ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
|---|---|---|
A0A9C9FZA2 | LCRQFGAALTPSEMVSANALLFGSVKTRRRLVDPSEPEPRVVQISGADPEQMARAAQQNVDLGAQIIDINMGCPAKKVCNKMAGSALLKDEPRVVKILGAVVAAVAVPVTLKIRTGWDLQHRNAVRIARIAEDAGIHCLVVHGRTRACGYRSPAEYQTIASVKNVLQIPVIANGDISNAGQALDVLRKTGADGVMIGRASLGKPWIFRSIVAGLGNDNSSSEPSLRQQQYIVLQHLQAMYAHYGEAHGVRVARKHLAAYCRGLPRAADFRRQVYTLIDANAQQAFVREYYERLQRLPGVLQAA | Function: Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines.
EC: 1.3.1.-
Catalytic Activity: a 5,6-dihydrouridine in tRNA + NAD(+) = a uridine in tRNA + H(+) + NADH
Sequence Length: 303
Sequence Mass (Da): ... |
A0A6L7VQM7 | MNLFCSDGIPEIHTDPAEVPGMYMVLGRVSARIDDLAAEEHELIKGAHASRQQAFAAGRRLARTALTHLGISVRPILRNERRPVWPEFVVGSISHTDHLAASAVASSMQYRGIGVDVEKISAVDERVASRVLDDDERRWIDELELPEWRTAMFSAKEAIYKATNPITDEFLGFRDVTLTIDEEALSFTARTEDSNKAASLLASGRGYFHRIEGHWLTTYVIGA | 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... |
A0A1G7L995 | MNIAILLAAGSGTRLGASLPKQFLEVCGKTILEHTVEAFESSDDIDEIAIVTREDYVEKVSELIGERHPKLKRVLMGGKERYHSSIAAIEAYTNDEDNIMIHDAVRPMVSKRIIRDCVEALKMYDAVDVAVPATDTILQVDENGLICNIPPRKMLRNVQTPQCFKRRVIAEAYRRGLADPEFVTTDDCGVVHRYMPEVPIFIVDGESTNIKITFKEDIKTFESYLNR | 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... |
A0A928UKY5 | MKKKQKLQFKSKSTSSEKKKKKANKDFSFAAGGKKQKSTKKTPFSPFFSKFKNKGQKTTEAGASSNRVLGKVKRHPDGFGFLIPLDGFKEDLYISKQDMLGVMTGDKVEVSVKARGDRYSGVKLNMVERSQQKVAGVIHKVSDTEGIINDAGNWGSRLRVFWPENQSVEDRSWVLASVTSYPGDVEGFQAQLDLALPGNANDPIYDIKKVIHENSIPHVFSQNILNQLKEFESYTIDPKQFTDRHNLEKDLFVTIDGKTAKDFDDAICVSKNPKGFCLQVAIADVSHYVKVDTALDDEALLRGNSSYFPGHVVPMLPAKL... | Function: 3'-5' exoribonuclease that releases 5'-nucleoside monophosphates and is involved in maturation of structured RNAs.
Catalytic Activity: Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.
EC: 3.1.13.1
Subcellular Location: Cytoplasm
Sequence Length: 705
Sequence Mass (Da): 792... |
A0A3M0YBB3 | GGSDTTAVALAAALKADECQIYTDVDGVYTTDPRIVPEARRLPRLTYEEMLELASLGAKVLQIRSVEFASKYSVPLRVLSSFEEGEGTLIAGEEDMEQALISGIAFNRDEAKLTIMGVPDEPGIAYRILGPIADANIEVDMIVQNVGADGTTDFTFTVHRSDYDKALEILQRTAKELGAREVSGDNRIAKISLVGVGMRSHAGIASTMFKALAAEGINIRMISTSEIKISVVVDEKYLELGVRTLHEAFHLAEEGRAEVSSLWQPG | 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: 266
Sequence Mass (Da): 28789
|
A0A9E5AA14 | MLLAYWVSNTEENSMAEAPVPAPSGSRKKMIALIVVGVLSLVGISVGVTMLLTGGKSDPASAAKAKDSEADDATAKEDGDAEAAAAEEKDAPDDEAAAQGEEGAEKPSAYVSLAPPFVVNFLDEKKRTKFLKAEISLMAKSPKVQAAIKENLPAVRNALVMLFGRQVFEQLMTPDGKEKLRVDALFEVRAVVTKVAGAKTGKGIGDLFFSSLVMQ | Function: Controls the rotational direction of flagella during chemotaxis.
Subcellular Location: Cell inner membrane
Sequence Length: 215
Sequence Mass (Da): 22656
Location Topology: Single-pass membrane protein
|
A0A3M1DMS2 | MILRRLIYREITRSFLAVFSLLTLIYLSTRFIRYLNQAVSGKIGADQILEMLGLRLTTSLVVLLPLCLFVAILLVFGRMHRDNEVVAIENAGLGIPFFLGTVLRYAAAAGVVILLLATFIAPRAEQRMAEIQARARSEADLIGITAGKFKEFSRGERVIYVEKMNDERTRMENVFLQVREGDKLGVLTSGSAALETDPETGDRFVVFRDGRRYDGVPGQLDYAITEYEKYAVRIDRGQARARKTIESMPVRTLLRGGRREYLAELQWRVSMPLSALLLALFGTLLAFSRVGREPYLGAVTAVLIYFTYSNLLGISKSLID... | Function: Part of the ABC transporter complex LptBFG involved in the translocation of lipopolysaccharide (LPS) from the inner membrane to the outer membrane.
Subcellular Location: Cell inner membrane
Sequence Length: 368
Sequence Mass (Da): 41858
Location Topology: Multi-pass membrane protein
|
A0A9E3M410 | MTSDIDNIIRPEIAGLKPYVSPSYEWRVKLDLNESPFDVPPEVKREIWKRVKRLQWQRYHDEFERPLVEKLADYENHDPDGVLIGNGSNELIFHSLLSVIRHGDTVLFPEPTFSLYRQNITVLGGQPESVMLNEADFSLNPDKLLAKAGAAGARAIVLCSPNNPTANLIPNEDIERVCREFGGLVLVDEAYTQFADGDAFELLERCQNLAILRTFSKAFGLAGLRFGYLLARPELAREIDKVQLPHHVSFFTQLAASTLIENAAVMKQRVESLKRERDSLIGRLDCIAGVSPLPSQSNFILIECTAVAARELFERLLARG... | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
EC: 2.6.1.9
Catalytic Activity: 2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Sequence Length: 358
Sequence Mass (Da): 40266
|
A0A9E5LZ95 | MRAHTRAFTLIEVLVALAVIAVGAAAVLSSLDTAARAADRVRERTFAGWVAMNRVVETRVLRATNLKESSADGEVEMAGRRWHWEEKVGPTAFTGLWRIEVRVRAADSTDWLAERQGALGESLAPAGSGRDPWDINAVNP | PTM: Cleaved by prepilin peptidase.
Function: Component of the type II secretion system required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm.
Subcellular Location: Cell inner membrane
Sequence Length: 140
Sequence Mass (Da): 15250
Location Topology: Single... |
A0A661FFI6 | MDKREVGRSFSEAAVSYDRLAELQRQVGEELLSRLDGEAASFSNIIDLGAGTGFCAEKLAQRAAVSRLLALDIAPGMLRQARERMASQGNVDFCVGDAEQLPVGSATVDLLFSNLAIQWCDSDRLFEGFYRVLKKEGLLLFSSFGPETLRELKVAWSHVDGHQHVNKFSEIDRLERLIREAGFKACSVERVQLKRHYGSVFELMRELKGIGA | Pathway: Cofactor biosynthesis; biotin biosynthesis.
EC: 2.1.1.197
Catalytic Activity: malonyl-[ACP] + S-adenosyl-L-methionine = malonyl-[ACP] methyl ester + S-adenosyl-L-homocysteine
Sequence Length: 212
Sequence Mass (Da): 23626
|
A0A523JLA4 | MTIANLARPEIRALKPYAAAVQVEDNIRLNANEVPWTSNHDRFRRPLNRYPEIRPAALTVLLAEHYGCQPDKLIVTRGTSEGIDLLIRVFCRAGQDSIATITPTFSMYRHYAAVQGAQLIECETSRDEGFAIDIDALLLACDDATRLIFVCSPNNPTGNVIPRDDLIRLLESRRNKSAIVVDEAYIEFAQQSSIIELLDRFENLIVLRTLSKARAYAGARCGSVIAAAPVIQLLSTVQAPYALATPVVECVEKILQPECIEEADVWTRKVVAERERLIAAIRELPFVRRIWPSSANFFLVQVQDAAALLEQSASDRILLR... | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
EC: 2.6.1.9
Catalytic Activity: 2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Sequence Length: 353
Sequence Mass (Da): 39294
|
A0A661ES86 | MIEPITYIRPQFDSGCLQSPLYADHYFGAADALAESRHHYLDANRLPERFTRCRQFAVAELGFGTGLNFLLTWQAWRQHAPATAHLDYLAVEKHPIAPESLQQIFALWPELAAQGQALLDLYPLALPGCHRVRFDDGRVSLTLVWGDAAEQLANLDGQMDAWYLDGFSPRSNPQMWSETVVQQVARLTCPGGTFSTFSVAGAVRRAVEKAGFSWQKQLGFGDKGQMLVGSLQQQAVTTGSAPWFNWPATKGDRRVAVVGGGIAGIATAYALTARQFEVTLLEQSTQLATAASGNPGGVISPFLAADHSLASRFSAAAFAF... | Function: Catalyzes the last two steps in the biosynthesis of 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at the wobble position (U34) in tRNA. Catalyzes the FAD-dependent demodification of cmnm(5)s(2)U34 to nm(5)s(2)U34, followed by the transfer of a methyl group from S-adenosyl-L-methionine to nm(5)s(2)U34, to fo... |
A0A3M2D2P2 | MAEEKALIDPDATPPLLPGMANLSVLRQAGILLGIAASVALGVAVALWSQTAEMKPVGHFSPDKLSDVINYLEQNKVDYKLSPDGTLMVEEAKLQKVKLDLTAQGLTGVGAADQFLKQDSGFGVSQRLEQARLLRAKENELAASISRFAGVKAATVHIAIPVRSSFIGRKEQPRASVALQLFTNSPLKEEQAEAIVDLVVGAVPGLERHRVAVTDQFGRLYNTSSNDAETRAIDKEFKAELKKQKELEQKIAELLSPIVGPENFTAQVTVDLDFTEKEQTQQLFNPDEPAVTEEKLMESTNGEGEAAGIPGALSNQPPAA... | Function: The M ring may be actively involved in energy transduction.
