ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
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Q8ZPD3 | MTIRFADKADCAAITEIYNHAVLHTAAIWNDRTVDTDNRLAWYEARQLLGYPVLVSEENGVVTGYASFGDWRSFDGFRYTVEHSVYVHPAHQGKGLGRKLLSRLIDEARRCGKHVMVAGIESQNAASIRLHHSLGFTVTAQMPQVGVKFGRWLDLTFMQLQLDEHAAPDAC | Function: Plays a role in the resistance against the toxic effects of L-methionine sulfoximine (MSX), a rare amino acid which inhibits glutamine synthetase (GlnA). Catalyzes the acetylation of MSX. It can also use L-methionine sulfone (MSO) . Also catalyzes the acylation of free L-amino acids using an acyl-CoA as acyl ... |
O13766 | MRLVLLFSCVLAVSSYAEIILAHSDENLLSRTKNNLSKWNENRLYDYGSKSTMSLPVSSLFPALQTLWIGVVADCSYVTHFTSRMEAKKHIFQEFEGVSTLYEDSFNINVQIHSLILPSAHDCSANVVDRPEISMSPRISIEEKLEIFSKWKYESPGNNVFEAISPHERESFPSEPQVSVLFTSSVKRSPHGVSWFATICSETHIENEWHVGPLSVVSAYPNDRLVVAHEIGHILGLIHDCNKKSCGDHSEACCPLSSSLCDAQELYIMNPSNSYTYANLRFSDCSILQLHSLVEKKYVSLSCLSKPSEKSVLRLGTCGN... | Cofactor: Binds 1 zinc ion per subunit.
Function: Has a role in the development of the spore envelope.
PTM: Glycosylated.
Sequence Mass (Da): 56440
Sequence Length: 512
Subcellular Location: Endoplasmic reticulum
EC: 3.4.24.-
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O43077 | MSNESIYSVLDLTQVIFEDRYLVKQKLGDGSFGTVYLAQRKEKNGLYETVAVKKLKNSSKPKPKHELLKLRESLALRKISKHPCLIDLLETFMDPYRNIFLVMEFMDCNLFQLFKRRQGRLFTKETAFNILLQIISGIEHIHKHGFMHRDIKPENILVKRISPKPISSRYSIKLGDFGLARPSVSSDPLTEYVSTRWYRAPELLLRSGSYNHSVDLYAFGCIVFEIYSLKPLFPGRNETDQLNRVCEILGNPGIDELDTLHYWSQAKELAKRLGFMLPPTKPYPIQKLLPQNCPEGHAKMIPCLLAWNPDVRPTAKYCKE... | Function: Protein kinase which is essential for spore formation.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 63224
Sequence Length: 559
EC: 2.7.11.1
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O14154 | MKHNEVFGWTLKVLSFLLVVIPANALDKHGWRKQSIYSLLTDRFASTNPKPCNPEDREYCGGNWRGIIDKLDYIQGMGFTAIWISPIIKNIEGRTKYGEAYHGYWPQDLYTLNPHFGTEQDLIDLADALHDRGMYLMVDTVVNHMGSSDPRNIDYGIYRPFNQSSHYHPMCPIEQDKPLSLEQCWIGTEDMTLPDIDTENPQIIETLYNFIHDQVKQFKIDGLRVDATKHVRRTFWPGFCESAGVYCQGEEWTGQADLFCEWQEYMDGLHNFPVQGVAAESVIPLNDRALRKTAIAMNLVAHHCKDSTLLGLFLESQDAP... | Cofactor: Binds 2 calcium ions per subunit. Calcium is inhibitory at high concentrations.
Catalytic Activity: Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.
Sequence Mass (Da): 58716
Sequence Length: 513
Subcellular Location: Endopla... |
P80540 | XKKPVRVAVTGAAGQIG | Function: Catalyzes the reversible oxidation of malate to oxaloacetate.
Catalytic Activity: (S)-malate + NAD(+) = H(+) + NADH + oxaloacetate
Sequence Mass (Da): 1663
Sequence Length: 17
EC: 1.1.1.37
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P19977 | AEPNVTVTGAAGQIGYALLFRI | Function: Catalyzes the reversible oxidation of malate to oxaloacetate.
Catalytic Activity: (S)-malate + NAD(+) = H(+) + NADH + oxaloacetate
Sequence Mass (Da): 2262
Sequence Length: 22
EC: 1.1.1.37
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Q9YEA1 | MITILGAGKVGMATAVMLMMRGYDDLLLIARTPGKPQGEALDLAHAAAELGVDIRISGSNSYEDMRGSDIVLVTAGIGRKPGMTREQLLEANANTMADLAEKIKAYAKDAIVVITTNPVDAMTYVMYKKTGFPRERVIGFSGILDSARMAYYISQKLGVSFKSVNAIVLGMHGQKMFPVPRLSSVGGVPLEHLMSKEEIEEVVSETVNAGAKITELRGYSSNYGPAAGLVLTVEAIKRDSKRIYPYSLYLQGEYGYNDIVAEVPAVIGKSGIERIIELPLTEDEKRKFDEAVQAVKKLVETLPPQLRE | Function: Catalyzes the reversible oxidation of malate to oxaloacetate. Can also oxidize tartrate. Can utilize both NAD and NADP. Catalytic efficiency for malate oxidation is 3-fold higher with NADP.
Catalytic Activity: (S)-malate + NADP(+) = H(+) + NADPH + oxaloacetate
Sequence Mass (Da): 33490
Sequence Length: 308
EC... |
A8EUE8 | MNNKTIGIIGVGNVGSTLAFILATNNICSNILLKDIKNNISEAMALDISQAMQETNSNTKITACLNNEDFKDCDIIIITAGIARKPNMSRDDLLITNAKIVASVMNDISKNNPNAIIIIISNPLDSMVYTALKSSNYPKNKILGMAGTLDSARMSYFIAEKLGFPNVNIKTSVIGGHGDSMVPLIDFSTVDGKKLNEVLSKEDIDDIVIKTKNGGGQIVKLLETGSAYYAPAYSTIAMIEAILNDTKKCFACATILNGEYGYKDIVSGVPVILGKDGVEKIIELEISDFEKEQFSNSINSVKESINILENNFFN | Function: Catalyzes the reversible oxidation of malate to oxaloacetate.
Catalytic Activity: (S)-malate + NAD(+) = H(+) + NADH + oxaloacetate
Sequence Mass (Da): 33995
Sequence Length: 314
EC: 1.1.1.37
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Q83C87 | MAKHVKVAVTGAAGQIGYALLFRLASGQAFGLDTTVDLHLLEIEPALPALKGVVMELEDCAFPLLRNMVVTSDPRVAFNDVNWALLVGAAPRKAGMERKDLLEKNGSIFAGQGKAINENAASDVRIFVVGNPCNTNCLIAMNNAPDIPKDRFYAMTRLDQNRAIGQLALKAGVDVPSVKNMIIWGNHSSTQYPDFYHATIDGKPATEVIRDKNWLLNDFISVIQQRGAAVIKARGASSAASAANAALDSVWSLINTTPADDNYSVALCAQGQYGVDEGLIFSFPCRTENGVVSVIEEIEHNEFGQQKLKETLDELREERD... | Function: Catalyzes the reversible oxidation of malate to oxaloacetate.
Catalytic Activity: (S)-malate + NAD(+) = H(+) + NADH + oxaloacetate
Sequence Mass (Da): 35469
Sequence Length: 328
EC: 1.1.1.37
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Q88Q44 | MDVQGELAQGKALDVWQAAVDSGSDTHVHGGAKAEMLEGSELVVITAGVPRKPGQSRQDVLSTNLPILDSIMADIKHHAPTATVLVVSNPVDVLTYRAWSVSGQGRDKVFGQAGVLDTARMKCFIAEQTGFSARDITALVLGGHGDSMVPLMRYCQIGSVPLSHFLSSEQIEQIVERTRKGGGEILGLKKTGSACDAPGVAIAQMVDAIANGRNRILPAVAILEGEYGRTDIAMGVPCVLAEKGLARIIELPLDAQEQAMFDHSADQVARDIAEMKAL | Function: Catalyzes the reversible oxidation of malate to oxaloacetate.
