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stringlengths 6
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stringlengths 11
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stringlengths 108
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A8FTT1 | MPNMRHRVNSLTEEHEENMQMSKLTGHLSSISTLFPVKNDASQTLTLGQLGLGCPCQLVSLWHYLRKNSPSRAVNIKIFESQFDALADFNLKLASLTSPDPRLPRDDEQSTMVEALLRADIVAIEGCQRLIFDDGRVILDIYLGDTLSQLKCILPTSVKGDMTDNSALIAHWNITEKVKAGSLDQAMLWQIAKLSRDNAALSFTDPESKETRQMMALARSVGLRTLETTVSETTVPETQQQTENKNLDTASDAIPLQERRALRHAQSDKFQYCPVSAANEGDEDCDGEIAIIGGGVASTHLALSLAQRNKKVRIFCSDANFAQQASGNKQGAVYPLLTPDNGHLSHYFQQGYLFTRRRLQALVDDKFAVSYDFCGVLQTGFDDRSSARLDKIINGQSWNEKMAYPIDAASATQIAGIDIDKAGIYYPLGGWICPHEFTRAAFDKAARLSDVSVEFNADITRIEQREGLWYLYKSVNVQHSCTDSHTPDDSEELEIGPFANLVLANGQGLTQFKQSEKLPATGFRGQVSHIPSRNALTKLSTVLCSHGYLTPGNNNFHCTGASYVKNPTNLDYCATEQVENLHKIRHSYVDKPWTEDVDITGHSARVGVRMVTRDHAPMMGCAPDTDSMLAQYEQHQHTKESIKFWKETPAPTHKGLFILGGLGSRGLTSGPLAAEALAAQLCGEVIPLSMPMLEMLNPNRFWMRKLIKGKAL | Function: Catalyzes the last two steps in the biosynthesis of 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at the wobble position (U34) in tRNA. Catalyzes the FAD-dependent demodification of cmnm(5)s(2)U34 to nm(5)s(2)U34, followed by the transfer of a methyl group from S-adenosyl-L-methionine to nm(5)s(2)U34, to form mnm(5)s(2)U34.
Catalytic Activity: 5-aminomethyl-2-thiouridine(34) in tRNA + S-adenosyl-L-methionine = 5-methylaminomethyl-2-thiouridine(34) in tRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 78823
Sequence Length: 712
Subcellular Location: Cytoplasm
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A9WKE3 | MNDTIAAIATPPGEGGIGIIRLSGPDAQSIALRIFRPVRPGRLRSHRVRYGHVIGPDGEVIDEALLTLMAAPHSFTREDVVEISCHGGALPVQLTLEAALAAGARLANPGEFTLRAFLNGRIDLSQAEATLDVIRAQTSAGLAIAQAQLGGWLAREVRAARTAILEPLAYITALIDFPEEGIEPQTVAGPIEQALATVERLLAGADQGMVLRNGARVVLVGRPNVGKSSLLNALLRVERAIVTPIPGTTRDTLEEMANLAGVPVVLIDTAGMRTSTDPVEQIGVERAAAALAGADLALLVFDSSQPFTPEDEAMLVATADRPTIIVWNKCDDPDVPPPPAPPHPKAMAVVACSARYGHGIDTLAKTIATTLLGGTLPAVGATHLVSNPRHRAALRRAAEFLRAAQETLAAGAATDLLAADLTGAANALGEITGETVGEDLLDMIFSRFCIGK | Cofactor: Binds 1 potassium ion per subunit.
Function: Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Sequence Mass (Da): 47166
Sequence Length: 452
Subcellular Location: Cytoplasm
EC: 3.6.-.-
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Q9Z768 | MLKHDTIAAIATPPGEGSIAVVRLSGPQAIVIADRIFSGSVASFASHTIHLGQVIFEETLIDQALLLLMRSPRSFTGEDVVEFQCHGGFFACSQILDALIALGARPALPGEFSQRAFLNGKIDLVQAEAIQNLIVAENIDAFRIAQTHFQGNFSKKIQEIHTLIIEALAFLEVLADFPEEEQPDLLVPQEKIQNALHIVEDFISSFDEGQRLAQGTSLILAGKPNVGKSSLLNALLQKNRAIVTHIPGTTRDILEEQWLLQGKRIRLLDTAGQRTTDNDIEKEGIERALSAMEEADGILWVIDATQPLEDLPKILFTKPSFLLWNKADLTPPPFLDTSLPQFAISAKTGEGLTQVKQALIQWMQKQEAGKTSKVFLVSSRHHMILQEVARCLKEAQQNLYLQPPEIIALELREALHSIGMLSGKEVTESILGEIFSKFCIGK | Cofactor: Binds 1 potassium ion per subunit.
Function: Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Sequence Mass (Da): 48715
Sequence Length: 442
Subcellular Location: Cytoplasm
EC: 3.6.-.-
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Q8KAS1 | MSPSDLHLPVPGHPIAAIATPVGVGALAIVRISGAGVLDLADRVFRKVHGSGKLAEAAGYTAHFGRLYDGEEMVDEVIALVFRAPRSFTAEQMVEFTCHGGPVVVGRVLRLMLDNGCRLAEPGEFTRRAFLNGRIDLLQAEAIGEMIHARTESAYRTAVSQMKGDLSVRLGGLREQLIRSCALIELELDFSEEDVEFQSRDELTMQIETLRSEVNRLIDSYQHGRIVSEGVSTVIAGKPNAGKSTLLNTLLGQERAIVSHMPGTTRDYIEECFIHDKTMFRLTDTAGLREAGEEIEHEGIRRSRMKMAEADLILYLLDLGTERLDDELTEIRELKAAHPAAKFLTVANKLDRAANADALIRAIADGTGTEVIGISALNGDGIDTLKQHMGDLVKNLDKLHEASVLVTSLRHYEALRNASDALQNALELIAHESETELIAFELRAALDYVGQITGKVVNEEVLNTIFDKFCIGK | Cofactor: Binds 1 potassium ion per subunit.
Function: Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Sequence Mass (Da): 51817
Sequence Length: 473
Subcellular Location: Cytoplasm
EC: 3.6.-.-
|
A0M2N6 | MKLNDTIVALATPSGAGAIAIIRVSGPDALEIVAPLFKAKSKKDLAKQPTHTLHLGNVMDGERTIDEVLASVFRAPKSYTGEETVELSCHGSPYIQQEIIQLLIRKSCRSAEAGEFTLRAFLNAKMDLSQAEAVADLINSENAASHQMAMQQMRGGFSNEIQKLREELLNFASLIELELDFAEEDVEFANRDQFKDLVSKIQTVLKRLLDSFATGNVLKNGIPVAIVGEPNVGKSTLLNALLNEERAIVSEIAGTTRDTIEDEMSIGGVGFRFIDTAGIRETKDVVESIGIKKTFEKISQAQVVVYLVDSSQIAVNRERLQQVRIEIEKIKNKFPQKPLLIIANKTDRLADEEIHNLKTKLEEISSHAERAQFLLLSAKTNLGVEELKEKLLEYVNTGALRNSDTIVTNSRHYAALLKALEEINKVEEGLNADLSGDLLAIDIRQALHHFGEITGEITNDDLLGNIFANFCIGK | Cofactor: Binds 1 potassium ion per subunit.
Function: Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Sequence Mass (Da): 52259
Sequence Length: 474
Subcellular Location: Cytoplasm
EC: 3.6.-.-
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Q1QS99 | MTATPLYRQDTIAAIATPPGRGGVGIIRLSGPASRDLAERILGHCPAPRHAHYGPFYDADAQVLDEGIALFFPGPHSFTGEDVLELQGHGGPVIMDLLLARCVALGARLARPGEFSERAFLNDKLDLAQAEAIADLIDASSRAAAENALRSLQGEFSTRVSALVDKLIELRMFVEAAIDFPEEEIDFLADGKVAAMLQGAQETLGEVRAAAGQGALMREGMNVVIAGRPNAGKSSLLNALTERDSAIVTDIEGTTRDVLREYIHIDGMPLHVIDTAGLRDTPDAIEKIGVARAWEEIEKADRVLLLVDATTTTQTDPMQLWPEFVARLPHPERLTLVRNKIDESGETEQSDLSTSPPIVRLSAKTGLGVDNLKEHLKAVMGFDATTEGRFSARRRHLDALDRAGDALDNGIAQLRGHGAGELLAEDLRDAQQALSEITGEFTADDLLGEIFGSFCIGK | Cofactor: Binds 1 potassium ion per subunit.
Function: Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Sequence Mass (Da): 49247
Sequence Length: 458
Subcellular Location: Cytoplasm
EC: 3.6.-.-
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A9KLX9 | MKTDTIAAIATGLSNAGISIVRISGDQAFAVIDKIFQTKSKAKRLSEMDSHTVHYGYIVDEEEIIDEVMVIIMRAPRSYTMEDSIEIDCHGGITVTKKVLEAVLKAGARIAEPGEFTKRAFLNGRIDLSQAEAVIDVIHANNELALKNSMKQLKGNVLHKVKDVRHSIILDTAYIEAALDDPEHISLEGFSDKLRDNVIGSIKELSELINTSENGRMIKEGIRTVILGRPNAGKSSLLNLMVGEERAIVTEIAGTTRDTIEETVFLNGLCLNLIDTAGIRETSDLVEKLGVEKSLKSAKEADLIICVIDASTPLNQDDKEILEFIKDRKAIVLLNKSDLDSVIEEEKINLLTNKPILKISAIDQTGIKDLEQTITEMFFEGNISFNDEIYITNMRHKNALVEAKVSLEQVIVSIENEMPEDFFSIDLMNAYEILGTIIGESVDEDLVNTIFKEFCMGK | Cofactor: Binds 1 potassium ion per subunit.
Function: Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Sequence Mass (Da): 50743
Sequence Length: 458
Subcellular Location: Cytoplasm
EC: 3.6.-.-
|
Q1MPF1 | MCDTIAAIATPSGTGGIGIIRISGPKSKERLTELFHSVSPKFTDFKPWMLHRGYLVAPTNEFLDDILAVYMPAPYTFTGEDVVELHCHGGHFLLLTILETVLCKNIRLAKPGEFSQRAFLNGRMDLTQAEAVAELIAASSRNEVLLASNRLKGLLGQKIIDIRRRIEELRVWICLAVDFPEEESGIFPLEKFINGLLEIHEIIQKLIHAAERSRCWKEGVTVALAGAVNAGKSSLLNALLGKERAIVTEHPGTTRDFLEECIIVNSLSIRLIDTAGLRVTSDPIEEQGIQKGREKIDEADVILFIIDGTVGVTEESKLLINNFGVERTILVWNKVDLKVPPSNWTELYTSSQVSGICVSAKTGSGIEELLVLLYNFVLSQHNAQEPTFDTIVPNMRQVEVFSLVLEEIRSLYEDIRSGIPYDLCAVMLENISSMLNSIIGFDTPEEVLNRIFASFCIGK | Cofactor: Binds 1 potassium ion per subunit.
Function: Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Sequence Mass (Da): 50924
Sequence Length: 459
Subcellular Location: Cytoplasm
EC: 3.6.-.-
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Q49UI4 | MDLDTITSISTPMGEGAIGIVRLSGVDAVDIADKLYKGKERLEDVTSHTINYGHIIDPESNEVVEEVMVSVLRAPKTFTREDIVEINCHGGILTINRILELTMTYGARMADPGEYTKRAFLNGRIDLSQAEAVMDFIRSKTDRASKVAMNQIEGRLSDMIKRQRQSILEILAQVEVNIDYPEYDDVEDATTEVLLGKSNEIKTEINKLLDTGTQGKIMREGLSTVIVGKPNVGKSSMLNNLIQDNKAIVTEVPGTTRDTLEEYVNVRGVPLRLVDTAGIRDTEDIVERIGVERSRKALGEADLILFVLNYNERLTDEDRKLYEVIKNEDAIVIVNKMDLDKHLDLDEVKDMIGDMPLIQTSMLKQEGIDQLEIQIRDLFFGGDVQNQDMTYVSNSRHISLLKQARNTIQDAIDAAESGVPMDMVQIDLTRTWEILGEIIGESASDELIDQLFSQFCLGK | Cofactor: Binds 1 potassium ion per subunit.
Function: Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Sequence Mass (Da): 51382
Sequence Length: 459
Subcellular Location: Cytoplasm
EC: 3.6.-.-
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P53163 | MSLRILAKRSSSIWMKTRVTPALISPITITTRFNSTTTTAPSHKDDVRPVDPKISKIVQDISQLTLLETSSLINELKTVLNIPEISMPMGGFMAGAAGAGAGNVPSSTGEAGSGAEEEAKPEAKTVFTVKLDSFDTKTKAKVIKEVKGLLGLSLVEAKKFVEAAPKVLKENVAKDDAEKIKKTLEDLGAKVSLE | Function: Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane.
PTM: N-glycosylated.
Sequence Mass (Da): 20650
Sequence Length: 194
Subcellular Location: Mitochondrion
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B2X050 | MAEKTTSTRYAVVTGGNKGIGYETCRQLASKGVVVVLTSRDEKKGIEAIERLKEESNFTDEHILFHQLDIMDPASISSLVNLIKTKFGRLDILINNAGISGVMVEGDVQVLKEILERYISIVFTEDENGEEGGWTKSGPGSVTNYELTKECIETNYYGAKRMTEAFIPLLQLSNSPRIVNVASSMGKLKLLCNKWAIEVLRDADSLTEEKVDQVVNEFLKDFTEKSTESKGWPSYFTAYKVSKASLIAYTRVLATKYPNFRINSVCPGYCKTDVNANTGSLTAGEGAESLVNLALLPNDGPSGLFFYRKEVTFF | Function: Involved in basal resistance against pathogens.
Catalytic Activity: (+)-neomenthol + NADP(+) = (1R,4S)-menthone + H(+) + NADPH
Sequence Mass (Da): 34758
Sequence Length: 314
EC: 1.1.1.208
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Q2ULB2 | MHFSSLSLPLTALSLVTPSLAYPQFKFEQRVARSNSSESRANAVKEAFVHAWDGYMQYAYPHDELHPISNGVGDSRNGWGASAVDALSTAVIMGNETIVNQILDHIATIDYSKTDDQVSLFETTIRYLGGMLSGYDLLKGPASNLVKDQAKVKTLLDQSQNLADVLKFAFDTPSGIPYNNINITSHGNDGATTNGLAVTGTLVLEWTRLSDLTGDTEYAQLSQKAEDYLLNPSPKSAEPFEGLVGSHINISNGAFADGQVSWNGGDDSFYEYLIKMYVYDPKRFSTYGDRWVKAAESSIKHLASHPEKRPDLTFLASYNDGQYGLSSQHLTCFDGGSFLLGGTVLDRDDFIQFGLDLVKGCHETYNQTLTGIGPESFGWDPKNVPSDQKELYERAGFYISSGAYILRPEVIESFYYAWRITGQEIYREWVWNAFVNINKYCRTDSGFAGLTNVNAANGGGRYDNQESFLFAEVLKYVYLTFAPDNEWQVQRGKGNKFVYNTEAHPVRVAA | Cofactor: Ca(2+). Can also use Mg(2+), but with lower efficiency.
Function: Involved in the maturation of Asn-linked oligosaccharides. Progressively trims alpha-1,2-linked mannose residues from Man(9)GlcNAc(2) to produce Man(5)GlcNAc(2).
