ids
stringlengths 6
10
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stringlengths 16
1.02k
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stringlengths 117
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I1L3N3 | MLCKPPLKCLKIVIMANLLTMFFVMEMIIVSGLSFGASGLNMNYYLLSCPFVEPVVKNTVNRALQDDPTLAAGLVRMHFHDCFIEGCDGSVLIDSTKDNTAEKDSPANLSLRGYEVIDDIKEELENQCPGVVSCADIVAMAARDAVFFAGGPVYDIPKGRKDGTRSKIEDTINLPAPFFNASELIKMFGQRGFSARDMVALSGAHTLGVARCSSFKHRLTQVDPTLDSEFAKTLSKTCSAGDTAEQPFDSTRNDFDNEYFNDLVSNNGVLTSDQTLYNSPQTRNIVNAYAMNQALFFLDFQQAMVKMSMLDVKEGFKGEVRKNCHKIN | Cofactor: Binds 2 calcium ions per subunit.
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue.
EC: 1.11.1.7
Catalytic Activity: 2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O
Subcellular Location: Secreted
Sequence Length: 328
Sequence Mass (Da): 36190
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A0A0R4J2Q8 | MAMALPLRRLSSTLNKPLASATSIYHRMSSSLSAQEKDKSRADWIKQLNDPLETIDPEIADIIELEKARQWKGFELIPSENFTSLSVMQAVGSVMTNKYSEGYPGARYYGGNEYIDMAETLCQKRALEAFRLDPAKWGVNVQSLSGSPSNFQVYTALLKPHERIMALDLPHGGHLSHGYQTDTKKISAVSIFFETMPYRLNESTGYIDYDQLEKSAVLFRPKLIVAGASAYARLYDYARVRKVCDKQKAVLLADMAHISGLVAAGVIPSPFDYADVVTTTTHKSLRGPRGAMIFFRKGVKEINKQGKEVLYDYEDRINQAVFPGLQGGPHNHTISGLAVALKQAMTPEFKNYQKQVLSNCSAFAQSLLEKGYELVSGGTDNHLVLVNLRNKGIDGSRVEKVLEAVHIAANKNTVPGDVSAMVPGGIRMGTPALTSRGFVEEDFEKVAEYFDAAVKLALQIKENTNGTKLKDFVAAMQSDEQVQSKIANLRHEVEDYAKQFPTIGFDIETMKYGK | Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
Function: Interconversion of serine and glycine.
EC: 2.1.2.1
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + glycine + H2O = (6S)-5,6,7,8-tetrahydrofolate + L-serine
Sequence Length: 514
Sequence Mass (Da): 56942
|
A0A4U9HQI5 | MGPVMLDVEGYELDAEEREILAHPLVGGLILFMRNYHDPAQLRELVRQIREASHHRLVVAVDQEGGRVQRFREGFTRLPAAQSFAALLGLEEGGKLAQEAGWLMASEMIAMDIDISFAPVLDVGHISAAIGERAYHEDPQKALQIATRVIDGMHEAGMKTTGKHFPGHGAVTADSHKETPRDPRPQAEIRARDMSIFKSLISDNKLDAIMPAHVIYPDVDPRPASGSPHWLKTVLRQELGFNGVIFSDDLSMEGAAIMGSYAERGQASLDAGCDMILVCNNRKGAVSVLDNLSPIKAERVTQLYHKGSFSRQDLRDTARWKTVNAQLEALHERWEAHKAGQ | Pathway: Cell wall biogenesis; peptidoglycan recycling.
Function: Plays a role in peptidoglycan recycling by cleaving the terminal beta-1,4-linked N-acetylglucosamine (GlcNAc) from peptide-linked peptidoglycan fragments, giving rise to free GlcNAc, anhydro-N-acetylmuramic acid and anhydro-N-acetylmuramic acid-linked peptides.
Catalytic Activity: Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.
EC: 3.2.1.52
Subcellular Location: Cytoplasm
Sequence Length: 341
Sequence Mass (Da): 37678
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A0A0G4IMP4 | MLSMPGVVIYGDDGQMLRGTALRKALREELAKLEAGTGEERRPSSPPASGAKEPEGEPLDDELPIIVDDASDEKDDEKDDGELDEVLVDKQAEAYEDDDTQGSDEGRDRNFRYRSITQASPFKWRATAPRLAFDRNNTILIVVTMYNEEQDELSLTLRAISRNIKHMCKILKRSALWKSVAVCIVSDGRAKANPATMKFASSLGILSVSTMEQAPKNTAVHLFESVIRLVDDEAAGTLLPPLQVVFAMKEQNRGKLHSHLWFFEGFAHVMKPKFTFLLDVGTLPQDSAFLGFYRALDASTNIAGVCGRMKTRHHGIVDYLNPIVAAQHFEYEVASVLDKAFESSLGYLSVLPGAFSAYRYQALLGEPLKHYFKSIFMADSDLRPFSSNMTLAEDRLLCYELIAKTNCSYTLCYVNTAVAETDVPHDLPSLLKQRRRWLNGSFFALLYALGHFFSFWRQSNHGVVRKLAITFEFLFYVLSVVIQWLTIGIFFLVVVLTSFDLGAPLDLCIVAGAIFVVLVAIQFLMAFRNDPKRLSWAYTGVSFLLAVYFVAILVITITFSLDQIQNGNLLLIATLFVAWGIYLVAGLMHGALGSILISFVAFLGMMPTMMIAFPIFAMSNTHDVSWGTKDLDQVTGSEDVNTRAMIKRRFLGFRRNLICFWLLSNIALVILVFALGAQTVFLETCIVSILVLNGSRFIGSTLYLTNGMATSSMIVKFAVSPITPRAYLSVLKLPFTMVASAFYFAITLLMWMPASAESSCAGSILVDLSRNDQWLTHLFTSDLPDPTQSFGSEVEPEKEVEDVNLVKRIRTYFIGIRWVVPAIALVIVVPCVIGILAILAPLAFPSNCPTVCNLLPFSFETLRMWKWFMIPVLVYPILAVSWAADGILRWAHTEFCSTDMITV | Catalytic Activity: [(1->4)-N-acetyl-beta-D-glucosaminyl](n) + UDP-N-acetyl-alpha-D-glucosamine = [(1->4)-N-acetyl-beta-D-glucosaminyl](n+1) + H(+) + UDP
EC: 2.4.1.16
Subcellular Location: Membrane
Sequence Length: 903
Sequence Mass (Da): 100687
Location Topology: Multi-pass membrane protein
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D7R6D7 | VLFQHLFWFFGHPEVYILIIPGFGAISHIVASYSNKPEPFGTLGMIYAMLGIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWLATIYGSKVKYDTPMMWALGFIFLFTVGGLTGILLSNSSLDIMLHDTYYVTAHFHYVLSMGAVFSMFAAFTFWFPLFSGVTFHSRWSKAQFILMFIGVNLTFF | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
EC: 7.1.1.9
Subcellular Location: Membrane
Sequence Length: 198
Sequence Mass (Da): 22342
Location Topology: Multi-pass membrane protein
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A0A0G4ITA0 | MAPSIEEWWAEIPPVTKALMIAAIGTTAVVSLGIVHPADLYLDTHAVVRHVQVWRLLTCFSFLGTIGIGWFLQLYIISKYGATLEKEYFRGATSRADFVFMLVFSASVLVLASLVVPGLYFLGPSLVTVLIYVWSRSDPHIPVTFFGFRFQAWQVPFLLMVFHVLMGGSALPDIVGILAGHAYYFSTTVVPRAYGVTLVKTPAFLIGQLAQEGPARAGMSWRRTGQGHRLAD | Function: May be involved in the degradation of misfolded endoplasmic reticulum (ER) luminal proteins.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 232
Sequence Mass (Da): 25579
Location Topology: Multi-pass membrane protein
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A1X4J0 | ILVGMWSGVLGLMLSVLIRMELAEAGKYIMDSHIFNVCVTSHAFLMIFFFVMPTMIGGFGNWLLPLMLGAPDMAFPRLNNLSFWLLIPSLFFLLMSSVLGDGVGTGWTVYPPLSSELGQPSVSVDLSIFSLHLAGASSIMGAVNFISTVINLWVEKSKYDLMSLFCWSVVITAVLLLLSLPVLAGGITMLLLDRNMNCSFFDPIGGGDPILYQHLFWFFGHPEVYILILPGFGLISQIILFESGKKQVFGTIGMIYAMMAIGVLGFVVWAHHMFTVGMDVDSRAYFTSATMVIAVPTGVKVFSWLATSFGSRMSFTTSMLWAIGFVFLFTVGGMTGLVL | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
EC: 7.1.1.9
Subcellular Location: Membrane
Sequence Length: 339
Sequence Mass (Da): 37112
Location Topology: Multi-pass membrane protein
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A0A0G4IS01 | MDASDHDVVAPPESAPDVPSPKSLSDDVFVGKESPVASSKDKCDEPVDEKKGAAIEIAADGAQALNEIETGAGDSDNQKEPSSNPDSLSPDRVSNQFVARHDANIGEKVDITPQRAALYKDTGEEEIHEPPELVSDTVQREPDIVRQTRQASVGQSSHDPRKSLSVVVVELSATRAVQTPLSMSKFSLQSGYYGMQGRRPTMEDFHAQIQHPEFNNLVPAVDLDGRQRHFFAIYDGHGGPWCAEYCSRTLHQNLIRNPLFKDDSKKALHDAVVETDDTFCALIRDKGLSESSGTTAIVAYIVDDLLLVANVGDSRAVMCRAGTAVSLSQDHKPNRKDERARILEMGGFVGRTLSQARAEAGPGGVIWSNMCNCACLQAAGPGIPPYRVYPGGLAISRSIGDLEMKATRLVVNTPEIAEVPLTDADEFIILACDGVWDVLSNDEAVKHVRAFRKRMGEHPMEAAKHLATLAFSEGSTDNISVLVIFLGKHDAPMNPTP | Function: Enzyme with a broad specificity.
Subcellular Location: Membrane
Sequence Length: 497
Sequence Mass (Da): 53797
Location Topology: Peripheral membrane protein
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A0A811ZTY7 | MPTAWATPGAPEAPPCANQSCAPSELVLLGFAHVPALRPLLATLFLAMFLLTLLGNALIVLLTALDPALRAPMYLFLRHLALVEMCFSLDIVPRLLLTLLRPGRGVSPAGCALQLLLVLSCVTSECFLLTTMAWDRYVAICRPLRYGAIVSPRLCHLLAATCWLAGVPVSLVFTIWLFRFPFCGPRGIRHFFCDIAPLLSLVCADTRVFEAHVLAATVLVIMVPFCLIAASYTKILATVLRMPSARGRHKALSTCASHFVVVLLFYGTTGVIHLRPKASYSPESKQVVSLSYTLVTPMLNPLIYSLRNKEVRAALGRVCCHGQESGPHE | Function: Putative odorant or sperm cell receptor.
Subcellular Location: Cell membrane
Sequence Length: 329
Sequence Mass (Da): 35862
Location Topology: Multi-pass membrane protein
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U6IZ32 | MDIIGEVPQERDESKFENLLKPIRLKYQSVIDKSNPYTKTRWCITFAFLALYVLRIYFIQGFHIISYALAIYILSLFIHSISPQVDPEFADLLDEAPTLPRTEADEFRPFIPRLLEAKFWYYATRAIIISLLCTFFSFLDIPVFWPILVVYFILLFTVMMKRQIKHMITHRYVPFSYGKPHPTGKVLVS | Function: Involved in the retrieval of endoplasmic reticulum membrane proteins from the early Golgi compartment.
Subcellular Location: Membrane
Sequence Length: 189
Sequence Mass (Da): 22309
Location Topology: Multi-pass membrane protein
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A0A0G4J7Z7 | MTQVTVTQPEKKRRRRNKAKAATAPSETQQENVGQKEALPEPASGGGEVPAETVGVAGDQVQSGDATAPQPAKKRRRGTRGKSQAVAGREAEPEAPNNVNQSGPVEEADPEPVNDGNENAQNEEDVKGAEGPSADVDDTSRNVNPADVALDYDFGSLELSTATRSALTDIGYERMTEVQARCIPLLLSGADVLGAAKTGSGKTMAFLIPAVELLYKAEFKPRNGTGVIVITPTRELALQIYGEARKLLKYHSQTHGIVIGGGNRKQEEDKLKRGVNVLIATPGRLLDHLQNTNFTFKNLIGLVIDEADRILEIGFEQELREIIKILPSKRQTMLFSATQTQKVKDIARVSTNKSPVYVGVDDHKEAATRKGLTQGYVVCPSERRFLLLYSFLKRNLKKKVIVFFSTCMSVKFHAELLNYIDIPVIELHGKLKQSKRTSTFFEFVNAERGILLCTDVAARGLDIPEVDWIIQFDPPSDPKEYIHRVGRTARGVAGAKGKALLFMLPQEVKFLHHLKYAKIPVCEFEFPTSKIANVQSQLEALIEKTYYLYKSAREAYRAYIQGYAQASLKDVFDVHSLDLEAVARSFGFTAPPKVPLKIALTGKNSRKRSRHGFNQDNPYGDAKTPPQFSR | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 630
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Sequence Mass (Da): 69558
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A0A6G1EL41 | MSAILAASLAGAAGLLALVGVAIFLIVLFLRHRRRASDSSESSSSGPAQPEQQGARCMTLEELSSATRNFSNVNLIGHGMFGEVYKGLLQDGTIVAIKKRHSPLSHEFIQEVNYLSSIRHRNLVNLLGYCQENGMQMLVYEYVPNGSVSTHLHGAELPTIK | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
EC: 2.7.11.1
Subcellular Location: Cell membrane
Sequence Length: 161
Sequence Mass (Da): 17479
Location Topology: Single-pass membrane protein
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U6JJS2 | MGLKRLNVIAAVANNGGIGKENKLPWKIREDMTFFSRITSTAQEGKKNAVILGRRTWLSFPPKFRPLPSRINVVVSTQLESVPEGTHLVKSFEDSLHLLESLIDSGQVDEVFIIGGHGLYKEALEQEVYPVRLYYTHIMKDFDCDTFFPSVDWERFKPIQLDTVDSDLRHSGDIEFRFAVYEKQPHPLNDH | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1.
