to culminate. The enzyme affects the growth rate of the cells but is not essential for growth.
Catalytic Activity: alpha-D-glucose 1-phosphate + H(+) + UTP = diphosphate + UDP-alpha-D-glucose
Sequence Mass (Da): 57885
Sequence Length: 511
Pathway: Carbohydrate metabolism; galactose metabolism.
EC: 2.7.7.9
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Q8SSC5 | MQESRSKESTLSGDEDKDVHRFLDEFDDKCTCKLLKEMKETLEGLKKSHPNPTNLDEFYRLFERYLRTRHEKIVWEKIRSPKDRIVQYNEIPEPTEKSKELLRKLAILKLNGGLGTTMGCVGPKSAITIKDGKNFIDLVVKQIRYLNSKYKIDVPLILMNSFNTEGMTDKIIFRYDGIKKFSQSKFPRISSETLLPVSPSHGDKGMYPPGHGDLFYSMKNSGMLEELLEGGYEYLFVSNIDNLASTVDLKLLEYFATNELGFLMEVTDKTRADVKGGTLIEYKGALRLLEIAQVPSNKKSEFTSFKKFTIFNTNNLWINLKEMKKKLEEGFFDLDIIENKKALDDETVIQLETAIGSAIKYFPNSCGVVVPRSRFLPVKTCSDLFLVESNLFVEKNGTLQLHPSRVPETCPTVKLIGENFSKIEKYEKCFKGIPDILELEVLTVSGNVLFGKNVVLKGTVIILADEKSKICVPDGSVLEDNIIYGNLPIIDH | Function: Plays a central role as a glucosyl donor in cellular metabolic pathways.
Catalytic Activity: alpha-D-glucose 1-phosphate + H(+) + UTP = diphosphate + UDP-alpha-D-glucose
Sequence Mass (Da): 55910
Sequence Length: 492
EC: 2.7.7.9
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P32861 | MSTKKHTKTHSTYAFESNTNSVAASQMRNALNKLADSSKLDDAARAKFENELDSFFTLFRRYLVEKSSRTTLEWDKIKSPNPDEVVKYEIISQQPENVSNLSKLAVLKLNGGLGTSMGCVGPKSVIEVREGNTFLDLSVRQIEYLNRQYDSDVPLLLMNSFNTDKDTEHLIKKYSANRIRIRSFNQSRFPRVYKDSLLPVPTEYDSPLDAWYPPGHGDLFESLHVSGELDALIAQGREILFVSNGDNLGATVDLKILNHMIETGAEYIMELTDKTRADVKGGTLISYDGQVRLLEVAQVPKEHIDEFKNIRKFTNFNTNNLWINLKAVKRLIESSNLEMEIIPNQKTITRDGHEINVLQLETACGAAIRHFDGAHGVVVPRSRFLPVKTCSDLLLVKSDLFRLEHGSLKLDPSRFGPNPLIKLGSHFKKVSGFNARIPHIPKIVELDHLTITGNVFLGKDVTLRGTVIIVCSDGHKIDIPNGSILENVVVTGNLQILEH | Function: Plays a central role as a glucosyl donor in cellular metabolic pathways.
Catalytic Activity: alpha-D-glucose 1-phosphate + H(+) + UTP = diphosphate + UDP-alpha-D-glucose
Sequence Mass (Da): 55988
Sequence Length: 499
EC: 2.7.7.9
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Q9M9P3 | MAATTENLPQLKSAVDGLTEMSESEKSGFISLVSRYLSGEAQHIEWSKIQTPTDEIVVPYEKMTPVSQDVAETKNLLDKLVVLKLNGGLGTTMGCTGPKSVIEVRDGLTFLDLIVIQIENLNNKYGCKVPLVLMNSFNTHDDTHKIVEKYTNSNVDIHTFNQSKYPRVVADEFVPWPSKGKTDKEGWYPPGHGDVFPALMNSGKLDTFLSQGKEYVFVANSDNLGAIVDLTILKHLIQNKNEYCMEVTPKTLADVKGGTLISYEGKVQLLEIAQVPDEHVNEFKSIEKFKIFNTNNLWVNLKAIKKLVEADALKMEIIPNPKEVDGVKVLQLETAAGAAIRFFDNAIGVNVPRSRFLPVKASSDLLLVQSDLYTLVDGFVTRNKARTNPSNPSIELGPEFKKVATFLSRFKSIPSIVELDSLKVSGDVWFGSSIVLKGKVTVAAKSGVKLEIPDRAVVENKNINGPEDL | Function: Converts glucose 1-phosphate to UDP-glucose, which is the major glycosyl donor for polysaccharides. Acts redundantly with UGP1 and is essential for the synthesis of sucrose, starch and cell wall, and callose deposition.
