ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
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A0A1Z8KW64 | MTRHLTPGEPLVLASDNPGKINAVSRLTAGVVDKVLGLRKLRLTQADETGTTFEENATIKALAAAKASGRPALADDSGLEVAALDNQPGVYMADWTYDGKGGRDEALGNAKILDALEKKGATDPAQRKATMVTVLALAWPDGDVRMVRGEVTGTIAELPRGANGFGFDPIFQPDGADKTFGEMNDDEKRGYSARTRAFEQFVANHLPPTGPAPVREQEPRRTLAH | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as ... |
A0A8B6XTX6 | MFMSLKGSAQMPIRATQGSAGFDIFAMEDVYLLKRATVKVPTGIRMQIPVGYYGQLLSRSPLAAQNITVEGGVIDSDYRGEICVLLKNNNDREFVIKTDLAIAQLVFLQCFSPQLFIVVPEEELTSTGRGIGGFGSTDCMQRI | Pathway: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 2/2.
Function: This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA... |
A0A951NVU1 | MLFNNLPSRPVSAPKVDGWKTTPINDCGEPLVAMGAFSDYPFLLTDAIYSGQRGSSPYLTTDLDGALITMFARRSVAEALMAAQSLLPAGLILVINDAYRPRAVQASLYQSFYRQLKAKQPTWDNDQLASESQKYVSLPSTNEASPAPHYTGGAIDLSLAKLPRRHWHKLLKLRRAIVRCHPSQWQLRYRLEMDYQVLSARATSLNFGAAFDHGGPASAAMYYEILAATRALTAPENSARTNRRMLAAAMHKAGFSAYEHEWWHYNLGNQMDARGVGAAFARYGGIELSSENHRHNAMRRQHWTNVLRLASGERWSPPTS... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes hydrolysis of the D-alanyl-D-alanine dipeptide.
EC: 3.4.13.22
Catalytic Activity: D-alanyl-D-alanine + H2O = 2 D-alanine
Sequence Length: 353
Sequence Mass (Da): 39394
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A0A1Z1W946 | MKKLSARRRHPLAAVVVLLLALAATGGLYAAFAPADKAQADETAQSLAIDEGKKLYAVGCSSCHGTGGQGSSDGPSLVGVGAAAVDFQVGTGRMPLQQQGAQAPKKKVIYSQAQIDQLAAYIASLGAGPNIPTEKQVSPEGADIAKGGELFRTNCAQCHNFTGEGGALTHGKYAPSLEGVSPKHIYEAMQTGPQNMPSFPDTTMPEKAKKDIIAYLDAVNGEKTESPGGLKLGGLGPVSEGLFAWIFGLGALIAVAVWVAARTAKAKKS | PTM: Binds 2 heme c groups covalently per subunit.
Catalytic Activity: a quinol + 2 Fe(III)-[cytochrome c](out) = a quinone + 2 Fe(II)-[cytochrome c](out) + 2 H(+)(out)
EC: 7.1.1.8
Subcellular Location: Cell membrane
Sequence Length: 269
Sequence Mass (Da): 27631
Location Topology: Multi-pass membrane protein
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A0A090TFP1 | MGLLIAAFEAEIFAPDPWRQIIGLGFLGALTTFSTFSMDNVLLMQQGAFLKMGLNIVLNVVLSISACWIGFQMLTKS | Function: Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Subcellular Location: Membrane
Sequence Length: 77
Sequence Mass (Da): 8413
Location Topology: Multi-pass membrane protein
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A0A3B8XPN7 | MSTTSKASSAQSSDPKSIGDHLGELRRRLTWVVLTLIVMSALAYSVHDALVSFVLSPIGDQKLVYLTPGGGFTFIFQIILYAGLLLTAPVLVYHLYRFVAPALPESMRHMGLRVVFLSSVLMLAGAAFGYFVAVPAALQFLMAFAGDFVQANLTADSYLNFLVAYVIGLGILFQLPLFLVAWNWLNPLPPGGLLSSQRFVIVGAFIAAALLTPTPDVLNQSLLAIPVIAVYQIGVVAVYITNKKKRRQPVQAQAPVVAAEPTMPAARHEQPVFDVQALLGSNIERRPTKPKPVQAVATKPVVIPKPVPQVRSTKSLDGFS... | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes.
Subcellular Location: Cell membrane
Sequence Length: 368
Sequence Mass (Da): 39651
Location Topology: Multi-pass membrane protein... |
A0A1F6SAH9 | MRQDDLIQIGKQNIMNTYSYFPVVIEKGEGCYLWDVAGKKYLDFVAGIAVNCLGYKQKEFIDSLYGQLQKLNHCSNLYYNQPQIELADILTKNSHFNKVFFCNSGAEAIEASLKLARKYGKKSHGENCYEIITMNQSFHGRTFGAITATGQEKYQKDLNPLLPGIIHSPYNDFEALKQKVTDKTCAILIEPIQGEGGIRPAEREFLHNVRDLCTKNDIVLIYDEVQCGIGRIGKLFGYEAYNIPPDVIALAKGLGGGFPIGAMMAVDKVADSFKPGDHASTFGGNPLACTAGKVVLGQLLNNGILKNAEIQGKYLRDQLI... | Cofactor: Binds 1 pyridoxal phosphate per subunit.
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 4/4.
Catalytic Activity: 2-oxoglutarate + N(2)-acetyl-L-ornithine = L-glutamate + N-acetyl-L-glutamate 5-semialdehyde
EC: 2.6.1.11
Subcellular Location: Cytoplasm
... |
A0A955GEV0 | MKIILASQSPRRKALLELMGLKFEVIPSNFEEYFDDDRPVDEVVKELGLGKALDVAKNYPDDIVIGSDLIVVIDGKQIGKPESEEEAKQMLRNISGRTHQLICSVAVVCLNRDYQKVETETAEVTIDKLPEDLIDEYVATGTTYDKAGGYAIQHPLLRLYVTKIEGRKDTIIGMPTNLVTKFLKDFNINSQEIDIKETDSRFFN | 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... |
A0A6I9S8U5 | MAKISIAIVCVAATAWLMASGAMAQVSEWDTATAAYYGDATGRDSLGGACGYGNLFKQGYGLETAAVSKALFNDGSTCGACYEIRCYNDSRWCAPGSITISATNFCWPHPASSNESASRCNPPRKHFDLPQPMFFKLVNDYRASIIPVQFRKVPCVKKGGIMFEMMGDPDFIQVLVYNVGGSGDVGLVWVKVNGADERFWQMDRVWGGIWRTNLRLVGYSLSFKVSSSDYKKEVQSDNVIPANWTFGQRFEGKQF | Function: Causes loosening and extension of plant cell walls by disrupting non-covalent bonding between cellulose microfibrils and matrix glucans. No enzymatic activity has been found.
Subcellular Location: Secreted
Sequence Length: 255
Sequence Mass (Da): 28084
Location Topology: Peripheral membrane protein
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A0A955GLV8 | MENKLSGFLLIDKPVGLSSFGVVYKVRRILKDLTGQKYKVGHSGTLDPAATGLLILAVGKSTKSLNALLKKDKTYVVSMRLGFASTTDDQEGQITKISNLVPTNSEVANTINKFVGQIMQTPPAFSAIKVNGRRAYHLARKGEPVKLEPRPVYIYEISNSKYEYPNISFSCRVGSGTYVRSLVKDIGQALQTGAYMTTLRRTSIDVFSVTNAHQIDELTLSNIESHLITIE | 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: 231
Sequence Mass (Da): 25416
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A0A1F7CN38 | MITEVSTTRFETSLGWLSIRGTPRGILSVTFGVEEAAPQEQVFPFLEQCMHELEEYFSGNRRAFSVPLVMRGSDFQQRVWDALLEIPFGQTVTYGQLAKEVGHPGAARAVGTAVGDNPLAIIVPCHRVLPASGGIGEYASGSDRKEWLLRHEGVISRSAPV | Function: Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irrever... |
A0A1F6SEV3 | MILSVTLNPSLDYVLQVNNLALEETQRAQGASFYASGKGINVSRMLVRFSVQTSSWGFVGGLNGDRLLRILEDEGIDSRFIPCNDETRINVIVTELPTYKQLRISAKGPNISGEELDKLYKRIKNLPEEIEFVTFGGSLPQGVSSDIYKNLIEIIQSKNVKCVLDTSNEPLTLGIQAKPYLIKPNLHELCQIIGTEKLRDLEEIKVAAAQIVKSGVKNVVVSLAKDGAIFVNENKIIHALAPNVEVKSKVGAGDSMVAGLIYALHRNMSEEDTIIYGIAFGTAAVLTPGTELAYKSDVEKLMGNIEIASIEENNYV | Function: Catalyzes the ATP-dependent phosphorylation of fructose-l-phosphate to fructose-l,6-bisphosphate.