EC: 1.5.1.3
Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH
Sequence Length: 191
Sequence Mass (Da): 21917
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V6CKR0 | MGKIMLVLGSLIGLCCFTITTYAFSPSGWTNAHATFYGGSDASGTMGGACGYGNLYATGYGTRTAALSTALFNDGASCGQCYKIICDYKSDSRWCIKGRSVTVTATNFCPPNFALPNNNGGWCNPPLKHFDMAQPAWEKIGIYRGGIVPVLFQRVPCKKHGGVRFSVNGRDYFELVLISNVGGAGSIQSVFIKGSKTGWMAMSRNWGSNWQSNAYLNGQSLSFRVTTTDGETRVFQDIVPASWTFGQTFSSPVQF | Function: Causes loosening and extension of plant cell walls by disrupting non-covalent bonding between cellulose microfibrils and matrix glucans. No enzymatic activity has been found.
Subcellular Location: Secreted
Sequence Length: 255
Sequence Mass (Da): 27538
Location Topology: Peripheral membrane protein
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A0A813TF02 | MVPFLMSKLDSNSSQSEISNQDEVLSHRLAQKIEPSNNADKAAEPHGLQPRMSDSLGNYEPRDQPTRTGPGEGGVPVILSPAEEQAAQKTISQYGFNMIASDKISMDRSIKDTRPAECKNWIYPEPRYLPKASVILVFFDEGWSVLLRTVHSVINTSPKELLKDIILIDDGSSDPDSKERLEKYIERWNGLVKLYRTGERVGLIAARTLGAEKSTGDVIVILDAHCECVTNWLPPLLTRIAMNRRALAVPIVDGLEWKTLEHTNIYGSSNFRGIWEWGFLYKETEVPAQELKKRKHQSEPYWSPTHAGGLLAIDRQWFFELGAYDPGIRVWGAEQYELSFKVWQCGGVVEWVPCSHVAHAYRGPRSHSSHVPGTSPYQTSINHMRLAEVWMDEYAEYYYIREPAIRSLNYGDVSERKKLREKLQCKPFKWFMENVAYDVLQKFPPPPKNVVWGECKNIKHSVCLNDRGASFGQPIGVSGCYRQGVWRLNEEGEISSGEHCFISDHDIIKKKFCLDHNGRWNPVGEWHYDKATKQIRSNKEHLCMETNGNDLKLNKCDEANEAQKWIWTEIHY | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 572
Sequence Mass (Da): 65481
Location Topology: Single-pass type II membrane protein
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A0A0G4IRI0 | MAGDWTQSSLNAMTADALRELCRDCKLSSSGRKSELVARLLQHKQSRGVAGTIASRKGVSEIEAIRRPSLEEKRVLPPEQRILPTRRQSPRRPVQTVNLNETVPMKVETRSVRQVSSVPVPAPVPEPVEPAARSPIAVKQEQGPIVSEEQEPIVSEEQEPVFQENQDPPAPVAVRQELSVTTSGHVEDRMEEDHFTAIPTETAPPSCISVAFVCHSNLNRSMEAHHVCRLADPFGNQGATLFSFGAGGRVNLPVPVASAAMSFEFGSATYLDMFNYLSTSDNEEFYRKMGVLDMLQRNMGVKEMPERWQLEGRHFDLIVSFELRIFDIILEDLDQRSPKQGRVAHIINIETVDNFAAAKVGGEHALKLLAMVQQSSDWENDLPSILTELESSASIQHAVMFY | Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
EC: 3.1.3.16
Subcellular Location: Nucleus
Sequence Length: 402
Sequence Mass (Da): 44677
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K7LP51 | MNNSSGGGGRGTLMGLSNGYCGRSPFTVSQWQELEHQALIFKYMLAGLPVPLDLVFPIQNSFHSTISLSHAFFHHPTLSYCSFYGKKVDPEPGRCRRTDGKKWRCSKEAYPDSKYCERHMHRGRNRSRKPVESQTMTHSSSTVTSLTVTGGSGASKGTVNFQNLSTNTFGNLQGTDSGTDHTNYHLDSIPYAIPSKEYRYVQGLKSEGGEHCFFSEASGSNKVLQMESQLENTWPLMSTRVASFSTSKSSNDSLLHSDYPRHSFLSGEYVSGEHVKEEGQPLRPFFNEWPKSRESWSGLEDERSNQTAFSTTQLSISIPMSSNFSATSSQSPHGEDEIQFR | Function: Transcription activator.
Subcellular Location: Nucleus
Sequence Length: 341
Domain: The QLQ domain and WRC domain may be involved in protein-protein interaction and DNA-binding, respectively.
Sequence Mass (Da): 38022
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A0A068WAJ6 | MMNSQMLNRSREKKLWCSLSVVMTSVPRFSSTVKELRILFSPVNASSAGVREFIGKSYVGLRNSNPGVKFMLREGNSISPRIYARYGFGKESFVSVDNASPTEIMDKICKLAKA | Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 114
Sequence Mass (Da): 12732
Location Topology: Peripheral membrane protein
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K7MJX3 | MNRTPKRGFSLIDFGCRDFKARISRSGNDVVGGEKAWEVGIHMADVDDAVAPLHYRFSPHRNRASLSEPLLPRVPLTVSSSSFSMLSGTHYMRLHIWNMDDVHNYYHSLITFDFVAPSTFFAESKPWMDKRVLKNVASTRPLSARIFKAIADPPTTSLQRLKGLTTGGLPTFVDVGNSFSAPAIVEDNFINQKVVMMGDDTWTQLFPHHFERSYPYPSFNVKDLHTVDNGCIEHLLLSLYEEDWDVLIAHFLGVDHAGHIFGVDSTPMIEKLEQYNTILESGPGSSHENTMLVVMGDHGQTLNGDHGGGSAEEVETAIFAMSFKKPLSFVPPEFDSCSCQLDLSIGFLILSTLCRFAIEVGLSKQAATSAFMKDFTSWIINIASGLPVWDYAAEVIPMVVLILLAAWLYKAASGSFFDWPWNYFIAKFVNIEGGKDGPLRNFSIMQWSLFATCLFFCSGHWCAFDGLRYGAAFIGFEEFVLVRQAILLAIHTFGFSIILPVFGLPLLVATKYQANLGKHFIFTQLSQIDVYNVWAHDSNYNYFHNIMCHNSKAAPPDGLGFICSEVCL | Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 568
Sequence Mass (Da): 63494
Location Topology: Multi-pass membrane protein
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K7LFK3 | MSKDKDATNLSRTFKYLLATQFLSRGIPFIFNTWIVRHLTQEDYALYAVQFHLLVTCILFLSREGFRRACLRMDLKCDGSSMGDVVKLMKVVWMSFPLGIFITIVVCLFVFWWQQISYSSPHGQAILINGFACILELLAEPVYILSQNLVLLELRLMVETVATLSRCLTMYFLIVKQTGMEKSIIFALSQSAYGACLFLGYWGYLLLSQKFRVSYLFPFREGKMIDFDQQLSKMCILFTFQSFRKLILQEGEKIVLVWLDTPYNQAVYGLVDKLGSLVVRLVFLPFEESSYVTFARSASGQYPGKSKKLGNSLTESLKLVLLIGLVFMAFGPSYSYSLIRLLYGEKWSDGEASTALRCYCFYVIVLAMNGISKFVR | Function: May be involved in N-linked oligosaccharide assembly.
Subcellular Location: Membrane
Sequence Length: 376
Sequence Mass (Da): 43046
Location Topology: Multi-pass membrane protein
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Q9XK92 | FGSLLGICLTTQIITGLLLATHYTADSTLAFTSVSHTCRDVQYGWLIRNLHANGASLFFMCIYLHIGRGLYYGSYLYKETWNTXVLLLLTLMATAFVGYVLPWGQMSFWGATVITNLFSAIPYIGQTLVEWAWGGFSVDNPTLT | Function: Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis.
Subcellular Location: Membrane
Sequence Length: 144
Sequence Mass (Da): 16032
Location Topology: Multi-pass membrane protein
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K7KHK1 | MLVDEWLHADDGYYKRPRGGQNQYGYNNNGEHVLNIPPPPGAGWGAAPQPPQMISSDMSNSSFSGSHGPVLPPPHPTVALGFNQSSFTYDELSAATGGFSQRNLLGQGGFGYVHKGVLPNGKEIAVKSLKSTGGQGDREFQAEVDIISRVHHRHLVSLVGYCMSESKKLLVYEFVPKGTLEFHLHGKGRPVMDWNTRLKIAIGSAKGLAYLHEDCHPRIIHRDIKGANILLENNFEAKVADFGLAKISQDTNTHVSTRVMGTFGYMAPEYASSGKLTDKSDVFSFGIMLLELITGRRPVNNTGEYEDTLVDWARPLCTKAMENGTFEGLVDPRLEDNYDKQQMASMVACAAFSVRHSAKRRPRMSQIVRVLEGDVSLDALNHEGVKPGQSSMFSSASREYGAEAYGADMMRFRKLALDSGVGSSEYGGTSEYGLNPSSSSSEQSSAEYARRTTGGGRMHTP | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
EC: 2.7.11.1
Subcellular Location: Cell membrane
Sequence Length: 461
Sequence Mass (Da): 50305
Location Topology: Single-pass membrane protein
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A0A0R0GV98 | MKQSEATSLAARKRGKWGYIWPMWTSLLLHLLAILLFTTGFLLTRTELPYHSHCSDVSHSPCFSSNNNGSCWTKPATNRLLIIVLDALRFDFVAPSTFFAESKPWMDKLRVLKNAASTRPLSARIFKAIADPPTTSLQRLKGLTTGGLPTFVDVGNSFGAPAIVEDNFINQLVQNGKKVVMMGDDTWTQLFPHHFERSYPYPSFNVKDLHTVDNGCIEHLLPSLYEEDWDVLIAHFLGVDHAGHIFGVDSTPMIEKLEQYNTILERVIEVLENQSGPGSSHENTMLVVMGDHGQTLNGDHGGGSAEEVETAIFAMSFKKPLSSVPSEFDSCSCQLDLDGKNVCISTMQQLDFAVTVSALLGIPFPYGSIGHINPELYALGADSWNSDASQKLSESDIWMQNYANALCINSWQVKRYVDAYSTSSAVGFSHDDLSRIASVYAQVENHWSHSTKKLLLDRQNDSDTLVPALKRQIDAYFKFLTTVSELARSKWTEFDLNMMGTGIGIMLVSLIFQVFTILRANKKHGVMFSSSGDSCIITGSIFTIFLLGIRACSFLSNSYILEEGKVANFLLSTSGIVTLRQSVIQGKLLKESIGFLILSTLCRFAIEVGLSKQAATSAFMKDYTSWIINIASGLPVWDYAAEVIPMVVLILLAAWLYKATSGSLFDWPWKYVILGTILSYMLIIVHWITDSDRFGGTLMSQNIGRTYIPRIIYAIALGQLLLLTFGQLFKNSSLDCKTILVAKTMAILSAWSSTVILLSGKQGPMVAFASIVGGYFIMKFVNVEGGKDEPHRSFSIMQWSLFATCLFFCSGHWCAFDGLRYGAAFIGFEEFVLVRQAILLAIDTFGFSIILPVFGLPLLVATKYQANLGKHFIFTQLSQMYTTYGLITAITTTFTILCVTIQRRHLMVWGLFAPKFVFDVFNLILTDVLICLASIYYFDQGKDDQELKS | Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 949
Sequence Mass (Da): 105572
Location Topology: Multi-pass membrane protein
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K7LMQ5 | MSVPPPLAAVMWMSFMVAQWPWLEHQALIFKYLKAGLSVPLDLLLPIYKSLQLMSSHPSMGYYGKNSWKRLPI | Function: Transcription activator.
Subcellular Location: Nucleus
Sequence Length: 73
Domain: The QLQ domain and WRC domain may be involved in protein-protein interaction and DNA-binding, respectively.