Catalytic Activity: alpha-D-glucose 1-phosphate + H(+) + UTP = diphosphate + UDP-alpha-D-glucose
Sequence Mass (Da): 51738
Sequence Length: 469
Subcellular Location: Cytoplasm
EC: 2.7.7.9
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Q54YZ0 | MMKPDLNSPLPQSPQLQAFGSRSSDLATEDLFLKKLEAISQTAPNETVKNEFLNKEIPSINKLFTRFLKNRKKVIDWDKINPPPADMVLNYKDLPAITEQRTSELASKLAVLKLNGGLGTTMGCTGPKSVIEVRSEKTFLDLSVQQIKEMNERYNIKVPLVLMNSFNTHQETGKIIQKYKYSDVKIHSFNQSRFPRILKDNLMPVPDKLFGSDSEWYPPGHGDVFFALQNSGLLETLINEGKEYLFISNVDNLGAVVDFNILEAMDKNKVEYIMEVTNKTRADVKGGTLIQYEGKAKLLEIAQVPSSKVEEFKSIKKFKIFNTNNIWVNLKAMDRILKQNLLDDMDIIINPKVADGKNIIQLEIAAGAAIEFFNNARGVNVPRSRFLPVKSTSDLFIVQSNLYSLEKGVLVMNKNRPFTTVPLVKLGDNFKKVSDYQARIKGIPDILELDQLTVSGDITFGPNMVLKGTVIIVANHGSRIDIPEGSEFENKVVSGNLHCGAL | Function: Plays a central role as a glucosyl donor in cellular metabolic pathways.
Catalytic Activity: alpha-D-glucose 1-phosphate + H(+) + UTP = diphosphate + UDP-alpha-D-glucose
Sequence Mass (Da): 56268
Sequence Length: 502
EC: 2.7.7.9
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O59819 | MLHRRIHFKSQSTLDFDSVAVSISASTMKNELDKLVLNSRVSDKKTFGIQMDNFFALYRRYLLHTVKGYECDWDSIRPLGPEDMIDYGDLPLCKNAGKYLNRLAVVKLNGGMGNALGVNYPKAMIEVRDNQSFLDLSIRQIEYLNRRYDVSVPFILMNSYDTNDETCKVLRKYAGCKIDISTFEQSRYPRVFVDSQLPVPKAAPSPIEEWYPPGHGDIFDALVHSGTIERLLAQGKDYLFVSNIDNLGASVDLNILSHVIDNQIEYSMEITDKTKADIKVGILVNQDGLLRLLETNQVPEQHREEFMSDKVFKYINTNNVWLYLPAVKRVVENRELNLDIMPNIETVYYNNEPARIIEFTTAIGSAISQFKKTEGIRVSRPRFISVKNSSDLFLVRCDLYNVDHGSLKIEESRLGFPPPVVRMSNEFKDIAELFCRIPYMPSMKDLVSLSISGNVYFGRNVILKGNIVIVASENTILCIPSNAVLENCVVTGNCKIMEC | Function: Plays a central role as a glucosyl donor in cellular metabolic pathways.
