ids
stringlengths 6
10
| seqs
stringlengths 11
1.02k
| texts
stringlengths 108
11.1k
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Q9XFM6 | MALELWQTLKEAIHAYTGLSPVVFFTALALAFAIYQVISGWFASPFDDVNRHQRARSLAQEEEPPIPQPVQVGEITEEELKQYDGSDPQKPLLMAIKHQIYDVTQSRMFYGPGGPYALFAGKDASRALAKMSFEEKDLTWDVSGLGPFELDALQDWEYKFMSKYAKVGTVKVAGSEPETASVSEPTENVEQDAHVTTTPGKTVVDKSDDAPAETVLKKEE | Function: MSBP1 can bind to multiple steroid compounds with different affinities. Negatively regulates cell elongation and brassinosteroid signaling. May act as a coreceptor with BAK1 and enhances its endocytosis.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 24405
Sequence Length: 220
Domain: The cytochrome b5 heme-binding domain lacks the conserved iron-binding His residues at positions 109 and 133.
Subcellular Location: Cell membrane
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Q9FVZ7 | MAAAVAELWETLKQAIVAYTGLSPAAFFTAVAAAAALYHVVSGIFAGPPPPPPPRPRDEPEAEPLPPPVQLGEVSEEELRQYDGSDPKKPLLMAIKGQIYDVTQSRMFYGPGGPYALFAGKDASRALAKMSFEPQDLTGDISGLGPFELDALQDWEYKFMGKYVKVGTVKKTVPVEDGAPSTSPETTETAAAAEPEKAPATEEKPREVSSEEVKEKEDAVAAAAPDEGAKES | Function: Binds multiple steroid compounds (By similarity). May act as a coreceptor with SERL2 and enhance its endocytosis (Probable).
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 24635
Sequence Length: 232
Domain: The cytochrome b5 heme-binding domain lacks the conserved iron-binding His residues at positions 108 and 132.
Subcellular Location: Cell membrane
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Q03455 | MNLQELLAKVPLLLSYPTIILSSNLIVPSHNDLISRAASTSAAEYADEKLIFFSTDHAIRLIFLPTFVASSFNLFAHYFNFINYSSRRKYYVLFTAIYFLSILTAIFHPIQSTCITLLIIKLLTTADESSPKIALNFKTILKTFVPFITLTLVILRWDPSFDASSGDVNKISTSLAAYALLILTLRYASPLILSTLSSSIGVVSKDTSVAQHSISRNKRFPLILVLPIFSFVLLYLMTIVNKTYNIQLLMVFVFFGCLSIFFLSLKDLFTEDGNQKKGGQEDEYCRMFDIKYMISYLWLTRFTILLTGIMAIVVHFLSFNEITSSIKTDLLSLLFVVVAEYVSSFSNKQPDSHSHNHAHHHSHLTDSLPLENESMFKQMALNKDTRSIFSFLLLNTAFMFVQLLYSFRSKSLGLLSDSLHMALDCTSLLLGLIAGVLTKKPASDKFPFGLNYLGTLAGFTNGVLLLGIVCGIFVEAIERIFNPIHLHATNELLVVATLGLLVNLVGLFAFDHGAHDHGGTDNENMKGIFLHILADTLGSVGVVISTLLIKLTHWPIFDPIASLLIGSLILLSALPLLKSTSANILLRLDDKKHNLVKSALNQISTTPGITGYTTPRFWPTESGSSGHSHAHTHSHAENHSHEHHHDQKNGSQEHPSLVGYIHVQYVDGENSTIIKKRVEKIFENVSIKAWVQVEPQNSTCWCRATSMNTISANPNSLPLQPIAN | Function: Probably act as a zinc ion transporter moving zinc from the nucleus/endoplasmic reticulum to the cytoplasm. Involved in zinc ion homeostasis and cellular distribution.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 80578
Sequence Length: 724
Subcellular Location: Endoplasmic reticulum membrane
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Q74ZL3 | MVHLPLSRSRSGRRAVPDLSRYQQFYEADAADGYSTGSGLSSAAASVASLRRPGVGMGRTQSLTGYGRTRSLGAARPSYLGAPPRTYSMSSQRRANSLRSNNGFGPPAVAAGNTITVKTTETKDLQGRTRTVTRQTVKHINGVRYVETTTTMTMPDGEYPDDFYGFEGDFTAKQTSSGHVYQNARGAPDISDIAEEESLEEYLDARDTAPALRIQLRAPPRVQQQRQLQRQRRLSDTNFPARRSAKSSPARQSSEEPPATTKPHRIRFDETPQIVGIDPPTQKKAPKKQMTEQEMYMHALDAARKKVYGEISQPALEAKQPHRSTMSKRMTLRDEATLAANTPPERSRPAKREVRKKEGHSHHNFLSVLRRDSSPKRHAVQPSERVHNKEKTLEMTPDSSSASSYEEARFEHSDEMYNKALEVAKKKYHLTQENSTRDNGTTECPRTPMTSLMSTNVSSDTAESTLLGTPVYSSNAPFDRSPQPSSGCETGNTTPKSIPRRPSFLDKLVRFSQEKYGYRPRRSISSQGHKAEHEHVFTDDIPPLPDIPLVDPMQVKPKDVPLPTVEPALGPTDVSPARVADPESNIETPRTLAPARSSISSSPRRSSPPQAFQELVPLQSTQSETTGDLADALALGDNSLDLLPGRVSEISPKTSFEHFVLAPEVPETDEKPAAAPAVAAEAPLSNPPSVVVVPSATSSVPAAQGAAPGVAVTEGPSLGGPAAPVRALHATKTAAAPAKKRSFFHKLFKKY | Function: May be involved in the control of meiotic sister-chromatid recombination.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 81930
Sequence Length: 751
Subcellular Location: Cell membrane
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Q6FX33 | MGFLTKKERRVPDLSRYDYHYQNKPAVDSSKYYVPREYGGKRLSASAAAAAIYTNPNPNATGVSRSYSLMHSYNPAAARQPPAGRTYSLRSDRASSITSNSRRPAAGKAQVRRASTQQRRASVDQELGTGVNQPRTNSITVTTTKVRDPQGRTKSITKKTVRRINGYEVVETTTTTTTTEPLPTQNGKMPANMDLVSVEDGTDVEEEHDDGLPSPQAHFDEFSGDFVAEDDLSSEVLQHQQQQYIEDIVEEETEEEEDPGHTGTKRLPGEFNEPPRTNIAARRSNSLTGSLSSLGAKKTISEEVPLDQTSSVSKFSDAMEYIPPTTTTAKPKKSNLRNSMTARKLAQPQQGQNQRRTVSFTQGSIDHMNTTKKKKQPLTEQEMYLQALEVAKKKVYKTDDPAVVGNAANNSNKRVSTMGKRMTLRDSAPVPRSSSMMMNKFHDQGSARNNVAQQQTDVRRSKSMTGSAVPPQAGKKKLTDEEMYEKALEIAQKRYNDLVSADTAAVGAASVGAASAATPVASTAPKKSGFKQRFTKTFHTDDNKSKINNASAGGMVSGGAAAVEVAPGVTTTDPVVAENVNEASQIERMDNVEMASASAANEYAAPAAGFRATSAPLYQSRSAEPVGAYAAPDAPISKYKIVDKILKFAQSNYGYQAHDDEEAAMVAPASAPATAPAGTSMAQPVVVPVERRSSVGKHGNTTTLPVETPLADNASESSFRHTHPQEQPVPLSQIEKKISVVSETGSRKAAPAATAAKTPATAPAMSYGTAKTPFIDIDAVDALSGHVPFEEATRHASVATAATAATGGTTGTAATTGTGTSKKKSFLRKLFGRK | Function: May be involved in the control of meiotic sister-chromatid recombination.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 89322
Sequence Length: 834
Subcellular Location: Cell membrane
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Q6CK58 | MVFGMNLGNRRKATRVPDLSRYDYHYNGSGGNSVNQGDNYLKSHELSADAAFAASARAGSLVNYPERGYTNISRANSLRMGHPGQQQQQSSYIPRSYSFTARGAYAPRTGNVGNRRSVSAIPRTGTASSRGVGSRTGSMTGSVARVGSRTGSFAGGGNGSIIIKTQEVKDMMGRTQSITTQTIRRINGMEYVETTTQTAGLVEDPQFHFQQFAENDEFPISDELSATPPAAPLSESQPRTNQRLANFNSNAINNSAANNIRSDSEEEGEEHFTDASDVVEESGAFAEDDQDHFLAKVNKVDVDNNSKSYTSRKPLVQKQGVQQQQEVQHQGISQVQNTEAKSVGRKSTMSKRMTLRDTPNAQLEPEKDTTDQATPDNNATKRKSIFKSKKRNEAVAVPTVPTSDQKTLSQEEMYAIALEIAQQKYGHPTKTVSHSTDNGSRNEMTPILEDADVEQPHVLPTTLHLPTREEQIQHEQLQQPTAAIPTNEKSRHPKKKVKSILDRVVQFSQENSGNQPPKQHRGKQYSQQPPDVAPSNGTTDNFDTNASGHNINHNNNNHNNNNNTSSSSSLRHESGANPVVVTEDTTVLAASTAATPVDVNEPGNPDHVIPASSPSIDNTPRINEKTKSKKKNEKGSFFKRLFKSNKTHINTK | Function: May be involved in the control of meiotic sister-chromatid recombination.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 71450
Sequence Length: 652
Subcellular Location: Cell membrane
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Q05812 | MVFGFTKRDRRVPDLSRYDYYYQNHEDYNKSPQLSAAAASAASAASPDRTNYSRSHSLVSHAPSIPRQRSSVKSPGRRLSTSSAAPPTSRAAAKQYSQKTYSLRSQRSGEYHLHPPGYTTNGSRMNSMTSGANVRRNYGKNKSTAGNNNDSRANSITVKTTQVTDPSGRTQSITKKTIRKINGYEYVETTTTTKNLVPLGDSQRHFDEFSENYMLQDDDILEEQASDNIHDIIEENETDNEKPYSPVSESHLQDDSELNVEKPDFPLGSYFHHKYSTDVMPLEEESSLSNFSDALDYIPPTHQTSSKYIHNKRKQASTTRRKKRPPAVKNAEAEAKKPLTEAEMYLKALEVAKRNVYHTDAASDNASAPLGSNKSRKSRMGQKMTLRSSSDSPTATANLVKSNVEVQPKRFTSSFFSRNTKSAPHEVHNHSVSTHFKSNKAVDPVPEPKSANTGLTDKEMYDQALKIAQARYYNSHGIQPEAVDNSTTAAKPRQVGVSHLGSTGSIPPNEQHYLGDSEIPVQSEVHEYEPIPLQKTKTTGSSKNKFKTMFDKVLQFSQENYGYQHKKEQGEQTPVTRNAEESFPAASISEGVTTAKPSSNEGVMTNPVVTDSPSPLQQQIDSTTASSNGQSQGNVPTSAVASTTRTRSPELQDNLKSSSSLLQDQTPQRQEDATDPTTSSTNELSAAEPTMVTSTHATKTIQAQTQDPPTKHKKSSFFTKLFKKKSSR | Function: May be involved in the control of meiotic sister-chromatid recombination.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 80530
Sequence Length: 728
Subcellular Location: Cell membrane
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Q5ZSH7 | MSLLKEFKEFAMRGNVMDLAVAVVMGVAFNKIVTALVDGIIMPCVGLLLGGINIAGLSFTVGDVQIKWGNFLQNVIDFIIVAFAIFVLIKLINLLQRKKANEPEPVTPEIQLLTEIRDLLARNSSKI | Function: Channel that opens in response to stretch forces in the membrane lipid bilayer. May participate in the regulation of osmotic pressure changes within the cell.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13941
Sequence Length: 127
Subcellular Location: Cell inner membrane
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B1MZU9 | MLSEFKTFIMRGNVLDLAVGVIIGGAFTGIVKSLTNNLISPIITFFTGGTSDLQNLKLVVTKELTFKYGAFLNDVINFLITAFVVFLLVKFVNRILRTNKKEEVKANPELEVLAEIRDLLEAQKKA | Function: Channel that opens in response to stretch forces in the membrane lipid bilayer. May participate in the regulation of osmotic pressure changes within the cell.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 14023
Sequence Length: 126
Subcellular Location: Cell membrane
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Q03SF6 | MLKEFKEFIARGNVMDLAVGVIVGAAFTAIVNSLVTNIINPLLGIFVGSIDFSNLVFTVGSAHFRYGAFINSVINFLIIAFVVFLLIKLINKLIAKPAEEPEEAVPSQEEKYLQEIVELLKQDKIEH | Function: Channel that opens in response to stretch forces in the membrane lipid bilayer. May participate in the regulation of osmotic pressure changes within the cell.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 14079
Sequence Length: 127
Subcellular Location: Cell membrane
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Q1WVR1 | MLKEFKEFISRGNVMDLAVGVIIGGAFTAIVNSLVKYIINPFLGLFVGAIDFSDLVFKIGNATFRVGSFLNAVINFLIIAFVVFLMVKGINKVLRQDKKEEAPAPKDPQLEVLEEIRDSLKKLDK | Function: Channel that opens in response to stretch forces in the membrane lipid bilayer. May participate in the regulation of osmotic pressure changes within the cell.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13891
Sequence Length: 125
Subcellular Location: Cell membrane
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Q929V3 | MKKMLVEFRDFALKGNVLDLAVAVVIGAAFGKIVSSLVNNIIMPFVGVLLGGLDFSDLSFKVGKSVIQYGAFIQSIVDFVIIAFAIFIFVKVLTSFIKKKEQPTEETPVPPTEEYLKEIRDLLKEQQK | Function: Channel that opens in response to stretch forces in the membrane lipid bilayer. May participate in the regulation of osmotic pressure changes within the cell.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 14242
Sequence Length: 128
Subcellular Location: Cell membrane
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Q5NNP2 | MSILTDFKNFISKGNVLGLGIAVIMGDAFNKIISSVTGDLLMPIIGAVFGGVDFSGFFIRLGAVPAGYTGSLTSYNDLKKAGVPLFGYGQFLTVVVNFVIVAFILFMIMKLAAKLQKELDKTEAKKEEKIAEAAPTPEDIVLLREIRDELRGKK | Function: Channel that opens in response to stretch forces in the membrane lipid bilayer. May participate in the regulation of osmotic pressure changes within the cell.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 16679
Sequence Length: 154
Subcellular Location: Cell inner membrane
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Q8R6L9 | MWADIYHKLVEIYDIKAVKFLLDVLKILIIAFIGIKFADFLIYRFYKLYSKSKIQLPQRKIDTLTSLTKNAVRYIIYFLAGASILKLFNIDMTSLLAVAGIGSLAIGFGAQNLVKDMISGFFIIFEDQFSVGDYVTINGISGTVEEIGLRVTKIRGFSDGLHIIPNGEIKMVTNLTKDSMMAVVNIAFPIDEDVDKIIEGLQEICEEVKKSRDDLIEGPTVLGITDMQDSKLVIMVYAKTQPMQKWAVERDIRYRVKKMFDQKNISFPYPRTTVILSEKKTN | Function: Mechanosensitive ion channel that participates in the regulation of osmotic pressure changes within the cell, opening in response to stretch forces in the membrane lipid bilayer, without the need for other proteins. Has high selectivity for anions, and may contribute to resistance to hypoosmotic shock.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32034
Sequence Length: 282
Domain: The C-terminal cytoplasmic domain is important for channel ion selectivity.