Catalytic Activity: (S)-malate + NAD(+) = H(+) + NADH + oxaloacetate
Sequence Mass (Da): 29434
Sequence Length: 278
EC: 1.1.1.37
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O59028 | MFEKGYVDENYIRVPKDRLFSFIVRVLTKLGVPEEDAKIVADNLVMADLRGVESHGVQRLKRYVDGIISGGVNLHPKIRVIREGPSYALIDGDEGLGQVVGYRSMKLAIKKAKDTGIGIVIARNSNHYGIAGYYALMAAEEGMIGISMTNSRPLVAPTGGIERILGTNPIALAAPTKDKPFLLDMATSVVPIGKLEVYRRKGKDIPEGWAINREGNITTKVEEVFNGGALLPLGGFGELLGGHKGYGLSLMVDILSGILSGGTWSKYVKNTSEKGSNVCHFFMVIDIEHFIPLEEFKEKISQMIEEIKSSRKHPEFERIW... | Catalytic Activity: (S)-malate + NAD(+) = H(+) + NADH + oxaloacetate
Sequence Mass (Da): 39751
Sequence Length: 360
Subcellular Location: Cytoplasm
EC: 1.1.1.37
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Q758T7 | MIEYMEYVLRQFERTTSWDRDYSYENITATSDNLLQFEIPDSLNLQISNQSTPNTFNTFELSNRSIINGSLSYLYTDCGQLDKIVQNSLKVPLQQRVDTYQCLRPGRTLGTSFRSQMLLYGRMYWPGSILEAMYCKRLTPQSQLVLKSLLSAAGESSILTLYWQRNAPWGSQDIVFSTNELLLGYRFLHNLSPGRSHEGSPHGQSTLSLGAEFWLGISNLLPGCSTALRYCTHATNTGKPITLTLSLNPLFGHISSSYSVKFSPGTTFCSKYDFNVYSIESNLSFGCEFWKSSAAAHKQATNEEETSIEVATETPVSDPR... | Function: Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis and may function in phospholipid exchange. MDM10 is involved in the late assembly s... |
Q4WVV6 | MLDFMDYIQLAFAEATNWNCDNSYSSLTATAQSLLDFSTPERLRVHLSSLATPHFATSYTLGTVGLIDGSVSYLYSTVPLNNTPSRSALIPLRKLARGYRQVQPPVAPVEDCGWQSCLGGLGSSESKPSGNDDSQPSPGRKATLLNATLHLPPPTILNALFLRRMSPTMQLSLAVCSTRGAPLSNSAPQASLLGQLSHDTGKYSNEYLFSTDNSLFGWRGLWNFGPDPRHPKENSSPQLSLLSAGAEAYYSPVSSLIGMSTGLRFSTLPAATEMPSSSSSASSTTTTSNHDTPISTFPYTLTLVLTPLTGSLSTTYSLRA... | Function: Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis and may function in phospholipid exchange. mdm10 is involved in the late assembly s... |
Q59LL4 | MYTYMEYLQKCFYKSTNWNEDNIYSNITATSQALLDFPIPNGFKIDSSSKTTDYSASSFTLSNHHQINGSLAYLYSSIPLTNTMGTKDVSLQDAIAGFRIIEPSVGLRSKLKNNIMSNRSSLLYGRMYFPGSALEAMIIKRLTKNSQLLIKCVNNPHLEKNGTMIVYLQNNTAKYSRELIYSTNEALIGLRCLYNLGDATSHNFTNINPAVIPKFDNSVVSIGTEIWYAARTMSPGLSAALRYSTRSTSTGKPLTMTLAINPIVGHVSSTYTVKTSVASTFCSKYDFNVFSYASNLSLGFELYSYANKKKNSFPSFEHHE... | Function: Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis and may function in phospholipid exchange. MDM10 is involved in the late assembly s... |
Q2H740 | MREFMHYVTNAFYGATGWNDDNTYKELNVTARELIDFPLPRGLRLTLSSLATPHFATSYQLGSVGIVDGSISYLHSSVPLTGIAARSDRIPLPALLRSYRRLHDLGSKDQQQYVGAEHAPTESTPPAVAKVDGSSLLYGRLYLPQSLLEGMVVRRFTPALQVQLSAVSERSLRNGGTLLGLVQYDKRKYGVEGLASTDGGLLGVRGLYNFGGDASSSAMNPPSGTSASETNGSGPSVEKERIYGRFSAGAELYYGTLNKSGGMSLGARFATLPAHRGTPLTATLTINPLMGNINATYAVLAREYCSLATKMEFNVYSYES... | Function: Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis and may function in phospholipid exchange. MDM10 is involved in the late assembly s... |
A8NWS6 | MHPFASYVLRTYYKATGWNEDNLYANLTRSSNAVLDFTVPRGLHFTVSKSPNPLFKTTYSMTAMPSLSGSLGYIFTSCDLNVLSSGTVRFKDMLDRFKVYDQPRRPEGKEEEWLAGERVDTRDYLLYGRFYLPSGRLDALYSTRLSPTVQLSVAAISDPISGTPVDGRRRTDPSNIMLNLQHDVGKWCTEYTYSAEDSMWGVRFLHNFGRLAPSSWETTNGENGTNTSAPGNASNSRAGVKRVDEEDAVEGGLRGRVSVGAELYFSAKERSAGVSTGIRFSTMPDATPPSAQIPPPSPFTPDPTTSGPSPALLNPRPYPQ... | Function: Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis and may function in phospholipid exchange. MDM10 is involved in the late assembly s... |
P0CO66 | MIGFSAFILRNYYAAIGWNEDNLYSSLTRTSSALLDFQLPQSLILQLANSPTPIFFTSYALDALPQLNGSISYITTSMPLDEIGSGRATAFKNVIERFRVFPPPKRPQPKDEVWLGGKRIEGRDYLLYSRLHLPSLHLSGLATTRLTPTLQAHLAFLSQPAHPTSTRPTPPQTPPSHTRQPSEPSTPAPSPTPGNVFISLQHDTGRYCGEYTYSVQDGMVGLRTLYNFGWHGDEESEVDKKERREREGKRIDEEEMMEGGLKGRFSAGGEVYFSAKQRSFGISTGLRFTTVPPTLPLPLNAPVPSPPTTLTLLYNPLIGF... | Function: Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis and may function in phospholipid exchange. MDM10 is involved in the late assembly s... |
C4QYM9 | MSFNINWDSIQKESLSAWTAELLNDALNSGKRPNVLCTDIQIEDLSFGTIPPDFEILEIGDLSSDSFRGIFKFNYDGDASITLRTKVQANPLKIYEDNLLDQFEDDQRELGEFIKPRFVMATDILEIPLNLKLSQIKLSSIIIIVFSRSKGLTLVFKNDPLESISVSSTFDRIKPLARFLQNKIETQISELFKEFLPSVLYKFSQKYTTENFADFHRELLHTQHPERNTENRVTLQDIDPEAPLIISPGSLMRLTTLSSSRQTLTLGGKISADKLNPDIITKNYFNELIPKTYNKFQLKADKVADIAQNIHSIKNLQSRI... | Function: Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondri... |
B0CXH5 | MSFTFNWPRFSDQFHYDAMQMLNTALNKGNKPPIIADKIEVVELEMGTQPPELEIRDIGDLTVDQFRGIFRLTYAGDAHLVLKTKVQANPLNHKQPDIHLMVGSGGMLAAKQPLVVPMLLRLSHFRLSSYVVLVVSKQKGITLVFKTDPLQNVDINSTFDSIAVIQKFIQREIEGQLRQMFREDLPGIIHRLSQQWVKAKVEAPYLSKHPPPPIPPEEISEPGDYGEEGEFPFGSPPNHHSLDPDPKIVLRPSLNNASIHQLSTLSHSNHTLSPYTRSLSHFTVRSVPPRGIGPSGLSASFERQPVKAKRKRTYRLGGRK... | Function: Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondri... |
A4QT54 | MAFNFNWSPLTADASFYKRARDLLTTALNKSPKPPIIVDDILVTEFNLGSVPPELEILEIGDLAEDRFRGIFKMTYSGDAFLTLKTRVQANPLNTYLYSKPSFTSPEPLAAASGLTIPLQITLSEIKLSAFIILVFSKQKGLTLVFRNDPLESLKVSSTFDSIQFVRDYLQRTIEGKLRNLMMDELPAIIHKLSLQLWCPEQMSKEDHEKTNEMDEQAVNPFASPPLDAVDAHGNLLDPIDISSIAVNGGAELQSLFSQKNLFRLGNLVNTQLTSSLFTPSVPEVIFRAKAGPVDKPEASSTTPLTTPSLVKSHSFHGTS... | Function: Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondri... |
A8QD14 | MSFNFTWPEFSAEFYEYAVQTLTTALNRGQKPKSIVGDIHVKGLHMGRVPPELEILEIGDLSRERFRGIFRFVYAGDAHLEFSTGVQANPLARGSEDHGIFSGPMTSRGMLFAASPLTVPMRVCLSDFKLRAIVVLVVSRTKGITLVFKNDPLESVKVSSTFDSVGVIQRYLQEEIEGQLREMFRADLPSIIHRLSQDWLRTESKEKVVPTPSAQPAKPAMPPVPSDVWPSHHTADVPLSVLALEEAAPSAYASHLTKLDTASQSSQGLKDLVQPAGSHPAGARTFHTTSRVRVPSSLESNAPPTPIALSSPGGLDVAGH... | Function: Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondri... |
Q7RZK9 | MAFNFNWSPLTADAGFYERARDLLTTALNKSPKPPIIVDDIFVTELNLGSVPPDLEILEIGDLAEDRFRGIFKMCYSGDAFLTLATRVQANPLNTYISAKPSFTSPEPLTASSSLTIPLQITLSEIKLSAFIILVFSKQKGLTIVFRNDPLESLKVSSTFDSIQFVRDYLQKTIEMKLRDLIMDELPAIIHRLSLQLWCPDQVPKEDEEAKEESDAAINPLATPPLDAVDAHGHRLDPAEISSLSLDGGPETQSLFSQKNLEKMDALASAHRTSSLLTPNILEVVFRAWAGQSDKPDATATPASTPNLHRTSSYQGSVHT... | Function: Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondri... |
A5DLK4 | MSFKVNWNTLETDSLREWTSQLLTDALNSGKRPPILASDIQIKDLNFGKVAPDFEILDIGELDSDRFRGIFKINYSGDFHLTLHTRVQANPLTIYQENSNASDAAFVTPNFLLASDPFALPLDLKLSDIRISGIGIIVFSRLKGLTLVFRNDPLDSIKVTSTFDTVQVLAKFLQNQIETQIRDLFRETLPTLIHRLSLKYLSSDDSSFLDDLRPQLAALHEETVSLMDIDPDVPYSPENLSRVSALFKSRETLRLAVPKIRHSVQRCRLEKFTKTQPSLVRCLHDNLNLDLVAAPQHTNEIPVELVSGADFSKTNHVLRE... | Function: Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondri... |
B2VS19 | MAFNFNWSPLIADTSRARDMLTTALNKSPKPPIIVDDIIVTELNLGTTPPELEILEIGDLAEDRFRGIFKMSYAGDAFLTLKTKVQANPLKTYLSNKPDFASPQPLAAAAGLTIPLQITLSNIRLSGFVILVFSKQKGLTLVFRNDPLESLKVSSTFDSIPFVRDYLQKEIEGQLRVLFMEDLPAIIHRLSLRMLSPEYQEIETEERLEGANDTTAAIDPLASPPEDAVDAFGNPLDEAQISAMSLDSGEIHASFSQKNILRLAALSESQRTLSLFTPGIREAVFRAWAGHPDRAESGAATPALTQGSLSRIQSTFGSLK... | Function: Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondri... |
Q9UUC9 | MSFRVKGWSDQFSESFYERATTLLTAALNKGTKHSMIADHITVKELDLGPQPPQLEILEVGDLAPDRFQGLFNLHYSGDASLVLQTKIRANPLSVQKSNVPSFSSRNTMLASRAPLTVPMFLRLSDLKLNGIVVLVFSKQKGITVVFRNDPLESVRVSSSFDSIPAIARFLQREIEVQLVSLFQEELPSIIYKMSRIWFAKSDSNLSFQKIPFTSPNQSHTSLANYNPDLLDGPPDYHESTKVDTHLPIKMGPLDVQTHPNIRSIASLALSRKALLPISSPSIPMSIYRSTPPDTIIQQLTTQSDDISAVSSPATQYSAS... | Function: Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondri... |
C4JQ45 | MAFNFNWSPLMADAGFYTRAQDLLTAALNKSPKPPIIVDDIAVTELNLGSIPPELEILEVGDLAEDRFRGIFKMSYSGDAFLTLKTRVQANPLNTFLITRPAYASPKPLAAASGLTIPLQITLSNFRLSGFVVLVFSKQKGITVVFRNDPLESLKVSSTFDSIPSVRDYLQREIEGQLRILFMDELPAIIHRLSLRLWVPEYRGLEAGIPETAIPSSLGPGEDTLLNPPKDPVDASGNLLSSAEIASLSLDSGVEMHSLFSQKNLLRLAALTNSQRTLSLFTPSIREVMFRARTGLADQGEGLGSGLMSPGSPALSRTHS... | Function: Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondri... |
B7NL82 | MSPCENDPPINWKRNLIVAWLGCFLTGAAFSLVMPFLPLYVEQLGVTGHSALNMWSGIVFSITFLFSAIASPFWGGLADRKGRKLMLLRSALGMGIVMVLMGLAQNIWQFLILRALLGLLGGFVPNANALIATQVPRNKSGWALGTLSTGGVSGALLGPMAGGLLADSYGLRPVFFITASVLILCFFVTLFCIREKFQPVSKKEMLHMREVVTSLKNPKLVLSLFVTTLIIQVATGSIAPILTLYVRELAGNVSNVAFISGMIASVPGVAALLSAPRLGKLGDRIGPEKILITALIFSVLLLIPMSYVQTPLQLGILRFL... | Function: Confers resistance to fosfomycin and deoxycholate.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 43863
Sequence Length: 408
Subcellular Location: Cell inner membrane
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Q21126 | MDNRGHFSSNGNFPPQGYHRREQSQEGMRIGNHHGPFSSGNMRSIGGSAQNQQQRHWTNMLNGSNNVENSWVCFSGNTSLADDPNVLSNFSALAQQRVNHFDTIVQERDNRNASFLNGSAVGNNLNTSFSVFGNLRGGDQDHRVLSDHTGIYTGLGSTGQNAVGTGIRLAADVANGNFLEQRAPTAMGHNQSYSALNQSLAPTLLDQYNQALLDQYNQSSQMAQGRGYPAPNIAYGLQNAGFPAPQIAHRPNTQNADPQAMNMNNRLRDHTFQMPHTNAQVPMSSLPGLFNLSMNHGSGNQQFQMNQSSSGPAPQLPNLS... | Function: P granule component, which acts redundantly with P granule component meg-2 to promote P granule segregation during embryogenesis, and germ cell proliferation and differentiation in larval stages . In its phosphorylated form, and together with meg-2, promotes the disassembly of zygotic P granules in the anteri... |
A0A0J6G7P5 | MNDKHKNFGFSTRAIHYGYNALENNGALIPPVYMTSTFAFPTVEYGAGCFAGEESGHFYTRISNPTLALLESRMAALENGEAGVAFSSGMGAIAATFWTLLRPGDEIIVNRTLYGCTFALLHHGIGEFGVVVKHVDMSNLAELEAAIGPATRMIYFETPANPNMQLVDIAAVSAIAHTHNDLIVVIDNTYCTPYLQRPLELGADVVVHSATKYLSGHSDITAGVVVTRQSLADRIRLQGLKDLTGAVLSPHDAHLLMRGIKTLALRMDRHCSSAQVIAQMLQDHPAVEWVAYPGLPSFPQYALASRQMKLPGGMIAFELK... | Function: Catalyzes the alpha,gamma-elimination of L-methionine to produce methanethiol, 2-oxobutanoate and ammonia.