Catalytic Activity: alpha-D-glucose 1-phosphate + H(+) + UTP = diphosphate + UDP-alpha-D-glucose
Sequence Mass (Da): 56740
Sequence Length: 499
Subcellular Location: Cytoplasm
EC: 2.7.7.9
|
P38709 | MTVFSGVNKIEFEGTFEGIGKDVVMSQMIRALQKHFPSIRDKNYEFSLFLHIFQRYVLENTSITHDLVCDKIRLPIIDEVVELDDIKNYGLLEGKLLSKLAILKLTGKANPIIGKESPLFEVKNGMSSLDVIVRQTQNLNVRYNSDVPLIFMTSLETESQVSNFLEEHYSSSKVRWKTVVQSSFPQIDKDRLLPIDLQINSHENDFWYPCGTGNLTDTLYFSGELDKLIAQGKEILFVSNVDNLGATGDLNILNFIINEKIEYLVEVVERTANVSNTGVLATYKGKLRSVYYNCLSNESASTCRIVNTNNIWIDLKKLKVLIESNSLNLPIHSSESKITHKNEEIECLQFKTQLVDCIAFFPNSRVLKVSRDRFLPLRTCKDLFLLKSTLYDLDSNGTFNLYPLKFGLLPSIDLGDEFATYETFKIGVPDIPNILELEHLTVMGNVFFGRNITLKGTVIIICDENDVITVPDGSILENVTIWHKSQLEDMNGY | Function: Plays a central role as a glucosyl donor in cellular metabolic pathways.
Catalytic Activity: alpha-D-glucose 1-phosphate + H(+) + UTP = diphosphate + UDP-alpha-D-glucose
Sequence Mass (Da): 56000
Sequence Length: 493
EC: 2.7.7.9
|
F4IY62 | MANPQASPILHHPQNHLSLFHFRTTTSPRSFSSLHFRKPLLFLSSSSSFSSKLQQSEQQCNNHQVRHVSTVPVEYSTPTPPESDDFLSEIDRLKSLLSKLDVSKDLRRKDAVIDADSRVRRFFSENRGGLSKVFGYLGLNSNEMFLVKCVIAAGQEHALCMNYEEAFGEEEEEYTVRSSVKNALYALVEMIERFDVNSSGYKGRREMGTVLDSEEIAHFRKFLTFLEEIEQFYDCIGGIIGYQVMVLELLHQSSKRRNTNRSQLVEESLGCQYLEMHTPSVLDLTQEEDYASQAALWGIEGLPDLGEIYPLGGAADRLGLIDSETGECLPAAMLAHCGRTLLEGLIRDLQAREFLYFKLYGKQCVTPVAIMTSAAKNNHEHVSSLCERLKWFGRGQSNFRLFEQPLVPAVSAEDGQWIVSKPFVPVSKPGGHGVIWKLAYDKGVFNWFYDHGRKGATVRQVSNVVAATDVTLLALAGIGLRYNKKLGFASCKRNAGATEGINVLMEKKNFDGKWEYGISCIEYTEFDKFDISNRSPSSNGLQADFPANTNILYVDLHSAELIGSSSNAKSLPNMVLNTKKRIEYLDQYGDYHSVMGGRLECTMQNIADNFFNKFPSRCHGSLEDKLDTYIVYNERRKVTSSAKKKKPHASAALHQTPDGALLDILRNGYDLLTECDIKLPMIEANDKYVDSPPPYLILLHPALGPLWEVSRQKFKGGSISSCSELQLEIAEFSWNNVQVDGSLIVTAENAMGSTTPNDNGEPILQYGLRCGKCKLHNVNVVNRGIDWNSKSNVYWRNDVNRLETCKIILHGNAEFEASNVTIEGHHVFEVPDGHKLKITSGNAGLSINLEALKEEVMETGSWYWNYQLNGSHIHLQQVEVSQS | Function: Involved in the biosynthesis of sulfolipids in the chloroplast. Catalyzes the first committed step in sulfolipid biosynthesis. Converts glucose 1-phosphate to UDP-glucose, the precursor of the polar head of sulfolipid. In addition to glucose 1-phosphate, can use galactose 1-phosphate, but with much lower activity. No uridyltransferase activity with other hexose monophosphates. Specific for UTP and cannot use ATP, CTP, and GTP.