Subcellular Location: Bacterial flagellum basal body
Sequence Length: 553
Sequence Mass (Da): 60107
Location Topology: Multi-pass membrane protein
|
A0A924V5Z1 | MKLDILSPYYWFLMAKKNSPKIPIQMSIPIISVGNINTGGSGKTPFIHFLVAEIKAKFPLKKIVIVSKSYKASLKFPQEVTELDLSRPDIFGDEPCLLKSIVDADVWSGPIKYKTLAAALRLKTYDLAIIDDGFSHRQIQRQLDIVLFDVSRSRAHYQIIPFGFMREPWSALKRASLVILTKLENQDKGRIHFFESEIQKYQKNLLSLDFVTKLNLKIKNIFLVTGIGNPEALVQNLKLLGYNVVKVQLYEDHYKFPLTEQIKIWQEYLSLKAESELEIVTTSKDLIKISHPELKQNLKLIELNISMSDKKLKVLHEKIS... | Pathway: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 6/6.
Function: Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form te... |
A0A6L8CML3 | MESCRLAHRHGPEQADRPGGPRVKGRVLGFDFGHKRIGTASGNRATGTTAPLETVAATRQGPDWPRLVGLVHAWRADELVVGLPLHMDGSESHLSREARRFGDELASRTGLPVALVDERLSSSEADDVLTLGSPPGKSRHRRRLAHRDSIAAELIVRTYLADNPAPTCNR | Function: Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
EC: 3.1.-.-
Subcellular Location: Cytoplasm
Sequence Length: 170
Sequence Mass (Da): 18475
|
A0A2G6EPI5 | MHTLVINCGSSSIKYGLYDTALEEVDFGRVERLLSADRGHGHRRAIAGILEKYADSDVGRVGHRIAHGGSEYTDSALIDQAVLDAIAARIPDAPLHNPYSLAAIEALREARPDLPQVAVFDTAFHATMPDTYREYAIDHEVAAREGIRRFGFHGISHQYASGEAARVLGRDIGKLKLVTLHLGNGASACAVEYGRSVDTSMGNTPLEGLVMGTRSGDVDAGVLLTLMRDGYGVDALEKLLINESGLKGLSGVGADLRDIEKAAAEGNDRAQLAIDVFAHRARKYIGAYAATMGGLDGVVFTGGIGEHSHIMRRRIVRDLE... | Cofactor: Mg(2+). Can also accept Mn(2+).
Pathway: Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis; acetyl-CoA from acetate: step 1/2.
Function: Catalyzes the formation of acetyl phosphate from acetate and ATP. Can also catalyze the reverse reaction.
EC: 2.7.2.1
Subcellular Location: Bacterial microcompart... |
A0A3M1UM88 | MLADGIRRLGLEIPPERQRRLLDYIQLLGKWNRVYNLTSVRKPQDMIARHLLDSLSVYPYVEGPRVLDVGTGAGIPGMVFALVQPDWELVLLDSSNKKLRFVRQAIEELGVENASVAHVRVEDYRPEAPFDTAVSRAFSSLEDMYQACRRLMKPDGKVLAMKGVYPVTEVEALSDPEVLLDVIPLAVPGLQAERHVVMLSPR | 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: 202
Sequence Mass (Da): 22... |
A0A969F2A3 | MKPLRRLLDGASGERRRDLEVLLCHVLGKSRAWLYSHGDEALPGVAARQLDTLLPRLSAGEPVAYLIGHKEFWGLPLFVSDAVLIPRPETELLVELALNRLPHRGTVLDLGTGSGAIAIAMRSERSDCQVTACDVSAAALSIARANAQRHTLDITFCEGDWCSGLASFDLILSNPPYISADDPHLPDLRFEPSLALIAGVDGLDAIRRITAQAPSHLNAKGHLIIEHGFDQGPAVRALFVAAGLRGLPRSPIWRGASVLRSARNERRSTASLQSSDHVAADRCGGSAAPARCARTDRGARWTRLARCVVSRSRRCGPAGT... | Function: Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif.
EC: 2.1.1.297
Catalytic Activity: L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-methionine = H(+) + N(5)-methyl-L-glutaminyl-[peptide chain release... |
A0A520T501 | MLSKKDYIGIFGGSFDPIHKGHIESLKSVTEQLNLSKVLVIPNKVSPLKDLSVASSLEKIKMLEIAFKDFKEIEIEDYELKKEGSSFMIETLQYLDKKLGKKKHFLLIIGEDSFQSFHRWKNYQHIIKMTSLLVMNRPGLKNDLTGKAIELHQDCIENTYGDNNFKKGKIYFIKIKPNPASSTHIRENIDDESVLSEGLDDDVLKYLKEQKIYNKHD | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
EC: 2.7.7.18
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide... |
A0A523LZL3 | MTLLIPDFSTTHVVVAGDVMLDKYLFGTTSRISPEAPVPIVHVQQTDERPGGAANVAVNLAALGATTRLIGVVGKDSAADSLQSILEELGIDCDFHRADDRPTITKTRVQSRGQQLIRLDQENVAELGDDSIVDTLKAAIGNAGAVILSDYGKGALTDVTRMIAACRDAGVPTLVDPKGSDFSKYRGASLITPNQSEFEAVVGVCNSDEDLVSHGNTLLTELALDALLITRSEKGMLLLETGLEPLFLSTQAREVFDVTGAGDTVIATLAAVIASGQDLSSAAALANIAAGLVVRKIGVATITPSEIRVAMHQRGQGGRG... | Pathway: Bacterial outer membrane biogenesis; LPS core biosynthesis.
Function: Catalyzes the ADP transfer from ATP to D-glycero-beta-D-manno-heptose 1-phosphate, yielding ADP-D-glycero-beta-D-manno-heptose.
Catalytic Activity: ATP + D-glycero-beta-D-manno-heptose 1-phosphate + H(+) = ADP-D-glycero-beta-D-manno-heptose ... |
A0A969SGQ9 | MHCPCLKFLFIAVVLLILSACGSAPKSTAPTTPTATTRPATTGGYYQDDGPGATKPSNLDSIADAIPKQEKFHSGANRPYTVFGRGYAPVVNNDPFRQTGIASWYGRKFHGNMTSIGETYDMYAMTGAHPTLPLPSYVRVTNPANKKSVVIRLNDRGPFHQDRIIDLSYAAAHRLDIVTRGSAPVLVERVFAGDASAPTPASAATQVSVPQTVITTTPISLEGKQLFIQLGAFSVQENAKIFSARMVRELDWNREPVEVVFKDNLWRVRLGPYQTRIEAEAIQARIKQSHDFSAVISTLKFYSMTLIFRTLFLASIAFFP... | 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: 338
Sequence Mass (Da): 37543
Location Topology: Lipid-anchor
|
A0A8T7BPN8 | MAGPALPIVTLIFLIYGLAGPYLPGFLSHGGYSLDHIIDINYFGTDGTFGIPLGASATYIAMFIVFGAFLARSGLGDLLMDIALGIAGHRQGGPAKVAIIGSSLHGMMSGSAVANVLTSGTATIPLMIKMGYRREFAGAVEAAASAGSQIMPPVMGIIALIMVQYTGIPYIKIAGYALLPALLYFFGVWMVVHLESVKLGLVGLPPDQLPDWRLKLKQKGHILVPVFVLIILLIVGFSPAYAVSYATLSVVIVSWFKKESRMGMDDILDALHSGGKGILMIAVATAAAGIISGMFGLTGIGIRFTVMLNDMASGSLVLSL... | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 414
Sequence Mass (Da): 43362
Location Topology: Multi-pass membrane protein
|
A0A8T7CFV1 | LPLGGYVKMLDERDCEISPQDQGRAFNHKPVSARLAVLAAGPLFNFLFAILIYWVSFMMGVTEVRPVVGAVVADSIADKAGLRAGDEIIAVDGNVTRSWQEATLAIIDDLVDDGQINVSLRENTGSERVIKLDAVAEKQALTEPGKLFEGLGIRRMPETVPAKVGRIVAGGAAEKAGLQVDDLIVGMGGQSIETWADVYEFVRARPGESSVLRVLRNDQPRELPIVIGEGVDQGQAIGLIGVAVADPRIEFQTRLRYGPIDAMVKAVDFTGEMTVFSVRMLWRMVTGDFSVKNLSGPITIAEYAGATAQMGFDVFIKFLA... | EC: 3.4.24.-
Subcellular Location: Membrane
Sequence Length: 388
Sequence Mass (Da): 41819
Location Topology: Multi-pass membrane protein
|
A0A937I6Y5 | MTKKIMIVSSGTGGHVIPALNISELLLSKGYEIIWIGTKNGIENRLIKNNKIKLFHITSTGIRGKNVFDKVKGILNFVKSIFQSIRIISKNRPLFVFGFGGYVSTSVSLAGFLYRLPIYAHESNSIPGSANKLNNLITKKTFQTFPNTFPKQSKVILSGNPLKKNFKNITCPDEKYQQNRHKTNILIFGGSQGAKFFNENIPASFSRFSNSIHIIHICGVNNKNKVEEQYKKFNIDAEVIEFSYEMDILYEWSDLIISRSGSMTLSEISISGRASILIPYLYATDNHQWNNAKYLCKNHAALMAEENYEFRENLERSIKR... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II).
