ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
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A0A6I6SUS1 | MRDKGQKAILNWSDQIETLGWRGLVWLPSAAGTARREAAALWQARAWTSPRWVSLAEPEDIEPQAWLPPDKARTRLGLEHDLIVFDAVTEGDFDADAFGALSGTLRAGGLLVLLTPPGGATSSRYMTRLLERLVHASGVARWMPGSPPQLPELPADPPRREEESGDSDCLTSDQAEAVRRLVRLRRRRPLVLTADRGRGKTAALGIACARLLGSARHEIWVTAPRSEAVEALFQRLEVLCPQGRRQGNRFSEAHGGRVEFVAPDELSARVESGEMGGQGSWLLVDEAAAIPAAMLGQWLAAFPRIAFATTVHGYEGSGRG... | Function: Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at the wobble position of tRNA(Met), by using acetyl-CoA as an acetyl donor and ATP (or GTP).
Catalytic Activity: acetyl-CoA + ATP + cytidine(34) in elongator tRNA(Met) + H2O = ADP + CoA + H(+) + N(4)-acetylcytidine(34) in elongator tRNA(Met) + phosphate... |
A0A3C0QTQ5 | MEFETVAAIIADQFDRDVDDLTEDTDILDDLNATSMDVVELIVAIESATDIRIPDEVVDSIRTIGDVANYLAEHAEVAEED | 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... |
A0A1C7HHW5 | MKPHISMIVARSRNGVIGNRGMLPWRLPEDLKFFKQTTMGLPIIMGRKTWESIGRPLPGRRNVVITSNPSYSAEGVEVVGSIEEAIKLFSSNDTVMIIGGASIYRQALPLADTVWLTQIDQDFDGDAYFDPLSEEDWKIVWEEEHAATEKQTLPYKFMRLERIRNTSY | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1.
Function: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.
EC: 1.5.1.3
Catalytic Activity: (6S)-5,6,7,8-tet... |
A0A1W2BF56 | MALAEILFFVLAGLTILSGLLTVLSKNPIHSILYLIITFFSISGHYVLLNAQFLAVVNIIVYAGAIMVLFLFVVMLMNLNKEDKSFGKPFVMLAGVIISALFFALTAGILLQSDVSANNSTLVSEGNIGLTEKIGVALYSDYVIPFELASILFMGAMIGAVLLSKKTDDLKTKD | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy i... |
A0A059AJW5 | MLVSSRRAAVGCSCSCSSVSRNSPCVPQESPPPRSNDSTSPPLAPQPATVVPPPGYAPLSNSPTSPPLPSPTPLPAFPNGGLPPWKLALIAGTGIGGLIVLIGVCTFVIFHRRKRRRLELGSYPPHGPKGFGKTFFGTISGRALGLSQRTFTYEELKIATDGFSNLNLLGEGGFGYVHKGVLSSGKVVAIKQLKTGSRQGEREFKQ | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
EC: 2.7.11.1
Subcellular Location: Cell membrane
Sequence Length: 206
Sequence Mass (Da): 21693
Location Topology: Single-pass membrane protein
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A0A0B4MHU3 | FIFGIWAGMVGTSLSLLIRAELGNPGSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLFLLISSSIVENGAGTGWTVYPPLSSNIAHSGSSVDLAIFSLHLAGISSILGAINFITTIINMRLNNLSFDQMPLFVWAVGITAFLLLLSLPV | 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... |
T5A7E4 | MARLTKSPKPKDVLPAPSTPLETSRPHGQDTARRGGPSREKMHQRLPPPVSLPSLTTAAYPGSRDSSLGRMSNSSLQLRSPTPLSTVTHASWPSQGGSQGAESSLSFSSSLLQEEAKLRWDSEVELKRVSRSLLRLQKWSLIVGLALLNGGLIYVCLRFWQVYYLSVVLLSTNTALQALMIVCIAGHFLFTGTLRLCRRRRNKSTRAETPPTVLEKLVLLLPCYNETREELTRSLDSLVAQKGIEQHPRVILIVVDGKVRGPGMSKTTQAYLTEDILDGDEERSFDNGYRARDGLLMPVKTQTGRYKGVPYVLVAKSFNQ... | Function: Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non-reducing end of the growing chitin polymer.
Subcellular Location: Cell membrane
Sequence Length: 458
Sequence Mass (Da): 51214
Location Topology: Multi-pass membrane protein
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A0A175VXU4 | MSRQSQQRKKLKKLHDNLDLNSNAASRQDTTEDSWDQKPISDLWLPPEPVKPLSHEEYIQQRLETEHIPPGFVSLNDKRPEAIESVWYMYRITGDPSWQEKGWRMFEAVIKATQTEDGHSAIHDVSSTEDPVKEDSMESFWLAETLKYFYLLFTTPDVISLDEWVLNTEAHPFRRPT | Pathway: Protein modification; protein glycosylation.
EC: 3.2.1.-
Catalytic Activity: 3 H2O + N(4)-(alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-gl... |
A0A1I8HWQ2 | MGITGLLPYLKASGRPISIRELAGQTVAVDTYCWLHKGAYACAEKLGSGQDTDQYVHYCMRYLRLLLANRLKVVLVFDGRNLPAKADDRAAYKRKALQLLAEGRSAEAREAFERCIDVTPSMALALMRSARKEGADTIVAPYEADAQLTHLCNAGLVDAVISEDSDLLAFGCKRVIFKLDSQGNGLLMDRRQIARQLCITASADDPSAPEATGSTGMTWAKFRWMCILSGCDYFSGVPGVGLATAAGIVKRTCLDLRGLANKLFLYAKKVQRLSKEQVEAVVRADLTFQYQVVFDPIERRQCRLNTPPSAAESEAEAPSN... | Cofactor: Binds 2 magnesium ions per subunit. They probably participate in the reaction catalyzed by the enzyme. May bind an additional third magnesium ion after substrate binding.
Function: 5'->3' double-stranded DNA exonuclease which may also possess a cryptic 3'->5' double-stranded DNA exonuclease activity. Function... |
A0A8T0RR56 | MEMLEQSTIKKARFEFPMVGLKQNAPEGDVEAAAERQELTVRIDIAKLHCPRCNHPFKPPIYQFFVPTAMASSQRTSATRAGTTAPTAYRRNTTLEDVVGWHRVLCPNAAYGCQAYVPYHECGDHQRECPCAPCGCSESGCSFAGSPPMLRDHLRDAHGWPVDKIRYGSPHDLCLPESQRRRLLVAEEDGRVFIVVAVGAPGECHEVSLACLRANAAAGPQCTCRMLVIGKAAGAASAPSVMMKMAGCPARPRWCPWLCIAKCFTGPPRRSTSAFASTRNLARDLASLMSSKGITMEATKTRKRGTNKLL | Pathway: Protein modification; protein ubiquitination.
Function: E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ub... |
A0A7R9PKY5 | MECSGGSVKPVVKHLPSVLMALDSILEGHSETEKRSAAKCFTIVKEVGTIRNPHPPTSLSITLLANMLVMLSSTAEDGEIEVRILVGVLQTEATPLLPLRCKKHSRVEGALSSTMSFCNCRMALANHKLGVDLLAIFFGIGAWIGINGIQSYSCLPYGNVAYHLSVTLGSMANPLACFLAFFLPYSSVRATSLMALICTLISCYIATTAVMSPSPPLVGTTGGEALVFIRSSYTATPGNWRREALVVSSLGHLTLRLHGTGGETIVVSLLGHLTLPLVGTTGGEALVVLSWVVFTGLISYIKVSVATLFRLEGGRALFWC... | Function: Plasma membrane transporter mediating the uptake by cells of the water soluble vitamin B2/riboflavin that plays a key role in biochemical oxidation-reduction reactions of the carbohydrate, lipid, and amino acid metabolism.
Catalytic Activity: riboflavin(in) = riboflavin(out)
Subcellular Location: Cell membran... |
A0A922HRR0 | MHTDFNQIKILNNNVSSSENESLEHSSITQQQQQQQPEQEEEEIVMKKSTLITDGQYYDLDSISNDLFDNIFEHLCLGVYFDFYKSHKLNSIRLREYSNPNDDIDSKVYENTKLDIFGHSVNGIKKLECACPNCSRTCAAFRLAPHLEKCLGMGRNSSRLASKRIALVIKNSNGTNSE | Function: Component of the transcription regulatory histone acetylation (HAT) complex SAGA, a multiprotein complex that activates transcription by remodeling chromatin and mediating histone acetylation and deubiquitination. Within the SAGA complex, participates in a subcomplex that specifically deubiquitinates histone ... |
A0A3D4JK83 | MNIADLILLSLGLSADAFAVAVTDGMSDRRMNAAKMIFISLVFGIFQGVMPSMGYLISQSFLSFITDYGHIAALLLLGGIGIKTIAESVKNDDECENEPGISFGTVMVQGLATSIDALAVGISFSAMQMNIVTSCAVIAAVTFICCIAGTAAGRKFGNILNNKARIAGGTVLIIIGIKIFIESVI | Function: Probably functions as a manganese efflux pump.
Subcellular Location: Cell membrane
Sequence Length: 185
Sequence Mass (Da): 19292
Location Topology: Multi-pass membrane protein
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A0A840I2R2 | MSDAPRSVRLWLLLLAVLVAAMVIVGGATRLTDSGLSITEWDLVLGALPPMSHAHWEEAFALYRQIPEYHRVNAGMTLSEFQGIYWWEWSHRNLGRIIGLAVFAPLLWFSVRGTVRGRLRWQLWGLFALVCLQGAIGWYMVSSGLSERVDVSQYRLALHLSTALLLYALIVWQFLSLSGSRAVAAGSKLGGWAWGMLAAISLQIVLGAFVAGLRAGKTFNDWPLMGGKIVPEGYFGEPSRFADLFERVAAVQFNHRIGAYLVLAFAIAFAVKCYRAGRDTRRYGASLLGAVTFQAVIGIATVMAAVPLWLGLAHQAGALV... | Pathway: Porphyrin-containing compound metabolism; heme A biosynthesis; heme A from heme O: step 1/1.