Catalytic Activity: H2O + L-methionine = 2-oxobutanoate + methanethiol + NH4(+)
Sequence Mass (Da): 43025
Sequence Length: 399
EC: 4.4.1.11
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P13254 | MHGSNKLPGFATRAIHHGYDPQDHGGALVPPVYQTATFTFPTVEYGAACFAGEQAGHFYSRISNPTLNLLEARMASLEGGEAGLALASGMGAITSTLWTLLRPGDEVLLGNTLYGCTFAFLHHGIGEFGVKLRHVDMADLQALEAAMTPATRVIYFESPANPNMHMADIAGVAKIARKHGATVVVDNTYCTPYLQRPLELGADLVVHSATKYLSGHGDITAGIVVGSQALVDRIRLQGLKDMTGAVLSPHDAALLMRGIKTLNLRMDRHCANAQVLAEFLARQPQVELIHYPGLASFPQYTLARQQMSQPGGMIAFELKG... | Function: Catalyzes the alpha,gamma-elimination of L-methionine to produce methanethiol, 2-oxobutanoate and ammonia . Is involved in L-methionine catabolism . In fact, shows a multicatalytic function since it also catalyzes gamma-replacement of L-methionine with thiol compounds, alpha,gamma-elimination and gamma-replac... |
Q826W3 | MDDGRGAGGFGGGPAVRALDTEAVHAGRDDLARQGLHAAPIDLSTTYPSYDSRAEAARIDAFAADGAEPAGPPVYGRLGNPTVARFETALARLEGTDSAVAFASGMAALSAVLLVRNAMGLRHVVAVRPLYGCSDHLLTAGLLGSEVTWVDPAGVADALRPDTGLVMVESPANPTLAELDLRALAHACGSVPLLADNTFATPVLQRPAEHGARLVLHSATKYLGGHGDVMAGVVACDEEFARGLRQIRFATGGVLHPLAGYLLLRGLSTLPIRVRAASSNAAELARRLAADPRVARVHYPRIGGAMIAFEVYGDPHEVIA... | Function: Catalyzes the alpha,gamma-elimination of L-methionine to produce methanethiol, 2-oxobutanoate and ammonia. Is probably involved in L-methionine catabolism. Is also able to catalyze the alpha,gamma-elimination of L-homocysteine, and, to a lesser extent, the alpha,beta-elimination of L-cysteine.
Catalytic Activ... |
A9WC41 | MSSADWMAWIGRTEQVEDDICLAQAIAAAATLEPPSGAPTADSPLPPLWHWFYFLPRAPQSQLSSDGHPQRGGFIPPIPYPRRMFAGARIRFHHPLRIGQPARREGVIRNITQKSGRSGPLAFVTVGYQIYQHEMLCIEEEQDIVYREPGAPVPAPTPVELPPVHDAITRTVVPDPRLLFRFSALTFNAHRIHYDRPYAQHEEGYPGLVVHGPLVAVLLMELARHHTSRPIVGFSFRSQAPLFDLAPFRLLARPNGDRIDLEAQGPDGATALSATVELGG | Function: Involved in the glyoxylate assimilation cycle used to regenerate acetyl-CoA and produce pyruvate as universal precursor for biosynthesis. Catalyzes the hydration of 3-methylfumaryl-CoA (mesaconyl-C4-CoA) to (3S)-citramalyl-CoA.
Catalytic Activity: (3S)-citramalyl-CoA = 3-methylfumaryl-CoA + H2O
Sequence Mass ... |
A0KFN8 | MSARQEFASHHATFNHVWSSLLLEELFRLGVRDIALASGSRSAPLTMAAAAHPGFRRHLHFDERGLGFMALGLAKGSGRPVAVIMTSGTAVANLWPAVAEAQLTGVPLIILSADRPPELIDNGANQAIDQQGIFGRYPVYQQNLPSPTATIPAAFVLSSVDQALAQQARTPGPVHFNCMYPEPLYPGDAYLDFSAYLAPLGDWLRSSEPWSPWQLTQAPCPCQPDWDELQGKRGLIVAGRIQDPVQAKAVAALAERLGWPLLADLQSQLRFDGRNLVHADLALQHSGFVAELARAEVLLQFGARLISKRLGQFIKQQPWQ... | Cofactor: Binds 1 thiamine pyrophosphate per subunit.
Function: Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carb... |
B2UPN5 | MNSPASFVKSLLAQCCLGGICEWVVCPGARNMALLQVLAAAEDLVKWTHFDERSAAFFALGRIQDIGLPVAVVTTSGTAAAELLPAVVEAYYQRRPLLLLTADRPAACRGSAAPQAIEQADLFGIYAPTIDLETPESLPEDILQDWDYASPLHINVCLPDPDPAWNPGSCDLYPAEPPEENGFRGSLAELARALRFKSRGGLVVMIGGLDPTEQAPARWLANELKAPVVADATSGLREELAHLALTDADALLREHPPAVLLRLGDVPVARFWRDLEDIPATEVFSVTRTGFSGLARPSSVVTGDLEAILHALGDIDTVGD... | Cofactor: Binds 1 thiamine pyrophosphate per subunit.
Function: Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carb... |
Q5E480 | MQPEQQVMLNQVWAELIIEELVRNGVKHICIAPGSRSTPLTLAASEHALLSIHTHFDERGLGFLALGIAKASNDPVAVIVTSGTAVANLLPSVAESGLTKEKLVLLTADRPVELINCGANQAINQQGIFSSHVCHSLQLPSPSQNVPAQWLLSRLDQACFVQQEQGGAIHINCPFPEPFYGKKDDSLLVDYLAPIQNWKADTSSYIQQTPYFSHVTLSPNWMQTARKKGVVIIGKVSLEEANCAAQLAKELGWPVLADPQSGYYSEWAHYDLWLQNSACFELLSEVECVLQFGARLVSKRLGAWLKNYQQAYYLIDPHSE... | Cofactor: Binds 1 thiamine pyrophosphate per subunit.
Function: Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carb... |
A0JZP6 | MTSENPLDPNNAYAAADDAPLSEGDPTGAPADSGSDTLTAIQAARVAVKTLLDGGVRYVVVSPGSRSAPMAYALAEADAAGRVELLVRIDERSAGFTALGLALSTGAPVAVLTTSGTAVGNLLPAVMEANHAAVPLVVLSADRPDELRGTGANQTTDQLDLFGEHVRFAVDVPAGTNPQRAVETALSAATGVFEDTPPGPVQLNLAFRDPLVPPPADHLPEATGRRTWQIGRGPEPLTLAPAPATLAERRTVVLAGHDAGPVAEAFARAHGLPLLAEPSSNSRFGPNAVGPYRLLLEHFGPDSAQPIERVVLFGRPTLSR... | Cofactor: Binds 1 thiamine pyrophosphate per subunit.
Function: Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carb... |
Q81K94 | MNNHIEALSYYLGAFVDELTLLNVCDVVISPGSRSTPIALLMEQHEGMNTYLHVDERSAGFFALGIAKAKKRPVALLCTSGTAAANYYPAVCEAFHSRVPLIVLTADRPHELRDVGAPQAMNQINLYGTFVKQFTEMALPEASEAMYHYARLTTQRMIASACLAPQGPVHLNFPVREPLIPDFSLESLWDKGRGEYTGVVQQGNAVMPSEYVDSLVGRLSHMEKGLIICGDDSHSEIAAFATQLAEKTGYPILADPLSNIRSGHHDKTMVIDCYDTFLRNELLKETWKPDVLIRFGGMPVSKALTQFIKKQTKAVHIVVD... | Cofactor: Binds 1 thiamine pyrophosphate per subunit.
Function: Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carb... |
A8H9P4 | MQTEHTAELNLLWGTLILEELARLGVKHVCMAPGSRSTPLTLAAAKQTKLSQHIHFDERGLGFMALGLAKASQAPVAIITTSGTAVANLYPAVIEAWLTHVPLIVLSGDRPPELIDCGANQAIIQPAIFAQYAKQINLPTPDLNIAPQALLSLLDEAICNQSQPVHINCMYREPLYPNEPKVDFEHYLAPVKQWQQHTAPYSQFANLTSGLMPTADALARFVHGKGVIVAATLAPEQKPEQLIELAQKLGWPIVTDAQSQLRQHPAAIGNIDQLLHQPKSKALLAQAERVIVFGGRILSKRLIGYLAEQNWKDYWQVLPQ... | Cofactor: Binds 1 thiamine pyrophosphate per subunit.