EC: 2.7.1.56
Catalytic Activity: ATP + beta-D-fructose 1-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H(+)
Sequence Length: 316
Sequence Mass (Da): 34598
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A0A955FZP6 | MAKTTSITNTSSRALSVAREWSADATLRLVLQVFAIALMAIIVGFFVQLALMAAPVISSMGVAGFLFDNNWDVAHEIFGAWPLVVGTVITSVIALIIGVPVAVSAAIYITEFAPARLRSTLALLLDLLAAIPSVVYGLWGVFVLIPTLKPIERWVASTFDFVPFIGGAVNGPNYFVAGLILAIMIIPIVSAISREVLSTVPLAEKEAALALGATRIEVIRLAVLPHSAAGIVSAVMLGLGRAIGETIAVTLVIGNAAIIGQSIFSQGYTLAAVVANEFGEAEPGSVHSAALIAAGVVLFILTFIVNATARVLIMRRTVKR... | Function: Part of the binding-protein-dependent transport system for phosphate; probably responsible for the translocation of the substrate across the membrane.
Subcellular Location: Cell membrane
Sequence Length: 329
Sequence Mass (Da): 34354
Location Topology: Multi-pass membrane protein
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A0A7W4HHI6 | MLQNKKSLGQNWLKDRFTLEEIAESARSEVDFCVEIGPGLGTLTSSLLKRFPKVVAIEFDEKLAHNLPNSFPGKNLEVINADVLDFDFSQLDGAFSVAGNIPYYITSPIIRKLLLLEKKPAKIVLLMQKEVADRILEEKGRYSFLTLFVQNYAEVEGGIFVERKLFTPPPKVDSASVIFYPREEALVSEEVLKFVKQCFANPRKKLHGMLPHFTGRSREEIMKIFEELGLDLDARPANLDLLEYEKLLNKIKEN | Function: Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits.
Catalytic Activity: adenosine(1518)/adenosine(1519) in 16S rRNA + 4 S-adenosyl-L-methionine = 4 H(+) +... |
A0A3P1SRS0 | MNPLVSIIMGSTSDMPVMEKAMIFLNDMEIPFEVNALSAHRTPKAVEEFAANAAGRGVKVIIAGAGMAAALPGVIAAQTTLPVVGVPIKGSVLDGMDALYSILQMPPGIPVATVAINGAMNAAILAMQIIALGDEKMAKRFSDYKSGLGKKIEKANKELEEIKFEYKV | 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 2/2.
Function: Catalyzes the conversion of N5-carboxyaminoimidazole ribonucleotide (N5-CAIR) to 4-carboxy-5-aminoimidazole ribonucl... |
A0A521GZY3 | MIGKGLSWLAHHPPLKQIGHAFRWFFRLKPIRFIGRILGFGYLASSWRELRKVTWPTWKESRRLTGAVIIFSVIFGALIAAVDYGLDKLFKEILLK | Function: Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation.
Subcellular Location: Cell membrane
Sequence Length: 96
Sequence Mass (Da): 11153
Location Topology: Single-pass membrane protein
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A0A514CH90 | MGRVLAIDLGTKRTGLAVTDLLKITANPLETIRTVDLDKYLKDYVQKEEVEAIVVGFPKSMDGSDTNMTQPTIRLKDRLAKTYPELEIVLVDERFTSKMAMQSMIAMGSKKKDRREKAGNLDKISAAIILQTYLDQL | Function: Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
EC: 3.1.-.-
Subcellular Location: Cytoplasm
Sequence Length: 137
Sequence Mass (Da): 15393
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A0A7W1KG84 | MALLALQFAEAQNPEGIAALGLNLKGFLFQLTTFVLLLLVLKRWVFPRLVATLEKRREVLERSLVQARQTEEALQSAESKASELLRKARLQADAALEDAKKQTEAIISKAEAVAVERSERILKESESQLEQQSIKLREQLRNELAELVVLTTEKVIERKLDDKNDRALIESSLKEMAR | Function: Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).
Subcellular Location: Cell membrane
Sequence Length: 178
Sequence Mass (Da): 20177
Location Topology: Single-pass membrane protein
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A0A6N2CX95 | MRLIKFFTLLICFSVFACTGSKNTDDRIIIEETQEDSRITTEEAIEVHKEETQRELLSSADYDTTLWTDINRIQPDILLDLRYATTNNFLEKQLYECARCFLRPETAKALQKVHLELRTKGYGLLVWDCYRPQSVQRKMWAVMPNPNYVANPERGSMHSRGVAVDATIVDEAGIPLNMGTDFDYFGRAAHYDNRDLPEEVLQNRDLLRATMEKYGLMGIRTEWWHFSMRDLGYPLDEMVWGC | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes hydrolysis of the D-alanyl-D-alanine dipeptide.
EC: 3.4.13.22
Catalytic Activity: D-alanyl-D-alanine + H2O = 2 D-alanine
Sequence Length: 242
Sequence Mass (Da): 28236
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A0A8C3USW0 | MAHGKEPPGFIPRARRCAASAPRPRTSGARGARPEPPAGPAPAHLSSTQPSLAHPVSARLSQPSPALPPPTHPGSPTPNPSQLSPPQPSPSPALPAPAQPNSPQPIPALSAPTQPGSPRRLCGPAAVCALWPPLLRWFPSPAGDRQRWHRRSGSAGIPALPESRGLAARPAAAARRQRGALALRPRRIPGAPAEPLGTGGMSAVRRKFGDEYQAVGLARCSARRERQRFVDKNGRCNVQHGNLGGESSRYLSDFFTTLVDLKWRWNLLIFLLTYTVAWLVMASMWWGIAYLRGDLHQAHGDAYSPCVANVYNFPSAFLFF... | Function: This potassium channel is controlled by G proteins. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised... |
A0A9K3PCL8 | MGNKVHIGWSHLFSHSNPLLLVEAWTSPSLRMSSHRKCFHMASRWSSTFSPSRQSSLLSLSSQQSLPSATKNYPSCLFSSNSTANSDHFQEELTSNSTSTILSIDKDVRTMDPEQLLATWRELPVINPTVTFDTLLVPSSSLQTYVQHPSLQSILAKPTNCELLQHVHPRIKLVQDYKDDGAATGKKQLLLLSSSSFSNNIDHSDSSLQQLLDQDPAIERGPPLSISLSYQQLSFQYILQQLLPLHLLPPPSAYEQIGHIAHFNLKEPYQPYQQWIGQVLVATTPGIDTVVQKVGTVSGKYRTYQYEILADTRRPISQGN... | Function: Specifically methylates the N1 position of guanosine-37 in various cytoplasmic and mitochondrial tRNAs. Methylation is not dependent on the nature of the nucleoside 5' of the target nucleoside. This is the first step in the biosynthesis of wybutosine (yW), a modified base adjacent to the anticodon of tRNAs an... |
A0A653FQC3 | MNISNSQVNRLRHFVRAGLRALFRPEPQTAVEWADANYYLPKESAYQEGRWETLPFQRAIMNAMGSDYIREVNVVKSARVGYSKMLLGVYAYFIEHKQRNTLIWLPTDGDAENFMKTHVEPTIRDIPSLLALAPWYGKKHRDNTLTMKRFTNGRGFWCLGGKAAKNYREKSVDVAGYDELAAFDDDIEQEGSPTFLGDKRIEGSVWPKSIRGSTPKVRGTCQIERAASESPHFMRFHVACPHCGEEQYLKFGDKETPFGLKWSPDDPSSVFYLCEHNACVIRQQELDFTDARYICEKTGIWTRDGILWFSSSGEEIEPPD... | Function: The terminase large subunit acts as an ATP driven molecular motor necessary for viral DNA translocation into empty capsids and as an endonuclease that cuts the viral genome from the concetamer to initiate and to end the packaging reaction. The terminase lies at a unique vertex of the procapsid and is composed... |
R6UMZ1 | MVKVLAPAKINFTLDITGKLENGYHTVDMVMQSVNLCDVVTVEKSQELILTCNKDSIPCDSSNTAYKAVKLFENLTGTACNVSVNIEKHIPAQAGLAGGSTDGAAVLVALNKLYNKGLSDSQLAELGGKIGADVPFCIYGGTMLATGIGTKLEKIKPNLDLQKYIILLCKPKINVSTPQAYKISDSRPFSSSVHSTAVINALISGDEAEFYKGLYNDFDSLLGLEPVQHIKEIMLKNGAHTSVMSGSGPTVYGIFTDSCLADKAYDILGREYTDVYKASCYGGCTVL | Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 3/6.
Function: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
EC: 2.7.1.148
Catalytic Activity: 4-CDP-2-C... |
A0A097GZS8 | MLVLGGEKSGKSAFARRVAKDYANVLCLVTMAPVNESVYFQHVCSRPIEWDVLEEPVALAICLLSNADAYDLIVLDDIGVWLSNVIALKMNVYYEIDCVLDALCRLKAKLVISKELGLGMLSNSVLALEYVNLLNCVNQLLARTLNSAYFVIAGQAVKIK | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 5/7.
Function: Catalyzes ATP-dependent phosphorylation of adenosylcobinamide and addition of GMP to adenosylcobinamide phosphate.