Sequence Mass (Da): 8405
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A0A2A2L7D0 | MARRYDSKTTIFSPEGRLYQVEYAMEAISHAGTCLGIMAEDGVLLAAEKRNVHKLLDDSVLNEKIYRLSNNISCTVAGITSDANVLINHLRWWAANYRLRFGEEMPVEQLVQELCNEKQRFTQRGGKRPFGVSLLYAGWDKHYGYQLYQSDPSGNYTGWKATCIGNNHAAAVSLLKQEYKEQSLEDAKKLAIKVLWKTLDVKLASEKIEMAVLKRKDGKTVLEELTDKELETLIAEHEKKEKEAETMAEKMPTPSDQTELAFLRLLERTKKLCDNVETNAHKIQAAAGQLEALLNKMHELNKAESNELVQYTRELNQLRIISQVAMQKSAENKLQQIERIPKLFPLLNGGGKETEEKEEEIGEQLQSSNEIKLKNKTIYEQELRDELFHRIHQDKKEIKHDEMQEQMANELLSLTRSLKENMKVAGNVIKDDNQRLVRMQQQVDSNEERLSAESVRLARHAYKCGFDCMLVFIVFFIFISFIWMVLVMKIFPKVSDWRKSTCQQSLRPQYRCLTHIHMGMRTGNYNVFFEFTVVIPVIKNLCLEDNLSNINALSPFVLMLAVLYSVILELATSPTSQVLHERNHFKDRYTEEQKLLDYILFNYEKAVRPVKNSSSTVVVKLGMTLTNLFDMDERNQVLTINVWLDQWNPADFNNIKSIRIPCDLIWLPDIVLYNSADDYTTGYMKSRAMLDFDGTVFWPPPTQLRSTCKVDVTLFPFDYQKCSLKFGSWTYHGFQLDITNRSNNIDLSMFVQSGEFDLVKVGLTKNDRSKTQSRSIRSEKSLGTHAVPSPTQI | Function: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 793
Sequence Mass (Da): 91439
Location Topology: Single-pass type IV membrane protein
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C6TMF0 | MANYGTTQRIPTSSTPQSTADTYEPEPKAPHEKFYSDFRIYCPINIPSTSEAAGVRIMRNMCNFGLYYTLFVWIILFITLIPQRKVSLILFVIMTYVTTLYFLLLRAFPNSVVLHRIIDKRVVLALLAIATAVQLILTKAGIHLAVTLASSVPVLLVHAVLWASYDAFEVEDSSAKGELAPLAGHSESVADNSDAV | Function: May be involved in both secretory and endocytic intracellular trafficking in the endosomal/prevacuolar compartments.
Subcellular Location: Membrane
Sequence Length: 196
Sequence Mass (Da): 21665
Location Topology: Multi-pass membrane protein
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A0A068WLC2 | MTGINTTVSVKIIMHPSRRIAVICLFLAFILCIINHLNILGILGGPRITKEVGNRLSHFKSEDTYKPLMCSINGYMSPGCYQLKNSTLVVDFKHIKYWCEMEGYLNPTEDVFHISNGGAQSISPLTFKTHEPLGYYMGNRFSSKPEGKARILLVDAEHTIPISRQWDPRGHPYPIQIAQFGLACYSRYRTLQSWKPSPHAFPYQMVVDFKSQFASHLNCSSDNNHCSFGEKAGSVSYKLTGANLSHNLTALITKGANWPRGTRLVINVSLRLSTRRRAQIHFACTDTFGEGSVVIENDYWALGYSESVDLKVVFFQKHCRKVVLLQNLEMVLMKAVDSINREAKAKPILKSLLLDSKTHKLMVVDAVELRYPRQSIDGDGPGVVQELLLFVPIKNERVEEVGSLRHLLVNTEFERQRFMAAAEWLVQNQAQDGSWRISAKHVLTRDIYLKPGWCSAMGQGQGISLLVRASHVTGDEVFLKAAHRALGPFSRSVQLSQSSDEECGVRANFLGQSTLPWYEEYPAIPSVFVLNGFIYSLIGLYDLSKMTIVNKSNNSVTARASQLLEEGVGTLVRVLPLYDSGTGSFYDLRHLSLAHAFRLSPRIERLTLSKQGVVDTRSGTLQALLKAGPNRARWQYHQIHLLQLYQLAAVIAPQHANLWHIYFDRWLAYLWGFRSDHN | Pathway: Glycan metabolism; heparin biosynthesis.
EC: 5.1.3.17
Catalytic Activity: [heparosan-N-sulfate](n) = [heparan-N-sulfate](n)
Sequence Length: 678
Sequence Mass (Da): 76484
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I1J3Y5 | MGGFAMGYTFDSKSGLTMAALLLMIVSFYAGILFGNNAPLYVSQLVSHSSSSSSPPNNVSSNGTTKFTNKVALTYWKTPLVIPETGMDVCPLTFNEYIPCHDVSYVATLAPSLDFSRKEELERHCPPLEKRLFCLVPPPKDYKLPIKWPLSRDYVWRSNVNHTHLAEVKGGQNWVHEKDQLWWFPGGGTHFKHGASDYIERLGHMITNEAGDLRSAGVVQVLDVGCGVASFSAYLLPLDIRTMSFAPKDGHENQIQFALERGIGAMISALSTKQLPYPSESFEMIHCSRCRIDFHENDGILLKELNRLLRFNGYFVYSAPPAYRKDKDYPVIWDKLMNLTTAMCWRLIARQVQTAIWIKENNQSCLLHNVEKKHINLCDAVDDSKPSWNIQLKNCVLVRNSKTDSYKLLPTHERHSVFSENLNMIGLSTFFCTSERS | EC: 2.1.1.-
Subcellular Location: Membrane
Sequence Length: 437
Sequence Mass (Da): 49442
Location Topology: Single-pass type II membrane protein
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A0A0N7B2Z1 | FFFVMPFLVGGFGNWLMPMMINSPDMAFPRLNNLSFWLLIPSLLLLILSMFISVGAGTGWTVYPPLSNKIFHSGVSVDLTIFSLHLAGASSIMASINMISTIYNIRVNFMMMNKISLFSWSILLTSILLLLSLPVLAGAITMLLFDRNLNTSFFDPSGGG | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
EC: 7.1.1.9
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 160
Sequence Mass (Da): 17637
Location Topology: Multi-pass membrane protein
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I1LIY2 | MVSVVLPLIIHFEPHYGQTNMLVYLGICSLVGSLTVVSIKAIGIAIKLTLDGISQIVYPQTWFFLTVAIICVITQLNYLNRALDTFNATIVSPVYYVMFTTLTIIATAIMIGPGQDISSIASEICGFITVLTGTIILHMTREQEESNMQKTFTWFIGEDLMKDVENEHLILIHDSDYLER | Function: Acts as a Mg(2+) transporter. Can also transport other divalent cations such as Fe(2+), Sr(2+), Ba(2+), Mn(2+) and Co(2+) but to a much less extent than Mg(2+).
Subcellular Location: Cell membrane
Sequence Length: 180
Sequence Mass (Da): 20136
Location Topology: Multi-pass membrane protein
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A0A160ACC0 | TLYFIFGAWSGMVGTSLSIMIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMMGGFGNWLVPLMLGAPDMAFPRMNNMSFWMLPPSLMLLLASSLVENGAGTGWTVYPPLSSSIAHSGASVDLAIFSLHLAGISSILGAVNFITTIINMRSTGISFDRMPLFVWSVGITALLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
EC: 7.1.1.9
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 219
Sequence Mass (Da): 23584
Location Topology: Multi-pass membrane protein
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A0A068WW14 | MKNHTILCKCFPSETCVKRSSECASLVGCFYSVQKDALGYVVDEHYGCLLNNSFSIISCLNFRGTNTTCCFSSNSSDYCNAHLPVNKHQNTSALFFPLTFFAVLCILLFILAFVYIKGNFSKHEKPLTKHSSTYFPEFTDSGSGSGKPFLVSRTIARQTILLVCIGKGRFGEVWRAVCNGEVVAVKIFSSRDGASWTRETQIYTTALLSHRNILAYYASDMISRGGCTQLWLVTAYHAAGSLHDFLSTAEGVTPQCGLKLARSIAAGLAFLHSEVVGFRGKPPIAHRDIKSKNILVMANNEACLADFGLALVKTSKGMNGEGTSDEASESGDALPPASLFAGTKRYMAPEILALYPLVWGGWVRARTQERQIDEKQSGECDEDNLSIPGELLECRHPLLSFDVYLSTDVYALGLVLWEIWRRCTGKQYELPYYDSVPSDPNFLQMYRVVVLGEPYDSPCNTLVDLPLPMQVCHLCNHILVGRIGATLEAHRHRRHGGSGRRPSLTMERRGSSDEEWLVRWADVIAECWHPRYTHRLSALRVRKTLTVIEATVS | EC: 2.7.11.30
Subcellular Location: Membrane
Sequence Length: 553
Sequence Mass (Da): 61504
Location Topology: Single-pass type I membrane protein
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A0A3N7G3G7 | MKSPCSPYVRRTPASGVRSTSERIPYSPTSSSYSGSSAVKKRDPLFAVAKSVAGVFGACLMPPEPEPNDSKAFGSSEELKAPSVVSNTSGSSERRQGSNRGIYSSPFNSVREREPGSVNFTMEEIYTATRNFSPTFKIGQGDFGTVYKGRLQDGTAVAIKRAKKSVYDKHLGEEFQSEIRTLAQVEHLHLVKFYGYLEHEDERIVLMEYVPNGTLREHLDCMHGNVIDLAVRVDIAIDVAHAVTYLHISPNYSQGHKVLQHSPHRKLSSQGSRFWFC | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
EC: 2.7.11.1
Subcellular Location: Cell membrane
Sequence Length: 277
Sequence Mass (Da): 30750
Location Topology: Single-pass membrane protein
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A0A0G4IU12 | MSTAMQELEARDALRFSWMRWPSTKVEASRVVAPLAAMYTPLAVQDYNGQVQYEPVSCSGKACRALLNPYSELDYHNRIWVCPFCLTRNHLPQCYNDIGQYNLPAELMPEYTTIEYVLPVEPVPPLHILFVVDTCTIDLELDKLRESLIAVLPQLPPNALVGLITFGKHVAVHELGFGECSKCYVFRGNPKNDNVSSTFVADMLGMSAPAAAGAPGPSPTNKNAQQQRQQHQHQPCFFMPAETCTPAVTSILADLVPDPWPVKGDERPSRATGVAASVAIGLLETVAAKRNGRVMFFSAGAASAGPGKIVSVKLEETIRSHHDLFKGNCPWYDKACKYYGGLADRLVASGHVFDLFACSLDQVGLAEMKVLPEKSGGFLVLSDMFRYNDENGSDVFAQSFAACFAAGPDGNLNMAFQGDIEVHTSREVKVSGAIGHLSSKNQKGASVSDKEVGVGGTVAWHLGGLNSTSSYAFYFDVVNTSASSQYSHLQFVTRYRDATGVARIRCTTCMVPLTDTSNDHGLSQVAAEFDQEAACVLVARLALFKAETEFTTDVLRWLDRMLIRLMAKFSSYTKDQPDSFRISPYMTFYPQFMFHLRRSQFLQVTNSSPDETAFYRMIFLRESVANSLTMIQPVLLAYDLCDASGAGGAPATVNAVLLDAASIGPERILLLDTFFNVILWHGESVASWKKSGLDQDPNYDYLKEFFQMARSDADAFIANRFPAPLFRNCEAGDSQSRFLLAKLNPSVTQNTASSYPGQAGPPPVFTDDVSLKVFMDHLRKLAVQN | Function: Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules.
Subcellular Location: Cytoplasmic vesicle
Sequence Length: 785
Sequence Mass (Da): 86265
Location Topology: Peripheral membrane protein
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A0A816ASH6 | MTSAPSDVPDAHTFYNNPQQQGLKERDESRILYMRNFNNWIKSTLINEYLQRLKNEQPERSNEIHVFDMGCGKGGDQLKWQSARVRFVTFADLTENSVEVCKQRYNERKNHSSYKADFYTLDCTKELIQEKLGSSKPCFDLVSSQFVLHYSFDKIESADRFLRNAAELLRVGGYFIGTTVNSCQLVQQCRAAESQQISNDVYSIHFDPSVDLSEKTGEGIPLFGAKYHFNLHQVVDCPEYLVYFPLLEKLAHKHGLELVDRQTFKDYFDNNKYSGEARNLLARMKALEYYELPSDRPDNNRGLPINHNQYRHAAKYINERNRENRHPIRSCRTLSEQEWEITRLYIIFAFKKTRYIKYDDDKLPSQ | Catalytic Activity: a 5'-end (5'-triphosphoguanosine)-(ribonucleoside) in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.56
Subcellular Location: Nucleus
Sequence Length: 366
Sequence Mass (Da): 42998
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A0A5B8MTF5 | MVVVRTAKAYAAFDGRTEVTDEDVGRVVGMCLGHRTRKDPLDPLGGVQKVNAVFKRIFADGLTYEDELIVPLRKQSGGAKAEQGGAKKKATGPVVKPVAEVSSAEKAQAAQKKKEAVVAPPPEAVFFGQWTEEEDELVLFQQSDQGRALSISYEDAAACLGRTSNAVKCRWHSQVKGKVETMSSEEYTLRLERGARRWFQFRKQG | Pathway: Porphyrin-containing compound metabolism.