Subcellular Location: Cell inner membrane
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P0C0S2 | MEDLNVVDSINGAGSWLVANQALLLSYAVNIVAALAIIIVGLIIARMISNAVNRLMISRKIDATVADFLSALVRYGIIAFTLIAALGRVGVQTASVIAVLGAAGLAVGLALQGSLSNLAAGVLLVMFRPFRAGEYVDLGGVAGTVLSVQIFSTTMRTADGKIIVIPNGKIIAGNIINFSREPVRRNEFIIGVAYDSDIDQVKQILTNIIQSEDRILKDREMTVRLNELGASSINFVVRVWSNSGDLQNVYWDVLERIKREFDAAGISFPYPQMDVNFKRVKEDKAA | Function: Mechanosensitive channel that participates in the regulation of osmotic pressure changes within the cell, opening in response to stretch forces in the membrane lipid bilayer, without the need for other proteins. Contributes to normal resistance to hypoosmotic shock. Forms an ion channel of 1.0 nanosiemens conductance with a slight preference for anions. The channel is sensitive to voltage; as the membrane is depolarized, less tension is required to open the channel and vice versa. The channel is characterized by short bursts of activity that last for a few seconds.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30896
Sequence Length: 286
Subcellular Location: Cell inner membrane
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T0DVE4 | MDEIKTLLVDFFPQAKHFGIILIKAVIVFCIGFYFSFFLRNKTMKLLSKKDEILANFVAQVTFILILIITTIIALSTLGVQTTSIITVLGTVGIAVALALKDYLSSIAGGIILIILHPFKKGDIIEISGLEGKVEALNFFNTSLRLHDGRLAVLPNRSVANSNIINSNNTACRRIEWVCGVGYGSDIELVHKTIKDVIDTMEKIDKNMPTFIGITDFGSSSLNFTIRVWAKIEDGIFNVRSELIERIKNALDANHIEIPFNKLDIAIKNQDSSK | Function: Mechanosensitive channel that participates in the regulation of osmotic pressure changes within the cell, opening in response to stretch forces in the membrane lipid bilayer, without the need for other proteins. Contributes to normal resistance to hypoosmotic shock. Forms an ion channel of 1.0 nanosiemens conductance with a slight preference for anions.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30402
Sequence Length: 274
Subcellular Location: Cell inner membrane
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P0DKS1 | MNIYKEIDNASNWISDNHILFIKYISNIILSLIILIVGYSASKVTQKIIKNFMIKKNIDIIISEFFCSIIKYSILIFTIVTSLGCIGIQTTSIIAVIGAAGIAIGLALQGSLSNFAAGVLLVTLRYFRTGDYVNLCGVKGKIKTVQIFCTKIKTKDGKIIIIPNNKIISSNIINYSEELHRLMEVIISTEYTSDIKNVKEIIIDVLKKETRIVKEKKITVRLKNLGESSLDFLVRGWVYKKELKQTTSDILEKIKIELDKNKINIPYKQIDVNLKYSKEK | Function: Mechanosensitive channel that participates in the regulation of osmotic pressure changes within the cell, opening in response to stretch forces in the membrane lipid bilayer, without the need for other proteins. Contributes to normal resistance to hypoosmotic shock. Forms an ion channel of 1.0 nanosiemens conductance with a slight preference for anions.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31701
Sequence Length: 280
Subcellular Location: Cell inner membrane
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A6W733 | MTTTPQPPPQPDETPEGAAGAATAGRDPLEIAADLVDDVSRELDPAELASLERLDQPRRILFVHAHPDDESIGTGATMARYAEAGAGVVLLTATRGELGEVIPPELAHLDPDALAEHRTGELATAMEALGVSDHRFLTRPDGTGYRDSGMVWLEPGRAAAGDDVDPRSLAAADPEEVAARIAEVVREVRPQVVVTYEPGGGYGHPDHVRVHEATVRALVLAAGDGSRGAGGAVPWQVAKVYEIVQPERPVREALRRLAETGAEGAGDPEGPLPSVVVPDGEVTTVVDGTGQVPAKIAALRAHATQVTLDLDAAVPAMRLSNGVPQPVWPQEHYRLVHGVAGGPYDAEGRETDLFAGIAPSS | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the deacetylation of 1D-myo-inositol 2-acetamido-2-deoxy-alpha-D-glucopyranoside (GlcNAc-Ins) in the mycothiol biosynthesis pathway.
Catalytic Activity: 1D-myo-inositol 2-acetamido-2-deoxy-alpha-D-glucopyranoside + H2O = 1D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside + acetate
Sequence Mass (Da): 37748
Sequence Length: 361
EC: 3.5.1.103
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D2PN56 | MSELPDRRLLLVHAHPDDETINNGATMARYVAEGAHVTLVTCTLGEEGEVLVPELAHLAADQSDQLGRHRIGELAAAMDELGVTDHRFLGGPGRYRDTGMIYDEQGNAAVPPDTRPDSFWQADLVTAANDLVTVIREVRPQVLVTYDEFGNYGHPDHVQAHRVATYAAALAAARSYREDLGPAWDIPKIYWTAISETAMRSSLRRLRESGDHTTFEGMDPDGPLGPMITPDRFIDCVIPADGYLDRKMNAMKAHATQITVDGPFFALSNNDGNEIFGDEFYRLVKGTAAPGSDGLEHDLFAGL | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the deacetylation of 1D-myo-inositol 2-acetamido-2-deoxy-alpha-D-glucopyranoside (GlcNAc-Ins) in the mycothiol biosynthesis pathway.
Catalytic Activity: 1D-myo-inositol 2-acetamido-2-deoxy-alpha-D-glucopyranoside + H2O = 1D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside + acetate
Sequence Mass (Da): 33186
Sequence Length: 303
EC: 3.5.1.103
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A0R2I7 | MSSHESPRLLFVHAHPDDETLTTGGTIAHYVARSAEVHVVTCTLGEEGEVIGERYAQLAVDHADQLGGYRIAELTAALQSLGLRGPRYLGGAGHWRDSGMAGTPSRGRQRWVDADLDEAVGALVAVIGEVRPHVVVTYDPNGGYGHPDHIQTHVVTTRAVAAAPEAVGWTVPKFYWTVTAISAMTAGLQALGDVPSEWIRVNAEDIPFGFGDDQIDAVVDVTAELPAKVGAMRAHATQITVAPDGRAFALSNNIALPVLGEEHYVLVSGEAGPRDSRGWETDLLAGLDLE | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the deacetylation of 1D-myo-inositol 2-acetamido-2-deoxy-alpha-D-glucopyranoside (GlcNAc-Ins) in the mycothiol biosynthesis pathway.
Catalytic Activity: 1D-myo-inositol 2-acetamido-2-deoxy-alpha-D-glucopyranoside + H2O = 1D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside + acetate
Sequence Mass (Da): 30819
Sequence Length: 290
EC: 3.5.1.103
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D1BS17 | MRTWPTPDVPPLPRTGAPAPVLVHDSTTQSLVEAAPGATATLYACGITPYDATHLGHANTYLAFDLLQRAWLDAGKTVVYTSNVTDVDDPLLERATATGVDWRELAREQTELYRTDMTALRMLPPATWTGAVESIPAVVEAVTALLDAGAAYRVDADVYADLSADPGFGRVAGLDDATMRALFAERGGDPDRPGKKHPLDPALWRGEQPGEPSWDGGKLGPGRPGWHIECAVIARDGLGLPFDVQGGGADLLFPHHEMSTSHARLLAGGAARVHVHAGLLAYDGHKMSKSRGNLVFVSRLLAAGTDPMTVRLALLAHHYREEWEWTDVELRTAQRRLDTWTSAILSTHDDGEPADTVLDAVRAALAADLDAPAALAAVDRWAANPGGDAGVVVATVDALLGIEL | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the ATP-dependent condensation of GlcN-Ins and L-cysteine to form L-Cys-GlcN-Ins.
Catalytic Activity: 1D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside + ATP + L-cysteine = 1D-myo-inositol 2-(L-cysteinylamino)-2-deoxy-alpha-D-glucopyranoside + AMP + diphosphate + H(+)
Sequence Mass (Da): 43002
Sequence Length: 404
EC: 6.3.1.13
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A0LWI8 | MTVLPASIRIEPHGRLAPALLPRVFALVDDATDTDGVQPLSEHVVLHLRYGGDERGCNLLLWVDDDEPRLAGYAHLDATDPVEAPSAELVIAPDFRGRGLGTMLVEAILARTGGRLRLWAHGELPAAQAMARRLGFARRRVLLQMRRDLFAPLPPVTLPDDVQIRTFRPGADDDAWIALNARAFADHPEQGSWTLEDLHRRMQESWFDPDGFFLAERDGELVGFHWTKVHGSPAGQASNGSSGHGHEPLGEVYILGVDPKAQGLGLGRALTIVGLRYLRSRRLPHVMLYVDATNAPAIRLYESLGFRHWGTDVLFERGGTANGEGTS | Function: Catalyzes the transfer of acetyl from acetyl-CoA to desacetylmycothiol (Cys-GlcN-Ins) to form mycothiol.
Catalytic Activity: 1D-myo-inositol 2-(L-cysteinylamino)-2-deoxy-alpha-D-glucopyranoside + acetyl-CoA = CoA + H(+) + mycothiol
Sequence Mass (Da): 35940
Sequence Length: 327
EC: 2.3.1.189
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C7M077 | MHALTTVENPSARLLPGVLALIRDVEAADGHEVLEAHRWIDLANADAESLHGIAVTLDDDTVVGYVHLRRHHRHGIELELLVAPDHRDEAASIVGALVEAASASLETLGPHEIFAWVPRHSRQVIDALEGLGFRADRAVRQLRRPLPLESDHPARPIDCPPFRTFRPGEDEDAWLEVNNRAFAWHPDQGDWDLETLLARERESWFDPAGFLLAEQDGRLVGFCWTKVHAPRSSSALGEIYVIATDPERAPRGLGSCLLVAGLDYLAHHDIPTASLYVEDTNERALRLYDRFGFVVDHEDVRLVWRLPAAS | Function: Catalyzes the transfer of acetyl from acetyl-CoA to desacetylmycothiol (Cys-GlcN-Ins) to form mycothiol.
Catalytic Activity: 1D-myo-inositol 2-(L-cysteinylamino)-2-deoxy-alpha-D-glucopyranoside + acetyl-CoA = CoA + H(+) + mycothiol
Sequence Mass (Da): 34642
Sequence Length: 310
EC: 2.3.1.189
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Q5EDG0 | MSGDGEWRQELDEQQLEDVRRLLLAVREADGRPEVEPAGALPGEFDGGEHLVACVEGEVVGYAHLNTTGNSFGHQVAELFVHPAHRNRGYGAKLLQALDERAAVGFRVWAHGDHPAARKLALKTGLERKRELLILHVDVEGADWPEPILRDGVSLRTFVPGQDEDAVVRVNARAFDWHPEQGALTVEDVRADERRAWFDEDGFFLAEERGEVIGFHWTKVHEPTPGRFGGERVGEVYVVGVDPAAQGGGLGRALTLAGLRYLASRGLRQIILYVEGDNAAALAVYTKLGFTRHETDVQYGR | Function: Catalyzes the transfer of acetyl from acetyl-CoA to desacetylmycothiol (Cys-GlcN-Ins) to form mycothiol.