Catalytic Activity: 4 H2O + N(4)-(alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 9A1,2,3B1,2,3) = 4 beta-D-mannose + N(4)-(alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 5A1,2)
Sequence Mass (Da): 56631
Sequence Length: 510
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Cytoplasmic vesicle lumen
EC: 3.2.1.113
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Q12563 | MHLPSLSLSLTALAIASPSAAYPHFGSSQPVLHSSSDTTQSRADAIKAAFSHAWDGYLQYAFPHDELHPVSNGYGDSRNGWGASAVDALSTAVIMRNATIVNQILDHVGKIDYSKTNTTVSLFETTIRYLGGMLSGYDLLKGPVSDLVQNSSKIDVLLTQSKNLADVLKFAFDTPSGVPYNNLNITSGGNDGAKTNGLAVTGTLALEWTRLSDLTGDTTYADLSQKAESYLLNPQPKSAEPFPGLVGSNINISNGQFTDAQVSWNGGDDSYYEYLIKMYVYDPKRFGLYKDRWVAAAQSTMQHLASHPSSRPDLTFLASYNNGTLGLSSQHLTCFDGGSFLLGGTVLNRTDFINFGLDLVSGCHDTYNSTLTGIGPESFSWDTSDIPSSQQSLYEKAGFYITSGAYILRPEVIESFYYAWRVTGQETYRDWIWSAFSAVNDYCRTSSGFSGLTDVNAANGGSRYDNQESFLFAEVMKYSYMAFAEDAAWQVQPGSGNQFVFNTEAHPVRVSST | Cofactor: Ca(2+). Can also use Mg(2+), but with lower efficiency.
Function: Involved in the maturation of Asn-linked oligosaccharides. Progressively trims alpha-1,2-linked mannose residues from Man(9)GlcNAc(2) to produce Man(5)GlcNAc(2).
Catalytic Activity: 4 H2O + N(4)-(alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 9A1,2,3B1,2,3) = 4 beta-D-mannose + N(4)-(alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 5A1,2)
Sequence Mass (Da): 55875
Sequence Length: 513
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Cytoplasmic vesicle lumen
EC: 3.2.1.113
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E9CXX8 | MKGSPVLAVCAAALTLIPSVVALPMIDKDLPSSISQSSDKTSQERAEAVKAAFRFAWEGYLEHAFPNDELHPVSNTPGNSRNGWGASAVDALSTAIIMDMPDVVEKILDHISNIDYSQTDTMCSLFETTIRYLGGMISAYDLLKGPGSHLVSDPAKVDVLLAQSLKLADVLKFAFDTKTGIPANELNITDKSTDGSTTNGLATTGTLVLEWTRLSDITGDPEYGRLAQKGESYLLNPQPSSSEPFPGLVGRTIDIETGLFRDDYVSWGGGSDSFYEYLIKMYVYDKGRFGKYKDRWVTAAESTIEHLKSSPSTRKDLTFVATYSGGRLGLNSGHLTCFDGGNFLLGGQILNRDDFTKFGLELVEGCYATYAATATKIGPEGFGWDATKVPEAQAEFYKEAGFYITTSYYNLRPEVIESIYYAYRMTKDPKYQEWAWDAFVAINATTRTSTGFTAIGDVNTPDGGRKYDNQESFLFAEVMKYSYLIHSPEADWQVAGPGGTNAYVFNTEAHPVKVFSRGC | Cofactor: Ca(2+). Can also use Mg(2+), but with lower efficiency.
Function: Alpha-mannosidase involved in the maturation of Asn-linked oligosaccharides. Progressively trims alpha-1,2-linked mannose residues from Man(9)GlcNAc(2) to produce Man(5)GlcNAc(2).
Catalytic Activity: 4 H2O + N(4)-(alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 9A1,2,3B1,2,3) = 4 beta-D-mannose + N(4)-(alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 5A1,2)
Sequence Mass (Da): 56874
Sequence Length: 519
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Secreted
EC: 3.2.1.113
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Q5BF93 | MRTLLALAALAGFAAARVPAYAITRPVMRSDSRADAVKEAFSHAWDGYYNYAFPHDELHPISNGYGDSRNHWGASAVDALSTAIMMRNATIVNQILDHIAAVDYSKTNAMVSLFETTIRYLAGMISGYDLLKGPAAGLVDDSRVDVLLEQSQNLAEVLKFAFDTPSGVPYNMINITSGGNDGATTNGLAVTGTLVLEWTRLSDLTGNDEYARLSQRAEDYLLHPEPAQYEPFPGLIGSAVNIADGKLANGHISWNGGADSYYEYLIKMYVYDPERFGLYRDRWVAAAESSINHLASHPSTRPDVTFLATYNEEHQLGLTSQHLTCFDGGSFLLGGTLLDRQDFVDFGLDLVAGCHETYNSTLTGIGPEQFSWDPNGVPDSQKELFERAGFYINSGQYILRPEVIESFYYAWRVTGDGTYREWVWNAFTNINKYCRTATGFAGLENVNAANGGGRIDNQESFMFAEVLKYSFLTFAPEDDWQVQKGSGNTFVYNTEAHPFKVYTPQ | Cofactor: Ca(2+). Can also use Mg(2+), but with lower efficiency.
Function: Involved in the maturation of Asn-linked oligosaccharides. Progressively trims alpha-1,2-linked mannose residues from Man(9)GlcNAc(2) to produce Man(5)GlcNAc(2).
Catalytic Activity: 4 H2O + N(4)-(alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 9A1,2,3B1,2,3) = 4 beta-D-mannose + N(4)-(alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 5A1,2)
Sequence Mass (Da): 55881
Sequence Length: 505
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Cytoplasmic vesicle lumen
EC: 3.2.1.113
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Q50103 | MFVNLTCLSEGNGSRGKALAESTQAELKTSWYLLGPAFVAAIAYVDPGNVAANVSSGAQFGYLQLWVVVVANVLAGLVQYLSAKLGLVTGQSLPQAISKQMSHPFRLGFWLQAELVAMATDVAEIVGGAIAFHILFRVSLLLGGVITGTVSLLLLMVKDRRGQLLFERVITGLLFVIVVGFTSSFFVATPSPEDMVNGLLPRFQGTESVLLAAAIIGATVMPHAVYLHSGLALDRHGHPHAGRSRRRLLRVTRLDVILAMTIAGIVNTAMLLVAAINLQHHQVTAYIEGTYTAIQDTLGATIAMLFAIGLLASSLASASVGAYAGALIMQGLLQRSIPMLIRRLITLCPAIAILALGFDPTRALVLSQIVLSFGIPFAVLPLVKLTNNRGLMGNDTNHPATTVLGWAVAILVSLLNVVLIYLTVTS | Function: H(+)-stimulated, divalent metal cation uptake system.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 45137
Sequence Length: 426
Subcellular Location: Cell membrane
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P9WIZ4 | MAGEFRLLSHLCSRGSKVGELAQDTRTSLKTSWYLLGPAFVAAIAYVDPGNVAANVSSGAQFGYLLLWVIVAANVMAALVQYLSAKLGLVTGRSLPEAIGKRMGRPARLAYWAQAEIVAMATDVAEVIGGAIALRIMFNLPLPIGGIITGVVSLLLLTIQDRRGQRLFERVITALLLVIAIGFTASFFVVTPPPNAVLGGLAPRFQGTESVLLAAAIMGATVMPHAVYLHSGLARDRHGHPDPGPQRRRLLRVTRWDVGLAMLIAGGVNAAMLLVAALNMRGRGDTASIEGAYHAVHDTLGATIAVLFAVGLLASGLASSSVGAYAGAMIMQGLLHWSVPMLVRRLITLGPALAILTLGFDPTRTLVLSQVVLSFGIPFAVLPLVKLTGSPAVMGGDTNHRATTWVGWVVAVMVSLLNVMLIYLTVTG | Function: H(+)-stimulated, divalent metal cation uptake system. Transports zinc and iron. Can also interact with manganese and copper (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 45004
Sequence Length: 428
Subcellular Location: Cell membrane
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Q9PB87 | MSPITILLIGIAMSTDAFAAAIGKGAAIGKPRLRDALYVAVIFGVIETATPIAGWLLGQIASHYIATFDHWIAFGLLSGLGIHMIVNGLKNNGNTCKDNADTHNRNSRWLPLAATALATSIDAAAIGISLAFLDIHISIVAAVIGLCTFTMVIFGVMLGRVLGTFVGNRAEIVGGIILIIVGSTILYEHLSNNG | Function: Probably functions as a manganese efflux pump.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 20252
Sequence Length: 194
Subcellular Location: Cell inner membrane
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A1JM85 | MNLSATLVLAFAMSMDAFAASIGKGASLHKPRFREAIRTGLIFGVIEAITPLIGWCIGLFASQYILEWDHWIAFSLLFILGCRMIFEGAKQQVEETEKMRSHSFWVLVMTAIATSLDAMAIGVGLAFLQVNIVHTAMAIGLATMIMATLGMLIGRYIGPLLGKRAEIIGGIVLIGIGFNILYEHIYRLA | Function: Probably functions as a manganese efflux pump.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 20650
Sequence Length: 189
Subcellular Location: Cell inner membrane
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Q747W9 | MELIDSFGRRINYLRLSVTDRCNLRCSYCMPAEGVEKLAHGDILSYEDLFRIARAAVAIGIEKIRITGGEPLVRKGIVPFLARIAAIEGLRQLVLTTNGLLLPEMAADLRSAGVQRLNISLDSLRADTFRAITRIGELQRVLDGIAAADAAGFPPPKINMVVMRGVNDGEVADFARLTIDRPCTVRFIEYMPATRENNWQSLTVPGREILDRISASYELEPVEKGACAGPSRDFRIRGAAGTLGVITAVSGHFCGDCNRVRVTSTGMAKSCLFSDEGFDLRPFLETSDPIILQEALRRIVGVKPERHGMSACKAEHQAFSMAKIGG | Cofactor: Binds 2 [4Fe-4S] clusters. Binds 1 [4Fe-4S] cluster coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine and 1 [4Fe-4S] cluster coordinated with 3 cysteines and the GTP-derived substrate.
Function: Catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate.
Catalytic Activity: AH2 + GTP + S-adenosyl-L-methionine = (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate + 5'-deoxyadenosine + A + H(+) + L-methionine
Sequence Mass (Da): 35621
Sequence Length: 326
Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
EC: 4.1.99.22
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Q8UER6 | MSDGQKLTHIDASGEAHMVDVGDKAETVRVAVAEGFVKMKPETLALIRDGNAKKGDVIGTARLAGIMAAKQTANLIPLCHPLMLTKVAVDITEDTGLPGLRVEAMVKLSGKTGVEMEALTAVSIACLTIYDMAKAADKGMEIVNIRLLEKSGGKSGDFRRQES | Function: Catalyzes the conversion of (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP).
Catalytic Activity: (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate = cyclic pyranopterin phosphate + diphosphate
Sequence Mass (Da): 17236
Sequence Length: 163
Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
EC: 4.6.1.17
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Q21R65 | MNALTHFDAQGQAHMVDVAGKAATHRIGIAGGRIEMLPSTLAIIEAGTAKKGDVLGIARIAGIMAAKKTSELIPLCHPLALTRVAIDFETDQADETRASSIFCTATVETVGATGVEMEALTAVQVALLTIYDMCKAVDRGMVMTGIKLLEKHGGKSGSFVNGT | Function: Catalyzes the conversion of (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP).
Catalytic Activity: (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate = cyclic pyranopterin phosphate + diphosphate
Sequence Mass (Da): 16968
Sequence Length: 163
Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
EC: 4.6.1.17
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Q0VQ23 | MTEQRFTHLDDSGRAQMVDVTDKDITQRAATAQARVRMQPSTLQMILAGEHPKGDVLATARIAGIQAAKKTWDLIPLCHPLLLTGITVTIEPEADDALCVQATCKLKGTTGVEMEALTAASVACLTLYDMCKAVDRCMVIESVCLLEKSGGRSGTFRRER | Function: Catalyzes the conversion of (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP).
Catalytic Activity: (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate = cyclic pyranopterin phosphate + diphosphate
Sequence Mass (Da): 17364
Sequence Length: 160
Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
EC: 4.6.1.17
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A8EX06 | MELTHLDDKNRPKMVDVSSKSETKRVAVASGEIKMSKEAYQAIISNNTKKGPVLQTAVIAAILGTKKTHELIPMCHPLLLTGIDCDIEEIPQNNTFKLYVTARLNGQTGVEMEALTGVSIGLLTIYDMVKAIDKSMIISNVQLESKSGGKSGDFKR | Function: Catalyzes the conversion of (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP).
Catalytic Activity: (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate = cyclic pyranopterin phosphate + diphosphate
Sequence Mass (Da): 17006
Sequence Length: 156
Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
EC: 4.6.1.17
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O66810 | MRTVDITTKIETLREAKAYGRIRLKPETVKLIKENKVPKGNLVEATKLSGIFGAKKTGELLPFCHPIPLDFVALEVKVNEDNLEVFSTVRGIARTGYEMEALTAVTTALLNVYDMCKALDDSMVIEEVKLLEKSGGKSDWFRRLDGVKVNLHAENEGLRKIAEDYLKELGATFAEEAELYISIGDNLPINKEIRSLERVISLYDFRRNPKEVGKEIRVGWSDDALIIILPESEEKIRFFFETFGGIIGNLLCRR | Function: Catalyzes the conversion of (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP).
Catalytic Activity: (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate = cyclic pyranopterin phosphate + diphosphate
Sequence Mass (Da): 28737
Sequence Length: 254
Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
EC: 4.6.1.17
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O28132 | MELTHIEDGKVRMVDVSHKDDVDRIAVAEGYIRLRSSTIEAIINKEVAKGNVIAAANIAGVMAVKKTPELIPMCHPIPITSVKFDFDIESVGIRVKCTVKSKGKTGVEMEALTGVSVALLTIWDMVKSLEKDERGNYPKTLIEVIRVVEKVKGGKE | Function: Catalyzes the conversion of (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP).
Catalytic Activity: (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate = cyclic pyranopterin phosphate + diphosphate
Sequence Mass (Da): 17101
Sequence Length: 156
Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
EC: 4.6.1.17
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P26944 | MTDQPLAGFTHFDAEGRAVMVDVSGKADTERSATARGSVLMQPETLALILQGGVKKGDVLSVARLAGIMGAKRTPDLIPLCHPLMLTSVKVD | Function: Catalyzes the conversion of (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP).
Catalytic Activity: (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate = cyclic pyranopterin phosphate + diphosphate
Sequence Mass (Da): 9674
Sequence Length: 92
Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
EC: 4.6.1.17
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C1DPC3 | MLTHLDSRGHAHMVDVTDKASTAREAEAEAWVRMRPETLELIQKGGHPKGDVFAVARIAGIMAAKKTHELIPLCHPLLLTGIKVELSAEGEDRVRIVARCKLAGQTGVEMEALTAASVAALTLYDMCKAVDRGLLIEQVRLLEKKGGKSGHYQAGQAM | Function: Catalyzes the conversion of (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP).
Catalytic Activity: (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate = cyclic pyranopterin phosphate + diphosphate
Sequence Mass (Da): 17077
Sequence Length: 158
Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
EC: 4.6.1.17
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Q749N8 | MSFNHFDDQGRAIMVDVSGKQPTLRTATAAATVSMQPDTLADLLAGRTTKGDVLGVARIAGIAAAKKTPELIPLSHPLAIHHAAIDFDTDQACGTVTVRATVRAFERTGVEMEAMTSAAVAALTIYDMCKGADKGITIGQIRLLFKEGGKSGTWQREEGQ | Function: Catalyzes the conversion of (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP).
Catalytic Activity: (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate = cyclic pyranopterin phosphate + diphosphate
Sequence Mass (Da): 16913
Sequence Length: 160
Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
EC: 4.6.1.17
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C5D4E6 | MSSFTHFNEQGRAKMVDITEKEDTIRVAVAQTSVTVNKEIYEKMTNRMIEKGDVLAVAQVAGIMAAKKTSDLIPMCHPLMLKGVDIQFAWHVEEEKALYQLLITVTVKTKGSTGVEMEALTAASVCALTVYDMCKALDKGMVIGPTYLVEKSGGKSGHYQRENSSVGGFANEQ | Function: Catalyzes the conversion of (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP).