EC: 6.6.1.1
Catalytic Activity: ATP + H2O + Mg(2+) + protoporphyrin IX = ADP + 3 H(+) + Mg-protoporphyrin IX + phosphate
Sequence Length: 205
Sequence Mass (Da): 22545
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I1JK63 | MVKFTIVVIFLFFMFPIAFADLRVGFYSSSCPRAEQIVGQVVQRRFNRDRSITAALLRMHFHDCFVRGCDASILIDSTRGNQSEKAAGANGTVRGYELIDEIKKALERECPSTVSCADIITLATRDSVVLAGGLKYDVATGRRDGHVSQSSEVNLPGPRSTVSRVLEVFSANGMSLDEMVTLLGAHTVGFTHCSFFRDRLNDPNMDPSLRAGLGRTCNRPNSDPRAFLDQNVSSSMVFDNAFYKQIVLRRGVLFIDQQLALDTLSKGLVTVFAGNNAAFQRSFADAMVKMGNIKVLVGNEGEIRRNCRVFNSAS | Cofactor: Binds 2 calcium ions per subunit.
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue.
EC: 1.11.1.7
Catalytic Activity: 2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O
Subcellular Location: Secreted
Sequence Length: 314
Sequence Mass (Da): 34586
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A0A0G4J2M3 | MAGGGGGAGAGIHAGYAAGPVFRAWQQPFVDVRPEDLVMPVFVTDADPRACQAVESLPGVNRYGVDALIDALHPLVDIGLRSVIVFGVVSSSQHKDAFASAATDPKGPAAVAIRQLKRAFPDLVVIADVCMCPYADHGHCGVIDADGRVDVESSVARLAQIALFYAQCGADVVAPSDMMDGRVHAIKDALRRDGFGSRVPVLSYSAKFASCFYGPFRDAAKSAPSKGDRSGYQLPPGSTGLALRAVARDIAEGADFVMVKPAGPYLDVISAVRQRCEVPVFAYQVSGEYAMLRHAASAGAVDLRQAALESLIALKRAGATVIITYFTPDILSWLRDARAA | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 1/4.
Function: Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen.
EC: 4.2.1.24
Catalytic Activity: 2 5-aminolevulinate = H(+) + 2 H2O + porphobilinogen
Sequence Length: 340
Sequence Mass (Da): 35748
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K7K4D8 | MSSPHNSSPDNETPDNSTPDDADNSSSPSSQSPPPSSPPPSSPPPSSPPPSSPPPSSPPPSSSSSPPPSSPPPSSSSSPPSPSPPTSNNPSPPSPNGSSQSPSPPGSSRSPPSFESPSPPHKSLDSPPSSRNSGSGSDSGSRDSNGGGGDDSSKAIVGAVLGIGSVLLILVIVCVVCSRKKKKNRMYYYAGEQSMGKGNNNNYYNSGQHPNYYGGPHGDHVVRMQQNGMGPGGGGWGAPPPPPPMMMSSAEFSSNYSTGPAPLPPPSPNLALGLKGGTFTYEELAAATNGFNDANLIGQGGFGYVHKGVLPSGKEVAVKSLKAGSGQGEREFQAEIDIISRVHHRHLVSLVGYSISGGQRMLVYEFIPNNTLEYHLHGKGRPTMDWPTRMRIAIGSAKGLAYLHEDCHPRIIHRDIKAANVLIDDSFEAKVADFGLAKLTTDNNTHVSTRVMGTFGYLAPEYASSGKLTEKSDVFSFGVMLLELITGKRPVDHTNAMDDSLVDWARPLLTRGLEEDGNFGELVDAFLEGNYDPQELSRMAACAAGSIRHSAKKRPKMSQIVRILEGDVSLDDLKDGIKPGQNVAYNSSSSSDQYDTMQYNADMQKFRKAVFSNSEEFGTSSGSSGEVSQKQQRL | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
EC: 2.7.11.1
Subcellular Location: Cell membrane
Sequence Length: 634
Sequence Mass (Da): 66905
Location Topology: Single-pass membrane protein
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A0A497TBM0 | MEKLIIAGADESGRGAVIGPMIMVGVSIHSDKEHFLRKFGVKDSKELTAKKREKLSKSIEKIAKDIIVLEIGACKIDNYRRSGISMNKLEAMKFAEIINLLEPKTAYIDCPDTNKAKIEGLIRRMLNNNVKLVVEHFADKKYPSVSAASIIAKVERDKRVKKLEREYGEIGSGYPSDPITQEWLRNWLKENKDFPEIVRKTWVTAEFMTKERLQRKLSSFFKNVLKFG | Cofactor: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
EC: 3.1.26.4
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Subcellular Location: Cytoplasm
Sequence Length: 228
Sequence Mass (Da): 26091
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A0A846Q7A2 | MISVKKIREVEKKAEAMGISEAIMMENAGANVARILNEKIGLKGKRILVFCGTGNNAGDGLVFARHSLVYGAKVDVYFVKDPKILRSDITRKNFGILGNIKSLGKPVKFYVKNIPRMKYDILVDALLGTGLKEIVSEEYAKVIEKFNSMEGFKTSIDCPSGINSDNGKLMGSAVKPDLTITLHDRKRGLNPGNSGEIIITDMGIPKI | Cofactor: Binds 1 potassium ion per subunit.
Function: Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX.
EC: 5.1.99.6
Catalytic Activity: (6R)-NADHX = (6S)-NADHX
Sequence Length: 207
Sequence Mass (Da): 22616
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A0A7J4TC79 | MAAIKTWIQALRIPFTTASVLPVILGLAIAWSQGNAWNWGHALLVIFAVAFLHLGTNAANDIYDHYSGNDAANQYHNAFSGGSRVIQEGKLSPREILFASLSLLFAGLLLGMVIAASLQSWTLAFLALAGFLCGFFYTAPPFRLGYLGIGEFLVFLMFGPIAVLVGYFALAQGFDLLPLLASIPVGILVMLILLLAEMPDLEADKKTAKKTFVVLFGRERAVYFLAISLLIAYLFVGTGVALRIMPPLTLLMLLTLPLAVGVLKKAKKHALEPMGIVPAIGGIITLHAATTAILIITFIALALIG | Pathway: Quinol/quinone metabolism; menaquinone biosynthesis.
Subcellular Location: Cell membrane
Sequence Length: 305
Sequence Mass (Da): 32651
Location Topology: Multi-pass membrane protein
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A0A0R2L7Q3 | MRKQERQAIISELITNETIGNQDELQKHLAAQGVSATLATLSRDLKELHIVKEPNASGKASYRMLQIPTAASAELFAQQFREVVIDFTQVEFMNVVKTTPSDGNALAAVVDDLDETKITGTLAGHDTILVISPSKDAASELHEQWQAYLN | Pathway: Amino-acid biosynthesis; L-arginine biosynthesis [regulation].
Function: Regulates arginine biosynthesis genes.
Subcellular Location: Cytoplasm
Sequence Length: 150
Sequence Mass (Da): 16462
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M4SS56 | MDALQGVETAEAATTAAALAATLDQSVYGDKPEAHPGKQASAAVRRTATRGICASGAKIGTSQALADALLCLCWTDTGSPPQGQGSVCRKNLGNTLTSTWDTASATVSAAYAQIKGACKLQTGHTITAANIAEALTAVKHKIAQHKEGGYLGKYEGEFSCDGKNANGVCIKYPDFSDKGNKAFEEIEWVKKLRSVETALRKREAAVARVDTLTTALETQTAAAWLIPQRAKTSQQKREGVSPKQHTSTGNGNKQQADQCEAIKKATECKEKQPNCEWQGKNDEDGPHCKVNKTHITKEAAQTGTNRGNEETTTDKCSQAKTSDECAAVKGDIPKDKKAVCGWIEGKCQNSRFPVNKKLTLMVSAFVSIAAF | Function: VSG forms a coat on the surface of the parasite. The trypanosome evades the immune response of the host by expressing a series of antigenically distinct VSGs from an estimated 1000 VSG genes.
Subcellular Location: Cell membrane
Sequence Length: 371
Sequence Mass (Da): 39496
Location Topology: Lipid-anchor
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A0A1V2BM56 | MAGQCIILMGVSGTGKTTVGQALAQALGAKFIDGDDLHPRQNIVKMAASQPLNDEDRGPWLERIADVIFSLEQKNESGVLVCSALKKRYRDRLREGSGSLRFLWLTGEYECILQRMQQRKGHFMPEALLRSQFAALEAPDASERDILAVDIAPDVASIVAQSLNLLEPQSLQGMPA | Pathway: Carbohydrate acid metabolism.
EC: 2.7.1.12
Catalytic Activity: ATP + D-gluconate = 6-phospho-D-gluconate + ADP + H(+)
Sequence Length: 176
Sequence Mass (Da): 19292
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A0A084WAJ7 | MAAKATAKPAIFGGLVRYYDEFYTLFNGLVQGYYLNRYGGSLAEVFYGLTRVSVKSKSFNKRDRNWSFVVLVVLPYALSKMETLCNHWREDYEAGKQISIERRLLFRLVPFVKAFYESVKLIHYVSYLANATETHSPALRILRLGLTYLSEEEESWSFKDIFQGKIRVATMLSTALLRWLELSAFFLQFIEWWQTEANIGDLSKLPIPDAPSLDTNASKYANVRLLLPVYSKSPTKRKQMPGH | Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Membrane
Sequence Length: 243
Sequence Mass (Da): 28051
Location Topology: Multi-pass membrane protein
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E0W0J4 | MELIEIWLLDKINARLVIKTKHFINDIEDNTTIVMQTDPLQILKYNYIELVKTSKTLKFIVDDNNLNEKGINWIKVILFPKIINIMLNSSNLKTIKNGDLKKKNFSFTNLVDIVRYYELYEKMKLKYAKFLIENWTENTDPKKFVYEDIGIASYLMLLWNSDNLPAGKEKKQKFVDLGCGNGLLVYILNSEGHLGVGIDLRKRKIWDSYNSDTILKEEIIIPSVDTIYPEADWIIGNHSDELTSWIPIMAKFSNDHCQYFVLPCCPYELNGQKFQRKNSSMSSYQDFIYYVKNISEMCDFNTLVDRLRIPSSKKVCLVGFRKGNFEKNHVTQSNSKIINYIKFNCQSDVDVQKNYVKNLKGGNTPDGNVKIRDSVEQVRNCTKLPHTVIDQILKAVMNELLNEKRNLYEIKNDGSSSHWNRGGTLSVESLANKINKDLLQELKKECKGLQTLEVPKVC | Function: Adenosyl-L-methionine (AdoMet)-dependent tRNA (uracil-O(2)-)-methyltransferase.
Catalytic Activity: S-adenosyl-L-methionine + uridine(44) in tRNA(Ser) = 2'-O-methyluridine(44) in tRNA(Ser) + H(+) + S-adenosyl-L-homocysteine
EC: 2.1.1.211
Subcellular Location: Cytoplasm
Sequence Length: 458
Sequence Mass (Da): 53061
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A0A384CR21 | MAAPLSVEVEFGGGAELLFDGIKKHQVTLPGREEPWDIRNLLVWIKKNLLKERPELFIQGDSVRPGILVLVNDADWELLEGAPWPGDPAAFHSLCLSLNTE | PTM: C-terminal thiocarboxylation occurs in 2 steps, it is first acyl-adenylated (-COAMP) via the hesA/moeB/thiF part of MOCS3, then thiocarboxylated (-COSH) via the rhodanese domain of MOCS3.
Pathway: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis.
Function: Acts as a sulfur carrier required for 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Serves as sulfur donor in tRNA 2-thiolation reaction by being thiocarboxylated (-COSH) at its C-terminus by MOCS3. The sulfur is then transferred to tRNA to form 2-thiolation of mcm(5)S(2)U. Also acts as a ubiquitin-like protein (UBL) that is covalently conjugated via an isopeptide bond to lysine residues of target proteins such as MOCS3, ATPBD3, CTU2, USP15 and CAS. The thiocarboxylated form serves as substrate for conjugation and oxidative stress specifically induces the formation of UBL-protein conjugates.
Subcellular Location: Cytoplasm
Sequence Length: 101
Sequence Mass (Da): 11229
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A0A7R9FP81 | RVLFIEIKGKTSRDPMEKLETLRLNIWNANIWLPGNVTWEDMKSKPGRPMPEFQDLLYAFPFSISFLLFRIIFDMLIMEPLARAEVQSVSTVGPCQQSKVGMGKEYMALSSDLFTHLLVPQGNGSLNAGRKWIEREKGSLRSVKEQLEIRKIRETGYRSVAHSIVFLFGVWTMADKPWLRNTDLCFWNPPHPVPWDIWWYYMLELGFHITQTLMLPFDVKNSDFLAQLTHHVVTIGLMMGSWTAGTIRIGSIVLLVHDCADVILQCGKLLKFFKGPDPDATVFKVFLAFTATWILTRVIYFPLYVNIPATKAILHFDYFYFASVSLVVLLWSLFLLHLYWTYLLLRVIYGMVFRKKKLHDNRSEDEDSDEDDEIGKNKSK | Pathway: Lipid metabolism; sphingolipid metabolism.
Subcellular Location: Membrane
Sequence Length: 380
Sequence Mass (Da): 44117
Location Topology: Multi-pass membrane protein
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A0A174GHJ5 | MLEKVKEIVAEGLDVNAADLTEETTFESLGADSLDLMDMVMTFEDEFGVEIDTEAIGDLKTIGSVVTYIEGLKK | PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine of apo-ACP by AcpS. This modification is essential for activity because fatty acids are bound in thioester linkage to the sulfhydryl of the prosthetic group.