Catalytic Activity: 1D-myo-inositol 2-(L-cysteinylamino)-2-deoxy-alpha-D-glucopyranoside + acetyl-CoA = CoA + H(+) + mycothiol
Sequence Mass (Da): 33223
Sequence Length: 301
EC: 2.3.1.189
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C5C246 | MQAYDDEIVGTALASNVLALADRVRTADGVEALSEQHRLALEHPGLRAHHLVVTDPAGAVVGYASVLGSSVEMLVDAAHRGEGVGHRLAEAALAVEPTLAFWAHGDLPGAAQLAEAIGLRRVRELWHLGRDLAPAGAGGDEAALLATPLPGGERLRTFGGTEAEEHAWLALNARAFASHPEQGAMTLEDLRVREGETWFDPSLLWLVHDDGDGALLASMWLKVPDAATGEIYVLGVDPGAQGRGLGRALTDRALDVLRARGVDRVELYVEGENARARALYEHSGFTPVAVHAQYGIP | Function: Catalyzes the transfer of acetyl from acetyl-CoA to desacetylmycothiol (Cys-GlcN-Ins) to form mycothiol.
Catalytic Activity: 1D-myo-inositol 2-(L-cysteinylamino)-2-deoxy-alpha-D-glucopyranoside + acetyl-CoA = CoA + H(+) + mycothiol
Sequence Mass (Da): 31485
Sequence Length: 297
EC: 2.3.1.189
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C7MGB3 | MITTTALVPARRSAVRTLLATVTEHDGVSPLDEAALLALDGEDARHLLLTADGAATDTHAAEATAGSAASADPADPADPAAPADPADPADETLLGYVSVLGDGTVQGMVDPAHRRRGHGSALLRAALALRPDAGVWVHGALEGSLAFLTDAGLTETRRLLTLRRDLGGAQPLPSAPAPTLEGLRLDTFEESRDAEAWVAVNVRAFADHPEQGALTRADLEQRLAQPWFDAEDMLVALRDETLVGFVWIKREQPGATDRDAEIYVVATDPSVQGHRVAGHLMATVLERLERDGVPGVELYVEADNAPALRLYENWGFEVSGRDVQLRATERG | Function: Catalyzes the transfer of acetyl from acetyl-CoA to desacetylmycothiol (Cys-GlcN-Ins) to form mycothiol.
Catalytic Activity: 1D-myo-inositol 2-(L-cysteinylamino)-2-deoxy-alpha-D-glucopyranoside + acetyl-CoA = CoA + H(+) + mycothiol
Sequence Mass (Da): 35181
Sequence Length: 331
EC: 2.3.1.189
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C7QKH8 | MTGISIGVVRRPNEADVATIRSLAEAAERADGVAPLPEQVLLHLKRSGDADADADTDAWHFVARRLSPQGSELTGYAFLDKSNAEEGPTAEVVVLPDARRQGVGGALLDALRMKVRRGDKPIRVWSHGALPAAAALAAKRGLEPVRELWVMSRPLADVPPAPTPPDGIRIATFRPGVDDEAWVEVNARAFAHHPEQGSMTVQDLRDRMAEPWFDPEGFFLAWRGAKLAGFHWTKVHDHSAYGDGPVGEVYVVGLDPAEQGHGLGRTLTEVGLRHLHDRGLGEVILYVEADNTPAVAVYTKLGFTRRSADVMYQL | Function: Catalyzes the transfer of acetyl from acetyl-CoA to desacetylmycothiol (Cys-GlcN-Ins) to form mycothiol.
Catalytic Activity: 1D-myo-inositol 2-(L-cysteinylamino)-2-deoxy-alpha-D-glucopyranoside + acetyl-CoA = CoA + H(+) + mycothiol
Sequence Mass (Da): 34116
Sequence Length: 314
EC: 2.3.1.189
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D5UJR1 | MSSDIEAPTSLTSMRGALPPAVADDVRALHLTTVRHDGVPPLSEQPLLWLSDQEAPVVHVLAWHAVTGGAQELVGYAQVDVGSSTTARAELVVAPGHRRRGTGRSLLAHAAQEAASIPGRRLHVWAHGDLPAARATAAATGLVVVRELWRMAVDVTQHPPGAPQLPPGVAVRAFVPGQDEDAWRRVNARAFAHHPEQGRMTSADLRARESEPWFDPAGFLLAERDGQLLGSVWTKVHPGSEAPDGAPGEEVGEIYVVGVDPDAQGLGMGRALTALGLAHLRDRGLRTVILYTGAENTVAVHTYRRAGFARTAVDVMYGPPPAGSPAHGTPLVRVTDTPSSPGDATMGS | Function: Catalyzes the transfer of acetyl from acetyl-CoA to desacetylmycothiol (Cys-GlcN-Ins) to form mycothiol.
Catalytic Activity: 1D-myo-inositol 2-(L-cysteinylamino)-2-deoxy-alpha-D-glucopyranoside + acetyl-CoA = CoA + H(+) + mycothiol
Sequence Mass (Da): 36655
Sequence Length: 348
EC: 2.3.1.189
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B0RAV5 | MSAFPPPPEPDAPRVAHVEPAPDAVRGILALADRARADDGVAPFNEQTRLTLGADGGPTLLLAHGTDDDPLGAAVVAHGDAGIEAELVVDPAHRRRGVGRALLDAVLAEAAGSPVSVWAHGDHPAARALADATGLDRARELLQLRASVAEARTGLGERQMPAGVALSSFTADDADDWVALNARAFASHPEQGRMTRGDLDDRVAEAWFDPASLLLARDADGRLAGFHWLKVDGGQAEVYVLGVDPDRAARGLGSALLAAGLDLLAERGHDEVDLYVEADNTPALALYRRAAFRDAAVDVQYRRA | Function: Catalyzes the transfer of acetyl from acetyl-CoA to desacetylmycothiol (Cys-GlcN-Ins) to form mycothiol.
Catalytic Activity: 1D-myo-inositol 2-(L-cysteinylamino)-2-deoxy-alpha-D-glucopyranoside + acetyl-CoA = CoA + H(+) + mycothiol
Sequence Mass (Da): 31915
Sequence Length: 304
EC: 2.3.1.189
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C3PIU4 | MNIETNTVPQNLDLAQRVEELAAAAETHDGVAPLSEQFLIGLRDDRLGHRHLLAIEGDEVLGVAALDGQTVELFVGVDNRGRGIGKALVDALPASPQIWAHGNLPAAQALAKRNEMDVVRRLLVMAIEGRDLRAAEEAPTTVDGLEIQTYTESVERFGREHVEAEWVRTNNEAFSWHPEQGGWDLERLHRGMEAEWFDPADVLFLWDSHGGAHSAPTMAGFHWLKWHAEDTPAFGEVYVVGLAEDYRGRGLGGPLLTAGLQRMVEKGADKVILYVEADNDPAVKAYERLGFSIAEEHCVWAKSD | Function: Catalyzes the transfer of acetyl from acetyl-CoA to desacetylmycothiol (Cys-GlcN-Ins) to form mycothiol.
Catalytic Activity: 1D-myo-inositol 2-(L-cysteinylamino)-2-deoxy-alpha-D-glucopyranoside + acetyl-CoA = CoA + H(+) + mycothiol
Sequence Mass (Da): 33540
Sequence Length: 304
EC: 2.3.1.189
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Q6NFH9 | MKMIETSLASASAALRDRVDEILAAATREDGCAPLSESFLNGLRRADDGHVHSCVMDSHDQVVGVAARDGDSAEVVVDPAFRRQGYGSFLIRHVVSQGVKNVWAHGDGAGAKAVAKALQLEQTRQLLVMAVEGDRLVESAQLQVPSGFRVLALNEAYESIPDIEQQWLRVNNEAFEWHPEQGGWDSARLAQARDTQWFRESDVLFLIDTAKRTVAGFHWTKRHGDLAEGADGEVYVVGLGSAYRRRGLGDLLIRMGLHHLEYEHARRVILYVEGDNESARRAYDALGFHVVESHVTYSPQSSS | Function: Catalyzes the transfer of acetyl from acetyl-CoA to desacetylmycothiol (Cys-GlcN-Ins) to form mycothiol.
Catalytic Activity: 1D-myo-inositol 2-(L-cysteinylamino)-2-deoxy-alpha-D-glucopyranoside + acetyl-CoA = CoA + H(+) + mycothiol
Sequence Mass (Da): 33488
Sequence Length: 303
EC: 2.3.1.189
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Q96DH6 | MEANGSQGTSGSANDSQHDPGKMFIGGLSWQTSPDSLRDYFSKFGEIRECMVMRDPTTKRSRGFGFVTFADPASVDKVLGQPHHELDSKTIDPKVAFPRRAQPKMVTRTKKIFVGGLSANTVVEDVKQYFEQFGKVEDAMLMFDKTTNRHRGFGFVTFENEDVVEKVCEIHFHEINNKMVECKKAQPKEVMFPPGTRGRARGLPYTMDAFMLGMGMLGYPNFVATYGRGYPGFAPSYGYQFPGFPAAAYGPVAAAAVAAARGSGSNPARPGGFPGANSPGPVADLYGPASQDSGVGNYISAASPQPGSGFGHGIAGPLIATAFTNGYH | Function: RNA binding protein that regulates the expression of target mRNAs at the translation level. May play a role in the proliferation and maintenance of stem cells in the central nervous system (By similarity).
PTM: Phosphorylated.
Sequence Mass (Da): 35197
Sequence Length: 328
Subcellular Location: Cytoplasm
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Q920Q6 | MEANGSPGTSGSANDSQHDPGKMFIGGLSWQTSPDSLRDYFSKFGEIRECMVMRDPTTKRSRGFGFVTFADPASVDKVLGQPHHELDSKTIDPKVAFPRRAQPKMVTRTKKIFVGGLSANTVVEDVKQYFEQFGKVEDAMLMFDKTTNRHRGFGFVTFENEDVVEKVCEIHFHEINNKMVECKKAQPKEVMFPPGTRGRARGLPYTMDAFMLGMGMLGYPNFVATYGRGYPGFAPSYGYQFPGFPAAAYGPVAAAAVAAARGSVLNSYSAQPNFGAPASPAGSNPARPGGFPGANSPGPVADLYGPASQDSGVGNYISAASPQPGSGFGHGIAGPLIATAFTNGYH | Function: RNA binding protein that regulates the expression of target mRNAs at the translation level. May play a role in the proliferation and maintenance of stem cells in the central nervous system.
PTM: Phosphorylated.
Sequence Mass (Da): 36939
Sequence Length: 346
Subcellular Location: Cytoplasm
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O22469 | MAAEEGKDEAGLDQVEEEFSIWKRNTPFLYDLMISHPLEWPSLTLHWVPSTPIPYSKDPYFAVHKLILGTHTSGGAQDFLMVADVVIPTPDAEPGLGGRDQEPIVPKVEIKQKIRVDGEVNRARCMPQKPTLVGAKTSGSEVFLFDYARLSGKPQTSECDPDLRLMGHEQEGYGLAWSSFKEGYLLSGSQDQRICLWDVSATATDKVLNPMHVYEGHQSIIEDVAWHMKNENIFGSAGDDCQLVIWDLRTNQMQHQVKVHEREINYLSFNPFNEWVLATASSDSTVALFDLRKLTAPLHVLSKHEGEVFQVEWDPNHETVLASSGEDRRLMVWDINRVGDEQLEIELDAEDGPPELLFSHGGHKAKISDFAWNKDEPWVISSVAEDNSLQVWQMAESIYREDDEDEDDDDEGNQNAQHSNENQK | Function: Core histone-binding subunit that may target chromatin assembly factors, chromatin remodeling factors and histone deacetylases to their histone substrates in a manner that is regulated by nucleosomal DNA.
Sequence Mass (Da): 47983
Sequence Length: 424
Domain: The DWD box is required for interaction with DDB1A.
Subcellular Location: Nucleus
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O22607 | MESDEAAAVSPQATTPSGGTGASGPKKRGRKPKTKEDSQTPSSQQQSDVKMKESGKKTQQSPSVDEKYSQWKGLVPILYDWLANHNLVWPSLSCRWGPQLEQATYKNRQRLYLSEQTDGSVPNTLVIANCEVVKPRVAAAEHISQFNEEARSPFVKKYKTIIHPGEVNRIRELPQNSKIVATHTDSPDVLIWDVETQPNRHAVLGAANSRPDLILTGHQDNAEFALAMCPTEPFVLSGGKDKSVVLWSIQDHITTIGTDSKSSGSIIKQTGEGTDKNESPTVGPRGVYHGHEDTVEDVAFSPTSAQEFCSVGDDSCLILWDARTGTNPVTKVEKAHDADLHCVDWNPHDDNLILTGSADNTVRLFDRRKLTANGVGSPIYKFEGHKAAVLCVQWSPDKSSVFGSSAEDGLLNIWDYDRVSKKSDRAAKSPAGLFFQHAGHRDKVVDFHWNASDPWTIVSVSDDCETTGGGGTLQIWRMSDLIYRPEEEVVAELEKFKSHVMTCASKP | Function: Core histone-binding subunit that may target chromatin assembly factors, chromatin remodeling factors and histone deacetylases to their histone substrates in a manner that is regulated by nucleosomal DNA. Component of the flowering autonomous pathway which positively regulates flowering by promoting transcriptional repression of the flowering repressor FLC. May promote histone deacetylation at the FLC locus leading to the formation of repressive chromatin structures. Forms a histone deacetylase complex with HDA5, HDA6 and FLD that represses FLC gene expression to control flowering time . Also negatively regulates cold-responsive genes. Acts together with PDP1 and MSI5 to regulate the function of the PRC2 complex on FLC . Required for systemic acquired resistance (SAR) toward pathogenic bacteria (e.g. Pseudomonas syringae pv tomato DC3000 (avrPto)) . Together with FLD and MSI4/FVE, contributes to dehydroabietinal-dependent (DA, a diterpenoid tricyclic diterpene) activation of flowering ans SAR .
Sequence Mass (Da): 55759
Sequence Length: 507
Domain: The DWD box is required for interaction with DDB1A.
