ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
|---|---|---|
A0A6P1MC90 | MIRILVVDDSETVRKLMTYELDRQEGMTVVGIASNGMDAVRKAAKLKPDVITMDVKMPIMDGLEATREIMCTQACPVVIVSQYWDQDNKQKVFEALAAGAIAVVNKPAGPGHPEYETSLSHLFKQIRMMSEVKVVTRRRSKPDPEKVPATVLKKSGVSCPPACRPDCPVSKRNGKLVVIGASTGGPVVLRQIFERLPAPYPLPILVVQHIAHGFLTGLVDWLGTATGHHILIAEQGMIPEPGKIYFAPDDRHMGLDPDGRIVLSKDPKEYSLRPAVSYLFRTAARHVGNRTIGILLTGMGSDGAAELKILKDTGAATVIQ... | PTM: Phosphorylated by CheA. Phosphorylation of the N-terminal regulatory domain activates the methylesterase activity.
Function: Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate resi... |
A0A520TVS1 | MIYFLPNLLTIFRFFLVYPVVICIFEKQFILAIGFFVLAGISDFLDGYLARKLEAISEFGMIADPIADKTLIIGTLVSLSIVGEIDLWLAYMILGRDMIAVVGFILASILLSPYKVKTHFSGKAYTAFLLVFLGITILASAEIFYYQLLNVLIISVLIFSIFFSLFDYFRDPGLRLLKKVF | Pathway: Phospholipid metabolism.
Subcellular Location: Membrane
Sequence Length: 181
Sequence Mass (Da): 20500
Location Topology: Multi-pass membrane protein
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A0A525C5Z5 | MKKILLTIALIFTMVAHAEVETIEKIAAVVNDKIILKSELDKELEISLNNFAASGGQLPPKNIIKEKVLEHMIIRKLQLSMAEKAGINIDDQQLDEAIRSIAKKNNLTIRQLAEEVEKQGGSFADFRESIRIEMITRQLQMRFVSRKINISEKDVENYLLSRKNAPQEEKQYKLAHILIEIPEAATPEEIKKQKELAEEVKGKLEAGEDFTRMAVSYSDSGSALKGGVLDWMTEQQVPSIFAEAVPDMKKGELSGIIQSPSGFHIFKILDIKGNETRIVEQNKVRHILIMTNEITSDDQAKQKLEQLKERIIQGDDFAKI... | Function: Chaperone involved in the correct folding and assembly of outer membrane proteins. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane-associat... |
A0A5J6V8R9 | MSGVTGLPDSAEGALGPVLVLIGPPGAGKSTVGQVLATRLGVPVHDSDRMIERAQGREISDIFVDDGEAFFRELERAEVLRALEEETGVLALGGGAVMQEQIAQALRASGRPVVFLDVSIADASRRIGFDASRPLLLVNPRASWTRMMNTRRPTYEELSTVQVSTGGKDPEQVADEVLSALGLAGSA | 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... |
A0A0X3Q282 | MPHVTVYRAARLKRYFAPFVSFATFFRLTFFVSSLFIPFLIAYRSSGFWLTRIISFEQPLFKATREIYFEAHSVDQTYSWSTIPGLNPQLTSSLTVPALYFVEFDDNNDGILDGCNLAFSLPITDTVIMFYALVVLAKTNGVRLLLMLSL | Function: Transmembrane component of the tectonic-like complex, a complex localized at the transition zone of primary cilia and acting as a barrier that prevents diffusion of transmembrane proteins between the cilia and plasma membranes. Required for ciliogenesis and sonic hedgehog/SHH signaling.
Subcellular Location: ... |
A0A2E0GR43 | MNSADEILKNAADSFAAITKISDDVEKAAQMITEALRQGGKVFFCGNGGSAGDAQHLEAEFLGRFLKERQPLPAIALTTNASAVTAIANDYDYSEIFSRQLQGLAKTGDVLVGISTSGNSANVIEAIKMASECGVKSIALTGXNSSEAGNLADIAICAPSTHTPRIQEMHIAIGHTLCEIAENSLSET | Cofactor: Binds 1 zinc ion per subunit.
Pathway: Carbohydrate biosynthesis; D-glycero-D-manno-heptose 7-phosphate biosynthesis; D-glycero-alpha-D-manno-heptose 7-phosphate and D-glycero-beta-D-manno-heptose 7-phosphate from sedoheptulose 7-phosphate: step 1/1.
Function: Catalyzes the isomerization of sedoheptulose 7-ph... |
A0A523LMT6 | MRRWFDSLEEREKILVLTAAVFIVCVAFWFGVWTPLDSGQKSAAARVEVWKVSLAALRPLKGQIQGSASGQSIQAGQDQSLVVIIDSTLRQRGLYESLQRSQPTPAGNGIRVEFESAAFDDMMLWLGDVNRQYGLLVQSGSFSLAAGDNPGRVNSTLTLER | Function: Inner membrane 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: 161
Sequence Mass (Da): 17704
Location Topology: Single-pass membrane protei... |
A0A8T7B3F3 | MTTSTSVRDDGPADYDAAYQTRFDIIAGWVENILLITVLLVMVLVASSQIVLREFFGAGFIWADELLRILVFWLAIVGGMAAARVNRHLRIDALNKLVGARAETAIMIAVSAVVVAVSTLFAWHAVRFVWDAYQFEEQVLGNVPAWPFLTILPFGMFVIALYYLRHAVVAAWRTVKGFVPTS | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 182
Sequence Mass (Da): 20234
Location Topology: Multi-pass membrane protein
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A0A357KRC8 | MSLEVSRDVKRAAAVLKTGGVIAYPTDTVFGLGCLPTNVAAIQTVLDIKKRSASKGLILLGANRAQLEPYISTDLSDADWHAITANQSEPTTWLVPAADGASSLLRGDHATIAVRITRHPASCALCVAANSAIVSTSANLSGQSPASAWDALPVEISKSVDLVLNDTCGNPDQPSRIRHLKNGNLLRG | Function: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Catalyzes the conversion of L-threonine, HCO(3)(-)/CO(2) and ATP to give threonylcarbamoyl-AMP (TC-AMP) as the acyladenylate intermediate, with the release of diphosp... |
A0A948AKL2 | MFHRMLDRMEEWLILSFMATATLVTFVSVAMRYLMGTGFTWATELTIYLFIWMAKFGAAYGVRTGIHVGVDYVVNKLEGSKRRYLVTTGIVLGIIFTGVISFFGVRWVIFIHGTGQISPDLEWPMWIIYLAIPFGSGLMCFRFIQSLTKFLRSGETTSAGPVADLREGALKEDAK | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 175
Sequence Mass (Da): 19757
Location Topology: Multi-pass membrane protein
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A0A523KKR1 | MQTNLPQDLLDTVSGKRADEILRACVHCGFCNATCPTYQLLGDELDGPRGRIYLIKGMLETGTGHSTVQTHLDRCLTCRACEPSCPSGVAYGELLEIGRDTLARHRRRPLLERLTRVALVHVVSRPALFRILVRLGAWIRWALPERLRGLLPAAPAGIRERSPREVVDVKRRVVVLEGCVQRVATPASNAALRRLLQDNDIGVLEISGEQCCGGLALHLGQTERAHQSMRRNIAALVGAGDGGETILSSASGCGVTVKDYGRLLAEDPLWSRKARRVAERTLDVAEFVDREQLRLRRDARFTRVAWQAPCTLQHGQGISG... | Cofactor: Binds 2 [4Fe-4S] clusters.
Function: Component of a complex that catalyzes the oxidation of glycolate to glyoxylate.
EC: 1.1.99.14
Catalytic Activity: (R)-lactate + A = AH2 + pyruvate
Sequence Length: 406
Sequence Mass (Da): 44276
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A0A6L7KYV4 | MRPTILLLVLLLSWLQYALWAGDKNVFDLKRLDAAVERTVQENIRLEQGNQRLLAEVIDLKQGGETVETLARFNLGLIKENEIFYQIIE | Function: Essential cell division protein. May link together the upstream cell division proteins, which are predominantly cytoplasmic, with the downstream cell division proteins, which are predominantly periplasmic.
Subcellular Location: Cell inner membrane
Sequence Length: 89
Sequence Mass (Da): 10312
Location Topolog... |
A0A520TH25 | MFNLPEILTIVIGALLALVFIDGIRRAIRIKRSSLKVDLIDVEEYVSKDFEEEWMQGFSDEPSEQEFEDKEEEMLVDIKPSNSLLILHLSSQRKDQFSKDSITEAINDLNFVYDEKGLFTILDEKRNIAFNILNGKKPGTFLEDNVSDDLALVLDPTNLSSPLESFDLLIDVSQSLKENFKCEILDEDRNLLTKQMIEHMRQQVLEYRRQFLASAG | Function: Essential cell division protein that stabilizes the FtsZ protofilaments by cross-linking them and that serves as a cytoplasmic membrane anchor for the Z ring. Also required for the recruitment to the septal ring of downstream cell division proteins.