Pathway: Lipid metabolism; fatty acid biosynthesis.
Function: Carrier of the growing fatty acid chain in fatty acid biosynthesis.
Subcellular Location: Cytoplasm
Sequence Length: 74
Sequence Mass (Da): 8075
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R1BFK4 | MPFWRSRDDGSDSASTTSRGSASLKPAGPPPPGEHSQRWPLTASLWRALRFHAGSIAYGAFLLAVTQLLRRGLQWLERQSAGGGTGVTMRCLRCYTRCLGRCMSYINSFAYIFVALDGDAFCSACRETFLLTARYPAQAVINVTVQSLLFGVQSVGIPLACGVVSYALISSGVWPTWVDAAGRWLEEAASGSPLTGPAADGAGVAQLAEGGGGGLSAQPLLRWMQDQPGVEPLLPSLAVAALALFVGRALASVYECTVSTIFVCAMRDAEAYGGAHVTSALRASLKLEGKGGTRNSAALARAKSANSRGLVVRGKGAEADVEAAAGRGYLRLWE | Function: Choline transporter.
Subcellular Location: Cell membrane
Sequence Length: 334
Sequence Mass (Da): 35033
Location Topology: Multi-pass membrane protein
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A0A2E7FQL2 | MLGLGWSEMLVIGIVLLVVVGPKDLPMMMRNVGRMMGTVRRMGNDFRREIDKAIAADEIAEAKKAISDPLKQTSAEINREFNSIRNGKVEPTGKLKPPATGEESVVDAIHAQAGMTPSRAEPSAASAALRAKVSESVAKPANAATTEAEQPAPIADAPAKTKVKAAPRKAATSTAKTSEPKSKAPAKAAKPAAAAKAAKKPAAKKTADEKPAAQQKSASKTGATKTTARKAAPARKKAVAETGGDK | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. Together with TatC, TatB is part of a receptor directly interacting with Tat signal peptides. TatB may form an oligomeric binding site that transiently accommodates folded Tat precursor proteins before their translocation.
Subcellular Location: Cell membrane
Sequence Length: 246
Sequence Mass (Da): 25420
Location Topology: Single-pass membrane protein
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A0A651GIP6 | MLARLHGGRERGEDRRSAGAGPAVGHVPTAVGWRAPRSGADVADVADPPDPAVPEDLQAAVPEGLLARARELRTNAYAPYSGFRVGAVVVTASGRRFEGVNVENVSYRLTTCAEQAALAAMCAAGPLEEVVVVAVAGDGPSPCTPCGACRQTIAEFGTDAVVHATGASGPVLTTSIAELLPDAFTTERLRDRGEVAGGGA | Function: This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis.
EC: 3.5.4.5
Catalytic Activity: 2'-deoxycytidine + H(+) + H2O = 2'-deoxyuridine + NH4(+)
Sequence Length: 200
Sequence Mass (Da): 20342
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A0A1B9BCA3 | MFAGIYTPSITPLREDGSIDLENWEKHVDNLIAAGINGVLLFGSIGEFYAFTVEEKQEAIRHMTKHVAGRTQLLVGTGGTNQEEVIALTNYADECGADAVVIVSPYYFGPSEEVAEKYFSAIAENTKLPILLYNFPDRTGSDLTPELVARLAGKYESIVGIKDTVDNASHTRKIVQAVHPIRKDFSVLSGYDEYYLSNRVSGGAGILTGMTNVEPETFVAMHRAYERGDYAIAIQQATRVANLMRIYDVSDLFITAIKAAVKVKGLPINTVAKEPALQANAQTEAAVRNILES | Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4.
Function: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
EC: 4.3.3.7
Catalytic Activity: L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O
Sequence Length: 293
Sequence Mass (Da): 32010
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A0A193KDD0 | MKKLLIILPILLALILSGCSSASSGTSAKTKQYASNHDLNGQASWYGNAFHGKLTASGETYNMRAYTAAHKTLPFGTIVRVTNTENNKSVDVKINDRGPYVKGRVIDLSLVAFNKIGDSSKGLAPIKIDILDDSNTFRYKH | Function: Lytic transglycosylase with a strong preference for naked glycan strands that lack stem peptides.
EC: 4.2.2.-
Subcellular Location: Cell membrane
Sequence Length: 141
Sequence Mass (Da): 15332
Location Topology: Lipid-anchor
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A0A7R8X6Z4 | MSAKNRQVCIFADEVEVINYLASTIQQSANEVLQEPAVCFFIGGSAAKLVCEAVTKIQSDWSRWRVAFCDERLVPSTHEESTYAAYAKYLQNSNPTLLNNFIKVDTSLPVDEAARDYEQKLHSLMSSEKGCSDLKWPHFDILVLGVGEDGHTASLFPSHPLLDEASKWVAPISDSPKPPPSRVTLTLPAIWAAGKCIFPVIGGGKADILKRILCPGDGGENLPVHRVMQSSKNTLWILDSKSAEKLEEFF | Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 2/3.
Function: Hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate.
EC: 3.1.1.31
Catalytic Activity: 6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate + H(+)
Sequence Length: 250
Sequence Mass (Da): 27564
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E0VMM1 | MIFLIFFGIFFISNSCFGANILYLVPLPAKSHYILGEKLVKELAGRGHEITIISSFKMSNPPKNIKEIIMPASLEDFGLFNKGKESGTFQLRKMSPIDFILFSAVGNMMTNKTLSDPNVRNLLKSNKKFDLIIGECFLTEGLLGGFSYKYKAPMIGVATFIPNTWSNEMVGNPASSAYVPEPILPYTNEMTFYERCMNFFYGMLSQYAYYNRHIPAQDKIMKSFFGQNVPDLRELIRNTSLVLVNHHHSMSFPRPYLPNMIEIGGYHVNPPKPLPKDLQKYMDESKDGVILFSMGSNLKSSDLPESRLVEILTAFSKLKQRVIWKFEKEDLPNIPENVLISKWLPQSDILAHPKVKLFVTHGGGLSLTEAVDRGVPVVAIPIFGDQPLNVKFVEKFKIGVGLEYEEISGKKLLESINEVLNNPMYDSNVKQKSKILKDNPMTQLETAMYWIEYVIRHDGAPHLRSATQNLTWYQIYLLDVFAFLAVVVLTFFFIVYKLLKCLKNCLCRGKKEKNVSSLKKNK | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
EC: 2.4.1.17
Subcellular Location: Membrane
Sequence Length: 522
Sequence Mass (Da): 59458
Location Topology: Single-pass membrane protein
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A0A1X4XYW6 | MNGLLLINKPSGIKSFDVVKKVKGKFNEKVGHSGILDKFACGLMVIGIGKATKLLSFFEKSYKVYKAKIIFGYETDSLDITGNIVHNNDYLPNIEEIYRTINQKFIGKAEQTVPIYSNVKVKGKRLYKYALSKQNVDLPTKTIYISSIDILSYNQGVLEIKVVCSKGTYIRALSRDIARSLNAYATVTYLERLYIYPFSINEAVDLSYVSQEHVIPFEKVKYMTKIDTLEVFNGIAN | Function: Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
EC: 5.4.99.25
Catalytic Activity: a uridine in RNA = a pseudouridine in RNA
Sequence Length: 237
Sequence Mass (Da): 26827
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E0W4F7 | MFSYCLRNTKRSKIYPDPEKFDPMRHAPEEKSKRENISALYFGEGPRICIGNRFGFFQVKVGLLTLLSSYRVSPCEKTPSQLKFNVGSLVLTVEGR | Function: May be involved in the metabolism of insect hormones and in the breakdown of synthetic insecticides.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 96
Sequence Mass (Da): 11007
Location Topology: Peripheral membrane protein
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B5T2Z3 | MMKVLIFIIMLNFNIMINNKQIMMKLLVMMLMVISLMFTYSINFNENWMNLYSWMGMDLLSYMLSLLSLWIIMLMFMVSLNFKNIKMFSFILLLLLLSLMLSFMSINYFMFYLYFEISLFPTFLLIMGWGYQPERINASMFMLLYTMFASLPLMIILFYLLSYFNSLNYLIILNNTMKFTYLKLLMYLYMIFAFLIKLPLFMLHMWLPKAHVEAPICGSMILAGVMLKLGGYGIIRSMMMMLNYSKYFNYIITIISLLGMFMLSVICLRQYDLKLLVAYSSVVHMGMMLLGAMSLTKWGMVGSYLMMMAHGLCSSALFILVNLSYKCSKSRNMLINKGMMNMFPTLSMWWFLFCICNMSSPVSLNLMSEIMIINVMLNWSFNSIYLLMASMYLSSMYSLYMFSYSQHGAYNSLINKMNINNMNEYLVLLLHWVPLNLIIMKIELFI | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
EC: 7.1.1.2
Subcellular Location: Membrane
Sequence Length: 446
Sequence Mass (Da): 52577
Location Topology: Multi-pass membrane protein
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R1EE71 | MFVHYLSKFVDWTDTFLMIGSKSFRQVSFLQVFHHATVGMIWGALLRKGWGGGTCVWGAFINSVTHVLMYTHYLVTSLGLHNPLKSQLTNFQLAQFASCVLHAALVFASETVLPARLAYIQLVYHPTLLFLFGFQMKWVPSWITGQTITGRESEAPEKKVA | Catalytic Activity: a very-long-chain acyl-CoA + H(+) + malonyl-CoA = a very-long-chain 3-oxoacyl-CoA + CO2 + CoA
EC: 2.3.1.199
Subcellular Location: Membrane
Sequence Length: 161
Sequence Mass (Da): 18184
Location Topology: Multi-pass membrane protein
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E0VIF1 | MTEVKKSWNVVSNLEEIIEILTSENFDKFGHHLFNSNIPEKCFLEPCILGVDEAGRGPVLGPMVYSVFFCSINDADILKDIGCTDSKVLTEKKREDIFDLINQNNDKLGWAVDLLSPNLISNRMLQRKKYSLNEIAQNSTIKLIESLLEKNITLKDIFVDTIGPADKYQEKLSKLFPNSKVTVKSKADLLYPVVGAASICAKVIRDTAVQQWKFPEKITIDAEFGTGYPGDPKTKKFLLESKDSVFGFPNLVRFSWSTSAKLLEEETLVEW | Cofactor: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Function: Catalytic subunit of RNase HII, an endonuclease that specifically degrades the RNA of RNA:DNA hybrids. Participates in DNA replication, possibly by mediating the removal of lagging-strand Okazaki fragment RNA primers during DNA replication. Mediates the excision of single ribonucleotides from DNA:RNA duplexes.
EC: 3.1.26.4
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Length: 271
Sequence Mass (Da): 30605
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Q7WTY7 | MTDRFPDGITVTTPNPADSGSGETLASPFPEPEPISTNPSKGAKVRPADRIFQGLAEGSGILIVALIAAIGVFLLMRAIPALARNEENFFLYGGNWVTTDTSAMHFGILDLLQVTVFVSVFALVLAMPVALGIAIFLTQYAPRRLAGPLAYMVDLLAAVPSIVYGVWGLYVLAPVLKPVAVWLNENLGWFFLFSTGNASVAGGGTIFTAGIVLAVMILPIITAVTREVFMQTPRGQIEAALALGATRWEVVRTTVLPFGLSGYISGAMLGLGRALGETIALLIILRGTQTAFGWSLFDGGYTFASKIAATASEFNDQFKAGAYIAAGLVLFILTFVVNSLARAAVGGKGRA | Function: Part of the binding-protein-dependent transport system for phosphate; probably responsible for the translocation of the substrate across the membrane.
Subcellular Location: Cell membrane
Sequence Length: 351
Sequence Mass (Da): 36936
Location Topology: Multi-pass membrane protein
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R1E841 | MAQPRGVRVGLCLALLCYLPSSASLALPEAFRRARARNARLQRSASSPAPRPPPSAAPLASGEVALPPSLEERLSSALGVRSLNPLQRLALPHALGGGDTLVHAETGAGKTLCFALPIAASLAAADGAASSPAACDGSVHALVLSPTLELCAQTAAVLNALLPGCAAVVATDEAARLLSGGAAASALAGARVLVSPASLALALLPASEAPAGGGRRASGAAMRADAGRSRGAGRRGGGGGRRPAAGGRGGGGRRFEEGGEGGAVTAVRSRSLEPGGLLGSLRLLVLDEADALLGTLGKYATQRQKESRSRHPKPAALVVKSLFTAAASRPPSSGTLQLLGASATVGRPLRRELQALSGRSLAVAQLPSSPPGADIGAPSASPAGSSRQAASSARAVGLPSTLELAVLTCEGDNTALALQRALGAAGEGAALVFVPDGRPVGPELRLLRQCGLPEAESLVDYLARRAGGGGAEGGGAGGGGAGGGGAPLRLVASPRSARGLDLPEVSLVVILGLPASADTLLHLAGRTARQGAAGRVVLIATPDEAAGRLGVLGAQLGVDLRARSSAVRERDEEWARTWAVHQQVVQAERKYNN | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 593
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Sequence Mass (Da): 58941
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R1EFE7 | MAETPGGKQSPGSKASKKVNDSKFGETIVEEIQVSVTVMLTGVALVEMGYDKELRAAMYEMADAWGCINTYLPQHVTRKRILDFQGETWKDKQETERPNKNYKRAPGWTNANSKPDAGAAAAPPSACPMRADGGAAPSGRAAAAEPPKASGCPVDHSKWSAWAGRSAAAAGGDGEADINPDNRMPVLSQQPAAGQDAVLDTSRVVSSIPQGRAGATERWVYPSEQQFYNALVRKGKDDGVDTAAMPSVLEYERLHCDTCDPAKVSLLRFQGRPFELSPKARLKTALGLAPRPFDRHDWTVDRPNPEVRYIIDYYDASASREAGGPLPSLHDPDGVPTILMDVRPAGDTPGELLDRARMVLQKGVVATLREALTPIATSDSTVSAPAAGGAAAEAAPPPPAVSEAAAVRSACASAMEALSACMQKGSDDAGCMQARMGLTMCIAQQVCSAEADLFHSYKGSADGEGGVA | Function: Lyase that catalyzes the covalent linking of the heme group to the cytochrome C apoprotein to produce the mature functional cytochrome.