Function: Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carb... |
A9GFL5 | MGGSNLHSAWAQLFVRALAQAGVRDLVLCPGSRSTPLAIAAMESEEVRCHSVVDERAAAFFALGQARVTGRPSVFVCTSGTAGAHALPAIIEAHQSFTPLIAITADRPWELADAAAAQTIDQTKLFGDHVRHFAELGLPDPSPLALRAVTRIAAQAVTRALSPTPGAVHINARFRKPLEPVDATGPEPWQAEWEALMRRAGTRVVSARAGVDGRAIEELAARCARAERGLIVCGPAESREDDARARRAVLALSRATGFPVLAEGTSQICFGGLTEGVVMPASFDSFLRAPEFRAANAPDLILELGAPPTSAGYATYIAEH... | Cofactor: Binds 1 thiamine pyrophosphate per subunit.
Function: Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carb... |
Q9CBA8 | MSRAALDKDPRDVVAMFDDVAHRYDLTNTVLSLGQDRYWRRATRSALRIGPGQKVLDLAAGTAVSTAELSKSGAWCVAADFSVRMLATGGARKVPKVAADATQLPFSDGVFDAVTISFGLRNIADYQAALREMARVTRPGGQLVVCEFSTPTNALVANVYTEYLMRALPQVARLVSSNPDAYIYLAESIRAWPDQVTLACQLSRTGWASPRWRNLTGGIVALHAADKPVR | Function: Methyltransferase required for the conversion of demethylmenaquinol (DMKH2) to menaquinol (MKH2).
Catalytic Activity: a 2-demethylmenaquinol + S-adenosyl-L-methionine = a menaquinol + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 24987
Sequence Length: 230
Pathway: Quinol/quinone metabolism; menaquinon... |
C4K014 | MRLSVSLLALAFGSLVAAAPNTKPRTCGSKPSMEFLAKSAEFAAKEASGELLNSLATIEVETYFHVVASGRTPSQGYLSDAMLANQLRVMNSDYGPHGIQFNLVRTTRTVNANWARDGDELGMKRALRQGGYNALNVYFLGDLGSLLGYCYFPTNASPGSTAFIRDGCVVVGQSVPGGNISNYNLGKTATHEVGHWFGGCFGSGDGVSDTPPQRSSTQGCPSSRDSCPGGGVDPIHNYMDYSYDVCMNQFTSGQRTRIYNMWNQYRARG | Function: Secreted metalloproteinase that allows assimilation of proteinaceous substrates.
Sequence Mass (Da): 28951
Sequence Length: 269
Subcellular Location: Secreted
EC: 3.4.24.-
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C9S5C6 | MLFKSLFVAAATAVGVSGHVAREAPRTFGCGTHEPSAEHVGMSKVLAAQEARVLESGNLTARATINVNVYFHVVAASQTVANGYLTDKMVTDQIAVLNRDFAPHDVAFRLAGTDRTVNTGWARDSNEIAMKRALRKGTYKDLNLYTQVSLTDNALGYAYFPTSGATSGSTTFIRDGVSIKAQTVPGGSQAGFNLGKTGTHEVGHWLGLYHTFQGGCTGSGDQVSDTPAQASFSSGCPIGRDSCPGQAGLDPIHNYMDYSDDSCYEEFTPGQDARIHSFWTTYRA | Function: Secreted metalloproteinase that allows assimilation of proteinaceous substrates.
Sequence Mass (Da): 30337
Sequence Length: 284
Subcellular Location: Secreted
EC: 3.4.24.-
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P40260 | MESRTTGPLTTETYDGPTVAFMILGAALVFFMVPGLGFLYSGLARRKSALALIWVVLMATLVGILQWYFWGYSLAFSKSAPNNKFIGNLDSFGFRNVYGKKFDEDAYPELAYATFQMMFSCVNLSIIAGATAERGRLLPHMVFLFILATIGYCPVTYWIWSPGGWAYQWGVLDWAGGGNIEILSAVSGFVYSWFLGKRNEKLLINFRPHNVSLVTLGTSILWFGWLLFNSASSLSPNLRSVYAFMNTCLSAITGGMTWCLLDYRSEKKWSTVGLCSGIISGLVAATPSSGCITLYGSLIQGIVAGVVCNFATKLKYYAKV... | Function: Transporter for ammonium (both charged and uncharged NH3 and NH4) to use as a nitrogen source. Can also transport methylamine. The affinity of MEP1 is about twenty times lower than that of MEP2. MEP3 has the lowest affinity.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 54202
Sequence Len... |
C9SSK8 | MQSKFLWIAAASAATAAAQVPARLCGTAQPTMDDLVIAAGLAAEGKDNRRGLHPEDPIVVPTLFHVLAINETVAGGYLTEKSLQDQLDVMNADFGPSNVIFNLTATTRTVNRRWAQDLDEIPMRRALRQGGQETLNIYFMPYVSGYLGYCTFPNFWDAGSDEFIYDGCAVLSDSLPGGSLARYNLGRTATHEIGHWFDLFHTFSGGCGCVGDMIHDTPAMLNATGGCPVGKDTCPDRPGLDPIHNYMDYSDDACMNEFTPGQNFRMRSAWYNIRTK | Function: Secreted metalloproteinase that allows assimilation of proteinaceous substrates.
Sequence Mass (Da): 30250
Sequence Length: 276
Subcellular Location: Secreted
EC: 3.4.24.-
|
Q0CFJ0 | MRLLSLAGAMALPLCVLAHPTHRTRGIARRGIDLTPYRLPGNAEYTSSRTSAMRSLLFERADGEDYVETAKKVLQSVHPDATFRVIDDHYVGDNGVAHVHLLQTAHGIDIDNANFNVNIDKNGKVLSYGNSFFSGKIPDSDPLTKRSFSDPVEALKAAATGLGIPLTADDVTSEGLDGTTSYTFKGTKGALSDPTADLVYLAKPDNTLALTWRVETDMNSNWLLTYVDAETAETIHGVVDYISDATYQVYPWGLNDPTEGSRQILEDPWDSKASEFTWIGDGKAKYKTTRGNNGIAQSNPDGGDDYLNNHRPESSSLKFV... | Cofactor: Binds 1 zinc ion per subunit.
Function: Secreted metalloproteinase that allows assimilation of proteinaceous substrates.
Sequence Mass (Da): 68841
Sequence Length: 633
Subcellular Location: Secreted
EC: 3.4.24.-
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C7Z3B7 | MRSVDSLLLLGLTGLASQANAHPAKRQPNDSPLSKRGVDLDAFRLPELAKYVPQDEVPDISNARIAPSSDYTKTAEEFVKSVVGKATFRLVSDHYVGTNGVAHVRFKQTVNDIDVDNADFNVNIGADGKVFSYGNSFYTGKIPGPLVKRDTSDPVTALKSTVEVLDLPVDASDAKAEPKGDEHYTFTDTSGTVKKPEAKLVYLIDGEQNLKLTWRVETDVLDNWLLTYVDADKTEKVVGVVDYVADLATYEVYPWGVNDPSKGSRSVVEDPWNIATSEFTWISDGSANYTTTRGNNAIAQVNPSGGTAYLNNYRPSSSSL... | Cofactor: Binds 1 zinc ion per subunit.
Function: Secreted metalloproteinase that probably acts as a virulence factor . Cleaves Z.mays Endochitinase A (CHIA) between residues 'Gly-29' and 'Cys-30' .
Sequence Mass (Da): 68995
Sequence Length: 637
Subcellular Location: Secreted
EC: 3.4.24.-
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Q9DGW5 | MSQEPEPGAMPYSPADDPSPLDLSLGSTSRRKKRKSHDIPNSPSKHPFPDGLSEEEKQKLERRRKRNRDAARRRRRKQTDYVDKLHEACEELQRANEHLRKEIRDLRTECTSLRVQLACHEPVCPMAVPLTVTLGLLTTPHDPVPEPPICTPPPPSPDEPNAPHCSGSQPPICTPPPPDTEELCAQLCSTPPPPISTPHIIYAPGPSPLQPPICTPAPPDAEELCAQLCSTPPPPICTPHSLFCPPQPPSPEGIFPALCPVTEPCTPPSPGTVYAQLCPVGQVPLFTPSPPHPAPEPERLYARLTEDPEQDSLYSGQIYT... | Function: Functions as a DNA-binding transcription factor. Promotes transformation, host cell growth, host cell-cycle progression through G1/S phase, and possesses antiapoptotic activity. Forms functional heterodimers with host JUN. These heterodimers bind with high affinity DNA sequences called MEQ-responsive elements... |
Q28C98 | MSSDAALILEAANFAAEKHKQQRRKDPEKTPYINHPLGVARILSHEGGITDTAVLQAALLHDTVEDTNTTFEEIELHFGQDVRNIVEEVTDDKTLPKMERKRLQMEHAPHCSQKAKLVKLADKLYNLRDLKRCTPEGWSEQRVQEYFQWASEVVKGLRGTNSILEGKLDHMFMDQGIAV | Function: ppGpp hydrolyzing enzyme involved in starvation response.