Catalytic Activity: alpha-D-glucose 1-phosphate + H(+) + UTP = diphosphate + UDP-alpha-D-glucose
Sequence Mass (Da): 99043
Sequence Length: 883
Subcellular Location: Plastid
EC: 2.7.7.9
|
Q7CRU3 | MQSVVFPNKILPYLLVAPQIILTVIFFFWPASQALYQSTMREDAFGLSSNFVGLANFSAVLSDESYLNSLKVTVIFSVLTALVSMGLALLLATAADRVVRGKGFYRTMMIMPYAVAPAVAGMLWLFMFNPAMGTLSYILRRNGIMWDPLLDGNQAMLLVVAAAAWKQISYNFLFFVAGLQAIPKSLLEAASIDGARGSRRFWTIVFPLLAPTTFFLLVVNTVYAFFDTFGIIHAVTGGGPAKATETLVYKVYNDGFVNLNLGSSAAQSVILMVIVIALTAFQFRFVEKRVHYG | Function: Part of the ABC transporter complex UgpBAEC involved in sn-glycerol-3-phosphate (G3P) import. Probably responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32198
Sequence Length: 293
Subcellular Location: Cell inner membrane
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Q18081 | MLLRILTFLAVCQVTTSHKILMFSPTASKSHMISQGRIADELANAGHEVVNFEPDFLNLTDKFVPCKKCRRWPVTGLNNYKFKKIQNGLSGDVFQQSSIWSKIFNTDSDPYQDEYTNMCEEMVTNKELIEKLKKEKFDAYFGEQIHLCGMGLAHLIGIKHRFWIASCTMSVSMRDSLGIPTPSSLIPFMSTLDATPAPFWQRAKNFVLQMAHIRDEYRDVVLTNDMFKKNFGSDFPCVEFLAKTSDLIFVSTDELLEIQAPTLSNVVHIGGLGLSSEGGGLDEKFVKIMEKGKGVILFSLGTIANTTNLPPTIMENLMKITQKFKDYEFIIKVDKFDRRSFDLAEGLSNVLVVDWVPQTAVLAHPRLKAFITHAGYNSLMESAYAGVPVILIPFMFDQPRNGRSVERKGWGILRDRFQLIKDPDAIEGAIKEILVNPTYQEKANRLKKLMRSKPQSASERLVKMTNWVLENDGVEELQYEGKHMDFFTFYNLDIIITAASIPVLIFIVLRISNISIITSSPKNKKD | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 59627
Sequence Length: 526
Subcellular Location: Membrane
EC: 2.4.1.17
|
A0A291PQG3 | MTLLRDLLLLYINSLLFINPSIGENILVFLPTKTYSHFKPLEPLFQELAMRGHNVTVFSGFSLTKNISNYSSIVFSAEIEFVNIGMGNLRKQSRIYNWIYVHNELQNYFTQLISDNQLQELLSNKDTQFDLIFIELYHVDGVFALSHRFNCPIIGLSFQPVLPIYNWLIGNPTTFSYIPHVYLPFTDIMSFWKRIINAVFSIFTAAFYNFVSTKGYQKHVDLLLRQTESPKLNIEELSESLSLILAEFHFSSAYTRPNLPNVIDIAGIHIQSPKPLPQDLLDFLDQSEHGVIYVSLGTLIDPIHTDHLGLNLINVFRKLRQRVIWKWKKEFFHDVPKNVLIGEWFPQIDILNHPRCKLFISHGGYHSMLESIYSSVPILGIPFFTDQHHNTAIIEKLKIGKKASTEASEEDLLTAVKELLSNETFKRNSQHQSSIFRDRPMSPMDTAIYWTEYILRYKGASHMKSAVIDLYWFQYILLDIILFYSLIVLILLCILRIFFRMLTK | Function: Catalyzes the transfer of a glycosyl group from a UDP-sugar to an acceptor molecule.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 58644
Sequence Length: 504
Subcellular Location: Microsome membrane
EC: 2.4.1.-
|