Catalytic Activity: holo-[cytochrome c] = apo-[cytochrome c] + heme b
EC: 4.4.1.17
Subcellular Location: Membrane
Sequence Length: 468
Sequence Mass (Da): 49327
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A0A402CRN4 | MTTDLLLRAAVGDDLLSNEPMSRHTTLKVGGPARWFWAARDVDDLSRVLTACTEHEIPYLFIGHGSNLLMSDAGYDGLVIQNRCKGSRIGAETYSESGVSFGSLFYQTAREGFSGLEWAIGIPGTVGGALVSNAGAYRGNIGPLVRSVRVFADGRDQEVGPEWMEFSYRDSRLRRSGIGRTVILSCMLHFEDRGDPETIIARAKDYQAQRRAKQPYAPSAGSFFKNVTDKAFAQTLPDLPDALKAAGVVPSGFLIEACGLKGLQVGGAQASEKHANFLINAGGATASDLRRLAYKVKGLVHEKFGVTLEEEVLYVGDWSEWTE | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation.
Catalytic Activity: NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
EC: 1.3.1.98
Subcellular Location: Cytoplasm
Sequence Length: 323
Sequence Mass (Da): 35087
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A0A9E6YYZ2 | QPGSLLGDDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGISSILGAINFITTILNMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNT | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
EC: 7.1.1.9
Subcellular Location: Membrane
Sequence Length: 175
Sequence Mass (Da): 18675
Location Topology: Multi-pass membrane protein
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A0A6P8LLP7 | MATGIALIYPALLTVLAENNYTIFPDETGVPHLIKIDNSPLTELELAILGINVESVSFNLYTRDNPMIGDVLNLNDVVSVRKSHWNPHRETIIVTHGWNANGRSSSCTLVRDAFLNVWDSNVIIVDWGNIAKNLLYSVVAKSVPRVALRVADFVNFLQTSAGLRTSKLKIVGHSLGAHVAGLSALEIGRSSQVAEVIALDAAKPMFEHKGPDGRVDKLDARNVQVIHTCAGYLGLNISVGTSDFFANDGRNQPGCVNDLIGACAHSRSYEYYSESVMNSKGFLGVSQNGAMAYMGGPTLDPKAKGTYTFQTNYQYPYAVGG | Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+)
EC: 3.1.1.32
Subcellular Location: Secreted
Sequence Length: 321
Sequence Mass (Da): 34734
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E0W2H3 | MSLAKKISFGNFCQLCSKIKSADHEKKIIILRNYISNWKKKAKDIESDGLNLDDSFFPIFRLLIPHLDRERGAYGIKERTLAKIYISILSLPKDGEDALKLLNCKNPKTSYFNNCDFASIAFCILRNRCAEGGQLSVEEVNKHLDKISTSHAANEPRNVDAELISLLKSTNAEEQKWLIRILLKDVKLGLSENVIFKCYHPDARELYDSSNSLRKICDLLNDPEIRLNEIQIQLFTPFKPMLSEECDIQKIDYYLKRSCHFFIETKLDGERFQLHFEEGNFKYFSRNGYDFTTNFGSSKREGNLSPRIFKRIPPHVKSFVLDGEMMSWDRITRSFSSKGKNLDVKNLKEGNHYQSCFCVFDILLYNGEVLTNKPLIARLEILEKIIEPEEGTIIILNRKQISSNSEVIDSLNEAIDNREEGIVMKESMSVYKPNVRKNGGWYKIKPEYTDGLAETLDLLIIGGYYGRGHLKGSVNHFLLGAAVNVSDDNILFYSTGRVGSGYSIKDLEDLSLKLKPYWKEAKNDRMPLSVKWGKEKPDVWIKPDKSYILEIKASEIVSSAIFKSGYALRFPRVEKIRYDKTWKECLTLHNLEEIAKIASGKLTASHFSQSNIPSFLPKKKAKTSIWNINSENFDFSGIKCISKLLQGKEICVFSGFKNIKKLDLEKKVVEFGGKLVKNPGKNTFCILAESDNHTRIKNIIKCGSYDILYSSCFFSFLKIENVKMPKLKPEHFLAMSKGTKEEFSKSYDKYGDHFTKKSTFDAIKHSLNAASQEGKNIVLTSDEIYEMDVNLFGKTSPYSIFRNHVGYFDQFKIVSDSSSKFSSDLDLFKIDFRFYGGKCSDAIDDSTVTHVITLSSDSSRINEINNENHKRKRKFHVVNEKWIESCIKENA | Catalytic Activity: ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.
EC: 6.5.1.1
Subcellular Location: Nucleus
Sequence Length: 891
Sequence Mass (Da): 102161
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A0A656Z8G7 | MISVTSAQLDAWLAAFIYPLARILAMLAAAPVFNNTGMPRQIRLVFGIAISLAIVPALPPIETIPPGSWHGIAVLGQQILIGAIFGLTLRIMFTAVDIAGEIIGLQMGLSFASFFDPRNSAQTSVMSSFLGLIMTLLFLAMNGHLLMLSVLAESFQLLPISTTAFAAPGFSALLAWSAVMFATGLMLALPLITALLIANISLGVLARIAPQLNIFAVGFPVTIVTGYAMLLFSLPHFGGVLQHLYDQGFDALAAVLQAGGALNPNPPAP | Function: Role in flagellar biosynthesis.
Subcellular Location: Cell membrane
Sequence Length: 269
Sequence Mass (Da): 28241
Location Topology: Multi-pass membrane protein
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E0W2C1 | MSDWTDPRCKDPFNYTALPRDQPPLMTCNGCCVKMVRNAKSPYESVRRTCTTQLQINLFMVDHVCMMESSNTGHMCFCEEDMCNSSPSIHLSLPSQLTSSLYLSSSHPRDLSYPPLFNSIAFKCF | Function: Required for homeostatic regulation of sleep under normal conditions and after sleep deprivation. Important regulator of the Sh K(+) channel, acting as a signaling molecule that connects sleep drive to lowered membrane excitability, possibly by enhancing K(+) channel activity and thus reducing neuronal excitability.
Subcellular Location: Cell membrane
Sequence Length: 125
Sequence Mass (Da): 14217
Location Topology: Lipid-anchor
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A0A196SKI7 | MELKSCLWCQDIEKSPIPEECLSEDVIVGIDEAGRGPVMDSKQLTAEKREHLLGDIQAADSIGYVIRTLSPKEISANMLQTKPFNLNEMSHKAAMDMIRELLRMKVKVTEVYIDTVGDPEKYESKLQAAFSFTTIKFKVSKKADALFKCVSAASIVAKTRRDHIIENHSWEEAYMEGKSFGATGSGYPSDPTTKAFLANCMHPVFGFPTFIRFSWSTIPKLIQEKNGAVVVWKESLEDEDSPHRRPKKKYRKEESRLCKEHSIESCSF | Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
EC: 3.1.26.4
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Length: 268
Sequence Mass (Da): 30364
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A0A913XIM4 | MASIGYRTNYTYGYIVEYSKPCFDSWLLIPGENLWNSGLRGFLYILAMFYFFLGIAIVADIFMSCIEVITSKKRKVTRYDPEKQESVEIEVFVWNETVANLTLMALGSSAPEILLAVIETAQELGRDPTGDDKDGLGTFTIIGSASFNMLLITAVCVISVPSGTVKMVREFGVFIWTAIWSLFAYVWLLVTLKWVSPGEVEIWEAFVTLAFFPLLVFTSWCQDHGWWCRSSRVLSVEPPEVRVVGMMERPSSHMMVHRSMELRVIEQHRISVSEHDIKELPKSKDKLKEVVSLWKGQKPDANSNETVESLAHAFKHFKEANAQPQNSTTARLRFRHAALNSLTASRHRVPKASKFVDRLDYDEGQKIMNALAKSVVGSKFIGTHALDQPGQNFNFGTQSYSVVKSAKHIDIDILLTNSRKRMSRAGTPHRLMSLPAPYDPCTQIDESKTAKLNQQNGNVKTANGKVKHSDKEELYTRRSSPSSSEQSIPMSVSHRTSLVSLPEETVYSIDYETRDGTAKKGRDYTNMKGTMTFQPGTTKHILRIPIIMHDEFSKNREFYVILKNPXPGNGVDLGESSLTRVTIIDDDEPGEFAFEQASYHANFVTEDVTCTVVRRKGCDGHVTIQYRTLNGTAVGGKPDDSDVDTWDFEQVDDGCLTFQHGETSKMLVIRINPESQKKNFIVLLHDPSPGASLGDKTAAVIHISNDVDDIVDRVANIITLEDQNQSLSKSWRMQFEEAIVLQGEEDEDGNVQPLSALDLTLHLLTMFWKVLFAFIPPRPFLGGWAAFVVSLMFIAGLTAVVEQLGKLLGCVVGLKNSVTGITIIAIGTSLPDTFASKTAALQDTGADAAIGNITGSNSVNVFLGLGLPWVISVCYHAAKGTTFKVSTNNLSFSVLVYTLCGGACIILLVLRRVFLKGELGGTPVQKWLTGLFLVFLWFLYXVLSSLMAYGYIPNTI | Catalytic Activity: Ca(2+)(in) + 3 Na(+)(out) = Ca(2+)(out) + 3 Na(+)(in)
Subcellular Location: Cell membrane
Sequence Length: 956
Sequence Mass (Da): 106228
Location Topology: Multi-pass membrane protein
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E0VI43 | MIFVSKIHTLLIFNKSTRLKRFFCTKPVRVRFAPSPTGLLHLGGLRTALFNYLFAKSQNGIFILRIEDTDLERKIDFATENLIKDLEWCGIKFDEGPYFQTERINIYKKYAKQLLENDSAYYCFCSKERLELLRKEMIKTGEVPRYDNNCRHMSKDEIDDKLKSGSQPCIRFKLTKYNEPIPDLIFDSIKHDVHEVEGDPIILKADGFPTYHLANVVDDHLMKISHVLRGVEWQISTVKHILLYKAFNWTPPLFGHIPLLLNADGSKLSKRQNDINIQQLRNNGYFSNAILNFVIKSGGGFNINHDEKCTKIFLMNELVNEFNVSRISNISSKIDLKDLDCYNHFEIERMLETNEGTNSLIDQVLQLLSEKYKNVTLDECVLKRDYIKQILHKMKKRIVNLKDLISNENSFLWFWDGQIKINENDAIIVENFLRDIDNIEWTFEGIKIFNKKFAADNKVKFSDLMKIFRFILIRAKEGPGVAEILLILGKDVVRHRLSVALNNFQAL | Function: Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).
EC: 6.1.1.17
Catalytic Activity: ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu)
Sequence Length: 507
Sequence Mass (Da): 59141
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A0A402CYP8 | MGTGKSAIGRAIARGLSVRHLDTDCEIERRFQMDIPRIFAEHGEAAFRSAEQDVLRRLTQRGSPAAAPPRLVISTGGGTPMREENVELLREIGQIVWLSAPIATVLQRVGRNLKQRPLLAGHQDNPQQRIRQLMAEREPRYASLAELRVDTSPFASPKDAAAHIISLLQQNEDI | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.
Function: Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
EC: 2.7.1.71
Subcellular Location: Cytoplasm
Catalytic Activity: ATP + shikimate = 3-phosphoshikimate + ADP + H(+)
Sequence Length: 174
Sequence Mass (Da): 19331
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Q5L7U3 | MKTKLIILLILTTMIHTNTVNAQHSQLKRADFQQTIDGKQTDLYFLRNKNGIEIAITNFGGRVVEFWTPDKKGHFEDIVLGHDHVDKYLHYKGERFLGATIGRYGNRINKGKFTLNGQTYQLPINDTPNSLHGGFKGFDMVVWDVEQPDSQTLQLTYLSKDGEEGYPGNLQVSMNYKLTDKNEFIITHQAQTDKETVINLTHHSFFNLHGAGNKDINDHILMINADKFTPVDRTLIPTGILQDVEGTPMDFRRPTPIGKRVNDSFEQLEFGHGYDHNWVLNRKTSNTPELAATVYEPASGRYLEVWTTEPGLQFYGGNFFDGTMTGKHEKKYNYRASLALETQHYPDSPNQPAFPSTTLLPGDTYKHICIYKINVQ | Pathway: Carbohydrate metabolism; hexose metabolism.