Subcellular Location: Cell inner membrane
Sequence Length: 2... |
A0A3C0L604 | MNLDSLTNHSIALIQGFCTDDHSITCAFSGAEDIVVLDLIQRTTRLIPVFAVDTARLHPETLAYVHQVQQHFNLDLTWIKPNPDAVAAFERQNGRFSFYEDGHLACCNLRKTEPLRAHLAHFDGWLTGLRRDQNPTRGALPELQIDPVFEGLSGPLKKANPIANWSREDIETYIKLRNLPQNPLVPRGYKSIGCAPCTRALKPHEHERAGRWWWEAGSDKECGLHQTPLQVSNTVEGPPLSQGQS | 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... |
A0A523LBX2 | MEDQIQTLADASLPWLSWLGPYVWLQAIIIVVVSLALAVASERLIVTTIGKLAKKTQSQLDDRIIEALRRPLFVSIFFIGLAVATYRLELAPTLTSVTLACLGTIATFIWLGFLIRLAGEVLAILSRISGRYEFVQPSTLPLFDNSAKLILMLGALYFIFLAWGINVSALLASAGIIGLALSFGAQDALANIFGGMSILADRPYQVGDYITLDTGERGEVTHIGLRSTRLLTRDDVEISIPNSVMGNAKIVNESGGPYQKFRIRIKVGVAYGSDLDEIEQVLVQTAIDHEEICDTPEPRVRLRGFGSSSLDFELLAWVEQ... | 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... |
A0A2E1ZMX3 | MVCEALIDFSVSDLNLHFVSNVDPAHLNGILKNLVPATTLFIIASKSFTTIETQLNAETAKTWLLSGMESTDLIKNHFIAVTSNIDAAREFGVEETNVLPIWEWVGGRFSLWSAIGLPIALLVGMPQFRELLAGAHSMDEHFQSTELNENLPVIMALLSIWYSGFFDCHSSAIVPYSQYLKLFPSYSQQLYMESLGKRVDIHGREIQTNSAEVLWGTVGTSGQHSYFQLLHQGTEFIPVDFIAFINTIDKSLNALERHQHLLANCFSQSLALMSGKPASGQASRSIPGNKPSNTLLISQLNPHNLGCLIALYEHKTFAQS... | Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Function: Catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate.
Catalytic Activity: alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate
EC: 5.3.1.9
Subcellular Location: Cytoplasm
Sequence Length: 372
Sequence Mass (Da): 41369
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A0A1H2TPL8 | MNISQYAPVVLFVFNRLDHAKQTIESLKKNKFSDKTDLFIYCDNYLKIKDEEDVRKVKDFVYTVTGFKSISIIEREQNYGLAKSIKEGVSSVIESYGKVIVLEDDIVTSPFFLSYMNKALQIYANEERVMHISGFNYPINNSEFESSYFSSMSACWGWATWKRAWDKFENNIELLENKITEKGKDKFIVSSNFTYWEQLILNKKKKLKTWFIYWYGTIYINNGLCLYPKSTYTQNIGLDGTGTNSQNGNVYYSELNTRDIDFFPSKIEEFENSNNSFKEFFDRVEKSKFEKYIINLVIKIFGLEGYKKVKKVISK | Pathway: Protein modification; protein glycosylation.
Subcellular Location: Membrane
Sequence Length: 315
Sequence Mass (Da): 37025
Location Topology: Single-pass type II membrane protein
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A0A2D4PJD7 | MKDPHLCPEGSQCLQASKCVLQLPENTEGSLAIDNEEHEAMTVEVKLLPRKLHFFCDARRKVKCFKHPSLLSTTRIINDQHDVNAINFQEVHEKATVALRIQAHSTGMVSGQCLVLAG | Pathway: Lipid metabolism; glycerolipid metabolism.
EC: 2.7.1.107
Catalytic Activity: 1,2-di-(9Z-octadecenoyl)-sn-glycerol + ATP = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + ADP + H(+)
Sequence Length: 118
Sequence Mass (Da): 13146
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A0A8T6HYW0 | MIPTVRAAVFLGMLATAGCGFQLRTWDLATTFQTVHLEAERGVNLHRDLGEALRSAGVRVVSGDADVVVALSDQRSDRRSASVTSDARTAEYELSLQVTVAVSDAEGTLLTESVLRSERVARLDRNSLVGSSEEGTLLVEEMRSDLVGRMLRTLDVLSRQAAGDGAATTTTNSGTEETSGAD | Function: Together with LptD, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane. Required for the proper assembly of LptD. Binds LPS and may serve as the LPS recognition site at the outer membrane.
Subcellular Location: Cell outer membrane
Sequence Length: 182
Sequence Mass (D... |
A0A8T7DWB4 | MVEFAELPVWVLVAIPVIVILFLLTLNQSRKKTNRKSHFSAEYFRGLNYLLNDEQDKALDIFVKLVETDWETIDTHFALGKIFRKNGEIDKAIKVHQGLIARPSLPDKYRNRVLLELGYDYLGAGWFDRAEGLFKEVLIHDPKSEMALNNLILIYQQEKDWHKAIDAAEILFSEKPAKVGSMISQYYCELADIARAKGDVSLVENYANQALRYDSSSVRATLLIADMAMEARDYKKARSMLLRIEKQDAEFIPMVIDKLVECHHHMDEPEALMDYMNDLEERQAELPLLESHAKVIELYKGKEDAIGYVMEKLSKAPSLR... | Function: Modulates cellular lipopolysaccharide (LPS) levels by regulating LpxC, which is involved in lipid A biosynthesis. May act by modulating the proteolytic activity of FtsH towards LpxC. May also coordinate assembly of proteins involved in LPS synthesis at the plasma membrane.
Subcellular Location: Cell inner mem... |
A0A524ATF2 | EMAHIILRGGADGPNYDRECIKKTHNQLKEEGLLAKIMVDFSHANSQKKFKNQLLVGDEIAKQVGDGSDKIFGVMIESHINEGNQPVGPLESLEYGVSITDSCIGWDDTENLLKTLAQAVQKRNS | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 1/7.
Function: Stereospecific condensation of phosphoenolpyruvate (PEP) and D-erythrose-4-phosphate (E4P) giving rise to 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP).
EC: 2.... |
A0A8T7A4X1 | MTTPDANNNVIGLVLAGGQSTRMGEDKALIDYHGKTQLESSVELLSEFCPEVFVSVSQANQNEETRQQFPTLVDDPDVQGPLAGIISAFRQFPNQTFLVVACDLPLLNRETLQYLLSQRDPGKQATAFISEFDGLPEPLCAIWEPDIVANIQAAIENGKSCPRKVLLNSDIQLIALPYQHALDNINTPDERDALSQS | Function: Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor.
Catalytic Activity: GTP + H(+) + Mo-molybdopterin = diphosphate + Mo-molybdopterin guanine dinucleotide
EC: 2.7.7.77
Subcellular Location: Cytopl... |
A0A2E9FHB9 | FGKRGIEGMIIAANYARRKNIPYFGICLGMQIAIIEFARYEAKLNQANSTEFNKSTPHPVIALVTEWKDKSGKLEQRNPNSDLGGTMRLGGQKCKLKKSSLSYRLYKKDKIIERHRHRYEVNPNYKDKLIECGLEITGMSSDNKLVEMIEIKKHKWFIGCQFHPEFTSNPRDGHPLFNNFILKALKSTK | Pathway: Pyrimidine metabolism; CTP biosynthesis via de novo pathway; CTP from UDP: step 2/2.
EC: 6.3.4.2
Catalytic Activity: ATP + H2O + L-glutamine + UTP = ADP + CTP + 2 H(+) + L-glutamate + phosphate
Sequence Length: 189
Sequence Mass (Da): 21806
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A0A7C1TYK2 | MNTQKRIIFFISDSTGITVEKWGHSLLSQFPDIDFQIISLRYVDSLEKIAKTRKQIEVAAKNSGMPPLVFSTLIELPLRAALKTEVAVFLDMFENFLDLLEESLQQKATHVRGSTHRITGQGTYMVRMDAVNFALRNDDGLRTQDYAQAEVILLGVSRSGKTPVCLYLAMQYGIFAANYPLVGEDLQFSLLPALLQGFRQKLFALTIEPQRLQKIRSQRHSGRHYAQIGQCRQEVAQAEELFAVNHLPVLDTSSVSVEEIATQILMQMQLKYVTP | Function: Bifunctional serine/threonine kinase and phosphorylase involved in the regulation of the phosphoenolpyruvate synthase (PEPS) by catalyzing its phosphorylation/dephosphorylation.
EC: 2.7.11.33
Catalytic Activity: [pyruvate, water dikinase] + ADP = [pyruvate, water dikinase]-phosphate + AMP + H(+)
Sequence Leng... |
A0A496VA32 | MKIGTPLSQSATRVMLLGCGELGKEVIMALQRFGVETIAVDGYLHAPGHQVAHRSHVVDLSNADALYELVAQERPHFLVPESEAIATELLVEIEQDGLTKVIPTARAASVSMNREALRQLAAEELDLPTVRYAFAKSYNELQMQINRGVGYPCLVKPMIAISGKGHSEVKGPEDVKAAWNYAMDSSGDNCSSVIVEEFIKFDYEITLLTVRAFGAAGEIETHFCEPIGYLKKQGHYVESWQPQRMTPASLHYARELAKKLTESLGGVGVFGVELLVKGDKVWFNEVCPYPHYAGMVTMATQAQNQFELHARALLGLSVST... | 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 (formate route): step 1/1.