EC: 2.7.1.156
Catalytic Activity: adenosylcob(III)inamide + ATP = aden... |
A6QAK0 | MNTKNLQNNNEEEITLKDILRILHRYRYMILIFVLFSAALSTYIAYFKPNIYKATTTVEVGLGHDEGGDILSRATEPGRLIADTEKEIIQSRYLAAKALKKVDFTHRYYTTRKFREIELYKDAPFKVGMLKGYGIPFNLYPVDAKQYRIEVKEAVDRNGTSWNYDKIHMYGEEVITPYFHLNIRRTKPAQDQAYHFVINRSNHPVGGVSVGQHTKASTILHISYEENVPLRAQEYTNALADAYMTQNIEKKTRQATLQLKFLDKELQNITENLKGSAVKIEEFKKGANTVSLSSKAENIIRKMSDAEAKLEALQIESEML... | Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
Subcellular Location: Cell inner membrane
Sequence Length: 770
Sequence Mass (Da): 87221
Location Topology: Multi-pass membrane protein
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A0A8C3XYP0 | MFSLQIKDIEVLNCEYGKNTINLEQFAIDICNHFMTTFCQVAYVKTYVQEVPWQRLHEDGVPHIHSFICVPDGIRFCEAEQCRNGPLVVFAGIKDLKLMKTTQSGFEGFYKNEHTTLPERHDRILCGELFCKWSYGECKDFDFDCIWKKIRECILEAFAGPPDCGEYSPSYQKTVNCIQMLVLSRLLWLPARKIGLFHRWSIVCLCSSLPPKSCDSATVPSYPFPPSGGHYRSTFTCDNVSIYHCCS | Pathway: Purine metabolism; urate degradation; (S)-allantoin from urate: step 1/3.
Function: Catalyzes the oxidation of uric acid to 5-hydroxyisourate, which is further processed to form (S)-allantoin.
Catalytic Activity: H2O + O2 + urate = 5-hydroxyisourate + H2O2
EC: 1.7.3.3
Subcellular Location: Peroxisome
Sequence ... |
A0A9E1LZB4 | MKEAAPKKTWFQTLRTLWVPLAIGVVTVAALAVVVGMVWKDYRTAMMDSQTRQMELVVQSTADSIRVLLEEYADRLDSIAGKAEASKAFRPTVARSDTIRDVWLENSNGEVIYSCYGLSAVCDVLITRTKNISYWQYHSGDEHYLVMKKKAGDETACLVVDSTVMYQQLISEIHVGRNGYIMIKNDDNLVVMHPEAVQWGIKVVEGRQRIYQGKELDMSSLSELLRAQQEEESGTLDYYSYWWADPDLPRVHKISAFRHLDVGGSFWIVSAVVDYDDFYEPVQQSFVKVALIFGGVALVLVLFMFQMFRLQERDRRSATE... | Function: May play the central regulatory role in sporulation. It may be an element of the effector pathway responsible for the activation of sporulation genes in response to nutritional stress. Spo0A may act in concert with spo0H (a sigma factor) to control the expression of some genes that are critical to the sporula... |
A0A3E2NDR2 | MREKIISKKNQIRSIVFMASLMAVTVVIVLKEYSIGELIKVVESIHVFYLFTGIALMFFYAGCQAMNFSMIMHRLGQAVSYKNCIDYAYIGNYFSAITPGACGGQPAQMYYMNKDKIHVDISAITIFLMVFESQIVIVLMGGVFAVLRFSILAKSAYWFIWLLFSGASVMLFLTAVLSALMFSRVMIPFLIDLVLQLGVKFHLFKKPKEIKEKLDILIISYREKSRMIIKNPDLFLKVFAVSMFQWIAYCLVTYLVYLSFGYRKNDCLDLMAGQSFINIAVAAVPLPGSVGIAEKAYLNVFGQFYPGEQLPSAMILSRII... | Function: Catalyzes the transfer of a lysyl group from L-lysyl-tRNA(Lys) to membrane-bound phosphatidylglycerol (PG), which produces lysylphosphatidylglycerol (LPG), a major component of the bacterial membrane with a positive net charge. LPG synthesis contributes to bacterial virulence as it is involved in the resistan... |
A0A975QRD1 | MKREFNDIMNSLKDSVADYKYYTDFDKVFVNVKKFKVELNILNSLLGSNQIEIDFMSLLDKFPVILNVVPLLLAVRKMELPIVDDKPIVFNFKERVMSDELYLKFMRKSGLFNLMENNKVKCLYDYIVGVEVGLDSNARKNRTGRTMENIVESYISRVECVEYFPEMRKKEIANRYNINLDRLILADETKKDAEKKFDFVIKTSDHLYLIETNFYTGGGSKLNETARSFKSIANDIRKIDGVSFVWITDGVGWRTAKNNLRETYDVMEHFYTLKDLEEAVLEEVIK | Function: A P subtype restriction enzyme that recognizes the double-stranded unmethylated sequence 5'-GATC-3'.
EC: 3.1.21.4
Catalytic Activity: Endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates.
Sequence Length: 286
Sequence Mass (Da): 33488
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A0A2G6HMB4 | MQITKKQLDPTHIQLNIAAGSEELEPAKEAVLKELSKEVKLSGFRKGHAPTAMVEKVVDQQLLTNRIIDRVVNDLYVAAVQQERVRAVAQPEVNLTKFVPYTALELTAKIEAVGDITLPDYKKFAVKKQVEAVTDKEVEHVIDELLERGAEKTEVKRAAADGDEVTMNFAGVDAKTKKEIAGAKGDDYPLVLGSGAFIPGFEPELVGLKAGEEKTFTVTFPKDYGVADMQGKKVEFTVTVKAVKKRKLPKLDNAFAAKLGPFKTVAELRGDIRKQIASEKDNQAQQKLENSILDKLGAKTQVAIPDSLIEQEIDLMEEDE... | 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
... |
A0A2T0BD35 | MNLYSLKMRASKSQDGIEKHISGAEKITGEDSLFIYSKALLTRALYHSKGKADFINIKIEKVNQEDILFLDALPVTTVNVSSYQDGIQKLLAMLEKIGITNASAVLEKLKDTYNMRGAMLLNVDTLERLEPNKDRGIRATYMDEVNSVMKKKDTKDHYNEAIVLATKVAYAPNIIGEICISDDPDYVTGYVASKENGYMRITKLKEMGSEDGGRIFLYRGDHSKVQDCIDYIEKREVLVKNISSILNKPYKTEESTKNKWNFIDKALENLKYNNLYRTMNEIKSAQSAHVTFQGKEMIMMASNNYLDMSNDSQVKAYALK... | Pathway: Cofactor biosynthesis; biotin biosynthesis.
Function: Catalyzes the decarboxylative condensation of pimeloyl-[acyl-carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON), [acyl-carrier protein], and carbon dioxide.
EC: 6.2.1.14
Catalytic Activity: 6-carboxyhexanoyl-[ACP] + H(+) + L-alanine = (8... |
A0A7L8AA06 | MNQLGSLPIYQQKKGISNYWVTWPLFTSEALELALKHIPSSTMVVLFRRLLQDLKHNRTGMPDLIMFNEKDYLWVEIKGPGDKLQNNQLRWLQFFSQHHIPAEVAYVQWQEST | Function: Nuclease required for the repair of DNA interstrand cross-links (ICL). Acts as a 5'-3' exonuclease that anchors at a cut end of DNA and cleaves DNA successively at every third nucleotide, allowing to excise an ICL from one strand through flanking incisions.
Catalytic Activity: Hydrolytically removes 5'-nucleo... |
A0A7T6ZWX8 | VQINSIINNNQLYNVIVTTHAFIMICFMIMPIVIGGFGNWLIPLMMGSPDMAFPRLNNISFWLVPPSLMMMICSFMINNGTGTGWTM | 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... |
A0A090T9Z4 | MPGALPVQASILGLTGIALMAGSAAAFNHLIDRRIDAIMARTHKRPLPSGDLSAGKVMAFASGIGIAGFAVLALGVNWLTAWLTFASLLGYAVVYTLYLKRATPQNIVIAGIAGAMPPLLGWTAVTGELHANAWLLVMIIFIWTPPHFWH | Catalytic Activity: (2E,6E)-farnesyl diphosphate + H2O + heme b = diphosphate + Fe(II)-heme o
EC: 2.5.1.141
Subcellular Location: Membrane
Sequence Length: 150
Sequence Mass (Da): 15899
Location Topology: Multi-pass membrane protein
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A0A086ZEF3 | MPKNKKPELSGLIVVDKPLGVTSHDVVAAVRGALGMRRVGHAGTLDPQASGVLVVGFGHGTRLLNYIVDHTKTYEATIRLGQTSTTDDSEGEITALAPVLLADDAGHITNELKNSGGLSSPRSKSDSGNVRVLTLQQIEQAIKEHLTGGIEQVPSSYSAVRVNGRHAYELARAGKDVRLDARRVTVNEFKVLDARTVLAPSDRTQAGSVVVDDPISGGLSADDSKPLDSTGSFDAADSKDSVDLTGWTGSADCPYREGRDESAGDWVPVVDVDVRISCSTGTYIRSLGRDLGRLLGEGGYLTRLRRTRVGRFDLEDPLIA... | 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: 444
Sequence Mass (Da): 47510
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A0A8D3C7V1 | MALRVLEIIFFLYFASHIPITLFIDLQALLPGQLYPQPLKDLLKWYAEEFKDPMVLDPPAWFKSFILCEAVLQTPFFPIAAYAFLKGGRKWIRTPAIVYSTHVATTLVPILAHVLFYQFPMKPYPGPQTPQERWLLVSIYAPYLLVPVLLLVTMLLSSTYNSISSTKTNTKKKN | Function: Intracellular orphan receptor that binds numerous drugs and which is highly expressed in various proliferating cells. Corresponds to the sigma-2 receptor, which is thought to play important role in regulating cell survival, morphology and differentiation. May play a role as a regulator of cellular cholesterol... |
S5WVV2 | TLYFIFGIWAGMVGTSLSLLIRAELGNPGSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLISSSIVENGAGTGWTVYPPLSSNIAHSGSSVDLAIFSLHLAGISSILGAINFITTIINMRLNSLSFDQXPLFVWAVGITAFLLLLSL | 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... |
A0A1W0XFJ0 | MDFSSSGNYEDDVDLEAPLTMEELHLSRQWGLLDRLNGNLWNDSGSGTGNDNYLWENTSMLINGIGAGSVSETDGRRALQWYPASYRILGTIMQTTIFFIGFFGNVMICVVVRKTKSLHTPTYCYLVSLAVADILLVSITIPEAIISYHLASRQWIFGKAGCVISTFCSFLAINAGSISILAFTVERYIAICHPMLAQKVCTISRARKIIAATWLIVGIWSCQWFYTSTSKPLIEATEPPMEQCAYRLERSGYAAVFMVDFVLFYAIPLLISVVLYTRMGFVLYRSVRVMRMNAHHQPHRKAPLESGMTLSNCSNWSSNG... | Function: Receptor for thyrotropin-releasing hormone (TRH). Upon ligand binding, this G-protein-coupled receptor triggers activation of the phosphatidylinositol (IP3)-calcium-protein kinase C (PKC) pathway.