Function: Catalyzes the conversion of heme O to heme A by two successive hydroxylations of the methyl group at C8. The first hydroxylation forms heme I, the second hydroxylation results in an unstable dihydroxymethyl g... |
A0A833QR61 | MPMPIMVSLNLIILTDWYGLFKQRITAEGQEEVAEDWLEKFSPWEIVRHDIVYSVRLFGHVEINPDRSGSDEGQFLSNVEFIWPMMMIGSSALQAGASILKEFIFIYGEKRLKGKIKT | Function: Allosteric enzyme that catalyzes the rate-limiting step in glycogen catabolism, the phosphorolytic cleavage of glycogen to produce glucose-1-phosphate, and plays a central role in maintaining cellular and organismal glucose homeostasis.
EC: 2.4.1.1
Catalytic Activity: [(1->4)-alpha-D-glucosyl](n) + phosphate ... |
A0A0L1JFD1 | MSSTRCGHLPKRDSLAATKNDVSGSNEEHQTALPGKTADRVFYEPHLNEILSGGSTSLIARLRPGVVLKYPRYSWWHAEAADRHPFVKDVKQSFEVEERILDILGAHPRIIRYIGVSEEPRGLLFGEASDGDLQTYIDQHHDNIDERLRLKWCIQAAEAVHYIHQKGVIHSDIRPDNFLLHSDSNSRLDLLLCDFGGSTCGDIDGGHLPDSGFFNPCWPWVSTEAVDIFSLGSIFYTIMTGHWPYRSPGPFKSLEEKMDYGEMVDGLFASRTYPPVDGLLGGAVIQGCWTERYSDVGALIQDHGYLSAR | Function: Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N... |
A0A182JWP8 | PKTATVPQTPLVQASYNTVQQQQQQQHLPASRPTTSLGTAARGNVNQTVVASAAARYKQTGVLLSDDIGVKLQEIYKRTNGSNARIKWPITNSRDAHRDEDVFIARANNPFGHSTKWRWSNETEQEDPLKVEVQASRDGRAKRGVYNLYSMIKCATGCDPIIYKGYGCYCGFLGSGQALDGIDRCCKMHDYCYSTANCPMFLEYFVPYLWKCYRGRPLCAIDHGEWGGPGSCASRLCHCDLSLSKCLRRYYCPRKRNVCTTSPWRLLQNLVMVF | Cofactor: Binds 1 Ca(2+) ion per subunit.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+)
EC: 3.1.1.4
Subcellular Location: Secreted
Sequence Length: 274
Sequence Mass (Da): 30887
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W2RLI2 | MCGGFGRRGKVPSPLILARLTPISEDHRGTPESPGRVVTLIERRFWATLKDSQISPDNEHVWGVAYHIVPSKVKEVREYLDIREINGYSIQYTPFHPANPETKDLHCLVYIGMPDNPQFLGAQDPRDVAETINRSIGPSGENREYLLQLDEALQSLSPTSHDYHISELASRVRAMAPAVRSTKQRQLSESRLRRISSTEQQEEIEKPE | Function: Catalyzes the cleavage of glutathione into 5-oxo-L-proline and a Cys-Gly dipeptide. Acts specifically on glutathione, but not on other gamma-glutamyl peptides.
EC: 4.3.2.7
Catalytic Activity: glutathione = 5-oxo-L-proline + L-cysteinylglycine
Sequence Length: 208
Sequence Mass (Da): 23597
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A0A6J1ILJ9 | MPSKFFSFRCLIFLLLLLLCNRLPPAHAARPAPVFASLPTQGLDENQTDSENMDEKCSGVSEEECLIRRTLAAHLDYVYTQKHTP | PTM: PSK-alpha is produced by endopeptidase digestion. PSK-beta is produced from PSK-alpha by exopeptidase digestion.
Function: Promotes plant cell differentiation, organogenesis and somatic embryogenesis as well as cell proliferation.
Subcellular Location: Secreted
Sequence Length: 85
Sequence Mass (Da): 9608
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A0A2D5VNJ7 | MPESKSLIKLLEKFERVRPGHLQFLDAVEIGTVVEDSAWDLSIAAKHFMNMFTDHPYYMNLAAFMLTEDHHDVTSKVNSPKHTFSAVTAKLHRRGVVTDKYAEFVTENADFLDSLINYDLDHNLDNYAVMLAKRLYIKNMPDGTPIERYQDVLMREAVWLNMPREHAIGDHTEDSSLFLCEEALRSDLKTCLDCISKRFQLLADGKYTHASPTKFNSAKTTPDKKKRAQLASCFLIPSGDTIDATSWTINELRQTLASGGGVGSDAVMRSETEFVDGGPGHAHGVQKFTQEAYHVAMTTNQGARPGSITEYISMLHPDA | Pathway: Genetic information processing; DNA replication.
EC: 1.17.4.1
Catalytic Activity: [thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-diphosphate
Sequence Length: 319
Sequence Mass (Da): 35761
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A0A151K3V8 | MTVDPSKSIPAFYAGQSILLTGGTGFLGKVFIEKVLRSCPDVREIFLLMRPKKGLSIKERLSKILNLPVSWIYKKKFL | Function: Catalyzes the reduction of fatty acyl-CoA to fatty alcohols.
EC: 1.2.1.84
Catalytic Activity: a long-chain fatty acyl-CoA + 2 H(+) + 2 NADPH = a long-chain primary fatty alcohol + CoA + 2 NADP(+)
Sequence Length: 78
Sequence Mass (Da): 8814
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D4YM41 | MTTTATVMNDILENRVASRIAAQDATVWGPKAEDEASKRLGWVNLHTRAQDIIDQVIELAQTCEHDRVVLAGMGGSSLAPEVMSNAYGKDLIVCDSTHPDQVAYTAQDLDRTLVIIASKSGSTVETDSARRFFTQKFRDAGIDPSSRLIAITDPGSPLDQRAQEEGWLAVFHADPTVGGRYSALTPFGLVPAGLVGVDIAQVVADAASIAPQLEQDSEENLAVRLGALLGAAHENGHEKLALDPHTEQFQGLGVWIEQLIAESTGKDGKGILPIAPQDCENATTVALGASDVHDADALVDLPLGAQFLLWEYVTAIASYV... | Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 2/4.
EC: 5.3.1.9
Catalytic Activity: alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate
Sequence Length: 506
Sequence Mass (Da): 53717
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A0A8J7M5P4 | MSKRAIFEEVSSPKAEAAAPAPVRGREARGAIALWLWLLAALVAAMVLVGGLTRLTDSGLSITVWDPVMGAVPPLSASDWEAAFEAYKTTTEYQVQNNWMTLEDFKPIFWWEWGHRFLGRVIGVVWLVGLVGFLVARAVPRGWLGRLVVPGLLGGVQGAVGWWMVASGLTGRLDVASYRLAMHLGLAFVIFMLLVWLAMRIRLDEVEALKARRRRFGGMGWAGSLGALIFLQIIVGALVAGIDAGRGYVDWPLMQGQFLPSESFDLVPPWRNFFENPALVQFCHRMLGYLVLIWALATAVALARRGHPRIRAAGFWLAGG... | Pathway: Porphyrin-containing compound metabolism; heme A biosynthesis; heme A from heme O: step 1/1.
Function: Catalyzes the conversion of heme O to heme A by two successive hydroxylations of the methyl group at C8. The first hydroxylation forms heme I, the second hydroxylation results in an unstable dihydroxymethyl g... |
A0A517YV63 | MIDIMTTLTTLAQATSVDAINLSDHVNNLIPELILLIGGTICLITGLGRESGTRKFTAVIAAISLILAIAFIPEFSKLKAGLYEITDLRSFIKLAACGIGFLLILVSASVPDLLPQTQKAEEAKKFEPGNIYRGEYYAFFLFSIVGLMLTAGANDLVWLFLALELTSLPTYVMVATAKQNINAQEAAVKYFFLGALSSAIFLYGFALIYGATGYTDLAEIKNVIEAQYVANSGLSGMLLIGLIFSILGFCFKIAAFPMHYYAADVYQGASSAVTAFLAFVPKTAGFVALILILSTVGWNYGPDQNHLPQVIEMLLWVIAV... | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ... |
A0A517YVI6 | MTEIHDLHNPQITHKPRIFILANRIKPQVVEAMHSFRPWLEERADIVAEPDMQTLFRETASDLPQADLAVVLGGDGTLLSQARALVDLEIPMIGVNFGKVGFLAEFSIADLKRHWKCICSGACRMSKRMMLDVMVYDEGTPEWGDGDETIMPKPIFRSVSLNDAAVVAGPPFRMIEIELAIEPKQTKSSATTINGDGLVVATPSGSTAYNLAAGGPIVSPGIDGICISAIAPQSIAFRPIVFNASCDVWLTLKRVNEGSELVLDGQESKPLCTGQQIYIRKHDRVLKLVHNPDMNYWQLLAKKMHWAARPSRD | Function: Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
Catalytic Activity: ATP + NAD(+) = ADP + H(+) + NADP(+)
EC: 2.7.1.23
Subcellular Loc... |
A0A1B6FQZ5 | MSKLPAVVQSAPYDPAYLFSPDNYAEPSFLGNKVPSIFGGLTGFISVIGHNFSQRRPLFAGLPVVIGATALGVAAGVWYQNRSERYWAERDAIYRHYIELHPEDFPAKERILVGDMLKPWVPTR | 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.