Q22295 | MHYSQMRWMFFCLTALLHGSFIVNAAKILVYCPSISKSHVLLCSKYADLLHNAGHDTVLFIPSYSKLLDNYDGAKHAKVWRLHNVTEAYDTKLGTLANVMENSHIGFIDRLTFDADFWIDMCADLLGKLPEMQHIIDYKFDLVIYNEIDPCTPAIVRLFNIPKTVLLSSEAIMDKVAWNLGLPTLPSYVPSVEENPNHDRMSFFERMSNVYKFFQSIVVHYLQDIHVLNLFRKEVSSDFPSIAEIIRNVSLVLVNTDEIFDLPRSYSSKFVYVGMLEAGKDENVTLPKKQDDYFKKGKSGSVFVSFGTVTPFRSLPERIQLSILNAIQKLPDYHFVVKTTADDESSAQFFSTVQNVDLVDWVPQKAVLRHANLKLFVSHGGMNSVLETMYYGVPMVIMPVFTDQFRNGRNVERRGAGKMVLRETVVKETFFDAIHSVLEEKSYSSSVKRISHLMKNKPFTSEERVTKWIDFVLKYETSEHFDLESNNLSIIEHNHLDLFFYLCIISLLNFVVYRKIFKRKSQS | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 60286
Sequence Length: 523
Subcellular Location: Membrane
EC: 2.4.1.17
|
Q22180 | MQLLTLPTLIFIFLNYGTPCLSLRILVYSPRMIPSHVAFVANIANLLGQRGHNVVVVDNVLRSDISNKLDLKVIEKVVKVETSANVAKLLADQSIPINFWSMRNEPEEQKKVMKQLGIIFLEQCKYLVSKEETVFNELKHLEFDFGIHEVFDICGIGIFEKLGIRKSVILSSTGMRDIVNEALGISSQLQDASILSDYGNSIPFYGIRRNLKFHSAWRNFFEVQSKTLEPLFETTSSFENLLRFSNLMFLNTHELADAHRPWSRRVHEIGGISFKFPMPLKNEYINLFNKYNSIILVSFGTTTPSFLMPEKYKNTLINTFQRFPDFLFIWKYEKDDEFTQKNKKGNVVFKKFLPQVDLLESRKIKLFITHGGQNSLLETFHSNTRTLITPLFGDQHRNAQIALENGLSHVLLKDQLANEELVYAAIKQGTESNKKLDDNLLKLSSNLKNAKQTSENLFLDTVESTYTDNLSPLNFEFYPKLYSSDQILLYLDSIAMFTLTLLTMILIRKFLL | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 58929
Sequence Length: 512
Subcellular Location: Membrane
EC: 2.4.1.17
|
Q22181 | MLWAFIVWLGALCIYGSAFDILIYAPRMMQSHVYFTARIANVLAARGHKVTVIDNVFRYDVDNELSSDIHEIISVEPSPEVTKLLNTGSLPTILWNSKASPEEQRTIMEGLGHVHRLQCTHLIENSTLIPKLQEIKFDFAIHEVFDSCGVGILEVIGVQKTVIVSSTGPMDVVPITLGISDTLNTPSLLSDYGSYLSFFEKRRNLKFLSGMLNFHEMQDSMISPLFKKYYGLKKPTGEIMRQANLLFYNIHEGSDGMRMRGRRSFDIGGIAFKDQKNLTMEYQTLLSDPRPKVLVSFGTAATSSHMPQNLKNSLMTAMKQMNNVLFIWKYEMEDNFTKQEELTTNIIFKKFLPQTDLLASSKIDLFVTHCGQNSLLEAFNSGVRVLAVPLFGDQHRNAKLAFENGLIEILPKSDIETPAKIVKAVKTGLEPNAKLDQNIVLISSLLRNSKENAENLLISTIEATYSTEFPPNFSKFPKNYHPNTLVRLIDSSIALVFMLFIFVFVNHFRKNYVGFKYPLSFSTK | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 59284
Sequence Length: 524
Subcellular Location: Membrane
EC: 2.4.1.17
|
Q20086 | MKSWLLLLGTIGWVTAGDVLFIPSTLYPVHAQTMSVLARELAERGHKVTWLEIGPERSDIVLHQQVSREFWPAQFGDRTLQEIYQFKNHTSHSELWNPQYTNENEQTTGWLASIRLCDSVLSRSKSKFDKMVEKQFSTVIVDDLYNSCGVLMAGLKKSVYIYWSMTGLRTESAWANQSPSPPSYLPVAGTGLTDDLTFSQRLYNVASYFKQLYIHQHIVQPRIDAVFQKYYPGVESTFEIERNASINFVNTPPIFDFSRPYMPRVNFIGAIQCRKPKELPKEFTSWISAYPDGFVVLSTGFTVQWNKSPEHIRQAYLDTFKYLPNLLFIWQTGLPNSSNLPSNLLVKPWLPLQDLLGHQKCRCHVSHGGLNSVIESVYHGVPVVGVPLTSRGYDNLLRITARDSGVMVEKSEFSGEILTAAINEVIENEKYKKEMLIFQDMVIDVPYTELYHAAFWVEFIERHQEVPHARSGADHLNFLQYFLVDVIAFFFFVIFCTLSIIYYTIRTVFRTIRSVVNGVRGVPKIVSRGKKNN | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 61143
