ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
|---|---|---|
A0A959RDQ9 | MSKKLVLVDGMAMVYRAYFALIGRPLINSEGKTTSAVYGFVNSLVKVLDDEKPEYVAVCFDTAEPTFRHEQFPEYKAQRMEIPTDMPWQIEKVKEVIKAFNIPMIEMHGFEADDIIGTLAKKAEEKGITTYMVTPDKDFMQLITDKILMLKPARSQSGGVVKDIEVIDEKGVQNKFGVPPWQVIEVLGLMGDSSDNIPGIKGVGEKTAIALIQEYGTIEDMYKNVDAISKPKLKEKIINDKEMAFLSKKLVTIKTDVPIKIKPEDLKREEPDAEELGRLFTELEFKTMIKRFMPGGASPKPEKGEAKPKKTAKPKEEKQL... | Function: In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity.
EC: 2.7.7.7
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Length: 958
Sequence Mass (Da): 109797
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A0A3A0BBW0 | MNENYFPITTYGMPILRQVTYKVTEIDSKLIENVQRMFLTMLNADGIGLAAPQVNLDHSFAVIDISMIEEFQEIKPFTMINPVIISKEGSIILEEGCLSIPGIRAEIERPEKIFVKYTDLSERDVELEADNLLARVIQHEIDHLSGKLFTDYLTIDQKRQLKDSLDEIKNGKVTTRYPLLIHSR | Cofactor: Binds 1 Fe(2+) ion.
Function: Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.
EC: 3.5.1.88
Catalytic ... |
A0A0C1QH26 | MSLTSPSIDQSEVDKFSRIADEWWDECGKFKPLHQLNPIRIKYIRDKVIKHFAIEKEAKPLSSMKILDIGCGGGLLTVPLGKLGADILGIDVTEKNIKIANAHKIKNNLADNINFLHTTIEKLEQENEKFDVVITMEVVEHVADLNSFLKSSLNVLKPGGLIFISTLNKTLKSYLLAIIGAEYVLRWLPVGTHDWNKFLAPEDIISRLAENNIKHSDPVGVSYNPLYQAWSISEDISVNYMLYGIKQE | Pathway: Cofactor biosynthesis; ubiquinone biosynthesis.
Function: O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway.
Catalytic Activity: a 3-(all-trans-polyprenyl)benzene-1,2-diol + S-adenosyl-L-methionine = a 2-methoxy-6-(all-trans-polyprenyl)phenol + H(+) + S-adenosy... |
A0A0C1QWC5 | MSENIKKNLIGLDKVELAAAIKELGESSFRAKQIWQWIYRIGIADFNHMTNLPASLREKLAESYTLERVQVSKELISFDETRKWLLKFSDTNEIEAVFIPEKTRGTLCVSSQVGCTLNCSFCHTGTQNLVRNLTAGEIVAQVLHAKDSLSDWNFKEENRKLTNIVMMGMGEPLLNYDNVAKALKIVMDPDGLGISKRKITLSTSGIIPLIEKCGDELGVNLAISLHAVRDDLRNTLVPINKKYPIKDLLNACRKYAPTQNSFRKVTFEYVMLKGVNDSKQDAKELVRLIEGIPAKINIIPFNKWPGTEYQCSDNRTIQEF... | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurrin... |
Q756Y6 | MLKYCRQLKTLHALQVRGTIHAGSKSYLVMKNRLEGSWAFNSDAKRFKHDGSMVQELEGEGKRGNASVLEEAWDTSGDDDILQHIAALEERRGEPDPSMCSGVASGTRLEVQMQRTEAEIKQSKEAPEPLIELPDVQILGSKTVDSKESIKNSAAGTQELAFLTQRPTLHEHISADQPQASDQRPSASPKRVQCFMLSDEQRNVLKLAEEGTNIFYTGSAGTGKSILLRELIKKLKTVHGRQGAVAVTASTGLAACNIGGITVHSFAGIGLGNSPKENLLKKVKRSRKHVQRWQNCKCLIIDEISMIDGELLDKLDYIAR... | Function: DNA-dependent ATPase and 5'-3' DNA helicase required for the maintenance of both mitochondrial and nuclear genome stability. Efficiently unwinds G-quadruplex (G4) DNA structures and forked RNA-DNA hybrids. Resolves G4 structures, preventing replication pausing and double-strand breaks (DSBs) at G4 motifs. Inv... |
A0A9D1LD97 | MPRLTVFPGALSGEVQAPPSKSILHRALICSALAGGNTVFPPAESEDIRATLSGLRALGAAFREEGQALRFASRREMCAPAEIDCLESGSTLRFLLPLSLALCGGARFRGRGRLASRPLDPYRDLFVRQGISWEKAPGEKLDLQVCGRLHSGEFPLRGDVSSQFVTGLLLALPLLEGDSRIRLTTPLQSASYVDCTLEVLQRFGVRVDCREDGYFVPGGQVFRPVDFQVEGDWSQAAVWLAADALGARIWVCGMSPDSRQGDRVVLDILGRMGAEAVWEGDRVLVRAQNLHGTTIDAADCPDIIPILALVASRAAGVTVI... | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7.
Function: Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-ph... |
A0A1D2YRT6 | MELNNIKDPKDIKNLSIKGLEQLSYEIRQFLIENLSKTGGHLAPNLGVVELTLALHYLFDSPTDKLIWDVGHQAYVHKIITGRANQFHTLRQFKGLSGFPKRSESEHDVWETGHSSTSLSAAMGLAIARDLKQEKHRIIPIIGDGALTGGMALEALNHIGHEKRKMMVILNDNTMSIAPNVGAIHNHLERLRTNERYLKVKDEIEFLMKKIPAIGGKVAKAAEKIKDSLKYLVINGALFEEMGLTYFGPIDGHNFEDLFTTLKLADKTDGPVLVHVVTKKGKGYRPAELNADKFHGISPYKIESGEVLKKEGPPTYTEVF... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Metabolic intermediate biosynthesis; 1-deoxy-D-xylulose 5-phosphate biosynthesis; 1-deoxy-D-xylulose 5-phosphate from D-glyceraldehyde 3-phosphate and pyruvate: step 1/1.
Function: Catalyzes the acyloin condensation reaction between C atoms 2 and 3 of pyruvate and glyc... |
A0A1I8P8A7 | MAKNKGNSAAETAYKGIYGALRVLVHLTAAVQFWYAIYYDYKFVHFPDSENRPSPFGGKFRFLTFLDAIIQALYYTISLVNDFVGTNEVSPKKLPMVRKIKDYLMTTFAFPIALHVGITFWGLYAVDRELVFPKALDAVFPTWLNHIMHTNIVVFIVLEMFISFRAYPSRVKGLTGLATFIGAYLVWLHIIKHYSGVWVYPILEVLQFPQRIMFFGGCLGLAVGLYIFGEVLNNLVWSKELKMAQRKHK | Catalytic Activity: 12-(9Z-hexadecenoyloxy)-octadecanoate + H2O = (9Z)-hexadecenoate + 12-hydroxyoctadecanoate + H(+)
Subcellular Location: Membrane
Sequence Length: 249
Sequence Mass (Da): 28584
Location Topology: Multi-pass membrane protein
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A0A1G1LD82 | MSDKVNIDQIAELARLNLKPEERLALSKDLDEILAYVDQLQELNTDQVEPTSHPLALENVFRQDSVAKCDVGDRVLEHAPKREEKYFKVPKVIEGQS | Function: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an ... |
A0A379FF35 | MVIPLERLFFSVNRFYPALVGNDIGCGMTLFQTEFNHSKLNLDKIEKKLSEMSDIAPIEWLIDNLPADMQNHPFAHSLGSIGGGNHFAEFQQIDQVINQALFTNSGINKKQLLLLVHSGSRGLGQSILRAHTEQFGHQGLVANTDAANDYLQAHDHALNYAKLNRHLIGHRMMEQIHTQGTVITDVNHNLVEPCELYNQQGWLHRKGATPAHHEIVVIPGSRGDHSYLVKPIISELSLHSLPHGAGRKWMRTECKGRLSHRFTPLQLSRTALGSRIICANKQLIYEEAPQSYKSIETVIESMRSLGLIEVIARLKPVITY... | Cofactor: Binds 2 manganese ions per subunit.
EC: 6.5.1.-
Catalytic Activity: a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + a 5'-end dephospho-ribonucleoside-RNA + GTP + H2O = a ribonucleotidyl-ribonucleotide-RNA + diphosphate + GMP + H(+)
Sequence Length: 531
Sequence Mass (Da): 59768
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A0A2Z2NKS8 | MMKTERTARVARFYHEGELQGNAELTLPKTASHHLITVLRTRQGDVIELFNGDGFNYRATVLETGQRTPGKRAQLQVHQACAAQNESPVLITLIQAISRGDRMDTTLRQSVELGVNHVQPVYSRHSAKPLDEKRTAKKMEHWQSILISASEQSGRACLPTLAPAISLQEALETLASRASSAPSLYVLDPTAQSSLTAQLRAMHLTQAAAADNDTSHPVSIGLIIGPESGLDADEIAKAVESGAHAATIGPRILRTETAGPACIALTQAILGDLDQ | Function: Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit.
Catalytic Activity: S-adenosyl-L-methionine + uridine(1498) in 16S rRNA = H(+) + N(3)-methyluridine(1498) in 16S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.193
S... |
A0A2Z2P3C4 | MIAESELNEALERGLQQLAGFGVPEIPASQRLQLVSLVALLSKWNKVYNLTAVRDPLTMVDRHLLDSLIMSRWLPASSAADDSQYDVMDIGTGAGLPVLPLALVRPDLRFLSIESNGKKIRFQQQALMELGVRNVTVLHDRVENVTDSAHMVLSRAFTAPVDFLKVAEPLCAPDGLVAVMLGHAERLPVSLGSAYTLSELVQVDVPGTDSARHVALCRRQHG | Function: Specifically methylates the N7 position of guanine in position 527 of 16S rRNA.
Catalytic Activity: guanosine(527) in 16S rRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(527) in 16S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.170
Subcellular Location: Cytoplasm
Sequence Length: 222
Sequence Mass (Da): 24... |
A0A2P0QI19 | MHASDLPSICVPLIGLIFPAIVMAYSFIFIENSSIN | Function: May help in the organization of the PsaL subunit.