Subcellular Location: Nucleus
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Q9SU78 | MESEAAATVQATRPRRAPRTPVTAILTDKRRRKPKSNNESQLPFLLQQSQKATVDDTYSQWKTLLPILYDSFVNHTLVWPSLSCRWGPQLEQAGSKTQRLYLSEQTNGSVPNTLVIANCETVNRQLNEKAHSPFVKKYKTIIHPGEVNRIRELPQNSKIVATHTDSPDILIWNTETQPDRYAVLGAPDSRPDLLLIGHQDDAEFALAMCPTEPFVLSGGKDKSVILWNIQDHITMAGSDSKSPGSSFKQTGEGSDKTGGPSVGPRGIYNGHKDTVEDVAFCPSSAQEFCSVGDDSCLMLWDARTGTSPAMKVEKAHDADLHCVDWNPHDNNLILTGSADNTVRVFDRRNLTSNGVGSPVYKFEGHRAAVLCVQWSPDKSSVFGSSAEDGLLNIWDCDRVGKKSERATKTPDGLFFQHAGHRDKVVDFHWSLLNPWTIVSVSDNCESIGGGGTLQIWRMSDLIYRPEDEVLTELEKFKSHVFTCTSKS | Function: Core histone-binding subunit that may target chromatin assembly factors, chromatin remodeling factors and histone deacetylases to their histone substrates in a manner that is regulated by nucleosomal DNA (By similarity). Acts together with PDP1 and MSI4/FVE to regulate the function of the PRC2 complex on FLC .
Sequence Mass (Da): 53995
Sequence Length: 487
Domain: The DWD box is required for interaction with DDB1A.
Subcellular Location: Nucleus
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Q9L0Q1 | MATVTFDKATRVYPGSTKPAVDGLDIDIADGEFLVLVGPSGCGKSTSLRMLAGLEDVNGGAIRIGDRDVTHLPPKDRDIAMVFQNYALYPHMSVADNMGFALKIAGVNKAEIRQKVEEAAKILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPQVFLMDEPLSNLDAKLRVSTRTQIASLQRRLGITTVYVTHDQVEAMTMGDRVAVLKDGLLQQVDSPRNMYDKPANLFVAGFIGSPAMNLVEVPITDGGVKFGNSVVPVNRDALKAASDKGDRTVTVGVRPEHFDVVELNGGAAKTLSKDSADAPAGLAVSVNVVEETGADGYIYGTVEVGGETKDLVVRVSSRAVPEKGATVHVVPRPGEIHVFSSSTGERLTD | Function: Part of the ABC transporter complexes DasABC-MsiK and NgcEFG-MsiK involved in N,N'-diacetylchitobiose ((GlcNAc)2) uptake. Responsible for energy coupling to the transport system.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 40396
Sequence Length: 378
Subcellular Location: Cell membrane
EC: 7.5.2.-
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Q40518 | MTSVGLAPVSGLRESSSHSVGVDRLPEEMNDMRIRDDKEIEAAIVDGNGTETGHIIVTTIGGRHGQPKQTISYMAERIVGQGSFGVVFQAKCLETGETVAIKKVLQDKRYKNRELQTMRLLDHPNVVCLKHCFFSTTEKDEVYLNLVLEYVPETVHRVIKHYNKLNQRMPLILVKLYTYQIFRALSYIHHTIGVCHRDIKPQNLLVNPHTHQVKLCDFGSAKVLVKGEPNISYICSRYYRAPELIFGATEYTTAIDIWSAGCVLAELLLGQPLFPGESGVDQLVEIIKVLGTPTREEIKCMNPNYNEFKFPQIKAHPWHKIFHKRMPPEAVDLVSRLLQYSPNLRCTALEAVTHAFFDELRDPNTRLPNGRVLPPLFNFKAHELKGVSAENLLKLVPEHARKQCPSLGL | Function: May mediate extracellular signals to regulate transcription in differentiating cells.
PTM: Autophosphorylated mainly on threonine and serine residues.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 46309
Sequence Length: 409
EC: 2.7.11.1
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Q9LYG9 | MAEQKSSNGGGGGGDVVINVPVEEASRRSKEMASPESEKGVPFSKSPSPEISKLVGSPNKPPRAPNQNNVGLTQRKSFARSVYSKPKSRFVDPSCPVDTSILEEEVREQLGAGFSFSRASPNNKSNRSVGSPAPVTPSKVVVEKDEDEEIYKKVKLNREMRSKISTLALIESAFFVVILSALVASLTINVLKHHTFWGLEVWKWCVLVMVIFSGMLVTNWFMRLIVFLIETNFLLRRKVLYFVHGLKKSVQVFIWLCLILVAWILLFNHDVKRSPAATKVLKCITRTLISILTGAFFWLVKTLLLKILAANFNVNNFFDRIQDSVFHQYVLQTLSGLPLMEEAERVGREPSTGHLSFATVVKKGTVKEKKVIDMGKVHKMKREKVSAWTMRVLMEAVRTSGLSTISDTLDETAYGEGKEQADREITSEMEALAAAYHVFRNVAQPFFNYIEEEDLLRFMIKEEVDLVFPLFDGAAETGRITRKAFTEWVVKVYTSRRALAHSLNDTKTAVKQLNKLVTAILMVVTVVIWLLLLEVATTKVLLFFSTQLVALAFIIGSTCKNLFESIVFVFVMHPYDVGDRCVVDGVAMLVEEMNLLTTVFLKLNNEKVYYPNAVLATKPISNYFRSPNMGETVEFSISFSTPVSKIAHLKERIAEYLEQNPQHWAPVHSVVVKEIENMNKLKMALYSDHTITFQENRERNLRRTELSLAIKRMLEDLHIDYTLLPQDINLTKKN | Function: Mechanosensitive channel that opens in response to stretch forces in the membrane lipid bilayer.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 83032
Sequence Length: 734
Subcellular Location: Cell membrane
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Q8VZL4 | MAGVRLSLLKSIQRSIKPHATAKSCSGLLNSHARAFTCGNLLDGPKASPSMISFSSNIRLHNDAKPFNYLGHSSYARAFSSKSDDFGSIVASGVTGSGDGNGNGNDWVEKAKDVLQTSVDAVTETAKKTKDVSDEMIPHVQQFLDSNPYLKDVIVPVSLTMTGTLFAWVVMPRILRRFHTYAMQSSAKLLPVGFSNEDVPYEKSFWGALEDPARYLVTFIAFAQIAAMVAPTTIAAQYFSPTVKGAVILSLVWFLYRWKTNVITRMLSAKSFGGLDREKVLTLDKVSSVGLFAIGLMASAEACGVAVQSILTVGGVGGVATAFAARDILGNVLSGLSMQFSRPFSMGDTIKAGSVEGQVIEMGLTTTSLLNAEKFPVLVPNSLFSSQVIVNKSRAQWRAIASKIPLQIDDLDMIPQISNEIKEMLRSNTKVFLGKEAPHCYLSRVEKSFAELTIGCNLIRMGKEELYNTQQEVLLEAVKIIKKHGVSLGTTWDNSTL | Function: Mechanosensitive channel that opens in response to stretch forces in the membrane lipid bilayer.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 53884
Sequence Length: 497
Subcellular Location: Mitochondrion membrane
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Q6PDM1 | MTMRSAVFKAAAAPAGGNPEQRLDYERAAALGGPEDESGAAEAHFLPRHRKLKEPGPPLASSQGGSPSPSPAGCGGGKGRGLLLPAGAAPGQQEESWGGSVPLPCPPPATKQAGIGGEPVAAGAGCSPRPKYQAVLPIQTGSIVVAAAKEPTPWAGDKGGAAPPAATASDPAGPPPLPLPGPPPLAPTATAGTLAASEGRWKSIRKSPLGGGGGSGASSQAACLKQILLLQLDLIEQQQQQLQAKEKEIEELKSERDTLLARIERMERRMQLVKRDNEKERHKLLQGYEPEEREEAELSEKIKLERQPELCETSQALPSKPFSCGRSGKGHKRKTPFGNTERKTPVKKLAPEFSKVKTKTPKHSPIKEEPCGSISETVCKRELRSQETPEKPRSSVDTPPRLSTPQKGPSTHPKEKAFSSEMEDLPYLSTTEMYLCRWHQPPPSPLPLRESSPKKEETVARCLMPSSVAGETSVLAVPSWRDHSVEPLRDPNPSDILENLDDSVFSKRHAKLELDEKRRKRWDIQRIREQRILQRLQLRMYKKKGIQESEPEVTSFFPEPDDVESLLITPFLPVVAFGRPLPKLAPQNFELPWLDERSRCRLEIQKKHTPHRTCRK | Function: Component of histone acetyltransferase complex responsible for the majority of histone H4 acetylation at 'Lys-16' (H4K16ac) which is implicated in the formation of higher-order chromatin structure . Greatly enhances MSL2 E3 ubiquitin ligase activity, promoting monoubiquitination of histone H2B at 'Lys-35' (H2BK34Ub) (By similarity). This modification in turn stimulates histone H3 methylation at 'Lys-5' (H3K4me) and 'Lys-80' (H3K79me) and leads to gene activation, including that of HOXA9 and MEIS1 (By similarity). In the MSL complex, acts as a scaffold to tether MSL3 and KAT8 together for enzymatic activity regulation . Isoform 2, isoform 3, isoform 4 and isoform 5 can medite histone H4 acetylation at 'Lys-16' (H4K16ac) .
PTM: Sumoylated with SUMO1.
Sequence Mass (Da): 67320
Sequence Length: 616
Domain: The coiled coil is formed by helices from two subunits in the MSL1 homodimer.
Subcellular Location: Nucleus
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Q2W5W8 | MSLWGPSKTVMVSADKALPGRASEIRVPERHYVLDTLLKPPFPVGMEVACFGMGCFWGAERLFWKTGGVYSTSVGYTGGFTLNPTYEEVCSAQTGHTEAVLVAFDPAEVSYTALLRLFWEGHNPTQGMRQGNDIGTQYRSAIYWTTPEQQAAAEASAKAYGEALRRAGFGAITTEIAPAGRFYWAEGYHQQYLAKEPGGYCGLGGTGVRYG | Function: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.
Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionyl-[protein] = [thioredoxin]-dithiol + L-methionyl-(S)-S-oxide-[protein]
Sequence Mass (Da): 22947
Sequence Length: 211
EC: 1.8.4.11
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B3PND9 | MKKIYVAGGCFWGVQGFLKTIKGIKKTTVGYANSLLENPTYELVKSHVTDAVETVEVIYDENILSLKDIVKKLFAVIDPTARNYQGPDHGRQYRNGFYFVDQEDGVMLRELMLEFSKKYEKPLATEILPLDNYYLAEDYHQDYFDKHPNAVCHIKF | Function: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.
Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionyl-[protein] = [thioredoxin]-dithiol + L-methionyl-(S)-S-oxide-[protein]
Sequence Mass (Da): 18069
Sequence Length: 156
EC: 1.8.4.11
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Q8TQV6 | MEGNEKAEQKNATSEESTDIFENPGEGLEKATFAAGCFWGIEEAFRQVKGVVATAVGYSGGHFEKPTYEQVCTLDTGHAEAVRVIFDPKVVSYKNLLDVFWKIHDPTTKNRQGPDVGKQYRSVIFYHNEEQKAAALASKEELEKAGVFKNPIVTEIVPVSEFYMAEDYHQQYFEKKGFLQNILRSFKK | Function: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.
Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionyl-[protein] = [thioredoxin]-dithiol + L-methionyl-(S)-S-oxide-[protein]
Sequence Mass (Da): 21284
Sequence Length: 188
EC: 1.8.4.11
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Q12TP4 | MERATFAAGCFWGVEAAFSKVEGVISTKVGYTGGTLKDPTYKDVSTGSTGHAESIDIIFDESVITYGELLEVLWNTHDPTTKDSQGPDHGSQYRSAIFYHDDAQREAALRSREQLERSGKYDSTIKTEIVKASEFSPAEDYHQKYFQKLQFKR | Function: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.
Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionyl-[protein] = [thioredoxin]-dithiol + L-methionyl-(S)-S-oxide-[protein]
Sequence Mass (Da): 17202
Sequence Length: 153
EC: 1.8.4.11
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Q2FQ35 | MGIAFFAGGCFWGIEAGFQKVPGVINTKVGYMGGHTIEPTYQEVCSDTTGHAETIALEYDDTAITYRKLLEIFFSLHNPTEVNRQGPDVGSQYRSVIFYTSPEQKEEAEMFIAEMNQSGRYHAAIATEVVPAETFWPAEEYHQSYFLKIGQRYGRSLF | Function: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.
Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionyl-[protein] = [thioredoxin]-dithiol + L-methionyl-(S)-S-oxide-[protein]
Sequence Mass (Da): 17829
Sequence Length: 158
EC: 1.8.4.11
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A9AB97 | MTNTETAVFGMGCFWSAEELFRKINGVISTEVGFMGGNIKNPTYGQVCRGRSGHIEVVNIIYNPKILKYDDLLELFWNNHDPTTPNRQGWDVGEQYSSHIFYFTEEQKLLAEKSFEKIQKNSELKIVTAIRKASDFFPAEEYHQKYFMKKNNCILNF | Function: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.
Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionyl-[protein] = [thioredoxin]-dithiol + L-methionyl-(S)-S-oxide-[protein]
Sequence Mass (Da): 18266
Sequence Length: 157
EC: 1.8.4.11
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A3CUG3 | MAPEKSLERATFGAGCFWGVEEAFRRVPGVVETAVGFMGGTVENPTYPEVCTGRTGHAEVVQVTYDPGTVSYRALLDTFWDAHDPTTPNRQGPDIGTQYRSVIFVHTPEQEAEARASKEEMDQSGKFRRPIVTAIEPAGTFWRAEEYHQQYFAKRGGGQCRTVW | Function: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.
Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionyl-[protein] = [thioredoxin]-dithiol + L-methionyl-(S)-S-oxide-[protein]
Sequence Mass (Da): 18307
Sequence Length: 164
EC: 1.8.4.11
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Q6LYY1 | MKNIKTTVFGMGCFWGAEEVFRKINGVVSTEVGFMGGTIKNPTYGQVCRGKSGHIEVVKIDYDPEIISYDELLDLFWNNHNPTTPNKQGWDVGEQYSSYIFYFDDEQKLIAEKSLEKMQENTDLKIVTIIEKAGSFYPAEEYHQKYFMKKNNSILNF | Function: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.
Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionyl-[protein] = [thioredoxin]-dithiol + L-methionyl-(S)-S-oxide-[protein]
Sequence Mass (Da): 18151
Sequence Length: 157
EC: 1.8.4.11
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O26635 | MMCLSRYEKATFGAGCFWGVEDAFRKVDGVVSTRVGYMGGHLENPTYEDVCTGLTGHAEVVEVTFDPDVVGYSDLLDVFWSIHDPTTLNRQGPDVGEQYRSVIFYHSDEQRRAAIESRRRLEESGRFRDRIVTAIEPAGTFYEAEEYHQQYLEKNPRRRCYLMRLLSTR | Function: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine (By similarity).
Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionyl-[protein] = [thioredoxin]-dithiol + L-methionyl-(S)-S-oxide-[protein]
Sequence Mass (Da): 19548
Sequence Length: 169
EC: 1.8.4.11
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Q9D6Y7 | MLSASRRALQLLSSANPVRRMGDSASKVISAEEALPGRTEPIPVTAKHHVSGNRTVEPFPEGTQMAVFGMGCFWGAERKFWVLKGVYSTQVGFAGGHTRNPTYKEVCSEKTGHAEVVRVVYRPEHISFEELLKVFWENHDPTQGMRQGNDFGTQYRSAVYPTSAVQMEAALRSKEEYQKVLSKHNFGPITTDIREGQVFYYAEDYHQQYLSKNPDGYCGLGGTGVSCPMAIKK | Function: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.
Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionyl-[protein] = [thioredoxin]-dithiol + L-methionyl-(S)-S-oxide-[protein]
Location Topology: Lipid-anchor
Sequence Mass (Da): 25988
Sequence Length: 233
Subcellular Location: Mitochondrion
EC: 1.8.4.11
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Q6AUK5 | MGVQHLLKLRMASPHPHPHPGAPLAARPLSALASFFLARPSSTAAAPPPRHVTLSCSRPHCNHNQWAASRCRGTAGRRRLQVVVAMSSSAPPPPPGSVQKSEEEWEAILSPEQFRILRLKGTEYPGTGEYDKLFAEGVYECAGCGTPLYKSSTKFNSGCGWPAFYEGFPGAIARTPDPDGRRIEITCAACGGHLGHVFKGEGFNTPTDERHCVNSISLKFIPASEDSKL | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the reduction of methionine sulfoxide (MetSO) to methionine in proteins. Plays a protective role against oxidative stress by restoring activity to proteins that have been inactivated by methionine oxidation. MSRB family specifically reduces the MetSO R-enantiomer (By similarity).
Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionyl-[protein] = [thioredoxin]-dithiol + L-methionyl-(R)-S-oxide-[protein]
Sequence Mass (Da): 24685
Sequence Length: 229
Subcellular Location: Plastid
EC: 1.8.4.12
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Q9M0Z5 | MADLVTVVKKTEEEWRAVLSPEQFRILRQKGTETPGTEEYDKFFEEGIFSCIGCKTPLYKSTTKFDAGCGWPAFFEGLPGAINRAPDPDGRRTEITCAVCDGHLGHVHKGEGYSTPTDERLCVNSVSINFNPAKPSSIT | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the reduction of methionine sulfoxide (MetSO) to methionine in proteins. Plays a protective role against oxidative stress by restoring activity to proteins that have been inactivated by methionine oxidation. MSRB family specifically reduces the MetSO R-enantiomer (By similarity).
Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionyl-[protein] = [thioredoxin]-dithiol + L-methionyl-(R)-S-oxide-[protein]
Sequence Mass (Da): 15332
Sequence Length: 139
Subcellular Location: Cytoplasm
EC: 1.8.4.12
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Q84JT6 | MPTSATAVAPSTGSVQKKDQDWRAILSPEQFRVLREKGTENRGKGEYTKLFDDGIYSCAGCATPLYKSTTKFDSGCGWPSFFDAIPGAIKQTPEAGGRRMEITCAACDGHLGHVVKGEGFPTATDERHCVNSVSLKFSEISSQ | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the reduction of methionine sulfoxide (MetSO) to methionine in proteins. Plays a protective role against oxidative stress by restoring activity to proteins that have been inactivated by methionine oxidation. MSRB family specifically reduces the MetSO R-enantiomer (By similarity).
Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionyl-[protein] = [thioredoxin]-dithiol + L-methionyl-(R)-S-oxide-[protein]
Sequence Mass (Da): 15412
Sequence Length: 143
Subcellular Location: Cytoplasm
EC: 1.8.4.12
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B0BYW4 | MEKVQKTEQEWEAQLTPEQFRVTRHHGTERAFTGEYHDLKAAGTYQCVCCGTELFTSDTKFDSGTGWPSFWAPADKTHVEEKTDRSLFMVRTEVLCAVCDAHLGHVFNDGPKPTGLRYCMNSAALKFVPKS | Cofactor: Binds 1 zinc ion per subunit. The zinc ion is important for the structural integrity of the protein.
Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionyl-[protein] = [thioredoxin]-dithiol + L-methionyl-(R)-S-oxide-[protein]
Sequence Mass (Da): 14807
Sequence Length: 131
EC: 1.8.4.12
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Q6FAL8 | MGKLNKTEREWQRELSPEEYRITRQKGTEPAFTGQYWNTKQSGTYVCRCCGTELFSSISKYDSGCGWPSFYKPINTTAIEEHDDFSHGMVRTEIVCHHCDAHLGHVFEDGPQPTGLRYCVNSASLQLKTDEKNDEETYP | Cofactor: Binds 1 zinc ion per subunit. The zinc ion is important for the structural integrity of the protein.
Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionyl-[protein] = [thioredoxin]-dithiol + L-methionyl-(R)-S-oxide-[protein]
Sequence Mass (Da): 15964
Sequence Length: 139
EC: 1.8.4.12
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Q8UGX7 | MSDLTSPKVNKSDADWREQLTPEQYHILREHGTERPFTGPYWNSTEKGLYRCAACDEPLFLSDTKFDAGCGWPSYFEPVKPGAVTEHRDSTHGMVRTEIRCANCGGHLGHVFPDGPPPTGLRYCINGHSMVFEPV | Cofactor: Binds 1 zinc ion per subunit. The zinc ion is important for the structural integrity of the protein.
Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionyl-[protein] = [thioredoxin]-dithiol + L-methionyl-(R)-S-oxide-[protein]
Sequence Mass (Da): 15140
Sequence Length: 135
EC: 1.8.4.12
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Q0A706 | MVEVEKSDAEWRAQLTDEQYAVCRQGGTEQPFSGAYYHCKEPGTYHCVCCDAPLFSSRAKYDSGSGWPSFWAPISDDHLRILEDRSLGMVREEVRCARCDAHLGHVFPDGPMPTGLRYCINSVCLDLKRSG | Cofactor: Binds 1 zinc ion per subunit. The zinc ion is important for the structural integrity of the protein.
Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionyl-[protein] = [thioredoxin]-dithiol + L-methionyl-(R)-S-oxide-[protein]
Sequence Mass (Da): 14724
Sequence Length: 131
EC: 1.8.4.12
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Q8PLY8 | MSFRDALNLPSSEITDESVYRDRRRLLQLLALTPALGVAGCAEADPPPPPKTVVTPAQARSGFRTAEELTRLEDVTSYNNFYEFGTDKTDPSKAAKTLKLSPWTVKVGGECEKPGSLSLDELLKGIASEERIYRLRCVEGWSMVIPWTGVPLGEVLKRFAPTSKAKYVAFTTLADPQQMPGVRYRSINWPYREGLRIDEAMHPLTLLATGLYGKPLPQQNGAPLRLVVPWKYGFKSIKSIVEIRFVEKMPETAWHDLQPSEYGFFSNVNPAVDHPRWSQKTERRIAGTASKLFAERIATKPFNGYADQVASLYAGMDLKKWF | Cofactor: Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
Function: Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.
Catalytic Activity: a quinone + H2O + L-methionyl-[protein] = a quinol + L-methionyl-(S)-S-oxide-[protein]
Sequence Mass (Da): 36143
Sequence Length: 322
Subcellular Location: Periplasm
EC: 1.8.5.-
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Q8ZAW9 | MHNTFTHTKNNTHTKNNTQAKNSGSQTKSNAVSLNKPRKLTEADVTPESIFYQRRKVLQALGITAATLALPASAQADLLAWFKGNEPPKAPSGKPLTFTPSAAYHPDLALTPEDKVTGYNNFYEFGLDKADPAANAGTLKTEDWQIKIDGDVVKPMTLDMDYLMKCFPLEERIYRLRCVEAWSMVVPWIGFELGKLLKLAEPTSNARYVAFQTLYAPDQMPGQKNRFIGGGLDYPYVEGLRLDEAMHPLAFMVVGVYGKTLPPQNGAPLRLMTPWKYGFKSIKSIVHIRLTRDQPPTTWNLSAPNEYGFYANVNPHVDHPRWSQATERVIGSGGILDVKRQPTLLFNGYAEQVASLYRGLDLRKNF | Cofactor: Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
Function: Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.
Catalytic Activity: a quinone + H2O + L-methionyl-[protein] = a quinol + L-methionyl-(S)-S-oxide-[protein]
Sequence Mass (Da): 40979
Sequence Length: 366
Subcellular Location: Periplasm
EC: 1.8.5.-
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P58769 | MAFALSLPSLPKRYQPAAIWSLYVIGLCPGLWYFYLAATGGLGFNPVKDFEHLLGIWALRFLCLGLLVTPLRDLFNVNLIAYRRALGLIAFYYVLAHFTVYLVLDRGLILGSIAGDILKRPYIMLGMAGLIILIPLALTSNRWSIRRLGSRWNTLHKLVYLVLIVGVLHFVLARKSITLEPVFYISTMVVLLGYRLVRPSIMTMKRNKRARPVRT | Cofactor: Binds 1 FMN per subunit.
Function: Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 24422
Sequence Length: 215
Subcellular Location: Cell inner membrane
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G8QMC1 | MTFQPTPRQLSAIKAALFLLTLLPALHYAHGLWSDSLGANPIEALTRGMGIWTLNFLFLTLCVSPLRKLSGWHWLLRLRRMLGLTAFAYGCLHLLTYLWLDQFWDVDAIARDIWKRPFITVGATAFLLMLPLALTSSHAAIRSLGGKRWQSLHRAVYAVAILGVVHYLWLVKRVALLDPIIYALVLAILLGWRVVERIRLNGPWPTRSTPPAVQPVVFMKRDAVAALGEPKKR | Function: Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain (By similarity). Probably involved in protection against reactive chlorine species (RCS) generated by chlorite and hypochlorite .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 26320
Sequence Length: 233
Subcellular Location: Cell inner membrane
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Q7WD13 | MPAAPLTARAIGRIKPLLFVAGLLPFARWFWLGANDGLSANPVEFLTRSSGTWTLVCLLVTLAITPLRRLTGQPALVRLRRMCGLFAFFYGSLHFLAWVWWDRGLDPVSMLQDVGERPFITVGFAAFVLMAALAATSTQWAMRKLGKRWQVLHRAVYAIGLLAILHFWWHKAGKNDLQQPLLYGSVLALLLGWRVAAWWRRRGAAR | Cofactor: Binds 1 FMN per subunit.
Function: Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 23238
Sequence Length: 206
Subcellular Location: Cell inner membrane
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A6WYN0 | MAAAAQTGKKKTVRPGEWKIWLLYAVGFVPAVWTFYLGASGNLGADPVKTFEHTLGLWALRFLILTLMVTPIRDLTGMAFLRYRRALGLLAFYYALMHFATYMVLDQGLNISAIVTDIVRRPFITIGMISLVLLVPLALTSNNWSIRKLGRRWNSLHKLVYVAIAGGAIHFIMSVKSWPAEPVIYAGIVSALLLWRLVRPHARNRKPVSRPRGEAMAVKK | Cofactor: Binds 1 FMN per subunit.