Subcellular Location: Cell membrane
Sequence Length: 561
Sequence Mass (Da): 63000
Location Topology: Multi-pass ... |
A0A1X0QBQ5 | MGIFNNLSAVTIFLLSSAITTLGNKFLVKNLNFHRHQLLIILQNIIIVSILVCYNFLVKNIINFKRFKKWCIITVFFSVMIVSNMKALSCFDVSIYTLYKNISIVFVAITEYAFFDRKLSPIGYLSFILIVGSSWTGKPLKKSELVGYLWMIINIFSTTAFVLLLKHIIDNESSRLECVFFTNCLSIPFLLILSYFIDDYNKPLNLTPFVYFLILFTSLTALITAFSTAWVLKLLTSTMFSIAGAINKVIVTAAGIVIFKEDLEFIKLISCCVATLSALLYYYDAVKYKRQS | Function: Involved in the import of GDP-mannose from the cytoplasm into the Golgi lumen.
Subcellular Location: Golgi apparatus membrane
Sequence Length: 292
Sequence Mass (Da): 33281
Location Topology: Multi-pass membrane protein
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C7QIS8 | MLPPDNHVHSEYSWDALAGSMERTCERAVEIGLPSIAFTEHADFSISEMTPESFFPDQWKPYVELVDGRSILTPPRIDLTGYLETLERCRDRFPTLRVLSGVELSEAHWFPEETADLLKRGGFQRILASLHTASARDEDYADIGVSIKRADPSAQYRGYLAEAVRLIEEYDGFEVLTHIDYPVRYWPHEKTPFDLLAFEDDIRLVLRTLARADKLMEFNTRIPLDPRVVGWWRQEGGKGVSFASDAHVPDAVGRGFQEAAEVARAAGFKPGADLFDFWVRD | 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: 281
Sequence Mass (Da): 31964
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A0A6A4TS44 | MFRYLNDVDDDPYMMDPFAAHRQQMSLFTPFAMDPFALAPQMQPHRAAPRRQAGPLTPFGMMGMGGGFMDMFGMMGEMMGNMERMTGSPNCQTFSSSTVISYSSSDIGAPKVYQQTSATRTGPGGIRETHQSVRDSESGLERLAIGHHIGARAHIMERSRNRRTGDREERQDYINLDESLFRAAVPSGASTGIYEALELRDGDKTRYKGKEKSERKSVIKKRFTLAALLQGVNVLEQEKLDNMMIEMDGTDNKSKFGANAILGVSLAICKAGAAEKGVPLYRHIADLAGNGELVLPVPAFNVINGGSHAGNRLAMQEFMV... | Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5.
EC: 4.2.1.11
Subcellular Location: Cytoplasm
Sequence Length: 1013
Sequence Mass (Da): 110522
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C7QAM1 | MKPARMRPIAALWEWQTSAACRGLESARFFSPSGERGNARAERERSARELCAGCIVREECARFAVESGEQHGVWGGVSRERATRR | PTM: The Fe-S cluster can be nitrosylated by nitric oxide (NO).
Cofactor: Binds 1 [4Fe-4S] cluster per subunit. Following nitrosylation of the [4Fe-4S] cluster binds 1 [4Fe-8(NO)] cluster per subunit.
Function: Acts as a transcriptional regulator. Probably redox-responsive. The apo- but not holo-form probably binds DNA... |
G8FGI0 | DVVEIEHWCQGEGKIGTRRDWILKDLASGEVIGRATSKWVMMNQDTRRLQRVSDEVREEYLVFCPRTPRLAFPEEDNGSLKRIPKLEDPAEYSRLGLIPRRADLDMNQHVNNVTYIGWVL | Function: Plays an essential role in chain termination during de novo fatty acid synthesis.
EC: 3.1.2.-
Subcellular Location: Plastid
Sequence Length: 120
Sequence Mass (Da): 13995
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A0A2S6QL97 | MTKSDKITANIGKANDSCLKRLSIKKTIVLIGLMGAGKSSIGRRLAEHLDFTFKDSDEEVELAARLSINEIFANLGEKKFREGERRVISRLLDDKPMVLATGGGAFLDSFTRDKIANNAISIWLKADLPTLVKRTSRRNNRPLLNNKDQKSTLKKLIDDRYPTYKLADITVESNDEAVENTLTKVVDALDNYLAEIK | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.
Function: Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
EC: 2.7.1.71
S... |
A0A2T7UJ04 | MKPKGQMKWVGLIALLLLLCAGGGGAWFYFDRLKGENTGLESEESKLSAAPKLYLALDPMVINLTDLGGDRFAQVGITFQIREEKSAEAIKKMLPTVRSAILIALSQKGSDELLSRPGKEKLALEILAEVGSVLGVKPNSPKTEEATLSKVEVMPLKSQALNPVVEVLFSSLIVQ | Function: Controls the rotational direction of flagella during chemotaxis.
Subcellular Location: Cell inner membrane
Sequence Length: 175
Sequence Mass (Da): 18878
Location Topology: Single-pass membrane protein
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A0A841RE12 | MAKICLVLTAPTMEENRRILERNLSLVDMVELRTDLLEESQYSLVPSFPGQSGVPVVLTCRKNCDGGNWTGAEEERMALLELWLDGGFAFIDIEMDVEPGPLSGKAAAMNTEIIRSFHDFDGVPEDLVETMNRFDGVMAKGAVYPRSSEDLFRLIEAAQQLKKERKSPFILLGMGNFGFPTRILAEKIGSFLTFCSDSEAPSGAPGHCTALDLNSIYRFRKISGKTVINSIIGNPVSQSRSPHLHNGWYEKEGLDAVYVPFLTDSPQWFMKTAELLEINGSSVTVPFKSDIIPLVDTTDKAVDAIGASNTIYRDGSGQWS... | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.
EC: 1.1.1.25
Catalytic Activity: NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH
Sequence Length: 484
Sequence Mass (Da): 52793
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A0A955GFP5 | MIGVDEVGRGAWAGPLLVVAVRLKSGKSLPKGLRDSKKLSKKKRDSLASKIIEVCDVGDGWVSSDVIDSLGLSVALKSACLLAVLKLDARNDESIILDGNVNYFKDTHYKKVSVKIRADDTEPIVSAASIVAKVARDKYMIDLSEIYPKFGFDKHVGYGTKLHRENLKKYGTTKIHRFSVKPIRDLIAL | Cofactor: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
EC: 3.1.26.4
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Seque... |
A0A0G0LH07 | MKKTKKIAIFHCGFVYSGGGERVVLEEARRLKEKGFDVLVYAPTLDRKKCYPEIVNDVGVKTFFPSYIDKIPYRNAIRMVLSSLLAPIFAFRFRDIDIFIGANQPGAWIAFCVAKLLKKPYLVYLNQPNRVVYPRPIDVAYGWYSTEKDYHMLYVMFQYLKPVITFLDKLSVVHSNKVFVGGAYMCDIIQNIYSIETHDNPAGAQFQPTEKIPSSNNTFTGVVTLGKSKIKKPYLLITNRHDPQKRFDYVINAFDQVLKKYPNVANLVVTGSPTKHTKELIKLVKKLELDKKVHFVGALTEAELAKAYANAVVYCYPSPE... | Pathway: Protein modification; protein glycosylation.
Function: Mannosylates Man(2)GlcNAc(2)-dolichol diphosphate and Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol diphosphate.
EC: 2.4.1.132
Catalytic Activity: alpha-D-Man-(1->3)-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodol... |
A0A3R6ZGD5 | RRGLGMLFLLWTDDDAMPLRGISYDQWLRHTDTWVLGRPIPDSIAHANLNDLNTDNSTHRPPTEGQRGMAHVNMPWTPDEYLYHVLEGNHTTLPREAADVIRFFSCRVWYVHDAYPDVESATDLAVKELLFALHTDRQVPTADALAAIDVDESLAYYLSLGAKYLPTVLQW | Cofactor: Binds 2 iron ions per subunit.