Catalytic Activity: (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate = cyclic pyranopterin phosphate + diphosphate
Sequence Mass (Da): 18911
Sequence Length: 173
Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
EC: 4.6.1.17
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Q8XZR3 | MPTIRVQEADFDLGAEIAALRAGRPQIGAVASFIGTVRDINDGSGVSEMELEHYPGMTEKALANIVDAAMQRWDLIDALVIHRVGKLRPEDQIVLVAVASGHRGEAFAACEFIMDYLKSEAPFWKKEQTAQGARWVDARVTDERALARWGIVTDNASAATAQAASANDQNQKDRDA | Function: Converts molybdopterin precursor Z into molybdopterin. This requires the incorporation of two sulfur atoms into precursor Z to generate a dithiolene group. The sulfur is provided by MoaD (By similarity).
Catalytic Activity: 2 [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-NH-CH2-C(O)SH + cyclic pyranopterin phosphate + H2O = 2 [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly + 4 H(+) + molybdopterin
Sequence Mass (Da): 19151
Sequence Length: 176
Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
EC: 2.8.1.12
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Q984P0 | MSAVLAPTVRIQRQDFDVAAEIAALTQGRADVGAVVSFSGLCRDEQGALSALELEHYPGMAEAEIGRIAAEAVERWPLQGLTVIHRHGKIRPGENIVLVVAASAHRQAAFEAANFLMDYLKSRAPFWKKEHRTDGSEGGWVEAKETDTQAAKRWKSSSE | Function: Converts molybdopterin precursor Z into molybdopterin. This requires the incorporation of two sulfur atoms into precursor Z to generate a dithiolene group. The sulfur is provided by MoaD (By similarity).
Catalytic Activity: 2 [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-NH-CH2-C(O)SH + cyclic pyranopterin phosphate + H2O = 2 [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly + 4 H(+) + molybdopterin
Sequence Mass (Da): 17369
Sequence Length: 159
Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
EC: 2.8.1.12
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P65399 | MHETRIVVGPAPFSVGEEYSWLAARDEDGAVVTFTGKVRNHNLGDSVKALTLEHYPGMTEKALAEIVAKARSRWPLGRVTVIHRVGELWPGDEIVFVGVTSAHRSSAFDAGQFIMDYLKTRAPFWKREATPEGDRWVEARDSDQQLAKRW | Function: Converts molybdopterin precursor Z into molybdopterin. This requires the incorporation of two sulfur atoms into precursor Z to generate a dithiolene group. The sulfur is provided by MoaD (By similarity).
Catalytic Activity: 2 [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-NH-CH2-C(O)SH + cyclic pyranopterin phosphate + H2O = 2 [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly + 4 H(+) + molybdopterin
Sequence Mass (Da): 16892
Sequence Length: 150
Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
EC: 2.8.1.12
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Q9ZIM9 | MKQFEIVTEPIQTEQHRDFTLNPHQGAVVVFTGHVREWTKGIRTEHLEYEAYIPMAEKKLAQIGDEINEQWPGTIVSIVHRIGPLKISDIAVLIAVSSPHRKDAYAANEYAIDRIKEVVPIWKKEIWEDGAEWIGHQRGYHDDAVERGQN | Function: Converts molybdopterin precursor Z into molybdopterin. This requires the incorporation of two sulfur atoms into precursor Z to generate a dithiolene group. The sulfur is provided by MoaD (By similarity).
Catalytic Activity: 2 [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-NH-CH2-C(O)SH + cyclic pyranopterin phosphate + H2O = 2 [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly + 4 H(+) + molybdopterin
Sequence Mass (Da): 17276
Sequence Length: 150
Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
EC: 2.8.1.12
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Q5HLX8 | MKQFEIVTQPIETEQYRDFTINERQGAVVVFTGHVREWTKGIRTQHLEYEAYIPMAEKKLAQIGKEIEEKWPGTITTIVHRIGPLQISDIAVLIAVSSPHRKAAYAANEYAIERIKEIVPIWKKEIWEDGAEWQGHQKGTYNEAKKGKAR | Function: Converts molybdopterin precursor Z into molybdopterin. This requires the incorporation of two sulfur atoms into precursor Z to generate a dithiolene group. The sulfur is provided by MoaD (By similarity).
Catalytic Activity: 2 [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-NH-CH2-C(O)SH + cyclic pyranopterin phosphate + H2O = 2 [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly + 4 H(+) + molybdopterin
Sequence Mass (Da): 17329
Sequence Length: 150
Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
EC: 2.8.1.12
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Q56210 | MPDLLTCDRHQIELSLAPIPLSAAAEFCHDDRYGAFASFVGWVRRVNVGRLVTGITYQSFQPLCRTVLTEICQEAEQVFGQELRIYVQHRLGETRVGDPTVLIGVGAIHRDEACEACRYVIEELKHRAPIWKLEHYEDGDSGWVPGNCLCQERRSRDRRGSTGPE | Function: Converts molybdopterin precursor Z into molybdopterin. This requires the incorporation of two sulfur atoms into precursor Z to generate a dithiolene group. The sulfur is provided by MoaD (By similarity).
Catalytic Activity: 2 [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-NH-CH2-C(O)SH + cyclic pyranopterin phosphate + H2O = 2 [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly + 4 H(+) + molybdopterin
Sequence Mass (Da): 18712
Sequence Length: 165
Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
EC: 2.8.1.12
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Q97CL5 | MINTYVEITEKDINPLDLINRVRRPDAGAIVTFEGTVRNDSDGVRVTALYYEAYKEMAEMQIADLIDEAKKKYNILDAAVCHRIGLVGLTEDSVVISVSSAHRSSAFEACRYIIDTIKERVPIWKRDILENGNGSWH | Function: Converts molybdopterin precursor Z into molybdopterin. This requires the incorporation of two sulfur atoms into precursor Z to generate a dithiolene group. The sulfur is provided by MoaD (By similarity).
Catalytic Activity: 2 [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-NH-CH2-C(O)SH + cyclic pyranopterin phosphate + H2O = 2 [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly + 4 H(+) + molybdopterin
Sequence Mass (Da): 15488
Sequence Length: 137
Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
EC: 2.8.1.12
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Q9KT77 | MDHRVSVQKEDFSVAQEYEALAQGSQAGAVVTFVGKVRDMNLGDNVVGLHLEHYPGMTEKSLLEICDMAQERWPLQRVRVIHRIGDMLSGDQIVLVGVSSAHRNAAFAACEFIMDYLKTRAPFWKKELTTEASRWIDSRDSDHQAAQRWE | Function: Converts molybdopterin precursor Z into molybdopterin. This requires the incorporation of two sulfur atoms into precursor Z to generate a dithiolene group. The sulfur is provided by MoaD (By similarity).
Catalytic Activity: 2 [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-NH-CH2-C(O)SH + cyclic pyranopterin phosphate + H2O = 2 [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly + 4 H(+) + molybdopterin
Sequence Mass (Da): 17032
Sequence Length: 150
Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
EC: 2.8.1.12
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Q98MK2 | MRRDIAGIVLAGGQSRRMGGGDKSLLPLGSGSVLDQILSRFGPQIEILALSANGDPERFSRFGLPVLADTVEGFAGPLAGILTGLEWAIAGTPCKAVVTAAGDTPFLPLDLVDRLAAAARDHPGSIAVASSAGRRHPTFALWPTECRDALRHFLVDEDNRRVSDFIERHGHVEVEFRFVQSAGLDPFFNINVPDDLAQAARLLQSMTS | Function: Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor.
Catalytic Activity: GTP + H(+) + Mo-molybdopterin = diphosphate + Mo-molybdopterin guanine dinucleotide
Sequence Mass (Da): 22239
Sequence Length: 208
Domain: The N-terminal domain determines nucleotide recognition and specific binding, while the C-terminal domain determines the specific binding to the target protein.
Subcellular Location: Cytoplasm
EC: 2.7.7.77
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Q92PB2 | MTGAPSHATFPPAVILAGGLSSRMGRPKAGLVLGGRSMLTRVIERLRPQVAGIAINLNADPDPASAFGLEVVPDTIPGFVGPLAGILAAMRHTVRKSPGASHVLTVPVDTPLFPKSLAARLKTAITSGGEIAVAFSAGEMHPLFALWPVALADDLEAWIHADEKRRVRAFIARHESATVEFPLIPTAAGPLDPFFNINTPEELRQAEAWLPYLEDREP | Function: Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor.
Catalytic Activity: GTP + H(+) + Mo-molybdopterin = diphosphate + Mo-molybdopterin guanine dinucleotide
Sequence Mass (Da): 23198
Sequence Length: 218
Domain: The N-terminal domain determines nucleotide recognition and specific binding, while the C-terminal domain determines the specific binding to the target protein.
Subcellular Location: Cytoplasm
EC: 2.7.7.77
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Q7UYZ6 | MRNELTAMPHAAPPPLLGVLLAGGRSSRMGTPKALLPHPSGGTFLTHSLDRLRLVCEEKIVVSLASEAHRAQVQLPPSVPALFDSQPALGPAMGVSVALQHASSNGFAGCLFTPVDLPDLSVDDLLSLVHAWRESPTQIVLAQQTDPERLQPLVGIYPVACMDSIQRVVESEHRSLYRSLRSSDHQTVAIPSTRLRNVNTPADLGPPFDST | Function: Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor.
Catalytic Activity: GTP + H(+) + Mo-molybdopterin = diphosphate + Mo-molybdopterin guanine dinucleotide
Sequence Mass (Da): 22640
Sequence Length: 211
Domain: The N-terminal domain determines nucleotide recognition and specific binding, while the C-terminal domain determines the specific binding to the target protein.
Subcellular Location: Cytoplasm
EC: 2.7.7.77
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Q9X7K0 | MRIAGIILAGGQGRRMGREKALVPLSGVPLIARVLALAPQVEAVAISANGDPGRFGLGLPVLPDRPGESGLGPMAGIRAGLDWAAGIGAEALVSTATDTPFLPEDLVERLAAAAPAHAQSFGRDHYTAALWRVATVPRIDALFAADERRIARLSGGAVAVPFDTTPDPFANLNTPEDLARAEDRLRQNAP | Function: Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor.
Catalytic Activity: GTP + H(+) + Mo-molybdopterin = diphosphate + Mo-molybdopterin guanine dinucleotide
Sequence Mass (Da): 19752
Sequence Length: 190
Domain: The N-terminal domain determines nucleotide recognition and specific binding, while the C-terminal domain determines the specific binding to the target protein.
Subcellular Location: Cytoplasm
EC: 2.7.7.77
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Q2IYY0 | MFGRRSMADPPAPPAIILAGGLAQRMGGGDKALRMVGGRTLLALVIDRLASQCDILALSANGDPARFADYDLPVIADPVDGFRGPLAGVLAGLDWVAEHRPAARWMLSTPADCPFLPRDLVARLHQARIDQQADIAVAASAGRSHPVIALWPVGLRIDLRRALLADDIRKVDRFTARYPRAMAEWPVEPADPFFNANTPQDLAEAEGLAMREPD | Function: Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor.
Catalytic Activity: GTP + H(+) + Mo-molybdopterin = diphosphate + Mo-molybdopterin guanine dinucleotide
Sequence Mass (Da): 23100
Sequence Length: 214
Domain: The N-terminal domain determines nucleotide recognition and specific binding, while the C-terminal domain determines the specific binding to the target protein.
Subcellular Location: Cytoplasm
EC: 2.7.7.77
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A8GLJ4 | MHEEITGIILAGGRATRMGGEDKGLIQIAGIPLYQYVLSRLRPQVSLMAISANRNQARYGESGLPIVSDLTPDFSGPLAGMLAGLKHAATEWVVFVPCDVPDFPATLVDQLWQQKGSSLAAYASDGERAHPTLALLHTSLAPQLKEYLARGERKLMLFLDAAGARKIAFSGQQAAFHNLNTREDCLRWQQEKGLTNE | Function: Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor.
Catalytic Activity: GTP + H(+) + Mo-molybdopterin = diphosphate + Mo-molybdopterin guanine dinucleotide
Sequence Mass (Da): 21485
Sequence Length: 197
Domain: The N-terminal domain determines nucleotide recognition and specific binding, while the C-terminal domain determines the specific binding to the target protein.
Subcellular Location: Cytoplasm
EC: 2.7.7.77
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Q8IU29 | MTVLSQIIKPDDMIKITSEFARLGDRCYLDNAGATLYPKSLITSINEDLLKNVYMNPHTDKNTKDYIEQIRCLILKHFNTDPSTYTLIFTSGTTQALKLVIESFQFMKNEDDDLNCGSFVYLEDNHTSVVGLRELAVDKDAEVVHIAHEDFLNVINTKAKQTSKYTNGGNCLVAYPAQSNFNGFKYPLNCIENIKNGCLNNHLKKHLCEINSDWYVLLDAAAYVATSKLDLAKVQPDFVSLSFYKIFGFPTGLGALLVKKSSENVLSQKRYFGGGTVDALLSNEHYHIKREIFHERFEDGSLSFLSIISLKQCLDTMYRIIPRIIHDDIMETISYHTFYLAKDLYCQLLDLRHRNGTKAIKFYLDSDFSDITKQGGVLTFNLVREDGTYIGFSEFQHMADLFNISVRTGCFCNSGSCQRHLHMSNKDMKDMYNAGHRCGDEVDLINEKPTGAIRISFGYYNTFEDVDKFVNMICRCFVNAKARKQKRIINHFVETPKIKHYNGNVNKIINEQIYFKNVDDVLINIPPMSTKIILKEICIFPIKSCGAFKILSGWNIGPKGFEYDREWMIVKDNGVCLTQKQNTRMCMIRPQIDLKQKVMILNFPGKTPISIPLENSINEVQKNGSLCHSKVCTDMIKGIDCGDEVADWISEALEVSFLRLIRQSSNDNRSLKKKKDEDKKLLSLSNQAQYLLINKATVKWLSEKIKDPLFTDDLNHLTDRFRGNLIIEMEQELLEREWHSVIIGNHEFKVEGQCPRCQMVCIDQQTGEKTVEPLRTIAEQFGGKLRFGIYLSYVGTVNKSDDRTLKTYSPIKAILNDDNISR | Function: Sulfurates the molybdenum cofactor. Sulfation of molybdenum is essential for xanthine dehydrogenase (XDH) and aldehyde oxidase (ADO) enzymes in which molybdenum cofactor is liganded by 1 oxygen and 1 sulfur atom in active form.
Catalytic Activity: AH2 + L-cysteine + Mo-molybdopterin = A + H2O + L-alanine + thio-Mo-molybdopterin
Sequence Mass (Da): 94082
Sequence Length: 822
EC: 2.8.1.9
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A6SRX6 | MEEYNKAVEEFRKHEYPMLKDAVYLDHAGTTLYSKSLMERYMGDMMSNLYGNPHSASTSSQLSTSRIENTRLNVLQFFNADPEDFDVVFVANATAGIKLVMDAFRCQEDGFLYGYHQDSHTSLVGVREDAVSSRCLDDDAVECWLSGSEALVRNEHNSEIGLFAYPAQSNLDGRRLPLSWPERVRNLSYEAQANTYTLLDASALVSTSPLDLSDVSKAPDFTVLSFYKIFGFPDLGALIVRKDSGAILQTRKYFGGGTVEVVVCLKEQWHAPKGQSLHENLEDGTLPFHNIMALEAAIDVHKSLYGSMECIANHTTFLARKLYEGLKSLQHANSEPACIIYSPGFSETSSNVQGPTIAFNVKNSFGAWVTNVEFERLASIKNYHIRTGGLCNPGGVASALELQPWETRRNFSAGLRCGGETDIYAGKITGVIRVSLGAMSTMSDVDSFLSFVNEFFVDHTVVSADEDGESQKSVDMYVESLTIYPIKSCGGFEIPKETAWEVRPEGLAWDREWCLIHQGTGQALSQKRYPRMALIKPTIDFDLGLLKLRYQGSTFPTLVDEISVSLSSDPSSYKNPNNIHSLSSRVCGDAIAAQTYFDHEINDFFSKILEAPCVLARFPAGGSGPSLRHAKAHMQKHQGPKRSAAIEKSSAHSFHDPPTPPDSDSENRKRPILLSNESPILAINRSSINMLNEEIAKSGGKLASASVFRGNIVLASTELTDSHHPYSEDHWSTLQIGSETYQMLGSCRRCHMICVDQDTAEKNEEPFVTLAKTRRFESKVFFGSHMCHVPSFSRHKKHQFPVIKVGDKVSIGL | Function: Sulfurates the molybdenum cofactor. Sulfation of molybdenum is essential for xanthine dehydrogenase (XDH) and aldehyde oxidase (ADO) enzymes in which molybdenum cofactor is liganded by 1 oxygen and 1 sulfur atom in active form.