Function: Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 24674
Sequence Length: 220
Subcellular Location: Cell inner membrane
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J4KLK4 | MALVEKIQLTDDFSVYANPAAKLEVEFIHKEIFIDKCYDVAPFPDDSFIVDAGGNIGMFTLYMKRKYPQSTILAFEPAPATFSTFQRNMELHNVSGVQAHQCGLGREDASLALTFYPQMPGNSTLYAEDKTNQMKSVDQNHPIAKLMQETHEVQVDVKRLSDFLGEVPNLKRVNLLKVDVEGAEMDVLRGLDDEHWDLIDNVVVELCDSKGDFATAKTLLESKGFAVAVERPDWAPPDLKMYMLIAKRN | Function: Methyltransferase; part of the pathway that mediates the biosynthesis of tenellin-type 2-pyridones, iron-chelating compounds involved in iron stress tolerance, competition with the natural competitor fungus Metarhizium robertsii and insect hosts infection . Methylates pyridovericin-N-O-(beta-D-glucopyranoside) produced by the UDP-glucosyltransferase GT1 to yield pyridovericin-N-O-(4-O-methyl-beta-D-glucopyranoside) (PMGP) . The pathway begins with the assembly of the polyketide-amino acid backbone by the hybrid PKS-NRPS tenS with the help of the enoyl reductase tenC. These enzymes catalyze the synthesis of the pyrrolidine-2-dione intermediates pretellinin A, 11-hydropretellenin A, 12-hydropretellenin A, 13-hydropretellenin A, 14-hydropretellenin A, 12-oxopretellenin A and prototellinin D. The cytochrome P450 monooxygenase tenA then catalyzes an oxidative ring expansion of pretenellin A and 14-hydropretellenin A to form the 2-pyridone core, leading to pretenellin B and pyridovericin, respectively. The cytochrome P450 monooxygenase tenB is then required for the selective N-hydroxylation of the 2-pyridone nitrogen of yield tellinin and 15-hydroxytellenin (15-HT), respectively. The UDP-glucosyltransferase GT1 and the methyltransferase MT1, located outside the tenS gene cluster, contribute to the stepwise glycosylation and methylation of 15-HT to obtain the glycoside pyridovericin-N-O-(4-O-methyl-beta-D-glucopyranoside) (PMGP). Additional related compounds such as 1-O-methyl-15-HT, (8Z)-1-O-methyl-15-HT, and O-methyltenellin A are also produced but the enzymes involved in their biosynthesis have still to be determined .
Sequence Mass (Da): 28021
Sequence Length: 249
Pathway: Secondary metabolite biosynthesis.
EC: 2.1.1.-
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P19888 | MKIKFVDLFAGIGGIRIGFERAAKRFELETECVLSSEIDKKACETYALNFKEEPQGDIHEITSFPEFDFLLAGFPCQPFSYAGKQQGFGDTRGTLFFEVERVLRDNRPKAFLLENVRGLVTHDKGRTLKTIISKLEELGYGVSYLLLNSSTFGVPQNRVRIYILGILGSKPKLTLTSNVGAADSHKYKNEQISLFDESYATVKDILEDSPSEKYRCSDEFIGQLSKVVGNNFELLHGYRLIDYRGGNSIHSWELGIKGDCTKEEIEFLNQLIANRRKKIYGTHQDGKALTLEQIRTFYNHDQLEVIIKSLLQKGYLREEENKFNPVCGNMSFEVFKFLDPDSISITLTSSDAHKLGVVQNNVPRRITPRECARLQGFPDDFILHSNDNFAYKQLGNSVTVKVVEKVIEDLFQNNVNELFGQMKLANVV | Function: A methylase, recognizes the double-stranded sequence 5'-GGYRCC-3', methylates C-4 on both strands, and protects the DNA from cleavage by the BanI endonuclease.
Catalytic Activity: a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = a 5-methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 48618
Sequence Length: 428
EC: 2.1.1.37
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O30640 | MAEYTPKERLYRALRKQQVDRMPAVCFTQTATVEQMEACGAYWPEAHSDAEKMATLAEAAHTVVGFEAVRVPFDITAEAEFFGCGIKAGDLKQQPSVIKPSVKNLEDLEKLKNYNLKEGRIAVVLEAVKILSEKYGKELPIIGSMIGPFSLAQHINGDAWFGNLFTGEEVVPALLDFCSDFNVAYAKAMVENGADTIAIIDPTASYELIGGEFYEKYALPYQKKIVDAMKELDVATVLHICGNTTNGLGIMDKTGVNGISVDQKVDIKTATGSVKNAIIVGNLDPVAVLWNGTPEEIAEASKKALDAGVGLLTVGCGTVSMTPTVNLQKMIECAKSHTY | Function: Methyltransferase involved in methanogenesis from methylamines methanol pathway. Catalyzes the transfer of the methyl group from the methylated corrinoid protein MtmC (MtmC1 or MtmC2) or MtbC to coenzyme M, forming the substrate for coenzyme-B sulfoethylthiotransferase.
Catalytic Activity: coenzyme M + methyl-Co(III)-[methylamine-specific corrinoid protein] = Co(I)-[methylamine-specific corrinoid protein] + H(+) + methyl-coenzyme M
Sequence Mass (Da): 36664
Sequence Length: 339
Pathway: One-carbon metabolism; methanogenesis from methylated amine.
EC: 2.1.1.247
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O93661 | MATEYALRMGDGKRVYLTKEKIVSEIEAGTADAADLGEIPALSANEMDKLAEILMMPGKTVSVEQGMEIPVTHDIGTIRLDGDQGNSGVGIPSSRLVGCMTHERAFGADTMELGHIDYSFKPVKPVVSNECQAMEVCQQNMVIPLFYGAMPNMGLYYTPDGPFENPGDLMKAFKIQEAWESMEHAAEHLTRDTVWVMQKLFASGADGVNFDTTGAAGDGDMYGTLHAIEALRKEFPDMYIEAGMAGECVLGMHGNLQYDGVTLAGLWPHQQAPLVAKAGANVFGPVCNTNTSKTSAWNLARAVTFMKAAVEASPIPCHVDMGMGVGGIPMLETPPIDAVTRASKAMVEIAGVDGIOIGVGDPLGMPIAHIMASGMTGMRAAGDLVARMEFSKNMRIGEAKEYVAKKLGVDKMDLVDEHVMRELREELDIGIITSVPGAAKGIAAKMNIEKLLDIKINSCNLFRKQIA | Function: Catalyzes the transfer of a methyl group from dimethylamine to the corrinoid cofactor of MtbC . The major or perhaps only DMA methyltransferase expressed under inducing conditions .
Catalytic Activity: Co(I)-[dimethylamine-specific corrinoid protein] + dimethylamine + H(+) = methyl-Co(III)-[dimethylamine-specific corrinoid protein] + methylamine
Sequence Mass (Da): 50228
Sequence Length: 467
Pathway: One-carbon metabolism; methanogenesis from dimethylamine.
EC: 2.1.1.249
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P33563 | MTQILETVDKSRLTVNPLLKNKSELGQFFTPSSISIFMACLFSEDKLNNAKVLDAGAGIGSLTSAFLARLISENIGKADLHLLEIDEMLEPYLSETLALFKDYIEINSQIIIDDFIEWAAYSLLDEESLLAKDKQRFTHAILNPPYKKIKSNSKHRKLLRKAGIETVNLYSAFVALTVDLMSDGGEIVFIIPRSFCNGPYFRHFRQHLLNKTSIKHMHLFESRDKAFKDDEVLQENVISKLEKGTVQEDVKISISTDDSFSVIRSYRYPFEKIVQPNDIEKFIHINTTNEETLIEKHPNVCYSLEELNIEVSTGPVVDFRVKENLREMPGEGTVPLFYPNHFVGTSLEYPKMMKKPNAIIRNEKVEKWLYPNGHYVVVKRFSSKEEKRRIVAGVLTPESVNDPVVGFENGLNVLHYNKSGISKEVAYGLYAYLNSTPVDKYFRIFNGHTQVNATDLRTMKFPSRDILISLGKWVIENIENVGQVEIDSKLEELLLNDRGNA | Function: A beta subtype methylase that recognizes the double-stranded sequence 5'-CTGCAG-3', methylates A-5 on both strands, and protects the DNA from cleavage by the BsuBI endonuclease.
Catalytic Activity: a 2'-deoxyadenosine in DNA + S-adenosyl-L-methionine = an N(6)-methyl-2'-deoxyadenosine in DNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 57198
Sequence Length: 501
EC: 2.1.1.72
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Q9Y6C9 | MADAASQVLLGSGLTILSQPLMYVKVLIQVGYEPLPPTIGRNIFGRQVCQLPGLFSYAQHIASIDGRRGLFTGLTPRLCSGVLGTVVHGKVLQHYQESDKGEELGPGNVQKEVSSSFDHVIKETTREMIARSAATLITHPFHVITLRSMVQFIGRESKYCGLCDSIITIYREEGILGFFAGLVPRLLGDILSLWLCNSLAYLVNTYALDSGVSTMNEMKSYSQAVTGFFASMLTYPFVLVSNLMAVNNCGLAGGCPPYSPIYTSWIDCWCMLQKEGNMSRGNSLFFRKVPFGKTYCCDLKMLI | Function: Protein insertase that mediates insertion of transmembrane proteins into the mitochondrial outer membrane . Catalyzes insertion of proteins with alpha-helical transmembrane regions, such as signal-anchored, tail-anchored and multi-pass membrane proteins . Does not mediate insertion of beta-barrel transmembrane proteins . Also acts as a receptor for the truncated form of pro-apoptotic BH3-interacting domain death agonist (p15 BID) and has therefore a critical function in apoptosis (By similarity). Regulates the quiescence/cycling of hematopoietic stem cells (HSCs) (By similarity). Acts as a regulator of mitochondrial fusion, essential for the naive-to-primed interconversion of embryonic stem cells (ESCs) (By similarity). Acts as a regulator of lipid homeostasis and has a regulatory role in adipocyte differentiation and biology (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 33331
Sequence Length: 303
Subcellular Location: Mitochondrion outer membrane
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Q791V5 | MADAASQVLLGSGLTILSQPLMYVKVLIQVGYEPLPPTIGRNIFGRQVCQLPGLFCYAQHIASIDGRRGLFTGLTPRLCSGVLGTVVHGKVLQYYQESEKPEELGSVTVQKEYSSSFDRVIKETTREMIARSAATLITHPFHVITLRSMVQFIGRESKYCGLCDSIVTIYREEGIVGFFAGLIPRLLGDIISLWLCNSLAYLINTYALDSGVSTMNEMKSYSQAVTGFFASMLTYPFVLVSNLMAVNNCGLAGGSPPYSPIYTSWIDCWCMLQKAGNMSRGNSLFFRKVPCGKTYCYDLRMLI | Function: Protein insertase that mediates insertion of transmembrane proteins into the mitochondrial outer membrane. Catalyzes insertion of proteins with alpha-helical transmembrane regions, such as signal-anchored, tail-anchored and multi-pass membrane proteins. Does not mediate insertion of beta-barrel transmembrane proteins (By similarity). Also acts as a receptor for the truncated form of pro-apoptotic BH3-interacting domain death agonist (p15 BID) and has therefore a critical function in apoptosis . Regulates the quiescence/cycling of hematopoietic stem cells (HSCs) . Acts as a regulator of mitochondrial fusion, essential for the naive-to-primed interconversion of embryonic stem cells (ESCs) . Acts as a regulator of lipid homeostasis and has a regulatory role in adipocyte differentiation and biology .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 33499
Sequence Length: 303
Subcellular Location: Mitochondrion outer membrane
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G5ECI1 | MRSSLLLLVFFLSIGWARYCVHNEKSWCQGHNIWGWCFHNKSSGVFNCDDNAFCVSQEQLKNKKSSGCFLRDNSSICCCNDADGCNLGFIGVQPKYAHGQQCTNSMEVPNEDIRQFRPCDDPFCYSVLTAEDDGGPTTVTRGCHSRKMVMHHMSKNEDDKYQNNTKWRETKQIAEMPSCAEILKDQPKVNGTTSMCVDFTYDQEAEDGEEVDEPIKMKGRLCCCAGSNKCNEHAMWADEGISLTEMLEEIEARKVPVDSSAPVNIILSIAFSIFLIHF | Function: Plays a role in mechanosensory transduction (touch sensitivity).
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 31379
Sequence Length: 278
Subcellular Location: Cell membrane
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P05302 | MNIIDLFAGCGGFSHGFKMAGYNSILAIEKDLWASQTYSFNNPNVSVITEDITTLDPGDLKISVSDVDGIIGGPPCQGFSLSGNRDQKDPRNSLFVDFVRFVKFFSPKFFVMENVLGILSMKTKSRQYVKDIIAEEFSNVGYKVCVIILNACDYGVPQSRQRVFFIGLKSDRPLNQQILTPPSKVIESEYTSLEEAISDLPVIEAGEGGEVQDYPVAPRNKYQENMRKGSTCVYNHVAMRHTQRLVDRFAAIKFGQSVKHVSEEHSQRKRGDANSISGKVFSQNNMRPYPYKPCPTVAASFQSNFIHPFYNRNFTAREGARIQSFPDTYIFQGKRTTMSWEKHLSQYQQIGNAVPPLLAQALAERISWYFENINLINDSNVSIKRMVQRSFMSQLNLENNVNVRQDDNYDKVHSF | Function: A methylase that recognizes the double-stranded sequence 5'-CTNAG-3', methylates C-1 on both strands, and protects the DNA from cleavage by the DdeI endonuclease.