Catalytic Activity: guanosine 3',5'-bis(diphosphate) + H2O = diphosphate + GDP + H(+)
Sequence Mass (Da): 20390
Sequence Length: 179
EC: 3.1.7.2
|
O08574 | MAQSSPPQSLQGLVPLGLLPGLGLGSAIGLHVSGLVLRFVRFLPFYATRRPSQPAGPARSTRTTQATAPRRTRPAPAGGQRQSASEREKLRMRTLARALQELRRFLPPSVAPAGQSLTKIETLRLAIRYIGHLSALLGLSEDSLRRRRRRSADAAFSHRCPQCPDGGSPSQAQMLGPSLGSAMSSGVSWGCPPACPGPLISPENLGNRISNVDPRVTPPYCPQIQSPLHQSLERAADSSPWAPPQACPGMQMSPEPRNKTGHWTQSTEPAELTKVYQSLSVSPEPRLSLGSPLLLPRPSCQRLQPQPQPQPQWGCWGHDA... | Function: Transcription factor with important role in somitogenesis. Defines the rostrocaudal patterning of the somite by participating in distinct Notch pathways. Regulates also the FGF signaling pathway. Specifies the rostral half of the somites. Generates rostro-caudal polarity of somites by down-regulating in the p... |
Q5EB52 | MVRRDRLRRMREWWVQVGLLAVPLLAAYLHIPPPQLSPALHSWKSSGKFFTYKGLRIFYQDSVGVVGSPEIVVLLHGFPTSSYDWYKIWEGLTLRFHRVIALDFLGFGFSDKPRPHHYSIFEQASIVEALLRHLGLQNRRINLLSHDYGDIVAQELLYRYKQNRSGRLTIKSLCLSNGGIFPETHRPLLLQKLLKDGGVLSPILTRLMNFFVFSRGLTPVFGPYTRPSESELWDMWAGIRNNDGNLVIDSLLQYINQRKKFRRRWVGALASVTIPIHFIYGPLDPVNPYPEFLELYRKTLPRSTVSILDDHISHYPQLED... | Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 38830
Sequence Length: 335
Subcellular Location: Endoplasmic reticulum membrane
EC: 3.-.-.-
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Q07646 | MVRRDRLRRMREWWVQVGLLAVPLLAAYLHIPPPQLSPALHSWKTSGKFFTYKGLRIFYQDSVGVVGSPEIVVLLHGFPTSSYDWYKIWEGLTLRFHRVIALDFLGFGFSDKPRPHQYSIFEQASIVESLLRHLGLQNRRINLLSHDYGDIVAQELLYRYKQNRSGRLTIKSLCLSNGGIFPETHRPLLLQKLLKDGGVLSPILTRLMNFFVFSRGLTPVFGPYTRPTESELWDMWAVIRNNDGNLVIDSLLQYINQRKKFRRRWVGALASVSIPIHFIYGPLDPINPYPEFLELYRKTLPRSTVSILDDHISHYPQLED... | Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 38907
Sequence Length: 335
Subcellular Location: Endoplasmic reticulum membrane
EC: 3.-.-.-
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Q09878 | MVATDSSDQVAKFDVSHKIIEDIVYSLSNRIFSYAEHVPLNRYLTQWNNSGRRNGFSNNVELFNLEARSGASAFLLGSYTAAISSPGVYSMMTPSSCLSLLNPLLSNIIPFYGASKPLVVHVAALAYLEQTYCADNVSVLDFSYANNFTVFASQSNVEAAHLALASTLAAKAAPVIHVYEPDAIVTTTDPSLPLLDSNAVVECFNSYQSEADPVSNASKALKHVNDYFNTSYAPAEYYGSQTASKVIVTFGKSETVAARALLAANPDVGVLSIRIFPFVAENIFNVLPTTCKSLVVLSQVRSTAVGTSSIYYSFLLATLL... | Cofactor: Binds 1 FAD per subunit.
Function: This enzyme catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate (By similarity).
Catalytic Activity: 3 H2O + hydrogen sulfide + 3 NADP(+) = 4 H(+) + 3 NADPH + sulfite
Sequence Ma... |
L0E1U3 | MPLVAHSNLPTFERLRKEGGTVLPNDYALHQDIRALHIGLLNMMPDAALAATERQFFRLVGESNQIAQFYMHPFTLAELPRGPGGQAHVERYYETFDTIQREGLDALIITGANVSQPDLALEPFWEPLAEVVEWAWKNVTSTLCSCLTTHAVMQSRYGERRRHRGAKLWGVFDHRVVDRTHPLVAGVNTRFDVPHSRFNDVSREQFDRHRLKVLVESERAGVHLAVSEDGFRLVFFQGHPEYDSISLLKEYKREVLRFVNGEREEFPPLPERYLSPQAAAILEEHRERVEQARQRRVPAPELPEPLLVGRLDNTWHDSAL... | Function: Transfers a succinyl group from succinyl-CoA to L-homoserine, forming succinyl-L-homoserine.
Catalytic Activity: L-homoserine + succinyl-CoA = CoA + O-succinyl-L-homoserine
Sequence Mass (Da): 41011
Sequence Length: 356
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; O-succiny... |
Q9KRM5 | MPIRIPDQLPASDVLRNENIFVMSESRASTQEIRPLKVLLLNLMPKKIETETQFLRLLSNSPLQVDIELLRIDDRPSKNTPEEHLNTFYRQFELVKNRNFDGLIITGAPLGLVQFEDVAYWQHLQNIMAWAKAHVTSTLYICWAAQAGLKLLYNLPKRTREEKLSGVYYHDIHKPFHPLLRGFDDRFLAPHSRYADFDAEFLAEHTDLDILATSDVAGVYLAATKDKRNVFVTGHPEYDAYTLHGEYVRDLGEGLNPAIPVNYYPNDNPDNKPCASWRSHGHLLFANWLNYCVYQQTPYDLEKFSEANFTKDE | Function: Transfers a succinyl group from succinyl-CoA to L-homoserine, forming succinyl-L-homoserine.
Catalytic Activity: L-homoserine + succinyl-CoA = CoA + O-succinyl-L-homoserine
Sequence Mass (Da): 36199
Sequence Length: 313
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; O-succiny... |
P84542 | GVTGFGFDLVRYLFAGVVDGR | Function: Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation.
Catalytic Activity: 5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine = L-methionine + tetrahydropteroyltri-L-glutamate
Sequence Mass (Da): 2246
Sequence Length: 21
Pathway: Amino-... |
P85918 | FALESFWDGKGNASAHAMEMTK | Function: Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation.
Catalytic Activity: 5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine = L-methionine + tetrahydropteroyltri-L-glutamate
Sequence Mass (Da): 2429
Sequence Length: 22
Pathway: Amino-... |
P31547 | MSEPMMWLLVRGVWETLAMTFVSGFFGFVIGLPVGVLLYVTRPGQIIANAKLYRTVSAIVNIFRSIPFIILLVWMIPFTRVIVGTSIGLQAAIVPLTVGAAPFIARMVENALLEIPTGLIEASRAMGATPMQIVRKVLLPEALPGLVNAATITLITLVGYSAMGGAVGAGGLGQIGYQYGYIGYNATVMNTVLVLLVILVYLIQFAGDRIVRAVTRK | Function: Part of the binding-protein-dependent transport system for D-methionine and the toxic methionine analog alpha-methyl-methionine. Probably responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 23256
Sequence Length: 217
Subcel... |
P46492 | MWGVVATATYETVYISFASTLLAVLVGVPVGIWTFLTGKNEILQNNRTHFVLNTIINIGRSIPFIILLLILLPVTRFIVGTVLGTTAAIIPLSICAMPFVARLTANALMEIPNGLTEAAQAMGATKWQIVRKFYLSEALPTLINGVTLTLVTLVGYSAMAGTQGGGGLGSLAINYGRIRNMPYVTWVATIIIVLFVMISQKLGDTLAKKVDHR | Function: Part of the binding-protein-dependent transport system for D-methionine. Probably responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 22935
Sequence Length: 213
Subcellular Location: Cell inner membrane
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Q9KTJ6 | MSFNTIAQWFALNSDLLLTATWQTLYMVAIAGAVGFALGIPLGVILHTTKKEGLLENLPLNRALGAVVNIGRSVPFLVLMVAIIPVTKLIVGTFIGTTAAIVPLTIGAIPFVARLIESALLEVPTGLVEAAQSMGATPLQIIRKVLLPEALPTILNSVTITLVTLVSYSAMAGTVGGGGLGDVAIRYGFHRYDITIMAVTVVMLIVLVQIIQSIGDALVRRVDHR | Function: Part of the binding-protein-dependent transport system for D-methionine. Probably responsible for the translocation of the substrate across the membrane (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 23762
Sequence Length: 225
Subcellular Location: Cell inner membrane
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Q8ZH39 | MSEAMMWLMARGVWETLMMTFVSGFFGFVLGLPVGVLLYVTRPGQIIANNKIYRTLSGVVNIFRSIPFIILLVWMIPFTRMIVGTSIGLQAAIVPLTVGAAPFIARMVENALLEIPSGLVEAARAMGATPMQIIKKVLLPEALPGLVNAATITLITLVGYSAMGGAVGAGGLGQIGYQYGYIGYNATVMNTVLVLLVILVYLIQLSGDRIVKAVTHK | Function: Part of the binding-protein-dependent transport system for D-methionine and the toxic methionine analog alpha-methyl-methionine. Probably responsible for the translocation of the substrate across the membrane (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 23218
Sequence Le... |
Q5E7R2 | MAKHLFTSESVSEGHPDKIADQISDAVLDAILEQDPKARVACETYVKTGMVMVGGEVTTSAWVDIEEITRETVREIGYVHSDMGFDANSCAVLNTIGKQSPDINQGVDKADPKEQGAGDQGIMFGYATNETPILMPAPITYSHLLVQKQAEVRKSGKLDFLRPDAKSQVTFQYDQGKIVGIDAVVLSTQHCDSVTTPDLREAVMEEIIKPVLPAEWLNKDTNFFINPTGRFVIGGPMGDCGLTGRKIIVDTYGGAARHGGGAFSGKDPSKVDRSAAYAARYVAKNIVAAGMADRCEIQLSYAIGVADPTSIMVETFGTEK... | Cofactor: Binds 2 divalent ions per subunit.
Function: Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the en... |
Q9K5E4 | MAQPTAVRLFTSESVTEGHPDKICDAISDTILDALLEKDPQSRVAVETVVTTGIVHVVGEVRTSAYVEIPQLVRNKLIEIGFNSSEVGFDGRTCGVSVSIGEQSQEIADGVDNSDEARTNGDVEEDDRAGAGDQGLMFGYATNETEEYMPLPIALAHRLSRRLTQVRKEGIVPHLRPDGKTQVTFAYDAQDRPSHLDTVVISTQHDPEVDRAWLETQLREHVIDWVIKDAGIEDLATGEITVLINPSGSFILGGPMGDAGLTGRKIIVDTYGGMARHGGGAFSGKDPSKVDRSAAYAMRWVAKNIVAAGLADRAEVQVAY... | Cofactor: Binds 2 divalent ions per subunit.
Function: Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the en... |
Q83A78 | MTHTTLFTSESVSEGHPDKVADQISDAVLDALIGQDPNCRVACEAVVKSGMVFVAGEITTNAWADVEQITRNTVLQIGYNDPHLGFDGETCAVVTAIGKQSPDIVMGVDGREDQELGAGDQGLMFGYASRETNVFMPAPITYAHRLVRQQALLRKNGRLPWLRPDAKSQVTLRYENGKPVAADCIVLSTQHSPEISQESLREAVIDEIIKPIMPPHWLDKHTRFLVNPTGRFVIGGPVGDCGLTGRKIIVDTYGGMARHGGGCFSGKDPSKVDRSGAYAARYVAKNIVAGGLADRCEIQVSYAIGVAEPTSISVETFGTG... | Cofactor: Binds 2 divalent ions per subunit.
Function: Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the en... |
Q2RK28 | MTRKLFTSESVTEGHPDKIADRIADAVLDAIYAKDNQARVACECLVSTGLILVAGQITTDCYVDIPRVARETVREIGYTRAKFGFDCDTCAVITSIDEQSPDIAMGVNEAWEKKQGEARDEVETLGAGDQGMMFGYATSETPEFMPMPIALAHALTRRLAAVRKERILPYLRPDGKSQVTVEYEDGRPVRVDTVVISTQHRPDIDMATLRDEVLETVIKPVIPAEMLDNRTRYFINPTGRFVIGGPQGDTGLTGRKLIVDTYGGMARHGGGALSGKDPTKVDRSAAYAARYVAKNVVAAGLADRCEVQVAYAIGVARPVS... | Cofactor: Binds 2 divalent ions per subunit.