EC: 5.1.3.3
Catalytic Activity: alpha-D-glucose = beta-D-glucose
Sequence Length: 376
Sequence Mass (Da): 42875
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Q17C24 | MGKLNTSYGNYCYQTGTMLDRAVTKYCTSRNDYSESTAGDEASLQLGRLICCRGGVRQMRYDYEDDNLGRVEDMSGRDGTKCDRDELDERHVEAIDESRLAYRAEGNSNIVLALIDDHQVLRLRKTTISCPGGKDTVDLERFVKFSRVIASCFSRRYVPHPKLGRLDTYDLDEFNKKLAKFRPVNRLAKEIQVRDCILYPDVAFLPVTLDPLTFRNQDFGQDTVRGHWQNTYCVEIKPKQGWCLDDLCYGEGLIRDQLFGCWNADQLIDLSSMDKCRFCLFQYSKLRNKMIGKISKYCPLDLFSGKPIRMLNAIKGLIGSPQNNLKLCKNGRIVYDEQQDKSVFNRILKDIFPRDGRTKEERKTVFMNLIKETLLKDFSNYEADHDRKLLTLRKDRKKKDKNLIHQRTCSTINYQFLPRNCALKQILDIQLLVKSTLPKVYSNLYQRDIGSSSASNPFAYIDELYEKYLDYLDEHCGQRSSTDRLDLLDDSYLNEQERYLLGASALDCSIMITFRRLAAREEDRLPAAARTHIVTIERMKFLVNVTIADLDPKSLKHCSKYVRQLQESIVHYREFMSKLRR | Function: Phosphorylates Ins(1,3,4,5,6)P5 at position 2 to form Ins(1,2,3,4,5,6)P6 (InsP6 or phytate).
EC: 2.7.1.158
Catalytic Activity: 1D-myo-inositol 1,3,4,5,6-pentakisphosphate + ATP = 1D-myo-inositol hexakisphosphate + ADP + H(+)
Sequence Length: 581
Domain: The EXKPK motif is conserved in inositol-pentakisphosphate 2-kinases of both family 1 and 2.
Sequence Mass (Da): 67576
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E0VFL7 | MDSLPIAYLTRSEIFSACHRLHSKDLTEEENKKIYGKCNNINGHGHNYKVEVTLKGPVSPVTGMVVNITDLKSYMDEVIMKKLDHKNIDEDVDFFKNGGIVSTTENLAIYIFNELRSLLPNPNLLHKVKIHETDKNSVVYRGEIT | Cofactor: Binds 1 zinc ion per subunit.
Pathway: Cofactor biosynthesis; tetrahydrobiopterin biosynthesis; tetrahydrobiopterin from 7,8-dihydroneopterin triphosphate: step 1/3.
EC: 4.2.3.12
Catalytic Activity: 7,8-dihydroneopterin 3'-triphosphate = 6-pyruvoyl-5,6,7,8-tetrahydropterin + H(+) + triphosphate
Sequence Length: 145
Sequence Mass (Da): 16503
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A0A402CXQ9 | MIPLIDPFGRAIQYLRISVTDRCNLRCVYCMPLDGVPYDAPEEVLSFDEIMRLVNLLAGHGLRKVRITGGEPLVRKNLPELVQRLAAVPQITDLGLTTNAVLLENQAQSLWDADLRRLNISLDTLQPDRFVKIARFAKFDEAMAGLAKAEALGFAPIKLNMVVMRGVNDDEILDMAALSLDHPYDVRFLEYMPIGQVTPWEWRASYVSNEEVIQRLSERFELQPIEAASSSTSRVFQIPGAVGRVGVINPISHKFCASCNRLRLTANGALVPCLADNYEYDIKTPLRAGASDEELIGHVKAALAHKPEQSDFEGRVERGGSIRIMAQIGG | Cofactor: Binds 2 [4Fe-4S] clusters. Binds 1 [4Fe-4S] cluster coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine and 1 [4Fe-4S] cluster coordinated with 3 cysteines and the GTP-derived substrate.
Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
Function: Catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate.
EC: 4.1.99.22
Catalytic Activity: AH2 + GTP + S-adenosyl-L-methionine = (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate + 5'-deoxyadenosine + A + H(+) + L-methionine
Sequence Length: 330
Sequence Mass (Da): 36626
|
E0W0K4 | MDYLGDIICLSLDSVIFGVCLKAYLRNKHALHSIENAPEFGIDKHLEVFLNKNSGKFPYIAVRGSVKALGPAIKSLNHPSISGVIQKLSIRDMSFREAHQDFGLTENQRTINEIFNSIPFALTSRRGDVEVEVIDALAAEILDLEVVSDRFDPSNLGFMDHMWGFFTGIRKRGLQTIEEILKEGAYITAVGEVQKDGGSLRIQPPTDGTPFFISTMPVNSLVRRLDEKVKYYGWISFGFGVLGIFLFGTLIRKYFKKHNEWLKKEAERKRLESTRKERRKNVRNTEDLPMDKLCVVCQSNPKEVILLPCGHVCLCEDCSEQITNFCPVCKSLIENKNPAYIS | Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
EC: 2.3.2.27
Subcellular Location: Membrane
Sequence Length: 342
Sequence Mass (Da): 38726
Location Topology: Multi-pass membrane protein
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A0A2K8N6D2 | MKAYPLSFRPVFQERIWGGSRLREFGYSGASDGIGEAWVISDHDHGPTPVADGPLAGKRLSEVMKANPEWFGLPPGARFPLLVKVIDASEDLSVQVHPDDRYARPRGDAGKTEAWFVLFAEPGASIVYGHRAQTREDFEKRMKEGAWGNLLVKVPVRAGDFFYVPAGTLHAIGRGLLILEIQQSSDTTYRVYDYDRVGADGRKRDLHVKEALAVTRCPSPKPQRPGYARSGRVGAVIEHLVRGEVFTIDHWLVDGEARVDECGVFRLISVIQGSGEVVWDHGRRSVAKGDHLLLPAVLHPVVLSGRFEALFSAPVISTRAK | Cofactor: Binds 1 zinc ion per subunit.
EC: 5.3.1.8
Catalytic Activity: D-mannose 6-phosphate = D-fructose 6-phosphate
Sequence Length: 321
Sequence Mass (Da): 35439
|
A0A6J1NAH3 | MADTTTYCRMLGHVLTIAMHVGNIVYMNRGFSPEVLQDPQLKAFGKLQPRYFTVWTFVLQIINACTGLVCDYLVISNSENKLYKLPKHLRGFKNTLFSAILWPSTWVVCSIFWGLYLYDRSLIFPEFIDKALTTTSNHIMHTAIIFVVLWEVYFTPRVEPRSHRRNILHILTHLLLYLAVLFYTHMQHGVWLYPIFSLVYGTIYFPLINIAIGVIALTFYYLQWTIINYLWSDSAKTKKIT | Catalytic Activity: 12-(9Z-hexadecenoyloxy)-octadecanoate + H2O = (9Z)-hexadecenoate + 12-hydroxyoctadecanoate + H(+)
Subcellular Location: Membrane
Sequence Length: 241
Sequence Mass (Da): 28217
Location Topology: Multi-pass membrane protein
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A0A174CXF5 | MKTNRKVICSSSAVRYAETLFELNIPKETIEKTREIFSEVPQITDVLDNPTIRQEKKEQVIDKVFPREMRNFLKIVCRYRKVRLLGEIFDAYDMRADEEEQIIRAVLFYTALPSEEQKKGMESFLCRKYGAKRAYIEMKKDDSLIGGFILRVGNDEYDRSTKGRLDRLEQRLTRR | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
Subcellular Location: Cell membrane
Sequence Length: 175
Sequence Mass (Da): 20756
Location Topology: Peripheral membrane protein
|
K4JC34 | VEKELLPGFHQFEWQPALKNVSTSCNVGIINGLSGWTSSVDDSPADTITRRFRYDVALVSALKDLEEDIMNGLRENGMEDSACTSGFSVMIKESCDGMGDISEKHGGGPLVPEKAVRFSFTVMSVSILADGAEDEVTIYTESKPNSELSCKPLCLMFVDESDHETLTAILWPIIAERNAMKESRLILSIGGLPRSFRFHFRGTGYDEKM | Cofactor: Binds 1 divalent metal cation per subunit. Mg(2+) or Mn(2+).
Function: Catalytic component of the RAG complex, a multiprotein complex that mediates the DNA cleavage phase during V(D)J recombination. V(D)J recombination assembles a diverse repertoire of immunoglobulin and T-cell receptor genes in developing B and T-lymphocytes through rearrangement of different V (variable), in some cases D (diversity), and J (joining) gene segments. In the RAG complex, RAG1 mediates the DNA-binding to the conserved recombination signal sequences (RSS) and catalyzes the DNA cleavage activities by introducing a double-strand break between the RSS and the adjacent coding segment. RAG2 is not a catalytic component but is required for all known catalytic activities. DNA cleavage occurs in 2 steps: a first nick is introduced in the top strand immediately upstream of the heptamer, generating a 3'-hydroxyl group that can attack the phosphodiester bond on the opposite strand in a direct transesterification reaction, thereby creating 4 DNA ends: 2 hairpin coding ends and 2 blunt, 5'-phosphorylated ends.
EC: 2.3.2.27
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Subcellular Location: Nucleus
Sequence Length: 209
Sequence Mass (Da): 23065
|
A0A7J4TDG7 | MQVQAVMVHPKALKKIKEKEKAKEQIMGYFAQASAAFPADQKKASLFIHKARRVAMKHRYRMPPELKRRFCKRCYAYLQPGVNARMRIHQGNKVVTCLDCNHIERIPFKK | Cofactor: Binds 1 zinc ion per subunit.
Function: Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends.
EC: 3.1.26.5
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Subcellular Location: Cytoplasm
Sequence Length: 110
Sequence Mass (Da): 12911
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A0A0D1W8F4 | MKKVAVIGAGYAGLAVSIGLARCNAMVRCIDIDEKKIERLSQGNVPIHEPEMEGMLRRQLADQRLTFSTDMIAGIMEADIIFIAVGTPGQEKGAPDVTAIFSVTDTIAQHIRKDVVVAIKSTVPPGTCEAVQTRLHDWIRGTYACDVVANPEFLREGRALRDFLEPDRIVLGGTDERAITVMQELYAPFVAAGVPFYMTDWRTAEMIKYSANSFLAMKVAFINEIARLCDAVGADVTVVAEALGADPRIGNQHLSPGPGYGGSCLPKDTEALALSARQAGAPLAIVEAVIESNRLQQKYVVEKIKREWSNLQGLCIAVYGLAFKANTDDMRESPAIPVIDWLLAEGVHVRVYDPQAMNQAYEIWGERIQYGMDAYDAAAGAHALVILTDWQEFTELHVDRLERIMAEKVIFDFRNACEAGIWRRHGFRYIGIGV | Pathway: Nucleotide-sugar biosynthesis; UDP-alpha-D-glucuronate biosynthesis; UDP-alpha-D-glucuronate from UDP-alpha-D-glucose: step 1/1.
EC: 1.1.1.22
Catalytic Activity: H2O + 2 NAD(+) + UDP-alpha-D-glucose = 3 H(+) + 2 NADH + UDP-alpha-D-glucuronate
Sequence Length: 434
Sequence Mass (Da): 47787
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A0A660TSV4 | MEIIVSDTIGFCSGVRKAIRGAEKALKGNSKIYCLGDIIHNKGVVNQLKEKGMVFVKSLDEIPNGASFIIRSHGLPFETIENIQKKAVHIYDFTCPKVKKSHKLVESLKNHKRPIVIVGNREHPEVKAIFSLTENRGIIIEKPEEVKTKLNTDECYVLVQTTFKPVLFYEIVKEIVSFTKKAIIYNTLCEETTKRQEEVKDLATKVDMIIVVGGKHSSNTKTLFSISNSMVKSVHIENADELQNDWFKEVHRVGIVSGASTPDDDIDRVIEKIYYFERNNEDETQR | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Pathway: Isoprenoid biosynthesis; dimethylallyl diphosphate biosynthesis; dimethylallyl diphosphate from (2E)-4-hydroxy-3-methylbutenyl diphosphate: step 1/1.
Function: Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis.