Function: Involved in the de novo purine biosynthesis. Catalyzes the transfer of formate to 5-phospho-ribosyl-glycinamide (GAR), produ... |
A0A8S4C1W5 | MTFATKLYTKLFGEQVGQDEFGNIYFRSTRILRDFGRENRWVCYNGLPIGGKVPSTWFLWLHYQADLPPNKNDAIHKSHHWEKNHMPNLTGTSFSYSPNKTDKRVKQSYKPWRPEVNE | Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
... |
A0A0X3PAX5 | SLPHSLYGSMTIFGWLLLPRLAFDRLQQVYARYIQLAVTLIGCASALEIFDFPAIFWLFDAHSLWHGSTIGIHYLIVKFAIRDCKYISSRQLALPKTRIL | Function: Involved in the lipid remodeling steps of GPI-anchor maturation.
Subcellular Location: Golgi apparatus membrane
Sequence Length: 100
Sequence Mass (Da): 11500
Location Topology: Multi-pass membrane protein
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A8MDA9 | MERAFTVASEDEVIRGEVTDVYFIRTVDVLKAAGLDKVKVRAEFHVMSLPRDYEWAVYTGLSEVLELVRRAGLKVNVYSMPEGTVFQAKEPLMIIEGNYIDFAVYETPILGILRHYSSISSKAARIKYRAMNKQCLFFGARALHPIIQPMADKAAYMGGCDGVANVVGARLLGIPASGTMPHALMIVFKAVKNDHTLAWVWFDRVVPGDVPRIVLADTFLDEREEALMAAKLLGERLSGVRLDTPSSRRGNMKAIVEEVKWTLELAGYRNVKIIVSGGLDEEAVSELSDLVDSFGVGTSIAFPPSVDISMDIVEYYDEGL... | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-ribonucleotide from nicotinate: step 1/1.
EC: 6.3.4.21
Catalytic Activity: 5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O + nicotinate = ADP + diphosphate + nicotinate beta-D-ribonucleotide + phosphate
Sequence Length: 413
Sequence Mass (Da): 45568
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A0A2E2YRA9 | MDNMELPDTTFSRIVDGVIVRVGRSLSWLWVILLSVIVVNVLLRYLFGEGRVEFEELQWHINSVAFLTAIVYAYKTDSHIRIDLISSGLSSRARVWIEMYGTLLLLLPFVVSIFSFSLSFVAHSWTVGEISQSPGGLPYRWILKSILTGAFVFLMLGICARITRLWAFLSQNHTDELT | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 178
Sequence Mass (Da): 20259
Location Topology: Multi-pass membrane protein
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A0A0X3NHR4 | MDRLTVLTSLVVCRTMKRRHVDLLLGVVHAAVAFYLVYLTNEVQPTAYMDEYFHEKQTHAYLAGRWSEWDSNITTPPGLYLLTAIFLKSREIFLGDNTRQDLNVTHFRYLNALHLGVNAFLVSSILSHLNRLPLPLHLLYLTSIVTLPVLFFTSFLFYTDQVSLAAVLATALAFLYKRRLTAFLLACFACSVRQTNIVWCAFLVGMSIASRLSSIRRKRGSPTEASPFSWFCVLLRSPVRVIQAVIQGIAYDAPLLTLVGGLFMAFVWWNGGVVLGDRSSHEFTFHIPQLLYFLAFCAAQTPLRFFLFLLH | Catalytic Activity: a dolichyl beta-D-glucosyl phosphate + alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodoli... |
A0A3M1ULQ7 | MNRRDALPLPFLVLRRGDLGPALRLSARLFLVLLAYYLLKPTRESLLLATGSAELRSYAVGTQALLLLLSLPLYRWAAERSRGERLYRRVSFFFLCQLGLFVPWIALGDSAWLGFAFFVWLGLFGVTQLAQFWALATDSLPPRRGERALPLIAAAGSLGALAGSQAAALAYPRLQAEGSLLLAILLLLASLAIPIRGRTRRPARPGQAPSPWRTWLGGLHLVFEDRLLRAIALFILLLNLVNTTGEYLLAGMVQAAAPPSGPERAAFIARFYGHFFFWVNLLALGLQLFVVARIYRRIGVAGAVLCLPLLILAGYLLLLI... | Function: Provides the rickettsial cell with host ATP in exchange for rickettsial ADP. This is an obligate exchange system. This energy acquiring activity is an important component of rickettsial parasitism.
Subcellular Location: Cell membrane
Sequence Length: 439
Sequence Mass (Da): 48552
Location Topology: Multi-pass... |
A8RBS1 | MKKVNILFMGTPEIAVAMLSRLLEDKYRIVGVVTQPDKKIGRKQLLTMPPVKELALAHDIPVYQPGSIKEEYEQLMELDIDVLITCAYGQFIPKALLEYPKFGSFNVHTSLLPKLRGGAPIHRAIMTGESFSGVSIQRMVAKMDAGAVCAQQKVEITQEDTMGTLYDKLAQVGADLLAKTLPKIINNEACFVEQREEEATFAYNITKEEELVDFECDVQTVYNHIRALIPQPCAYAYVHQKKLKFHKARMIRDNQPHVCGQIEGLIDQGIAIGAMNGYVLIDELQMEGKAKTDAKSFYNGIGKNLIGYIINSEQ | 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... |
A0A1H9LKQ2 | MASKLLLVDGHSILNRAFYGMPDLTNSEGLHTNAVIGFLNIFFKLLDEENPDYVVVAFDTSAPTFRHDIFKEYKGTRKPMPAELHEQVPLLKEVLDTMGVRRYEEPGLEADDILGTLAKRAESQGMIVTLVSGDRDLLQIASDNILIANPKTKGGQTTVERYHTQEVIDEWGVTPEKFVELKALMGDSSDNIPGVPKVGPKTAKELMQTYGSIAGIYEHVEEITKNAIRESLKANKESCDLSYTLALIKTDADFELPWDSAKRVNYLNENAYKEYKRLGFKRLLSKFSQEVVDKAFASVGESGNTNAVDAAFNAASNAAD... | Function: In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity.
EC: 2.7.7.7
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Length: 1018
Sequence Mass (Da): 113543
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A0A673GX09 | MIYSNSNPVVFFDIAADNEPLGRVTFEVSVRENFRALCTGEHGFGYKGSIFHRVIPQFMCQGGDFTNHNGTGGKSVYGPRFPDENFRLKHTGAGILSMANAGPNTNGSQFFICTAKTEWYVNHLHESAFISCGYECVMLCVCVLCVCVVCLFVCVCVLCFVCVCVVCVCCLWCVCVLFVVCVCCLWCVCVCVLFVVCVVCGVCVCVVCGVCVGFVVCFPGWMGGTLCSAALKTGWMW | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
EC: 5.2.1.8
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Length: 237
Sequence Mass (Da): 25813
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A0A956XJ34 | MINDITLRSDMTVDLLAHNGNDMDIANAARVSVGDGRGGNPYEISGLINYLMKHRHGSPFEHGYLKFHVECPIFVAREFMRHRAGWSYNEVSGRYSVLEPVFWVPTTTRGIVNEGTSARPRLEPDAFIANQTIAQMQSFYEEAWEAYRLILNGDVVNEVARAVLPVGIYTSFIASCNPRSLMHFLSLRINHPDNQYDTYPQAEIQEVAEKMEKHFKAHWPLTWEAFNAHGRVSP | Cofactor: Binds 4 FAD per tetramer. Each FAD binding site is formed by three monomers.
Pathway: Pyrimidine metabolism; dTTP biosynthesis.
Function: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (... |
R5QFB2 | MTKTRETVKKYTMPCIAMRDTVAFPEVPITLEVSRQITKRACDSAMKADGSIFLVCQKDPTADSPESERDFYATGVVANIRQLIKGSPNGSYSVIAEPKSRAELLSLSKDKYITCEVLEKNIYLEDGGGVRAEALMRDIKGQVNALMKQLPRFSRELWLIVSSIKSASLLCDFVSANLVENIEDKQALLAEYDPMRRMELLLLILEHERAVLAEEDGINRKVKERIDRSQREYFLREQLKVIHEELGDGGEDDEDIEDYYKKLDSGRYPKEVADKLKKEIRKLRRTPVGSADGAVLRGHIETCLEIPFGIRTHDRTDISA... | Function: ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield ... |
A0A444L5H8 | MFLNMPVETPIETAGLKKRVGLILKLARPHFLVPGALLYAMGAIIAQLRGWSCPLDRAVFGYAVFFLAHLSVSFSNDYHDRNSDRIAGRTFFSGGSGVLLEHRELERAALRIAQALLLLSFVAALAFTIKYGFSAAFLIFATAGGLLGWFYSAPPLKLSYRGLGEAVTALAAGLIMPGMGYFVVSGQLDSWFVMLSVPLACYGLYFILTVEIPDFEADRAAKKMNIVTRIGVKKASIISLASAIFGTGLLAGLHFLGFSGGAFDLAKLAVLSFLPFAAATASLVALTSKGLSAVRHTAINMFGLVGFLSASVLVLFLELI... | Pathway: Quinol/quinone metabolism; menaquinone biosynthesis.