... |
A0A267G771 | KGEATEDYISNKTDRCLSDTAIKTVSGLGIGILCSVLFLRRRPWPAVLGTGIGLGMGVANCDNDFKTPHSLVSQQIRVAQRQNDPLLGSK | Function: Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane.
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 90... |
A0A655XYH9 | MEHKIVHVGDIPVANDKPFTLFAGMNVLESRDLAMQICEHYVKVTDKLGIPYVFKASFDKANRSSVHSYRGPGLEEGMKIFQELKETFGVKIITDVHTEAQAQPVADXXXXXXXXXMWWM | 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: 120
Sequence Mass (Da): 13613
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A0A0D8IG36 | MKKFFMKAIFVSIVITMIFSNCIVVAAAENQAFDVNAKAAILMDASTGTILYEKNIHEALPPASVTKIMTMLLTMEAIAENKITLQDKVVVSERASSMGGTQLYLEPGEMKTVEDLIKGMAIRSANDACVAIGEHLAGSEEGFVEQMNARAKELGMENTHFVNTNGLPAEGHVTSAYDIALMSRELLKHKEIHKWLTTWMDTVDVGIKNASTQELVNTNRLIRTYKGANGIKTGSTSEAKYCLSASATRGNTTFIAVILTAPTSPIRFSEAAKLLDYGFANYSTTKVIEKGGSLGSVLVEKGKVPQANVVANDDLSVLTK... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors.
EC: 3.4.16.4
Catalytic Activity: Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanin... |
A0A7R9HVD4 | MPNTGSQRKYIILVNSIVPLVGELKEEFKYQPVYINIAQARLQRARAIMNDKHGNRETLFVAVHVRRTDYTGYLRRKGVTVTADINYYRHAVAWMLRKLISDSASSRNIAFILASDDKVWCKAKLLPEIQEEIQSFGNETNLGGSSVFYLGDVETPKLDLVMLSSCNHSIISYGTYGLWSALMVNGWTVVYDMSPHTSQNKKARPNKTIFLLEVKPTCPKGVVTVVDGGRLCNKILEYVSVWSLSRSYGLVPYVPDSIHSALRNVFTQLRIPPFLSCIILIDLIVPLIGVLKEEFKYQPVYTNSAQARLRRARANVNDEH... | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 322
Sequence Mass (Da): 36413
Location Topology: Single-pass type II membrane protein
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A0A951SXR5 | MRLFIIRFSYSLLLYIVWPMYSIAQFFSKQARQFATTRKEGKATIQEFLSSEVDVTEFRFWLHASSVGELDQAIAVARSIRKNRKYKNSKILITGFSLSIKKLPTLPEANLSCYLPLDYQLTWSKIFKNQNRSNTQNTKDRKITDFSNLIFITFTWDVYPNLLFQLKKVNSKSFLCSAALSKDSWRLKYSFWLQPVYNLFDGIGAVDQPNKTRFLQLLNDQDRVQVTGDSRYDTVFYKLENSKLTDANLKPILNIKSAFILASTYNACDQQLFPELPTWLKAYPNRDLWIFPHHIDEHRLKECEANLANYGIQSHRFSEL... | Pathway: Bacterial outer membrane biogenesis; LPS core biosynthesis.
Function: Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of 3-deoxy-D-manno-octulosonate (Kdo) residue(s) from CMP-Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A.
Catalytic Activity: CMP... |
A0A6N2UMS4 | MEKRQKINRAEQYSLLLLAGGKSSRMGRDKAELSLDGKSFLSCQVTKAEQLAIREIFLSGHGTGKLIKERTESENRVHIHEISDIYKDRGPLGGIHACMKSMETPYCLVLPVDVPQIPERVLEELLTIHERKKSLAFSSDAGSSRASKNSDRPLLLIHNSRKEPLIAIYPVSMAEEIEEIIKLGSASVFQFLDKTGYDLCAISVEEWQVQNINTPKDYIELQKYMEKRNEK | Function: Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor.
Catalytic Activity: GTP + H(+) + Mo-molybdopterin = diphosphate + Mo-molybdopterin guanine dinucleotide
EC: 2.7.7.77
Subcellular Location: Cytopl... |
A0A2T2WTM8 | MTLMASVYGITSALTLACALRVLLADRPLTAGYFMTATMIGIGVLFWELKSPMLAGIQILIYGGGILVMVLFVIMLTPSGQSWLPRPGAWRITWLLIPVSGYVAARSYPLHRPVILGRSLGRWLLMGQGFSLEILAMFLLLTLASALAVATDPPNEEDAS | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy i... |
A0A7R9F738 | MQQSDFEIKLTVFERGYSSDADIRTKESTSVVKRVLLYDPTVPGKGTKDDIFLNVKQMALSLSDQYKKYGNKIAWVSIKLSINSNYGKKEHLLMDFAVVDLVIKKLSPDSLIMMCQTNMEFRQDYLNRVRMNTILHWQVFSPLPFTEYYLNSMGPRNKELDINKNHGYYDTSFAKHISFYAMDYSKARNQVELDIPIIHSDRDVSKEKPPPVHPTEIRTSISPFSAVGLNTTSALANYATEAVHPTEIRTLIFPSSAVGLNTTSALANYATEEGYIHRNCTRICEEGAWETNLSTPDRDSNLDLPIIGSLVYCKCSALGH... | EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 326
Sequence Mass (Da): 36858
Location Topology: Single-pass type II membrane protein
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D4YL28 | MNRMSSAHPHPDWATLPNLITLLRLGFVVPIVILVLNHAQPVLTVVLLAVFGASDWIDGYLARALNQVSATGAVLDPVADRIGVAMIALALAVAGHLSLGVVLTIAAVDAALAVTYLVTRPARAPKVSRVGKVRTAVLMSGLALIGLSLVPALLPVGTAGRILCVIGAFLHAVAGFGYVRALLRDSHTDPPDM | Pathway: Lipid metabolism; phospholipid metabolism.
Subcellular Location: Membrane
Sequence Length: 193
Sequence Mass (Da): 20038
Location Topology: Multi-pass membrane protein
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A0A1B6FH25 | PQFNDGTVLLTGATGALGTLVLEKLLRCCNGLNKIFVAVRGKNGASADQRLKELLTTKVFDRVRLEQREALSKVELVDMDLGWESHSSRIAPTVTMIIHCALVTDFTHSLIDAVEVNIKQTIALMQLAYSCKKIEAFVVATSTLCHSRERVLEERFYPPPVTASGMCVVIDSLAQHPLSNDSSGCFRLILGDICASLVTLTITEDILRQGRKFLPLAIVRPSMLVASYKEPLAGWLPPSPKGVMRLLAYAMQGRLSTLRTEPDVKAELIPADLAASALIAVAAHTSSVRRNWHNKETEDSGNLYQIVLDSEIPIYNLVSS... | Function: Catalyzes the reduction of fatty acyl-CoA to fatty alcohols.
EC: 1.2.1.84
Catalytic Activity: a long-chain fatty acyl-CoA + 2 H(+) + 2 NADPH = a long-chain primary fatty alcohol + CoA + 2 NADP(+)
Sequence Length: 468
Sequence Mass (Da): 52513
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A0A0K9FAK9 | MSSPILMLLNPISITLIILIFTEKWFGGAQSVYVGTMIGTALIAILDALKDANIMVEQINSTFGFIPLFTSGAGWIITGLLGAIIGYIFSNKSVVHSSKSVSN | Function: Component of the transport system for branched-chain amino acids.
Subcellular Location: Cell membrane
Sequence Length: 103
Sequence Mass (Da): 10965
Location Topology: Multi-pass membrane protein
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A0A850SM85 | MKYILMLTVCAGALALAGCSKKSKEAEAPAPAVEAAAPVSPAAPHSDNALLAEWTGPYGGVPAFDRMDVALLKPALEEGMAAQLAEIDAIANNPEAPTFANTIVAMEKTGALLDRATTYWGIWAGNMSSPEFRAVQQEMAPKLAEFGDKITQNEKLFARIKAVYEAEADNDLRPDQRRLVKLIHDDFVRSGAALDAAGKARTAEINKRLAELHTKFSNNVLHDEESYVTYITKEQLGGLPESFVAAAAAAAKERGRDGEYAITNTRSSMDPFLTYSTDRALREKVWKTYYNRGDNGDEYDNNAVIAEILKLRDERVALLG... | Cofactor: Binds 1 zinc ion.
EC: 3.4.24.70
Catalytic Activity: Hydrolysis of oligopeptides, with broad specificity. Gly or Ala commonly occur as P1 or P1' residues, but more distant residues are also important, as is shown by the fact that Z-Gly-Pro-Gly-|-Gly-Pro-Ala is cleaved, but not Z-(Gly)(5).
Sequence Length: 727
... |
A0A0L1J0I1 | MMFSVPTRQRLFLVTRRRPLVVASRFNSRLASTLRNPASRPNDSCFNSKRAAYAAGGTSLAILGLMWTGRNRCDAPDDARDKRALSTVPLTKLLSGWVAFAFCSSPTWVGMSESLYNILSRIPLVSSITNAVVMQTFFNQFLGGQTIAECISKIEALRSEEIGTLLGYNIEAELDGSSKDMQLILEQTQHVLSSIEAQGKLSRRLWPDTTATGGDNRCWVRIKVTGLLSNPVALYHGSNAILNARAEKGLDKDVPYPGLPHDGDWEAALNGDGVTHADRKELVALRAVLEKIISKARENNVRIVIDAEQSWYQPVIDSLT... | Function: Converts proline to delta-1-pyrroline-5-carboxylate.