Function: Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the en... |
P78003 | MAKTIKHPRWGRYVAEAVGRGHPDKICDQIADSILDECIKQSPTSHVACEVFASKNLIMVGGEILTTGYVDVVQTGWKVLNRLGYTENDFSFLSCINSQSSEINQAVQSNDEIGAGDQGITVGYACSETEQLMPLGSIVAQALVQRAARIIDQYPFIKHDMKSQVVLNYTGNKVQCESVLMSVQHTQDVSLDQLRQTIINQVILPVLTEYGLNDPKIKHLVNPGGSFVVGGPMADTGLTGRKIIVDTYGPYANHGGGSFSGKDPTKVDRTGAYFARFIAKHIVSLGWAEECEVSISWVFSQPLPQSIQVKCFNINKEFSE... | Cofactor: Binds 2 divalent ions per subunit.
Function: Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the en... |
Q87UV4 | MTATAQRQLPLDTTGAGQLAQQAELHPELNRAHVRFINLGKTYHGKQGAVEALGSIDLAIQRGEIFGIIGRSGAGKSSLIRTINRLEQPSSGRVLIDQVDIGEFNEDKLVELRRRIGMIFQHFNLMSAKTVWQNVELPLKVAGVPKEQRARKVTQLLELVGLQDKHKAYPAQLSGGQKQRVGIARALVHDPAILLCDEATSALDPETTQSILGLLREINQRLGLTIVLITHEMAVIRDICHRVVVLEQGRIVEQGPVWQVFGDPQHEVSKTLLAPLQLGLPKEWAERLSEYPQRPDAAILLDVHFTGVSDEGPDLAALFA... | Function: Part of the ABC transporter complex MetNIQ involved in methionine import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + L-methionine(out) = ADP + H(+) + L-methionine(in) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 41335
Sequence Len... |
Q0SFY5 | MIEVRSVTKRFGKGSRSVEVLHDIDFSVGTGQIAAVIGQSGAGKTTLSRIISLLERPSEGRILLDGTDVSGLSERRLRDQRRAIGTIFQASSLLARRTAAENVALPLEFAGVGRSERRARVAELLGRVGLSDKADLYPRQLSGGQRQRVGIARSLALAPKVLVSDEATSGLDPNTTRSILALLRELRDDLGLTIVLITHEMDVVRQVADVVTVLDAGRVVESGPVIELLRDPHSELGVGLLPDRSHITAEDRDVLWHVTYGSDTVPTNWIELLGKATGRSIGVLSGTVESVGGRPAGRVTISVAGEHPSVGDLLSSWGLH... | Function: Part of the ABC transporter complex MetNIQ involved in methionine import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + L-methionine(out) = ADP + H(+) + L-methionine(in) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 36030
Sequence Len... |
Q57T09 | MIKLSNITKVFQQGARTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESELTKARRQIGMIFQHFNLLSSRTVFGNVALPLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSHPKTPLAQKFIQSTLHLDIPEDYQARLKASPETDSVPMLRMEFTGQSVDAPLLSETARRFNVNNNIISAQMDYAGGVKFGIMLTEMHGTQ... | Function: Part of the ABC transporter complex MetNIQ involved in methionine import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + L-methionine(out) = ADP + H(+) + L-methionine(in) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 37631
Sequence Len... |
A4J778 | MSILFSPAQIGTLQLRNRIIMTPMHLGYTPNGEVTDQLIEFYRVRARGGAGLIVVGGCGIDRIGNAYGMTQLDDDRFIPGLRRLADAVQAEGAKIVAQLYQAGRYAHSALTGQPAVAPSPIPSKLTGETPVELTEEKIAEIVASFAKAAKRAKTAGFDGVEIIASAGYLISQFLSPLTNKRTDRYGGDLQARMTFGLEVVAAVREAVGSDYPIIVRVAGNDFMPGSHTNTEAQVFCQAMEKSGVNAINVTGGWHETQVPQITMNVPPGAYAYLAYGIKQAVSIPVIACNRINTPDLAEAILQEGKADFIGMARSLMADPE... | Function: Metal reductase able to reduce Fe(III)-chelates to Fe(II)-chelates, as well as soluble Cr(VI) and U(VI), using NADH as electron donor. Cannot use NADPH as an electron donor. Is unable to reduce riboflavin and FMN with NADH as electron donor. May have an in vivo role in metal reduction in D.reducens, which is ... |
Q8VE43 | MRGAVWAARRRAGQQWPRSPGPGPGPPPPPPLLLLLLLLLGGASAQYSSDLCSWKGSGLTREARSKEVEQVYLRCSAGSVEWMYPTGALIVNLRPNTFSPAQNLTVCIKPFRDSSGANIYLEKTGELRLLVRDIRGEPGQVQCFSLEQGGLFVEATPQQDISRRTTGFQYELMSGQRGLDLHVLSAPCRPCSDTEVLLAICTSDFVVRGFIEDVTHVPEQQVSVIYLRVNRLHRQKSRVFQPAPEDSGHWLGHVTTLLQCGVRPGHGEFLFTGHVHFGEAQLGCAPRFSDFQRMYRKAEEMGINPCEINME | Function: Hormone induced following exercise or cold exposure that promotes energy expenditure. Induced either in the skeletal muscle after exercise or in adipose tissue following cold exposure and is present in the circulation. Able to stimulate energy expenditure associated with the browning of the white fat depots a... |
S2L5R8 | MDSDTLMPELPSDSVGLVAPQTAHFDVPLALACGKTLQSYDLVYETYGKLNASRSNAVLICHALSGHHHAAGYHSREDRKPGWWDAHIGPGKSIDTDRFFVISLNNLGGCHGSTGPCAINPDTGRQWGPDFPMMTVGDWVHSQARLADRLGIERFAAVIGGSLGGMQVLQWSLAYPERIANAVVIAATPKLSAQNIAFNEVARQAIRSDPDFYDGWYAEHDTLPRRGLKLARMVGHITYLSEDAMGSKFGRDLRSDDLNFGYDVEFQVESYLRYQGDTFSTSFDANTYLLMTKALDYFDPAAAHDGDLAAAVAPASCPFL... | Function: Transfers a succinyl group from succinyl-CoA to L-homoserine, forming succinyl-L-homoserine. In vitro, has also serine succinyl transferase activity.
Catalytic Activity: L-homoserine + succinyl-CoA = CoA + O-succinyl-L-homoserine
Sequence Mass (Da): 42772
Sequence Length: 390
Pathway: Amino-acid biosynthesis;... |
A0LCI7 | MTHEPLTASVGIVTPQHVRLFGASTPLQLDGGTLLHSVDVSYETYGTLNQERSNAVLICHALSGNAHAAGYHSKDDKRPGWWDHYIGPGKPFDTNRYFVIASNNLGGCDGTTGPSSIDPATGMPYGLNFPMITIGDIVRVQHALVRQLGIERLMAVVGGSMGGMQALQWALDYPHMVPASVIIAAAPRLTAQNIAFNAVARQAIMADPHFNGGDYYTLPGDPTTKARPESGLALARMMAHITYLSEQGLHERFGRRLQDRDALSYGFETDFAVESYLSYQGSSFVKRFDANSYLYITKAMDYFDPFPDAETTVQRLTGVE... | Function: Transfers a succinyl group from succinyl-CoA to L-homoserine, forming succinyl-L-homoserine.
Catalytic Activity: L-homoserine + succinyl-CoA = CoA + O-succinyl-L-homoserine
Sequence Mass (Da): 43454
Sequence Length: 394
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; O-succiny... |
Q8W3L1 | MSRYLARYMVSRYFSSASSRPLHVCIVGSGPAGFYTADKVLKAHEGAHVDIIDRLPTPFGLVRSGVAPDHPETKIAINQFSRVAQHERCSFIGNVKLGSDLSLSELRDLYHVVVLAYGAESDKDLGIPGESLSGIYSAREFVWWYNGHPDYSSLKPDLKTSDSAVILGQGNVALDVARILLRPTTELASTDIATHALSALKESSIRKVYLIGRRGPVQAALTAKELREVLGIKNLHIRIKQTDLSVTPADEEEMKTSRARKRIYELLSKAAAAAKTSEADPDQRELHFVFFRQPDQFLESDERKGHVSGVNLQKTILESV... | Function: Associates in vitro with the adrenodoxin-like protein MFDX1 to form an efficient low potential electron transfer chain that is able to reduce cytochrome C . Functions as accessory mitochondrial protein involved with BIO2 in the plant biotin synthase reaction .
Catalytic Activity: H(+) + NADP(+) + 2 reduced [a... |
Q9M0V0 | MIGHRISRLGSTIVKQLAREGYLATYGTKNLHRSYGHYLQSLPVVPRQARTSQEAWFLKSHKFCTSSTTSSENGDEETEKITIIFVDKDGEEIPVKVPIGMSVLEAAHENDIDLEGACEASLACSTCHVIVMDTEYYNKLEEPTDEENDMLDLAFGLTETSRLGCQVIARPELDGVRLAIPSATRNFAVDGFVPKPH | Cofactor: Binds 1 [2Fe-2S] cluster.
Function: Associates in vitro with the adrenodoxin reductase MFDR to form an efficient low potential electron transfer chain that is able to reduce cytochrome C . Functions as accessory mitochondrial protein involved with BIO2 in the plant biotin synthase reaction .
Sequence Mass (Da... |
Q8S904 | MVFHRLSRLGSRIVKELPRERHLSMCGKRILQRSYGQYLQSSPMLQRQTRSFKEALFSNNHKFCTSFSTTSEKGGEKTEKINVTFVDKDGEEIHIKVPVGMNILEAAHENDIELEGACEGSLACSTCHVIVMDTKYYNKLEEPTDEENDMLDLAFGLTATSRLGCQVIAKPELDGVRLAIPSATRNFAVDGFVPKPH | Cofactor: Binds 1 [2Fe-2S] cluster.
Function: Associates with the adrenodoxin reductase MFDR to form an efficient low potential electron transfer chain that is able to reduce cytochrome C.