EC: 1.17.7.4
Catalytic Activity: H2O + isopentenyl diphosphate + 2 oxidized [2Fe-2S]-[ferredoxin] = (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate + 2 H(+) + 2 reduced [2Fe-2S]-[ferredoxin]
Sequence Length: 286
Sequence Mass (Da): 32509
|
A0A7R8X0J0 | MRDRVFEWELAGEWAEDVQWWFMDYWTLSFVFVAVYLILVFWGRILVVYRGLPEVYRSIRHDSLYHSMCLGMNLRHIPMVSVLAILFVISKFIELGDSVHRPSEAAFPLPPLGVLARFFIILNVLPHAFMYPYYTAGRRNWEGTHRTKGILLNLAIRFELLRPTRKMKEARRSTSCVTSEDGLLLSSLSLRSILNALPQSQLHRSRVQGKRIRGTIGKKSRFFPTSEDSKRNSTPLGLLPLTDSDFILSSKAKTDARQPGKKPHDYSAESHGMMFPEGIVEEEYDSPHQSRARPALGPNMFHDPSAYPKPNYPIFNGSRYEQLTKSHEYLRESGIPFERENLPYFFVFEWELAGEWAEDVQWWFMDYWTLSFVFGAVYLILIFWGRRWMASRPPYDLQKPFIAWNVFISVFSILVVNRCLPEVYRSIRHDSLYHSMCFVT | Catalytic Activity: a very-long-chain acyl-CoA + H(+) + malonyl-CoA = a very-long-chain 3-oxoacyl-CoA + CO2 + CoA
EC: 2.3.1.199
Subcellular Location: Membrane
Sequence Length: 440
Sequence Mass (Da): 51525
Location Topology: Multi-pass membrane protein
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E0VWC4 | MSQLNLVLEKLYEEYYKKTSTKLKIVDAYLLYVFLTGVTQFVYCCLVGTFPFNSFLSGFISCVSSFILGVCLRLQVNPQNKSDFMGISAERGFADFIFAHVILHLVVMNFLG | Pathway: Protein modification; protein glycosylation.
Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 112
Sequence Mass (Da): 12716
Location Topology: Multi-pass membrane protein
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A0A402CTZ4 | MPNPKLIIGTRGSALALTQTNTIADALRRVHLGLEVEIRTINTRGDATQAANVPLASFGEKGIFAKELETALLDGEIDLAVHSMKDLAHTMPPGLVLAAVPKREDPRDALIGSTLDSLRQGALVGTGSVRRRALFSSRRPDLRFLEIRGNIDTRLKKLEDGGYDAICLAAAGLKRLGLADRVTEYLDPEWFVPDPGQGALALQTRESDVQVRGLLSAVNDMASFVTTRAERGFLRAVGGSCQTPVGAHARHIDGGLMLRAMLVGDDGLMRRAEAGGAPGMAEELGARVAKMLR | Cofactor: Binds 1 dipyrromethane group covalently.
Function: Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
EC: 2.5.1.61
Catalytic Activity: H2O + 4 porphobilinogen = hydroxymethylbilane + 4 NH4(+)
Sequence Length: 293
Sequence Mass (Da): 31303
|
F0VJ37 | MSLARRTQQPLLALPPRAVFSRGLGPGFAPPFQSRRRSCARRDPSTSWLSPSVALPPLRNSLLSASAHHASLPTSFPAFHDPRKAHFSTVQTHEETHETSTAPRILSSSSSDIVENLAAECFLVDVFGRGHGLPASAGEGAERAKAENAESAAKQRTERRDLRAPLLFLWRNDKTIVIGRHQNAWSECNIQKMDESGVKLARRYTGGGAVYQDLGNTCFTFLDPVATHNKERNNKIILRALEKAFGIKCSASGRNDLVASDGRKFSGAAYSKLPHGWLHHGTVMREVDCEALGRYLTPSKEKLASKSIKSVTSRVVNLKTLHAGITHDNLCDAITDSFLEEYGSSADRNVVRGMDSVENLQLEGTEYRMREHPVFQNHFRTLSNWEWRYGHSPAFERSLSHRFPWGSFDVHVNVAQGYVTDAKIYSDCLFPDLVDAFTEAVRGCRFTELELRRAILDITLEKTSPELDCFLRDFADWLSTASQE | Pathway: Protein modification; protein lipoylation via exogenous pathway; protein N(6)-(lipoyl)lysine from lipoate: step 1/2.
EC: 6.3.1.20
Catalytic Activity: (R)-lipoate + ATP + L-lysyl-[lipoyl-carrier protein] = (R)-N(6)-lipoyl-L-lysyl-[lipoyl-carrier protein] + AMP + diphosphate + H(+)
Sequence Length: 484
Sequence Mass (Da): 54042
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A0A402CZP4 | MRAAASVTRSYLWPVLSVAAATGCFSLLRPYVDKGQASLLYLPIVLACAVRFGFGPAILGALLSFLCWDLFFLPPFYTLAVDDPKDWLSLAIFLLAAVVTARLAAQARAQTQEARTRESEIETLFEASETVSRVIRADRVLAALADQLQTLCGATRCLVFRRLGPGVALQLAPDGANEVPIDAQTLGRIASLAEAACANDRVIGLGASQHLWAKAVTDTDASLGGDGARIGVYIPLHAADALVGVLHVGPRGDSRPYSALEERLILTLANHAAVVIARDRLTQQAAEATALREADTLKDALVSLVSHELRTPLAAIKASVSGLLQPGAVWDPDARQEALVAIDGEADRLSGVVNNLLDLSRLEAGAWLPRKDWCDLAEVAGTALDRLPPAEASRVALETQDNLPLVQADYTQIALVLTNLMENAIKYTPSGSPIQVTMRAENDRTNSGQDGVLVTVRDFGHGFALGDEERLFDRFYRGAKHQGGAVHGTGLGLALCQAVIRAHGGRIWAANAPPGEPDGAIFSFFLPKG | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 529
Sequence Mass (Da): 56295
Location Topology: Multi-pass membrane protein
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A0A6P6F8A3 | MAKTTDSIRDVRKRTTESKSELQSIENKQNNDFLVNYQNQSYNIQKFLRYHPGGTKILRYFKNRSLEKAFEEFPHSQAAFHLLQEFTLNQEKYQKYENLIDWDKAILGQVGSLGHHYWEWVNLPVYRDIKLFKSNILESLTITPWYLIPIVWIPMSLYFFYKGLARIAAINTESTVFEPLTSFIFGIFIWTMLEYVVHREVFHFKPPDNSKLFITLHFLLHGVHHKAPFDKRRLVFPILPALLVAKLLLMIYNMVFPQTIIYFILSGTMTGIGIKIFIFIDFIININDVSNVKKICLIGYMIYDLTHYYLHHGAPKFGTYMYLMKRNHNYHHFLHHDLGFGITSKLWDYIFRTNICLRQLLKPIEW | Cofactor: Binds 2 Zn(2+) ions per subunit that likely form a catalytic dimetal center.
Pathway: Lipid metabolism.
Function: Catalyzes stereospecific hydroxylation of free fatty acids at the C-2 position to produce (R)-2-hydroxy fatty acids, which are building blocks of sphingolipids and glycosphingolipids common in neural tissue and epidermis. Plays an essential role in the synthesis of galactosphingolipids of the myelin sheath. Responsible for the synthesis of sphingolipids and glycosphingolipids involved in the formation of epidermal lamellar bodies critical for skin permeability barrier. Participates in the synthesis of glycosphingolipids and a fraction of type II wax diesters in sebaceous gland, specifically regulating hair follicle homeostasis. Involved in the synthesis of sphingolipids of plasma membrane rafts, controlling lipid raft mobility and trafficking of raft-associated proteins.
EC: 1.-.-.-
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 366
Sequence Mass (Da): 43623
Location Topology: Multi-pass membrane protein
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R1EUF5 | MHSPRAANNEPSSSTDIERPALSISPPAGGPSPAPCACAPCSAPRCQSAPLPLVIVVIIALNYIPYVLWTLERRRHLALTITLVVIFHALLGLVVCAWAYTCGTDPGVPPSQWQRRMAALAKARPGSSELKVCRRSGLYKPPRSHFCSVTRRLTLNMDHYCPWVANTVGHYNRKFFLLFLLYTCLLLAYVLLSIAPQLPDLFDWALDGDGRWVGGVAYAVVLGVMLAVDVLLLLLLGPFMCLHWKMAMRNQTTIDGDKLPQYDIGLSANLEQILGRRRLHWFCPCYCDGPVGDGVHWPTKTGGAALVPLGGSGTPLRTSAAASPRQACAGGCAPAAASSASASTAAGSRPASPRASPARASGGAGPSSQPAAPYRAVPALVYSAPAASPEAAGAPVQVSAAAVSHPAR | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 408
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 42983
Location Topology: Multi-pass membrane protein
|
R1DEG2 | METSLNRCLEATGANFGRASARFGPWAGAEERAEEEAAAPVYRSAKPPSSDMPRLTRGFSVHVPWLGRISGGTSAQKRLQTLAVFSFSLYGLLPLIAISWFVVLLCLINPLTLPFILGYLYFVFVADKAPTAGSRAPFLRQLTTWWHAYCDYFPMLLVKTAEYVLGYHPHGIISVGAFGAFATDGARTLSLVASGAQPREGRGFSSLFPGIERRLVTLPINFTVPFGREYILSMGACTSDKATFRSVLGRGSGSAVVVVVGGAEESTMVTPGQIDLVLERRKGFVREAIMAGASLVPVLAFGENDLYAVFHTDDTHPIARLQRVVRRHFGVALPLFRGRSMFITEFGLMPNRKPIAIVVGGPLAPPPLDDARRAAFRPKWGPDDAPSNDDARMVDAMHTEYVDALSALYEAHKEQPWNLAGINRQGTFRVLK | EC: 2.3.1.-
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 432
Sequence Mass (Da): 47220
Location Topology: Multi-pass membrane protein
|
A0A8T5IWI0 | MVKSWKKEIIGEKIIIINSKNKSLLGMEGNVIEETKNTITLGNGKKLLKSHITIKINGEIIEGKTLQKKPEDRIKK | Function: Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
EC: 3.1.26.5
Subcellular Location: Cytoplasm
Sequence Length: 76
Sequence Mass (Da): 8583
|
A0A378YGM8 | MARVVVEVMPKAEILDPQGQAIVGALGRLGHPGISDVRQGKRFELDVDDNVSDDELERIAESLLANTVIEDWKVVRL | Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 1/2.
Function: Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the ammonia molecule from PurQ to PurL.
Catalytic Activity: ATP + H2O + L-glutamine + N(2)-formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide = 2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ADP + H(+) + L-glutamate + phosphate
EC: 6.3.5.3
Subcellular Location: Cytoplasm
Sequence Length: 77
Sequence Mass (Da): 8494
|
A0A660SXT5 | MLLRAWLINLFPELWKNSIDVNILKRINLPRNASCLVALSGGGDSVAMLDLAYKESVNYGLTLYAAKVMHGIRSGEEEEAEARLCERLCKERDIPFEVLTADVDTVEDIQLRYGCGPEQAARDFRRNLLENHKVKITADYILFGHTADDNLETVFMRLLSGSGPEGLSGISQDTSSTFRPLLGLTRSDLREYLVSRDIPWIEDRTNMENIYRRNRLRNELIPLVTDIFPGWEKALETLGERSKEAADALSRAAASQLPCRKTGDDCCWNEADWDSASEYLKALSLWEAFNHLDNSRIPDRQLPWKSLKEARRSINEKRSWNAFGLKLEISDAVVRMSRSGGRGSSWVHILLEYADIIDDFESVLGGYHIKASFSKASAKAPGLRYIKMYHGDWPLELRFAAAQKSLKLVKRCITEKKPVKKFPDSQGKLVYILIEPVKEGIHAG | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34) in tRNA(Ile2) + L-lysine = AMP + diphosphate + H(+) + lysidine(34) in tRNA(Ile2)
EC: 6.3.4.19
Subcellular Location: Cytoplasm
Sequence Length: 444
Domain: The N-terminal region contains the highly conserved SGGXDS motif, predicted to be a P-loop motif involved in ATP binding.
Sequence Mass (Da): 50294
|
A0A651GL02 | MRERPIGVFDSGLGGLTVLHAMVDLLPAEDLLYLGDTARYPYGERDLADLQRISLAVAEELVDRGIKLLVVACNSATAAALPELREALDVPVVGVVDPGVRAAAATSRTRRAVVIGTRATVASGVYEDAADRLDLGLVVRTVPCPGLVELVEEGRTSGPEVTAIVRDRLAPLLSARIDTLVLGCTHFPMLARPISEVVGRDVTLVSSADETAFEVRDLLERLGWLREEEEAAGGRRHYLTTGDPDTFAALGERFLGAPLGSVERVTLAALEPRTPVDPTRRRGSRRAGRRQAEESRWSSAAT | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Provides the (R)-glutamate required for cell wall biosynthesis.
EC: 5.1.1.3
Catalytic Activity: L-glutamate = D-glutamate
Sequence Length: 302
Sequence Mass (Da): 32449
|
A0A6J6ANA3 | MQRLPKIVRVLAVISFTLVVVLFAALIVNSFQNAGKPLTTLTPQGPSSESIQKLLVPVTSIAAVVFVGVLGAALLISWKFRERKDSDPDEFPEQVHGKTALEIGWTILPALILAGIAVGTVMTLINLNREEPNSINVQVAGQQWWWQYKYDVNNDGNFDGPEDITTATEMVIPAGRPIQVTTTSNDVIHSFWIPGLNGKRDAVPGLRNPLKLQADEPGIFRGQCTEFCGLSHANMRMLVRAVSTSDYDAWVKNQLKDHAADPTDPTALAGKKVWQALCAQCHVIDGINDVKMKETKPPLVSGVAPDLTHLMTRGTFAGSIFNLYEPVGSDGSPLPMGDVAAAGDPGAALTGGKVNTATVNRVTLEAWLRNAPALKPMYPQGGRGMPNLNLTEEQIDQLVAFLETLN | EC: 7.1.1.9
Subcellular Location: Membrane
Sequence Length: 406
Sequence Mass (Da): 43860
Location Topology: Multi-pass membrane protein
|
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