Catalytic Activity: di-t... |
A0A2D9XJ69 | MSFDSLNKNDLSFWLAYIESLNIKEIELGLNRVIQVAQNLGVEAVAEKTIMIAGTNGKGSCVAAMEVILRDLGYKVGCYTSPHILRFNERIKLDGAEIAEEILCAAFLAVENARGDIKLTYFEFTTLVAFLIFSKRKLDFALLEVGLGGRLDAVNIIEADVAVITSIDLDHQEWLGKDRESIGYEKAGIIKKNRPVVYGDSNPTKSVLATAESLNSKIFLKGRDFDHQIKTEDESFDWSGGRDMNENISGLPIPNLAIENVSIGMQALSLAGIEMDVKVLRSSLRRLYLPGRFEKCVDALTGVSVVLDVAHNPAAASMLA... | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 2/2.
Function: Functions in two distinct reactions of the de novo folate biosynthetic pathway. Catalyzes the addition of a glutamate residue ... |
A0A6L7MZY6 | MKRMLVNATQPEEVRVAMVDGQKLYDLDIENHSLEQKKGNIYKGRITRVEPSLEAAFVDFGGERHGFLPFKEIARSYHRGGGRRGGQEREDGRNGRTAIADAVSVGQELIVQVEKEERGNKGAALTTFPSLAARYLVLMPNNPRAGGISRRIEGEEREALRQSLSGLNIPEDMGVIIRTAGIGRSAEELQADLDYLLQLNDAINEAGKRRGPALLYQENTVVVRALRDCLRHDVGEVLIDDEEAYDQARDFTEQVMPNFLGRIKRYNDAVPLFSRYQIESQIETAFQREVRLSSGASVVIDPTEALVSIDINSARATKGA... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Endoribonuclease that plays a central role in RNA processing and decay. Required for the maturation of 5S and 16S rRNAs and the majority of tRNAs. Also involved in the degradation of most mRNAs.
EC: 3.1.26.12
Catalytic Activity: Endonucleolytic cleavage of single-stra... |
A0A2E9FJM5 | MGRIKDSFERAENQESKTLITYYVAGDNNLNFSKKVFLSLLSHADIIEIGVPFSDPMAEGSVIQRSHERALSSXISFKKILSLVKELRIHNQDKPIVLMGYMNNFLSXGESLFKKIKNAGVDGLIIVDLPYEESXFFYNKLKDIDLDLIRXISPTTPKKTIEKIVKFSSGFLYYVSFRGVTGAKLSNFKEVQDNVKYIKSKTKLPVVVGFGIKEGEIAQKMSKISDGVVIGSRLIDIVQQNNFRLNDSLKFLEKSLKKFRRDVRKK | Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5.
Function: The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
EC: 4.2.1.20
Catalytic Activity: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-s... |
A0A6L7N556 | MTDFGRRHRLVAPRRFREVFGQRNLRGGRYFTLYQLPNDVGVHRLGLAVSRKVSRSAVGRNRIKRQVRESFRRYREGLAADPESAGGIDFVVVARPLASGTENSELRRDLDRLWRLVN | Function: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of... |
A0A923P3D3 | MGQPVRVRVSPFAPREQSVPFPACDKQSDKERTLTDVQVSLETGAGLERRLRVQVPASRVEQELEARFRSAARTVRLKGFRPGKVPDGVVRQRFGPQIRQEVIQEVVQSSYSEAIAREKLRPVGSPRIESEPEVPGEGIAYTAIFEVYPEFSVAGLDAMVVEKAEVSVTEADIDQTIERLRKQRGQWQPAGRAAVAGDRVVLDFAGTLGGEPVEGGKAERFAVVIGEGRMLPGFESALVGTTDGADKSFDVTFPADYYEEKLRGQTVTFQVHVHEVTALELPAVDAEFIRRFDVASGDLAEFRRLVRENLEREALAKVQA... | Function: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
EC: 5.2.1.8
Subcellular Location: Cytoplasm
... |
A0A1Y4GT85 | MWLRFAVTGAWDGARASAFLRGQGMSAALLRRIKTEGPGILLDGVPVYAGHAVAAGQTVSVRLPPEQDTTVSPQPIPLRVVYENDHLALIDKPAGMTVHPTLGYADGTMANAWMGRLAQRGEKGAFRPVNRLDKDTSGLVVCAKNAFSAALLAGEVEKRYLAIVCGEMPPGSGEIDAPIGRCEDSIIRRRVHPSGQPSCTRYTVLAAGGGYSAVRLHLLTGRTHQIRLHMAHIGHPLAGDWLYGYGPTDTIRRHALHCFAVRLPEPMRAPEWVFSAPPPDFQRLYRVILDAKRW | Function: Responsible for synthesis of pseudouridine from uracil.
EC: 5.4.99.-
Catalytic Activity: a uridine in RNA = a pseudouridine in RNA
Sequence Length: 294
Sequence Mass (Da): 32051
|
A0A1X6NIA4 | ADGAPPAATVHLIVDRREARGSGAVRAAFLDRLGREAGLGGRVVERTLAVGDAVLVARITPAGAAAFAGAPPAGTEVVLDELIERKTVDDLASSFRDARYEEQAYYMAAAGLPSLVYVVEGDPDPPGEGAGGISPRGKAHLASLAVTAGFVVKHTRNLDETAAYYASLVRHRERRLATAGGLEGYLTAKRAAATAASAGAAAAAAAGGGGGGGGGSGGSGSGHKAPARTLQQLWALQLHVLPGVAAGRVADVMAAGYTTPAALAAAYGGVTDGAAGAALLAGIEPAPGHRRVTAAVSSYLYNLFCAKSYGNVLL | Function: Interacts with EME1 to form a DNA structure-specific endonuclease with substrate preference for branched DNA structures with a 5'-end at the branch nick. Typical substrates include 3'-flap structures, D-loops, replication forks and nicked Holliday junctions. May be required in mitosis for the processing of st... |
A0A661DU28 | MSLDFGPVQTLGFAVLVLYTGIFLVARLRFLSENNIPVPVVGGFLFALVASFLLGQFNIRFGFDMSMKEPMMLAFFSCVGLGADMRMLSKGGKQLLLFVVACLLYLIIQDGIGLVTALSLDLHPLVGLLSGSITLSGGHATGAAYAQQFSDSSNIAGAMELAMAVATFGLILGGIIGGPVAGRLIKKHNIQVPHKAPDEHGIVLQHDDSAYAPVNEDNFLLAFFYVLLSIIFGKLISVWFAAHVMTLPDIVWCMFVGVVIGNITIHDRLPKAHQPSIDLIGNIALSLFLVMALMSLNLWGMISMAGPLLVLLGTQFIGMV... | Function: Catalyzes the sodium-dependent transport of glutamate.
Subcellular Location: Cell inner membrane
Sequence Length: 405
Sequence Mass (Da): 43227
Location Topology: Multi-pass membrane protein
|
A0A2E7U4U8 | MVFVHEWQRKPAGKYLALVEQRVVNGLPSNRTMSHSFPKQARILDGSVYSSVLKRPQKKLVTGPVQIKARDNGLEFARLGLVVPKRGTARAHDRNRMKRTIREQFRLTRNSLPPKDMIVQVFSKVSVEQLRDILSRQFAALSAGRV | Function: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of... |
A0A6N9AUN4 | ISCVLFARTVYRNKIRQIPDHGREVVLEGYLTIFSQRGSYQFFVENVQIESSKEGELYQEYLRLKKELDELGYFDPENKKSLPTFPRRVGIITSPTGAAVHDIIQAFKRRNPTIQLTLFPTSVQGENASKEITAAIELANQLMNVDVLLISRGGGSLEDLSVFNDRSVADAVFLSRIPIVSGIGHDTDVTIVDWVADKPMPTPTAAAEMISTPSINEMLLKLSTFETDLQNRVLSRLGEFTQQIDLAEARLVHPKERITNLKSQFSAYGKRLVSEISRTVDTQSGTVKVNYQRLLNQSPTPRIDQYSKNLVSAADRLMQS... | 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 Location: Cytoplasm
Sequence Length: 394
Sequence Mass (Da): 43812
|
A0A962SAG7 | MNDKSQAIPEQPSHSLFGEELNIDFQYYLRVLRKHKWAIIAMTVLVTGLAAFYAFTATPIYQSTATLLIESKKANIVSIEEIYGFDGNNEEYYQTQFELLKSRALAEKVIDKLNLKEHPLYVNSDDPGPFSLNTLRHLGLGSDSEEAATQPGESALEPISDIITAENTSATDPVVGDEAAGDLFAGTAEFTAEDRELQLLVNKFTNALTIEPVRRTQLVKITYESPDPELAALVANTVGDTYIESYLDAKMEMTQKAAEWLSDRLGGLQLKLDESERRLIEFREEHQLIDVAGTVGALNEQQVTIATTALSTAQRELAEA... | Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
Subcellular Location: Cell inner membrane
Sequence Length: 815
Sequence Mass (Da): 90626
Location Topology: Multi-pass membrane protein
|
A0A9C9YST5 | MKILFATSEAFPLVKTGGLGDVAGHLPLALQQLGAEVTLALPAYRSVLEKVDAPVVGWVSTSHGYALLRETTLESSGPRLWLIDHPTFSERPGPPYVDESGEPWRDNSIRFGAFSQALAKLAIGHSGAKEHFDIVHCNDWQTGLVPAYLSVEPERPATLFTIHNLAYQGIFPASCLETLHLPGELWSPLDGLVFHGQLSFIKGGLVFADRLNTVSPTYAREILDDAFGYGLTGLLNHRKRDLSGILNGVDLDEWNPATDRYIPQNYSSATLDDKAINKAALQKEFGLPPDPGAFLIGNVGRIVEQKGVDLIIDALPLLMK... | Pathway: Glycan biosynthesis; glycogen biosynthesis.
Function: Synthesizes alpha-1,4-glucan chains using ADP-glucose.