Pathway: Polyol metabolism; myo-inositol degradation into D-glucuronate; D-glucuronate from myo-inositol: step 1/1.
Catalytic Activity: myo-inositol + O2 = D-glucuronate + H(+) + H2O
EC: 1.13.99.1
Subcellular Location: Cytoplasm
Sequence Length: 171
Sequence Mass (Da): 19518
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A0A0A6ZDD7 | GLLLFPRATKNLRRIWAFQSILLLSIVMILSIDLSIQQINSSYIYQYIWSWIINNDFSLEFGYLIDPLTSIMLILITTVGIMVLIYSDNCMSHDQGYLRFFAYMSFFSTSMLGLVTSSNLIQIYIFWELVGICSYLLIGFWFTRPVAANACQKAF | Catalytic Activity: a plastoquinone + (n+1) H(+)(in) + NADH = a plastoquinol + n H(+)(out) + NAD(+)
Subcellular Location: Membrane
Sequence Length: 155
Sequence Mass (Da): 17934
Location Topology: Multi-pass membrane protein
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A0A1W0WSD5 | MPPNTMHKDLLMSSVVLPPPPPPPPRTTTTTTTTHTAGIILFPGSSSASRQSGLTQAGTMRLSPTPPFITRPSRSIRQIIIFVLLMVSLTLFLLMKSVSNSDDGLVNDGGNNNLNENDDARPDAAGRDESTAGGVVGPIWRPLQQRILAWTGVAVPPPDRLPQRWYLQSNVTRIVSTEVLGKLNGLWPEDSPGSDRIEEQLLHKPVAASSNRPEMNKTRVIYVPEGLAGWGVSDGRDVFRRDNCPVDDCELTGNKDTAMTADAILSKHRFGDLKREFHPSSQIWILYLLESPFHTPSFSHAKGSINWTATYRKTVNWLAP... | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 520
Sequence Mass (Da): 58441
Location Topology: Single-pass type II membrane protein
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A0A5P9KFT7 | SFWLLPPSLTLLLMSSLVESGAGTGWTVYPPLSSGIAHSGASVDLAIFSLHLAGASSILGAVNFITTIINMRSVGMTFDRMPLFVWSVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF | 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... |
A0A2U9CC36 | MASAASTNLNAVRDTMDVLLEISRLLNTGLDLESLSICVRLCEQGINPEALSAVIRELRKASESLKFRADLLLANGSPSNPGGAPASGGAKPVYATPSPVESTPQNNECRLVEVKGAKLASFTVRDTELICLPQAFDVFLKHLVGGLHTVYTKLKRLDISPVVCNVEQVRVLRGLGAIQPGVNRCKLISRQDFDTLYSDCTNASSRPGRPPKRLQSVTEGGAHHMLSHSGLMHAGIMPPADLSALAKKIKLEAMAGYHSNQQHGGPNGENGDHNPGLVLEQLPFMMMSHPLIPASLAPASVSMAMGQMNRLSTLASMANV... | Function: Required for gamma-tubulin complex recruitment to the centrosome.
Subcellular Location: Membrane
Sequence Length: 861
Sequence Mass (Da): 94944
Location Topology: Multi-pass membrane protein
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A0A2U9BF50 | MQVLGWTILLLCQWILRKVQGLEKQVDFSELGQVGSVMKTLQYVYGGGSVGGTTGGVVKPPYQTRIFSTSIDQTPMKTKPPTYSFFNPYDTTRNQSLLLDQTGYRSKRKPSLKTSMKTKKIFGWGDFYFNVKSVKFSLLVTGKIVDHINGTFTVYFRHNSSSLGNVSVSIVPPTKVVEFEVLQQQQLHPHTQQDVQIQETQQSTVDPKETKTFNCRVEYEKTNRSKKPKPCLYDPSQTCFTENTQSHAAWLCAKPFKVICIFISFFSIDYKLVQKVCPDYNFQNALQSFGEESPDKLFVILMCVFVFDPSYCHEFDLNSN... | Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
Function: Interconversion of serine and glycine.
EC: 2.1.2.1
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + glycine + H2O = (6S)-5,6,7,8-tetrahydrofolate + L-serine
Sequence Length: 889
Sequence Mass (Da): 99228
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A0A0S8FH28 | MTPLEKALFLARIVAWRLRWERRDLDYHPGKGVSEKFLTGRDAAALIPDGATVISSGMAGNSRCSTFFWAIRERFESEGRPRGLTWISVGGQGGRGKAPGTVEEVGRPGLVTRFISGHMETTKSMLALAEEGKLDLHVLPQGEMTELIEGQARGVTRVRSKTGVDTFLDPRRGSGSAVVDRNGFNLVKADGEALVYQLPPIDVALFCGAYADARGNVYLNDVATLTETWESIRAARANGGLAMAVVGGLIDEDPSEPRVSTDELDVVVVNPYNEQTIMAPQASPWKMFCPGGDGDDRAAIERLRFINRVLRLTPVRGPVE... | Function: CoA transferase having broad substrate specificity for short-chain acyl-CoA thioesters with the activity decreasing when the length of the carboxylic acid chain exceeds four carbons.
EC: 2.8.3.8
Catalytic Activity: acetate + an acyl-CoA = a carboxylate + acetyl-CoA
Sequence Length: 566
Sequence Mass (Da): 617... |
A0A346E0I3 | MILRKFFWKKKIIPCIIKNNGRVIMQAWINKYCFFKTIYYNIIHFWSRSRKKIWIKGSTSLNFQIVKSISIDCDNDTFLINVKQINNICCHFIKKSCFNEIYKKNN | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9.
EC: 3.5.4.19
Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-5'-AMP + H2O = 1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide
Sequence Len... |
A0A6A4T3Z8 | MRLKVGFVSRSLLFIGTFLGLVVLWSSLSPKPSDDNPFEKREDSLLPKGDLANHFKPVVPWPHVEGVEVDLNSIRLKHEDAPATCVTAFCVPGGNNKRQQIDRQHMDNMLALCKYWHYDDRLLTSSVVIVFHNEGWSTLMRTIHSVIKRTPRRYLAEVVMIDDYSNKVHLKERLEEYIKQWNGLVKLFRNEKREGLIQARSIGAHKASKGQVLIYLDAHCEVGINWTVCTVPLIDYIDGNEYTMEPQQGGDEDGLARGAWDWSLLWKRVPLSQREKAKRKHTTQPYRTVCTVPLIDSIHGQKFTIESQGGGDENNFARGA... | Pathway: Protein modification; protein glycosylation.
Function: Component of the ESCRT-I complex, a regulator of vesicular trafficking process. Required for the sorting of endocytic ubiquitinated cargos into multivesicular bodies. May be involved in cell growth and differentiation.
EC: 2.4.1.-
Subcellular Location: End... |
A0A0E9WE34 | MAGALCVPLGYLLMVELRCSHYTALGASLLLLMENSLIAQSRFMLLESVLIFFLLLAIMSYLRFHNAQRLSSPHKWAWLVLSGISCACAVGVKYMGALHLYSTFVSGRLPHLATYWRQNTK | Pathway: Protein modification; protein glycosylation.
Catalytic Activity: a dolichyl beta-D-mannosyl phosphate + L-seryl-[protein] = 3-O-(alpha-D-mannosyl)-L-seryl-[protein] + a dolichyl phosphate + H(+)
EC: 2.4.1.109
Subcellular Location: Membrane
Sequence Length: 121
Sequence Mass (Da): 13581
Location Topology: Multi... |
A0A8B7DJI5 | MGNYLPYFNRRTDNGVEIINANAVYRFPPKSGSYFGTHFMMAGEKFENMNPERFLFGENSDLNYLPNKPMPFPYSIGKSNEPSNTVRSLVHLRKDTLKLLKISSQYWIEFVFDTDIACSVEVYLMANEFLTTDSLKYASRKPELSTEPVKFRKGANQVFRTCLLIDPEDFQPSELNYIPGNSEIPLVIQISVDDIDFPGQSEATLAGIEKLSEGIFTIKFMKQKIMVDGFCFITQEIYGIENKSGELNEFDGDDVDDNIECVICMNNLRNTIMLPCRHLCLCETCGEQMRTSSSRCPICRANFNALLQIKAVRKKKYPPG... | Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.27
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Length: 514
Sequence Mass (Da): 58282
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A0A8B7D854 | MKEYKKYIVINLLAAFIYICSSEPEGNVYQSIAHLEPLVEIERRLIKVAREYLDDEKFKLKSLQGFAKSVRESLELSKDDPIKYLGNPVNSYLLIKRFTSGWKDLADLLSINDEKANDIKTILKANEVFLPTYDIDMVGATAAMFRLQDTYNITAREIAEGEISGIKKTKHKLTAQQCLEIAEMAHDSRRYVHMASWLKEAERIMNDPTLKDRRGNITRLQINEFLAWMNYLSNDMKEALKYTNLVLKEDPSNAQALKNKPIYEWYVFHNQKGNEPESQYMEMAKQIQDVFIASRYARACRRDQRTKTIAVKDVNNLVCF... | Function: Catalyzes the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins.