Subcellular Location: Membrane
Sequence Length: 36
Sequence Mass (Da): 3925
Location Topology: Single-pass membrane protein
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A0A2H0SR05 | MIIGLIDSGIGGFSILRATQKALPHHMYVYLADQANFPYSQRSTKNLIELAKEHARVLIEKHNCSLIVLACNTLSVAALAAVRTAFPDTRFIGTVPPVNVAAKSLGNDANILVLSSERTAKSEYLQQLLENLSGPNWEILGSTDLVEAIEAGDAAKVKQVLTAIRDSYPKITFSGIVLGCTHFPLVANEMQETWPDAELFSPSDGVVKQLKQISPVEPTEQLSSTPLFLTTPDYSSSLQLEKRYHATL | 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: 248
Sequence Mass (Da): 27050
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A0A7S1T7A7 | AGMWITKWHGFEQHGVYGPSVPPAELVSPSTSQTFHVHGALRMESTAAVAYTGTLAALCIATGVLYSRVYASDPGWVTDDVAPHESGSQKTAPPCQYCGVRPPLRSRHCLNTGQCVRKFDHYCHLLSTAVGDLNHADFFLFILCELTLSSETLARPR | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 157
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 17117
Location Topology: Multi-pass membrane protein
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A0A087TUN9 | MKRIAVIGAGSAGLAAAKACKEEGLNFVIFERSGRVAGLWNYRDEDIDGLACVMKTTVINSSKEMSAFSDFPPPKDFPNYMHNRMMCKYFHMYAEKFGLLDKIRYYQEVTKVEQAPDYEETGRWILKAENTNDKTITEETFDGVMICTGHHGYPHIPKFPGQEDFKGKIIHTHSLRVPDAFKDQRVMIVGVGNSGLDAAVDISNVAKQVYLSTRRGTWIMFRLGSYGLPADTQFLTRSFDFIKSVCGMSVANSYVERYLDSKFNHEIYNLRPKHRYFAQHLAINDHLPNKILSGTIVVKGDVDRFSEKGVIFKGEENVTK... | Catalytic Activity: (2E)-geranial + H(+) + NADPH + O2 = (1E)-2,6-dimethylhepta-1,5-dien-1-yl formate + H2O + NADP(+)
EC: 1.14.13.8
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 531
Sequence Mass (Da): 60780
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A0A1D2YTS2 | MGKHLLGCQDLSIEEIKSILNKAQYFLENNDNLFSYREAYRDKFVVNLFLEPSTRTRFSFEVAEKKLGIQVLNFESNISSLQKGESLYDTLKTFEAQGMDIVVIRLREEGILQHFSRRLNLSIINAGEGKKAHPTQALLDLFTIKQYFNDLKGLNVAIIGDIAHSRVARSNYYLLKKFGANIFFSGPPNLMAPDLENNYLPIDEAIRRADVVMMLRIQAERHSDNKIKSKEAIVEYNRKFGFTEERLQYLQSHAIILHPAPVNRGVEMDDIVVDHQQSKIFEQIHNGVWVRMAILDRALGVN | Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 2/3.
EC: 2.1.3.2
Catalytic Activity: carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-aspartate + phosphate
Sequence Length: 302
Sequence Mass (Da): 34716
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A0A959ME53 | MLYIEVGNSTLKLAHRNSDGTFRVSRFTHPTHLLEEIPPKAEMLLAPVAESQVGNILPQLKERGTVRLLGRDQFREFLADSYDTPETLGLDRILQLFALDVDAIVISCGTAITIDALFRGSPFWGAILPGFTTASRGLSAQAPALPVVSSNDTVLLPARSSRTSIANGILLGTTLALQGLADMLADEIGASQSLPVIVTGGEAEVLRSFWRREREVTVRPALLFEGMARKGAKAQRDKEEGGSILPR | Cofactor: A monovalent cation. Ammonium or potassium.
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5.
Function: Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
EC: 2.7.1.33
Subcellular Location: Cytoplasm
Catalytic Activity: (R)-pant... |
A0A933CZX2 | GVPGTVAGLLAALDSYGTMTRDDVLSNPIELAERGFHIGDALAASLLEYHSELTFFPSTSRVFTNNGEPYRAGELFKQPALARTLQAIRANGMKGFYGGEVADLIVAEMKRSGGLITEDDLLLYTTVERRPVAGTYRGFEIISAPPPSAGGMVLIEMLNLLEPFDLRRTRAGSYQTLHLLVAAAQRAYADRAKFPADPDFVNVPIETLISKRHALDRQPPIDPRFATSSARISYGTIDVDHDETTHYCVADSFGNVVSATVTLNSLYGCKLTVDGAGFLLNNEMGDFVIKPGESNQFGLVGGEANTIAPHKRMLSSMTPT... | PTM: Cleaved by autocatalysis into a large and a small subunit.
Pathway: Sulfur metabolism; glutathione metabolism.
EC: 2.3.2.2
Catalytic Activity: an S-substituted glutathione + H2O = an S-substituted L-cysteinylglycine + L-glutamate
Sequence Length: 435
Sequence Mass (Da): 46987
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A0A2G6EC48 | MIKVFNIKSIILNYKIIIITFYFLVSCSSSRDYSEYNSVKGKFIESGVASWYGPNFDGMKTANGETFDMQDMTAAHRTLPFGSLIKVVDSDTKKYIIVRINDRGPYAKQRIIDLSKRAAEKLGIIRKGTANVNLYLLNQKVLPSNLKTPHYTVQIGSFFKKDDAINLSKNFNNSFIIQATISKKIYYRVYVGRFDTKQEANLIKRKLSDKGYKGFVKQFEN | 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: 221
Sequence Mass (Da): 25338
Location Topology: Lipid-anchor
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A0A7S1X9S8 | MDGARVRELVGWPRPLPLEDERARLLREVGQVLCDHFDGDVTALISAANGSAVRLVGLVTQHFPGFRDHAIYRGQQVFLYKRAQIWVGDLWGAFGGQGL | Function: Catalyzes the hydrolysis of queuosine 5'-phosphate, releasing the nucleobase queuine (q). Is required for salvage of queuine from exogenous queuosine (Q) that is imported and then converted to queuosine 5'-phosphate intracellularly.
EC: 3.2.2.-
Catalytic Activity: H2O + queuosine 5'-phosphate = D-ribose 5-pho... |
K0KKU6 | MLKQEQLSTSPISYHDHAGHDHHHSHSHGDFDHEESPFTLNKESNLKDYLYNNRLWAEKMNETKPGLFESNGKGQNPHTLWIGCSDSRYNETVLNISPGEVFTFKNIANMISIDDLTTVSTLEFSINVLKVKKIIICGHTDCGGIWNSLSYNDLGPTNSNLQNYLKQIDELRDLKINELNEISNLKLRAKKLAEFNVLKQLDILKRQKPVINAVAKGELEIWGLMYNVDSGFLEVIEQ | Function: Reversible hydration of carbon dioxide.
EC: 4.2.1.1
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Length: 238
Sequence Mass (Da): 27166
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A0A959RPT9 | IRNKFDDYVLENLERTYKLVENNKMQIGFGISSGDDVKRFSSFCDGVIVGSAVIKSLANDDSNFTNTIKLVKELKSACKN | Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5.
EC: 4.2.1.20
Catalytic Activity: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan
Sequence Length: 80
Sequence Mass (Da): 8953
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A0A975FZB9 | MFVTTWLSVLISTYTKGVVPIWPANAVVLAAMLARPEGQWAPLLAFGFVGGLLGNLAGGNPTALSVILSASNAIEVSICSFGLRFVLKGPPDFSKRRDLVTFVLLCSAAAITSALTTSRFFEGYRGRESLRDILMWTLSDGLGLLIVTPALISFTGPKLRAALGGAGKWRAAAMLAAFAATDCMAFLQTRYSVLFVVSAAMLVLVFELETVGAAAGLVLTALIGEGLSVFGFGPTPLVGQTAHESELSLQIFLGVSAVLNLSVGAALARSRRLQADLAESEARYRLLTDKAVDITLRYDPDWIIEFVSPAVRRLGYEPAA... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 929
Sequence Mass (Da): 99190
Location Topology: Multi-pass membrane protein
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A0A5B9P3V3 | MLTTATTVNTDSRTRFFDTCWTPKIGLSHPDLYGDEESAPVGSDQAVEIQPLSVTHSCVNFKQPTRFFPGLRGNLNSKRPERRFRASKAHKLLTRSVSCLIKDGITPIFDRNLCLNTTALKIEIADQQQLKVNFDPLIKIASAILDDHGVSKGELSIALVDDPTIRELNNQYLQHDWETDVISFVLDEGEGWLAGQLIVSTDTAMRIAKEVGSTVEAELALYVAHGTLHLVGFDDLDENSAIEMKAAEKEYLQLFSIECINREA | Cofactor: Binds 1 zinc ion.
Function: Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.
EC: 3.1.-.-
Subcellular Location: Cytoplasm
Sequence Length: 264
Sequence Mass (Da): 29391
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A0A8R1IEC2 | MDAWPAKKNKISSAPFLWDYSPAIPIIAAVISLSVISNFLATSFTDPGILPRAENIEVIELDRQIAEEHNPHHDPAVPRPRFREATINGERVKMKYCTTCRFYRPPRCSHCAVCDNCVLMFDHHCPWVGNCIGQRNYCYFYRFVFCLSVLILYLFSCSVAHICLLSQNMPFGDVMRKTPGSAVVIIICFFTIWSIFGLSCFHTYLLCSDLTTNEDLKGIYRKKRRAAVQTSTSSAPDWHNQEPKNPFYSGSLKSFTGRLFKSRLPSVLDANGYINDQPTIVIQVPKFPPETR | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 292
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 33248
Location Topology: Multi-pass membrane protein
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A0A8R1EPF0 | XYFFFFLCSLSIHMLYVFGLCFVFVWTGTDSNARNNVISPPYLCAIVLLALCAVLCVPVIGLTVFHLVLVARGRTTNEQVTGKFTSGYNPFTIGCWGNCKRTLCHSQIPP | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 110
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 12227
Location Topology: Multi-pass membrane protein
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A0A933YME3 | MKLQPIAHRSYDIAIERGALAAFVKRIKTTSSDLFIITDSNVERLHGRRVHQLLFDAGVESMLLSFPAGEGSKNMRVVNALQTQLLRHGIRRDSLVIALGGGVVGDVAGFVASTILRGVQFIQLPTTLLSQVDSSVGGKVGVDHPLGKNLIGAFHQPAAVFIDPGFLITLPVREFRNGLAEVVKIAAALDRSLFAFLERNAGSLRKNNARLLTEVIKRSVRLKARVVERDEFDKDLRKTLNLGHTFGHALESALNFRIRHGEAVAIGLVAEAAIAVRLGLLLKRDFDRLVNVLKVLGLPTTIPSLTSRKKFFAALYADKK... | Cofactor: Binds 1 divalent metal cation per subunit. Can use either Co(2+) or Zn(2+).