EC: 2.4.1.21
Catalytic Activity: [(1->4)-alpha-D-glucosyl](n) + ADP-alpha-D-glucose = [(1->4)-alpha-D-glucosyl](n+1) + ADP + H(+)
Sequence Length: 488
Sequence Mass (Da): 53118
|
A0A496WKU0 | MTLRHGIHEIWLVLLLLLGAAAFSSARAGVRVLHQEPAHYPGIARVARLEGRVEVSVVVATTGNVTSVRVINASHPFFRQPAKLAAWLSRFSPAVLNGVAVVDSVHLSFEFSNDPDEIALGTIWERDSREQEIDLVRDQV | Function: Interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates. It could act to transduce energy from the cytoplasmic membrane to specific energy-requiring processes in the outer membrane, resulting in the rele... |
A0A8H6Z7Z5 | MSSVVRNGRRGTRAIELCIQIFVLSIIAYGLYITTVEIAYKWLIIYHGQRIIGGLYLTTVLFLISVLGLVYLSLIAGRGTHNVPRYSVPDTDDLTEPYECIDSDGNLATCAKCNGAWKPPRTHHCSTCGVCRMEFDHHCPWVGNCVTRARMKRFLALLFLVPVAYSVSILPVYHPLMRYMALALDVSHHDPWANQVWWDWYGSWIFFGGPLGRWIFGMVLGFRILKAVRRDDLPLLEQPSLRLFSISALGVIFSLFTLILAIWTIKDLLRGLTTLDAMQESRQKQAPRFVRVPRKASCTPRDDGAEDNGADDEIAGSRNV... | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 380
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 43092
Location Topology: Multi-pass membrane protein
|
A0A8T7JEC5 | MISAALSKIAGVLDGQLIGEDGEFIGVCLDSRRLVGRNLFVALRAERDGHDFASSACQRGAAALLVERPLALDIPQIVVADTSLALTELASWWRDQLRQTRFFAVTGSNGKTTVKNMLAGVLSKQGTTQWTQGNLNNHLGVPLTLFSISPSCRFAVIEMGASGPNEIAKLCSLVRPHVSIGLNAGNAHLEGFGTEENLRRAKGEIFARAPMQSKCVYWVEQPMVEDWLQQIGARQKAGFGLSSSANVRLDGEWIVTDGEQCELQLQLAGQHNRLNAAAVIAATVPEYCDLATACAALSQVMPEPGRLEVLLDGQIRVIND... | 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... |
A0A348UQK3 | MAVEQRVGSAGGKTWGSVRLGHLFGIEIRLDPSVLLMFALIVITLAQGLFVEWHPDWSKTRQWTTALFAASALLGSLLTHELAHALAARSFRIRVPRITLFLFGGAAEIESDAETPGAECVIALAGPLLSLTLAIAFAVIGQSELSEAQRKLLLSDPAQALASSGPLTTACLWLASINLMLALFNLIPGFPLDGGRVLRALVWRFSGNFVLATRVAGAAGQYVGWLLMLSGVWLLLGQGRPGGLWYVFLGWFLSHLARASLTDVVMRHALGRQKVRDLMQTRFDSVDAGVDVHEFVEQYLLRGPQTLWPVREQGIITGMA... | Cofactor: Binds 1 zinc ion per subunit.
Subcellular Location: Cell membrane
Sequence Length: 420
Sequence Mass (Da): 45444
Location Topology: Multi-pass membrane protein
|
A0A0V0J665 | MDLNSLVRTFAVLIFGLSSTEADLVNIHMYTNPNCTTPCDGSTNFLYDVISRTSKGVVHFILPGNMTKTPISILMVEAANSKEIQVNWTRFLNRTTSLFHESIILDSKINSYGIILNEICTFSDINDDAEITELQVQKECLHFLGKNLLWSHTVTRSARAITFLYMANHSLESKDNFDHYPQKCRWSPGKGRFFSCSRSRYFIGTYGE | Function: Required to protect lysosomal transporter MFSD1 from lysosomal proteolysis and for MFSD1 lysosomal localization.
Subcellular Location: Lysosome membrane
Sequence Length: 208
Sequence Mass (Da): 23684
Location Topology: Single-pass type I membrane protein
|
A0A2E1KC23 | MKKPRNIPKQWGKVRIIGGLYRSRFVKFVQAKGLRPTADRVRETLFNWLDSVVSNAKVLDLYAGSGVLGIEAISRGAKHVVFVDKNPEVVLQLNRTLVSFEIQNCLVLETSANEWLSASNASARGSIAGSQLAEVGPFDIAFVDPPYKECSILESCNLLENSGLLKPNSNVYVESDDAIHQALMPTNWQCVKSKKAGKVYFYLYQRFKRDS | Function: Specifically methylates the guanine in position 966 of 16S rRNA in the assembled 30S particle.
EC: 2.1.1.171
Catalytic Activity: guanosine(966) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(2)-methylguanosine(966) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Length: 211
Sequence Mass (Da): 23571
|
A0A2G6EX74 | MTSECYSDARYFEAGLYGLADIQQSIAHLIGQATYLSDTEKQQLIDCCFFAAQAHAGQVRQSGEPYACHPIKVAGILAKEVHFDLPVLQAAVLHDVIEDTPVSKDELEEVFGAEVAGLVDGVSKLEKDKGLSAKELQARTFEKLVHAMQADPRVVMIKFADRMHNMQTLGVLRPDKRKRIANETLDVYVPIASHLGMFIFKTELEELAFKHLYPWRYQVIQRWVKENVKRKEIVAQTIKELHLQFTKQGVNATIRERRRNLLNIYRKLKKNRLKRRPFERTSIPFIVLTDSVDDCYRALGVIHQFYMSVFHKLTDYIASP... | Pathway: Purine metabolism; ppGpp biosynthesis; ppGpp from GDP: step 1/1.
Function: In eubacteria ppGpp (guanosine 3'-diphosphate 5'-diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance.
EC: 3.1.7.2
Catalytic Activity: gua... |
A0A947LDU7 | MKLLLHPLAKPMVFCLALLPFAWLFYAAATDQLGANPAEALIRSTGDWTLRFLCIVLAVTPLRVISKTPALARFRRMLGLFVYFYVLIHFLSYSWLDMGFVVPDIAADIVKRPFILVGFTSLLLLTPLAATSFNRAIRALGAKRWQLLHKLVYVVAGLGLLHFFWMRAGKNNFNEVFVYLFILGSLLGWRVWHFGNKKLF | Cofactor: Binds 1 FMN per subunit.
Function: Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by t... |
A0A3M2DIF1 | MKYATAYIGLGANLGDPVQQLHQALAAITRLTGTKLVQASSFYRNPAIGPEQPDYVNAVAEILTSLAPLDLLDALQAVERKAGRRREYEQRWGPRPLDLDILLYDNKVIEHERLVVPHVEMRHRPFVIFPLLEIAPHITLPTGEPVASLAKALSPECLRKI | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 4/4.
Function: Catalyzes the transfer of pyrophosphate from adenosine triphosphate (ATP) to 6-hydroxymethyl-7,8-dihydropterin, an enzymatic step ... |
A0A480BTJ2 | LAWWLAHTRTRLKPLIEAVTALPLVLPPTVLGFYLLVLFAPGAPLGGAWLGLTGHTLTFSFSGLVLASMLYSLPFVVQPLQGAFEAVGRGPLEAAAVLGARPLDAFFTVASPLALRGYLTATVLGFAHTLGEFGVVLMVGGNIPGRTRVISIAIYEQVETLNFAAAHLLAAGMLVFSFA | 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: 179
Sequence Mass (Da): 18815
Location Topology: Multi-pass membrane protein
|
A0A2D9QHR8 | MRGPERGFKLVSSTAYLSLGSNVSPEKNIQFALDQLTKIFGKIDSSSTYQTKSVGFEGSDFLNLVVRINTDLDPAELIRQLHRIEEMTGRVTGTKAFNDRTLDIDVLIYEDLVDLDLNIPRDEILKYGFVLEPLAELDPNGMHPTEKITFLELWNMLKENLDASQKI | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 4/4.
Function: Catalyzes the transfer of pyrophosphate from adenosine triphosphate (ATP) to 6-hydroxymethyl-7,8-dihydropterin, an enzymatic step ... |
A0A2D5T638 | MSLNKEQVQHIAMLAKLNLSDEEYAESVEKLSKIVDFVDQLSTVNTADITPMAHPVDAIQRLRIDDITETNKRDYYQKNAHEVFDGLYLVPKVLD | 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 ... |
A0A3M1KHP7 | MLILASQSRYKRQQLEVLGLGARSIAPDANEALLNGETLREASARLAQLKAQIISRSHPNATVIGSDQTAHLEGETEILRKPGGFERAFGQLMKCSGRTVLFHSGICLVHPAHPPLTHIETTRVTFRQLDEDTVRRYLEKEQPWDCAGAFKCEGLGISLFERVASNDPTALVGLPLIALSRLLRQVGYPVP | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes 7-methyl-GTP (m(7)GTP). May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: H2O + N(7)-methyl-GTP = diphosphate + H(+) + N(7)-methyl-GMP
EC: 3.6.1.-
Sub... |
A0A349UZA5 | MNEKLTIWAKEFLFLALIVTVSGVVGYLYESPLLGVVSGAVLLLALHFAQVFALSRTLSQAATAGSKSHLVLSPIGRFLQKEIRNLFALQTDQAASVARYKKRGRKRQRALSDAISDFRNFIEALPDAVVMLDQEHRVVFWNQAATHLLGISSALDRKRSIESLINDSDFTKFMKDVSDQPFEVFSPTSSKHLLSIRVVSTNDQRYLLQAQDMTRVRQLEDVRRDFVANASHELRTPLTVVHGYLETLMDHYPQEESSELMRIFRQMHLQTDRIKRIVEDMLMLSRLDRDPEKSNEMIDMDEFFQAGYEEAVTLASEKKH... | Function: Member of the two-component regulatory system PhoR/PhoB involved in the phosphate regulon genes expression. PhoR may function as a membrane-associated protein kinase that phosphorylates PhoB in response to environmental signals.