EC: 1.5.5.2
Catalytic Activity: a quinone + L-proline = (S)-1-pyrroline-5-carboxylate + a quinol + H(+)
Sequence Length: 724
Sequence Mass (Da): 80542
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G5E3K2 | WVRNWAVWRYFRDYFPVRLVKTHNFLPSRNYIFGYHPHGIMSFGAFCNFGTEATGFSKKFPGIKPYLATLAGNFRMPVLREYLMAGGICPVARETIDYLLSKNGSGNAVIIVVGGAAESLNCRPGANSVTLRHRKGFVKALQHGA | Pathway: Glycerolipid metabolism; triacylglycerol biosynthesis.
Catalytic Activity: (9Z)-octadecenoyl-CoA + 1-(9Z-octadecenoyl)-glycerol = 1,2-di-(9Z-octadecenoyl)-glycerol + CoA
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 145
Sequence Mass (Da): 16201
Location Topology: Multi-pass membrane pr... |
A0A8J4G2T0 | MLPASTRPAVALAAAAALAGVAVPTSSMMRCSAAAVSTLRAAVRTLIHGDVVCAATATTIGGVALRAFGATAASSSPVTAAVATATAAAPPSRDLPSASGTHIVSATPSFAADGAATVSVCDAAARPHGSLGTGYEAGPCLGQRPSSQTDSSDAATAATATSPSALSFSDYRTVFEGQSTWRLLRAYGVLRICGLKPLTNHAEALLTTSRRLLGDKATDALVKSTFFAHFCAGEDVPEVQDTVDRLQAVGVGAILDYAAEDDVGPTTAAASKQPAPGVEPAMEARSGLSEPSPRALGVVGRTYDYASEEQCDRHVDHFLA... | Function: Converts proline to delta-1-pyrroline-5-carboxylate.
EC: 1.5.5.2
Catalytic Activity: a quinone + L-proline = (S)-1-pyrroline-5-carboxylate + a quinol + H(+)
Sequence Length: 529
Sequence Mass (Da): 55147
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A0A1B6FD90 | FMDKFVKIALKNDRHVLLSVVYFGEEGLTEARLIMSKVAGKNGHASSLRLLALNETFSRAKGLRVGAERPWDQPGVLRDQQDVLLFMCDVDVVFSARFLDRCRWNSRPGSRVYYPVVFSLYNPHVVYTLQGKKVPSETDQLVISRDTGFWRDFGFGMTCQYKSDFLRVRGFEEEMVGWGMEDVLLYRKYIRSRIKVVRATDPGIFHIWHHKVCTGEQQSSDQYRACIRSRALNEASHAQLGFLAFRDEKNAKIPAQTNNKPAKRKRPTAAHNKPTNSKSQTSTQTKTTKDSRKKTKQNDVTTKKFRSEEVKEQPISENNR... | EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 330
Sequence Mass (Da): 38026
Location Topology: Single-pass type II membrane protein
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A0A1B6FAF2 | MTRVHSWIVVFTIVACVGQLEANIGETPYRPGGDEIGTRGLLDNTLRNRLKYLYGVTQTKPIFSFQSSGTAGKDNSKCNWPITSVSFNHPIQSPIDLITHKAVTMDLPTLGIIKGNTDGVLAKLYNSGHTVYVYIEEEAFFRPHLIGGPLKTKYIFEQMHFHWGSEDIWGSEHFIDGESFAVEIHAVHYNSKYSTYANASAQPDGLAVLTIFAEAHTTDNEKLNPMYHLLPNITKAKSSVELPSWDALKWVASALSTNYEYYTYPGSLTTEPYTENVIFILLPKPITLSVVQLNAFRNIHGDNDHRVTDNKRQLQPLHNR... | Function: Reversible hydration of carbon dioxide.
EC: 4.2.1.1
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Length: 329
Sequence Mass (Da): 37058
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A0A833VIC5 | MDFGGVLTMDSFLASSSSSSSSLSTSNGAFSEHNKGLFASSCLKHTRSSGDLEATDLGFPKMARTEMKMRHEHSKYSSYRPGSGSLFPGGTQMLSFSSPGKESCSVLSSDGALPYHHHHHHSSQSSLEPSYFRNGEASMNNGIMSRIRGPFTPSQWMELEHQALIYKYIVANAPVPTALLISIRRSLAPAAFSPFSSFASSPMGWGPLHLGYAGSSDPEPGRCRRTDGKKWRCSRDAVPDQKYCERHINRGRHRSRKHVEGRTANAGQAPMRPAPAPDSNAGGSSAAAHTSAGDLNRALLNEPSTTDHGSPSLSLLTCTN... | Function: Transcription activator.
Subcellular Location: Nucleus
Sequence Length: 481
Domain: The QLQ domain and WRC domain may be involved in protein-protein interaction and DNA-binding, respectively.
Sequence Mass (Da): 51580
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A0A0N5AF90 | MRYGLVLLLALAAVVTSTPLVKKPLLPSKYAMANKLWKMAHEPKNKKAMCVACTVIVDGVQILLKQNKTDEEIENFVIILKNIPEFYYSKTCKTLAIEADYVCDHFVHEFGDEAFFVLERVLVTPHEICGALVEDCGTAVNPLNQMWNLTIPARKPQVKPWPTPAPNKPTMRILHLSDIHVDRHYAVGSEAECEEHHPFYEFCCLEFPNERPTTPAVPAGKWGMPYKCDIPYITFESLIKQISEREKVDYIYITGDMEAHNIWDYTREDTMANLNNISSVIHKYFPKTPIFEAIGNHEGVPMDAIAAHGMEEYDKRGPQW... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Converts sphingomyelin to ceramide.
EC: 3.1.4.12
Catalytic Activity: a sphingomyelin + H2O = an N-acylsphing-4-enine + H(+) + phosphocholine
Subcellular Location: Secreted
Sequence Length: 554
Sequence Mass (Da): 63570
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A0A090V295 | MRRNLSRRPQTLFFAMQLALGGAFLALTSAQALAAETESQTPIQSPDILLGPLFADVQTAKLFPDQKTFADAVPKSDPYMILADYRMQRNQSGFDLRHFVEMNFTLPAPNEKYVPPAGQTLRQHIDGLWTVLTRTTDRTDKWDSLLPLPEPYVVPGGRFREIYYWDSYFTMLGLAESGHWDKVEDMVANFAHEIDAWGHIPNGNRTYYLSRSQPPFFAFMVELLASHKGDEALKTYRPQLEKEYSYWMEGADTLQPGQANKRVVKLEDGSVLNRYWDDRDTPRPESWLDDVTTAKNNPNRPATEIYRDLRSAAASGWDFS... | Function: Provides the cells with the ability to utilize trehalose at high osmolarity by splitting it into glucose molecules that can subsequently be taken up by the phosphotransferase-mediated uptake system.
Catalytic Activity: alpha,alpha-trehalose + H2O = alpha-D-glucose + beta-D-glucose
EC: 3.2.1.28
Subcellular Loc... |
A0A1I8FLF0 | SRRRRRRAREKQEVTLSKPRWAPPWTASSIRNSPNLKLNSAAAARASQLVPGVTSCRAFIRLDLRYLMPFFTRTFTHKEVTEGRQMMTTLTDKWRQEMKMRAAAGAAECCKCSGQAPGPGALIGKVEGKIHQPWRKLHSQAAPEGAGRLSRMHLFAADAADGVQRARMETNGDAPQVPQFEPLLPAAAGCPPHRVRLPRRRTVGFNRRRRSRHGRLCRSLDGLSEATLAGLSDMGMSSMTPIQARAATSWASAKTGSGKTLAFLVPAVELMRRLEFQAAQWDWLHCDIALLGSSACRLIGVLQRPRNLAKGCTNPHRYAG... | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 486
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): 53956
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A0A0L1IK43 | LSKHKKKKKMRSRAVAIGEVEIDERDRKDYFSPSTGLFEDYCSSIIARYGLNTPGMIQQREVNNVQYDYHDEMSPSEKIFTVTTSDGAVFYSRTVVLAIGPGRTKVFPFKLTDEEANGGCHSTEIRSFPSPNVKRKIQQRQQTNLMVVGGGLSSAQIVDMAIRKGVSKVWFLLRSDFKVKHFDIDLTWMGKFKNYEKAAFWSADTDEERLEMIKTARNGGSITPRYQKILKQHAARHRVSIHSRTVILSREYCPMSQTWRLTTDPPIPDLPRIDYIYFATGMQADVNELPLLQQMNREYPIETKQGLPCITDDLMWKADL... | Pathway: Siderophore biosynthesis.
EC: 1.14.13.196
Catalytic Activity: L-ornithine + NADH + O2 = H2O + N(5)-hydroxy-L-ornithine + NAD(+)
Sequence Length: 389
Sequence Mass (Da): 44141
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A0A6J1IK66 | MAVNAVNAVNPTPLRLPSAIPTGKWISNARVCLPRKPPTQSTSSFNKNFRSRSNFSLKPSSSSLASVGNAGYVEEPSTNVKFSTSFTLPGCSTSLSLLGTAANISGYREKVFAIIGVKVYAAGLYINSSISNELNAWRGRSAAAIQEDSSLFNIIFQCNNHYL | Pathway: Secondary metabolite biosynthesis; flavonoid biosynthesis.
EC: 5.5.1.6
Catalytic Activity: a chalcone = a flavanone.