Sequence Mass (Da): 22121
Sequence Length: 197
Subcellular Location: Mitochondrion
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P57381 | MKITKNKILKNKKIINFKYQKLLDLFYNVNNQKKNNQLLSYLYSFSGKIIFSLTEEKSLKKILRFLMRHKIHPQYIKRIIDIKKEIDYFYMIEEIKNGFIDKKNNILFLCTKDLLPILIDDKYIGNIKKNTNNINKFNLSQLILNHPVMHIEHGIGRYKGLTTIETASIQSEYLVISYAEGDKLYVPVSNLHLVSPYTGTSIENAPLHKLGGDDWNKEKHKISKTVYDHAAQLLHIYAKRESKTGFAFKKNIEKYDLFCNDCSFKTTSDQNEVMKFVLKDMSKPIPMDRLICGDVGFGKTEIAMRASFLAVSNKKQVAIL... | Function: Couples transcription and DNA repair by recognizing RNA polymerase (RNAP) stalled at DNA lesions. Mediates ATP-dependent release of RNAP and its truncated transcript from the DNA, and recruitment of nucleotide excision repair machinery to the damaged site (By similarity).
Sequence Mass (Da): 93881
Sequence Le... |
O26066 | MIQSSLYRALNKGFDYQILACKDFKESELAKEVISYFKPNTKAILFPEFRAKKNDDLRSFFEEFLQLLGGLREFYQALENKQETIIIAPISALLHPLPKKELLESFKITLLEKYNLKDLKDKLFYYGYEILDLVEVEGEASFRGDIVDIYAPNSKAYRLSFFDTECESIKEFDPITQMSLKEDLLEIEIPPTLFSLDESSYKDLKTKVEQSPLNSFSKDLTSFGLWFLGEKAQDLLIVYKSIISPRALEEIQELASLNELDCERFKFLKVLENAQGYEDLEIHAHALEGFIALHSNHKITLLAPNKTILDNAISALDAGN... | Function: Couples transcription and DNA repair by recognizing RNA polymerase (RNAP) stalled at DNA lesions. Mediates ATP-dependent release of RNAP and its truncated transcript from the DNA, and recruitment of nucleotide excision repair machinery to the damaged site.
Sequence Mass (Da): 113090
Sequence Length: 999
Subce... |
Q5JJ82 | MFPERGASEEEVLRELEEKTREDLTFDSGKILGSMCTYPHPFAVKVVMKYIDRNLGDPGLHIGSQKIEKEAVDMLANLLGLEKGYGHIVSGGTEANILAVRAMRNLAGIEKPELILPESAHFSFIKAAEMLGVKLVWAELNDDYTVNVKDVEKKITDRTIGIVGIAGTTGLGVVDDIPALSDLALDYGLPLHVDAAFGGFVIPFAKALGYEIPDFDFRLKGVKSITIDPHKMGMVPIPAGGIIFREKKFLDSISVLAPYLAGGKIWQATITGTRPGANALAVWAMIKHLGFDGYKEVVKEKMELARWFASELKKIPGIYL... | Function: Catalyzes the decarboxylation of L-aspartate to produce beta-alanine. In vitro, can also catalyzes the decarboxylation of L-glutamate to produce 4-aminobutanoate, but this activity does not seem necessary in vivo. Shows much higher activity with L-aspartate than with L-glutamate. Does not decarboxylate L-tyro... |
Q58499 | MILLVSPIDVEEAKEAIAGGADIIDVKNPKEGSLGANFPWMIKAIREVTPKDLLVSATVGDVPYKPGTISLAAVGAAISGADYIKVGLYGVKNYYQAVELMKNVVRAVKDIDENKIVVAAGYADAYRVGAVEPLIVPKIARDAGCDVAMLDTAIKDGKTLFDFQSKEILAEFVDEAHSYGLKCALAGSIKKEHIPILKEIGTDIVGVRGAACKGGDRNNGRIDRELVKELKELCK | Function: Catalyzes the formation of 4-(hydroxymethyl)-2-furancarboxaldehyde phosphate (4-HFC-P) from two molecules of glyceraldehyde-3-P (GA-3-P).
Catalytic Activity: 2 D-glyceraldehyde 3-phosphate = 4-(hydroxymethyl)-2-furancarboxaldehyde phosphate + 2 H2O + phosphate
Sequence Mass (Da): 25099
Sequence Length: 235
Pa... |
Q6LZC1 | MILLVSPKDVAEAYEAIEGGADIIDVKNPPEGSLGANFPWVIKETREATPEGMLVSAAIGDVPYKPGTVTLAALGATVSGADYIKVGLYGTRSYQEALDVMKNVTKAVKDAGENKIVVAAGYADAYRVGAVDPLVIPKVARDAGCDVAMLDTAVKDGKTLFDHMDLDLLREFVEETHKYGMKCALAGSIKIEEIPMLKEIGCDIVGVRGAACTQGDRNAGRIQKDLVKEIVKVCRD | Function: Catalyzes the formation of 4-(hydroxymethyl)-2-furancarboxaldehyde phosphate (4-HFC-P) from two molecules of glyceraldehyde-3-P (GA-3-P).
Catalytic Activity: 2 D-glyceraldehyde 3-phosphate = 4-(hydroxymethyl)-2-furancarboxaldehyde phosphate + 2 H2O + phosphate
Sequence Mass (Da): 25114
Sequence Length: 236
Pa... |
A5UNQ5 | MLLLISPINHEEALESIKGGADIVDVKNPKEGSLGANFPWVIRDIREITPEDKLVSATLGDVPYKPGTVSLAAMGAHVSGADYIKVGLYGTKDYDEAVEVMENVAKTIKDVDNDTIVVASGYADAHRVGAVDPMEIPKVAKDAGCDLAMLDTAVKDGHTLFDYLSIEDLEKFVNEAHSYGLKTALAGSVKKEQLKPLNDIGCDVVGIRGAACVGGDRNTGKIHHTAVAELKELCDSF | Function: Catalyzes the formation of 4-(hydroxymethyl)-2-furancarboxaldehyde phosphate (4-HFC-P) from two molecules of glyceraldehyde-3-P (GA-3-P).
Catalytic Activity: 2 D-glyceraldehyde 3-phosphate = 4-(hydroxymethyl)-2-furancarboxaldehyde phosphate + 2 H2O + phosphate
Sequence Mass (Da): 25250
Sequence Length: 237
Pa... |
A6USK6 | MILLVSPKDVAEAYEAINGGADIIDVKNPPEGSLGANFPWVIKEIRSATPNGMLVSAAIGDVHYKPGTVTLAALGATISGADYIKIGLYGTRSYQEAVDVMKNVSNAVKSEDPKKIVVAAGYADAYRVGAVDPLIIPKIARDSGCDVAMLDTAVKDGKTLFDHLSIDLLKEFVEETHKYGMKCALAGSIKKEEIPMLKEIGCDIVGIRGAACTKGDRNEGKIQKDLVKEIVKICKE | Function: Catalyzes the formation of 4-(hydroxymethyl)-2-furancarboxaldehyde phosphate (4-HFC-P) from two molecules of glyceraldehyde-3-P (GA-3-P).
Catalytic Activity: 2 D-glyceraldehyde 3-phosphate = 4-(hydroxymethyl)-2-furancarboxaldehyde phosphate + 2 H2O + phosphate
Sequence Mass (Da): 25179
Sequence Length: 236
Pa... |
Q58097 | MLSKRLLNFESFEVMDILALAQKLESEGKKVIHLEIGEPDFNTPKPIVDEGIKSLKEGKTHYTDSRGILELREKISELYKDKYKADIIPDNIIITGGSSLGLFFALSSIIDDGDEVLIQNPCYPCYKNFIRFLGAKPVFCDFTVESLEEALSDKTKAIIINSPSNPLGEVIDREIYEFAYENIPYIISDEIYNGLVYEGKCYSAIEFDENLEKTILINGFSKLYAMTGWRIGYVISNDEIIEAILKLQQNLFISAPTISQYAALKAFEKETEREINSMIKEFDRRRRLVLKYVKDFGWEVNNPIGAYYVFPNIGEDGREF... | Function: Catalyzes the transamination reaction between 4-(hydroxymethyl)-2-furancarboxaldehyde phosphate (4-HFC-P) and alanine to produce pyruvate and 5-(aminomethyl)-3-furanmethanol phosphate (F1-P), the precursor for the furan moiety in methanofuran.
Catalytic Activity: 4-(hydroxymethyl)-2-furancarboxaldehyde phosph... |
C7P8V7 | MILFFEYAIASGFEDEGILEEGKMMFNTLLNQFLEIDNVTSLIHKDFADDYKDFENLKIVEIEDDKDIEIKLNDILKNEKIDYALTIAPEDENILYNLTKIIEKYPVKNLGCSSNAIKVAGDKYLTYLTIKDYVKTPKTFKPKKYVIKKIDGCGGKFNLFDENFLIQEFVEGESLSVSLIVGKKIYPLSLNRQYIDERGFVGGEVNIKHRLKDEIFNEAIKAVKCIDGLNGYVGVDVIVNDEIYIIEINPRITTTIYGLKTEPSLAELLIKNANNEELTFKVEGKEFTINK | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: Catalyzes the formation of an amide bond between tyramine and the gamma carboxy group of L-glutamate. The enzyme also accepts phenylethylamine in vitro.
Catalytic Activity: ATP + L-glutamate + tyramine = ADP + gamma-L-glutamyltyramine + H(+) + phospha... |
Q58225 | MLLLQSILITKIMVIQLILFFEYALASGFEDKNILKEGKMMFDTLLKQFLEIDKVISLLYKDFVDNYIDFKNLEIVKIKKENEIENKLKSLLKSENIDYALVVAPEDEDILYNLTKIIESYPVKNLGCSSEAIKIAGNKYLTYLAIKDAVKTPKTFPPKKYVVKKIDSCGGKFNLFDENFLIQEFIDGENLSVSLIVGKKIHPLSLNRQYIDKRGFVGGEVNINHKLKDKIFNEAIKAVKCINGLNGYVGVDVIVNNDGIYIIEINPRITTTIYGLKTNPSLAELLIKNANNEELKFKVKGEKFTIDK | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: Catalyzes the formation of an amide bond between tyramine and the gamma carboxy group of L-glutamate. The enzyme also accepts phenylethylamine in vitro.
Catalytic Activity: ATP + L-glutamate + tyramine = ADP + gamma-L-glutamyltyramine + H(+) + phospha... |
Q57900 | MHIVKIGGSLTYDAKPLLKALKNYAKENNKKIVIIPGGGEFANVVRKIDKALNISNSLSHKLAIKCMDLIGEVYAEIGYIKAYDTLFDLKREIEKEKIAILLPSKILLSTDIAEHSWAITSDSLSLYIGKLLDVREVIIATDVDGIYDKFPGGKLLNIINANDIKGLTSVDETFPILLKQFKMNAYVVNGRHPERVMDILEGKHNIYTKIVGIDKI | Function: Catalyzes the formation of 5-(aminomethyl)-3-furanmethanol diphosphate (F1-PP) from 5-(aminomethyl)-3-furanmethanol phosphate (F1-P) and ATP . In vitro, can also act as an adenylate kinase that catalyzes the transfer of a phosphoryl group from ATP to AMP, generating two molecules of ADP .