EC: 1.14.11.2
Subcellular Location: Endoplasmic reticulum lumen
Sequence Length: 542
Sequence Mass (Da): 62507
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A0A0E9QBS5 | MLTALTMLALFYPNLLGDPDNFTPANPIVTPPHIKPEWYFLFAYAILRSIPNKLGGVLALLSSILVLIVVPILHTSKQRGLTFRPSLPTTILNFSSRYTSTNMNRRNTSRTSVHYHRPSSISTLFFPIPSAKPLVG | Function: Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membra... |
A0A7W4HQ69 | LTKAAGTLDPAQHNAQQLERATRAYHSYPKVRLPFYGQQRIITRAHTATEPSPYTIACLGDTWLAVDELVAPSGRRMGVADFLRGHRP | 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... |
A0A3P1SYC5 | MVYIELPSKKERKTSFYLAMEEYVAREVEVRDAFFIWQVAPSVIFGRNQSIENEVNTEYCRDNGVQMFRRKSGGGCIYADKDNMMLSFVTSSNHVGLTYNRYIMMVVGALHGIGIPVTADRRNDILIDGCKVSGSAFYHIQGRSVVHGTLLYDTDMRNMTESITPKGKKPESKGVKSTRSRITLLKHHTTMSIEEVRKSIIESICDSTKTLTADDVKKIEEIEKEYLGDGFIYGKNPEYRIKLEHKIGDKGKIEARMTVKNDIIKDIDLKSDFFVSDCTDAIRNSLRGIPLNRERITDALADNGGEINVNTYKEYIADAI... | Pathway: Protein modification; protein lipoylation via exogenous pathway; protein N(6)-(lipoyl)lysine from lipoate: step 1/2.
EC: 6.3.1.20
Catalytic Activity: (R)-lipoate + ATP + L-lysyl-[lipoyl-carrier protein] = (R)-N(6)-lipoyl-L-lysyl-[lipoyl-carrier protein] + AMP + diphosphate + H(+)
Sequence Length: 325
Sequence ... |
A0A4Q2ZLW4 | MKHYGLIGYPLSHSFSPAYFNERFRKEAIEATYTAYPLESIDAFPELVQQERLSGLNVTIPYKEAILPFLHQLDPHAAAIGAVNCMAFRNGRLTGYNTDWLGFRNSLVNRLNPLPVGALVLGTGGAAKAVVYALTQLQVPYRMVSRTFRNGGLVYEQLDPTVLAQYPLLINTTPLGTWPDVAARPPVPYELLTPRNALYDLVYNPEETAFLRSGREQGCAIKNGLQMLHEQANESWNIWQAFPGETGHSDLF | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.
Function: Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydr... |
T0M266 | MNSPSTILYFTSSFPDHRILCGFLYNVDPAVVKYVEVGFPSSDPRYDGPEIKETHEIAEKNFQSDHLEQYADILGKKNVRTYLLTYYRDLARQSSDFIPHLSDSGFSGVIVPDLLVDYSAIASDVITRIQGSLDFIPFFNPATPDGVIERISRMTESWIYYGLQPATGIRIPYDLEEVSRRIIELLPGREVNFGFGIRSMDQIGRIMDLGSKGVALGTLLVPMVRENRLDDFVELQEQIREVQDHVKG | 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... |
A0A2U9CI93 | MNQVCIWPTLGSSAVNSCHSDVNCLQPGTDWDKKTALDLTPQKGLTTVSSAVESMEQLNDPPVARRLVLCFDGHITLAPNDLRVQDNSNHFCTIGGSVAVLDLYQQSTAEASDERSTNQVVSEREVRKAVIVCVGGGDDAGAHRDDRCLPLRDRRDGCALIRISPCESGGRARFSPASRISIFRASQGVFEKGQIMPSAPFHRILRPLLFGTFILGCFVTLFLMYFKPSTSWLSGPVESTASTERVKNLFSTKSDKNVTTVLIWLWPFGQTYDLSVCSSLFNIEGCFITADRNLFNKSDGVIIHHRDICTDLSNLPPLQR... | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 555
Sequence Mass (Da): 63185
Location Topology: Single-pass type II membrane protein
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T2M2C5 | MNKKDNSDVFSSKEDNKKEDVLNDHSSHLAENDQVFILSNKVSSPLFKPEIDMTWLFLIGLAASLRIYNLSTPKAVVFDEVHFGKFISYFMKNRFFFDVHPPLGKLLYAAAGYFSGFDGSFEFDKIGQEIPPNQIHHVYVLRLVPSLFSVFLVPVVYEIILELGCTYWFAVLGGVLICFDNMLVVQSKFILLDSIMLFFIAFSICCYIKFVKEYTRPFCFYWWVYLVSLGISLTATFSIKYNGFLTILLLGGIIAYEMWIIMGDVTVPAKSVIYHMLARTGCLVVLPLFLYIVQFYILLNVLYKSGPHDNLMSSAFQRTL... | Pathway: Protein modification; protein glycosylation.
Catalytic Activity: a dolichyl beta-D-mannosyl phosphate + L-seryl-[protein] = 3-O-(alpha-D-mannosyl)-L-seryl-[protein] + a dolichyl phosphate + H(+)
EC: 2.4.1.109
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 553
Sequence Mass (Da): 63096
Lo... |
A0A2E0VWZ8 | MIISAIVARSKNNVIGLGNQIPWYLPADLKYFKKTTLDHHVIMGRKTFESIGRPLPKRTNIVVTRDIYFVASGCVVAHSVEEALELAKRNAEDEAFIIGGSEIYNLSLPYIDRLYLTEVLAEFEGDKFFPAIDLENWKEIKSEPFKADEKNEYDYVFKVLEKVNTEHDLS | 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... |
A0A1H7SNP8 | MATRSVVLEVRQIALATELISLGARLPLLEAETSLSRDRLTRLYKEVRGESPPKGMLPFSADWFMSWQANAHSSLFYNIFRVIRGHDGAPIQSIVKSYRLYLEHVQLHAVEPVLSITRAWTLVRYFAAGLLEGVACTRCGGHFVAHAHDPKSGFVCGLCRPPARAGKRGRRAGAARETGLPEHNDAPARG | Cofactor: Binds 1 zinc ion per subunit.
Function: Functions in complex with FlhD as a master transcriptional regulator that regulates transcription of several flagellar and non-flagellar operons by binding to their promoter region. Activates expression of class 2 flagellar genes, including fliA, which is a flagellum-sp... |
A0A7X3VSV2 | MAELTRAQIAEITRIARRAGAAIMDIYNRPGELEVVEKTDLSPLTRADIAAHEIITRDLGRLLPDIPIVSEEGDETANRRLLAAEKFWLVDPLDGTKEFIRKDVGHFAVCMALIEDNSPTFGVIYAPALDEMYYGGKEYGSYEELRGGGAVKLAGDGQPTGAVMVSRSHLRQETKEYIRRHYPDHDPLAVGSQLKFAHIAKGLADVYPRIEPYGCHTWDVAAGHAILEGAGGRMSRPDGAGMDYRNEDTQAGPFIARRP | Function: Converts adenosine-3',5'-bisphosphate (PAP) to AMP.
Catalytic Activity: adenosine 3',5'-bisphosphate + H2O = AMP + phosphate
EC: 3.1.3.7
Subcellular Location: Cell membrane
Sequence Length: 259
Sequence Mass (Da): 28517
Location Topology: Peripheral membrane protein
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A0A2I7ZG98 | FLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGVGTGWTVYPPLAGIQAHSGGAVDMAIFSLHLAGVSSILGXMNFITXIFNMRAPGVTMDRLPLFVWSILITAXLLLLSLPVLXGGITMLLTDRNF | 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... |
C7QJR0 | MSRADPAAGRFARLISGTALDVKTMMRFDVVIEIPAGSRNKYVMDHRLGRIRLERQLFTSTSYPADYGYIPGTLALDGDPLDAIVLLDDPAFPGVEVSVRPVAVYRSRDEGGQDDKILCVPAGDPRYEDIQDLGDVAQERLDEIGHFFDIYKDTEPGRQASPGTWADRAAAEAVITADRRRLAEAEAAAE | Function: Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions.
Catalytic Activity: diphosphate + H2O = H(+) + 2 phosphate
EC: 3.6.1.1
Subcellular Location: Cytoplasm
Sequence Length: 190
Sequence Mass (Da): 20869
|
A0A1G6QEZ8 | MERLFLLSARSRGLPVWVRYVATTLIVVVCLLLRLWIFGHQPGLPFLMFFPAVILVGLAFDRGTGVYAALLSGLLSVWFLVEPTGSLGIDKASDLLALILFLAIALFTAFVMEALHVALRRLAQERQGLAIANAELADMAKARGTLLSEAVHRARNDLQRLAATLHLQAGAVQEASARRALQDASSRIMALARINARLDEHRNDGHAVVQSRGFLEGLAQDLREAAVALRPIALAVQAEDHAVPMARAVPIGLIVNELVGNALKYAFPDEMDGRVSVQFRRDGEDFVLAVEDNGIGLDPAKPPQGSGLGTRISRALAGQL... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 347
Sequence Mass (Da): 37292
Location Topology: Multi-pass membrane protein
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A0A091TCM6 | RWKIQPNDFKRNYSPGQHPKVVYLLYEIRWSRGTTWRNWCSNNSTQHAEVNFLENCFKAMPSVFCSITWVLSTTPCGKCSRRIQEFLRVHPNVTLEIYAAKLFKHLDRRNRQGLRNLAMNGVIIRVMNLADYRYCWKRFVAY | Catalytic Activity: a cytidine in mRNA + H(+) + H2O = a uridine in mRNA + NH4(+)
EC: 3.5.4.36
Subcellular Location: Nucleus
Sequence Length: 142
Sequence Mass (Da): 17036
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A0A2G9FSD5 | MTSLTIRIIPCIDVDYNNVVKGTKFSDLTTIGSPSLLANKYSVSGADELCLLNVTASSDNKMILYDTISRIADTCFIPLTVGGGIRTIKDVECLLKAGADKVAINSASVMNPEFIANCVERFGSQCIVSSVDCKAVNGTWEVFSHSGLRSTGIDALEHICKLVQYGAGEILLTSIDKDGTNGGYDIPLLKSVSQLVNVPVVASGGGSEFRHVVSAIIEGGVSAVLLASALHYDRYSVSQLKYFLGRCGILVRDDYLSYGLCD | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 5/9.