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7.
Function: Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP)... |
K0KP51 | MVADESAKKSDSHPDELVPDHEPSSPTRELPELTFSNVIADILYGFKQLIFNPEFTKIVIPILLVVESIAVKLIKGFISYTEIDYTAYMEQVTIINSGELNYANIFGGTGPLVYPAGHVWIYRFLSWLTYGTKNIEVGQTFFGWLYVITLALVFLVYLRLNVPPWTVHLLTLSKRLHSIYVLRLFNDCFTTFFMVVTVLTLQQASVWKTSRPRLSKLLSNQIAGILFGIAISIKMNALLYLPGFGIAVYFLNNEVILRALVPLVVVVLTQAVISWQFLFSGAEIRDSYLANAFDFKRRFLYKWTVNWRFLSADIFNSTKF... | Pathway: Protein modification; protein glycosylation.
Function: Adds the first Dol-P-Man derived mannose in an alpha-1,3 linkage to Man(5)GlcNAc(2)-PP-Dol.
Catalytic Activity: a dolichyl beta-D-mannosyl phosphate + alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-Gl... |
A0A4Y7RKA4 | MLFNLDSAASGTKRNKLLRLLKRYRYYLTILFSICCFILLCIFIILSPVSSKSRARDVVVTVPVQASANQVGRILKQSELVRSSLIFSLYARWTGMDSLIKAGEYRISNSLSTPEVLKELVDGRYAAHEFTVPEGFTTAQVADLLVSKGLVDRDKFFAAVANEDFPYDFIQSLPKGDKRLEGYLFPDTYQVMRGSSEKSIIEMMLQRFEKEMKDLDYLNQAKAGHVSLHEAVTVASLIEREARIDEERPLIAGVIYNRLNRQIQLQLCATVEYALGTYKPKLYYKDLEIDSPYNTYRIMGLPPGPIAMPGRNSLLAAVRP... | Function: Functions as a peptidoglycan terminase that cleaves nascent peptidoglycan strands endolytically to terminate their elongation.
EC: 4.2.2.-
Subcellular Location: Cell membrane
Sequence Length: 356
Sequence Mass (Da): 40302
Location Topology: Single-pass membrane protein
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W5PCF2 | SPQPLMEPHNHSSLSEFVLLGFPRVGHIRGWIFVLLLLAYLFTICGNMLIFLVIRLDAALHTPMYHFVSILSFLELWYTATTIPKMLANLLSDKKTISFSGCLLQTYFFHSLGASECYLLTAMAYDRYLAICRPLHYPAVMTPMLCAKMAAGCWTCGFLCPISEVILVSKLKESYSLTLDRTLAVVYSVLTPLVNPIIYSLRNKELIKAIKRTIFRKGERASPT | Function: Putative odorant or sperm cell receptor.
Subcellular Location: Membrane
Sequence Length: 224
Sequence Mass (Da): 25320
Location Topology: Multi-pass membrane protein
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W5PXK2 | MTAIIKEIVSRNKRRYQEDGFDLDLTYIYPNIIAMGFPAERLEGVYRNNIDDVVRFLDSKHKNHYKIYNLCAERHYDTAKFNCRVAQYPFEDHNPPQLELIKPFCEDLDQWLSEDDNHVAAIHCKAGKGRTGVMICAYLLHRGKFLKAQEALDFYGEVRTRDKKGVTIPSQRRYVYYYSYLLKNHLDYRPVALLFHKMMFETIPMFSGGTCNPQFVVCQLKVKIYSSNSGPTRREDKFMYFEFPQPLPVCGDIKVEFFHKQNKMLKKDKMFHFWVNTFFIPGPEETSEKVENGSLCDQEIDSICSIERADNDKEYLVLTL... | Function: Acts as a dual-specificity protein phosphatase, dephosphorylating tyrosine-, serine- and threonine-phosphorylated proteins. Also acts as a lipid phosphatase, removing the phosphate in the D3 position of the inositol ring from phosphatidylinositol 3,4,5-trisphosphate, phosphatidylinositol 3,4-diphosphate, phos... |
A0A2G9PML4 | MTLNLCSDIYLYGLSLLLAMAELLELDGSHGEGGGQILRSALALSAFTGKPFRITNIRKGRCTSGLKNQHLHCIKALEMMCDAKVEGAEPGSSEVTFYPGKMKGGRYDIDVGTAGSVTLLLQSLLVPSINASSKVRLNITGGTDVKWSMPFDYLKEIVVPHLRRFMDISLKLKKRGYYPEGGGGIEIIMKAKPVHQKIHLLDRGKLVKIVGVSHASCILMPAEVAERQAKSAGFHLGRLGCPVEIRNEYSETDGPGSGVMLWAVFSDGDSVSPYRIGADSLGAKGKRAEDVGEEAAFRLIKQLESDAPIDENLADNLVPF... | Function: Catalyzes the conversion of 3'-phosphate to a 2',3'-cyclic phosphodiester at the end of RNA. The mechanism of action of the enzyme occurs in 3 steps: (A) adenylation of the enzyme by ATP; (B) transfer of adenylate to an RNA-N3'P to produce RNA-N3'PP5'A; (C) and attack of the adjacent 2'-hydroxyl on the 3'-pho... |
W5PML0 | MENSTEVTGFILGLSSAPELRSPLCITFTLTDLVTLVGNLGMVTLILLDSRLHTPMYFFLSNLSLVDFGYSSAVTPKATAGVLIGDKFISYNACPAQMLFFVAFATVENYLLASMAYDRYAAVCRPLHYTTTMVASVSAHLAIGSYICGFLNACFHVGDVFSLPFCKSITVLHGCCETEYLLSCRLTRMPHLPVILASQKFHAYFTRMCTQVNFTFKCITLFNFHNNTKNRVISSLVSISSHFISLLSLSLFSLSFPHSYYNMITFYIYSIFIALYFYQYNPLSAINTQSEKETKKSWKSNKLIFRNIFQVSKIKLNRPT... | Function: Putative odorant or sperm cell receptor.
Subcellular Location: Membrane
Sequence Length: 477
Sequence Mass (Da): 53459
Location Topology: Multi-pass membrane protein
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A0A078KB65 | MFYKLPKLSYAYDALEPYFDKKTMQIHHTKHHNTYITNANLALSKIPEVMQNMSVEMLLTNLNKVPEKQRYILRNNAGGHANHSLFWRILTPNANNPHGAIKCAIESNFINLENFRNQFDNYAKLHFGSGWIWLIINKYGKLLIKSTFNQDNPLAPKYLGGFESTPLLCIDVWEHAYYLKYQNRRVDYINAFWNLINWDFIENLYTTTLSKISR | Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
EC: 1.15.1.1
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Length: 214
Sequence Mass (Da): 25241
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A0A3N5R106 | MSLYLMIDLGAVLVPFLFSFHPQIAFYKQWRYALPAILLTAIPYLIWDQWFTAEGIWGFNPTYHSSLLIGDMPIEEILFFICIPYACLFTYWSFRQLAPLTLPKRALTPLYAGLFLIFGLMSTLGHGLWYTFVDGLFAGAILLTTWFIQRDLLLRFFPVYLIVLVPFFIVNGLLTGMAIPEPIVWYNDAENLGIRTVTIPIEDFAYAFSMLLMSTLLFEVLRKRSER | Pathway: Carotenoid biosynthesis.
Subcellular Location: Membrane
Sequence Length: 227
Sequence Mass (Da): 26281
Location Topology: Multi-pass membrane protein
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A0A5N0TA42 | MTHGQDTAAKGAPGGAPFLLVFIYRVYAWLIFFPVVAIWSFLCGWMAVLAAVVISPSFGSRVVGGTWARVIGWLTPIRVRVEGREHIDPDQTYVVVCNHVSQYDIISVYGWLPLDLRWVMKQELRKLPGIGIACEKVGHIIVDRSNPEAAKRSITDALERIGDGVGILFFPEGTRSLDGRLRPFKSGAFRLAEEQGLPILPVSIVGTREVLPAKTFKLLPGKVRLVVHPPIAPGDRSATELKSLSRDAVASGLEALPRQG | EC: 2.3.1.51
Catalytic Activity: a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphate + CoA
Sequence Length: 260
Domain: The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate.
Sequence Mass (Da):... |
A0A3R7R9P0 | MKFLVSDSTGKKAQIIASIALFFFLVLVLFYFFFFTLQFNLCIKSIHIISIISWMAGLLYMPRIFLYHSLASPETDQYKTFEIMEERLFKVIMNPAMILSWICGLYLIWTVPYTQIGWFRIKMIFTLFLSSYHVYLAFLIRDFKNKKSRYSPKYFKIINEIPTVIMIVIVFLSIMKPF | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; protoporphyrin-IX from protoporphyrinogen-IX: step 1/1.
Function: Catalyzes the oxidation of protoporphyrinogen IX to protoporphyrin IX.
EC: 1.3.99.-
Subcellular Lo... |
A0A8J7E8D1 | MLALFDRLKLFCLALGCLALGGLTLISASPAYADALSTQADLINNSGTTIGTVRVEQGHKGVLVNLQAKDLPPGYHGMHFHAVGDCSDLEAFKSAGGHVNPFDMPHGFRNPDGPHEGNLPNLVVAADGTVDVELYSDLVQLDAGAAKLLDADGTALIIHTDQDDHYSQPIGGSGGRIACAVIK | Cofactor: Binds 1 copper ion per subunit.
Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
EC: 1.15.1.1
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Length: 183
Sequence Mass (Da): 19054
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A0A2I1GFA6 | MFGILAPHLKEFTDDLSDEIKYQKIKHGVKDVKEFLEKLANRGKVDPLSNDFAKYLDENDKLKYLRYEFTIPKARDIVSDGVEALSPEDDSVYFCGNSLGLMPRRTRDLVNQELDVWASSGVVGHFKHKHKRPWISIEDNVIDKMAEIVGAKPIEVAVMNTLTSNLHLLMASFYTPTTKKNRKKILIEPMAFPSDLYAVESQIRFHGLDPAKELIKVTPPEGENVVPLDNILKIIEKEGHTISLVLFSGVHYYTGQFFKIKKITEAAQKKGCIVGLDLSHAVGNVVLKLHKWGVDFAAWCSYKYLNSGPGGIAGIFLHER... | Pathway: Amino-acid degradation; L-kynurenine degradation; L-alanine and anthranilate from L-kynurenine: step 1/1.
Function: Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3-hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3-hydroxyanthranilic acid (3-OHAA), respectively.
Catalytic Activity: 3-hydroxy-... |
A0A1X2HII2 | MVYAVCYYPKSRHEEFKALGFDDSKKLTDEKREALAKVIESNLDWVGWVVNVLAPQDISRHMLRRPAYNLNEQAHDATIALISQVLDNKFNVTDIYVDPVGPSQSYKQKLTRYFPGIAITIEPHADALYPSVSAASICAKVTRDQILRHWIWLEPGLEGTLSKEFGSGYPSDPNTVRWLDKHMDPSFGYPSIVRFSWGTIAKRVDSIEWSEDEDEKEEKEKKKNKRKQQQQQQQQQTAEERSPPSPAHSRGRIYKAICLESVNVGK | 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: 266
Sequence Mass (Da): 30494
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A0A7S5L1V1 | MIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWKVYPPLWGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTTINMKPPAISQYQTPLFVWSVLVTAVLLLLSLPVLAAGIT | 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-cytoc... |
A0A5B9P1W7 | MRSQTPQLIVIMGVCGCGKSSVGEALSLRTGISYHDGDDFHSDANRNKMSQGIPLTDEDRQPWLESIVAFAQQQCEQGRSLVVACSALKKAYRDTLRTLDAPVKFVHLTGSKATIASRLADRKGHYMPETMLQSQLDTIESPTGENGAVEVSIEQTVDQIVSQAMELLDLTTEG | Pathway: Carbohydrate acid metabolism.
EC: 2.7.1.12
Catalytic Activity: ATP + D-gluconate = 6-phospho-D-gluconate + ADP + H(+)
Sequence Length: 174
Sequence Mass (Da): 18970
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B9T5P6 | MGFLKFFSIFSSDNHSHHNSSHSNNSALPSHALLLREDLVKSPENFITSNGFSVFNYLRRLLSGKKIHGGARTDEEEKVYSWLYALAQSDKDLVYEYVRSTERDAPLVKVSLFSDEVCHSSISCCKGLSFSEAERRLKENGPNVPLEYHFPSWWHLLWTAFFHPFNIILIVLSALSYITSDSPNGCILLILVFISVSLRFYQENSSSKAAMKLYEFVKCPVKVQRCAGRVVQTELVVQVDQRDIVPGDIVIFEPGDLFPGDVRLLSSKQLVVSQSSLTGESWTTEKTANTKENASTPLLELKNICFMGTNVVSGSGTGLV... | Function: Mediates magnesium influx to the cytosol.
Catalytic Activity: ATP + H2O + Mg(2+)(out) = ADP + H(+) + Mg(2+)(in) + phosphate
EC: 7.2.2.14
Subcellular Location: Cell inner membrane
Sequence Length: 863
Sequence Mass (Da): 95864
Location Topology: Multi-pass membrane protein
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J2GFS8 | MRFIAKFILWFVAISVAVTVLYRFVPPPVTVTMLIDGNGITKDWEPLSNIDRSMVAAVVAAEDGKFCSHNGFDTDAIEKAMERNAKGGRIRGGSTISQQTAKNVFLWQGDGWTRYARKGLEVWFTFLIENLWDKRRIMEVYLNVAETGIGTYGVEAGAQRYFGKSAAHLTPAEAGRMAAALPSPKKRSVKNPAGFTRRYGNTIAARIGTVKREGYDACVYE | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Peptidoglycan polymerase that catalyzes glycan chain elongation from lipid-linked precursors.
Catalytic Activity: [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-(1->4)-Mur2... |
W5NQN4 | MGDWGFLEKLLDQVQEHSTVVGKIWLTVLFIFRILILGLAGESVWGDEQSDFECNTAQPGCTNVCYDQAFPISHIRYWVLQFLFVSTPTRHLPVAARGAPSAEGGGAPGAASLGTYVASVLCKSVLEAGFLYGQWRLYGWTMEPVFVCQRSPCPYLVDCFVSRPTEKTIFIIFMLVVGLISLVLNLLELAYLLCRCLSRGVRARQRQDAPPAPGTSSEPYADQVFFYLPMGEGPSSPPCPTYNGLSSSEQNWANLTTEERLASSRAPLFLDPPPQTGQKSPSRPSSSASKKQYV | Function: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell.
Subcellular Location: Cell junction
Sequence Length: 294
Sequence Mass (Da): 32345
Location Topology: Multi-pass membrane prot... |
Q9TTP5 | DPVMGDQRNGEGAMYVPDDLLPVYREKVVPVADIITPNQFEAELLTGRKIHSQEKALEVMDMLHSMGPDTVVITSSDLLSKGSDYLMALGSQRTRAPDGSVVTQHIRMEMHKVDAVFVGTGDLFAAMLLAWTHKHPNNLKVACEKT | Pathway: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal 5'-phosphate from pyridoxal: step 1/1.
EC: 2.7.1.35
Catalytic Activity: ATP + pyridoxal = ADP + H(+) + pyridoxal 5'-phosphate
Sequence Length: 146
Sequence Mass (Da): 16088
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A0A2Z2NMW1 | MSPFLVSFKLALWTMLLLLPIGLLLGRWLAFTRVRSKPWIEAILFLPLVLPPTVIGYYLLVLFSPETISGAAAVKLFGAPLVFTFPGLVVASIVVNLPFAVQPIQLAYSTLPLEVREAAWVSGLSPSRTWWHIELPLTWQGMLASGTLVFAHTLGEFGVVLLVGGNIDGVTRTVSIAIYDSVQAFDMQTAGWYSLILVAFSLLALLVVRKSSPTP | Function: Part of the binding-protein-dependent transport system for molybdenum; probably responsible for the translocation of the substrate across the membrane.
Subcellular Location: Cell inner membrane
Sequence Length: 215
Sequence Mass (Da): 23437
Location Topology: Multi-pass membrane protein
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A0A2Z2P347 | MKLPPRPICDADPSALSIEQALERIQNGLPRITETEDIDCSNALGRICAQDVISPMSVPSFRASAMDGYAVRAADCENPLRLEGRSIAGHPGTDHMPAQSCQRITTGARVPDDADAVVQQENVERCDDMIVVKVAPHAGLHVRNPGTDSQEGDILLSKGSRIGPSELALLAAHGITHLVVFRVLRIALLSTGDELREPGNLLEPGQIYDANRPLLQAMLASSAVELIDLGICKDSEEALEETLNAASEVDIIISSGGVSVGDADHVRSVLERTGQVDLWKIAMKPGRPLTFGFSRPGQCYFGLPGNPVSAAITALIFVNP... | Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
Function: Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP.
EC: 2.10.1.1
Catalytic Activity: adenylyl-molybdopterin + H(+) + molybdate = AMP + H2O + Mo-molybdopterin
Sequence Length: 417
Sequence Mass (Da):... |
A0A952ILJ0 | MTFTPIITRFSLDSLFPDHGKRTLVMGILNITPDSFSDGGMLYKSENMQAAVETAGKLLSAGADILDVGGESTRPGAVEISVEKECGRILPVIQMLAKNYPDATISVDTRKALVATRAIKAGAHLINDVSGLQFDPTMAQVAAETGAGLVIMHSQGTPQTMQVNPTYDNVVAEVMTFFEHQVSVAQKAGVDSAQMILDPGFGFGKTLDHNLTLLKGLREIKTLGFPVLVGTSRKSFLTLPLPKAKGSNLPASDEREALTAATLAIAVEQGVDLLRVHDVETQGPVVQFLDRLYR | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2.
Function: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7... |
A0A9D1LBI8 | MRVFSNCHTHTIFSDGRATAEEMVLAALERGMRSLGFSDHSVQTFDQYYTMSLESERESFLEIQRLRDQYGEKIRIWHGVEQDTHGIVRREEYDYILLAQHYVEKGEMRCPVDSRPRREELFQFRDSVYGGDGAQMAADYFFLAGEAARVFRPDIFAHFDVIRVFNREGELYDARDARVLQAEEEALKKIAASGAMLELNTGGMARGYLSEPYPEWDFLPLWKEMGGRLIFGSDSHVPQFLQYDFDRCAMRLREMGFRSVWELGGLGEALFVEREL | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 8/9.
EC: 3.1.3.15
Catalytic Activity: H2O + L-histidinol phosphate = L-histidinol + phosphate
Sequence Length: 276
Sequence Mass (Da): 32095
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A0A445MXG0 | MSIYFPKALQENFRTKIFFIFTFFFFVMSLSLISYFIHNQITTTNTALIEKGAFLAKILARNSRIGVFSENERLLVNAVEAAFEQEEVMEVSVFNHEGNLLKKQERSTAQSSRVSSIFNSDPVEIMSKQDFPYYREVNSQLEFWEPVISGSTVNSEEPILFGENQTNNQNRIIGLIRITLDKKPLNTKVQQVLIRSVSLGVLFLITGAFIVYLVAKGVTKPLKRLTASVKALETGDVVKKIPVKILDEIGRLALAFNHMSESLQTRTKALEESEKKYRSILQNIEEGYYECDPSGTFMFINDSMAKILDYPKDEVLGTNY... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Cell inner membrane
Sequence Length: 786
Sequence Mass (Da): 87763
Location Topology: Multi-pass membrane protein
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A1K1V4 | MDSSRQREAFSTDVLQAAPYPVAIIGAGALGLSLASRLIRSGPVALVASNADAAQRLRAGVRVGAVVERFDGFAAPRLPRADWVVVVVKAGGTRDALRSALAMRPRGVLSLQNGLLDLEPAGTGTCVAQGVTTMGAFRTDEGVMPVSDGETLMPQGFEPLAALFQQAGLPARIEVAMQAARLAKLLVNVVLNPLTAVFRVRTGELLAAPYMNHVEALVAEAWPVLRAAGLMLEFDEARAKVWSVVRSTADNRTSMLQDVLAGRRTEREAITGAFLRLADGNGAAVPTHRALHTLLGQIDADRC | Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 2/2.