Catalytic Activity: AH2 + L-cysteine + Mo-molybdopterin = A + H2O + L-alanine + thio-Mo-molybdopterin
Sequence Mass (Da): 90173
Sequence Length: 813
EC: 2.8.1.9
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Q9N0E7 | MAGGAAHPGAELLPFARFLDSSLQPLVYGYGRGTLHELRAREFGRLAGTVYLDHAGTTLFPQSQITSFMKDLMENVYGNPHSQNISSKLTHDTVEQVRFRILAHFHTSPEDYTVIFTSGSTAALKLVAEAFPWVSPGPEGSGSCFCYLTDSHTSVVGMRKITAAMNVSSIPVRPEDMWSAERQDAAAAGDPAGQPPHLFCYPAQSNFSGTRYPLSWIGEVKSGRRRPASRPGKWFVLLDAAAFVGTSPLDLSVHQADFVPISFYKIFGFPTGLGALLVNNRLAALLRKTYFGGGTAAAYLAGDDFYVPRESVAERFEDGTISFLDVIALKHGFDALERLTGGMESIRQHTFTLAQYTYTALSSLRYPNGAPVVQIYSDSDFSSPEVQGPVISFNVLDDHGNVVGYSQVDKMASLHNIHVRTGCFCNTGACQRHLGISDEMVKKHLQAGHVCGDDVDLIDGQPTGSVRISFGYMSTLEDAQAFLRFIIATRLHSSHGQPLPLATPGEAGAPPEDSEAQNAVPAARARGSSSPQEDTSPHSGVWNNSPTAVDAEGLCPPLLEATGTQQTTSEKAADVPDGDLRSHVITNLFLYPIKSCAAFEVIRWPLGSQGLLYDRSWMVVNHNGICLSQKQEPRLCLIQPFIDLQRRIMVIKAQGMEPIEVPLEENSEQVQICQSKVCADRVNTYDCGEKISNWLSKFFGRPYHLIKQSSDFQRNAKKKHGKDQSAHTTATLSLVNEAQYLLINRSSILELQQQLSTSCENGKEELFPMNNLISRFRANIITNGTRAFEEEKWDEISIGSLRFQVLGPCHRCQMICIDQQTGQRNQDVFQKLSERRERKVKFGVYLMHTSLDLSSPCYLSVGSQVLPLLKENMEHHDIPATE | Function: Sulfurates the molybdenum cofactor. Sulfation of molybdenum is essential for xanthine dehydrogenase (XDH) and aldehyde oxidase (ADO) enzymes in which molybdenum cofactor is liganded by 1 oxygen and 1 sulfur atom in active form.
Catalytic Activity: AH2 + L-cysteine + Mo-molybdopterin = A + H2O + L-alanine + thio-Mo-molybdopterin
Sequence Mass (Da): 97205
Sequence Length: 882
EC: 2.8.1.9
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A8X493 | MPYLDHAGSTLPSKTQLEELAKLQTQLILANPHSHHSTAIKTQQIVSSARHRILRYFNTTADDYFVVFTNNTTHALKIVAENFNFGHRTQEGVVSEISAVLKGGPSNFAYFNDSHHSVVGLRHVVLGKVDAISCVNEDVVKEECIPKVENSLFVFTAMSNFLIPFQINEKLISGWSVCVDAAALVSGTRLDLTAHRPNFVAFSFYKIFGYPTGIGALLVKKDSSKSIEKTSFAGGTVQSVDEMTMHFVIRDFERAYEEGTINSYGIAQLQKGFEEIERCGGMQAIRAHTYDLRSKAVQILQSKTHPNGKKVVEIYSQPHIQVSPETQGAIVAFNLVRPDNGYYGYTEVEKMCAIFGIELRTGCFCNIGACKKYLGITSEMIKENMSKGKRCGDEIDLINGRPTGAVRISFGRMSTEQDIEVLKQMIDTCFVSSEKVFSPSLQSLKIDSFLPTVVNLFSFPIKSVGSVAKSRYELTPRGFKHDREFLVVKDDVTLNLKMHPELCRLTATIVNDEELHIQTFDQNDNLVIPMSLSLKENDAKVVCKKTIATFDCGDKVGQWLENALDMTNCRLLRVAGESKKNFVNDSPFLLINEASVYMLARHIDMDVQDILTRFRSNIVVRGLPPFIEDTAKRLSIENLEFEVVDKCTRCEMICVDPMTGEKDPSLLLALRDYRNKQKMTFGIYIRQSNFEPGQFVEAGSAVRFFTD | Function: Sulfurates the molybdenum cofactor. Sulfation of molybdenum is essential for xanthine dehydrogenase (XDH) and aldehyde oxidase (ADO) enzymes in which molybdenum cofactor is liganded by 1 oxygen and 1 sulfur atom in active form.
Catalytic Activity: AH2 + L-cysteine + Mo-molybdopterin = A + H2O + L-alanine + thio-Mo-molybdopterin
Sequence Mass (Da): 79290
Sequence Length: 707
EC: 2.8.1.9
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Q2HE65 | MARTDDQAKSVDTRYNARVESLRDKEYPMLNGSIYLDHAGTTPYPKSLMDRFAKEMTSNLFGNPHSASASSQLSTARIEDIRLRVLRFFNADPAEFDLVFVANATAGIKLVADALRTAPDGFDYSYHQASHTSLIGVREEARNSLCLDDQEVDDWLGGGCPFENDSEDRPVLFAYPAQSNMDGRRYPLNWAEKVCRGGTRKTYTLLDAAALVCSSPLDLSQANAAPDFTVLSFYKIFGFPDLGALIVRRDAEEAFDTRRYFGGGTVDMVVCLKEQWHAPKAQFLHERLEDGTLPVHSIIALDAALDVHKQLFGSMRDVASHTAFLSAMLYTRLELLRHGNGQSVCVLYSPGPETANNGLSSGPVVSFNIRNSQGAWISLAEVEKLATLKGFHIRTGGVCNPGGIASALGLEPWEMRRNFSSGFRCGTDLDIMAGKPTGVIRASLGAMSTISDVDSFVEFIAEFYRDASLSPARTEPVPQPHDPSRLRIHSMSIYPIKSCCGFQVPSGTDWEVRPEGLAWDREWCLVHQGTGQALSQKRHSKMALIRPALDFERGQLRVSYAGELPAHQPREISIPLSKNPSLFRSSSSRSRSSRVCGEEIQAQTYSSTAINSFFSDVLGVPCLLARFPAGGHGKSMRHSKAHLQKHQLSLLPTARPALPGSFPPSPPDSDTEKTVSRRILLSNESPILAITLPSVTELNREIHLSKPGLKEVSPAVFRANIVMTPADPDVPLAPYAEDSWSGIKVGPQQHEFEMLGACRRCHMVCINQETAERARSRL | Function: Sulfurates the molybdenum cofactor. Sulfation of molybdenum is essential for xanthine dehydrogenase (XDH) and aldehyde oxidase (ADO) enzymes in which molybdenum cofactor is liganded by 1 oxygen and 1 sulfur atom in active form.
Catalytic Activity: AH2 + L-cysteine + Mo-molybdopterin = A + H2O + L-alanine + thio-Mo-molybdopterin
Sequence Mass (Da): 85612
Sequence Length: 778
EC: 2.8.1.9
|
A2VD33 | MDTRSLQDFQDLCTFDVFKSFGHYYGYGVDQQALIDQEFKRIKGVTYLDHAGTTLFPESLIKGFHDDISRNVYGNPHSHNSSSRLTHDTVESVRYKILAHFNTSPEDYSVIFTSGCTAALKLVADTFPWKPMSNKEPGSQFCYLTDNHTSVVGIRGATALQGVGTISVSPREVETRARNKTQTNGEEECSTPHLFCYPAQSNFSGRKYSLSYVKGIQSQQLYPACEHHGQWFVLLDAACFVSCSPLDLSQYPADFVPISFYKMFGFPTGLGALLVRNEAAEVLRKTYFGGGTAAAYLVEENYFIPKPNLASRFEDGTISFLDIISLHHGFETLQKLTGSMTNIQLHTFGLARYTYTVLSCLCHSNGKHVAQIYCDNDFQSIAEQGAIINFSLLDCHGRTVGYSQVDKMASLFNIHIRTGCFCNTGACQHYLAISNQNVKSNLHAGHICGDNIDLVDGRPTGSLRVSFGYMSSFEDCQNFLRFVVNCFVDKPLILDQTKLAKLNSAAPIEPSSSYSPSPDRMAVSEVTMSKDGKKDGSSCTLTNLFIFPVKSCASFEVTEWPLGPQGLLYDRLWMVVNENGVCLSQKREPKLCLIQPVVCLAANTLKLQISGSEAITVPLDPSLEKSDLRTSQSKVCGDRVQTVDCGEEVSAWLSEFLGKPCRLIRQRPEFLRDMKFGQGDCCPTPLSLVNEAQFLLINRASVCFLQEAIANRYNSDNEETWRDTEQLVQRFRANLVISAQEPFAEDNWSHLTIGNTQFQVIGKCGRCQMIGVDQKTATRTQEPLRSLSECRSGKVTFGVYLAHQSARNSTHPVLSIGSHVIPKISDSTDKF | Function: Sulfurates the molybdenum cofactor. Sulfation of molybdenum is essential for xanthine dehydrogenase (XDH) and aldehyde oxidase (ADO) enzymes in which molybdenum cofactor is liganded by 1 oxygen and 1 sulfur atom in active form.
Catalytic Activity: AH2 + L-cysteine + Mo-molybdopterin = A + H2O + L-alanine + thio-Mo-molybdopterin
Sequence Mass (Da): 92399
Sequence Length: 831
EC: 2.8.1.9
|
Q559G8 | MLIFIISIIITIASIIFLFETVFNKNSNTINNNNNSNNNNNNNNNNNNNNNNNKNNIKENNIDKNKEIKIKEKLILNNNDPKENDLKYKEEFNNFLNKFSKNQEYGYKDNLIDNELRNHYNNNNNNNNNNNNNNKDDQFPKLKDIVYLDHAASTLASMNQIEEISKELKNSMFCNPHSVNPIGLKTKEEVDSIRENILNYFNAPYRQYSVIFTSGCTDSLKKVGEYFAWTKNSKFYYSLESHNSLLGIREYACESIGGSSTTSFQPIPSLYFKCNNNQFNDILEIIGNNDDNNNESYSLFGYPGQCNYSGTKYPLELINRIQKKYPKCKVLLDAASLVSTSSFDLTKYPVDFMTISFYKMFGYPTGIGALIVKNDSGEKCLINKKYFSGGTVNVSMAQERFHVDRPSLSERLEDGTINFMNIISLKHGFNIINNQLGGIDNVKLHTFSLTQYCKEEMLKLYHSDNSKQQQLCIIYSDNHFKDSSKQGSIINFNIFRSNGELFGYNQVEKLASLSSIYLRTGCFCNPGACHGYLNLSKKDIEQHLKDGHVCWDSKDILNGKPTGSVRISFGYMNNFNDVYKFINFLKSNFINDHKFEKEVIKSNKKINNNLCDISDNISCSGSCGGSCGSSGSGIEDYQVQYSNNIKEEKEEEEKEEIENLKNEKDNDEVLLSEIYIYPVKSCSGHKVVNDKWELVPSGLKYDREWTIIDQSGNYINQKKLPILALIQTEIDLINDKLILTAPEMKVLSIPLSYYPISAFDQIQVCGDKVDGLLYGDKDFSNTSGSSAGSGGGGGGNIDNISEWLYQFIGKRCYLVRKSPESHRKSKVDSSNEISFANESPYLLINEESVSDLKKRIIKDNPDSVPSDWNWISKHSFRANFIITGGKAYQEDLWSQFQLISKQQNDTTQSSSSPLVFNSVGDCNRCKMICINQKMGIEEREPLSTLASYRRSGGKIIFGQHLNFADSIKRNNSHTNDTALSSNESSISSSNPIFLHVPSKLKVLSERY | Function: Sulfurates the molybdenum cofactor. Sulfation of molybdenum is essential for xanthine dehydrogenase (XDH) and aldehyde oxidase (ADO) enzymes in which molybdenum cofactor is liganded by 1 oxygen and 1 sulfur atom in active form.
Catalytic Activity: AH2 + L-cysteine + Mo-molybdopterin = A + H2O + L-alanine + thio-Mo-molybdopterin
Sequence Mass (Da): 114389
Sequence Length: 1007
EC: 2.8.1.9
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Q9VRA2 | MTSYRPEFSASEQSQIDAEFSRLASNKSVYLDHAGTTLYAESQVTAAAEQLQRNVICNPHTCRLTGDFVDQVRFKILEFFNTTAEDYHVIFTANATAALSLVAENFDFGSSGEFHFCQENHTSVLGMRERVRENGIYMLRENEISGGKHKANGKVHEVSGKTGNSLLTFSAQCNFSGYKIPLEVIEQIQIDGLAKPGKELWSSLGEKKKNMHNDYYICLDAASFVATSPLDLQKYRPDYVCLSFYKIFGYPTGVGALLVSRRGAEVFQKRRFFGGGTINYAYPHAMDYQLRETFHQRYEDGTLPFLSIVGLLEGFRTLERLVPRTDEFSTMERISRHVFGLAKYLEDQLRQLHHPNGEPLVKLYNKVGYQDKSRQGGIVAFNVRTESGSFVGFGEIACVAALHGILLRTGCFCNIGACQYYLGLDEDALDAIYKRAGRICGDYFDLIDGQPTGAVRVSFGYMTTIQDVDKLLQMLRSSYLATKPLQRIQFIEEQAEQLPPLLKERVQLLRPKLLQMAIYPVKSCAAFKIELPGSWPLTDQGLKYDREWMIVDMNGMALTQKRCTELCLIRPVIKVDQLELQFGENSTISVPLSLDDQAADTAKCVSKVCRQPVEGLDCGDRVAQWLSENLGMEGLRLLRQSGQRNSSKDQQKLSLVNQAQFLLLNKSSVRSLQFEEPLDETVDRFRANIIIDTGSAFEELTYKALSIGGIQFQVEGPCQRCDMICINQRTGERSPETLTTISRLQKGRMRFGIYITRIPQDTKELEPKEQHMTCGDVVLVE | Function: Sulfurates the molybdenum cofactor. Sulfation of molybdenum is essential for xanthine dehydrogenase (XDH) and aldehyde oxidase (ADO) enzymes in which molybdenum cofactor is liganded by 1 oxygen and 1 sulfur atom in active form.