Function: IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ... |
A0A3B9AMP6 | MQISDWYAIAKALHLIGMVSWMAGIFYLVRIMVYHAQSKEKAPEIRLVLQDQFTGMEWKAYKVIIQPAVVITWAAGSTMLFIQSAWLQQPWMHVKLTLLVLLTVYTHGLKDHVKKLEAGTSIRTHLFFRAWNEVPTIAMVGIIFLAVFKDRINFFTLFIGLILFVLLIGWGIWKVNRRSS | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; protoporphyrin-IX from protoporphyrinogen-IX: step 1/1.
Function: Catalyzes the oxidation of protoporphyrinogen IX to protoporphyrin IX.
EC: 1.3.99.-
Subcellular Lo... |
A0A935G302 | MQKTCFLLGFMGSGKTYWGQRLAEAAGLPFRDLDAMIECGEKNPAGQIFAERGEAAFRQLERTYLHLLAQGKPSIVATGGGTPCFFDNLAWMNAQGITVYLYTPVPVLVERLRRDNDRPLLKNIPPSGLEDYIRDLVSVREVFYQKAQFTVPFHLDSAVYLDRLLRVFSGAN | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.
Function: Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
EC: 2.7.1.71
S... |
A0A7W4EAN3 | MDTIRLFRRFQPTNYDITLDLQREKRTFTGKVVLDGTLHDGDAIPLHAKGLAITEVVIDGQPAQVSHHEHDEIRLIAPDLAPGEHTIAVTFSGTITDAMHGLYPCYYKVDGQPQELLATQFESHHAREVFPCVDEPEAKATFRLTLITETDTTVLSNTPIQNQQAKDGRLHTTFEQTPRMSSYLLAFVTGDLQVKRATTSSGIDVGVWATKAHPHSYLDFALDAAVRLIEFYRDYFGVPYPLAKCDHVALPDFSSGAMENWGLITYRETALLANPSGPVSSRRYVATVIAHELSHQWFGNLVTMRWWDDLWLNESFANVM... | Cofactor: Binds 1 zinc ion per subunit.
EC: 3.4.11.-
Catalytic Activity: Release of an N-terminal amino acid, Xaa-|-Yaa- from a peptide, amide or arylamide. Xaa is preferably Ala, but may be most amino acids including Pro (slow action). When a terminal hydrophobic residue is followed by a prolyl residue, the two may be... |
A0A8D3E5Y1 | QTWQLRRRSGPPHGGTCPDGYRALSTGELRELLRDDDKMDRIIRLNETKFMEGNVSVDEFLDAFQSSRKTYHVRRAQAEKTQEIAQATRQPCKSNPGTPLPGHGQPVGLRVIGQLSGGWPANGRPVRVQQLYRPNPQQPEPPFR | Function: Component of the ESCRT-I complex, a regulator of vesicular trafficking process. Required for the sorting of endocytic ubiquitinated cargos into multivesicular bodies. May be involved in cell growth and differentiation.
Subcellular Location: Endosome membrane
Sequence Length: 144
Sequence Mass (Da): 16282
Loca... |
A0A8D3CJM1 | MIRAILIFNNHGKPRLSKFYEHYSEDTEQQIIRETFHLVSKRDENVCNFLEGGMLIGGSDYKLIYRHYATLYFVFCVDSSESELGILDLIQVFVETLDKCFENVCELDLIFHVDKVHNILAEMVMGGMVLETNMNEIIMQVDAQNKMEKSETLLFHRPNTSPKSATIESLTSSKFDMQ | Function: Part of the AP-3 complex, an adaptor-related complex which is not clathrin-associated. The complex is associated with the Golgi region as well as more peripheral structures. It facilitates the budding of vesicles from the Golgi membrane and may be directly involved in trafficking to lysosomes. In concert with... |
A0A8B7D907 | MENESDSLLLNLEPYTPKEKSAYVKKKSIQKEKGYEQKKSFVKSTHSNLIKSKSQSYVDPAHFTTISSLFNKNPDIPQVISNNNVSNVEEVVFSSENVSDLPISDRLRNNLRDQFKFKSLTQIQMISIPPLLNGKDAMIKSPTGSGKTFCYAIPIIDKIIKMKPSIGRQDGPFALIIVPTRELALQTFNIVQDLCKSCISIVPGMLIGGEKCKSEKARLRKGINIIVATPGRFQYHLKETSCLNVSKIKYLVLDEADKLLSMGFEKTIKEILGFLDQHSSLKRQSVLLSATLSKDIENLASLSLSNHVFVDSSKKDDFDP... | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 657
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): 74720
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A0A8B7DH20 | MKITDENLLKHKPELRGKSYIAASYVKFVELAGSRAVAITPNLSDNQLNTIFNSINGLLFPGGNVNLVDSKYYYLTKRLAEMASKLNDEGIHFPILGICRGMQALVKHSKELMVPTDSQNFTSSLKWHKESPLFRNSFYLIKKDTELYNITSHFHQYSFLPTISINTTFDVIATSIDRKGKEFVSIIQDRTLPFYGVQFHPEKILFEWAPTIAIPHNSKAVRFSQSIANGFMDEARKNNHSFKSYLDENNFTLVRQNPIYIGDFLDSHSPFVQIYTFP | 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: 278
Sequence Mass (Da): 31859
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A0A1W0WKP7 | MRKHILLVTIPSYGHIIPLLELARRIAPFHRVTFAVSQFELGEIRQRELVSSEDPFTLHGIPDGYFLLESEKSQSGQIFQKIHQFVIPGTVAFLKALPIPSPHDTDHKNEGSAPSLQDPVDVVIGDNILGVALRVLHERGIPFHIFNTASSSMTYVSLLVCEDTPSRPDPPNDNQMKFIEAPDPTVTPKPISDAIKTMFLQMHEMTLLAAGIVENSVYELEVDAVEAIRKHPDMQGRPFRSVGPLIPTTERTSGTNGERAKEIEAWLDKQESLSVIYISFGTVAAPKVADMQEIIGALKAIGKPFIWSLRKEEQARLPAE... | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
EC: 2.4.1.17
Subcellular Location: Membrane
Sequence Length: 463
Sequence Mass (Da): 50889
Location Topology: Single-pass membrane protein
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A0A386M5D8 | IRAELGHPGALIGDDQIYNVXVTAHAFIMIFFMVMPIMIGGFGNWLVPXMLGAPDMAFPRMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSFXIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGITFDRMPLFVWSVVITALLLLLSLPVL | 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... |
A0A4Q6ASN3 | PVPGAMALIGKGLYFSRLASYRQALSAFQEANRLLININADSLKGRCYAGAGNCYKNMSEYPAAIENFQHALEWYSKTKNPEYIAGIHSEFGQVYQLKGDLDRARHHLRIALSLLADNKHSPAYLNTAHTMANVYGMSNLLDSALLLDREGLDIALKMKLPVLQSPFLDNIANCYFYSGQTDSAAWYFKKAMAIDSASGNKKQISDGFANLGYMESVKGSFRQAESYYRKSLDFAHAAGYKQGVRKAMDYLALLYAKHGMFDRALAAREQYIAVNDSIRNEKTEARLAELTTLYETKKKEQQLAVQAATLSSQRMFIVVI... | 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... |
A0A6I5YNE9 | MRIGIATIIGGTMVLASGVMAARPDWRWPAFPAGVTAPALPQGSSMSAARVALGRRLFYDRALSHDNSMACADCHSQARGFTDGQPTHVGATGEMGVRNVPGLTNVAWRGGLTWTDAGLTTLEAQAMVPMTGRKPVEMGMAGDDAQLARRLDADPCYRRMFARAFPGAKGDMGYAGVTAALGAFQRTMISFGSPYDRGALSPLARKGAAQFAAAGCAACHQGPDFTDGQVHYVGTAAPGEPDGSLYGGKPPPPGFEPPPERFRTPTLRNVAVTGPWLHDGRSGSIDQAIRRHAAAQLAGVEMPALLAFLDSLTDREFLER... | PTM: Binds 2 heme groups per subunit.
Cofactor: Binds 2 heme groups.