Sequence Length: 163
Sequence Mass (Da): 17469
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A0A481P8B4 | MYQKVGASPWPFLGATGLWVVAVGFISYVFFHGWSYLFYGLFCVLCVAGFWWRDVFREVGCLGCGTSSVLGYYKAGFILFLISEAFLFFSFIWSYVHFGCMSLVQVGCYWPPRGVVPIDAWGWPFFGTCLLLSSGVSSQVAHGYLKIGDKVGCFFWMVVTVILGVWFVIVQGKEFSTAKFSMADTVFGGCFFIVTGCHGAHVLVGLVFLLVNLFRMVVGGYWPSNHWGFRAGLWYWHFVDGIWIVVWSVLYHWGGWDYVGF | 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, comple... |
A0A351ZC69 | DKGIEINTSGLRQGFGDTFPDIKYVRLFKDMGGELLSLGSDSHTVADIGANIADGAKIAAEAGFTRLAYFKKRRPYFIDID | 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: 81
Sequence Mass (Da): 8857
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A0A1I8HX50 | ALIGPQAVTVDPGINERGLVVIPEAIVLGAGQGARKKLLGIDVVAHLLAKAGRARQAPVSVAHAKNLLIAEVARQTGTVDSVASIADRILVVAVERADDGPDEVPVEPVLGLGFGQASGAVVPQPGREVPFAYGQGDGRGDKNKDGQEAQRHHFISKSSRAILDFVCDLLRYRDTAVQLETLANPAGTKLLWQSRQQPPNSPTDDQYTEMSSPIDTNCMTLTRFILEEQKKHKSASGDFTNIMTAICTAVKAVSSAVRRAGMNSMFGMAGGQNVQGEDVKKLDVLANDLFINMLSSTFKVCAMVSEENKDLIVVDSEHEG... | Pathway: Carbohydrate biosynthesis; gluconeogenesis.
EC: 3.1.3.11
Catalytic Activity: beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-phosphate + phosphate
Sequence Length: 544
Sequence Mass (Da): 58631
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A0A8J7FPG8 | MKGLLRLNLLVSVVFVLAFVLTLFGLIRQGEKDIEREIGASIHFAEQMIEAAQYDPSRLQPLLNGNTRHIHFYLNHLPAAYDRDNDVPAWFSDLLQPKGAFVARPWRYPLMNGELLYVVATPDDEIDEVWESALMLAGLFLGGALLSNLMIFWGVRQGLKPISKILETLEQEKSGPFCTRLQHYSMPEADQLADHFNRMAEALEQEQYGNRQLTKQLMELQESERTRLAHTLHDDLGQYVTGIRAQAYMICQAADQQLVVEKTAERIVGHCDEMQKSFRHLIRDLHPVILHQLGLKDALCNLAEQWQESSGIPVKLEMAN... | Function: Member of the two-component regulatory system NreB/NreC involved in the control of dissimilatory nitrate/nitrite reduction in response to oxygen. NreB functions as a direct oxygen sensor histidine kinase which is autophosphorylated, in the absence of oxygen, probably at the conserved histidine residue, and tr... |
A0A951Y2B5 | MSGATAQPKASAPPPLYGLVLAGGRSKRMGRDKSAILYGDRPQVETTFQLLSPLCVQTFISNRSDQSCTPGHEGKPQLHDRYTDLGPLGGLLTAFDTHPSCAWLVIACDLPFLKRETLDHLIANRDPKCDATAFRSHHFEGLPEPLCAIYEPAMRARLQQFAADGITCPRKALVRSNTHLIDLPDPHALENANLPEEFEAARAALAAGSAVELNTASKKERQIRVCLYALLREKANRSELALTTTARTALDVYGELQQQFALPWEADRFRVAINDTFCSWDAAVRDGDCLHVIPPVAGG | Function: Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor.
Catalytic Activity: GTP + H(+) + Mo-molybdopterin = diphosphate + Mo-molybdopterin guanine dinucleotide
EC: 2.7.7.77
Subcellular Location: Cytopl... |
T5A9H9 | MRAHKTKQAVVGATVCNYRGFTAAQRRPPAPPLRRQAQAITPHLYEYLAPKALRSDDDSILISGAHLRSLLVASPTHRPLTQAPPAHVLPPPLLASTSPLSRRRIPQLPAHTPGHRQHGRRTALPLNPSELNVLRAQYEKEGDMVGVQTKFNYAWVSNACPLGEQIALAHLIRWHIQLSRLRFPCLHTVEQGLVKSNGRGDQQLGVRLLSEIFRLSPERRRECLYYLALGNYKLGNYGEARRYNGLLLDKEPANLQASDLRQLIDAKVAREGLVGVAILSGVSIAAGVVGAFFFRNARRT | Function: Has a role in mitochondrial fission. Has a role in outer membrane fission but not matrix separation.
Subcellular Location: Membrane
Sequence Length: 300
Sequence Mass (Da): 33302
Location Topology: Single-pass membrane protein
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A0A1L5FCZ4 | MGFNVINMNTWERGEIGPSYSVLNDKTKVMGDLYTSFNTVFLNFYEDMVNALNSYKSDTNFTTQFQDNFFIVSCLPWFNYTSFNVNNEGSSSFLFPMVTWGKFFKESNKIVMPVTIQVHHAVADGYHCSLFFSNVQEISSNPERYL | Function: This enzyme is an effector of chloramphenicol resistance in bacteria.
EC: 2.3.1.28
Catalytic Activity: acetyl-CoA + chloramphenicol = chloramphenicol 3-acetate + CoA
Sequence Length: 146
Sequence Mass (Da): 16895
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A0A1I8ILZ9 | DEYSNPGSQTRRPNFQLGDPIFLWQPRSRHRLIADLMICIDRTPCSIQPPPWDPSSRQQQQQPRRWMPKFYFVPRDYLQDEYSNPGSQTRRPNFQLGDPIFLWGEAVMLIADLMESGYLMAHDLDLLRRHKPFHERPLDLSRRVPFINKLQDLVVQVVLISESVRLQQMLATFGVQSQTPTQVEPITLWPSKNLIRVQECLGRCDRLSLSGRPLRPIGQLGTAKFYRVPGRTVLCYPLLFEMRDFYLLHDMDMVIDEVRTNLLFLSTWWRLKGRPTFCFLLREDMIRAAGAKQLIAFLTSMRSGWVNDVRVLLGRAQNLL... | Pathway: Glycan biosynthesis; glycogen metabolism.
Function: Phosphorylase b kinase catalyzes the phosphorylation of serine in certain substrates, including troponin I.
Subcellular Location: Cell membrane
Sequence Length: 758
Sequence Mass (Da): 86509
Location Topology: Lipid-anchor
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A0A833VW71 | MADDANDSNRPNTRSNMDLNLYLGLPRSPRRARPDLGSDLALSSIPMNSSSSSSVASIEDSNTPANRSSSIHIETAESHAHPPYSPSTPAMDPNPQMDRTPPSPEYTPYFPSYESFNTSYPPLADPNPLPPVHELDEATNPSLMIVDDPAAFSVETHVPYSPPYVAPPSLPPVPPPQQAYIPHPRAQENPNDDITFSFYPQLPPPYMTSGRSELLRPEIRFRRLIETSSRLRARRFRSSFPHGSGANNPNMASASTIGVTAAEPQAGQETVACVERTAEANVRKDKVKLEAGTMEEEASDEESKENAQNISANFECNVCF... | Pathway: Protein modification; protein ubiquitination.
Function: E3 ubiquitin-protein ligase.
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
Subcellul... |
A0A267DFA9 | MKKYLFVFALIITALIFLLASLYSFVFDVEYNKCDMTYMFQYPEYIPVTLPASVRRKFPEYNLFVYTEGHSEPVSRSVFEGSPLLFIPGNDGSHKQVRSLASVAIQMRKTLGTKTRFDCFAVDLNSEFSALHGPFLYRQSEFVRHVVDHIESLYSSRAKFSIVLVGHSMGGLVARHAMTLEDFDRGRVPLIVTLATPHQRPVLASDSEMLSFYSDMNSYWRKNRATGLGHVALISIGGGDRDLEVALPLTRIDSGLTLPRNALWASASHVRNAWASTDHRCIVWCKQLVIALCRSLFSTAAAGRSDAQSVVVEFRRHLLP... | Function: Involved in inositol deacylation of GPI-anchored proteins which plays important roles in the quality control and ER-associated degradation of GPI-anchored proteins.
EC: 3.1.-.-
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 377
Sequence Mass (Da): 42455
Location Topology: Multi-pass mem... |
A0A2I0MS56 | MWDIQKGLEVIVEKNEDGDQKIEQDGIKPEDKAHKAATKIQASFRGHITRKKLKGEKKGDAPASESDAADKKEDGPAGGAAENKESEARLLPPQKQPPLTVPSWRRAAKTAARQQRRRKGMEPPTRAQSSQPHRLPLLLPPRRKSPLLLPKRKVPLKLPLITRRP | PTM: Palmitoylated. Palmitoylation is essential for plasma membrane association.
Function: This protein is associated with nerve growth. It is a major component of the motile 'growth cones' that form the tips of elongating axons. Plays a role in axonal and dendritic filopodia induction.