Function: Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid.
EC: 1.1.1.169
Catalytic Activity: (R)-pantoate + NADP(+) = 2-dehydropantoate + H(+) + NADPH
Sequence Length: 303
Sequen... |
A0A448UW27 | MPVPHYSSSAMDGYAVAGAPPWRLVSPDYPEDARTNVHRLAVPIAAGEATPILTGGLLPEGTEAIVREEHSHRYEGAGALGSGIHYLDMAEGYTVPKPGTDIRYAGAELSPGAILSSRGDLITAQRAAFLGVNGFDELPVLKNVPVRCAFTGNEVITFGMPSPGQVRDAFGGFLEVSLAAAGCEVRPSARLADIAEEFHTFVTTSTARILIFTGGSSTSGVDMVRQTLTDIGAEYIFESVRVRPGHPALAAKIPAPTEGMNAGQERLVLGLPGNPLAAYTALYSYLPVILAGLRDLPIPALDRAELATDIPPLRKRSQHR... | Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
Function: Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP.
EC: 2.10.1.1
Catalytic Activity: adenylyl-molybdopterin + H(+) + molybdate = AMP + H2O + Mo-molybdopterin
Sequence Length: 371
Sequence Mass (Da):... |
K0KMT5 | MSEPEVKIKEENERIPAAFELTKYVDDDVKDEQAPKNFGGPLPTFKWLCENLFDKLDKTINHTNYYSAGGATVTDQKQRIVEHFFREWRSTVGPNIYPALCLILPHKDRTRIYNIKDQVLGRRILEILKIPKNSETTSKIMNWKRSRSAKAARMSDICIEVIQARRTDKKGGELSIGDVNDILDEMSKDEFKKEQQNKMLIELLDKMCFLELRYFFDILLKKNVVKNMENRILNTWHPDAQQYLSVVTSLKTVAYKLYDPNERLNKTDLSINLSKPFAPQLALKPNLSYSRVVQKLENDFFIEEKMDGERIQMHYDNYGK... | 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: 950
Sequence Mass (Da): 111063
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A0A562J657 | MLKININLLFTIINLLVLYFLMKKFLFNPINNILDKRKSLLEQQYAEANLTKDNALKLKIEYEDALKTTNDLSKQIIDETKAQAKIEYDNIIRSANEEAGKIIANAHKNIESQHSKELLKMKTEIANLAMDTATKIIGANVTPQSNKIIYERFLTEAGELDGTKDSR | Function: Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).
Subcellular Location: Cell membrane
Sequence Length: 167
Sequence Mass (Da): 19043
Location Topology: Single-pass membrane protein
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G0WXZ9 | GVKEYKLNYYTPEYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYHIEPVPGEETQFIAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALAALRLEDLRIPPAYTKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEAIYKSQAETREIKGHYLNATAG | Cofactor: Binds 1 Mg(2+) ion per subunit.
Catalytic Activity: 2 (2R)-3-phosphoglycerate + 2 H(+) = CO2 + D-ribulose 1,5-bisphosphate + H2O
EC: 4.1.1.39
Subcellular Location: Plastid
Sequence Length: 230
Sequence Mass (Da): 25757
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A0A0R2V8G6 | MIQLALEKNQLEEVTRDVYLLKGATDGSRDFKLMLKSPIIHADKKMAIIKAVFDDQVGVIMRSFLDILVRKGREGWLPEALNAYVEMYNQHQGITPVVLTTAYPVSDEIRDMLMDKLRGQANLEEIEVVTKVDESLIGGYILRYEDKMIDTSIARGLAILKDDFDNNDYIRKF | 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 c... |
A0A975ISU6 | MTDWTPQPVDDDPPPPGPRPAAPQPRSFGGRGGPPKPKRKIAWGLLGVVAVAVLLILGAFAAAETWVVRELLPGIPEIPDRSALMAVNQTPGMTFEDANGAVIARRGARHGHAVTLAELPPYVPRAFLAVEDKRFYSHGPVDLRGVIRAAWINWRAHRTVQGGSTLTQQLAKTLFLTPDQTLKRKLQEAVIANRLEQLMTKDQVLELYLNRIFFGDNSYGLDAAAQTYFGKPASALSLQEAALLAALPKAPTRLALTNDMPAALARSHIVLDHMRDEGWITVAQEQVALNRPPRLAPEQPGEGDYGYVLDMAAAQAVQIT... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
EC: 2.4.1.129
Catalytic Activity: [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate = [... |
A0A3N5L2V3 | MRVSQSKIDEIASAVDIVEIISQYTNLRKAGRSFMGRCPFHEEKTPSFSVSQEKGVYHCFGCGKSGNVFTFIMDMDNVTFSDAIKTLAEKANIPLEFYDEPEDDRNQIESLYEIHKQAARYYYDTLMSHDGIYAREYLEIRGIKPDMLPKFGLGFSLRYKDSFYQKFKDNFSVEDLNASGLVYGEDPKDKFRGRLMFPIISESGRVVAFGARKLFDDDYVQAKYVNSPETKIYNKSKTLYGLSFAKNSIKEKGYVILVEGYLDLISLVQNGILNVAASSGTSLTNLHVRILSRYTNEIVIVYDADKAGQLAARRAIELIL... | Cofactor: Binds 1 zinc ion per monomer.
Function: RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.
EC: 2.7.7.101
Catalytic Activity: ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.
Sequence Length: 602
Domain: Contains an N-termi... |
A0A3N5LB98 | MAKFLPSNPRLRSLILCTISGALLALSFPPFKTWFFSYFGLAIMLYLIFNSLKFRQVFARGYVLLFVFNAISLYWIAGWESDDIFLKIGGVATVIVHPLFMIIPVLLTYLIYKTAGRIYAMFLFPLLWTGFEHWHNLTEFSYPWIELGNTEVYNLNRIQFAEYIGVHGITFLICVISVLIFLLASKIYKREWKLNSSNTIVTTTILILLILIPNITSGIILNSNSNNSYYSSPDSSKNIKAAIVQPNVDPFKKWASENKDAIVTKYINGLNAGLKYNPDLLVLHETAPPFNFLEDYNLNYASRFFDFVNLNKKYVVIGIP... | Pathway: Protein modification; lipoprotein biosynthesis (N-acyl transfer).
Function: Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation.
Catalytic Activity: a glycerophospholipid + N-terminal S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipopr... |
A0A445MRX2 | MLKCPELLIPTSLYLLIVLLLSPFPPCPVNAADSPSNSAIEPFTGNTMGTTYHIKVVTQNNDDKKLLSTLIEEKLKDVNQSMSVYVPDSEISLFNNAKKGKAIQISFEFYSVMVTSQKLYRITGGAWDGTVKPLVDLWGFGTKKEITTPPSSDVIRALLENTGFDQITIQNQTLQKHNSAITLDLGSIAKGFGVDAIGQLLKDQGYINFLVEIGGEVLASGEKTPGKPWIVGINKPDKWDNSNVAYLSFPLRDKALATSGDYKSFSMIEGEAYSHIINPATGYPVDNGVVSASVISDNCTFADGLATALMVMGQEKGIKL... | Cofactor: Magnesium. Can also use manganese.
EC: 2.7.1.180
Catalytic Activity: FAD + L-threonyl-[protein] = AMP + FMN-L-threonyl-[protein] + H(+)
Sequence Length: 351
Sequence Mass (Da): 38193
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A0A952IA56 | MGKLTVYRGGIYHALSPEHGEGWQDGALVVDASGTIVDCGLWQQVNQKIDLSGCEQVTLQPGQCILPGMFDLHTHLPQYQVTGCEAADLGQWLDAYILPEEARFEDTAYAAAMADVFFKQLLAKGTTTAAVFLTSHVEATTLAFETAARYGNRVVMGLNLMDRFGEGDGPEGLVRPVADLLRDTEDLYQTWHGANEGRLQYAWMPRYAASCSDPLLAGVGALYRKYPEAYCHTHISEQLGEIETVLRLFPQVETYTGVYEAAGLLGPKTLLAHGVHLSQQERARIREHQSTLVHCPSANFFLKSGRFPLKEMLADQVKLG... | Cofactor: Binds 1 zinc ion per subunit.
Pathway: Purine metabolism; guanine degradation; xanthine from guanine: step 1/1.
Function: Catalyzes the hydrolytic deamination of guanine, producing xanthine and ammonia.
EC: 3.5.4.3
Catalytic Activity: guanine + H(+) + H2O = NH4(+) + xanthine
Sequence Length: 443
Sequence Mass... |
A0A445MX67 | MVLSSVEQPSSVVIALSGGVDSSFSAFLLKSTGWQVYGLHFVLPAPEEIIYARKGAVKKFSAHLNIPLEFVDLLEAFNTQIIEPFCMSYVQGLTPNPCVICNPTIKFERLLWFAKEHGIHYLATGHYARLIRRQASGVTGLYRGKDITKDQSYFLHRLNQTYLSRAVFPLADMNKAEVSIRARDIGLPVEAIPESQDICFLPTGNYRTLVEEKLGPDIKRPGDIINAMGKVLGRHTGIYGYTIGQRHGLNISSTRPYYVKELRRETNQVVVGRKEDISSKVVFAHNFNWVEGMPAQREFPVQAQVRYRHRAAPGVLTVLS... | Function: Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34.