Catalytic Activity: AH2 + L-cysteine + Mo-molybdopterin = A + H2O + L-alanine + thio-Mo-molybdopterin
Sequence Mass (Da): 88104
Sequence Length: 781
EC: 2.8.1.9
|
Q2K2X0 | MTLIVEAKQRLGAFSLDAAFTSEGGVTAFFGRSGSGKTSLIRIIAGLARPDGGRVVLDGERLTETTAGIFVPKHRRRFGYVFQEARLFPHLSVRANLSYGRWFAPKAGRSESFDHIIDLLGIETLLERSPAKLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDEARKAEILPYLERLRDETEIPIVYVSHSIAEVARLANQVVVLSDGKVQATGPAVDILSRPSAAADRKEAGALLEGTVESFDARHRLSTVTLKSSQLHIPSAVLTPGRPVRIRIPSRDVMLATARPEGLSALNILEGRIEAISPGEDGTVEIRIDCAGDAILSRITALSCERLDLRPGKTVFAIIKTVALEG | Function: Part of the ABC transporter complex ModABC involved in molybdenum import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + molybdate(out) = ADP + H(+) + molybdate(in) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 38324
Sequence Length: 355
Subcellular Location: Cell inner membrane
EC: 7.3.2.5
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Q92LU2 | MRLEVEARLRLGSFAIDAAFGSEGGVTALFGRSGSGKTSLVNIIAGLLRPDQGRVVLDGDTIADSERRLFTPVHRRRFAYVFQEARLFPHLSVRGNLAYGRWFAGAARSGPEFGRIVEMLGIGHLLDRMPSKLSGGERQRVAIGRALLAFPRLLLMDEPLAALDDARKAEILPYLERLRDETRIPIVYVSHSVAEVARLAERVVVMENGRVKASGKTAAVLNEPFPTSGPGRREAGALIEGIVDSHDEGHELTVVRAGDCLIRVPHLVAEPGQRLRLYIAARDVMLATRRPEGISALNVLPGTIVGLSSPRQGSIDVRVDCGGNVIAARVTTLSRDALDLRPGKQVHAVVKTVALDY | Function: Part of the ABC transporter complex ModABC involved in molybdenum import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + molybdate(out) = ADP + H(+) + molybdate(in) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 38720
Sequence Length: 357
Subcellular Location: Cell inner membrane
EC: 7.3.2.5
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Q08381 | MISARFSGRQGDFTLDAAFDVPGQGVTALFGPSGCGKTTVLRCMAGLTRLPGGHLVVNGVTWQEGRQITPPHRRAVGYVFQEASLFTHLSVRENLVYGLRRARGPLRISEAEVTQLLGIDPLLRRPTATLSGGERQRVAIGRALLSQPELLLMDEPLSALDRISRDEILPYLERLHASLQMPVILVSHDLSEVERLADTLVLMEAGRVRAAGPIAAMQADPNLPLIHRPDLAAVIEGVVIALDPAYGLSTLQVPGGRIVVPGNLGPIGARRRLRVPATDVSLGRHAPTDTTILNALPAVILGAEAAEGYQITVRLALGASGEGASLLARVSRKSFDLLGFQPGEQVVARLKAMALSAPAQTGG | Function: Part of the ABC transporter complex ModABC involved in molybdenum import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + molybdate(out) = ADP + H(+) + molybdate(in) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 38546
Sequence Length: 363
Subcellular Location: Cell inner membrane
EC: 7.3.2.5
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Q2J1U0 | MRAIAPRSIRGEFRGRLGGFALDAAFSVPATGITGLFGPSGCGKSTVLRCLAGLQRLPGGRCDVDGDVWQDEATFLKPHQRPIGYVFQEASLFQHLSVRANLLYGAPRGGADAAEGAVGFDEVIELLGLSHLLDRAPRNLSGGERQRVAIGRALLSQPKLLLMDEPLSALDRLTKDEILPFLERLHARLSLPVIYVSHDITEIERLADHLILMRAGKVLAAGPLTELQSDPALPLATARDAAVNVDAIAESYDSVYGLLTLRLDGGRLLVPSAPVQPGEARRIRIAAGDVSLAREAPHRTSILNILPARIATTSPVGPNEVLVVLALGPGGQGARLLARVTRRSWDQLQLAAGDELFAQIKGVALAPERGAARDSAS | Function: Part of the ABC transporter complex ModABC involved in molybdenum import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + molybdate(out) = ADP + H(+) + molybdate(in) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 40103
Sequence Length: 377
Subcellular Location: Cell inner membrane
EC: 7.3.2.5
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Q21BF6 | MRDVSRSIQAQFRGALGRFALDAAFTVPATGITGLFGPSGCGKSTVLRCIAGLQQLPGSTFAIDGDVWQDASQFRQPHQRPIGYVFQEASLFAHLSVKANLLYGAPRDAAHARDSITFDEVIELLGLAALLERSPRHLSGGERQRVAIGRALLSQPKLLLMDEPLSALDRLTKDEILPFLERLHERLALPVIYVSHDMAEIERLADHLVLMRKGQVLAAGPLAALQSDPALPLAASRDAAVNFEATVEDYDPGYGLLTVAVDGGRLLVPAPPAQRGEHRRLRIAAGDVSLARELPHNTSILNVLPARIVSHNPLGDSEILVVLALGGNGEGARLLARVTRRSWDHLELADGIGLIAQVKGVALAPGRNTGTHASSPGLRGR | Function: Part of the ABC transporter complex ModABC involved in molybdenum import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + molybdate(out) = ADP + H(+) + molybdate(in) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 40798
Sequence Length: 381
Subcellular Location: Cell inner membrane
EC: 7.3.2.5
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Q2RWI9 | MLDIDVLRQQGALRLSIAFRAGKGVTALFGRSGAGKTSVISMVAGLSRPDGGRIVVDDRVLFDGAKGIDLAPEKRRVGYVFQEGRLFPHLTVRQNLAFGMNRVPAAERYVGEDDVVDLLGISALLDRRPAKLSGGEKQRVAIGRALLASPRILLMDEPLASLDAQRKDEVLPFIARLPRRFSIPILYVSHAMDEVLRLADTLVLIAEGQVAASGPLEEVLARPDIPDFAAQRDAGAVVAAKVAGRDIPFGATLLDTPAGLLRTRPIDLPLGTKVRVRIAAADISLALERPRMVSVQNILAATILAIGEPEDGRLSVDLDAGPPGGPPCRLWASITARARHDLGLVPGLRVHALIKAMSLLRDELVEHSPH | Function: Part of the ABC transporter complex ModABC involved in molybdenum import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + molybdate(out) = ADP + H(+) + molybdate(in) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 39673
Sequence Length: 370
Subcellular Location: Cell inner membrane
EC: 7.3.2.5
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Q3S2U5 | MASHQSEKEKPQSCTTEVQVSHVTGLKLGLVVTSVTLVVFLMLLDMSIIVTAIPHITAQFHSLGDVGWYGSAYLLSSCALQPLAGKLYTLLTLKYTFLAFLGVFEVGSALCGAARCSTMLIVGRAVAGMGGSGLTNGAITILASAAPKQQQPLLIGIMMGLSQIAIVCGPLLGGAFTQHASWRWCFYINLPVGALAAILLLAIHIPKSVPTSDCTMPAPRAVGVRVILSQLDLLGFVLFAAFAVMISLALEWGGSDYMWDSSVIIGLFCGAGISLVVFGFWERYVGNSMAMIPFSVASRRQVWCSCLFLGFFSGALLTFSYYLPIYFQAVKDVSPTMSGVYMLPGIGGQIVMAIVSGAIIGKTGYYIPWALASGIIVSISAGLVSTFQPHTSIAAWVMYQFMGGFGRGCGMQTPIIAIQHALPPQMSALGISLAMFGQTFGGSLFLTLAKLVFSAGLDAGLREYAPAVSAEAVTAAGATGFRDVVPANLLSQVLLAYCKGIDHTFYLAVGASGATFLFAWGMGQVGLIWWGEERTGFGRDERV | Function: Efflux pump; part of the gene cluster that mediates the biosynthesis of monakolin K, also known as lovastatin, and which acts as a potent competitive inhibitor of HMG-CoA reductase .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 57408
Sequence Length: 543
Subcellular Location: Membrane
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Q9UQ07 | MKNYKAIGKIGEGTFSEVMKMQSLRDGNYYACKQMKQRFESIEQVNNLREIQALRRLNPHPNILMLHEVVFDRKSGSLALICELMDMNIYELIRGRRYPLSEKKIMHYMYQLCKSLDHIHRNGIFHRDVKPENILIKQDVLKLGDFGSCRSVYSKQPYTEYISTRWYRAPECLLTDGFYTYKMDLWSAGCVFYEIASLQPLFPGVNELDQISKIHDVIGTPAQKILTKFKQSRAMNFDFPFKKGSGIPLLTTNLSPQCLSLLHAMVAYDPDERIAAHQALQHPYFQEQRKTEKRALGSHRKAGFPEHPVAPEPLSNSCQISKEGRKQKQSLKQEEDRPKRRGPAYVMELPKLKLSGVVRLSSYSSPTLQSVLGSGTNGRVPVLRPLKCIPASKKTDPQKDLKPAPQQCRLPTIVRKGGR | Function: Able to phosphorylate several exogenous substrates and to undergo autophosphorylation. Negatively regulates cilium length in a cAMP and mTORC1 signaling-dependent manner.
PTM: Autophosphorylated.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 48014
Sequence Length: 419
Subcellular Location: Cytoplasm
EC: 2.7.11.22
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Q9WVS4 | MKNYKAIGKIGEGTFSEVMKMQSLRDGNYYACKQMKQHFESIEQVNSLREIQALRRLNPHPNILALHEVVFDRKSGSLALICELMDMNIYELIRGRRHPLSEKKIMLYMYQLCKSLDHMHRNGIFHRDVKPENILVKQDVLKLGDFGSCRSVYSKQPYTEYISTRWYRAPECLLTDGFYTYKMDLWSAGCVFYEIASLQPLFPGVNELDQISKIHDVIGTPCQKTLTKFKQSRAMSFDFPFKKGSGIPLLTANLSPQCLSLLHAMVAYDPDERIAAHQALQHPYFQVQRAAETQTLAKHRRAFCPKFSMVPESSSHNWSFSQEGRKQKQSLRHEEGHARRQGPTSLMELPKLRLSGMTKLSSCSSPALRSVLGTGANGKVPVLRPLKCAAVNKKTDTQKDIKPHLKHYHLPTINRKGGEY | Function: Able to phosphorylate several exogenous substrates and to undergo autophosphorylation . Negatively regulates cilium length in a cAMP and mTORC1 signaling-dependent manner .
PTM: Autophosphorylated.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 48065
Sequence Length: 420
Subcellular Location: Cytoplasm
EC: 2.7.11.22
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P44206 | MKLKSLLIACLLSSLSFSALADRIITDQLDRKVTIPDHINRAVVLQHQTLNIAVQLDATKQIVGVLSNWKKQLGKNYVRLAPELENMAMPGDLNSVNIESLLALKPDVVFVTNYAPSEMIKQISDVNIPVVAISLRTGEVGEKGKLNPTLTDEDKAYNDGLKQGIELIAEVFEKKQQGDELVKAAFANRKLLADRLGDVSADKRVRTYMANPDLGTYGSGKYTGLMMEHAGAYNVAAATIKGFKQVSLENVLEWNPAVILVQDRYPDVVPQILNDQGWANIQALKDKKVFLMPEYAKAWGYPMPEALALGEVWLAKALYPQRFQDVDLDKMVNDYYQKFYRTSYKPDNAAR | Function: Part of the ABC transporter complex MolBCA involved in molybdate import . Functions as a low-affinity molybdate transporter . Binds to both molybdate and tungstate, but not to sulfate or phosphate .
Sequence Mass (Da): 39205
Sequence Length: 351
Domain: Nucleotide binding is coupled to a conformational shift at the periplasmic gate. This shift is akin to unlocking a swinging door: allowing just enough space for molybdate to slip into the cell. The lower cytoplasmic gate, identified as gate I, remains open throughout the MolBC-A mechanism, and cytoplasmic gate II closes in the presence of nucleotide.
Subcellular Location: Periplasm
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Q57130 | MQPDSYPKILFGLTLLLVITAVISLGIGRYSLSVPQIGQILWAKATALEIDPVQQQVIFQVRLPRILTALCVGAGLALSGVVLQGIFRNPLVNPHIIGVTSGSAFGGTLAIFFGFSLYGLFTSTILFGFGTLALVFLFSFKFNQRSLLMLILIGMILSGLFSALVSLLQYISDTEEKLPSIVFWLMGSFATSNWEKLLFFFVPFLLCSSILLSLSWRLNLLSLDEKEAKALGVKMAPLRWLVIFLSGSLVACQVAISGSIGWVGLIIPHLSRMLVGANHQSLLPCTMLVGATYMLLVDNVARSLSDAEIPISILTALIGAPLFGVLVYKLKRGGMNE | Function: Part of the ABC transporter complex MolBCA involved in molybdate import . Responsible for the translocation of the substrate across the membrane . Functions as a low-affinity molybdate transporter .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 36531
Sequence Length: 337
Domain: The transition from the outward-facing to the inward-facing conformation is realized through the asymmetric motion of individual subunits of the transporter . Nucleotide binding is coupled to a conformational shift at the periplasmic gate. This shift is akin to unlocking a swinging door: allowing just enough space for molybdate to slip into the cell. The lower cytoplasmic gate, identified as gate I, remains open throughout the MolBC-A mechanism, and cytoplasmic gate II closes in the presence of nucleotide .
Subcellular Location: Cell inner membrane
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Q57399 | MNKALSVENLGFYYQAENFLFQQLNFDLNKGDILAVLGQNGCGKSTLLDLLLGIHRPIQGKIEVYQSIGFVPQFFSSPFAYSVLDIVLMGRSTHINTFAKPKSHDYQVAMQALDYLNLTHLAKREFTSLSGGQRQLILIARAIASECKLILLDEPTSALDLANQDIVLSLLIDLAQSQNMTVVFTTHQPNQVVAIANKTLLLNKQNFKFGETRNILTSENLTALFHLPMFEQQAQYKESFFTHFVPLYKTLLK | Function: Part of the ABC transporter complex MolBCA involved in molybdate import . Responsible for energy coupling to the transport system . Functions as a low-affinity molybdate transporter .
Catalytic Activity: ATP + H2O + molybdate(out) = ADP + H(+) + molybdate(in) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 28520
Sequence Length: 253
Domain: The transition from the outward-facing to the inward-facing conformation is realized through the asymmetric motion of individual subunits of the transporter . Nucleotide binding is coupled to a conformational shift at the periplasmic gate. This shift is akin to unlocking a swinging door: allowing just enough space for molybdate to slip into the cell. The lower cytoplasmic gate, identified as gate I, remains open throughout the MolBC-A mechanism, and cytoplasmic gate II closes in the presence of nucleotide .
Subcellular Location: Cell inner membrane
EC: 7.3.2.5
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Q10459 | MHINTPVLLAIIYFLVFAPKSADAWWLLSKTDTSSANSGSSPILCKNVPGLTPQQKRMCHENPNIIKYLISGLRSALHTCEYTFQREAWNCTLTLPGVGTSPLQIASRESAYVYAISAAGVSHSLARACSKGLIDDCGCGETPQGSGSVAVSQASSRSSSDFVWAGCSDNVKFGNTFGRKFVDQYDRQHATEPRSQMNLHNNRVGRRLLVNAMNKECKCHGVSGSCVTKTCWKVMPKFDEFASRLHQKYQLAKLVTNNDQKLTVRSSPSAGSSGRSERFARNMDASSKQMRNELIYLDASPNYCAIDVKDRECGENCPNICCGRGWRTTREIVDEPCHCQFVWCCEVKCKTCKKLVERNYCL | Function: Ligand for members of the frizzled family of seven transmembrane receptors. Required in embryonic development for endoderm specification and the correct positioning and orientation of the mitotic spindles and division planes in blastomere cells . Involved in cleavage axis determination . Binds to receptor tyrosine kinase cam-1 . Together with wnt ligand lin-44, plays a role in controlling vulva precursor cell P7.p lineage orientation during vulva development, probably by acting as a ligand for tyrosine kinase receptor lin-18 . May act redundantly with other Wnt ligands such as cwn-1 and cwn-2 to control seam cell polarity .
PTM: Palmitoleoylation is required for efficient binding to frizzled receptors. Depalmitoleoylation leads to Wnt signaling pathway inhibition.