Subcellular Location: Cell membr... |
A0A5N9C1S5 | MSIYSISELNKYLKTLLNFDNILQDIWVQGQIGSFTKAASGHSYFSLRDSDSTINCVMFKGISGITEIETGMSVVAHGRVSVYEPRGQLQMIVDVIQPEGVGLLQIQFDQMKEKLDKEGLFNESRKRGIPKFPNRIAVITSPTGAVWQDIQNVIRRRYPVVELLLIPSIVQGDSASKSLVNSFEILNTLNKVDVVIVARGGGSLEDLWPFNEELVARAVYSSSVPVISAIGHETDFTIIDMVADLRASTPSIAAEIAVPDKEELLTSVKDSGSKLLFYLENLLKRNRVYLESFPKNLEKFIVDLDLFRMKIDDCLNSIVK... | 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... |
W2EBR5 | MNNDIVVAKRYAKALFEVAQEQNTVSQVEEELKVMVELIQGDRELDAFLNHPNVESDVKNDVLQKTLEGKMSAPVLNTLKLMVSRKRIGILPVLLHDFVDIANEKLGRANAVVHTPFALNPEQEKDLIDYFAKLTGKTIRLETVLDSSLIGGVTVQIGDRVYDGSLKGKLDRLQKSLKQAQSL | 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... |
A0A1V6HJ47 | MNITIIANRYAKALFILAQEKNLIDQVYQDMLIVSDVFSKNKNLQRILSSPIYTPAKKLSLLKALFSKHISSFIFRFIELVLRKDRALIIGYIADSYIEIYKEFMNILTVELETAASIDEMTRKEIIRQLTELTKKTIDLVEKVNPKLIGGFIFRYDDRKYDASLRHKIQLLSKEFEKNPYIK | 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... |
A0A0K1EBU6 | MIRSAPPVLPLGTRAYRGRLLTPVQAAFPGPARVARAGASSPPPASRPPASRPPASRPPVSRPPARPSTLPPRPAERARLRYIDDAILLVAPEGHIVSAEPAALTSFRGPILDLRPAVLIPGFVDAHLHFPQTRITGSASGPLLEWLDRSVFPEEARFHDPAYAAAVADDFIRRLLLAGTTTSVAFSSAHPTATDQLFDALHRTGLRGVAGLTLMDQNCPEALRLGHREAVPAMRDLIQKWHGKDEGRLRFVITPRFAPSCSRALLEAAADLADEHQLFIQTHIAEQPAEAEAALRACPWGTDYLDIYDRLGLLGPRTLF... | 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: 476
Sequence Mass... |
A0A800N641 | MAEQPAITANTNPAPGTDPLLEQPDGQGVAVNAPPGALASTADRAAPSVATGFFQQPAVQKSIPAVVVIVVILISIMVYSLFNGASFRPLFEGISQKDQSAIYTALIAADIPVKLDPVSGNVTVSTDDYHEAKLLLASQGLPESSIGGFNLIRKDQSMGTSQFMEKMRYKLAMEEELATSIATIDSIRRARVHLAIPKQSVFIRNREASKASVVIFQHQGRAITNGQVEAIIHMVASSIPFMEAESVSVVDSHGKLLHSKSASNDFNLTNEQLQYRNQIEDMYRTRVLSILSTFLGKENIHAEVNAEVDYTLIESTSQLF... | Function: The M ring may be actively involved in energy transduction.
Subcellular Location: Bacterial flagellum basal body
Sequence Length: 612
Sequence Mass (Da): 65609
Location Topology: Multi-pass membrane protein
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A0A1B9F970 | MDKQYLYTPRIVISAFRGGAGKTVASLGITRAIKDLGLKVSSFKKGPDYIDAKWLKLASGGPCYNLDPFLMDNETIKASFISRAQGADIAIVEGNRGLYDGVDIEGTSSTAELAKLINAPVIVILDCTKMTRTAAALALGLKNLDPDVKIKGIVLNHIVRARHERIVRQSIETYTGIKVLGVIPRFKKDPMPMRHLGVTPVEEHPDAENSISSVSKMIQENIDIDAVIDIAKSAGPLALSDGLEAQSVFHCLTQPKRVRIGVLMDEAFQFYYPENLEALQKNGAQIEFISAINTPKLPDIDLLYIGGGFPETQAEKLSKN... | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 10/10.
Function: Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source.
EC... |
A0A5N9GJY4 | MEKFKTQLKTWIEIGRPFSWTASIVPVCLGGAIAFRDEQFSLTIFLLALLASILLQAGTNVINEVFDVRSGVDTYDSPRASRTIVEKRLDSAVAYRGGVIIFLAAALIGIYLTYERGYAILLIGIVAILIGYTYTAPPIQFKYRALGVPVVFWTMGPLMVLSAYYVLAQSLTWEAFLASIPVGFLVASILHANDVRDIEDDARAGFRTLALATGRNAGAILHLMMMGASFAMVIVLAALVILPLWALITLIALPPTFQATLGMIRGGVGPEADPVKYLPRIDEATAKVHLLFGLLLSISYVVSGFSS | Pathway: Quinol/quinone metabolism; menaquinone biosynthesis; menaquinol from 1,4-dihydroxy-2-naphthoate: step 1/2.
Function: Conversion of 1,4-dihydroxy-2-naphthoate (DHNA) to demethylmenaquinone (DMK).
Catalytic Activity: 1,4-dihydroxy-2-naphthoate + an all-trans-polyprenyl diphosphate + H(+) = a 2-demethylmenaquinol... |
A0A522VIR0 | MPNHSRTGVIVASFAVAMMLRIIPWPDDWAAFNPDWVLLALIYWCIALPERVGIGVAWGLGLLCDVLGGKILGQQALVYTVVAYLCLKIYRRLRLHPITQQTLAVLGYLLFAQLLNYWILNVKGLGPIPWNYWLSSVYGAAFWPLVFLLLRYLRRTFHVQ | Function: Involved in formation of the rod shape of the cell. May also contribute to regulation of formation of penicillin-binding proteins.
Subcellular Location: Cell inner membrane
Sequence Length: 160
Sequence Mass (Da): 18300
Location Topology: Multi-pass membrane protein
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A0A522VS34 | MTARLKKFLYVMLPVPASIALFAALRSHLADDPWLHGMAVAVAPGAFAMILMAVALLGVIVWSFIKRLRYLDEEKFKAIFEGSNDAIMLLTHEGFFDCNQRTLTMFGLTSKQEFCGVHPSVLSPPRQPDGRDSHTAADENIQHALTHGQHRFEWLHRRKDGKNFSAEVLLSAFDYGGKKVLQATVRDITERKQAEKAMREWNETLESRVMQRTAELEIAMREAESASRAKSDFLANMSHEIRTPMNAVIGLTRLAMKTQLDAKQRDYLQKISHSAAALLGIINDILDFSKIEAGMLTIERVDFDLSSVIDHIANVCNVRA... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Cell inner membrane
Sequence Length: 987
Sequence Mass (Da): 107303
Location Topology: Multi-pass membrane protein
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A0A1B9F5L8 | MGGPDSLDAIRPFLFNLFSDRYIIRLGPSFLQRPIAWLIAKKRAPKSAQNYELIGGKTPLTEITIEQAKLLEGRLNEELGPKYGEEFKCVVGMRYWHPRTPDVLKELKDTGVKKVLGLSLYPHYSRATSGSSIEEFKSCCDSLGLSWDVIDRFPTHPAYISALCEVLDEGQKKIGNKDFHLVYSAHSLPKKFIDEGDPYLEDINATIRALESQTGIKGTLSFQSRSGPVKWLEPQTDIHLLELVKSGKKRLLCLPISFVSDHIETLYEIDILFKSIVKEAGGELFKTPGLNTRPSFINALYELVVEKLGENKWLR | Pathway: Porphyrin-containing compound metabolism; protoheme biosynthesis; protoheme from protoporphyrin-IX: step 1/1.
Function: Catalyzes the ferrous insertion into protoporphyrin IX.
Catalytic Activity: 2 H(+) + heme b = Fe(2+) + protoporphyrin IX
EC: 4.98.1.1
Subcellular Location: Cytoplasm
Sequence Length: 315
Sequ... |
Q55EN7 | MVGKREEKKRLLSDDSSITINDDGAGGAKFADEPEKDGCTTGILRALGLKEKKKPKKDMNKEKEFNDKFREISMLDKDSMLNRTGSPLSGLSEEEVKRRLGVYGKNVIAQVKPISWYKLLFVAFTHPFNIVLTIIATVSIATQDYATFAVVMFMVLLSAVLRFYEEHKSSKAFIHLKSLVKTTVTVLRTIKGVSTEVQIDIEDVVPGDIVPLKAGDVFPGDVRILESNSLFVSQSSLTGEFLPVEKGPDASEEQTTIFDTPNVGIMSTNIVSGSGIGVVFDTGCRTYISSISEILTSTQTTNAFDVGVKKVAYLLMGFGV... | 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: 954
Sequence Mass (Da): 105597
Location Topology: Multi-pass membrane protein
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A0A8C5DB74 | ILWVFMGSLIYLPVLGVSENRPSVLRGDELVVCPENERNVKYRGYVHSVHLDSVTLGFGAKLLNIFIEGMKFSVEFIMNRLTLRVQHRAVELAVTSNLRHVLFPAETSSSCQNSNLPKLTLFNRLLEKNPEQYHAIQHIVAGSSRPAPYLLFGPPGTGKTVTLVEAIKQIEKTQTNCHILACAPSNSAADLLCKRIVETHVDKHKVYRMYASCLDPRVVPEELKACSNLVGDTFSYPDKETLMSYKIIVSTMMTAGRLVTGGIPFGHFTHVFLDEAGHAVEPECLIPLAGLLDPESGQVVLAGDHKQLGPIVRSPFALQY... | Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
EC: 3.6.4.13
Subcellular Location: Cytoplasm
Sequence Length: 610
Sequence Mass (Da): 68810
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A0A7T3F8C8 | MAVPALAEGTPRLVVTDVDSTLIGQEVIDELGARAGARERIAAITERAMRGELDFAASLRERVAALAGLSASVLEEVREDLVLNSGARELVARLHARGDRIGAVSGGFCAILDSLGASLGLDRTLANGLEIADDGSGPRLTGRVLGPVVDAAAKRRALTAWAGELGVAEEATTAMGDGANDLLMVEAAGLGVAYCAKPTLDAAAAARIPVPRLDALLALLG | Pathway: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 3/3.