Catalytic Activity: AH2 + ATP + S-sulfanyl-L-cysteinyl-[protein] + uridine(34) in tRNA = 2-thiouridine(34) in tRNA + A + AMP + diphosphate + H(+) + L-cysteinyl-[protein]
EC: 2.8.1.13
Subcellular Lo... |
A0A0R2K2X8 | MTKIKICGLQTLADVKKCNAIEPDLVGFVFAKSPRQLNFRMAQALRNQLKSEIISVGVFVNTPIGKIQSLVQADIISQVQYYGKLTNEKINDLHQFDARVIQVVSNESEIKQAADAVMFDKSRGRGLIPDHFNVPQTTKSTYLSGGITTKNVVKAIQETHPDVVDVSSGSETNGEKDFTKMQRLTNLVHKFKEKNNEY | Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5.
EC: 5.3.1.24
Catalytic Activity: N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Sequence Length: 198
Sequence Mass (Da): 22128
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A0A1V5SH07 | MKIKPDSFVTFLLLLFSIIITFVLHSQTFTLLTTGEINQVLSPDPWYVVRQTELAAHSFPSYTWFDPFTSFPDGAIIFWGPFLPLVGGLITNILGFKNEPALILSISWIPVLTAMLTIPLTYWYGKEIRGRWCGVAAALLIAVIPGSYLIRSMYGYADHHIFESFFMLAYSLSFLVTFNRLYESEEEPEIKMAILGGGVTGLLLGLGMINAPTMVIAAAITSLFVIFAGYQLIKLTKNLLPFSIFICFSSCIGAILTLLFFTPDMTREVPFIFDPVSLALVLIIPALFSVFYLITQIIIQNADQSIKKPLLAIFVAGLTT... | Pathway: Protein modification; protein glycosylation.
Catalytic Activity: an archaeal dolichyl phosphooligosaccharide + [protein]-L-asparagine = an archaeal dolichyl phosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine.
EC: 2.4.99.21
Subcellular Locat... |
A0A2Z2NR99 | MNSILDHAEVNAIVEGRHPEPFAVLGQHPLADASAAALSGSSVIRTFQPHVQSVNVIDEQGKKSALTRVHPDGLFEHVFNTPAGPYRLELANEEQSWEVIDAYSMTSPMGEMDRYLLNEGTHQELYNVLGSNSMQFNGVAGVQFAVWAPNARRVSVVGDFNDWDGRRHVMRAHPGSGVWDIFIPGVGNGALYKFEIIANDGRMLPLKHDPYAPYFEQPPGNASIVFESQFIWSDDEYQEKKKGVDMRERPISIYEVHAGSWRLNMHGESLTYVEMAKTLLPYAIENGFTHIELMPITEHPFDGSWGYQPIGLFAPTSRFG... | Pathway: Glycan biosynthesis; glycogen biosynthesis.
Function: Catalyzes the formation of the alpha-1,6-glucosidic linkages in glycogen by scission of a 1,4-alpha-linked oligosaccharide from growing alpha-1,4-glucan chains and the subsequent attachment of the oligosaccharide to the alpha-1,6 position.
EC: 2.4.1.18
Cata... |
A0A914I7B7 | MFIRRIVKQNNVLISEDFDGTLLDSPKIVMLFSKIPPSFCTVLRAASTSSPARGPNVKTFEIYRYDPEKPEQKPFLQKYDVDLTQCGTMVLDALIKIKNEMDPTLTFRRSCREGICGSCAMNIGGENTLACICNINKDTKYSTKIYPLPHMYVVKDLVPDMTLFYEQYASVQPWLQKNRPTELGKIENFQSQAERDKLDGLYECILCACCSTSCPSYWWNSDKYLGPAALLQSYRWIVDSRDDKAKERLARLTDPFSVFKCHTILNCTKTCPKHLNPAKAIGEIKKLLTGIDTKPEPKQASNKNICSVRAVKDAQQLEGE... | Cofactor: Binds 1 [2Fe-2S] cluster.
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; fumarate from succinate (eukaryal route): step 1/1.
Function: Iron-sulfur protein (IP) subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible ... |
B3CV04 | MHAKNISGFDVNYLSDECNAKEYTVHELSLHIKSAIEYQFGVLKVRGEVSGLKIASSCHSYFNLKDDKAVLNCVCWKTTLNLVKIKVEDGIEVIATGRLTTYSGQSRYQLVVENICIAGLGSLMQIFFQRKEKLMKEGLFDNSRKKKLPAFPMVIGVITSISGAVIRDIAHRVNDRFPSKLLVWPVTVQGNNSANEVASAIQECNNMLTSNNDLAPEVIIIARGGGSVEDLWSFNEEIVVRAIASSVIPIVSAIGHEVDFTLADFAADLRAPTPSAAAEMVVPVLADIKMRLNNSMNQINHVTFNYLKCSVMSLNNCGNI... | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
EC: 3.1.11.6
Subcellular... |
A0A1G0CWY2 | MSLQQKIEQTIAVLQQAARDFAPVCFANSLGAEDMVLTDLIAKHQSDIEMFSLDTGRLPQETYDLMQTVRKRYSVPLKIYFPDSVLVEEYVAQNGVNGFYDSVELRKRCCYIRKVEPLKRALSGKRAWVTGMRRDQAVTRASLEVSSFDADHGLQKFNPLLDWTNAEVWEYIKQNDVPYNKLHDKFYPSIGCAPCTRPVTPGEDIRSGRWWWENPENKECGLHIA | Pathway: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate.
Function: Catalyzes the formation of sulfite from adenosine 5'-phosphosulfate (APS) using thioredoxin as an electron donor.
EC: 1.8.4.10
Catalytic Activity: [thioredoxin]-disulfide + AMP + 2 H(+) + sulfite = [thioredoxin]-dithiol + adenosi... |
A0A914HM35 | MHLLNIRLRPCPPPLDKFHCFHGGKCVVEFEGQRIMNNSIFCRCVHNFHGDRCQLSFDPHVFGYSQTNNGVEGGASSVIAVLLILMIVVFIWCLALHWRCPEDILLIDRVMTSENEGAVPTEEIKNLVKEPDEATNGFYFQQTMYRIRDPRKSVPFYTSVLGMRLLKQLDFPEAKFSLFFVGYKKSDEIPADETEQKKFALSTHSTIELTHNWECDPNFAGYHNGNSDPRGFGHIGIAVPDVYAACARFEQMGVKFVKKPDDGRMKGLAFILDPDGYWIEIFNPNSVLIDLVVPSENGCAIPVEEERQWQRTHMEMKMWR... | Pathway: Secondary metabolite metabolism; methylglyoxal degradation; (R)-lactate from methylglyoxal: step 1/2.
Function: Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione.
EC: 4.4.1.5
Catalytic Activity: (R)-S-lactoylglutathione = glutathione + methylglyoxal
S... |
A0A935THJ2 | MTERQNNILNFIKEFVDTNGFPPSYREIGNHFNISSTFGVKRHLDALVKKGYLNVFSNSNRSITLTEKSEILFNEKKENNSIKIPILGKVAAGYPVLSNQNYDGTLYVDTSLIKKGFNYFGLKVRGESMIDDGILEGDTVIVKAQSEASNNDIIIALVDNDTTVKRYFRKKDSIELIPANKNFETIVVKNNNEFSILGKVVAVFRIYN | Function: Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually ... |
A0A0B2UXA2 | MWRRTPYQMLEQAQTALSAKQRNTSGWYFHKRKASFGMGWSLKSASVLAVSLSSLDLALTCMAICWHAKWPSTRAFTEQFTNYSFLSSTADFFAVCCIRILLLALGPLLLLTQSQAYRTIDKLSHLILSISILFYAFSPTKLLALSEESSVLFVGDYMVMMWNFVASIVMVRVWKGVYLGIAASYVPLEEELPEDDEEEDAYEKKQQPKKTFELILRLLEYCQREWIWHLSGFTWLFVYSITRIFVPYYTGQVVATVVQAKKEHPTDPNFGYALLVDSVKLMAIISFASAISGGFRGGSFEYAYARINRAIRYNLFSSLV... | Catalytic Activity: a peptide antigen(in) + ATP + H2O = a peptide antigen(out) + ADP + H(+) + phosphate
EC: 7.4.2.14
Subcellular Location: Membrane
Sequence Length: 851
Sequence Mass (Da): 95127
Location Topology: Multi-pass membrane protein
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A0A952IBB0 | MAEGTMMMSKESKKTVELPSRRFFVTDLPDVMELPYSHMVTEAFTVNHLRNVLRLKSGESVLVVDANQEISYRATLDEIERDQVLVTLVSKVSELDSAAMTTIILGVGLVKGDRWDWVLQKTTELGVRRIMPLETERTVVQVKNTAQKQGRWSQIVRSAAEQSEGLFLPEVSAPLTPREFGEMVAIYGQKAVLVERGADRQTFNTVLSGWDLTQPVVLAVGPEGGWTQEEVEILMGLNFQPVSLGDRVLRAETAAMAAISAVVYEQGA | Function: Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit.
Catalytic Activity: S-adenosyl-L-methionine + uridine(1498) in 16S rRNA = H(+) + N(3)-methyluridine(1498) in 16S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.193
S... |
G4E1C2 | MDNPSKSLISLAAALQQIDQAIIALPGEEIVPVSEARGRVNAQTLTARQDSPPYTNAAMDGYALRAVDIAPRGATRLRCVGQALAGHAYPHPLKAGECVRIMTGAGLPQGADTVVMQEVVTRHDDQVSIPAPPRPGEHVRRQGEEFQATDPVCMPGRCLNSADLGLLASQGITEVLVRRKVRVALFSSGDELAQAGTARTQAQIYDSNRPLLQAALETLPVVLVEMGTLPDAPAALRERLQHASTQADVIITTGGVSVGEADRMPEVLAELGTLHLWRLALKPGKPLAFGQIQHAWFFGLPGNPVSALLTFMLCVRPALL... | Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
Function: Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP.
EC: 2.10.1.1
Catalytic Activity: adenylyl-molybdopterin + H(+) + molybdate = AMP + H2O + Mo-molybdopterin
Sequence Length: 412
Sequence Mass (Da):... |
Q759J1 | MQGSVRAIRSLARQFRTMSVEKIYYPRKVQTAASDASLTLNHTSFRIKDPKVSVPFYEKHFGMQLLQKLEFPEQQRDVYVMSFPKQVNKLENGAPGIFHLSGTLHLAHSHGTENDAGYRPNNGNEEPHRGFGHICFSVADLPKECERLEAEGVAFKKRMSDGRQKNIAFALDPDGYWIELIQYNLSDAEPVDLGPKFNHTMLRVKDATKSLEFYQNVLGMSLLEVSEHANAKFTLYFLGYPAADERLKRESILELTHNWGTEDDADFSYHNGNAEPTGYSHMGVSLSDPAPLCADIEETYPDLEWELRYNKGSIKNLAVL... | Pathway: Secondary metabolite metabolism; methylglyoxal degradation; (R)-lactate from methylglyoxal: step 1/2.