Sequence Length: 533
Subcellular Location: Membrane
EC: 2.4.1.17
|
A0A291PQF1 | MIFFYFLTLTSFISVAFSYNILGVFPFQAKSHFGFIDPLLVRLAELGHNVTIYDPYPKSEKLPNYNEIDVSECFVFNTLYEEIDTFIKTAASPFSSLWYSFEETLAVFQKENFDKCAPLRELLNSTVKYDLLITETFLTDITLLFVNKFKIPFITSTPNVPFPWLADRMGNPLNPSYIPNLFSDYPFDKMTFFNRLWNTLFYVMALGGHNAIILKNEEKINKYYFGSSVPSLYNIARETSIMLINAHETLNPVIPLVPGMIPVSGIHIKQPAALPQNIEKFINESTHGVVYFCMGSLLRGETFPAEKRDAFLYAFSKIPQRVLWKWEGEVLPGKSENIMTSKWMPQRDILAHPNVKLFISHGGLLGTSEAVYEGVPVIGIPIFGDQRTNIKALEANGAGELLDYNDISGEVVLEKIQRLINDPKYKESARQLSIRYKDRPMSPLDTAVYWTEYVIRHKGAPHLKTAAVDMPWYQYLLLDVIAFLIFILVSVILIIYYGVKISLRYLCALIFGNSSSLKPTKKVKDN | Function: Catalyzes the transfer of a glycosyl group from a UDP-sugar to an acceptor molecule.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 60071
Sequence Length: 526
Subcellular Location: Microsome membrane
EC: 2.4.1.-
|
P34317 | MYLPIFCIFLSVVDSLRILQIVPGFTNSHVLFNYRLAETLRFLGHDVKMWTQMEMAMLDTGNNKLPEGVSEYRIPIHFTDTLKTEGLKVFQSMMFESGDAHDLWWTGQEFKDMRVEACEQMLRHDESVYEDFRKDGFDVAIAHFHDLCPLAIAKKMNVKRVIWITHGTSIYEFSAVQLGLRTIPSTIPHPLSSAGFSQLFLDRVQNTLWHLSLLDFVNLPQNLLVDENLFYREFVGADQDDLWDLAKTTVPSLLINGDRMLDFPRPLPIHIAFSGELGVSKGKKLVMEKWLEDIIEKPSDGLIVFSLGTVSNTTNMPAQMINSFLGAFGKLKTYTILWRMEKSVAGAEKYENLHLVKWLPQKDIMRHPKMKLMIAHGGYNSFLEAAQAGIPAVLMPLFADQKINAKRAQRYGMATVLDKLDLTINNVYGAIKEALKPEYSTNAKKLSAMLSDQVARKPYSALRYSLKLATSPKPSLFTLKSQHLSFLEFHNLDIFSIVLLTAFIVCF | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 57727
Sequence Length: 507
Subcellular Location: Membrane
EC: 2.4.1.17
|
F8WLS6 | MGSLSSSDYSKKPHAVCIPYPAQGHINPMLKLAKLLHYKGFHITFVNTEFNHKRLLKSRGSDSLKGLHSFQFKTIPDGLPPSDVDATQDIPSLCESTTTHCLVPFKQLLQKLNDTSSSEVPPVSCVVSDAVMSFTISAAQELDIPEVLFWTPSACGVLGYMHYAQLIDKGLTPLKDASYFSNGFLDQVLDWIPGMEGIRLRDLPTFLRTTNPDEYMIKFILQETERSKKASAIVLNTFQELESEVIDSLSTLLPPIYPIGPLQILQNQVDDESLKVLGSNLWKEEPECLEWLDTKDPNSVVYVNFGSITVMTNDQLIEFAWGLANSKQNFLWIIRPDLISGESSILGEEFVEETKERGLIASWCHQEQVINHPAIGGFLTHNGWNSTIESISSGVPMICWPFFAEQQTNCRFCCNKWGIGMEINSDVKRDEVESLVKELMVGEKGKEMKKKALEWKNIAEVTTTKPDGSSYSNLEKLIKVLKSKPSH | Function: Iridoid glucosyltransferase acting exclusively on 7-deoxyloganetin. No activity with 7-deoxyloganetic acid.