Sequence Mass (Da): 40191
Sequence Length: 362
Subcellular Location: Secreted
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Q9XTC6 | MDNSSQSKPSSSSSSHSPSPAAITPTQRTTRDSGLCSTIDIPEIQAQCIDNLNSHYLGKGTYGLVEKTRYRKTRQDDFRPAAIKYSSQLHMATLIREAKVMWDLRNHPNIIKIYGLYKSPRNGQGVVMEYMDCGSMADLLYDRTHINYTIDHVASWMFQLSSAVDFFHSNSQVHRDLKLQNMLLSDRYRTMKLCDFGTFTSMHQSMTSNRGTPITMAPEVFRCEQYNMKSDIYSIGIIMWQIIARNHPYRRDLSVPGLLYNVATANLRPQELECNPILSEFYKKCWNDNADIRPTSSECVEYFTLLKDEYPNGSVPLSDSSTNGPAETPPPHAHRPTMLGTSSGSGIGSNNRTPTASKLLNPQQPGQGHRRNRSETFVVQPDLPYPTVPGEAGASRIPKSQSEAKNFRDRAKSEQRQPHRDARPPPPFEHRRDSNDEEKHAVFMNICSNEETRPIDPDTRDEKSLEIFHQHCDNNKQYADAWVIKKEVMRAKHELIAQWPQHDHTVELLERKYYLEQEIARYRDIQDDNYFSTERM | Function: Part of the Wnt signaling pathway essential for the specification of the mesodermal cell fate in early embryos. Stimulates the wrm-1/lit-1-dependent phosphorylation of pop-1 and plays a role in the initial nuclear accumulation of wrm-1.
PTM: May be autophosphorylated.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 61543
Sequence Length: 536
EC: 2.7.11.25
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A0A0K3AWM6 | MHRHILILFLFGCLSADQRLSSTSISSMNGFSTTRKCEHITIPMCKNLDYNQTVFPNLLGHTTQSEAGPAIAQFNPLIKVKCSEDIRLFLCTVYAPVCTVLEKPIQPCRELCLSAKNGCESLMKKFGFQWPDQLDCNKFPVTDLCVGKNSSESSNSKNYRSSNDVTFGVSTIANEVVLSPKKCPHHMHTTSGSHFSLPLLSGRLPECSLTCEADNQVPMMFDGRVRRILRIWTAAWSVACFVCSLFTLVTFLVDLSRFAYPVRPILYLAFCYLAISTVYMIGVVGEDGFACGTYGSTPTTLVTQGGENVGCSALAVVHYFFFMSSCAWWLVLCLAWFLAANLKWGAESIAALSPYFHAMCWGVPAVLSVTVLVTNSVDGDVFTGICSVGNLNPSALVYFFFTPIVVSLALGAVLLVCGIWSMIRIRSYIKLQHADVERNISKLEKLMLRIGAFAIMYSLPTAMNAAIMWYQAVNMPAWLEGWLHHRCVRLQDRELFGFTYPVDDCPMDPKVAAPEIIVFLLKYVSQLVVGITCAIWVVSSKTLSSYHKAYLALSSRSPTVPAHVDQVNMR | Function: Receptor for Wnt proteins . Most frizzled receptors are coupled to the beta-catenin canonical signaling pathway, which leads to the activation of disheveled proteins, inhibition of gsk-3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes (Probable). A second signaling pathway involving PKC and calcium fluxes has been seen for some family members, but it is not yet clear if it represents a distinct pathway or if it can be integrated in the canonical pathway, as pkc seems to be required for Wnt-mediated inactivation of gsk-3 kinase (Probable). Both pathways seem to involve interactions with G-proteins (Probable). Required in embryonic development for the correct positioning and orientation of the mitotic spindles and division planes in blastomere cells . During early embryonic cell divisions, directs the asymmetric positioning of transcription factors such as pop-1 and dsh-2 in daughter cells in order to determine cell fate specification . Acts redundantly with other Wnt receptors such as lin-17 to control vulval precursor cell specification and also the polarity of different cell types including distal tip cells, seam cells, AVG interneurons and P-cells and their descendants . Plays a role in the migration of cell types including distal tip cells and the QR neuroblast descendants, QR.p and QR.pa during larval development . Negatively regulates the unc-6/Netrin receptors unc-5 and unc-40 to control distal tip cell polarity and migration . Acts through ced-5/DOCK180 and ced-10/Rac to control both distal tip cell migration and the phagocytic clearance of apoptotic cell corpses . Furthermore, it is also required for the migration and axon guidance of the different neuronal cell types including CAN, ALM, HSN and the two mechanosensory neurons AVM and PVM . Mediates Wnt receptor cfz-2 in directing ALM migration, but may also act redundantly with the Wnt receptors cfz-2 and mig-1 to direct the migration of other neuronal cell types including CAN and HSN . Mediates Wnt ligand egl-20 in the control of the anterior-posterior axon guidance of AVM and PVM neurons .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 63198
Sequence Length: 570
Domain: The FZ domain is involved in binding with Wnt ligands.
Subcellular Location: Cell membrane
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Q21154 | MTQDKPIVETISNAGEQVTNVFGQFWQLVTSKNTTNNGDSKPIKIEQLPIYAEDNAPLKQKFLPEEPLPLQREFATIRIACEQEYDRVAERFKVVDCAMTQTKKAATKCNAYLTEEWTALPKAAAITVGGMAGFVLGLKRGPVGRLLTTTIGLATMAAFCYPIEAVDVAKTGRAHAEQTWYSFQESPTPSAIVKTNLSPPK | Function: Sustains mitochondrial morphology probably through maintaining cristae morphology . May act as a component of the MICOS complex, a large protein complex of the mitochondria (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 22082
Sequence Length: 201
Subcellular Location: Mitochondrion outer membrane
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Q46203 | MKKLLKSALLFAATGSALSLQALPVGNPAEPSLLIDGTMWEGASGDPCDPCATWCDAISIRAGYYGDYVFDRVLKVDVNKTFSGMAATPTQATGNASNTNQPEANGRPNIAYGRHMQDAEWFSNAAFLALNIWDRFDIFCTLGASNGYFKASSAAFNLVGLIGFSAASSISTDLPMQLPNVGITQGVVEFYTDTSFSWSVGARGALWECGCATLGAEFQYAQSNPKIEMLNVTSSPAQFVIHKPRGYKGASSNFPLPITAGTTEATDTKSATIKYHEWQVGLALSYRLNMLVPYIGVNWSRATFDADTIRIAQPKLKSEILNITTWNPSLIGSTTALPNNSGKDVLSDVLQIASIQINKMKSRKACGVAVGATLIDADKWSITGEARLINERAAHMNAQFRF | Function: In elementary bodies (EBs, the infectious stage, which is able to survive outside the host cell) provides the structural integrity of the outer envelope through disulfide cross-links with the small cysteine-rich protein and the large cysteine-rich periplasmic protein. It has been described in publications as the Sarkosyl-insoluble COMC (Chlamydia outer membrane complex), and serves as the functional equivalent of peptidoglycan. It is present but some of the disulfide bonds are reduced in reticulate bodies (RBs).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 43261
Sequence Length: 402
Subcellular Location: Cell outer membrane
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Q7RTY1 | MELKKSPDGGWGWVIVFVSFLTQFLCYGSPLAVGVLYIEWLDAFGEGKGKTAWVGSLASGVGLLASPVCSLCVSSFGARPVTIFSGFMVAGGLMLSSFAPNIYFLFFSYGIVVGLGCGLLYTATVTITCQYFDDRRGLALGLISTGSSVGLFIYAALQRMLVEFYGLDGCLLIVGALALNILACGSLMRPLQSSDCPLPKKIAPEDLPDKYSIYNEKGKNLEENINILDKSYSSEEKCRITLANGDWKQDSLLHKNPTVTHTKEPETYKKKVAEQTYFCKQLAKRKWQLYKNYCGETVALFKNKVFSALFIAILLFDIGGFPPSLLMEDVARSSNVKEEEFIMPLISIIGIMTAVGKLLLGILADFKWINTLYLYVATLIIMGLALCAIPFAKSYVTLALLSGILGFLTGNWSIFPYVTTKTVGIEKLAHAYGILMFFAGLGNSLGPPIVGWFYDWTQTYDIAFYFSGFCVLLGGFILLLAALPSWDTCNKQLPKPAPTTFLYKVASNV | Function: Extracellular pH-and Na(+)-sensitive low-affinity creatine transporter . Functions also as a pH-independent carnitine efflux transporter .
Catalytic Activity: creatine(in) = creatine(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 55794
Sequence Length: 509
Subcellular Location: Cell membrane
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M0RCI4 | MGFQKSPDGGWGWVIVVVSFFTQFLCYGSPLAVGVLYVEWLDAFGEGKGKTAWVGSLASGVGLLASPVCSLFVSSFGARPVTIFSGFLVAGGLMLSSLAPNIYFLFFSYGIVVGLGCGLLYTATVTITCQYFDSRRGLALGLISTGSSVGLFIYAALQRMLIEFYGLDGCLLIVGALALNILACGSLMRPLQTSDCPFPEKIAPENVPDRYSIYNEKEKNQEETMTFQDKGYSNEDKCLPNGDWGRETSLPKNPTGAAHTKEPEPYKKKVVEQTNFCKQLAKRKWQVYRNYCGETASLFKNKVFSALFVAILLFDIGGFPPSLLMEDVARSYHVREEDLTIPLISIFGIMTAVGKLLLGILADFKWVNTLYLYVATLIITGLALCAIPLAKSYVTLAILSGILGFLTGNWSIFPYVTTKTVGIDKLAHAYGILMFFAGLGNSLGPPIVGWFYDWTQTYDIAFYFSGFCVLLGGFILLLAILPCWGMCNQRLPKPAAPTTFFYKVASNV | Function: Extracellular pH-and Na(+)-sensitive low-affinity creatine transporter . Functions also as a pH-independent carnitine efflux transporter (By similarity).
Catalytic Activity: creatine(in) = creatine(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 55569
Sequence Length: 508
Subcellular Location: Cell membrane
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Q44456 | MNIVIGLIITFGCIIGGYMAMGGHLNVLVQPFELMIIGGAGLGGFIMANPMKVVKDSGKALGEAFKHSVPKERNYLDVLGVLYSLMRDLRTKSRNEIEAHIDNPEESSIFQSAPSVLKNKELTSFICDYVRLIIIGNARSHEIEALMDEEIETILHDKLKPYHAITTMGDSFPAIGIVAAVLGVIKAMGKINESPEVLGGLIGAALVGTMLGIILSYSICNPLASQVKIVRTKQHRLYIIVKQTLIAYMNGSVPQVALEYGRKTISNYERPSIDAVEQEMMNPGGENKAA | Function: MotA and MotB comprise the stator element of the flagellar motor complex. Required for rotation of the flagellar motor. Probable transmembrane proton channel (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31529
Sequence Length: 290
Subcellular Location: Cell inner membrane
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O67122 | MDVGTIIGIIAAFLLILISILIGGSITAFINVPSIFIVVGGGMAAAMGAFPLKDFIRGVLAIKKAFLWKPPDLNDVIETIGEIASKVRKEGILALEGDIELYYQKDPLLGDMIRMLVDGIDINDIKATAEMALAQLDEKMSTEVAVWEKLADLFPAFGMIGTLIGLIQMLRNLNDPSALGPGMAVALITTLYGAILANAFAIPVANKLKKAKDMEVLVKTIYIEAIEKIQKGENPNVVKQEAAIMLGVELPEEV | Function: MotA and MotB comprise the stator element of the flagellar motor complex. Required for rotation of the flagellar motor. Probable transmembrane proton channel (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 27263
Sequence Length: 254
Subcellular Location: Cell membrane
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P28611 | MDKTSLIGIILAFVALSVGMVLKGVSFSALANPAAILIIIAGTISAVVIAFPTKEIKKVPTLFRVLFKENKQLTIEELIPMFSEWAQLARREGLLALEASIEDVDDAFLKNGLSMAVDGQSAEFIRDIMTEEVEAMEDRHQAGAAIFTQAGTYAPTLGVLGAVIGLIAALSHMDNTDELGHAISAAFVATLLGIFTGYVLWHPFANKLKRKSKQEVKLREVMIEGVLSVLEGQAPKVIEQKLLMYLPAKDRLKFAEQGEAQNGEKKEEEA | Function: MotA and MotB comprise the stator element of the flagellar motor complex. Required for rotation of the flagellar motor. Probable transmembrane proton channel (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 29339
Sequence Length: 270
Subcellular Location: Cell membrane
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Q44902 | MNLASIIGWGVGFGAILISMAFTPTGLGVFWDLSSVFITVVGSFSALMASSEVVAVKKIPTYLGFFFRRNSYAKVSIIKILVELSEKARKEGLLSLDDELEQINDPFFKSGMRLVVDGADPEVIRTMLYLELDQMQERHKVGSDLFKTWAKLAPAFGMTGTLIGLVALLGNLEDKSALGSSMAVALITTLYGTIMANLMFTPVQLKLEKIDTEEAAVKTMIIEGVLSIQSGDNPRILEQKLMTFLTPKDRSQLNSSIGGE | Function: MotA and MotB comprise the stator element of the flagellar motor complex. Required for rotation of the flagellar motor. Probable transmembrane proton channel (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28354
Sequence Length: 260
Subcellular Location: Cell inner membrane
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Q53174 | MDIAAAIGLIGAIVMVVGSMIYAGGVAPFVDIPSLVIVVAGTAFIVLAMKPLPVFLGHFKAMMKVFKPSRFDMNEVISTMVELSNLARKDGIMALEGKAVPDAFFEKGLQLLVDGTDEAKLVKQLKYEIKAMKARHEAYQGAVKAWIDIGPAMGMVGTLIGLVLMLGNMSDPKSIGPAMAVALLTTLYGALMANVIFAPILNKLEGYSADEVTYRELVIEGLRGIARGESARMIEDQMVCALDRKQQMKRKAA | Function: MotA and MotB comprise the stator element of the flagellar motor complex. Required for rotation of the flagellar motor. Probable transmembrane proton channel (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 27195
Sequence Length: 253
Subcellular Location: Cell inner membrane
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P09348 | MLILLGYLVVLGTVFGGYLMTGGSLGALYQPAELVIIAGAGIGSFIVGNNGKAIKGTLKALPLLFRRSKYTKAMYMDLLALLYRLMAKSRQMGMFSLERDIENPRESEIFASYPRILADSVMLDFIVDYLRLIISGHMNTFEIEALMDEEIETHESEAEVPANSLALVGDSLPAFGIVAAVMGVVHALGSADRPAAELGALIAHAMVGTFLGILLAYGFISPLATVLRQKSAETSKMMQCVKVTLLSNLNGYAPPIAVEFGRKTLYSSERPSFIELEEHVRAVKNPQQQTTTEEA | Function: MotA and MotB comprise the stator element of the flagellar motor complex. Required for rotation of the flagellar motor. Probable transmembrane proton channel. Overexpression of MotA, with or without MotB, restores motility in a pdeH disruption, (a c-di-GMP phosphodiesterase) suggesting there is an interaction (direct or indirect) between the c-di-GMP-binding flagellar brake protein YcgR and the flagellar stator.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32011
Sequence Length: 295
Subcellular Location: Cell inner membrane
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P65411 | MDLSTILGLVLAVASISLGDILEDGNPLHIIHLSSVIIIVPTSLFAAMTGTHARYVKAAYKEIKIVFLNPKINLNETIKNLVELATLARKDGVLSLEGRVAQIEDDFTRNGLSMIIDGKDLKSVKESLEISIEEMEEYYHGAAHYWETAGETAPTMGLVGAVMGLMLALQKLDNPAEMAAGIAGAFTATVTGIMCSYAIFGPFGHKLKAKSKDIIKEKTVLLEGILGIANGENPRDLENKLLNYIAPGEPKKSQFEG | Function: MotA and MotB comprise the stator element of the flagellar motor complex. Required for rotation of the flagellar motor. Probable transmembrane proton channel (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 27710
Sequence Length: 257
Subcellular Location: Cell inner membrane
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O07886 | MDIASFIGLFGGFAIIIFGAVLGGSARGLFHVPSLLITVGGSYLTLFLTYPLSYAVGVFRVIARVFHAADFHEREIVQRLYALAEKSRRTGLLALEEEIQDFDDDFVRTGLRNVVDGVDGDAIKALMESELTHMEDRHNTWISLLNSWAALAPGYGMLGTVMGLIGMLATLEDKSSLGSNMATALITTFYGSLVQNWFITPVATKLQYQHDLEVKSKEMVIEGVLSIQAGDHPRVLAQRLLTYLSPKMRKELEMELIKD | Function: MotA and MotB comprise the stator element of the flagellar motor complex. Required for rotation of the flagellar motor. Probable transmembrane proton channel (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28645
Sequence Length: 259
Subcellular Location: Cell inner membrane
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P28612 | MARKKKKKHEDEHVDESWLVPYADILTLLLALFIVLYASSSIDAAKFQMLSKSFNEVFTGGTGVLDYSSVTPPENESDGIDEVKKEKEEKEKNKKEKEKAADQEELENVKSQVEKFIKDKKLEHQLETKMTSEGLLITIKDSIFFDSGKATIRKEDVPLAKEISNLLVINPPRNIIISGHTDNMPIKNSEFQSNWHLSVMRAVNFMGLLIENPKLDAKVFSAKGYGEYKPVASNKTAEGRSKNRRVEVLILPRGAAETNEK | Function: MotA and MotB comprise the stator element of the flagellar motor complex. Required for the rotation of the flagellar motor. Might be a linker that fastens the torque-generating machinery to the cell wall (By similarity).