Subcellular Location: Cell membrane
Sequence Length: 322
Sequence Mass (Da): 34476
Location Topology: Multi-pass membrane protein
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A0A956ZS07 | MRSSPTGASLFEQLRGKLIVSCQAREDNPLHGAGYMAAMARAAELGGAAAIRVNAPGDTRAVMTAVNLPVLALYKVDYPDSEVRITPTLADTQALLTTGAQMIALDATDRPRPHGELLADSVSAIHTAGSLAFGDCARPEDLAGAIAAGCDAIGTTLAGYTEETLSESTEPDFATLAWFVRHSPVPVYAEGRFWTPEQVARALDMGAHCVCVGTAITNPWKITEYFIRESERARQP | Pathway: Amino-sugar metabolism; N-acetylneuraminate degradation; D-fructose 6-phosphate from N-acetylneuraminate: step 3/5.
Function: Converts N-acetylmannosamine-6-phosphate (ManNAc-6-P) to N-acetylglucosamine-6-phosphate (GlcNAc-6-P).
EC: 5.1.3.9
Catalytic Activity: an N-acyl-D-glucosamine 6-phosphate = an N-acyl-D-... |
A0A957AFA1 | MKSLTIGRIQGIDIKLHPSFLLIGVWVIYQWAIRQGSGIAGTIYGLALVLAIFVLVLLHELGHSMMAHEYGLRVRDITLVPFGGIARIEQMPSQPRVEAMISVAGPLVNLALAFLLLPVLLMVGLATGSDSIHDFARFGLGDVSLTGFLFYLLLANLTLAIFNLLPAFPMDGGRILRAGVTPIVGRQGATTVAVAIGITLGILIGILGLLSGEYLIVIVMAFVVLAAMAEGRAVRLEESMRRLRVGQFAVWDRGGVSPDDPIAMALRQGARDLPVTENGRLVGMVWRQQLIDAMSHGGLQRRISEIMDQQFVSIPSDTSV... | Cofactor: Binds 1 zinc ion per subunit.
Subcellular Location: Cell membrane
Sequence Length: 385
Sequence Mass (Da): 41843
Location Topology: Multi-pass membrane protein
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A0A2G2L751 | MSSISKLKTIFNYPLVKILIGALYPLGFSPIDIWQATLLSLGLLVYLIIDTYHFNRNLHIPEERTLVKKAIISTCFFWGVGAYGVGTSWVYVSIHEFGNAALPLAVLITALFVLVLTMVKVGFGYLIHQLVSLCGKSFLILIIPFAWVVSEFVLSTLFNGFPWLLAGYSQMDGPLVSLATWFGVYGVGWFMLAIISVSIVLGECLFALYKINQSVDPSHQSALKSIRNKSFMILLIIMSFPLSSYLMQPEEIIPQEKVSLDVALVQPNISQDKKWKREYFSEIIDTLYLQTNEHWDADLIVWPEGAIPAYKHQVYDVFAD... | Pathway: Protein modification; lipoprotein biosynthesis (N-acyl transfer).
Function: Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation.
Catalytic Activity: a glycerophospholipid + N-terminal S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipopr... |
A0A5C7JU56 | MSAHVSFLSMEPVTRVVTIGTFDGVHLGHQRLIANTRDRAIELGARSTIVTFEPAPASVLRPDRFAGRICTAGRKLRLLESLGANEIAVIEFDRALASRSPEDFLTELKEQTGLIELWVGEGFALGRDRVGDVARISEIGESLGFRTIAMPRVIDGGEVISSSSSRRAIEAGNVRFAAESLGRPKTVAL | Pathway: Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step 1/1.
EC: 2.7.7.2
Catalytic Activity: ATP + FMN + H(+) = diphosphate + FAD
Sequence Length: 189
Sequence Mass (Da): 20428
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A0A1Y0I9F0 | MLTETRLAIAEIAEILEAKIIGDASSEISSLATLQAAKTGQLAFLSNPVYKKHLAKSQASAIIVAPDVVTELFVERGGSWQFVSGEPLQSTFLVLDNPYLGFAKLTHLFDTAYQFEPRIETSAVIHPSVHVPDDCYIGHNAVIGEGCVLGRSVYIGANVSIGVNCHIGDRTRLWASVVLYSDITLGQDCIIHSGVVIGSDGFGNAKDGEKWFKIAQLGGVTVGDNVEIGANTTIDRGALGDTIIGDGVRIDNQVQIAHNVVIGDDAALAGCVGVAGSTTIGKRCVIGGATGVGGHLDIADDVYLTGMTMVTKSIKAPGLY... | Pathway: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
Function: Catalyzes the N-acylation of UDP-3-O-acylglucosamine using 3-hydroxyacyl-ACP as the acyl donor. Is involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.... |
A0A369T4E8 | MPPEFLNNSPGRPDASGQTFYCDGAQPLPNMRVILMGLGVVGKAFLRMLIEKAPELRSKYGLNPTLVAVSDSRSSVYSEIGLDPKLILDQKNERGSLAGLEGETDLRGADLVREVEAEVLIEMTPSNFRDGEPGLSHIKAALNTGKHVITANKGPLALEMPALVEMFRESGLMLLFSGTVGGGTPFVRFVRRCLVGERILAIRGVLNGTTNYILTMMESGIPFSEALAEAQRLGYAEADPSNDIDGWDSAAKLVILSNLAMESDATLRDVEVAGIRGVEVGRELLSQGKTVRLIASADGSGLRVRPEVIDRKDPLAVSGA... | Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 3/3.
EC: 1.1.1.3
Catalytic Activity: L-homoserine + NADP(+) = H(+) + L-aspartate 4-semialdehyde + NADPH
Sequence Length: 368
Sequence Mass (Da): 39244
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A0A7X5S2R0 | MKSINPMQLLRRRAEETLSETMRRLGDVQQTWQSAVAQQQQLQHYEQEYQQALRQGMTDKGMCVADLINQQAFILSLGQVVKQQEKHVNHCAEAVIQARQLWVKDKQRLNAFETLIVRREAAEMMRQNRQDQKLMDEFAQRAARKREQR | Function: Flagellar protein that affects chemotactic events.
Subcellular Location: Cell membrane
Sequence Length: 149
Sequence Mass (Da): 17666
Location Topology: Peripheral membrane protein
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S3XM37 | MYQVLSLKYRPKNFDELIGQEAVSRSLSNALDSKRLANAYLFSGLRGSGKTSSARILAKSMLCKNGPTSHPCEVCDSCKMANENAHIDIIEMDAASRRKIDDIRELIERTKTYPSISRYKVFIIDEVHMLTKEAFNAFLKTLEEPLEHIKFILATTDPLKLPATILSRTQHFRFKPISQNLVINHLANILNKENTPFEDEALKIIARSGEGSLRDSITLLDQSISFTNGSVNAKEVASMLGLVDPVKIDEILNIVLKRDRKGVISILDELSSYEADSIIDQLTLNLKDKFLSKNPKFNVFMYERFFRVLSEAKTMLNMGS... | Function: DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity.
EC: 2.7.7.7
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Length: 574
Seq... |
R7IQS4 | MKIILASKSPRRKELLSQVGYTYECVVSEKEENTDAVQPSDVVKELSQQKAEDVCAKIEKEGQMEEDCLVIGADTIVAKDSEIFGKPKDTEDARRMLSALQGREHSVWTGVTLIYLRDGKKKKKVFAEETKVHMYSMSEQEIEEYIRTKEPEDKAGAYAIQGYAAKFIKKIDGDYNNVVGLPVARIYQELKKLTKEDSTVLQVQQTEDLMPDVKWYDKAVFYHIYPLGLCGCAHENTGVPEEHFDKLNEWAVHAGNIGCTAIYIGPLFESVGHGYETTDYKMVDRRLGTNDDFKKFVENCHNNGIKVVVDGVFNHTGRGF... | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: H2O + UTP = diphosphate + H(+) + UMP
EC: 3.6.1.9
Subcellular Location: Cytoplasm
Seque... |
A0A1V5L9N2 | MAKDNNYIVFARKYRPMDFDDLVGQEALVKTLSNAMNNNRLAHAYLLTGIRGVGKTTSARIMAKGLNCIGADGKGGITIKPCGQCSHCKSIMEGRNIDVIEIDAASNTSVDNVREIIEGTKYTPVSARFKIYIIDEVHMLSKSAFNAILKTLEEPPSHVKFIFATTEVKKIPITVLSRCQRFDLKRLTIENMVKHLSNLASKEGVEIDEDALNILATLSEGSARDGVSLLDQAVSHSNGVKITAETIKKMIGIADRTETTSLFNHMMSGDIAKALKNIEAQYQSGVEPYLILNDLLEITHLVTRAKVGCELDKAMLSENL... | Function: DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity.
EC: 2.7.7.7
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Length: 585
Seq... |
A0A1A9GJV6 | MESPLALYRRYRPETFSEVIGQDHVTEPLRAALANNRVNHAYLFSGPRGCGKTTSARILARALNCEQAPVADPCGQCDSCRDLARGGPGSIDVIEIDAASHGGVDDARDLREKAFFAPVRSRYKVYIIDEAHMVTTQGFNALLKLVEEPPPHLRFIFATTEPEKVLPTIRSRTHHYPFRLIPPRLLSSYLTELCELEGVPIAQAALPLVVRAGAGSARDTLSVLDQLLGGAGSEGVTHALATGLLGYTPDSLLDEVVDAFAAGDGAAVFGVVDKVIETGQDPRRFTEDLLRRLRDLVIVAAVPDAPATGLIDVSEDAGER... | Function: DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity.