EC: 2.7.13.3
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phos... |
A0A2D5I5X5 | MSFKILFMGTPSFSVPILKSLNLSNHKILEVYTQPPKKKDRGQKISFSSVHRFSNEINIPVRYPTTLRSKVELEHIKQLKPDIVVVVAYGQIIPSEFLDLQNILFINIHASLLPKWRGAAPIQRAIMNCDNETGISIMKIEEELDAGPILLKSKIEITKNNNYEELSNKMSSLGAKLILDALDLISKKKANFVPQQQEKATYAKKIKKTESKIDWNLEAKNIVAKVNAFYPNPGCWFNLKGSRIKIIKAVEIQASGPPGEIINNSFTIGCSENAIQILELQKEGKNKISAKEFLKGNNLEVGFNILKDV | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
EC: 2.1.2.9
Catalytic Acti... |
A0A6N9AVU0 | MSVKYLSTVKTIGNARQAARALLSEETDTAALDADLLLSAALSVNRNLLEALDATELGPCQATNFKHLLQRRLSGEPIAYITQSKSFWTIDLQVSPATLVPRPETELVVERALFHCQAIESPELADLGTGSGCIALAIASEVSAAHLVATDISVDALEVAKQNCKALELDNVSFSCGSWTEALPYHRFDIIVSNPPYIANDDQCLADKFMRFEPPLALIGGSDGLESIRRIVTGVRKHLKPGGWLIIEHGYDQGDAVRNLFESNGLKACSTFKDLADLDRVTEGRNS | Function: Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif.
EC: 2.1.1.297
Catalytic Activity: L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-methionine = H(+) + N(5)-methyl-L-glutaminyl-[peptide chain release... |
A0A6N8VTV2 | MMLSCNTNKLRGSLHFNHSLKRLNTWRVGGAAECFFKAEDADALTYFLRYCVADYPIFYLGLGSNVLVRDKGIRGIVISLGYGFSWIEQRSDDTICAGAATSCAQLARFYVNHGMSGLEFMVGIPGTLGGAMKMNAGAFGGEIWDHVAAVETISRDGTKKRYMRDEIDVGYRYVDMPADECIISGEFKRSPSTEDKTRLQAQLKEYLNARNQSQPVNVPTCGSVFKNLQGSSAAQLIEGCGLKSYTVGGATVSEKHANFIVNKGDATAADIEELIAHIQSTVNARSGVQLQPEVVIVGEQHD | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation.
Catalytic Activity: NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
EC: 1.3.1.98
Subcellular Location: Cytoplasm
Sequence Length: 302
Sequence Mass (Da): 32928
|
A0A2E8KUI5 | MISVPSRFLSKFKLNSVRSLFILVVAFFLIFLLAKNQKEEETYSGKVMGTTWQVTLLTNKNHKNQIQNIFNGIDKAMSTYKDYSLLNEINSLSINTFKLINEDMIKVLEESLRICELTNGAFNISVGRAVNTWGFGPRNKEIFDKNKLLSNTHRHSCNTYEIIDNSIYKLQDVHLDLSAIAKGYAIDKASAYLEENNVENYFIELGGEVSFKGKKEQGFWSIGILNPKNIYEPLFILSSKNIGDNSLATSGNYLNKKIIGENTYSHTINPYTNLPIGDRSTLSVSVLNKSAMTADALATALNVMGVEKGIQFANLNSIEA... | 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: 345
Sequence Mass (Da): 38936
|
A0A6N8FAX9 | MSTVSQSATALNPLHLYRSLQDLNVITADSTTQPSIVVALSGGLDSMVMLRLMLELRYQYQVSFSAIHINHGLSENADDWQSFVTQYCQINDIELSCHQLVLEKTAQRSLEQIARDARYAVFADSLPVGTFVLTGHHLLDQVETFMMRLSRGSGSKGLSAMRPCADLPNSMGQSKQIRLVRPLLSLSKAELIQYAKQEFLDWIEDESNACLDFDRNFIRHKVSPTLTERWPHMASAIKTTTDLLSRESDLLSLYLQQDLSGLIENRVFGFECLNLAKLAQLNTLKQPELVRLFIANHTTRTPSRNVLTEVMTTVINSKED... | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34)... |
A0A368BS95 | MNILFAATPDIALETLEVIYHSKHELLGVICSEEKRSGRGLKIKKSPIRNFAEEKKVKIFSYEDIKDPSFMSVLGKLNIDLLLVFAFGHIISESLINLPKYGSVNIHTSLLPKYRGAAPIQRCLINCENETGISFMKMDAGLDTGPVIETFKIEIKEGMNTEDLEKIMSSISSINILQTIDYIELNNLNLIEQNENDASYASKINKQEALIDWSKPAIEIIGKINGLCPNPCAYSRYQNERIIFYRAVPSPIESQGAGKIISSEKNELLIGGIDKCVSIKELARESKKRMTYKNFFNGSKNFFLKNEIFE | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
EC: 2.1.2.9
Catalytic Acti... |
A0A847C0M5 | MKIRQKIDIKNLTLDDLTELLGGLGKERFRARQLMQWIYRHGVVSFDAMTTLSKEFRRELAQIAFISTLTPQVVEESRDGTRKFLFLLGDGESIEAVRIPMDKERATLCVSTQVGCAMGCAFCLTGTLGLRRNLDTAEIVNQVCAVMAEEPVGNIVFMGMGEPLANFDNVVKALNILQMEEGFDFSARKLTISTCGLVPEMKRFGEGCSVGLAVSLNAATDEVRDRLMPVNRRYPLAQLMAACRGFPLKQRQRITFEYILIQEVNDSLEDARRLVRLLHGVKAKVNLIPFNEHPASSFRRPPEDRIEAFQKHLLDRGLVA... | 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.
EC: 2.1.1.192
Catalytic Activity: adenosine(2503) in 23S rRNA + 2 reduced [2Fe-2S]-... |
A0A349SGS8 | MARVTVEDCLEKIDNRFDLVLVAAKRTRQLMLGADPLVPDDRDKPTVIALREIAEGLVTSEILTEKEITAEEYFSDFSGSDERSEAVEDGATLEPLDASKDSASIEDEAPRRETDGAGSEATDEHDHAADAEKDAPN | Function: Promotes RNA polymerase assembly. Latches the N- and C-terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits.
EC: 2.7.7.6
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Length: 137
Sequence Mass (Da): 14933
|
A0A946YCD0 | TQILEYLPAVLGAIVLLLIGWGVARLLRYATEKLAGKMVDRLAHTRPMDTRVQQPHAYNAAPTIASRIVFWIVLLFFVLAASELLELKVVSDLLGSITGYLPHLLTGLLMLFIGLWLAEVTRAVIRRTGTSNGIEQSDVLGRLGQILVLLVVFSMAAGQVGIDNTLLVILVAVFFAVTLGAIAMAFSIGAKTTIANLLAAQSIAQAYSQGDYIRIGEIEGKILRITRTCLILETPEGQTLIPAKRFSEQDSVLIANNIST | Function: Mechanosensitive channel that participates in the regulation of osmotic pressure changes within the cell, opening in response to stretch forces in the membrane lipid bilayer, without the need for other proteins. Contributes to normal resistance to hypoosmotic shock. Forms an ion channel of 1.0 nanosiemens con... |
A0A962U5V6 | MEDLFPYPVARIGLIGGGQLGRMMVKAAKRLGCTCVVLDPLQGSPAGQVAGHQIVGDYSDPAMLRELAESCDVVTFELEDIETETLLRLEAEGHKIHPRPELLAIIQDKYRQKCFLRDAGIPTSEFVDMPAPERDGFAAFGYPLVQKARRGGYDGRGVVVMPNAQSYDTHLPVAGYVERFVEAEKELAVMVARNVHGECRAYPTVEMRFHARDNVLDFLVAPAQVSDEVARRAEALAVRTVEAMDGVGVFGIEMFLTAEGELLVNEVAPRTHNSGHHTIEACVTDQFEQHLRAILGLPLGDTRQLTPATMVNLLGEPGYQ... | Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5-amino-1-(5-phospho-D-ribosyl)imidazole (N5-CAIR route): step 1/2.
Function: Catalyzes the ATP-dependent conversion of 5-aminoimidazole ribonucleotide (AIR) and HCO(3)(-) to N5-carboxyaminoimid... |
A0A849WJR0 | MKRLYTVSKKSQNFEKYLDGTFSATDVALVLETHNLNSLEESITFEIKNRDQIVKPNWLQILLTLSKPYKFIYLFFPVLFILLDFLIHGVEFDQLTTVLSVISAILLFLGINLMSDFRDHLQGFDRVNENHKSKPIFLGWVRAIRVKQSALCLIFLSFLFSIPVLIAFPRLLFIVVITGTIIFYSLLRRKKSYRDHLFGDVFWAILVGPLLSTGMQVAFSGIVQLKYFLFGCVWGILIFFRIQISNFEHILSSSLAKVKNLVNYFGFEHSKKFLFSIWTLFLLSFVFFQAAFHHWLIWMGTVLIIFFMGYKQFRLLYKLS... | Pathway: Quinol/quinone metabolism; menaquinone biosynthesis.
Subcellular Location: Membrane
Sequence Length: 363
Sequence Mass (Da): 42302
Location Topology: Multi-pass membrane protein
|
A0A351CWG2 | MRFTETKIQGTFIIDIDPITDSRGYFARTWCTKELEARGLDASACQMNLSSNAKAGTLRGLHYQDEPYAEAKLVRCNKGAIFDVAVDLRPDSKTRYQWIGVNLDADNHKGLWIPKGCGHGFQSLIDDSEVLYISSTEYCPAAENGAHYADPKFNIQWPLAVTEVSEKDRNWPYLQ | Pathway: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
Function: Catalyzes the epimerization of the C3' and C5'positions of dTDP-6-deoxy-D-xylo-4-hexulose, forming dTDP-6-deoxy-L-lyxo-4-hexulose.