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 29483
Sequence Length: 261
Subcellular Location: Cell membrane
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P0CAX7 | MINVQAKPAAAASLAAIAIAFLAGCSSTKPVSQDTSPKPATSPAAPVTTAAMADPAADLIGRGCAQYAAQNPTGPGSVAGMAQDPVATAASNNPMLSTLTSALSGKLNPDVNLVDTLNGGEYTVFAPTNAAFDKLPAATIDQLKTDAKLLSSILTYHVIAGQASPSRIDGTHQTLQGADLTVIGARDDLMVNNAGLVCGGVHTANATVYMIDTVLMPPAQ | Function: Induces expression of human (host) matrix metalloproteinase-9 (MMP9) in a TLR1/TLR2-dependent fashion; the acylated 20 first mature residues (residues 25-40) induce the most expression, but whole recombinant protein (non-acylated and non-glycosylated), and mannosylated but not acylated protein (residues 26-220) also induce expression .
PTM: O-glycosylated. Contains 0-3 mannose residues attached to residues 48-49 in various configurations; the dominant glycoform is Thr-48(Man)/Thr-49(Man2) with an unusual Man(1->3)Man linkage, but Thr48(Man3)/Thr49(Man0) through to Thr48(Man0/)Thr49(Man3) are also seen .
Location Topology: Lipid-anchor
Sequence Mass (Da): 22070
Sequence Length: 220
Subcellular Location: Cell membrane
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Q2M385 | MNNFRATILFWAAAAWAKSGKPSGEMDEVGVQKCKNALKLPVLEVLPGGGWDNLRNVDMGRVMELTYSNCRTTEDGQYIIPDEIFTIPQKQSNLEMNSEILESWANYQSSTSYSINTELSLFSKVNGKFSTEFQRMKTLQVKDQAITTRVQVRNLVYTVKINPTLELSSGFRKELLDISDRLENNQTRMATYLAELLVLNYGTHVTTSVDAGAALIQEDHLRASFLQDSQSSRSAVTASAGLAFQNTVNFKFEENYTSQNVLTKSYLSNRTNSRVQSIGGVPFYPGITLQAWQQGITNHLVAIDRSGLPLHFFINPNMLPDLPGPLVKKVSKTVETAVKRYYTFNTYPGCTDLNSPNFNFQANTDDGSCEGKMTNFSFGGVYQECTQLSGNRDVLLCQKLEQKNPLTGDFSCPSGYSPVHLLSQIHEEGYNHLECHRKCTLLVFCKTVCEDVFQVAKAEFRAFWCVASSQVPENSGLLFGGLFSSKSINPMTNAQSCPAGYFPLRLFENLKVCVSQDYELGSRFAVPFGGFFSCTVGNPLVDPAISRDLGAPSLKKCPGGFSQHPALISDGCQVSYCVKSGLFTGGSLPPARLPPFTRPPLMSQAATNTVIVTNSENARSWIKDSQTHQWRLGEPIELRRAMNVIHGDGGGLSGGAAAGVTVGVTTILAVVITLAIYGTRKFKKKAYQAIEERQSLVPGTAATGDTTYQEQGQSPA | Function: Plays a key role in the innate immune response following bacterial infection by inserting into the bacterial surface to form pores (By similarity). By breaching the surface of phagocytosed bacteria, allows antimicrobial effectors to enter the bacterial periplasmic space and degrade bacterial proteins such as superoxide dismutase sodC which contributes to bacterial virulence (By similarity). Shows antibacterial activity against a wide spectrum of Gram-positive, Gram-negative and acid-fast bacteria . Reduces the viability of the intracytosolic pathogen L.monocytogenes by inhibiting acidification of the phagocytic vacuole of host cells which restricts bacterial translocation from the vacuole to the cytosol (By similarity). Required for the antibacterial activity of reactive oxygen species and nitric oxide (By similarity).
PTM: Monoubiquitinated in response to bacterial infection; ubiquitination is required for vesicular localization and antibacterial activity and can be blocked by bacterial cell cycle inhibiting factor (cif) (By similarity).
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 78587
Sequence Length: 716
Subcellular Location: Cytoplasmic vesicle membrane
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Q752H4 | MKGLILVGGYGTRLRPLTLTVPKPLVEFCNRPMILHQIEALAAAGVTDIVLAVNYRPEVMVETLKKYEKQYGVSITFSVETEPLGTAGPLKLAEKVLKKDNSPFFVLNSDVICEYPFKELAAFHRAHGGKGTIVATKVDEPSKYGVIVHDIATPNLIDRFVEKPVEFVGNRINAGLYILNPEVIDLIELRPTSIEKETFPILVEQKSLYSFDLEGYWMDVGQPKDFLAGTVLYLNSLSKRHPEQLAKGDNIVGNVIIDPSAKISGSAKLGPDVVIGPNVTIGEGVRITRSVVLSDSTINDHSLVKSTIVGWHSTVGKWCRLEGCSVLGDDVEVKDEVYVNGGKVLPHKSISANVPKEAIIM | Function: Involved in cell wall synthesis where it is required for glycosylation. Involved in cell cycle progression through cell-size checkpoint (By similarity).
Catalytic Activity: alpha-D-mannose 1-phosphate + GTP + H(+) = diphosphate + GDP-alpha-D-mannose
Sequence Mass (Da): 39471
Sequence Length: 361
Pathway: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; GDP-alpha-D-mannose from alpha-D-mannose 1-phosphate (GTP route): step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.7.13
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Q4U3E8 | MKALILVGGFGTRLRPLTLTLPKPLVEFGNRPMILHQVESLAAAGVTDIVLAVNYRPDVMVAALKKYEEQYNVRIEFSVESEPLGTAGPLKLAEKILGKDDSPFFVLNSDIICDYPFKQLAEFHKKHGDEGTIVVTKVDEPSKYGVVVHKPNHPSRIDRFVEKPVEFVGNRINAGIYILNPSVLKRIELRPTSIEQETFPAICSDGQLHSFDLEGFWMDVGQPKDFLTGTCLYLTSLAKRNSKLLAPNSEPYVYGGNVMVDPSAKIGKNCRIGPNVVIGPNVVVGDGVRLQRCVLLENSKVKDHAWIKSTIVGWNSSVGKWARLENVTVLGDDVTIADEVYVNGGSILPHKSIKQNIDVPAIIM | Function: Involved in cell wall synthesis where it is required for glycosylation. Involved in cell cycle progression through cell-size checkpoint (By similarity).
Catalytic Activity: alpha-D-mannose 1-phosphate + GTP + H(+) = diphosphate + GDP-alpha-D-mannose
Sequence Mass (Da): 40124
Sequence Length: 364
Pathway: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; GDP-alpha-D-mannose from alpha-D-mannose 1-phosphate (GTP route): step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.7.13
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O93827 | MKGLILVGGYGTRLRPLTLTLPKPLVEFGNRPMILHQIEALAAAGVTDIVLAVNYRPEVMVSTLKKYEEEYGVSITFSVEEEPLGTAGPLKLAEEVLKKDDSPFFVLNSDVICDYPFKELADFHKAHGAAGTIVATKVDEPSKYGVIVHDRDTPNLIDRFVEKPVEFVGNRINAGLYILNPSVIDLIEMRPTSIEKETFPILVEQKQLYSFDLEGYWMDVGQPKDFLSGTCLYLTSLSKKHPEKLCKEKYVHGGNVLIDPTAKIHPSALIGPNVTIGPNVVVGEGARIQRSVLLANSQVKDHAWVKSTIVGWNSRIGKWARTEGVTVLGDDVEVKNEIYVNGAKVLPHKSISSNVEKESIIM | Function: Involved in cell wall synthesis where it is required for glycosylation. Involved in cell cycle progression through cell-size checkpoint (By similarity).
Catalytic Activity: alpha-D-mannose 1-phosphate + GTP + H(+) = diphosphate + GDP-alpha-D-mannose
Sequence Mass (Da): 39975
Sequence Length: 362
Pathway: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; GDP-alpha-D-mannose from alpha-D-mannose 1-phosphate (GTP route): step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.7.13
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A6QQZ7 | MPALSTGSGNDTGLYELLVALPAQLQPHVDSQEDLTFLWDVFGEKSLHSLVKIHEKLHYYEKQNPVPILQGAAALADDLAEELQNKPLNSEIRELLKLLSKPNVKALLSVHDTVAQKNYDPVLPPMPDDIDNEEDSVKIIRLVKNREPLGATIKKDEQTGAIVVARIMRGGAADRSGLIHVGDELREVNGIPVEDKRPEEIIQILAQSQGAITFKIIPSIKEETPSKEGKMFIKALFDYDPNEDKAIPCKEAGLSFKKGDILQIMSQDDATWWQAKHEGDANPRAGLIPSKHFQERRLALRRPEILVQPLKVSSRKSSGFRRSFRLSRKDKKTNKSMYECKRSDQYDTADVPTYEEVTPYRRQTNEKYRLVVLVGPVGVGLNELKRKLLISDTQHYGVTVPHTTRPRRSQESDGVEYIFISKHLFETDVQNNKFIEYGEYKNNYYGTSIDSVRSVLAKNKVCLLDVQPHTVKHLRTLEFKPFVIFIKPPSIERLRETRKNAKIISSRDDQGAAKPFTEDDFQEMIKSAQIMESQYGHLFDKTIVNDDLAVAFNELKTTFDKLETDTHWVPVSWLHS | Function: Acts as an important adapter that promotes epithelial cell polarity and tight junction formation via its interaction with DLG1. Involved in the assembly of protein complexes at sites of cell-cell contact (By similarity).
PTM: Phosphorylated by aPKC which promotes dissociation from the cell cortex.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 65534
Sequence Length: 576
Domain: The phospho-regulated basic and hydrophobic (PRBH) motif is sufficient and important for interaction with phospholipids permitting cortical localization (By similarity). Phosphorylation of the PRBH motif by aPKC inhibits the association of the protein with the cortical membrane (By similarity).
Subcellular Location: Membrane
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Q5T2T1 | MPALSTGSGSDTGLYELLAALPAQLQPHVDSQEDLTFLWDMFGEKSLHSLVKIHEKLHYYEKQSPVPILHGAAALADDLAEELQNKPLNSEIRELLKLLSKPNVKALLSVHDTVAQKNYDPVLPPMPEDIDDEEDSVKIIRLVKNREPLGATIKKDEQTGAIIVARIMRGGAADRSGLIHVGDELREVNGIPVEDKRPEEIIQILAQSQGAITFKIIPGSKEETPSKEGKMFIKALFDYNPNEDKAIPCKEAGLSFKKGDILQIMSQDDATWWQAKHEADANPRAGLIPSKHFQERRLALRRPEILVQPLKVSNRKSSGFRKSFRLSRKDKKTNKSMYECKKSDQYDTADVPTYEEVTPYRRQTNEKYRLVVLVGPVGVGLNELKRKLLISDTQHYGVTVPHTTRARRSQESDGVEYIFISKHLFETDVQNNKFIEYGEYKNNYYGTSIDSVRSVLAKNKVCLLDVQPHTVKHLRTLEFKPYVIFIKPPSIERLRETRKNAKIISSRDDQGAAKPFTEEDFQEMIKSAQIMESQYGHLFDKIIINDDLTVAFNELKTTFDKLETETHWVPVSWLHS | Function: Acts as an important adapter that promotes epithelial cell polarity and tight junction formation via its interaction with DLG1. Involved in the assembly of protein complexes at sites of cell-cell contact.
PTM: Phosphorylated by aPKC which promotes dissociation from the cell cortex.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 65524
Sequence Length: 576
Domain: The phospho-regulated basic and hydrophobic (PRBH) motif is sufficient and important for interaction with phospholipids permitting cortical localization . Phosphorylation of the PRBH motif by aPKC inhibits the association of the protein with the cortical membrane .
Subcellular Location: Membrane
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Q8BVD5 | MPALATGSACDMGLYELLAALPAQLQPHVDSQEDLTFLWDVFGEKSLHSLVKIHEKLHCYEKQNPLPILHGAAALADDLTEELQNKLPNSEIRELLKLLSKPNVKALLSVHDTVAQKSYDPVLPPVPDDIDDEEDSVKIIRLVKNSEPLGATIKKDEQTGAITVARIMRGGAADRSGLIHVGDELREVNGIPVEDKRPEEIIKILSQSKGAITFKIIPSTKEETPSKEGKIFIKALFDYDPKEDKAIPCKEAGLSFRKGDILQIMSQDDVTWWQAKHEGDANPRAGLIPSKHFQERRLALRRPEIVVQPLKLSNTKSSGFRRSFRLSRKNKKINKSMYECKKSEQYDTADVPTYEEVTPYRRQIHDKYRLIVLVGPVGVGLNELKRKLLMSDAQHYGVIVPHTTRARRSQESDGVEYIFISKHLFETDVQINKFIEYGEYKNNYYGTSIDSVRSVLAKNKVCLLDVQPHTVKHLRTLEFKPYVIFIKPPSIERLRETRKNAKIISSRDDQGTAKPFTEEDFQEMIKSAQIMESQYGHLFDKIIINDDLTVAFNELKTTFDKLETDTHWVPVSWLHS | Function: Acts as an important adapter that promotes epithelial cell polarity and tight junction formation via its interaction with DLG1. Involved in the assembly of protein complexes at sites of cell-cell contact (By similarity).
PTM: Phosphorylated by aPKC which promotes dissociation from the cell cortex.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 65540
Sequence Length: 576
Domain: The phospho-regulated basic and hydrophobic (PRBH) motif is sufficient and important for interaction with phospholipids permitting cortical localization (By similarity). Phosphorylation of the PRBH motif by aPKC inhibits the association of the protein with the cortical membrane (By similarity).