EC: 2.7.7.7
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Length: 755
Seq... |
A0A4W2E5D3 | MVLLRMVVLILAGSPVYQDEQERFVCNTLQPGCANVCYDIFAPVSHLRFWLIQSVSVLLPSAIFGVYVLHKGAELAARRSRGLEDASEDHDAPGLTPGARRCLTVPDFSSGYVVHLCLRTLTEAAFGALHYLLFGFLVPKRFSCTHPPCTSVVDCYVSRPTEKSILMLFVWAMCALSFLLTVADLVCSVCWKTQGRPGTPFLSQTETGLGPHFPGVQLWVSLLS | Function: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell.
Subcellular Location: Cell junction
Sequence Length: 224
Sequence Mass (Da): 24638
Location Topology: Multi-pass membrane prot... |
A0A957AK86 | AARRQAPPATTGSRPAPMQAPRHGLAQVIDTLEARLQAAGARVATASTVSAVLRHGQGYAIAQATGETITADAVICAAPAPMAAGVLDPLDTCLAEHLRAIPHASVANLTLAYPRQVLPRALVGSGYLTPRTERRPVKACTWVSAKWAGRAPDDASLIRVSFGGAGMDQIVDLGDDDLLRLAQEELRTVLGITAQPSFTRLFRWPQAMPQYEPGHLGRLTQIDACLDGYPNLALAGNAYRGVGLADCLQSGEVAADRLLNYFSSRTASTRYEA | Pathway: Porphyrin-containing compound metabolism; protoheme biosynthesis.
Function: Involved in coproporphyrin-dependent heme b biosynthesis. Catalyzes the oxidation of coproporphyrinogen III to coproporphyrin III.
Catalytic Activity: coproporphyrinogen III + 3 O2 = coproporphyrin III + 3 H2O2
EC: 1.3.3.15
Subcellular... |
A0A091MW15 | QTVLEEMNRLGMIVDLAHVSVETMKVVLNHSKAPVIFSHSSAYALCSSRRHVPDDVLR | Catalytic Activity: an L-aminoacyl-L-amino acid + H2O = 2 an L-alpha-amino acid
EC: 3.4.13.19
Subcellular Location: Membrane
Sequence Length: 58
Sequence Mass (Da): 6489
Location Topology: Lipid-anchor
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A0A1Y0I3W8 | MSDSDQFENTSNDSPSMDTVADEADPNQDDDFNAGSDALEVIHAEFAIPLDLAEKRLDQAVAAFMPEHSRGRIQGWIKSGALTLNGAAAKAKDKVIVNDKVAIRAEIEGLERWSPEAIPLDIVFEDEHILVVNKPVGLVVHPAAGHPRGTLVNALLHHCPEVDKLPRAGIVHRLDKDTSGLMVVAKSLIAHTSLVNQLQDRSMGREYEAIACGMMTGGGTVHEPISRHPHNRLKMAVHPTGKDAVTHYRVLEKFAAFTHIHCKLETGRTHQIRVHLAHIHHPLVGDPIYGGRLKLPSGANEEITTLLRSFTRQALHARRL... | Function: Responsible for synthesis of pseudouridine from uracil.
EC: 5.4.99.-
Catalytic Activity: a uridine in RNA = a pseudouridine in RNA
Sequence Length: 356
Sequence Mass (Da): 39353
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A0A673KTZ4 | MSTVHEVIVARHCGMRVFALSLITNKAVMNYDSEEKANHEEVLQTGKQRAEQLERSRSGG | Pathway: Purine metabolism; purine nucleoside salvage.
EC: 2.4.2.1
Catalytic Activity: 2'-deoxyguanosine + phosphate = 2-deoxy-alpha-D-ribose 1-phosphate + guanine
Sequence Length: 60
Sequence Mass (Da): 6744
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A0A1G0ZBC3 | MRIGGKKIEKVRVYGDPFLGKKAESVKNIDDKLLKFSEVLTNTMREFDGVGLAATQVGAGIRVISLGVPIPRDENEVQIISSPGEALLLNRMPLVLVNPEIVSYGPDICVKEEGCLSVPDIYAPVARPSKVVVSAQILGGESFTVECGGLLARAFQHEIDHLDGILFVDRLSKEAYERIEPALGKLKRRYARLKFLRKLIRKDNE | Cofactor: Binds 1 Fe(2+) ion.
Function: Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.
EC: 3.5.1.88
Catalytic ... |
A0A0J9XBP2 | MSSPNSAPNNNNNNSNGNSRRFTSSSPLFFSSSPAPYEDPGTNRSVATPRQPSQLREVSSPLAYSSDGITPRSHFSERTDATPRPARQRRGDIFSSEVNTPRREVPNSDFGEPSSHHTYSMQDGDTPMANPDEPVRVIWGTNVSIAEAQSTFREFILGFKEKYRIRADQGSIEPGEGENLVYVNMLNQMRVLGLSNLNLDVRNLDAYPPAKKLYYQLINYPQEIIPIMDQTVKDCMVSLATENGNISHETIEMEIESRIYKVRPYGLVEQKGMRELNPGDIDKLVSIKGLVLRATSIIPDMKEAFFKCSVCNHTVSVEIE... | Function: Acts as component of the MCM2-7 complex (MCM complex) which is the replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such tha... |
A0A1Y0I342 | MLNSDALHQLKQLKKDIKASRNLATGRVKGSNSKFGFVTLNDTGKDIYLSADEMQKVFPGDEVEIEILTNEKNKDYGVIERLIQSELSTFIGRVRKKNKNSFAEPDVPGLQRWLFIHPGKLQNAQEGDFVRCKILQHPIRNGKPQVAVLDVVGAEKQVGIEKLYTISKHEVRDNWSQAILDECAQITDEVILREGANREDLTQLPFLTIDSAATQDMDDALYATATDTGWSLSVAIADPTAFIAPESAIEKEAALRGSSVYYPGSVISMLPEHIANQLSSLVPDQNRLALVCKLEITAQGDVDSFNITQAVVQSHGKLSY... | 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: 663
Sequence Mass (Da): 73889
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A0A1V5L9J8 | MSSLSKSVAVFGGYTMLSRITGFVRDLLIAKYIGAGMVADAFFMALRFPNLFRSMFAEGTFNVSFVPIFSSKLAVNDKDGALDFANRAFSLLFYMLTTFIIILELLMPFMIFMFAPGFSKDKEKLDLTIELTRITFPFLLFISIVSLQSGILNSFSKFAASAFSPTIINLTMISVLLVSSKFSNDYAHYLSFGLIFAGIIEVIWLHHFLKKEGVLLKLKKFGKEIFSDDVLTLLKRTGPGIVGAGIYQINLFVDTFFVSFLEKGSVSWLYYATRLFQLPIGVLGASMAVALLPMLSKQLASKNFGEANKTMNKSIIFMAI... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Involved in peptidoglycan biosynthesis. Transports lipid-linked peptidoglycan precursors from the inner to the outer leaflet of the cytoplasmic membrane.
Subcellular Location: Cell inner membrane
Sequence Length: 518
Sequence Mass (Da): 57363
Location... |
D1BD62 | MGKDGFNLVVVANRLPVDMSVADDGTVSWQRSPGGLVTALEPVMQSADGAWVGWAGSPGLEADPFDADDMRLVPVTLSAGEVERYYEGFSNDTLWPLYHDVIAPPAFHRQWWDTYRKVNQRFAEAAAEQAADGAMVWVQDYQLQLVPGMLRRLRPDLKIGFFDHIPFPPLEIFQQLPWRRQVVEGLLGADLIGFQRAGDAANFSRAVRRLTDLTTRGQMIQVPADGDLPARAVRAAPFPISIDSKRFDELARTPEVQARAKEIRKDLGDPKIVMLGVDRLDYTKGIRHRIKAYGELLQDGSLDPAECTLVQVASPSRENV... | Pathway: Glycan biosynthesis; trehalose biosynthesis.
Function: Probably involved in the osmoprotection via the biosynthesis of trehalose. Catalyzes the transfer of glucose from UDP-alpha-D-glucose (UDP-Glc) to D-glucose 6-phosphate (Glc-6-P) to form trehalose-6-phosphate. Acts with retention of the anomeric configurat... |
M1N384 | MNKIKKYYILIPIITAILSLIVIVSTALDTNLINKSYSIFTEDMNSNNVSTVVVNSSPKMTIILNNGDKYYTDNPHTDTLVEKLLLKGIEVKNENTPPLTKSIPSGIFVLSIISIMAMLLYKVKGKNSVTSIEMQDFSKDQKNALDFNAVAGNEEAKESLMDIVDFLKNPEKYQKYGARMPKGVILYGDPGTGKTLLAKAVAGEAGVPFYALSGSDFVQVYVGVGAARVRNLFKKAKTQGKAVIFIDEIDAIGKARSNGKNGSSNDEKDQTLNALLTEMSGFGQDDGIVVIAATNRLDMLDKALLRPGRFDRHIEVSLPD... | Cofactor: Binds 1 zinc ion per subunit.
Function: Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.