EC: 3.1.3.3
Catalytic Activity: H2O + O-phospho-D-serine = D-serine + phosphate
Sequence Length: 221
Sequence Mass (Da): 22512
|
A0A3B8X4D0 | MAKLPDPETVDPGELLRAYESGEIDLICVLGPTASGKTRYAVELARALGKAEILSADSRQVYAGMDIGTGKDLGEYGDVPYHLIDIVPAGMKFNIYQYQSDFADAWADVRRRGAIPILCGGSGLYIESATRAYKFEKDNGVPVSRLPQSVYYIGTLVTREERVARIDRRLEERLQEGLVEEIQSLLASGIPADDLIYYGLEYKFVTQYVLGQLSYEDMVVALGNAIHQFAKRQMTWFRGMERDGVRIHWVRP | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
EC: 2.5.1.75
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylall... |
A0A0P7X453 | MKNFETKILTPDGPVFNGLAASVNVPGTEGNFQILSDHASLMSALEPGEIRVNQTEGTGEVRFSVSVGFVEVNDNNVTILAEAAERVENIDVERAQKALDRAKERIQAAVNNSEIDVLRAEAALQRAQNRIQLARRSN | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane.
Subcellular Location: Cell membrane
Sequence Length: 138
Sequence Mass (Da): 15044
Location Topology: Peripheral membrane protein
|
A0A944D586 | MSKKRLFLLDAYALIFRGYYALIKNPRINSKGEDTSAVMGFMNSLFDVIKREKPDHLAVCFDKGGSTERVEIFPEYKANRAETPDAIRLAVPYIQEILKAMHIPVVIQEGMEADDIIGTLAKQAEKEDYQVFMVTPDKDFGQLVSENIFMYRPARMGNGIEIWGIPEIQKRFGVERPEQVIDYLGMMGDASDNIPGLPGVGEKTAKKFLAEFGSMENLLANTDQLKGKMKEKVSENAALGMLSKQLATINIHCDVQFNETAYELSTPDSEKVQAIFETLEFRRLTEQFLKLFFGPKEPQEATATNPEKTTATSSSKKADT... | 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: 948
Sequence Mass (Da): 106002
|
A0A938HWB6 | MPPERRNRAPTPASKPTAVPAGLTYRDAGVDLAAAASTKEIIKRLALTTHTAQVKGPAGFFAGAMEFPPGSDTLLVASTDSVGTKVKVAAAAHRYRGLGIDVVNQNVNDILAAGGEPIFFLDYIGLGRMDSKVVAEIVEGVAEACRAAGCSLIGGETAELPGMYAPGEFDLVGFVVGAVRKDRIITGADAALGDALIGLPSSGPHTNGFSLIRKVFGTDQDPGAINESPRELEGLSLADALLAPHRSYLSDLRPVLRDVRGLAHITGGGFFKNLPRSIPPHSTAVIERDSWAVPPLFRLIQSRGRILDEEMYRVFNMGIG... | 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 2/2.
Catalytic Activity: 2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ATP = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + ADP + H(+) + p... |
A0A7X2FTE1 | MNNPLPFPAGPNAATIPLILASGSEARAEMFRAAGLDVQLHPANVDEESFRNALRADRVTTSAAAEALAELKAMKVSGRYETGIVIAADQMLDCGGVWFEKPVDRDHAVGSLRALSGKKHQLVSSVVLFRNGARIWHHTGIAEITMRNLSNDYIDRYLDHIGDEVFQTVGCYKIEGMGMHLFSEVKGDHFTILGMPLLPLLDILREQGVVA | Function: Nucleoside triphosphate pyrophosphatase. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + H2O = a 2'-deoxyribonucleoside 5'-phosphate + diphosphate + H(+)
EC: 3.6... |
A0A3G3B6I0 | PSIDVSIFSLHLAGISSILGSINFIFTIMNMSPNNMMKEMNSLFVWSIFITTILLLLSLSVLAGAITMLLSDQNLNMHLFDP | 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... |
A0A097EMV5 | MKKTFTTILCSVMLLPSLSMAAPIPSGYDFIPIQEEMQIAQPVTEKHGMVSSQEALASQVGVQILKEGGNAIDAAVAVGFALAVTLPRAGNLGGGGFMIIHLNKEDKNIAINYREKAPAKASKDMFLNDKGDVDYNKVSGSYSASGVPGTVAGLIDAQQKYGKLKLAQVIQPAIKLAEDGIPVSYDLHQSLETAKPWLEKSPEAMKTFYKKDGSVYQVGEILKQPELANSLKLIAKDGKKAFYEGEIAHKIADAMAKNNGLITLEDLKNYDVQEMKPLKGEYRGYTIYSMPPPSSGGLILIELLNILENFPLSDYGNNSA... | 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: 580
Sequence Mass (Da): 62763
|
A0A3C2C7K8 | KGATTGISASDRAKTILAIMDEETKPGDLMRPGHIFPLRAREGGVLKRAGHTEAAIDLTRLAGLKEGGVICEILNEDGSMSRLPELLKFGEKHDLKVVSIEDLINYRMRQGDLVERIEERDIKTHFGDFKFYVFEEKPTEQIHYALTKGTWTTDEAVLVRVQSSGTYFDVFSRLSNGEHPLMQKVTDLINAEGKGAVVFINNVSNKENTLSRIQHFLNFQDGTNDQPTIAPNFRDYGIGTQILKDLGINKFKVITQNPNIKPIISGYDVEVSEMIAL | Pathway: Cofactor biosynthesis; riboflavin biosynthesis; 2-hydroxy-3-oxobutyl phosphate from D-ribulose 5-phosphate: step 1/1.
Function: Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate.
EC: 4.1.99.12
Catalytic Activity: D-ribulose 5-phosphate = (2S)-2-hydroxy-3-oxo... |
A0A0S8EZU1 | MESLDLNNPTVLGAIVAVAALILIGIIIGLVRARKKRALPEAPRAAPPEALEEERPKIEAPEAREATAEPTQPIQIEDLVPGAAPEPLPTLIPEPTVVPPPRPPADLGAFRSGLRSTRGNLISRLAGVFRKGRELDESMLDEVEEVLITADVGVHSTQRILEALRAKMSSGELGSADDAWEAIREESRTILASSGRGLSLRQKPTVILVVGVNGVGKTTTIGKLASRFDRQNKTLLLAAGDTFRAAAVTQLEVWGRRVGCEVVKGKDRADPGSVIFDAIQKAKDTNVDIVIADTAGRLHTKVPLMDELKKLGRTVEKALG... | Function: Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Acts as a receptor for the complex formed by the signal recognition particle (SRP) and the ribosome-nascent chain (RNC).
Subcellular Location: Cell membrane
Sequence Length: 420
Sequence Mass (Da): 44801
Location T... |
A0A1G3PNH5 | MACPPHPDRKSREGRSLRVLGIDPGLQRLGYAVLDVKGSELVPLSYGLVTTEKESQKNTRLYQVYQDVESLIEKYEPDVLGLETLIFAKNSRTAMVIGEVRGALLILGMAHGLTIREFTPLQVKTQVCGYGRASKSQVQNAVRILLSLAENPSPDDVADAIAIALCAAKPL | Cofactor: Binds 2 Mg(2+) ion per subunit.
Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair. Endonuclease that resolves HJ intermediates. Cleaves cruciform DNA by making single-stranded nicks across the HJ at symmetrical positions within the homologous... |
J2MPV9 | MNTLNLGERTIALDKDGYLADLDDWSTEVATALAAAEDIELSPEHWEILELLRGFYREFQLSPATRPLIKYTALKLGADKGNSLHLNRLFKGTPAKLAAKLAGLPKPTNCL | Function: Part of a sulfur-relay system.
EC: 2.8.1.-
Subcellular Location: Cytoplasm
Sequence Length: 111
Sequence Mass (Da): 12236
|
A0A1Z5HRT2 | MILMTFEEAYRVMRGKLLSGDPAAQFRGVSIDSRQIKPGELFFAFPGQRVDGHQFVVEALGKGAAGAVVMRKVHRWPQDKALILVDDTLKAFQSLSRYHRRQFEIPVIGVTGSNGKTTTKDMIASVLAESGPTLKNSANFNNEIGLPLTIFHLSYSHKATVLEMAMRGRGEIAELCYIAQPTGAVITNIGPAHYELLGSLENIARAKGELLEAIPPTGFAVLNGEDQWCIRLASRCRGKVLFYGRGDNADIRALDVRPVTGEGMAFTVRVGTDKESMFIPVLGEHNVLNALAAVGVGYQLGMSLQAIARGLKKVRLSPMR... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Involved in cell wall formation. Catalyzes the final step in the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the precursor of murein.
Catalytic Activity: ATP + D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-d... |
A0A0S8HP60 | MAILFYVQDIEYKLSGKIELKDLIKKIINLHNKKTGEINIILTCDEKLLDLNKKYLNRDYYTDIITFDYSEKERISGDLYVSIERIKENAKEYKVNEEDELKRVIIHGILHLLGYKDEKEKDKYKMRKKENELLKKINKKEE | 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: 142
Sequence Mass (Da): 17117
|
A0A5C7Q030 | MITKTSQELAYEQEESVIGALLKQPDKIELVKSIVAPDCFFVQRFRWVYESMLSLHERGLHIDAVTVGDELERHGHMQELGGRMALSTLRENNRWDNPESYAVKILDYAAKRELLEQAGVMATWSNNGRDASAIRDDMMKRLSEIRVPNHRASQHTQTMKEALSKNWDTVNNGNPHGVKTGFIDIDQLLDDALYPPDFMVIAGRPGDGKTSLLLSIAKNAAESGKRVAVFSLEMSNEQVVMRIISMETGVPFGAMRRGRMTREQWGKYNSAVEKYENLPLYLNDLPAITISQIQRVLRELQALHGKIDLVLVDYLQLGGA... | Function: Participates in initiation and elongation during chromosome replication; it exhibits DNA-dependent ATPase activity.
EC: 3.6.4.12
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 443
Sequence Mass (Da): 49947
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A0A0R0MA81 | MNFMPISNCRWHGLALVAAMLDQASKSLITKILALGEQVPVTTYFNLVYVLNPGAAFSFLADAGGWQRYFFIVLTLLVSACLAHMLRTQRPRCESLGLSLILGGAVGNVLDRITRGKVVDFLDFYWNEMHWPAFNLADVFISMGVWALIWASFREKQSKTTPDREAQTSPHGS | Pathway: Protein modification; lipoprotein biosynthesis (signal peptide cleavage).
Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, ... |
A9HQP7 | MSSILPHDVVVEELWGNARIDPLLAQERVLAERMNSRRQQEFSAGRAVARRAVQRLGLEPLPLLKGANGAPLWQDGVVGSITHCEQYCAAAVASNSAYRGIGIDAEPNKPLPEEVRPFILHPYEVAWIASAPASAMSWDTMIFSAKEAFYKLWSSVTGFWCDFKDGYVQIDRAKRAFSLSFQDNGRMNRLTNCHSMSGMFHLSNGIILTTVVANW | Pathway: Siderophore biosynthesis; enterobactin biosynthesis.
Function: Involved in the biosynthesis of the siderophore enterobactin (enterochelin), which is a macrocyclic trimeric lactone of N-(2,3-dihydroxybenzoyl)-serine. The serine trilactone serves as a scaffolding for the three catechol functionalities that provi... |
A0A3N7GTD5 | MKVYKFGGASVRDAASVKNVVRVLRNHGCDACLMVISAMGKTTNALENVVDSYFADRDFDELLLSIHRWHLSLMEELFAADHKIFGEVDAVFAGAKAFLDNNASRDYNFVYDQIISIGELLSSKIVSAYLQLSGMNNTWLDARDFIKTNAVYREGEVDWDLTETRIAELNTDAFYITQGFVASDANGNSVTLGREGSDYSAAIFAYCLNAEYMTIWKDVPGVMTGDPNKFPDAVLIDSLSYEEAIEMAYYGASVIHPKTLQPLKQKEIPFFVKSFVQDDKPGTKICKDSAPLQREVYILKEKQHLLRVSTRDFSFIAEDH... | Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 1/4.
EC: 2.7.2.4
Catalytic Activity: ATP + L-aspartate = 4-phospho-L-aspartate + ADP
Sequence Length: 329
Sequence Mass (Da): 36928
|
A0A3N5RD87 | MVFLWFRAIRIKFILASIIAVSNGIAISYWKTGSVDPGYALLTYFGIMCLHISVDLLNDYSDFKRGIDTNTKRTRYSGGTGVIPENLISPRLIYCVGVVFLILGGLTGLYFVTIKGIVILILLSFAIISIYFYSTNIVNAGLGELFVAIKGCMIVMGSYYIQSDTIDLTSVFVGIIIGLLSAVVLLVTSFPDYEADKKSGRRTLVILSGKQKSVKIVAGLIIATCGMIIGGAIFNVIPVFSTIGLLSIPFAVKAIHKLKRFNEPSQLVSSMANSIIYSRICGLLLAISFII | Pathway: Quinol/quinone metabolism; menaquinone biosynthesis.
Subcellular Location: Cell membrane
Sequence Length: 291
Sequence Mass (Da): 31625
Location Topology: Multi-pass membrane protein
|
A0A8C5GDD8 | MDNGNNDVQAELDSVEAELELVELQLSQLLQKQTDLTSRRNFLLQQLEEACEAALPSSSSSSSSCRLDLQHYDGSDFSWSADVQRHLSDSFHLSTFRKLQLRAINLTLSGRDVFVVMPTGGGKSLCYQLPAVLTQGFTLVVTPLVSLMEDQLMALKAVGVPAAMLNASSSKLENKSVLAGMVDPSSAFKLLYVTPEKIAKSKLFMSRLEKAHKAALLSRIAVDEVHCCSQWGHDFRSDYKLLGILKRQFPDVPLIGLTATASTSLLNDCSNILSVREPITVSSSFNRTNLYYEVRLKSSDSDAITDICSLIKNRYNQQSG... | Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
EC: 3.6.4.12
Subcellular Location: Nucleus
Sequence Length: 650
Sequence Mass (Da): 73003
|
A0A1B9F588 | MPILANPLCCQGWKCCIVSALHFPHSLANLAKSIIRGFRFKEQTKEKGIGMIIFVSGTDTDCGKTFVASHLCLAFKRLGVKVGYQKWVSTGNKDFSDDARMVYRLLGREDFPLPGSLETPYCFSIPASPHLAAEKDQAIIELDTLKKATLDLKKQLEVLIIEGAGGLLVPITRDVLLAQFVKEMDIPVLLVARAGVGTINHTLLSLNYIKQEGLKFKGLIMNEQEPTDPKIFMDNLKIIEQFSGISPLCKIHFSSSIDNSPLDEVIVAARKLLNES | Pathway: Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 1/2.
Function: Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to form a ureido ring.... |
A0A917UIH1 | MTLQDPTQTPLAPTPAPDLDSFGGTPATWIVFTVLTFALGGLLYPVVTTLLSGMLFPAQANGSLITRGGTVIGSELIGQPFSGDRYFIGRISAAGTGYDPTAASGSNLAGSNPALRERVQADSASIARREGVTPDQIPADLVTASGSGLDPHISPEGAALQVRRVARARGLSETQVQTAVRDATEGGVIGEPRVNVLRLNLALDALKPGTGS | Function: Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit acts as a catalytic chaperone that increases the ATP-binding affinity of the ATP-hydrolyzing subunit KdpB by the... |
C0EV71 | MNKKKSRNQFMISGILNIKKEPGFTSHDVVAKLRGIVHQKKIGHTGTLDPDATGVLPVCLGKATKLCDIIGDWDKTYEAVLLLGRETDTEDTSGQTLKEREVTVTEEEIRDIILSFQGSYDQIPPMYSAKKVNGKKLYELARQGIVIERKPCPVTLSSIIIKKIDLPYVTFEVTCSKGTYIRSLCRDIGEKAGCGGCMAGLVRTRVSSFKIEDGFTLSEVEAMRDADTLLEHIVPVDEVFLHLPAFFVKKEGEKLLYNGNPISLSLCALDENSSISNWQLYEDLSSNEQMKMEEADTEDLGKKEKSGKDGKQYSSYTVGN... | Function: Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
EC: 5.4.99.25
Catalytic Activity: uridine(55) in tRNA = pseudouridine(55) in tRNA
Sequence Length: 350
Sequence Mass (Da): 39393
|
D0JBQ3 | MNLHEYQGREILNSFSIQVPYGILASSPEESVEAAKIIFKRTGKKSLVIKAQIHAGGRGKAGGIQIAKTLDEVYEKSKNILGKFLITPQTSKKGKLVRKILLSEDIYSNELNSPIEYYLSILLNRDIEKDIILYSKEGGVEIENLSKKNPNKIYTEEIDPILGLQLFQTRKIAFNLGMDSDTLKNFSSFLISLYKAYKAYDALLLEINPLIKTFDNKIIPVDIKIVLDDNALFRHKKYAINNDSKDIDFLEKEANEAHLNFLKLEGNVGCMVNGAGLAMATMDMIKFCGGEPANFLDIGGSADKKRVEKAFSLILRDKSV... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; succinate from succinyl-CoA (ligase route): step 1/1.
Function: Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus r... |
A0A096ZWK2 | LIRAELSQPGALLGDDQLYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGISSILGAINFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTT | 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... |
A0A6P1YHZ1 | MPIPVLSDVPEALRFLSRLPIPSDGDLKREEHDRPFMERVAPAFPIAGGLIGLIGSIVLLIALTVHLGAWVSAILAIAVTTALTGALHEDGLADCADGLGGQSVERRLEIMKDSRVGSFGVLALVLATLLKVATLQALVAHSSLAAAAALVAAGAISRVAGPYMLALLPAARAGGLAAGAGRPSRSACATGAVIGIIIAFVMVVPSFGVTALISGLSFGIITFFGLRRLARAQFGGQTGDVAGAAIALVEIAFLLGLLIFARQF | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7.
Function: Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-riba... |
A0A5N9G9X8 | MIEGPPDGDWHYELITPGLLQVERVIRRVHAGRTRYQYAEVIEGAAFGHSLVLDGKTQSTEADEFAYHEALVQPSMIAHPNPVDVFVAGGGEGATIRQALSHKTVERVVMVDIDEEVVDLCRQHLPNHHRGSFDDPRLTLHFADAFAYLEETDERFDVVIIDVPDPLEEGPAYLLFTREFYTLLRNRLKPGGLAVAQSGPTGPAFYEQCFSAVANTAASVFPSVILSEAFVPAFASTWGFVISSLGPDPSALSPDEVDRRISERVSGELGYLDGITLRGMTSVPKYLREAVAKESRIITRDNPLYVP | Pathway: Amine and polyamine biosynthesis; spermidine biosynthesis; spermidine from putrescine: step 1/1.
Function: Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to putrescine (1,4-diaminobutane) to yield spermidine.
Catalytic Activity: putre... |
A0A7T3CGD6 | MHRSDQTPSPSPAAFAGRPVTGTSPGEAVPVGARVSLRVPASSANLGPGYDTMGLALGLYDELTVTRTAEGLAFELEGEGAQTVPRTPEHLIVRAIRAAWAAAGLTGELPGLGIRARGRIPHSRGLGSSASAIVAGVVAGSALLPEDLRLSEQALLQVCSDLEGHPDNVAPSLFGGLAISWGEEHPEGPRWRSARVPVDPRVHPVVAVPDYEVSTRLARELIPAQVPHALAAADAGRAALLVRALSGAPELLPAATRDYLHQEHRCEAMVPTARMVRALRDRGFAAVVSGAGPSVLVLAESADRAEQAAREMRHLGAEAA... | Pathway: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 4/5.
Function: Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate.
Catalytic Activity: ATP + L-homoserine = ADP + H(+) + O-phospho-L-homoserine
EC: 2.7.1.39
Subcellular Location: Cytoplasm
S... |
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