EC: 5.1.3.13
Catalytic Activity: dTDP-4-dehydro-6-deoxy-alpha-D-glucose = dTDP-4-dehydro-beta-L-rhamnose
Sequence... |
A0A0C2VIH3 | MNQDTQLVQEDEIDLGSLFKVLKRHKYGIAFITAIFVAIAWIFLYFQPSIYSAYTLLEVRGKKAGVNTNDFLAQELGGMGAMEKVDREMEILKTLDINKKALNAVNYQVRYYEDDGLKKIESYENIPIDVKDIKVESKELTSISLKLTPARGGFYLSVSNTIKDRLGFLTVSSDLLDYDKLLEINGFKFKIQKIKNFNTPIYFMVYGNYENFFDSMVAPNLSISQLNKNASIIKIEYKDNLPPRAIKYVDALTQSFIAESVKDKSSQNNKIIDFIDTQLISIKEKLKETETELEAYQAQNNLVQPSVQAETLIKELSALD... | Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
Subcellular Location: Cell inner membrane
Sequence Length: 780
Sequence Mass (Da): 88564
Location Topology: Multi-pass membrane protein
|
A0A919ZVU6 | MNINLFYISNNKSNSDHENKLLSRLKSPIKVSLIRIPVKKKFKSKLEQIEHEAKLLRAKIDFSKPFFCFDRRGRKFSTNEFSQFLIKLNMEASLIIGGAFGLSESLKNESNEIISLSDMEFSHEVFRIMVLEQLYRASCVINNHPYQQIEE | Function: Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA.
Catalytic Activity: pseudouridine(1915) in 23S rRNA + S-adenosyl-L-methionine = H(+) + N(3)-methylpseudouridine(1915) in 23S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.177
Subcellular Location: Cytoplasm
Sequence Length: 151
S... |
A0A351MBD7 | MCHRARKIPVDHGWTGVRPTEYSSSGHVPRASEPTRRSPTLEAQVFISRSQSLLDGRDPLALVDAVLATYSKCAIAFSGAEDVVLIDLAKRTGRPFRVFCLDTGRLHPETYRYLERVREHYGLTIDVLHPDTQQVEDFVRAKGLFSFFVDGHQECCGIRKVSPLRKHLAGLDAWLTGQRRDQSPGTRSTLEMLEVDSFTGQSGKPLLKANPLTWLSSDEVWQYIRERGVPYNELHAQGFRSIGCEPCTRATLPGQHEREGRWWWEEQTRKECGLHSRS | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
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
Subcellular Location: Cytoplasm
Catalytic Activity: [t... |
A0A2E4LGI2 | MAKETFSIVILISGQGTNLQALINARSSYKIDAVISNNRNAAGLDRAKRSGIETFVIEHGSFDSRIGFEKCLAAKIKEINPNLIVLAGFMRVLGSEFIRLFSGKIINIHPSLLPKYPGLNTHKRVLEDRQSLHGATVHFVTEELDGGAIIAQDSVPVFYDDTVETLAARVLEKEHILYPKVVESLAASEIQTKNEDV | Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide from N(1)-(5-phospho-D-ribosyl)glycinamide (10-formyl THF route): step 1/1.
Function: Catalyzes the transfer of a formyl group from 10-formyltetrahydrofolate to 5-phospho-ribosyl-glycinamide (GAR), produc... |
A0A920MHC9 | MSNTYWLNGKYINKEDAYLSPLTHTLHYGLGAFEGVRSYGSSNGDNVNIFRLKEHTERLFESAKIINVPINHNIDEVMEAQIGVISKSNLKDAYIRPLLYLNDERLGLDIVGMSSHLMISCWDWPTYFGAESIEQGIDVMVSSFTRQFPNSLMTKSKISGGYVNGVMAHDQAKNNGYQEAILLDTNGFVAEGSGQNIFIVKDGNLLTLN | Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 4/4.
Function: Acts on leucine, isoleucine and valine.
EC: 2.6.1.42
Catalytic Activity: 2-oxoglutarate + L-isoleucine = (S)-3-methyl-2-oxopentanoate + L-glutamate
Sequence Length: 209
Sequence Mass (Da): 23335
|
A0A352KRH3 | MKIKRFFANDMRQALRQVREVMGPDAAILSTDKLEDGVEIIAAMDYDSKILASSRREQSHMAKQAVSSSQTGGRELAEETASAPTTYEKRVAGTTYEDLAHRLAVDDAQDAELDDFDTPEVPPVVNAPHRESTSAIRQALSGLKIESNFGDSKTMDQLREEMQGLRDLMEQRFAGLAWGNLENNSPLRASLLRRLDLLGFEAEVATHLTDLEFASNDLDSAWQKVLNNLVDQLKEYPEDLTSHGGIVALVGPTGAGKTTTLAKLAARFSMKHGSESVALITTDCYRIAAHEQLRAYGRIMGIPVRVAEGLQALREQLNEA... | Function: Necessary for flagellar biosynthesis. May be involved in translocation of the flagellum.
Subcellular Location: Cell membrane
Sequence Length: 463
Sequence Mass (Da): 50905
Location Topology: Peripheral membrane protein
|
A0A351SCB4 | MILGTGVDIVDIRRFQRMYERHGDRLARHILADQEWDSYRAQKKPYRFLASRFAAKEAVVKAFGTGFGKGITPRTIATVSNTLGAPALSLTGGAADKAQQLGANRFHISLSDEASYVVAMVVIEKTSGV | Function: Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.
Catalytic Activity: apo-[ACP] + CoA = adenosine 3',5'-bisphosphate + H(+) + holo-[ACP]
EC: 2.7.8.7
Subcellular Location: Cytoplasm
Sequence Length: 129
Sequence Mass (Da): 14085
|
A0A967CBU1 | MVSKKETAQRHPADIPVTTLKGVGPVVAAKLERLNITTAEDLLFHLPFRYEDQTKRTLIADLRPDGECVIEGQAISSQVQFGRRRSLIVTIEDETGRLPVRFFHFNRSQQAQFDANPRVRCYGRIRKGPRGLEMIHPQYDRNPKASLPDTLTPVYSVVEGLGQAKMQSLVRQALAIPGLEAAFKPLLKNRPAADLWAALTMLHSPPAEEDLAAIQRGEHPTQRLLAFEELTAYQLGMMLWHRETQAEPSRPLECPAPMFDAFIARLPFNLTGAQTRVVNEIFHDLRQPSPALRLIQGDVGAGKTVVAALAALAAMASGTQ... | 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 + ... |
A0A947PLR8 | MKPSPTSITDKLTIWLSVIMAVTLFFAGIATYWSVSLSLHKTAREELGSKLTMILHLVEEENPDGNMENLRHHINDAIVGHGNLLVWLLNEDDEVVYGDPTLMSEDFLMHDFLMRNISGRLLAVSRITFPNAGHLQLRSGVIALDLTPATQLLDSLLYFLLLVGSLAVLLTFSFAHLATRRGLRPLRKLSTQAAAIAPTSFSQRLNVSGIDRELLELAVSFNSVLDRLESSYRQAEAFNADVAHELRTPLAILISGTQLALSVDRPIKHLRETLESNLEELEILKSLVNDMMFLAQADHGTLPTDMKVTCLQTEAHKVCE... | Function: Member of a two-component regulatory system.
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Cell inner membrane
Sequence Length: 452
Sequence Mass (Da): 49929
|
A0A9C7PMT5 | MLIAAAALPAVFKYISLFAQVYGEALRLGPESGSGVKIPSLTQRDWVNALLFVLPLATLMTAFLLGYSPSMSGFIGLMTALLTGLVLSPEFRRKPIKIVKAFSLGGVSAANIMVAVALIGIVLGVVNETGIAIRFAIAISSFGESYLIVALLLAMFGALILGMGLPTLPAYLIIAIMIAPAIIKAGVDPIAAHMFVLYYAVYSSIVPPIAYGFLCRCTDCGRLSAGDLLDCASSIGDWSACSLCFCLFTVIVVSS | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 255
Sequence Mass (Da): 26727
Location Topology: Multi-pass membrane protein
|
A0A962S864 | MNFVLLLWIISLFGLVFNLSSSVEIGIYNETPIPDPIKKNTIMSLCLPTAIQSDVFTNFGIPTGAGRCGGVQPIVKKIVGEPGDTISVTENGVIVNGTLLPNSTLSEVVIKGYDWGNIYKDYTLSSGEYFVLGDKHPDSLDSRYFGPVKKTWFIAALEPLWLI | 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: 163
Sequence Mass (Da): 17844
Location Topology: Multi-pass membrane protein
|
A0A9K3CZV8 | MRVLLLALLLAGLCLCADVQPVVGILTLSDDDAQPELSSFPASYVKWLEGAGARVIPLYYSMPFEEMHTILDQLDGVLFTGGTQLISFHPINPFSAAGQYVFNYAMDNNMPLWGIPWTTTCRCGAPALGTCLGFELISCILLDDNVLKATDAYNITMPVEITECGKSTRMYSSQPHSEQTQSDFLSLPLSTNTHNWGIYPEQVEVPAFDDFCIASYNTDRVGQRFVSSYEHKTKPIFATQYHPEKSIYEWSTDVAINHSHAAVQAMQSLAMAFVDECRKYTHVFQDQAWLDDNLIYGYSPEYTGLNGSHFEQQYYFSDDV... | Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)(n) + (n-1) H2O = (6S)-5,6,7,8-tetrahydrofolate + (n-1) L-glutamate
EC: 3.4.19.9
Subcellular Location: Secreted
Sequence Length: 323
Sequence Mass (Da): 36316
|
A0A7C6XAD3 | MSPDLWMLLIFAACLALGMPVAFALGLGGAAGIVTGLSPDMLATLGTNTYNSIAKYPLIAIPLFILTGIIFERAGVAASLVNFAQSLIGRRHGGLALVAVLVCLIMGGMSGSGPADAAAVAMVMLPSMTKAGYPRPFSASLIAAASSTAILIPPSIALILYSVMMPGLDLRALFAAGLFPGLLAG | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 185
Sequence Mass (Da): 18664
Location Topology: Multi-pass membrane protein
|
A0A833IQZ0 | MRALLLAAVVLLAGCAEQSETPWRGRILVMGTVVELSLYGLTDDEAQALGQRIEADLQRLHDRLHPWQGNGELRRVNAALRDGQPVAASAGLAALLRHAQTLTRASDGLFDPAIAPLIRLWGFHQETTPAQPPPPGELRAWRARRASLDELRFDPTSASDACVENAGPRTAETQDSRPGAAPAEECAGTRLLPPAQGLELDLGAFAKGYAVDRAVEAARRAGARAAIVNAGGDLCTLGRPAKRDWRIGIRHPRESGVLAAVRLQPGECIFTSGDYERYFQHQGRRYHHLLDPRSGEPARGAQSLTVITEQGTLADAAATA... | Cofactor: Magnesium. Can also use manganese.