Function: Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione.
EC: 4.4.1.5
Catalytic Activity: (R)-S-lactoylglutathione = glutathione + methylglyoxal
S... |
A0A1F8C3P4 | MAIIFDGKKFVKDREVALRIRIAGMGGVKPKLASILAGNDPASTLYVNLKKKAAERVGAEVEIYTIHDRIGPDHIVRLIKYLNADSQTHGIMVQLPLPKRLRENQNEIIGAIAPNKDVDGLRADSPFVHPTSLAALQILAFAESWLKRKIKKLAVVGASGMVGRHVVAEAVHLGYKIQKFTSLNKGQLRVRGSAADAMITATGKPGLIKADMVGKGVIVIDVGSPKGDVDPAVSKKAGFITPVPGGVGPVTVFCLLENLVTAAYAQSI | Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
Function: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate +... |
W5PFB9 | MISPFLVLAIGTCLASSLVPEKEKDPKYWRDQAQQTLKNALRLQTLNTNVAKNVIMFLGDGMGVSTVTAARILKGQLHHNPGEETKLEMDKFPYVALSKTYNTNAQVPDSAGTATAYLCGVKANEGTVGVSAATQRSQCNTTQGNEVTSILRWAKDAGKSVGIVTTTRVNHATPSASYAHSADRDWYSDNEMPPEALSQGCKDIAYQLMHNVKDIEVIMGGGRKYMFPKNRTDVEYELDEKARGTRLDGLNLVDIWKSFKPKHKHSHYVWNRTDLLALDPHTVDYLLGLFEPGDMQYELNRNNVTDPSLSEMVEMAIRIL... | Cofactor: Binds 1 Mg(2+) ion.
Catalytic Activity: a phosphate monoester + H2O = an alcohol + phosphate
EC: 3.1.3.1
Subcellular Location: Cell membrane
Sequence Length: 459
Sequence Mass (Da): 50284
Location Topology: Lipid-anchor
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E1YLP2 | MGGKKNMKLNIFTPGEIFSEEEVEKIIIEGVNGYFCLLPGHIDYVAAIVPGILFYTLTGGEEVFVAVDEGLLVKKDREVFISVRGVIEGAGLGSLKRAVEENFEILDNHEKRARSILAKLEVDFARRFLELK | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane.
Subcellular Location: Cell membrane
Sequence Length: 132
Sequence Mass (Da): 14729
Location Topology: Peripheral membrane protein
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F9QCF2 | MDIIKAKTLDEFFHFNDIKPKNKSLYILALTHPSKSQNNKLQSYERLEFLGDSLLQFITTSYIYKKYPKMLQGKGTLLRSKVVSTASLSEISQMIGLPKLVYSAGGEAAREVKSSSNVQADLFESITGAIFEDLGLKETIKFVGKFLYPAIDKFYNKENKDAKTVLQEIFQSMNKMSVVYQVETLDEKHFVAKAIHDGIVYGEGVGLSKKEAEIKAAENALKKLNLETKENK | Function: Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the o... |
A0A959MR01 | MAEKETTRVEAFSDGVFAIAITLLVLGLVEPHIEATTTNEELFKGLWHIWPSYLGFIISFTTILIMWINHHEIFRIVGTVNKKFLISNGVLLMMVTFINFPTKVFSSQLQTDSAVAATAFLMGSYVLVAAAFLWWWQEAKKLKKNNVPDEVISKISRSYALGVPSYMICLILAFIWIPLSIAIFAVMSIFWITFLRVPIYQPPKHTN | Catalytic Activity: K(+)(in) = K(+)(out)
Subcellular Location: Membrane
Sequence Length: 207
Sequence Mass (Da): 23534
Location Topology: Multi-pass membrane protein
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D7FEN1 | MNGHKYLARRVTESELAQKSPFVMLNKEAPNAHKRMGDYGLAVVQQSDNSFVLLATQFNPLTLNRASAEEIQDHECAILR | Pathway: Lipid metabolism.
Catalytic Activity: a CDP-1,2-diacyl-sn-glycerol + H2O = a 1,2-diacyl-sn-glycero-3-phosphate + CMP + 2 H(+)
EC: 3.6.1.26
Subcellular Location: Membrane
Sequence Length: 80
Sequence Mass (Da): 9014
Location Topology: Single-pass membrane protein
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A0A952ID82 | MSGLFEEAKRLRLKKRFSQNFLIDEAILDRIVGLLSLSSNETVLEIGPGAGFLTERLLPGTGQVIAVDVDPRMVQYLSQKFSAEPTTPKDGLTESLALVQHDILKFPFEKIPVDQFQVVGNLPYNITSPILFSLVGELDTPKYPLRNRLSRITLMVQKEVGERITATPGEKAYNALSVASQFWFEPELAFMVPAGAFYPKPAVDSAVITLTPRAAPAIEVMDYKMLSRLVKTAFNYRRKTLRNALLHGGWIPASDLDTLLNAVGIDGKIRPQQLSITDFGHLANEYAKTHANLSRQD | Function: Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits.
Catalytic Activity: adenosine(1518)/adenosine(1519) in 16S rRNA + 4 S-adenosyl-L-methionine = 4 H(+) +... |
A0A2I0QWX7 | MNTISVSSKERNYQIHVGKDIRHQSGGFLKEFSYSKVAIITDENVAKLYLDDVRKSLEPYFEVEELIVPAGELSKSLHQFEEIQSKLIEKGFDRHSALIALGGGMIGDLVGFVASTYMRGIGFIQMPTTLLAHDSSIGGKVAINFDGTKNLIGQFYSPELVIYDVDTFNTLNDRELRSGFAEMVKHGFIESKDFLTTIKNDMSESINFKDKEFINILAESILIKKRYVQTDEYEKSIRRYLNLGHTWGHAIEASSKDSELRHGECVMMGMLFALYLSDQMNGQENQLFNDSIIAWIRKLNFQLIPRESKLDEWLYQMQRD... | Cofactor: Binds 1 divalent metal cation per subunit. Can use either Co(2+) or Zn(2+).
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7.
Function: Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP)... |
A0A959R4I7 | MIHTIDPTKDFFFIAGPCLVEGEEMMGRVAEHLSSIARRLNVQLILKGSFKKANRTSLHSTVTIGEEAALKILAEAGRTYSLPTLTDIHTEEDALNAAKYVDVLQIPAFLSRQTDLLLAAGQTGKAVNIKKGQFMAPEDIGYAVEKVQSVSGGGDVMVCERGVSFGYHNLVVDMRGLIRMRQFGVPVIFDATHSTQQPSLGTSSGGERQFALPLARAATAVGVNALFFETHPDPANALSDGATQIPLDEAAEFMRQVVLFHQLQSELAGEHGVSH | Pathway: Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis.
Catalytic Activity: D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + phosphate
EC: 2.5.1.55
Subcellular Location: Cytoplasm
Sequence Length: 275
Sequence Mass (Da): 29673
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Q751I9 | MDYGQDFNVARVTDAERRYEERDRARAEEWNDMRKGAEIHRRVRRHLQNRLRPGQTLTEVVELVENATRKFTGTDEHGRFAATPKAQGIGFPTGVSLNHCAAHFTPNAGDTTVLRHEDVMKVDFGVQVNGHIIDSAWTVTFDPRYDPLLEAVREATYTGIREAGIDVRLTDIGEAIQEVMESYEVTLGGQTYQVRPCRNLCGHNIVPYQIHGGKSVPIVKNGDETKMEEGEHFAIETFGTTGRGYVVQSGECSHYAKNPGALPAPTLSRAKALLRTIDANFGTLPWCRRYLDRLGEDKYMFALNHLVKQGIVQDYPPLVD... | Cofactor: Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe(2+)-... |
A0A0B2W2G4 | MSNIRMANDEQIAQLRCDIQCEKAKIRAERNRLKAVVSQGRCPSDATEAGKNRDGWNSVGAAEQLEVLTYQQQLNKTDKIGRVADWIGLVHFGDRCRRGDRNGHYYGSGGGGSEYDYADDDDESTFQLVDFSKPQRSMTQRGVRIRQQQLAYRRMIQKEEERRNQMTYDQNQKIKRSIAKEQQKAFKQWQKRGGARSQGRDRRRLSQWDKCNRRDLPASISVRPEWQVLEEVEFPQLAKLYLPNVEPGQDINGHRYGRLYYYDRSFDKVTVKTERALQHCGGTFYSLTTTEDPIIQQLARENVGNVFSTDIILATLMTAT... | Function: mRNA cap-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifica... |
A0A2G6EJY0 | MKQSIIIFVLFFTVNGFISKLVFNEKKMSNKKLEKITLGNGCFWCTEAVFEKLDGVISAVSGYSGGTTENPTYKEVCTGKTGHAEVIQVTFDSSKISIEKILEVFFKTHDPTTLNRQGNDVGTQYRSVIFYHNAKQKEIAEQIKDKLDNAKIFNKPIVTQITKFTNFYLAENYHQNYYELNKSQPYCEFVITPKIEKFNKVFKELLKK | Function: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.
EC: 1.8.4.11
Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionine = [thioredoxin]-dithiol + L-methionin... |
Q757N4 | MCRRTSQRNLRMFSHHSHSGEYVAHGADTLEAVVAEALRQGFHTYCLTEHMPRLDEAYLYPEERSGAAARDLRGLAELFGRYVEHAARLRQHVDGMAVLVGMEAEACDRQHVAYAKRLLQDFGSHVQFCVGSVHHVYGIPIDFSQTLWDSALQQAGGNLKRLLADYFDWQYYMLRELQPEVVGHFDLIRLYLPRDRFWVELGTGAVSDTYLGGNWTHIALVSARIVSLWEDVQSRVVRNLEYIASYGGLVEINSAGLRKGLADPYPHRDVALLVKRYAGARFVLSDDAHSVSQVGTEYVRTLEYVENVLQLEGLFYLAEA... | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 8/9.