EC: 3.4.24.-
Subcellular Location: Cell membrane
Sequence Length: 577
Sequence Mass (Da): 63384
Locat... |
A0A359M4C9 | MTSALLTDLYELTMAAGYFSAGKTGERATFELFVRRLPQNRSFLIAAGLPQAVEYLLNLRFTKDEIDYLRGLPQFHNAPREFFTYLADIRFTGDLFALPEGTPFFAGEPVLTVRAPIVEAQLVETYLLSMAGFQTLIASKAARIAEVAGPRSAVEFGTRRAHSPEAGVLAARAAYIGGCSGTSNALAGMRFGIPVFGTAAHSWVLSFETEREAFERLQQLLGPHSVYLLDTYDTVEGARLAAALGEPIFGVRLDSGNLVALSRAVREILDRAGLPHARIMATGDLNEYKILELCAAGAPIDAFGVGTDLATSSDSPSLGA... | PTM: Transiently phosphorylated on a His residue during the reaction cycle. Phosphorylation strongly increases the affinity for substrates and increases the rate of nicotinate D-ribonucleotide production. Dephosphorylation regenerates the low-affinity form of the enzyme, leading to product release.
Pathway: Cofactor bi... |
A0A139SWL8 | MTIKTHWIINNADLAQQCEYWQQLEFIALDTEFVRVNTFYAKVGLIQVSDGQSAWLIDPLPIDAWQPFADLLKNPNILKVLHAAGEDLEVFSRICGALPAPLFDSQLAAAFLNWGASLGYSALVEKTLGVTLPKGETRSNWCQRPLSPAQTQYAAEDVLHLARLYQVLHPLLSAQKMAWLLEDGAQMTSALCPPPAPELAWQSVKLAWKLSAQQLAVLRAICAWREQTARERDRPKGWIVHESALYPLACFAPKSLAALSRIEGIDAQTVRRDGQTLLALIKQAAALPPEQWPLPLPAPLPPSAKKLLQILREVAGQQAQ... | Function: Exonuclease involved in the 3' processing of various precursor tRNAs. Initiates hydrolysis at the 3'-terminus of an RNA molecule and releases 5'-mononucleotides.
Catalytic Activity: Exonucleolytic cleavage that removes extra residues from the 3'-terminus of tRNA to produce 5'-mononucleotides.
EC: 3.1.13.5
Sub... |
A0A444TWN5 | MQAACDSVLDDIEDMVSAQDPKPHDRQFARKNIVPRASKRRQQQTEDPQADSVIPGTQKIWMRTWGCSHNNSDGEYMAGQLAAYGYKMTENPSEADLWLLNSCTVKNPAEDHFRNSINTAEVTERFVLTWRLQLSFRVQQIDRVVEVVDETIKGHSVRLLGQKKDNGKRLGGARLDLLKIRKNPLIEIISINTGCLNACTYCKTKHARGDLASYPAEELVERARQSFLEGVCEIWLTSEDTGAYGRDIGTDLPTLLWKLVEVIPEGAMLRLGMTNPPYILEHLEEMAKILNHPRVYAFLHVPVQSASDSVLMDMKREYCV... | Cofactor: Binds 1 or 2 [4Fe-4S] cluster. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the methylthiolation of N6-threonylcarbamoyladenosine (t(6)A), leading to the formation of 2-methylthio-N6-threonylcarbamoyladenosine (ms(2)t(6)A) at position 37 in tRNAs... |
A0A177ECP0 | MDIGVIGVGVMGENLVMNMLDKGHSVAIYNRTHEKTTKLIGQVSSEKQDMAQGCASLEELVKALRQPRKILLMVKAGRVVDAFIEKLRPLLSKDDLIIDGGNSHFNDTTRRCQESAGHHYFIGCGISGGEEGARHGPSLMPGGDVLAWEGALPLFSSIAAVSTSKTPCCEWIGGEGSGHLVKTVHNGIEYAEMQILADMYQVLRGTRDPASIEQMLSGWRDKGTSGFLLEALQTVFKKAHNGQPIIDQIVDEAQQKGTGAWTAEEGLRAGVPIPTISEAVTSRVISSMKQVRTSLGSLPSGAEASSEGFTEGELMKAFML... | Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 3/3.
Function: Catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate and CO(2), with concomitant reduction of NADP to NADPH.
EC: 1.1.1.44
Catalytic Acti... |
B8FMZ8 | MTEENMAEEKQMPLTEHLEELRSRLIVCVVTVLVGFFVSYGFKEQLFALVARPLNIAMGEGGKLIFTSLTEPFIAYLKISFFGGIIIALPVILYEIWAFVAPGLYSKEKKVIFPLVFLGCLFFAGGASFGYFIVFPMGFKVLLAFGGDVADALPSMKEYLGLATKLLIAFGVVFELPLFIVTFSRMGMVTPQMLRKGRKYALVIFVICGAILTPPDPFSQLMMAAPLVILYEISIIGAVIFGKKPEPETDVDDIDDID | 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 inner membrane
Sequence Length: 258
Sequence Mass (Da): 28511
Location Topology: Multi-pass membrane p... |
A0A2M7BN98 | MDYTDKTVKLEVMIHKFIFQSGFSLGSFILEFVQSIVLALSVFVLMYLFVAQPNEVKGNSMLPNFINGEYLLTDKLTYQFSEPKRGDVIVFKAPPSEPCAESECEYIKRIIGIPGDRIKVEGGQVYLNGELLDQFFLPADFVSDSGEFCKEGEEVTVPTGMYLPFGDNRSHSRDGREFGVIKKESIVGRAFFVYWPTTSIGLVPTVRF | 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: 208
Sequence Mass (Da): 23458
Location Topology: Single-pass type II membrane protein
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A0A5B8UWU0 | MAQKRNRSIFNTFGQLSSSLIWMGENKSRPAYIRYLITLFLVLAATGLKLYFKQTIGISSPYLLYFGIVCLSAILSGIGPAIFAAFFSAFLADYLFIPPLDTIELLPKDLVKTIIFLCECSLITLLSSGVTVAYRQIRQNQLLFKAMIEKGTEGIVLTDADNKRIYVSQSIERIIGYTADEFIDMPPWALAHPDELPEMIRDMAELKKHPGKNISFVHRIKHKNGDWVWLENSITNLLEDEAVKAIVANFYNVSERILMEQKKDDFISIASHELKTPVTSLKASLQLLDNVKNDPSSPIIAKLVTQANRSTEKITSLIEQ... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 488
Sequence Mass (Da): 54653
Location Topology: Multi-pass membrane protein
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A0A265E8T1 | MKISYYNGEFKSDDEISVDYNDRAFYFGDGVYEVVRVYDNAFFTLGEHMDRLVRSASEIEINGLDREKLIDIITELKEQNSIENGSIYIQVSRGINPRNHAYPAGAEPVILAYMNEMARPSHQMDNGVEVITANDYRWLKCHVKSLNLLANVMEKERAVRAGAHETLLHRDGVVTEGSSTNVFIVSDGVLRTHPANHLILNGITRQEVLKIAEAQGLEYAEKAFTLDELKSADEVFITSTTQEVTPVSHVDGEKVGDGAKGSITQKIQEEFDQRIHELNLVK | Function: Acts on the D-isomers of alanine, leucine, aspartate, glutamate, aminobutyrate, norvaline and asparagine. The enzyme transfers an amino group from a substrate D-amino acid to the pyridoxal phosphate cofactor to form pyridoxamine and an alpha-keto acid in the first half-reaction. The second half-reaction is th... |
A0A328R628 | MTIVRDILDLIKVRILFSALLTTVLGYFLAVDSASFDVLFLFWLCLGLGFIFSSAAAINHVMEVGTDALMDRTQNRPLVKKRISLLSFWIGVLVLLLFGTAILYIKFNLMVLVLSLFILIFYDVVYTPLKKITVLNTWIGAFPGAMPVLCGWFSVRDDLDFLIIVIFSIYYWWQLPHFFAIAWMNKESYLNAGLKMMSVDDKGGHKTAFHLCLSTFIFLVFLTLPFFFNYVGYIYFIPLMGLSILFCYYIFLFCIHKTVLASKKILFCSILYPPLILLFIVLDSLV | Pathway: Porphyrin-containing compound metabolism; heme O biosynthesis; heme O from protoheme: step 1/1.
Function: Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.
Catalytic Activity: (2E,6E)-farnesyl diphosphate + ... |
A0A0Y0DMS4 | GMVGTALSLLIRAELGQPGALLGDDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGVGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTIINMKPPALSQYQTPLFVWSVLITAVLLLLSLPVLAAGINMLLTDWNLNTTF | 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... |
A0A956V0G8 | MPSTRSTGSTRHISAAIDALRQVWRGGTDAGRELVNAIDHIEAARAGAPYQIVAELNALAAAVRTLPKESEARKRSIQTVAEELKKLGADMVASTQPPVEKGKLTSALVPQKRASTSAGPRGVTPVSPTDVLSALPGIGSKKLKPFNEGLHLFTVQDLLQFLPRKHIDYSRSANLSDPLQMRGDIVVQGTLNNIQVIRTGTPRVQARLSNETGTIRITWFSTYIQNQLHEGNRIIVAGALSPGHGGLQLTNPEWEFVGAGSVFQSDALVPIYPLTKGISQKMMRQHTRNALDATRERLIDWLGDARPYIDDDVWEFLPDI... | 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 + ... |
A0A133UVC7 | MQVELMEKEGTEMKVKIVGEGHSFTNVLRKKLHEDERIEIASYNIDHPLLSDPVLRVKTSEKKSPKRALIRAAKSLSEEYEEIKMKLEKALEQ | Function: DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
EC: 2.7.7.6
Subcellular Location: Cytoplasm
Sequence Length: 93
Sequence Mass (Da): ... |
A0A673LHH2 | MSVHLSLSLSLSLYLCPSICQSVCLSLYLSVCSSICLSLYPSLTLCLSLYLSVCLSVSSSVCLSLYPSLTLCLSVSARIRRYSEVMALPDSFIQKQQLDASMADTFLEHLCLLDIDQEPITARNTSIICTIGPASCSVTKLQEMVKAGMNIARLNFSHGSHEYHGETIRNIREAVETLTSDPLYYRPVAIALDTKGPEIRTGLVKGSADAEVMLERGALVRVVTAEADHDKTDGSVIWMDYPSLPRVLKKGSRVFIDDGLLALKVLEIGETWVETRVENGGILGSRKGVNLPGAELVNLPAVSDRDRSDLLFGVEQDVDI... | Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5.