Function: Flavin transferase that catalyzes the transfer of the FMN moiety of FAD and its covalent binding to the hydroxyl group of a threonine residue in a target flavoprotein.
EC: 2.7.1.180
Catalytic Activity: FAD + L-threonyl-[protein] = AMP + FMN-L-threonyl-[protein] + H... |
A0A2E7XLE3 | MMDSRKGIALYGGTFDPVHFGHLRSALEVHQILGVSETRLVPANIPPHRDSLSTTAEQRLAMLYLAVEDSEFLKVDDREIRRQGKSFTVDTLKSVRQEMTQDAPLSFIIGADACVLLHEWHAWESMTEYAHLVILERPGYLAHEPAGDVADWLKGKLVDDPQCLSQQSAGLVCRMRLTQLDVSATKIRDLVQRGDSIEYLLPRDVNRYIDKHQLYRKVQT | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
EC: 2.7.7.18
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide... |
A0A2E6BFC4 | MAGQQDWIVGIHAVTELLKRNPQDVLELWLQQDRNDKRLDEVRALASELGLKTRQVGRDELEKHLGGAPRKGGKPRNDRLPVHQGAIALCQWRDTTKDEAFLNKLLESLDHPPLLLVLDEITDPHNLGACLRTADAAGVDAVIVPKDNSAPMNLTVRKVASGAAEKVHLVAVTNLSRTLSALQQRGIWIYGAAGEATQSLYEADLKGPLALVMGSEGKGMRRLTREHCDYLLSIPMAGAVSSLNVSVATGVCLFEVVRQRSG | Function: Specifically methylates the ribose of guanosine 2251 in 23S rRNA.
Catalytic Activity: guanosine(2251) in 23S rRNA + S-adenosyl-L-methionine = 2'-O-methylguanosine(2251) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine
EC: 2.1.1.185
Subcellular Location: Cytoplasm
Sequence Length: 262
Sequence Mass (Da): 28528
|
A0A2E5J9F0 | MSLTLKVDLVNLELLQDLKKWGLLLKEEKNNHCIFVGIGSNIDRVKNIKSCIKLIQSKFEDIKISPVYETRSMGFDGPNFYNLVCSFYTFLDLYNLKKNLNNLELDHGRSLNETKFSSRTLDIDILYYDNLIISNDIIKLPRKEILDYDFVIQPLTDLAPNFIHPEVKIKHKNILEKEDFEKNIIKKIDFIF | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 4/4.
Function: Catalyzes the transfer of pyrophosphate from adenosine triphosphate (ATP) to 6-hydroxymethyl-7,8-dihydropterin, an enzymatic step ... |
A0A2E6LLJ0 | MGTHGILDLDIGNSRLKARLSFSEGCVQHRVVEHGSNFPGQELNTFCGNAVGAIRVSNVAGDRMANALRHWARKFAHPDPVFAIVSRRCAGVETEYADLGSDRWLVMLGGFAVAGSTCCIVDVGTAATIDLVTKNGLHAGGLVLPGLRAMARSLVMETAGVRSLPRASFGAPALHLERCVSAGALFAISGAVDRAVTWLREREGDHPKVLVTGGDGPLIAAHIAGARYHQDLVFSGIDVAMPLCAIAERQELKLYSLGDQGPTAAGISMGDRECPSFPVS | 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... |
A0A9D0UMM1 | MTRPGSLTLRLTLLFSAVALIGFLGFGWLVGRAIDQHFSAEDVKELKVVAQAVETLLAGRPQSAPLAPLKQRFADILVGHHGALLHVRDAAGRLLYASPAPDLSRIPLPAPARLARGTVQHWQDGGHHYRVYVKQYPAAAPGPYTVMVAVGIDFHLRFIDDFRHMLWLMIAGGMVVMGLLSWLAVRQGHKPLHRIVEQISRISAAELNTRLDPDTVPRELKELALSFNALLERLEEAFRRLSDFSADIAHELRTPVTNLMTQTQVALSQARDADAYREILYSNAEEYERMAQMISDMLFLAQADRGAAPLNNEPVDLAGE... | Function: Member of a two-component regulatory system.
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Cell inner membrane
Sequence Length: 470
Sequence Mass (Da): 51778
|
A0A952NKH3 | MRLIVAARKSDLARLQAYQVGEALQKAHPQIQVQYHFRESLGDREQSNPLWQMPAKGVFTEDFVGGLESGEFDLVVHSWKDLPTEKREKTEVVATMKRADARDVLLVRKAAFTENLKTWRVLSSSPRRSYFLQKAWPRLAPKNNPPLEFHSVRGNIPTRLTKLHEGQGEALIVAKAALDRLMSSTREEFGDAQGVIRKVLNDSRFMVIPLQIEPPAPAQGALAIEIRKDRTDLRELLKAIHCPETFAAAQWERSQLATFGGGCHLKLGALQAELQGFQLRLVMGAPPQGEPVEKIWLEKPEAVAGSGSRVPGTFRSEDFY... | Function: Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
EC: 2.5.1.61
Catalytic Activity: H2O + 4 porphobilinogen = hydroxymethylbilane + 4 NH4(+)
Sequence Length: 495
Sequence Mass (Da): 55635
|
A0A972KXH8 | MKFRTPLSKVRGLGAAHDGTGEFWIQRMTSIASIPLTLFLIGSSLYLIGADYNAVRGYISSIFVAPALILVIVVFIWHMYIGMKEILIDYVHAPALKFTALILNMFYTIFLGLISVYAILKLSFGV | Pathway: Carbohydrate metabolism; tricarboxylic acid cycle.
Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH).
Subcellular Location: Membrane
Sequence Length: 126
Sequence Mass (Da): 14021
Location Topology: Multi-pass membrane protein
|
A0A9E3HXU8 | MLSKKMQAALNDQIQSELYSSYLYLSMSSWFKAQNLEGFAGWLEMQAQEEMGHVMKFYGYLHDKGADVELQALPAPQKSWKSPLAVFQDTLKHEQMVTGRINDLCALADSNNDNATRVLLNWFVEEQVEEEASAQAVIDKLKMVEGYPGGIYLIDKEMGGRTVAQDQGGN | Function: Iron-storage protein.
Catalytic Activity: 4 Fe(2+) + 6 H2O + O2 = 12 H(+) + 4 iron(III) oxide-hydroxide
EC: 1.16.3.2
Subcellular Location: Cytoplasm
Sequence Length: 170
Sequence Mass (Da): 19104
|
A0A9E5M456 | MLLRFDDVSLAFGSRPLLDHVSLLVDEGERVCLVGRNGEGKSSLLRLVAGLATPDDGSVWIRPGARIALLAQDLDAVADACVRDIVEGGLPTDAGESWETTPRVEAVMSRLGLDGTAQFASLSGGWRRRALLGRALVGDPDVLLLDEPTNHLDIAAIEWLEGAMLAYRGALLFVSHDRAFVNRLATRVVELDRGRLSSWPGDYDDFVVRKTLQLANEAKANADFDRKLAEEEVWIRKGVEARRTRNEGRVRALMAMRSERRARRERIGRAEFAVAEAVESGKRVFEAQHVGVAFGDHEVIRDLELKIQRGDRIGIVGPNG... | Function: Probably plays a role in ribosome assembly or function. May be involved in resolution of branched DNA intermediates that result from template switching in postreplication gaps. Binds DNA and has ATPase activity.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
EC: 3.6.1.-
Subcellular Location: Cytoplasm... |
A0A972C2X3 | MSAQPQIHDIPGGIHPPENKCQSTARGIEQPPLPRQLILPLLQHIGTPAEPVVQVGEQVLKGQLLARAWGQFGCALHAPTSGTISAIGPAPYPHVSGLAEPAITLEADGEERWAELEPITDYTRLEPLALLEKIAAVGISGLGGAGFPTAPKLASRPDHRIHTLIINGAECEPYITADDMCMREFPAQIVAGIEVLMHILKPQRVLIGIEDNKPEAIAALSQAAEAKPAIQVLAIPTKYPSGGEKQLIQILTGEEVPSGGLPADIGMLCQNIGTALAIHDAVLLGRPLISRIVTLTGDALQRPSNVQALIGTPIEELLAF... | Cofactor: Binds 2 [4Fe-4S] clusters per subunit.
Function: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane.