Catalytic Activity: a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = a 5-methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 47081
Sequence Length: 415
EC: 2.1.1.37
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Q86KU6 | MEEYKEIMQNKKGKVDVTPIANFFREEVKQQITKNCWKPRVVAFLTSDDQGAIDYSKWTKLACQKDGIEFILKRVERVDLEDLIIEANNDSCVHGILVYYPVFGGMMDSYLQDVVSPTKDIEGLSTQNRFNLYHNIRFMDGETATKKCVIPCTPLAMVKIIDNLGIYDKSLAMGEHLKGKTVTIVNRSEIVGRPLAAMLANDGAIVYSIDINGIIIFQSGKRHGTIKMSETNVTREEAISKSDILILGVPSPNYKVNSDLIQDGTIVINFAGCLNVDESIQEKSILVPTIGKVTIAMLERNLLRLFNNQISNK | Function: Catalyzes oxidation of cytoplasmic one-carbon units for purine biosynthesis.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NAD(+) = 5,10-methenyltetrahydrofolate + NADH
Sequence Mass (Da): 35069
Sequence Length: 313
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
EC: 1.5.1.15
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P24600 | MKTIDLFAGCGGMSLGFMQAGFEIVAAVDNWRPAINTYQQNFTHPIHELDLAQIDAAVSLIKTHSPELIIGGPPCQDFSSAGKRDEGLGRANLTLDFAKIVLAIQPAWVIMENVERARLSKIHQQACSMLGDEGYSLAQVVLDASLCGVPQLRKRTFVIGHRHGSIADLANVLQQRLAKQSLTVRDYFGESLDTDYYYRHPRTYERRAIFSVNEPSPTIRGVNRPIPATYRMHPKDAGDVSLARPLTTKERSLIQTFPLDFKFVGTKSEQEQMIGNAVPVNLAFFLATSLQAYLNQPRMQQLSLLPSFF | Function: A methylase that recognizes the double-stranded sequence 5'-GRCGYC-3', methylates C-? on both strands, and protects the DNA from cleavage by the HgiDI endonuclease.
Catalytic Activity: a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = a 5-methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 34439
Sequence Length: 309
EC: 2.1.1.37
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Q9RLM4 | MMSLKIQPAVPKKSDKPSATNRDCQNFKREKNNLPFQLTDKSCNLDISIRQERKKTLIFSFFSGAGFLDLGFELSGFDIAFVNEVHPPFLEAYKYSRSRMDIPKPKYGYFKGSIDECLYAEKAKDLAGWVKKEKQNGIIVGFIGGPPCPDFSIAGKNKGKDGENGKLSQSYVDLICKNQPDFFVFENVKGLYRTAKHREFFNALKRQLSDFGYVCTEKLINAIEYGVPQDRERIILVGFLSQHVDALQKFDWDAHISFPDALEKDWPTTEEVGRVVSQPANIYPELTVQYWFNRNGVDTHPNASKHFQPRAGLEKFQTISEGDDKKKSYKRLHRWRYSPTAAYGNNEVHIHPYLPRRISAAEALAIQSLPKEFELPDNMTLSNMFKTIGNGVPFLAAKGIAMTLKSYLENHYERTKTDGC | Function: A methylase that recognizes the double-stranded sequence 5'-RCCGGB-3', methylates C-2 on both strands, and protects the DNA from cleavage by the NmeDI endonuclease.
Catalytic Activity: a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = a 5-methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 47931
Sequence Length: 420
EC: 2.1.1.37
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Q9P786 | MSNTNKSEPNHSCKVVYASRVAETFVEQLKQHVNLFEFAPKLVGFLSNSDPAARMYADWTNKTCTEIGFQYELREVPKDDLEDAIVEANNDPSVNGIMIYFPVFNDGQDQYLQQVVSPDKDVEGLCHKYVMNMYHNIRHLDPEKTKKSILPCTPLAIVKILEYLGVYNKIINYGNRLYGKTITIVNRSEIVGRPLAALLANDGAKVYSVDIHNVQCFTRGAGIRSKKHDVADTNFKLEDVAPISDVIICGVPSANYKFPSNLVRDGAVCICFSSEKNFDAASLKEHAGIYVPSIGKVTIAMLLRNLIRLTSYQLNKPVDI | Function: Catalyzes oxidation of cytoplasmic one-carbon units for purine biosynthesis.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NAD(+) = 5,10-methenyltetrahydrofolate + NADH
Sequence Mass (Da): 35814
Sequence Length: 320
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
Subcellular Location: Cytoplasm
EC: 1.5.1.15
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Q02046 | MSKPGRTILASKVAETFNTEIINNVEEYKKTHNGQGPLLVGFLANNDPAAKMYATWTQKTSESMGFRYDLRVIEDKDFLEEAIIQANGDDSVNGIMVYFPVFGNAQDQYLQQVVCKEKDVEGLNHVYYQNLYHNVRYLDKENRLKSILPCTPLAIVKILEFLKIYNNLLPEGNRLYGKKCIVINRSEIVGRPLAALLANDGATVYSVDVNNIQKFTRGESLKLNKHHVEDLGEYSEDLLKKCSLDSDVVITGVPSENYKFPTEYIKEGAVCINFACTKNFSDDVKEKASLYVPMTGKVTIAMLLRNMLRLVRNVELSKEK | Function: Catalyzes oxidation of cytoplasmic one-carbon units for purine biosynthesis.
PTM: The N-terminus is blocked.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NAD(+) = 5,10-methenyltetrahydrofolate + NADH
Sequence Mass (Da): 36240
Sequence Length: 320
Subcellular Location: Cytoplasm
EC: 1.5.1.15
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Q9I6B7 | MLRSLFRRLFKYLLWFMAASVVLVAVLRWVPPPGTMVMVERKVGSWVDGQPIDLQRDWRSWEQLPDSLKVAVIAGEDQHFAEHHGFDLPAIQQALAHNERGGSIRGASTLSQQVAKNVFLWSGRSWLRKGLEAWFTLLIETLWTKQRILEVYLNSAEWGPGVFGAQAAARYHFGLDAERLSRTQASQLAAVLPSPLKWSAARPGPYVRQRAAWIRQQMWQLGGDDYLLRLER | Function: Peptidoglycan polymerase that catalyzes glycan chain elongation from lipid-linked precursors.
Catalytic Activity: [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+)
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 26547
Sequence Length: 232
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.4.1.129
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Q88CS3 | MLSTLIRRLSRALLWFVAGSIVLVLVFRWVPPPGTALMVERKVQSWVNGEPIDLQRDWEPWENISDELKVAVIAGEDQKFASHWGFDLPAIQAALAHNERGGNIRGASTLTQQVAKNLFLWSGRSWFRKGLEAWFTALIELFWSKERILEVYLNSAEWGKGVFGAQAAARYHFGVDASRLSRQQAAQLAAVLPSPIKWSASRPSAYVASRAGWIRRQMSQLGGPSYLMQLDSSRKL | Function: Peptidoglycan polymerase that catalyzes glycan chain elongation from lipid-linked precursors.
Catalytic Activity: [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+)
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 26565
Sequence Length: 236
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.4.1.129
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Q88AF9 | MLQIILRRLMKALLWFAAGSALVVLVLRWVPPPGTALMVERKVESWFDGEPIDLQRDWEPWDKISNNLKIAVIAGEDQKFAEHWGFDVDAIQAAILHNEQGGSIRGASTLSQQVSKNLFLWSGRSYLRKGLEAWFTMLIELLWSKERILEVYLNSVEWDEGIFGAQAAAQHHFRTNASALSEQQASYLAAVLPNPRQWSASHPSGYVSRRAGWIRQQMRQLGGDEYLQGLNSSRRW | Function: Peptidoglycan polymerase that catalyzes glycan chain elongation from lipid-linked precursors.
Catalytic Activity: [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+)
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 26917
Sequence Length: 236
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.4.1.129
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Q2K330 | MPARRRWFENRPVLKRIVLAVLALVVLPYVLIFFYLLPFIHPVSTLMLRDLVLLRGYDRRWVSLDEISPVLVQSVMMSEDGQYCFHGGVDWAEMRMLVEDTLKGQATRGGSTIPMQTAKNLFLWNSRSFVRKAMELPLAVSTDFVLSKRRLMEIYLNIAEWGPGIYGIEAAAQHHFKVPASKLTRRQASLLAVSLPNPIDRKAGKPGRGLRRLAGVIERRAQGSGEYIKCIYE | Function: Peptidoglycan polymerase that catalyzes glycan chain elongation from lipid-linked precursors.
Catalytic Activity: [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+)
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 26556
Sequence Length: 233
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.4.1.129
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Q8NJJ1 | MGKKAIQFGGGNIGRGFVAEFLHKAGYEVVFVDVMDKMVEALQQNKSYKVTEVSEEGEHTTTITNYRAINSKTHESDVIQEIATADVVTCAVGPHILKFIAPVIAKGIDARTESKPVAVIACENAIGATDTLHGFIKQHTSQDRVESLYDRAQFANSAIDRIVPQQAPNSGLDVRIEKFYEWAVEKTPFGSVGHPDIPAIHWVDNLEPYIERKLFTVNTSHATTAYFGHFRGKKMIADALEDEEIRGLVHKVLEETASLIVAKHDISEEEQKEYVKKIVSRISNPYLEDKVERVGRAPLRKLSRKERFIGPASQLAERGMKYDSLMDAVEMALRFQNVPGDDESAELANILNEQRAEDATIHLTGLDEEHPLYPAVLERVRKVQQGTK | Function: Catalyzes the NAD(H)-dependent interconversion of D-fructose 6-phosphate and D-mannitol 1-phosphate in the mannitol metabolic pathway. Has a strong preference for NADH over NADPH. Required for protection of conidiospores against exogenous stresses such as high temperatures and an oxidative environment.
Catalytic Activity: D-mannitol 1-phosphate + NAD(+) = beta-D-fructose 6-phosphate + H(+) + NADH
Sequence Mass (Da): 43363
Sequence Length: 388
EC: 1.1.1.17
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Q2UIM3 | MTLQAIKYSGGKLAIIDQLQLPHVEKYVTIHTSEEGWHAIKEMRVRGAPAIAIVAALALASELTTLIARNQLSSNAIETQTFITEKLHYLVSSRPTAVNLSDAAGKLETIVAESVKMPESTGHAVATAFIQAAEAMLAKDVEDNRMIGEYGAKWISENALSKNFTKATVLTHCNTGSLATAGFGTALGVIRALSSTDTLRHAYCTETRPYNQGSRLTAFELVHDRIPATLITDSMAAALLARAEIGVDAIVVGADRVAANGDTANKIGTYGLAVLAKYHGVKFLVAAPLTTIDLVTKSGNEITIEERPASEVTTVRGTCEDGGASEAVKMETVCIAAEGINVWNPAFDITPGALIDGIITEKGVVEKDSDGLFHLEELFKA | Function: Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
Catalytic Activity: S-methyl-5-thio-alpha-D-ribose 1-phosphate = S-methyl-5-thio-D-ribulose 1-phosphate
Sequence Mass (Da): 40449
Sequence Length: 381
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 1/6.
Subcellular Location: Cytoplasm
EC: 5.3.1.23
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Q0CFY3 | MTLQAIKYNNGDLAIIDQLQLPHVEKYVTIHNSEEGWHAIKDMRVRGAPAIAIVAALALASELHGLMAHDKLSPEAEDVQTFVVEKLRYLVSSRPTAVNLSDAARKLEVVVAQSARAPGATGKTVATAFIQAAEEMLVKDVEDNKKIGEHGAQWILKNSLEGHGKATVLTHCNTGSLATSGYGTALGVIRSLASADSLQHAYCTETRPYNQGSRLTAFELVHDALPATLITDSMAAALLASKKAGVNAIVVGADRVAANGDTANKIGTYGLAVLAKYHNVKFLVAAPLTTIDLNTKSGDQIVIEERLASEVTSIRGPRDNTGSEDVELVTVCTAAKGINVWNPAFDVTPAALIDGIITEKGVMEKDSAGMFHLEELF | Function: Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
Catalytic Activity: S-methyl-5-thio-alpha-D-ribose 1-phosphate = S-methyl-5-thio-D-ribulose 1-phosphate
Sequence Mass (Da): 40070
Sequence Length: 377
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 1/6.
Subcellular Location: Cytoplasm
EC: 5.3.1.23
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O31662 | MTHSFAVPRSVEWKETAITILNQQKLPDETEYLELTTKEDVFDAIVTLKVRGAPAIGITAAFGLALAAKDIETDNVTEFRRRLEDIKQYLNSSRPTAINLSWALERLSHSVENAISVNEAKTNLVHEAIQIQVEDEETCRLIGQNALQLFKKGDRIMTICNAGSIATSRYGTALAPFYLAKQKDLGLHIYACETRPVLQGSRLTAWELMQGGIDVTLITDSMAAHTMKEKQISAVIVGADRIAKNGDTANKIGTYGLAILANAFDIPFFVAAPLSTFDTKVKCGADIPIEERDPEEVRQISGVRTAPSNVPVFNPAFDITPHDLISGIITEKGIMTGNYEEEIEQLFKGEKVH | Function: Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
Catalytic Activity: S-methyl-5-thio-alpha-D-ribose 1-phosphate = S-methyl-5-thio-D-ribulose 1-phosphate
Sequence Mass (Da): 38860
Sequence Length: 353
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 1/6.
EC: 5.3.1.23
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Q2NL31 | MTLEAIRYSRGSLQILDQLLLPQQSRYEAVGSVRQAWEAIRAMKVRGAPAIALVGCLSLAVELQAGAGGPGLAALVAFVQDALSFLVTARPTAVNMARAARDLADLAAQEAEREGATEEAVRERVICWAEDMLDKDLRDNRSIGDLGAHHLLKRAAPQGGKVTVLTHCNTGALATAGYGTALGVIRSLHNLGRLEHAFCTETRPYNQGARLTAFELVYEQIPATLIADSMAAAAMAHQGVSAVVVGADRVVANGDTANKVGTYQLAIAAKHHGIPFYVAAPSSSCDLRLETGREIVIEERPDQELTDVNGVRIAAPGIGVWNPAFDVTPHDLITGGIITELGVFAPEELQAALSATIS | Function: Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
Catalytic Activity: S-methyl-5-thio-alpha-D-ribose 1-phosphate = S-methyl-5-thio-D-ribulose 1-phosphate
Sequence Mass (Da): 37826
Sequence Length: 358
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 1/6.