EC: 2.7.1.40
Catalytic Activity: ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate
Sequence Length: 473
Sequence Mass (Da): 51641
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A0A2H0Q7P7 | MLSKESLVKAGFMDQIVVIFKQLGVDQTIAHQFIVFVVMFVLLKTLFFDKLQFVLELREAKTTKLDGAADAKFGEADKMASEYEEKMKSVNAQAMNQVSEVKAKALSKQKTELKKVEDELEDEVEAKRQQFMQEVASKKEAILKNADQLSDGLVEKLIQ | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
A0A4W2I276 | RLPDQKTSPSGKSATLRLCSWNVDGLQTWIKKKCLDWVKKKPQISCASKRPNVQRTNYQLNFKSCLGYPISTGEEEHDQEGRVIVAEDDAFVLVTAYVPNAGGGLVHLKYRQHWDKAFCKFLKGLASCKPLVLCGDLNVAHEEIALRNPKGNKKNAGFTPQEQQGFGKLLQAVPLSDSSQHLYPNTAYAYTFWTYMMNAQS | Cofactor: Probably binds two magnesium or manganese ions per subunit.
Function: Initiates repair of AP sites in DNA by catalyzing hydrolytic incision of the phosphodiester backbone immediately adjacent to the damage, generating a single-strand break with 5'-deoxyribose phosphate and 3'-hydroxyl ends.
EC: 3.1.-.-
Subcel... |
A0A177ECF7 | MTETLKKSFGQHLLKNPGIITALIEKARIRPTDTVLEIGPGTGNLTLKLLERAKKVVAVEKDKKIATDLLKRVGQKRRKLQLVIGDAIEVDYPEFDLCISNTPYQISSPLTFKLLTYPFKAAILMFQREFALRLCATPADPYYCRLSVSVQIRANVQHIMKVSKKSFRPPPKVESSIVRIEPKRHQPNINLNEFDGLVRLCFSRKNKTIGSIFRQTAIKNLIFRNTQAESSEGVPAGEGVFGVVGSPDFTEDPNDDGSSDGEGNDLAEQEPLPPVNEQALRRALEESGFEKERAAKMTVEDFLFLLIKFKENGVSFSA | Function: Specifically dimethylates two adjacent adenosines in the loop of a conserved hairpin near the 3'-end of 18S rRNA in the 40S particle.
EC: 2.1.1.-
Catalytic Activity: adenosine(1779)/adenosine(1780) in 18S rRNA + 4 S-adenosyl-L-methionine = 4 H(+) + N(6)-dimethyladenosine(1779)/N(6)-dimethyladenosine(1780) in ... |
A0A143WXY4 | MCDNSVSVRSERDARSRRPQQGTVVRGAARCRKAIHEMMEDSYVETKVEALEDNRTKVTVTVDAADIDARIKKTYKDFANKYNFPGFRKGKAPRPIIDNALGKEAVLATVTDDVVNGSYPLAIDDCGLYPVSKPEFDESGLVEGGKPYAFSFTVAVKPELELSSYDAVSIELPAEGATDAEVDEQIEALREHYHTFEDASAATKVKTDSYIDLAMKATDDKGEEIPSLTTESRPYGLGANLFPAEFDEQLVGLKKGQSATFTLDMPADPPIMLSALSGKTDKIAFEVEVKAVKKKILPEVTDEWAKDTLGFESAEDLRSR... | 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
... |
A0A4Y3PHG3 | MNKAIDISVLDGVIKRTIETVETSKTQIFDIAEDARQQGNSLKFDLHELRQEISKVIQKVDALELAYRKSRNRLVQVSRNFHMYTEDDIRIAYEEASRIQVELSIYRERENNLKRRRNDLERQLRTLEETIVRAEKLVSQMGVVLGYLTGDLSKIGEALESAKQHQLMGLKIIQAQEEERKRVAREIHDGPAQSMANVVLRSEIVERMLKNERILEAQMELHELKEMVRLSLADVRRIIFDLRPMALDDLGLVPTLQKYIQTCEERIRASIDLVVFGVEPPLRSSVKAAIFRLVQECLNNVEKHAGASSVQVKLEFLQES... | Function: Member of the two-component regulatory system DegS/DegU, which plays an important role in the transition growth phase.
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Cytoplasm
Sequence Length: 380
Sequence Mass (Da): 43440
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A0A1G1BB86 | MKNAAPKYIFKNNDNTWANIFDGIKTARQIILFLDYDGTLVPIMEKPSLAVMSYQMEEILRDLNRKGNISIFLVTGRAHSDIKKIFRVKDVTIISNHGFQITGKNINWSHPDIKHFLPSLRKTKLLLMKKLNFFPSTFLEDKRITMTVHFRNAEKKHIPLLKKTVRNIVVNYKEDLHTTSGKKVVEVRPNIRWNKGEAVLKIMKRLRIRNEATKILYVGDDKTDEDAFKALKHKAVTIVVGRKQNSHANYYVRNTDEVQKVLQSIHSIT | Pathway: Glycan biosynthesis; trehalose biosynthesis.
Function: Removes the phosphate from trehalose 6-phosphate to produce free trehalose.
EC: 3.1.3.12
Catalytic Activity: alpha,alpha-trehalose 6-phosphate + H2O = alpha,alpha-trehalose + phosphate
Sequence Length: 269
Sequence Mass (Da): 31252
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A0A2W4JE66 | MVFVGAGAPAGRDEEWAERIRRHRERRAAHWETVETIHIAAALRAADAPVLIDCLATWLARICDEAGAWDAAPGWKERLEHEVEELVQAWRAARVPVVAVSNEVGSGIVPSTPSGRLFRDELGVLNSRMASESDAVLLMVAGRPIRLEAP | 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... |
A0A1F6C3E4 | MLTVLVIIHLLICFILVLSILLQSGKGGSLAGAFGGAGAAGAVLGTRGAATMLSKITTYTAILFLVSCMGLTFISRGGSGTQVQTSAQKEAAKRGGFTPLSAPVPAQQTPAQPAEKK | Function: Involved in protein export. Participates in an early event of protein translocation.
Subcellular Location: Cell membrane
Sequence Length: 117
Sequence Mass (Da): 11775
Location Topology: Multi-pass membrane protein
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A0A4Y3PND1 | MLRTDGQMPLWIRIYLLAFGLSAVIILFFCYQITAVSSEHSMQREYSRSLDRHVMFASAMKMYAASIEKMAFNPGLRQELLTRAAQNYGRYYTDGKSYIAMTSLDGEKLYSSFSPADEKIMELDPPKDGRRSFVIRQSGEHSVLFVSGWMSIASQLYRLDYENDVTDMVAGQQTLATQIALWFSAGMILLAIGLYVLIRHALRPLAQLGTQAKALARGNYDPRIAVARRDEIGQLALEFNHMADAVQSHMELLRREVKERETLIASLAHELKTPLTSIMGYASLLENYELEQAEKQKALRLIHSESKRLDDMSKKLLNLF... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 492
Sequence Mass (Da): 55041
Location Topology: Multi-pass membrane protein
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A0A1F3K7D8 | MNNNRVLLGMSGGIDSSVAAMLLKEQGFDVMGVTLRLWSMADGLHSISEPAYLTEARYLAAKIGIPHQVVDVRPDFYEKVITYFKEEYLRGKTPNPCAKCNVVLKWEVLNREAIKNRCTYIATGHYVNKWESNQRVYITRGVDTDKEQSFFLWGLTHGILKKAMFPLGQMTKQKVRNIAVDRGFKVLDDKKESAGVCFIPDGNYHSLLIGLMQKEGLKPQKGWFVDSNGDFIGYHKGFPFYTVGQRRGLGLSPTEPWYVTKIDALQNQIVLGKQADLFQKQMVVENYHLLYPDDFEQEVITRIRYRKQSAPSRVTILDEK... | Function: Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34.
Catalytic Activity: AH2 + ATP + S-sulfanyl-L-cysteinyl-[protein] + uridine(34) in tRNA = 2-thiouridine(34) in tRNA + A + AMP + diphosphate + H(+) + L-cysteinyl-[protein]
EC: 2.8.1.13
Subcellular Lo... |
A0A2G2L7I1 | MAAFEYVALDTKGKQIKGVMEGDTPRQIRQLLKEKNLIPIDVESINKRDKSSGTSTKAGVSKLKIGAADLALITRQIATLIRAAIPVEETIKAVAEQCEKTKQKTMLLGIRARVVEGHSLADALSEYPRVFSELYRSMVAAGEKSGHLELVLERLAEYTESRQAISQKITGALVYPVILSVVSIGIVGFLLGSVVPEITKSFTKSGQELPWLTEALLSLSDYVQSWGVLTFIIIFAMVSGFKYLLRTPSLRLKWDKWKINAWIIGKVIRGLNAARFARTLAILNASSVPLLEGLKIAGDVMTNAELKVAVAEAATRVSEG... | Function: Component of the type II secretion system inner membrane complex required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm.