EC: 7.-.-.-
Subcellular Location: Cell inner membrane
Sequence Length: 585
Sequence Mass (Da): 62791
Location Topology: Peripheral membrane protein
|
A0A973IA04 | MTGLILFGIALLCLFLGYSVAFTFAGVSVFVGVLVLGTDLFAFMPYRIMSIMENTILMAIPMFVFMGIVLQKTGLAERLLESSAKLFGSIPGGIAISTIIVGALLAASTGVVGASVVAMGVISLPVMLKNKYHEPTATGVICAAGTLGQIIPPSIILIILGDVMGVPVGDLFRAAVIPGCLLIIAYTL | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 188
Sequence Mass (Da): 19453
Location Topology: Multi-pass membrane protein
|
A0A523L348 | MTASNPSQALLRRTAGFPRLKRLTKAKDFGRVFANPTRSSDRYFTALSHPNTGNTARLGLTVSRRIARNAVDRNRLKRLVREVFRCQQDLPLLDFVVLANKAAPAAENRVLRDSLQRHFDILVARMD | Function: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of... |
A0A7C3CSZ2 | MSASASMLVPSPMLRAGFWGGLRLHLNALLWMAVGSLSIFLSLLFINQSAVPDKPEKQTYSTSFEVKQIAKPKPKKVVKKRRPRKSRAPVNPAPMVNLDTALSGIDFGLPAFSLDDMGEVDESLLGDTRNVVMTSDMVDVAPRVRKRAPLDYPPRAKHKEIEGYVVISLLIGTDGRVQKAKVIESSPPEVFDDAALRSVRSWVFEPARYKGQAVETWANQTIRFDLG | Function: Interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates. It could act to transduce energy from the cytoplasmic membrane to specific energy-requiring processes in the outer membrane, resulting in the rele... |
A0A354W335 | MMVPDLDVPNTLNFPTSAAWGASLETPGDVAEAKHEADKLGLPFLCLGSGSNVVLMPHLKRFVGRISNRAIQVLDTDTDWVDVNVGAGLLWQDLVEISLSEGWFGLENLALIPGTVGAAPVQNIGAYGAELGTFVVAVTIVDDGGQIHRLNAEACGFGYRDSVFKQQPNWTITDVTLRLFRHPRVNLRYEALRSHFSGQTPSPHAVAAFVTALRQDKLPDPATHPNVGSFFKNPVISPDDADRLRQLGLDLFPQGDQVKASAAQLIDRSGCKQYRVGSIACWPRQPLVFVNYGGGTATDLIEFADQVQRRVADQYAIQLE... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation.
Catalytic Activity: NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
EC: 1.3.1.98
Subcellular Location: Cytoplasm
Sequence Length: 327
Sequence Mass (Da): 35585
|
A0A351CM15 | MESVFIDNVEFPYEDSNSILEFSNKALDDKIIPTLCDDDNLRPYGACRVCSVEVQYNEDGPKRTVASCHTPVTPGMRIYTNSDSIKALRKNIVELVLSDHPPECLTCEVNGNCELQDVAASVGVRQIRYAKGDNHLDREKDLSHAYMRMDLSKCINCSRCVRACDEVQGQFTLTMTGRGFESRITTDNDMLFGDSSCVSCGACAQTCPTSAISDVFQSKSVEADKKIRTICSYCGVGCNLEVAVKNDEVLSIRAPQDAINSGHTCLKGRYAFKFYNHEDRLTSPLIRKNGELMPCSWDEALDFIKDKFQSIKAEHGPDSI... | 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 ... |
A0A9C9BTB2 | MSWYVIIPTLMALISPKSGRFNVTAKGGLLENRFFDYKLAMPCIILFTLNGIGLFIGLGNIFLWGTSETGTVILNLGWITYNLIILGAAIAVTREKKQQRNFVRLASNVEAAIKLSGNKLVQCKVHNLSEGGAAINISDESLLTRGERVDLILKDTLSEMSVTVPAEVMRIGDNRVQFMFQEMSSAQMNVLMLMLYSREGNWNHWVTERSGDNPLREFFQVSKHAIRTVFFLLSPRTLFNGIRVIFRQLLGIKPATVTAVAIFSVACIFLFSLAYMPKADAQTAGSYDVTSTYSLEELGADKDIRIEPAYGRQNFPFSLR... | Pathway: Glycan metabolism; bacterial cellulose biosynthesis.
Function: Binds the cellulose synthase activator, bis-(3'-5') cyclic diguanylic acid (c-di-GMP).
Subcellular Location: Cell inner membrane
Sequence Length: 997
Sequence Mass (Da): 111609
|
A0A6N8VIZ4 | GGLSSYLGPGQAILYTLLDLRRRHITLRTYINMLEETVIILLARYGIAAHCRPDAPGVYVSRAKIASLALCVYKGCCYHGIALNVDMDLTPFDAIVPCGLAGVKMTQVSDYGVQISATEACYLLADILAGRLNSHCSNDTLAS | Pathway: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 1/2.
Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-A... |
A0A2D7FY15 | MSEDDLLSQEEKDALIKGVESGDVDTDQTDIGSSEARAFNFASRELRLLDSLPRLQTVSELFVEASSDAIGKMFRADPAIEPNPLTTRAQQDFIESLSSLCHVAVCTMSPLEGRWILALETRLLYILVDRYFGGKGLAPSANRNKQFTPIEQRLARQVTDLLLTELALAFEDVAVLEPAIESIEENPEHLTLPVSHEPVIQLSLNIGFVEDAGLCHIVLPYAMFETIKDKLNLASETKAPKYNDEWQPKIRQGLRQANLKVTAELDELNLTLRQILDLVPGDVLPIKSPDNVTVKAEGEVLFFGKFGTTEGHNAVKITQS... | Function: FliM is one of three proteins (FliG, FliN, FliM) that forms the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation.... |
A0A2E2WTE3 | MSLSKVPLSPHLQVYRLPLVALVSISHRACGVVNGLGYALFIIFLISIATGYETYKISYIILTSTIGKILVSLWIFSLYLHMSNGVRHLFWDFGYGFSGNSPLISSFIVLASSIILTGVTVLLYLF | Cofactor: The heme is bound between the two transmembrane subunits.
Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH).
Subcellular Location: Membrane
Sequence Length: 126
Sequence Mass (Da): 13921
Location Topology: Multi-pass membrane protein
|
A0A1X6NZP3 | MAGLAFSAGASSGGWGLRPAAAAGATTTSRGSVRRVAPAALGVARRRALTPGVGGGGGIGARPSWARRAATQPALVAVARGGGAPPAGDDRGSGDDAAAAAAAAAAAAAASSPSSARRRPKAGVLGLFFVVATFAWSVLFFVPMVLMHPAILAFDRIRRRAHDAVALSWLRISLWTVGLAPRVVHPERLLSNNQPVMYVTNHASNLDVYAIAYLRRRFKYVSKSEIFRVPIIGWAMALTGNLSLKRTDRKSAMATFRGMVRLLQSGTSMVVFPEGTRSKTGRLGRFRPGAFKAARTAGVPVVPVTIQGTREVMPYDALVP... | 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: 369
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):... |
A0A2D7G3N1 | MKESDRLFLSAAIELAKKGLMTVAPNPPVGCLILKNGCIIGRGFHQKAGEGHAEINALSSAKESPEGATVYVSLEPCAHQGKTPPCVEALIQAKVRRVIIGHLDPNPLVSGKGVILLRDAGIEVEAENMPEALKLIESFQTRMTQKRPFVRIKTASSIDGAISMASGESKWITGEEARADVQYWRARSDAIVSGVGSVLHDNPRFTLRTAEFKSVRQPIRVILDSRFRTPRDANVLTDGAPTLVVSNSGIECFGSLSPSELEKADGVIPNGPRDLENLLKLLALLDCNDVLVEAGAKVVSSFLKRDLWDEWVSYVAPILL... | Cofactor: Binds 1 zinc ion.
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 2/4.
Function: Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5'-phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)-pyrimidinedione 5'-phosphate.
Catalytic Activity: 2,5-diamino... |
A0A9C9DK72 | MDDDSNMKWTILENPDAVARTACERIVQASKQAITDRGEFHIVLAGGSTPEKTYGLLAAAECDWKCWHLWFGDERCLPRDHPDRNSVMVERALSGKVAIPAKQIHVIPAELGPELAAKQYAKSLACVSLFDMVLLGMGEDGHTASLFPGHTYPAGESVLAIYDSPKLPAERVSLSTEALARCRQLLFIITGREKAGAIAQWRNGTQLPASMVRGQGKTEVISDQSAFIA | Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 2/3.
Function: Hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate.
EC: 3.1.1.31
Catalytic Activity: 6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate + H(+)
Sequen... |
A0A962SAS5 | MTTQTRSAVDSIDKTSWVFRPVLLLKPLVFLLCLAPLVLMVTALLTDRLGANPIESLSHETGQWALRLLLIGLLATPLQQQFRWLWTVRIRRMIGLFAFFYASLHMLVFIWLDQQWDWPLIAGEILEKPYLLAGVLGLLLLLPLALTSSNSMMRKLGRRWKSLHRWVYIAVLAGCVHFVWLAKGDKPEPLVYLSIFLGLLIWRFARLVKK | Cofactor: Binds 1 FMN per subunit.
Function: Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by t... |
A0A2D6VAY1 | MRGPQPLGYARISLLLTLLLGGCGEPQQPTYEFIRGATMGTYYRVQXEPSTSCRPSQFVLDQQLLAFNQSLSTYIADSELSLLNQAPAQALRPISERLNVALVAAFELWRDSSGAFDVTVGPLVNIWGFGPDQGLPWPPSEAAQVNAXXSVGMQHIELLPNKQIRKRLAAAYIDLSAIAKGQAVDEIAEIMSGMGCEHFLVDIGGEVRVKGLNSAGKXWRVGIEVPRAGQQGSVQRVLGVSGQSVATSGDYRNFRVVXGLRVDHVLDPRSGIPADNNVLSVTVVHPSAMWADAYATALMVLGXDAGLAYAESRGLATLIL... | Cofactor: Magnesium. Can also use manganese.
Function: Flavin transferase that catalyzes the transfer of the FMN moiety of FAD and its covalent binding to the hydroxyl group of a threonine residue in a target flavoprotein.
EC: 2.7.1.180
Catalytic Activity: FAD + L-threonyl-[protein] = AMP + FMN-L-threonyl-[protein] + H... |
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.