Catalytic Activity: ... |
Q58250 | MKIMILGIDIGGANTKITEIEGDNYKIHHIYFPMWKKKDELEDLLKNYNDNVDYVALVMTAELADCYKTKKEGVEDIIDKVEKAFNCPVYVFDVNGNFLTSEEAKKNYLDVSASNWNATAKFVAEFIKDSCILVDMGSTTTDIIPIKDKEVLAEKTDLDRLMNNQLVYVGTLRTPVSFLANKIEFRGKLTNLSSEYFAITADISLILNKITEEDYTCDTPDGAGKDFESCLTRLVRVLCADREMVKDDELIDFANKLYNKLLELIRENVDTIAKRYNLNDVVITGLGEEILKDALDEYNIISIKETYGKDVSLATPSFAV... | Function: Catalyzes the condensation between 5-(aminomethyl)-3-furanmethanol diphosphate (F1-PP) and gamma-glutamyltyramine to produce APMF-Glu.
Catalytic Activity: [5-(aminomethyl)furan-3-yl]methyl diphosphate + gamma-L-glutamyltyramine = (4-{4-[2-(gamma-L-glutamylamino)ethyl]phenoxymethyl}furan-2-yl)methanamine + dip... |
Q9P6N1 | MPSIILYCSWNQDRGFLSIGSENGYQVYRSNPFTLCFSKKANGASICEMLYESSLLAFVNISPESTRLLKLVDIKRDIVLCRIFYPSPVLSVRFTWNRLVVLIKGSIYVYNLKNMELINTLNTSKGNVIAFAVHENYVAYNSPTNPGDIYLASLDTAIPVTLIHCHSSAVQVVDFHPRGHLIATASAKGTVIRVITTSDGELVTELRRGYIPASIVSISFHPVEPFLACASENGTIHVFKISKQPSDPNSSPTSSVTVSSSWSKYLTSNVAKVWDTRKEFATAKIPEASFYGKIIFSSSGPHIQVASYSGHYYRFAVNLK... | Function: Required for cytoplasm to vacuole transport (Cvt) vesicles formation and autophagy (By similarity). Has a role in sporulation.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 37108
Sequence Length: 335
Subcellular Location: Cytoplasm
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P26188 | MKELLYYTFIETEVTGAFLVFREKTQNLVFASLGNDKLFLLGKVEGFLKKHEKQDTMYDLQELKEAETYKKSIENYTICLENKMPLPSGAIPFEFLFGTDFQRKVWNELLNVEHGHVVTYGDIAKRIGKPTAARSVGRACGSNNLALLVPCHRIVGSNRKLTGYKWSCKLKEQLLNNEKENSLSLSRL | Function: Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irrever... |
Q59268 | MQEKTKRIIKEDIEAVRAYSDCFDVEMPDLDENGEVIGLPAPYPREVAGTVRSGYRIYDLAKKAKERGWPIQNPILGRNTAEETYGESQEMYAYADKFDETLFHFVHAEATRHIDPLKGRELINQSRGKGGITPIGEREFIAMGGGSKHPVRINATGDTPHLSIINALIAGFDGTDIGPVIHVHFGGRGIHDYKTKVVNGYKAIQICAENNIFVQLDSHKHLNNIGGTDGMALAMCLLSEGLAVHAGLPWELSAIQMNVAGINIYADLAVMRAFRKACHSKSIIAVPETFQNPPGNLVAEAAHFSRMAVTAKLGGADFYR... | Cofactor: Contains a mixture of adenosylcobalamin and oxygen-stable cob(II)alamin.
Function: Involved in the fermentation of nicotinate to ammonia, propionate, acetate and carbon dioxide.
Catalytic Activity: 2-methyleneglutarate = 2-methylene-3-methylsuccinate
Sequence Mass (Da): 66750
Sequence Length: 614
Pathway: Cof... |
P10620 | MVDLTQVMDDEVFMAFASYATIILSKMMLMSTATAFYRLTRKVFANPEDCVAFGKGENAKKYLRTDDRVERVRRAHLNDLENIIPFLGIGLLYSLSGPDPSTAILHFRLFVGARIYHTIAYLTPLPQPNRALSFFVGYGVTLSMAYRLLKSKLYL | Function: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.
Catalytic Activity: glutathione + RX = a halide anion + an S-substituted glutathione + H(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 17599
Sequence Length: 155
Subcellular Locat... |
P79382 | MADLTELMKNEVFMAFASYATIVLSKMMFMSTATAFYRLTRKVFANPEDCSSFGKGENAKKYLRTDERVERVRRAHLNDLENIVPFLGIGLLYSLSGPDLSTAILHFRLFVGARIYHTIAYLTPLPQPNRGLAFFLGYGVTLSMAYRLLKSRLYL | Function: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.
Catalytic Activity: glutathione + RX = a halide anion + an S-substituted glutathione + H(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 17650
Sequence Length: 155
Subcellular Locat... |
P08011 | MADLKQLMDNEVLMAFTSYATIILAKMMFLSSATAFQRLTNKVFANPEDCAGFGKGENAKKFLRTDEKVERVRRAHLNDLENIVPFLGIGLLYSLSGPDLSTALIHFRIFVGARIYHTIAYLTPLPQPNRGLAFFVGYGVTLSMAYRLLRSRLYL | Function: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.
PTM: In vitro, peroxynitrite induces nitration at Tyr-93 which activates the enzyme.
Location Topology: Multi-pass membrane protein
Catalytic Activity: glutathione + RX = a halide anion + an S-substitute... |
Q99735 | MAGNSILLAAVSILSACQQSYFALQVGKARLKYKVTPPAVTGSPEFERVFRAQQNCVEFYPIFIITLWMAGWYFNQVFATCLGLVYIYGRHLYFWGYSEAAKKRITGFRLSLGILALLTLLGALGIANSFLDEYLDLNIAKKLRRQF | Function: Catalyzes several different glutathione-dependent reactions . Catalyzes the glutathione-dependent reduction of lipid hydroperoxides, such as 5-HPETE . Has glutathione transferase activity, toward xenobiotic electrophiles, such as 1-chloro-2, 4-dinitrobenzene (CDNB) . Catalyzes also the conjugation of leukotri... |
Q3T100 | MAVLSKEYGFVILTGAASFLMVTHLAINVSKARKKYKVEYPTMYSTDPENGHIFNCIQRAHQNTLEVYPPFLFFLAVGGVYHPRIVSGLGLAWIVGRVLYAYGYYTGEPRKRQRGALSFIALIGLMGTTVCSAFQHLGWVRTGLNSGCKSCH | Function: Displays both glutathione S-transferase and glutathione peroxidase activities toward oxyeicosanoids. Catalyzes the Michael addition reaction of reduced glutathione (GSH) to electrophilic eicosanoids to form GSH adducts, as part of detoxification or metabolic shunt processes. Mediates GSH conjugation to leukot... |
O14880 | MAVLSKEYGFVLLTGAASFIMVAHLAINVSKARKKYKVEYPIMYSTDPENGHIFNCIQRAHQNTLEVYPPFLFFLAVGGVYHPRIASGLGLAWIVGRVLYAYGYYTGEPSKRSRGALGSIALLGLVGTTVCSAFQHLGWVKSGLGSGPKCCH | Function: Displays both glutathione S-transferase and glutathione peroxidase activities toward oxyeicosanoids, as part of cellular detoxification as well as synthesis of bioactive metabolites . Catalyzes conjugate addition of reduced glutathione to the alpha, beta-unsaturated C=C carbonyl group of eisosanoids such as l... |
Q9CPU4 | MAVLSKEYGFVLLTGAASFVMVLHLAINVGKARKKYKVEYPVMYSTDPENGHMFNCIQRAHQNTLEVYPPFLFFLTVGGVYHPRIASGLGLAWIIGRVLYAYGYYTGDPSKRYRGAVGSLALFALMGTTVCSAFQHLGWIRPGLGYGSRSCHH | Function: Displays both glutathione S-transferase and glutathione peroxidase activities toward oxyeicosanoids. Catalyzes the Michael addition reaction of reduced glutathione (GSH) to electrophilic eicosanoids to form GSH adducts, as part of detoxification or metabolic shunt processes. Mediates GSH conjugation to leukot... |
Q54GA9 | MPFDTKSIFPDFIVFPSAISTIAIGLWSVQAYKLGEARKRYNVKAPHVQGDPEFERIAHEYQNTSEALGAIIPATFMFSYYISPKCSLLLGGTWLVSKMLNCCSYCCKKEKENDCAKNVHTCLSHISFFALLGGSAFGIGSSLYNRYKL | Function: May perform the conjugation of reduced glutathione to electrophiles.
Catalytic Activity: glutathione + RX = a halide anion + an S-substituted glutathione + H(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 16626
Sequence Length: 149
Subcellular Location: Membrane
EC: 2.5.1.18
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Q9RFR0 | MSLVVFPFKHEHPEVLLHNVRVAAAHPRVHEVLCIGYERDQTYEAVERAAPEISRATGTPVSVRLQERLGTLRPGKGDGMNTALRYFLEETQWERIHFYDADITSFGPDWITKAEEAADFGYGLVRHYFPRASTDAMITWMITRTGFALLWPHTELSWIEQPLGGELLMRREVAAMLYEDERVRRRSDWGIDTLYTFVTVQQGVSIYECYIPEGKAHRLYGGLDDLRTMLVECFAAIQSLQHEVVGQPAIHRQEHPHRVPVHIAERVGYDVEATLHRLMQHWTPRQVELLELFTTPVREGLRTCQRRPAFNFMDEMAWAA... | Cofactor: Divalent cations such as magnesium, calcium and to a lesser extent manganese, nickel and cobalt.
Function: Involved in the biosynthesis of the stress protectant 2-O-alpha-D-mannosyl glycerate (MG) which is produced in response to growth at supraoptimal temperature and salinity, and protects several enzymes ag... |
Q5F407 | MRLRNGTVATVLVFITTFLSLSWYTAWQNGKEKLIAYQREFHALKERLRIAEHRTLQRSSELNAILEQFRRAVAETNGSKNALNNFSDETLKLLKELTSKKSLQVPNIYYHLPHLLKNEGSLQPSVQVGLGRTGVSIVMGIPTVKRKVKSYLTETLHSLIDKLSPEEKLDCVMVVFIGETDLDYVNNVVASLEKEFSTEINSGLVEVIAPPATYYPDLTNLKETFGDSKERVRWRTKQNLDYCFLMMYAQKKGVYYIQLEDDIVVKQNYFSTIKNFALQLASEDWMILEFSQLGFIGKMFQSPDITLIVEFIFMFYKEKP... | Function: Glycosyltransferase that catalyze the transfer of GlcNAc from UDP-GlcNAc to the GlcNAcbeta1-2Manalpha1-3 arm of the core structure of N-linked glycans through a beta1-4 linkage and participates in the production of tri- and tetra-antennary N-linked sugar chains (By similarity). Involved in glucose transport b... |
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