EC: 3.1.3.15
Catalytic Activity: H2O + L-histidinol phosphate = L-histidinol + phosphate
Sequence Length: 344
Sequence Mass (Da): 39090
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A0A3M0GG04 | MQKEKTTLQDQQKTTPNQDLVTARKEALSQANESGSNSFEWLNENSRKFLEAGYLTEGVSPEQRIREVAERAEEILKIPGYADKFYHYMSEGYYSLASPVWSNFGKKRGLPISCFGSHISDDIGNILFTQSEVGMMSKLGGGTSGYFGKIRHRGAPIRNNGEASGAVHVMRLFESMVDVVSQGSVRRGRFSPYLPIDHPDIMEFLEIGSEGNPIQELTHGVTVTNAWMDEMIAGDVQKRTVWAKVLQSRGEMGYPYVFFTDNANNGAADVYQDKNHPIYASNLCTEIMLPSNDDWSFVCVLSSINVLHYDKWKDTDAVET... | Pathway: Genetic information processing; DNA replication.
Function: Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.
EC: 1.17.4.1
Catalytic Activity: [thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-diphosphate + H2O = [... |
A0A959MDC3 | MNQTDHTEESVEAGGLATAGEGKSASDAFRKLLWGTGYSLLGLLILRTFVFAPYAIPTRSMEPTILPGDAVLINQLPYYIRTPEFFPFTHWPIPHLELGGLGSLERGDVVLFRSPELYLSEDHSILFKRAVALPGDTVALVDGMIVVNGRDPEPLSLPTVHREPMDVKKAWPLLRKKRMVVVPYKGYELPLDSVTAEAWRDVLYAEGVNVTYKNRIVFINGGPATRYRFKQDYFFALGDNSTNSRDSRHFGFIPHKNLIGEAIIIFWSSGEDGIRWGRIGKGVE | Catalytic Activity: Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.
EC: 3.4.21.89
Subcellular Location: Membrane
Sequence Length: 284
Sequence Mass (Da): 31793
Location Topology: Single-pass type II membrane protein
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A0A136MW06 | MSNSLRYFDISLHENLIDEFYDELKKYGRIYMYRFMPDYDMYARPIDQYPAKSQHAAAIMLMIQNNLDPKVAKYPQELITYGGNGAVFQNWAQYRLTMKYLSEMTDKQTLVLYSGHPLGLFPSHKKAPRVIVTNGMMIPNHSKKEDWNKYNALGVTQYGQMTAGSFMYIGPQGIVHGTTITLLNAGRRKGVGKDDLKGTVFVTSGLGGMSGAQSIAALITGTVGVIAEVDDDAIHQRIIDGYINKDNVYKDLPQLLDAIKTNKEQGNAISLIYHGNIVELWEALAESDIEVELGSDQTSLHNIDDLGYCPVGYTFEEAKK... | Cofactor: Binds 1 NAD(+) per subunit.
Pathway: Amino-acid degradation; L-histidine degradation into L-glutamate; N-formimidoyl-L-glutamate from L-histidine: step 2/3.
Function: Catalyzes the conversion of urocanate to 4-imidazolone-5-propionate.
EC: 4.2.1.49
Subcellular Location: Cytoplasm
Catalytic Activity: 4-imidazo... |
A0A7L9AW13 | NGGFTKVWLSLKTVFFPSIIGILVWFWQRIHMLERKPVLLEKMLLSLGIALCFLNAPLEYLTLQFDLPFMLLLGDIRQGVFYAMLFSFWLVFAGEHMLIQDTSAQSSLKQYWRHLSAVAMGCISLFIFDMCERGVQLRNPFYSIWVTDIGTNLALTFIILTGISTRV | Function: A segment polarity gene required for wingless (wg)-dependent patterning processes, acting in both wg-sending cells and wg-target cells. In non-neuronal cells wls directs wg secretion. The wls traffic loop encompasses the Golgi, the cell surface, an endocytic compartment and a retrograde route leading back to ... |
A0A5B9PH21 | MSNTIPPDAVHGPIFPVPLSKEALSRRVKEIAGPLARRAAAKPRKSLPGIRVMGTGIATGSQKIDNCQLAELGCDSDWIVQRTGIQSRFHTGEDQAVSDMCIAAAKQCLANAKVDPKTIDLIVIGTMTADHASPSTACMVQAALDCPAMAMDLNAACSGFVYSMITASQFITTGSAKRALVVGADMISMLTDPKDLKTYPLFGDGAGAVLLTSDTNPDQHSASGILDFHLAAEGKLGHTLLVPAGGSRLPLSQDVLDNRMQYLKMDGRPVFKWAVRTIPEAVHGALDRTGMTLDDIDVIIPHQANIRIIDAAIETLGIPS... | Pathway: Lipid metabolism; fatty acid biosynthesis.
Function: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the tot... |
A0A136N0Z0 | MKIHPIINKIINVLRLKEINTTSLSNNANRLTLSSLGMSNHTGIYPHSNNRTLQAPAYEIIRFRNPVSALKPIHKSHFQQKTHKVKTIHIAIFGIGNVGGTLIDQVLASIVDIEEKKHIRLKIFAIANSSRLLLDKNGMDTDWHEKFNSEGRPYEVQNVVDFARFHHLDNLIAIDNTASAQFVQNYLQLVQQGFHLISSNKIGNTMSYDFYQELRHILKKHHRDYLYETNVGAGLPLIDTIKLLHLSGEKITAIKGVFSGSLSYLFNTYSISDRPFSSILTAAIDHGYTEPDPREDLSGNDVARKLLILARELDLKSELS... | Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 3/3.
EC: 1.1.1.3
Catalytic Activity: L-homoserine + NAD(+) = H(+) + L-aspartate 4-semialdehyde + NADH
Sequence Length: 442
Sequence Mass (Da): 49495
|
A0A507D3S4 | MLSTVTRTSAVNLSRTSTATTSPASTATRLSSIKQHLVAIASASNSTSTSRTRNMAPVAREITKTFDYLVIGGGSGGVASARRAASYGVSVGLVEYAAMGGTCVNRGCVPKKIMWSTASIAESLHEAKGYGFDVAVNSFNWNLVKQKRDAYIRRLNGIYDNNLNKEKVEHIHGRAKFVSERVVEVEGKLYQGKHVLIATGSKATLPPIPGAQKYGITSDGFFDLEEMPKKVAVVGAGYIAVELTGVFHYLGADVTLFIRHPTFLRTFDPIIQNVLMDEYRKAGIKIVTDSKFHSIENLSTENNLSKNLKCAVEDTLKNST... | Cofactor: Binds 1 FAD per subunit.
Function: Maintains high levels of reduced glutathione in the cytosol.
EC: 1.8.1.7
Catalytic Activity: 2 glutathione + NADP(+) = glutathione disulfide + H(+) + NADPH
Subcellular Location: Cytoplasm
Sequence Length: 523
Sequence Mass (Da): 56805
|
A0A3N5KMP3 | MLALAKEKISEIAYLKSVGPKRAEAFEKLGFHKITDLFNVYPRDYLFNTKIDKLSQYIDKNVVICAEIMDKQMPRRPNHPTRLLVSDGTGRLAVLIWGNAFYREKQFLVGNKYLFWGKVGFNNFEGIVQFDLRDHKKYEAGDDELLKYPYIPIYILSQELKKTWIRPLILTKIIFNAIRKCSSDIHENLSPEIRDENGLLEHKKALLRLHFPINLEDVEMSRQTLAFEELFYLQLIMALKKRKVENQETGIVFEKTGVRVEKLFHELLAFELTDAQKRVIREIRADMKKPKPMNRLLQGDVGSGKTIVAVFAMLVAIENG... | Function: Critical role in recombination and DNA repair. Helps process Holliday junction intermediates to mature products by catalyzing branch migration. Has a DNA unwinding activity characteristic of a DNA helicase with a 3'- to 5'- polarity. Unwinds branched duplex DNA (Y-DNA).
EC: 3.6.4.12
Catalytic Activity: ATP + ... |
A0A3N5K095 | MTRSRPKVSVIVPAAGSGTRIGGDIKKQFLPLKGKPIIVQTLQQFEHCPDVDEVALALPESAMSEMESMVERYRLHKVSKMVMGGAKRQDSVRNVLNRLNVNDSDIILVHDGVRPFIEAKRITHLIKVCKEYDAAVLAVQPKDTIRRSTGGGFFDQTLDRTALWLIQTPQAFRAKLLLKAFEKAKKEKFYSTDEAALVERLGVKIRIVEGSYDNIKITTPEDLELGMLIYDRWRAKDWL | Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 2/6.
Function: Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
EC: 2.7.7.60
Catalytic Ac... |
A0A2G6E9I4 | MNSLVIGITGGIGSGKSTVSKFFANEGYTVLLADDIAKSIMVKDQSVVQKIIAEFGEKAFVKNKLNRKFLAKEVFNNPKKIEKLNAIVHPPTISLIKNEIQKLNGKESLIFVEAALIFEAKMENLFDYILLVTADEDIRIDRICKRDNVKLSEIKKRIENQIPEKVKKGLSDFTIENNLDLNELKNKTLFFLELFKNISNDKVEK | Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
EC: 2.7.1.24
Subcellular Location: Cytoplasm
Sequence Le... |
A0A0C2J1F0 | MSADLRRRIASAEAELQSLREQLVQVEQEERLQQHQHAPPSWPWPLQSDEYERYARQLILPGVGVDGQLRLKKASVLIVGAGGLGCPAALYLAGAGVGHLVLVDGDTVEASNLHRQIGHTSATVGAYKVDSLAAAMRARNGSVRYTVHREHLTVDNVGRLVGGGEAEESERSEDTKIDLVLDCTDHPAIRYLISDACVRAGIPLVSAAALRTDGQLAVLNHPVGAGPCYRCVFPRPPPAASQTSCAEGGVLGPVVGVMGVLQALEAIRVLVSGSAPVTVTTAKTVPPAPTLTLFSAGGAGGGLVPPSFRTVRLKGRRADC... | Cofactor: Binds 1 zinc ion per subunit.
Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
Function: Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Also essential during biosynthesis of the molybdenum cofactor. Acts by mediating the... |
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