Subcellular Location: Cytoplasm
EC: 5.3.1.23
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Q0ITU1 | MGELGALQSIVYHRGSLRLLDQRKLPLEVDYIDVKCSGDGWNAIRDMVVRGAPAIAIAAALALAVEVSGLEDFTGTPAEAAVFVSEKLEYLVSSRPTAVNLSDAATKLRSLVSRTAETEKDAKAIFQAYIDAAETMLVDDVSDNKAIGSHGAEFLKQKLEVSKDISVLTHCNTGSLATAGYGTALGVIRALHSGGILEKAFCTETRPFNQGSRLTAFELVHDKVPATLIADSAAAALMKSGCIQAVIVGADRIAANGDTANKIGTYNLAISAKHHGVQFYVAAPITSIDLSLPSGEQIVIEERSPNELLNSEGGLGKQVAASGISVWNPAFDVTPANLITAIITEKGVITKSDADETFNIKDFIQSAKLYSTMQ | Function: Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
Catalytic Activity: S-methyl-5-thio-alpha-D-ribose 1-phosphate = S-methyl-5-thio-D-ribulose 1-phosphate
Sequence Mass (Da): 39508
Sequence Length: 374
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 1/6.
Subcellular Location: Cytoplasm
EC: 5.3.1.23
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A4S068 | MSSLEAIRYARGNLELLDQLALPLETKYIDVRDCNACWRCIKDMNVRGAPAIAIAAALALAVELEAKRGTLTTCEAAEAFVRERFDHMYTSRPTAVNLGEAKNRIQALAKRLSESGDVSGMIEGVIEGCEAMHAEDVASCRAIGDKGAAALLRACGAKDGENIKVMTCCNTGSLATAGYGTALGVIRALWESGRLERAYCLETRPYNQGSRLTAYELVYEKIPGTLICDNMAAALMARGDVDAIVVGADRVAANGDFANKIGTYSLAVNAKHHGVPMFTAAPVTTLDPETATGADIHIEERPGEEVTHSLGKRVAAEGIDVWNPSFDVTPAALLTGVITEHGVIEKNASGLFPVADFVAQAKGGT | Function: Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
Catalytic Activity: S-methyl-5-thio-alpha-D-ribose 1-phosphate = S-methyl-5-thio-D-ribulose 1-phosphate
Sequence Mass (Da): 38658
Sequence Length: 365
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 1/6.
Subcellular Location: Cytoplasm
EC: 5.3.1.23
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C1G9Q3 | MPLIAISYSHGKLSILNQLFLPHQTTYDPIYSACDAWHAIHDMRVRGAPAIAIVAALSLAVELYDLIQKGKLSDQAKEVEIFIREKLEYIASSRPTAVNLVEAAGRLGKIVVARSCGEGVTGREVAEEYIRAAEKMLEDDVKDNRGIGEFGAKWIMKQAIDGAEGKGKVAVLTHCNTGSLATAGYGTALGVIRSLHAANSLKHAYCTETRPYNQGSRLTAYELVHDNIPATLITDSMAAALLAHKSAGVGAIVVGADRVAANGDTANKIGTYGLAVLAKHHGVKFLVAAPRTTIDMNTKSGEGIAIEERPRQEMTRIRGPRVGGEQDGLGAMETITVAADGIDVWNPAFDVTPASLIDGIITEIGVVEKDRDGEFHLERVFE | Function: Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
Catalytic Activity: S-methyl-5-thio-alpha-D-ribose 1-phosphate = S-methyl-5-thio-D-ribulose 1-phosphate
Sequence Mass (Da): 40893
Sequence Length: 382
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 1/6.
Subcellular Location: Cytoplasm
EC: 5.3.1.23
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A6LE92 | MRFNEQADGVIILDQTLLPGKEAYLTLTTAEEIWDAIYKLKVRGAPAIGVAAAYGIYVCARRIDTAEKSVFVNEFRKIKEYLAGSRPTAVNLVAALNRMERVLVAHPTLSVPEWKELLYKEAIAIREEDAAACRQIGENCLELLRPGMGILTHCNAGHLAVSEYGTALAPIYLGQERGYGFKVFADETRPLLQGARLTAYELSRAGVDVTLICDNMASVVMRKGWVHAVVVGCDRVAANGDVANKIGTSGVAILARHYKIPFYVLGPTSTIDGSCPDGDSIVIEERNPDEVTEMWYSRRMAPKDVKVYNPAFDITPHELITAIITEKGIFYKNNR | Function: Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
Catalytic Activity: S-methyl-5-thio-alpha-D-ribose 1-phosphate = S-methyl-5-thio-D-ribulose 1-phosphate
Sequence Mass (Da): 36938
Sequence Length: 335
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 1/6.
EC: 5.3.1.23
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Q7U4V1 | MTLPPSLRWTGDHLELLDQRRLPEEVSFLKLHQWRDVAEAIATMAVRGAPAIGVAAAWGVVLAAQANEDLDLAVSVLKSSRPTAVNLGWALDRIKASPAAQEPVDPQGLAAVAAALEADDRARTQTLVDHGVGLLASGSRVLHHCHTGAIATAGVGTALGVIAAGHARGVVRHAWLDETRPRLQGAALSAWELGCLGVPCTVIVDGASGLLMRRQEVDAVLVGCDRVAANGDVANKVGTYNLALVARAHGIPFYVCAPGSSMDRSTSDGDAITIEERPQEEITQHRGQRLAAPGAAAWNPAFDITPAHLVTALITEFGVIRPPYRDALQALPLDRQP | Function: Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
Catalytic Activity: S-methyl-5-thio-alpha-D-ribose 1-phosphate = S-methyl-5-thio-D-ribulose 1-phosphate
Sequence Mass (Da): 35488
Sequence Length: 337
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 1/6.
EC: 5.3.1.23
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A5D1G8 | MLDTMRWTGDGLLELLDQTRLPFEKSYIKCTEYTDVAEAIKRLAVRGAPAIGAAAAYGLVLAARKIRANTKKEFLTELEARARELAATRPTAVNLHWALNRMLRKMRLAEPEDAGLLCDLLLEEAQAIFREDITGNRRMARYGLELIPEGARILTHCNAGALATAGYGTALGLVRAAHEAGRRVSVYAGETRPLLQGARLTAWEMLQEGIPVTLITDSMAGYLLAKGKADLVVVGADRIAANGDVANKIGTYSLAVLAREHKIPFYVAAPVSTIDLSLASGEEIPIEERDSSEVTHLAGRPVAPEGVNVWNPAFDVTPARLITAIITDRGIVKPPYDENLRKTVEGLNRNLVIELTAEDGKSNL | Function: Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
Catalytic Activity: S-methyl-5-thio-alpha-D-ribose 1-phosphate = S-methyl-5-thio-D-ribulose 1-phosphate
Sequence Mass (Da): 39529
Sequence Length: 364
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 1/6.
EC: 5.3.1.23
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C0QUC0 | MRKIKDIRPIQLKDHKLYVINQLKLPKEKEWLELSTYQQVAEAIEKMIIRGAPLIGIVGAYGFAIGVKQILDEGRSLDDVRDVFDRLKNTRPTAVNLFWALERVWKKFERWTEEGRSGEELVNLLFKEAERIDLEDYHANKAIGGYGQVLLPERCNVLTHCNTGALATSGWGTALGVIRSAFENGKDITVYVDETRPYLQGSRLTAWELVEEGIPHYLITDNSAGFLMSKGIIDAIIVGADRITANGDVANKIGTYTLAVLAEAHGIPFYVAAPTSTFDLDTDSGKDIPIEERSQLEVKKCGGCDIAPEETEALNYSFDVTPASKITAIITEKGIISHVDKEHITKFLRYRGV | Function: Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
Catalytic Activity: S-methyl-5-thio-alpha-D-ribose 1-phosphate = S-methyl-5-thio-D-ribulose 1-phosphate
Sequence Mass (Da): 39383
Sequence Length: 353
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 1/6.
EC: 5.3.1.23
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B2AML6 | MATLQAIKYSRGKLLVLDQLRLPHENHYDEVSTAEEAFDCIRSMRVRGAPAIAIVAALAHAVELHNGDCTATEPEEVIAHIEKRLDYLKESRPTAVDLSNAITLLKLATRAANLEGLAHPEAKEAILNTYIQTAEEILAKDLHNNTSIGSYGTAWLQQQYSASSEKPISVLTHCNTGSLATSGHGTALGIIRTLHSEGLLKHAYCTETRPYNQGSRLTSFELVFEGIPSTLITDSMAGALFNLHRERMNIGAVIVGADRVVRNGDTANKIGTYQLAVLARHHGVKFVVAAPTTSIDLETGNGSAIEIEERKREELTQISGAIVNEDGTVDTSKTARVAIADQRIGVWNPAFDVTPHELIDAIVTERGTVVKGADGKFDFSQVLPERLASVAARQL | Function: Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
Catalytic Activity: S-methyl-5-thio-alpha-D-ribose 1-phosphate = S-methyl-5-thio-D-ribulose 1-phosphate
Sequence Mass (Da): 42785
Sequence Length: 395
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 1/6.
Subcellular Location: Cytoplasm
EC: 5.3.1.23
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A7MK09 | MSKESQLEALVAACHWIGAKGWAPATGGNMSLREDARWCWLSESGKDKGSLTTDDFLQVDIATNLAPSGRKPSAETGLHTLIYRLFPEANCVLHVHTVNATVLSRVEKSDALHLSGYEMQKSLAGQITHLDDVPVAIFDNDQDIDALAERIARHHRQFPLRYGFLLRGHGLTCWGSDVAVARRHLEGLEFLFECEMQRRLLERA | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the dehydration of methylthioribulose-1-phosphate (MTRu-1-P) into 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P).
Catalytic Activity: S-methyl-5-thio-D-ribulose 1-phosphate = 5-methylsulfanyl-2,3-dioxopentyl phosphate + H2O
Sequence Mass (Da): 22791
Sequence Length: 204
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 2/6.
EC: 4.2.1.109
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Q66I75 | MSSVVNAAYAEYNGKEKGDQEDPRVLIPQLCRLFYELGWVTGTGGGISLRHGEHIYIAPSGVQKERIQPEDLFVCDIDEKDISCPPPQKKLKKSQCTPPFMNAYTMRGAQAVIHTHSKSAVMATLLFPGKEFRITHQEMIKGIRKGNSGTNFRYDDTLVVPIIENTPEEKDLKERMARAMDMYPDSCAVLVRRHGVYVWGETWEKAKTMCECYDYLFDIAVQMKQSGLDPSAFPTEEKGIV | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the dehydration of methylthioribulose-1-phosphate (MTRu-1-P) into 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P). Functions in the methionine salvage pathway. May play a role in apoptosis.
Catalytic Activity: S-methyl-5-thio-D-ribulose 1-phosphate = 5-methylsulfanyl-2,3-dioxopentyl phosphate + H2O
Sequence Mass (Da): 27231
Sequence Length: 241
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 2/6.
Subcellular Location: Cytoplasm
EC: 4.2.1.109
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Q54NY7 | MSNFDSEHPRVLIPELCKLFYGNGWVTGTGGGISIKRDKEIYIAASGVQKERILGEDIFVMDENENEISTPPTEKKLKASQCTPLFFNAYKYRDAGAVIHTHSQHAVMVTLLYQTEFIITHQEMIKGILSGHGENAKYLQYFDRLVIPIIENTPHERDLKERMHKAMEKYPNANAVLVRRHGVYVWGPDWVKAKTMCECFDYLFEIAIKMKQMGLDPTEVPHANEECCYDC | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the dehydration of methylthioribulose-1-phosphate (MTRu-1-P) into 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P).
Catalytic Activity: S-methyl-5-thio-D-ribulose 1-phosphate = 5-methylsulfanyl-2,3-dioxopentyl phosphate + H2O
Sequence Mass (Da): 26521
Sequence Length: 231
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 2/6.
Subcellular Location: Cytoplasm
EC: 4.2.1.109
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B4M1W5 | MALSIFKDLPGEHPRNLIPSLCRQFYHLGWVTGTGGGMSIKYNNEIYIAPSGVQKERMQPEDLFVQDIDGKDLQLPPEIKGLSKSQCTPLFMLAYRHRNAGAVIHTHSQHAVMATLLWPGKTFRCTHLEMIKGVYDEADKRYLRYDEQLVVPIIENTPFERDLADSMYAAMMEYPGCSAVLVRRHGVYVWGQTWEKTKTMSECYDYLFSIAVQMKQAGLDPEKFENALQA | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the dehydration of methylthioribulose-1-phosphate (MTRu-1-P) into 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P).
Catalytic Activity: S-methyl-5-thio-D-ribulose 1-phosphate = 5-methylsulfanyl-2,3-dioxopentyl phosphate + H2O
Sequence Mass (Da): 26284
Sequence Length: 230
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 2/6.
Subcellular Location: Cytoplasm
EC: 4.2.1.109
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Q8EKK8 | MGIRAIVVDTAGTTTDLTFIQDVLFPYSVKALPDFLAQNQHNVLVENCICDTRDIALEPDADLNRVTEILQQWVREDRKATPLKTLQGLIWKQGYAHDEFKGHIFPDFIEAVKRFSAQNLRIYSFSSGSVDAQKLLFSHSDGGDLTEMFNGHFDTRTGNKLDKQAYCNILNTISLSPKQVLFVSDVIEELKAADAAGMMTCQMVRDSKQRTGDFRTINSFDKLVIE | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene).
Catalytic Activity: 5-methylsulfanyl-2,3-dioxopentyl phosphate + H2O = 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + phosphate
Sequence Mass (Da): 25472
Sequence Length: 226
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 3/6.
EC: 3.1.3.77
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