Catalytic Activity: 7-deoxyloganetin + UDP-alpha-D-glucose = 7-deoxyloganin + H(+) + UDP
Sequence Mass (Da): 54611
Sequence Length: 487
EC: 2.4.1.324
|
F8WKW8 | MFPWLAYGHISPYLELAKRLTDRGFAIYICSTPINLGFIKKRITGKYSVTIKLVELHLPDTPELPPHYHTTNGLPPHLMATLKRALNGAKPELSNILKTLKPDFVIYDATQTWTAALTVAHNIPAVKFLTSSVSMLAYFCHLFMKPGIEFPFPAIYLSDFEQAKARTAAQDARADAEENDPAAERPNRDCDSIFLVKSSRAIEGKYIDYLFDLMKLKMLPVGMLVEEPVKDDQGDNSNELIQWLGTKSQRSTVLVSFGTEYFLTKEEMEEIAHGLELSEVNFIWVVRFAMGQKIRPDEALPEGFLERVGDRGRIVEGWAPQSEVLAHPSTGGFICHCGWNSVVESIEFGVPVIAMPMHLDQPLNARLVVEIGAGMEVVRDETGKFDRKEIARAIKDAMVEKTGENTRAKMLDVKGRVELKEKQELDEVAELLTQLVTETTQSSN | Function: Glucosyltransferase catalyzing the beta 1-6 glucosylation of the sugar moiety of crocetin glucosyl esters to produce crocetin gentiobiosyl esters. Weak activity toward curcumin glucosides, but no activity with flavonoid glucosides, coumarin glucosides, 4-nitrophenyl glucoside or crocetin. Involved with UGT75L6 in sequential glycosylation of crocetin to crocin (bis(beta-D-gentiobiosyl) crocetin).
Catalytic Activity: beta-D-glucosyl crocetin + UDP-alpha-D-glucose = beta-D-gentiobiosyl crocetin + H(+) + UDP
Sequence Mass (Da): 49798
Sequence Length: 444
EC: 2.4.1.330
|
E7CQW6 | MSPSSHKPLILACGLPLSGHIMPVLSLVHGLTDDGYEATVVTGRAFEQKVRDVGADFVPLEGNADFDDHTLDDLVPGRKDMAPSFDRTVQDVEHMMVATLPEQFAAIQRAFKKLSASGRPVVLVSEVLFFGAHPISLGAPGFKPAGWICLGVLPLLIRSDHTLGLDNDRSPEAHAKKLAMNHALEHQIFVKATAKHKEICRELGCTEDPKFIWEHSYIAADKFLQLCPPSLEFSRDHLPSNFKFAGSTPKHRTQFTPPSWWGDVLSAKRVIMVTQGTFAVSYKHLIVPTLEALKDEPDTLTVAILGRRGAKLPDDVVVPENARVIDYFNYDALLPHVDALVYNGGYGGLQHSLSHSVPVVIAGDSEDKPMVASRAEAAGVAIDLKTGLPTVEQIKEAVDSIIGNPKFHEASKKVQMELESHNSLKILEESIEEIASHDFGLLTKSDEETEDIPVKGPALAVSS | Function: Catalyzes the first glycosylation step of sophorolipid biosynthesis, the coupling of glucose to a hydroxylated fatty acid to give rise to a glucolipid . Can glycosylate all hydroxyl fatty acids generated by cytochrome P450 monooxygenases CYP52M1, CYP52N1 and CYP52E3 into their corresponding glucolipids. Main products are 17-O- and 18-O-(beta-D-glucopyranosyl)-octadecenoic acids .
Catalytic Activity: 18-hydroxy-(9Z)-octadecenoate + UDP-alpha-D-glucose = (9Z)-18-hydroxyoctadec-9-enoate 18-O-beta-D-glucoside + H(+) + UDP
Sequence Mass (Da): 50467
Sequence Length: 463
EC: 2.4.1.-
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