Subcellular Location: Periplasm
Sequence Length: 334
Sequence Mass (Da): 34968
|
A0A930RT45 | MFNRKKPQQTPPRELTPWELAQQNSPRVEQPVPEEPVQKVKKKKEPRPKKTKPKSQGITNATLLKGIFIVCAGWSIYFISPLSKVSDIEVVGLNQVPVELVQENDGINKGQSIWTVLANRYRTANLLKNASPKIKDASVQLVAWNKMRLNIEENPAVGYYQSDDKHYELLADGQIIEVEADATPKDYPLLYMFTDDTQYKALAKQLEKVPASVIREIVEIQYPNDTKNHQKIYLKMKDGNRVIGNLKDIGDKLGYYPSITKQLNGKKGTVDMEVGIYFTPDTTVQ | Function: Cell division protein that may be involved in stabilizing or promoting the assembly of the division complex.
Subcellular Location: Cell membrane
Sequence Length: 285
Sequence Mass (Da): 32357
Location Topology: Single-pass type II membrane protein
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A0A2N1W4L1 | MVNNSNIERVIGLVKESVKKYKAPVLERFNDEIKDPFWVLIPCILSLRSKDETTAVVARRLYNFAPRPEDILKIPQAQLEKMLYSTGFYRQKAKSVSQITKLIIEKYKGQVPDTIEELLTLPGVGRKTANLVVTVAFKKPGICVDTHVHKICNRWGYVKTKNADETEMKLRKILPKKYWIKINYWLVLYGQNICLSVSPKCSGCLLFSYCPRIGVKKSR | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: DNA repair enzyme that has both DNA N-glycosylase activity and AP-lyase activity. The DNA N-glycosylase activity releases various damaged pyrimidines from DNA by cleaving the N-glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The AP-lyase activity cleaves the ph... |
A0A2H6CGG9 | MLSSCAWYFNKRFPRITYKKFLLFFVLFSATVANIGLEKLIQFSVPVLNVVYPVIIALILLSFINKYVSCDTIVYRSVVGIILFVSLNDGLKEFNSSWDYITPFVTLPFSDLGFSWIIPAVVVGVIAKGISFAWRK | Function: Component of the transport system for branched-chain amino acids.
Subcellular Location: Cell membrane
Sequence Length: 136
Sequence Mass (Da): 15461
Location Topology: Multi-pass membrane protein
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A0A1W0WM43 | MVDYEIDPSYGDTISADQQDNLTKRDRKKGGGKGDLPVGQSSPEKRVTFLEQDVHGEFRGRPSVPGPSAYETQPFRSSYMDSQFTENIGRQMRVPDQIRPYEESAGSYIGYQNNGVRANAMQQMSVPDRILVAGNDQHLSMRDNRPRELELDDMLYGFRGASNQPVQVQTPPRTLTVNQHSFPAANGLDSEPIEDGPMIAPFSASALSENNNMEQSLNLQAEKNMTSSLRGSKSIMLRSAGALTPSGRSGLPDTPGTRLVIDLYKRVEVLERENHYRYLREMVGYALVLGYVALKSMSFFIKR | Function: Plays a role in mitochondrial and peroxisomal fission. Promotes the recruitment and association of the fission mediator dynamin-related protein 1 (DNM1L) to the mitochondrial surface.
Subcellular Location: Membrane
Sequence Length: 303
Sequence Mass (Da): 33834
Location Topology: Single-pass type IV membrane ... |
A0A1W0WMG9 | MALSSKSSKSDFIPEAGDQQQLDHGLKGGPAVAELPNLAYPLTSASISPQVNSAWSYRDALAKPRLPISVSTVPEKSILPSLTNVSKEPPDFAFISDPDTLDYLAGVGSKLMIILRGVSGSGKSTLCVRIKKELTEAKVQVDVASADHFFNQPDGTYRFNPALLQQAHEACQRDCERFCAAEESRVVVVDNTNIFEWEFRPYIQLAHRYHFVTLLIEPRTAWRYDWRQLAKRSTHGVQASVIESKVEKLKRNVVIPVYYGFMVSADDSGKLRLLAAKLARTMLQVDELSQAADGEADLLVNEFAKRSDDELVAWKESDQF... | Catalytic Activity: a nucleoside 2',3'-cyclic phosphate + H2O = a nucleoside 2'-phosphate + H(+)
EC: 3.1.4.37
Subcellular Location: Melanosome
Sequence Length: 468
Sequence Mass (Da): 51815
Location Topology: Lipid-anchor
|
A0A481XSB6 | RMNNMSFWLLPPSLTLLISSSIVENGAGTGWTVYPPLSSNIAHSGTSVDLAIFSLHLAGISSILGAVNFITTIINMKLNNLSFDQMPLFVWSVGITALLLLLSLPVLPGAITMLLTDRNLNNSFFNPAGGG | 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... |
A0A159PU16 | ILIRAELGHAGSLISNDQIYNVIVTAHAFVMIFFMVMPILIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLILLLSSSIIENGAGTGWTVYPPLSSNISHAGASVDLAIFSLHLAGISSILGAVNFITTVINMRSSGITFDRMPLFVWSVLITAILLLLSLPVXAGAITM | 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... |
A0A090S0R9 | MWIGCSDSRVPAERLTGLYSGELFVHRNVANQVIHTDLNCLSVVQYAVDVLKVKHIIVCGHYGCGGVNAAIDNPQLGLINNWLLHIRDLYLKHRNWLGELPREMWVINSVK | Function: Reversible hydration of carbon dioxide.
EC: 4.2.1.1
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Length: 111
Sequence Mass (Da): 12590
|
A0A1X0QA56 | MKPLKVTMTNSLVMHYNLHKQMDMVEPYKATYKDLVNFHSPEYIKFLSTVSPANENSFLPEVNRFNVKDDCPIFPGLYDYCRSVAGATMMAANKLNSGEYETIINWSGGFHHAKVCEASGFCYVNDINLGILELLKIHNRVLYIDIDVHHGDGVEEAFYITDRVMTASFHKYGDFFPGTGRLDDVGFGKGKNYSINVPLKDGIDDKSYEDIFVPVIQKIIEVFQPSAILMQCGGDSLSGDRLGCFNLTHAGHGRCVEFVKSFNLPLILVGGGGYTIDNVAKAWTYETGIVVGSRLDEDIPYNQYLTYFAPNYKLKIPPMS... | Catalytic Activity: H2O + N(6)-acetyl-L-lysyl-[histone] = acetate + L-lysyl-[histone]
EC: 3.5.1.98
Subcellular Location: Nucleus
Sequence Length: 407
Sequence Mass (Da): 45951
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G9G775 | DILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYHIETVVGEENQYIAYVAYPLDLFEEGSVTNMFTSIVGNVLGFKALRALRLEDLRIPPSYSKTFQGPPRGIQSERDKLNKYGRPLLGYTIKPKWGLSAKNYGRAVYEHLRGGLDFTKDDENVNSQPRWRDRFLFCAEAIYKAQAETGEIKGHYLNATAGTCEEMIKRAVFARELGVPIIMHDYLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGMYFRVLAKALRMSGGDHIHAGTVVGKLEGAREMTLGFVDLLRDDFIEK... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Catalytic Activity: 2 (2R)-3-phosphoglycerate + 2 H(+) = CO2 + D-ribulose 1,5-bisphosphate + H2O
EC: 4.1.1.39
Subcellular Location: Plastid
Sequence Length: 376
Sequence Mass (Da): 41796
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A0A7W1ERR0 | MSLLDMSYGDEAPQIVNAVIENSKGSRLKIEFDKDLETFVLDRVHQTHLGSPAEYGFIPSTLDEDGDALDVLLISDDPMPMGLTVPMRVVGVMYMIDSGEVDNKLVGVPAHDKVYDNIQDIGDVSKHWQNSVQHYFEHYKDLKGDTVEIKGFAGVDEAIKVFDECVERYKK | Function: Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions.
Catalytic Activity: diphosphate + H2O = H(+) + 2 phosphate
EC: 3.6.1.1
Subcellular Location: Cytoplasm
Sequence Length: 171
Sequence Mass (Da): 19196
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A0A2N1W2T8 | MAKKAAIKRKTKETDIDLSLGVNKSGAYKIDTQVPFLTHMIEQLSRHSNVDIALKVKGDIQIDAHHITEDTGIVIGKALAKALGDKKGIARFGSACGVLDEALVRVVLDLSGRTYCEVNLDLKEKKTGNFDTELIEEFFHGFARGGNLTLHVDQIKGKNTHHIAEAAFKGLALALKAALKKDGITVKSTKGSL | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 6/9.
Catalytic Activity: D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
EC: 4.2.1.19
Subcellular Location: Cytoplasm
Sequence Length: 193
Sequence Ma... |
A0A220EZ95 | FLFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLMSSSMVENGAXTGWTVYPPLSSIIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGITFDRMPLFVWSVVITA | 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... |
A0A0E9RYW6 | MHLLPNFAECWWDQVILDILLCNEGGIWLGMTVCRFLEIRTYHWASIK | Pathway: Lipid metabolism.
Function: Catalyzes a base-exchange reaction in which the polar head group of phosphatidylethanolamine (PE) is replaced by L-serine.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + L-serine = a 1,2-diacyl-sn-glycero-3-phospho-L-serine + ethanolamine
EC: 2.7.8.29
Subcellula... |
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