Subcellular Location: Membrane
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Q99549 | MEQVAEGARVTAVPVSAADSTEELAEVEEGVGVVGEDNDAAARGAEAFGDSEEDGEDVFEVEKILDMKTEGGKVLYKVRWKGYTSDDDTWEPEIHLEDCKEVLLEFRKKIAENKAKAVRKDIQRLSLNNDIFEANSDSDQQSETKEDTSPKKKKKKLRQREEKSPDDLKKKKAKAGKLKDKSKPDLESSLESLVFDLRTKKRISEAKEELKESKKPKKDEVKETKELKKVKKGEIRDLKTKTREDPKENRKTKKEKFVESQVESESSVLNDSPFPEDDSEGLHSDSREEKQNTKSARERAGQDMGLEHGFEKPLDSAMSAEEDTDVRGRRKKKTPRKAEDTRENRKLENKNAFLEKKTVPKKQRNQDRSKSAAELEKLMPVSAQTPKGRRLSGEERGLWSTDSAEEDKETKRNESKEKYQKRHDSDKEEKGRKEPKGLKTLKEIRNAFDLFKLTPEEKNDVSENNRKREEIPLDFKTIDDHKTKENKQSLKERRNTRDETDTWAYIAAEGDQEVLDSVCQADENSDGRQQILSLGMDLQLEWMKLEDFQKHLDGKDENFAATDAIPSNVLRDAVKNGDYITVKVALNSNEEYNLDQEDSSGMTLVMLAAAGGQDDLLRLLITKGAKVNGRQKNGTTALIHAAEKNFLTTVAILLEAGAFVNVQQSNGETALMKACKRGNSDIVRLVIECGADCNILSKHQNSALHFAKQSNNVLVYDLLKNHLETLSRVAEETIKDYFEARLALLEPVFPIACHRLCEGPDFSTDFNYKPPQNIPEGSGILLFIFHANFLGKEVIARLCGPCSVQAVVLNDKFQLPVFLDSHFVYSFSPVAGPNKLFIRLTEAPSAKVKLLIGAYRVQLQ | Function: Heterochromatin component that specifically recognizes and binds methylated 'Lys-9' of histone H3 (H3K9me) and promotes recruitment of proteins that mediate epigenetic repression . Mediates recruitment of the HUSH complex to H3K9me3 sites: the HUSH complex is recruited to genomic loci rich in H3K9me3 and is required to maintain transcriptional silencing by promoting recruitment of SETDB1, a histone methyltransferase that mediates further deposition of H3K9me3, as well as MORC2 . Binds H3K9me and promotes DNA methylation by recruiting DNMT3A to target CpG sites; these can be situated within the coding region of the gene . Mediates down-regulation of CDH1 expression . Also represses L1 retrotransposons in collaboration with MORC2 and, probably, SETDB1, the silencing is dependent of repressive epigenetic modifications, such as H3K9me3 mark. Silencing events often occur within introns of transcriptionally active genes, and lead to the down-regulation of host gene expression . The HUSH complex is also involved in the silencing of unintegrated retroviral DNA by being recruited by ZNF638: some part of the retroviral DNA formed immediately after infection remains unintegrated in the host genome and is transcriptionally repressed .
PTM: Phosphorylated in M (mitotic) phase. Phosphorylation by CDK1 promotes dissociation from chromatin.
Sequence Mass (Da): 97182
Sequence Length: 860
Domain: The chromo domain mediates interaction with methylated 'Lys-9' of histone H3 (H3K9me), with the highest affinity for the trimethylated form (H3K9me3).
Subcellular Location: Nucleus
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Q3TYA6 | MAAAAEEGMSAAALVMSVPDSIGRSPESEGVGAGDEEKDAATKGTVAVGDSEEDGEDVFEVERILDMKCEGGKNLYKVRWKGYTSEDDTWEPEVHLEDCKEVLLEFRKKLAENKAKAVRKDIQRLSLNNDIFEADSDSDQQSDTKEDISPRKKKKKIKCKEETSPEDLRKKRTKMGKLKDKFKTELESTSEIIGFDVKTKKRIWEVKEELKDSKKPKKDEIKETKELKKANKRAEVRDLKIKIREDVKENRKTKKERYIESPLESESPNDSLILEDDSEDFISDNREENQNVRSVRDKTAQETVQEGIFEKHLDDLISIEEDAGTRVRRKKTKPRKFEEPKEIKKLESTNAFLERRAIPKKQRNQDKGISNLELNKLPSPVFAQTLKSSRLSGEEKSLKSPDLAEEEKEKKNEPKGKYQKRYDLDKEEKARKEPKVLKSFKEIRNAFDLFKKTTEEKNDVLENNSKREEISLDSKIMNDNKTKDKCSLKEKRNTRDETDTWAYIAAEGDQEVSDSVCQTDETSDGRQPVLSLGMDLQLEWMKLEDFQKHLDGEDEPFITTNRIPNNLLRDAVKNGDYIAVKVALNSNEEYNLDQEDSTGMTLVMLAAAGGQDDLLRLLITKGAKVNGRQKNGTTALIHAAEKNFLTTVAILLEAGAFVNVQQSNGETALMKACKRGNSDIVRLVIECGADCNILSKHQNSALYFAKQCNNVLVYELLKSHLETLSRVAEETIRDYFESRLALLEPVFPIACHRLCEGPDFSTDFNYMPPQNMPEGSGVLLFIFHANFLGKDVIARLCGPCSVQAVVLNDKFQLPVFLDSHFVYSFSPVAGPNKLFIRLTEAPFAKVKLLIGAYRVQLQ | Function: Heterochromatin component that specifically recognizes and binds methylated 'Lys-9' of histone H3 (H3K9me) and promotes recruitment of proteins that mediate epigenetic repression. Mediates recruitment of the HUSH complex to H3K9me3 sites: the HUSH complex is recruited to genomic loci rich in H3K9me3 and is required to maintain transcriptional silencing by promoting recruitment of SETDB1, a histone methyltransferase that mediates further deposition of H3K9me3, as well as MORC2. Binds H3K9me and promotes DNA methylation by recruiting DNMT3A to target CpG sites; these can be situated within the coding region of the gene. Mediates down-regulation of CDH1 expression. Also represses L1 retrotransposons in collaboration with MORC2 and, probably, SETDB1, the silencing is dependent of repressive epigenetic modifications, such as H3K9me3 mark. Silencing events often occur within introns of transcriptionally active genes, and lead to the down-regulation of host gene expression. The HUSH complex is also involved in the silencing of unintegrated retroviral DNA by being recruited by ZNF638: some part of the retroviral DNA formed immediately after infection remains unintegrated in the host genome and is transcriptionally repressed.
PTM: Phosphorylated in M (mitotic) phase. Phosphorylation by CDK1 promotes dissociation from chromatin.
Sequence Mass (Da): 97467
Sequence Length: 858
Domain: The chromo domain mediates interaction with methylated 'Lys-9' of histone H3 (H3K9me), with the highest affinity for the trimethylated form (H3K9me3).
Subcellular Location: Nucleus
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Q9ZU25 | MYRTAASRARALKGVLTRSLRPARYASSSAVAETSSSTPAYLSWLSGGSRAALTSLDMPLQGVSLPPPLADKVEPSKLQITTLPNGLKIASETTPNPAASIGLYVDCGSIYEAPYFHGATHLLERMAFKSTLNRTHFRLVREIEAIGGNTSASASREQMSYTIDALKTYVPEMVEVLIDSVRNPAFLDWEVNEELRKMKVEIAELAKNPMGFLLEAIHSAGYSGPLASPLYAPESALDRLNGELLEEFMTENFTAARMVLAASGVEHEELLKVAEPLTSDLPNVPPQLAPKSQYVGGDFRQHTGGEATHFAVAFEVPGWNNEKEAVTATVLQMLMGGGGSFSAGGPGKGMHSWLYRRVLNEYQEVQSCTAFTSIFNDTGLFGIYGCSSPQFAAKAIELAAKELKDVAGGKVNQAHLDRAKAATKSAVLMNLESRMIAAEDIGRQILTYGERKPVDQFLKSVDQLTLKDIADFTSKVISKPLTMGSFGDVLAVPSYDTISSKFR | Function: Substrate recognition and binding subunit of the essential mitochondrial processing protease (MPP), which cleaves the mitochondrial sequence off newly imported precursors proteins.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 54402
Sequence Length: 503
Subcellular Location: Mitochondrion matrix
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O04308 | MYRTAASRAKALKGILNHNFRASRYASSSAVATSSSSSSWLSGGYSSSLPSMNIPLAGVSLPPPLSDHVEPSKLKTTTLPNGLTIATEMSPNPAASIGLYVDCGSIYETPQFRGATHLLERMAFKSTLNRSHFRLVREIEAIGGNTSASASREQMGYTIDALKTYVPEMVEVLIDSVRNPAFLDWEVNEELRKVKVEIGEFATNPMGFLLEAVHSAGYSGALANPLYAPESAITGLTGEVLENFVFENYTASRMVLAASGVDHEELLKVVEPLLSDLPNVPRPAEPKSQYVGGDFRQHTGGEATHFALAFEVPGWNNEKEAIIATVLQMLMGGGGSFSAGGPGKGMHSWLYLRLLNQHQQFQSCTAFTSVFNNTGLFGIYGCTSPEFASQGIELVASEMNAVADGKVNQKHLDRAKAATKSAILMNLESRMIAAEDIGRQILTYGERKPVDQFLKTVDQLTLKDIADFTSKVITKPLTMATFGDVLNVPSYDSVSKRFR | Function: Substrate recognition and binding subunit of the essential mitochondrial processing protease (MPP), which cleaves the mitochondrial sequence off newly imported precursors proteins.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 54053
Sequence Length: 499
Subcellular Location: Plastid
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Q8AVM3 | MWVLILLLAGMPPVLCIDISMHPDAFGVVGKSIKLKCSFTSSYPISDIVAVDWTYRQLNGGSTVTILHFQNKPYPILEGPFKDRIIWEGDVRRGDASISLTDLRLTDNGTLSCIVWNPPDVHGNVPQTKLTVTIENLFFQFNTVILLSALVFIPSALVSLLLLIRMRRSINRGRTKNLKWRKKSPIEESQDCVYDDNENTPLHPTLPQEQSPGCFMKFCLRCLDDSDED | Function: Mediates homophilic cell-cell adhesion.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 25865
Sequence Length: 229
Subcellular Location: Membrane
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O39519 | MERILYQVFPSDTNYSYDPPAVTAPSQGSSQTDFGKVVIALVVILVSVGVFYLAYTLFLKDCILLFKAKKQRTTTEIGFGQTPARNQDHPGP | Function: Involved in the viral transport within, and between cells.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 10172
Sequence Length: 92
Subcellular Location: Host membrane
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Q67593 | MDPYGSRPSHPDDGALHGILVAFIAVLCLIGCLWAAYRLFLKECLTDCSQHTSSGVVAGPRPAATGPTAVVVHNGAEAQRSSAF | Function: Involved in the viral transport within, and between cells.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 8751
Sequence Length: 84
Subcellular Location: Host membrane
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P0C648 | MDPQNALYYQPRVPTAAPTSGGVPWSRVGEVAILSFVALICFYLLYLWVLRDLILVLKARQGRSTEELIFGGQAVDRSNPIPNIPAPPSQGNPGPFVPGTG | Function: Involved in the viral transport within, and between cells.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 10906
Sequence Length: 101
Subcellular Location: Host membrane
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P10838 | MAVHVENLSDLAKTNDGVAVSLNRYTDWKCRSGVSEAPLIPASMMSKITDYAKTTAKGNSVALNYTHVVLSLAPTIGVAIPGHVTVELINPNVEGPFQVMSGQTLSWSPGAGKPCLMIFSVHHQLNSDHEPFRVRITNTGIPTKKSYARCHAYWGFDVGTRHRYYKSEPARLIELEVGYQRTLLSSIKAVEAYVQFTFDTSRMEKNPQLCTKSNVNIIPPKAETGSIRGIAPPLSVVPNQGRESKVLKQKGGTGSKTTKLPSLEPSSGSSSGLSMSRRSHRNVLNSSIPIKRNQDGNWLGDHLSDKGRVTDPNPERL | Function: Plays an essential role in cell-to-cell movement and long-distance transport of the viral genome. Mechanistically, movement protein is recruited by viral replicase complexes formed on RNA1 to punctate structures on the host cortical endoplasmic reticulum. In turn, interacts with the viral genome and mediates virion movement from cell to cell. Acts also as a suppressor of RNA-mediated gene silencing, also known as post-transcriptional gene silencing (PTGS), a mechanism of plant viral defense that limits the accumulation of viral RNAs.
Sequence Mass (Da): 34647
Sequence Length: 317
Domain: The C-terminal domain is essential for localization to cortical punctate structures at an early stage of infection.
Subcellular Location: Host cell wall
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Q2SF51 | MTVKKADVLLVGGGVMSTTLGTMLMQLDPSLNIVMVERLDHVAHESTYGWNNAGTGHAGYCELNYTPETGDGDIEITRALAINASFEVSLQFWSYLVERGGLPSPDEFINTCPHESFVWGESDIAFLRKRHQLLSAHHLFKDMEFSDDPRTLQDWMPLVMEHRDPMQKVAATRVRYGSDVDFGSLTRNMVEHLQKNANFELLLSHPVKSLKQTSDGRWNVQLSDSRNGGSKTIDAGFVFLGAGGGALPLLQKSGIAEGDGYGGFPVSGQWLVCKKPDIVKRHYAKVYGKAAIGAPPMSVPHLDTRIINGEPALLFGPYAGFTTKFLKTGSSFDLFGSIRANNFGPIMSVGINNMDLTRYLIKEAMQSHSDRVKSLLNYFPEAKEDDWTLAEAGQRVQIIKRDAQGRGKLEFGTELVASKDGTLAALLGASPGASVAVKAMVDVIERCFKDRLSSADWTAKLKEMIPSYGESLVDNAELLHSVRSRTLSVLGLDKKRL | Catalytic Activity: (S)-malate + a quinone = a quinol + oxaloacetate
Sequence Mass (Da): 54587
Sequence Length: 497
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; oxaloacetate from (S)-malate (quinone route): step 1/1.
EC: 1.1.5.4
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Q9Z9Q7 | MSSIQNKTDVILIGAGIMSATLGSLLKELKPEWEIKVFEKLANAGEESSNEWNNAGTGHAALCELNYTAEKSDGTIDISKAVKINEQFQISRQFWAYLVSQNLISNPQDFIMPIPHMSLVQGEDNVAYLKKRFKALSNIPLFEGMEFSNDPEKLKEWIPLVMEGRTSNEPIAATKIDSGTDVNFGALTRMLFEHLKEQNVEVHYKHSVKDIKRTSDGSWSVKVQEIESGTIEYHTANFVFIGGGGGSLPLLQKTGIPESKNIGGFPVSGLFMVCNNPEVVEQHHAKVYGKAKVGAPPMSVPHLDTRYIDNKKSLLFGPFAGFSPKFLKTGSNFDLIGSVKPYNVFTMLAAGAKEMSLTKYLIQQVMLSKEKRMAELREFMPNAKSEDWDIVVAGQRVQVIKDTEAGGKGTLQFGTEVVSSADGSIAALLGASPGASTAVHVMLEVLEKCFPHHMLEWQPKIKEMIPSYGVSLAENRELFQEIHQSTAEALGLSEKELVHS | Catalytic Activity: (S)-malate + a quinone = a quinol + oxaloacetate
Sequence Mass (Da): 55081
Sequence Length: 500
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; oxaloacetate from (S)-malate (quinone route): step 1/1.
EC: 1.1.5.4
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O24913 | MSMEFDAVIIGGGVSGCATFYTLSEYSSLKRVAIVEKCSKLAQISSSAKANSQTIHDGSIETNYTPEKAKKVRLSAYKTRQYALNKGLQNEVIFETQKMAIGVGDEECEFMKKRYESFKEIFVGLEEFDKQKIKELEPNVILGANGIDRHENIIGHGYRKDWSTMNFAKLSENFVEEALKLKPNNQVFLNFKVKKIEKRNDTYAVISEDAEEVYAKFVLVNAGSYALPLAQSMGYGLDLGCLPVAGSFYFVPDLLRGKVYTVQNPKLPFAAVHGDPDAVIKGKTRIGPTALTMPKLERNKCWLKGISLELLKMDLNKDVFKIAFDLMSDKEIRNYVFKNMVFELPIIGKRKFLKDAQKIIPSLSLEDLEYAHGFGEVRPQVLDRTKRKLELGEKKICTHKGITFNMTPSPGATSCLQNALVDSQEIAAYLGESFELERFYKDLSPEELEN | Cofactor: The FAD is tightly bound.
Function: Catalyzes oxidation of malate to oxaloacetate in the citric acid cycle. Donates electrons to quinones of the electron transfer chain.
Catalytic Activity: (S)-malate + a quinone = a quinol + oxaloacetate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 50713
Sequence Length: 450
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; oxaloacetate from (S)-malate (quinone route): step 1/1.
Subcellular Location: Cell membrane
EC: 1.1.5.4
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