Subcellular Location: Cell inner membrane
Sequence Length: 407
Sequence Mass (Da): 44524
Location Topology: Multi-pass membrane... |
A0A1E7QJP5 | MIVFTGIQPSGVIHLGNYIGLMKQLIGIQDQYKSFFCIVDLHTITANKLAPNELRGNVFKMVAAHLACGINPEKAVIFNQSIVSGHTELSWLLGCYTPIGWLNRMTQFKDKAGRDKQKASLGLYSYPVLMAADILLYNAQYVPVGDDQKQHLEITRDIASAFNKHYRQDYFVLPEALINSSRVMSLRDGTKKMSKSDPSDYSRINFDDSDKSIINKIKKAKTDSILGFDIDTLSARPEVCNMVNIYSALSDIKVDMLCNTISKYSMERFKKELVDIIISTISPVRKKMTELLSDKDYLLKVLKHGGDKAAGITHQNIKKI... | Function: Catalyzes the attachment of tryptophan to tRNA(Trp).
Catalytic Activity: ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + H(+) + L-tryptophanyl-tRNA(Trp)
EC: 6.1.1.2
Subcellular Location: Cytoplasm
Sequence Length: 329
Sequence Mass (Da): 37081
|
A0A4U0F588 | MNEAVRPVVAVVGSINMDFVVESPLFPLPGQTVLGKSISYFPGGKGANQAVAAARLGADVRMIGAVGGDEFGGKLEAVLRKEGIDTRGVRVTDGATGIASILVSGGENTIVVVPGANGALRPEDVHGNAGLIEAADIVLVQLEIPFETVEAALRLAKTAGKKTVLNPAPAGVFPDEWLQWTDIVTPNETELAALVGAERLDDPAVLESAMRKLHDRGAERIIVTLGANGAVLSARNGEIVRVPGRKVEVVDTTGAGDTFHGALAAAWAGGASLAEALQTAVDASALSVTRQGAQTGMPAAAELERWRRE | Cofactor: Requires a divalent cation, most likely magnesium in vivo, as an electrophilic catalyst to aid phosphoryl group transfer. It is the chelate of the metal and the nucleotide that is the actual substrate.
Pathway: Carbohydrate metabolism; D-ribose degradation; D-ribose 5-phosphate from beta-D-ribopyranose: step ... |
A0A956ZRY0 | MTLQSDSQREPVSLAVAILAAGKSTRFNSSGPKHVHPVAGVPIVKRIISAARAINPDHICVVINPEMTDLATQLDMEGQFDTAIMEVPTGTAHAVLAAIEALPEVDYIISVLGDNPLLTDEIMLKLVQDALEKDATVTLLTCKLDDAAKYGRIARDDEGRVTAIIEFVNDDPSQREGITEINSGIMVLKRNWALEAIRTLPMDPVKKEFFLTDLVTVAVAEHQDGEPWPVDAVIGPENVSVGINTRVEQANADAIVRKEMRLKHMTAGVSMVGPETIFIDETVTIGQDTTLLPGTILLGNTSIGRGCTIGPYAVLIDATI... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
Function: Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl c... |
A0A7X2PLT3 | MFFKKKAPKPPPERHWIADWAFNIVLLVWFTSTVAQPFVVPTASMETTIMTGDHLIVDKIPYSPPGAITKYFLPYQEVRRGDVVVFRYPLNINMPYVKRVIGIPGDKIQFVEKKLILNGKPAEEPYAQFTGPNLDPYAANFPTVSPSYVYPRGAEMLRDNVKDGVLNVPEGFYLCMGDNRENSDDSRYWGLVPRENIMGKPLIIWWSFEASTEHLAGYSVDQVINLIKNFIPKTRWKRTFQFIKAYPLGY | 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: 250
Sequence Mass (Da): 28774
Location Topology: Single-pass type II membrane protein
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A0A7X2PPH7 | MSVILTIIHVIVCLFLVIVVLLQSGKAADLAGAFGGMGSQTVFGPRGAATALSRATTASAVIFMVTSLGLSVISTRQSGKAGGGAKSVLESVKDPNAAPTPTAPGSVPPPMAPVPGGAQQPTIELLDPTTGKVVSTQPLVIPPPPAAGQKQEKKK | Function: Involved in protein export. Participates in an early event of protein translocation.
Subcellular Location: Cell membrane
Sequence Length: 155
Sequence Mass (Da): 15458
Location Topology: Multi-pass membrane protein
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A0A956WCQ6 | MVDRDESLPPDGSEITGEEGKERAGELDRLISLSDGVFAFAMTLLVVTVEVPQMSDEAARTRLHHDIVDLWPQVLSYIVGFLVIAFLWASHRRNFARIQDFDARLVRLNIALLLLVAFLPFPTGTLGEYGNLAFPVILYAVILAMISVLFIVMIDHMDRNRHLMTRGGRNYDFARAKTRHLVTCGILLLSIPISLMFPGFGQVVWILLIFNHQITEWLLPHLPKRFQERGQS | Catalytic Activity: K(+)(in) = K(+)(out)
Subcellular Location: Membrane
Sequence Length: 232
Sequence Mass (Da): 26365
Location Topology: Multi-pass membrane protein
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A0A961M769 | MDAKVSDTKDGNAANTTASAGSADPLLDCLEFIARRFGISFSPAGALSGLPLKTGRLDEENFARAAARFGLSARTLAREVYDIPSMVLPAVMLLKNGDACVLTHLDKKHHRAKIFYPHEKTGERAIDLSKLAEAAIGAAIYITPDSSPTAEAFYSASDPADRRGHWFWMPVRRAWSSWLQVVIAAFMVNLLGLAVPFFIMNVYDRVIPNLAIPTLFALTGGVVIALTFDLLLRQVRALVLDRAGRRIDMGLSARLFDQLMRLRMTEHQAGAGVLASQVREFDTVREVFTSQTVIAVTDFFFIGIFLFAIWTLVGPIAWVP... | Function: Involved in beta-(1-->2)glucan export. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation.
Subcellular Location: Membrane
Sequence Length: 745
Sequence Mass (Da): 79958
Location Topology: Multi-pass membrane protein
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A0A673ILK2 | MHDPLLIHLILPVRVGAAICNFYVSGFWCHLLPATFMHTSETKGAFRLPQLCKFCDIESTACNATGVCESSCNITAICENPDEVCVSAWRNKGNAIIETVCHNPALPFHGQYLTDYNNTVCLMKQVKGMEEDFYICSCNEEECNAQLFFTYGKTLKKLTLLLIKDKNQFNSVGKQDYFSDSTDILSVNSLHFDQFLGNLQEFLTQHVIGWDELCRLGWSLARGVAHLHGDRTPCGRAKAPIVHRDLKSVNVLVKADLSCCLCDFGLSLRLDNSMSPEELANSGQVGTARYMAPEVLESRMDLENIESFKQADVYSMALVL... | EC: 2.7.11.30
Subcellular Location: Membrane raft
Sequence Length: 421
Sequence Mass (Da): 47454
Location Topology: Single-pass type I membrane protein
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A0A1D2RG62 | MKILKSDFGHGAVKIAVENLDDLWYLSHVVCPGDIVKSLTTRRIKGKEDTRAGRDVRKTITLAVRVERCEFRSDSDVFRILGTIAEETEDVPLGEHHTFNVGKESVLTIIKDSWSKTEIKQLKDAEKFSLRPKLLIAVIDDGNANIGLVRESKTDYFEVSRNIGGKYDATGRQLRKDEFYHEAAKFIDELMKRENVQSVILAGAGFEKSNFHRFVSDKYPLLAKNSMVENIGSHGRNGIMEVMKRDESKIAGQLGAIRDERLIEKLLEEIGKDTGLGAYGPGEVEKAVNTGAVETLLVTDNYFLEKRARMEPVMQAVTDT... | Function: May function in recognizing stalled ribosomes, interact with stem-loop structures in stalled mRNA molecules, and effect endonucleolytic cleavage of the mRNA. May play a role in the release non-functional ribosomes and degradation of damaged mRNAs. Has endoribonuclease activity.
EC: 3.1.-.-
Subcellular Locatio... |
A0A4U9J835 | MSERFDSSWDSIIKPLFQTSKLQELSEFVRNERSLHQVFPSADLVFNAFRLTPLNNLKVVILGQDPYHNDGQAHGLSFSVPAGIAIPPSLRNIYTELVTDIPGFKYPNHGNLSKWAEQGVLLLNATLTVRAHEAGSHQKKGWEFFTDEIIKSIFRPSRKCCFSYFGEVMQSRNRL | Function: Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine.
EC: 3.2.2.27
Catalytic Activity: Hydrolyzes single-stranded DNA or mismatched double-stranded DNA and polynucleotides, releasing free uracil.
Sequence Leng... |
A0A1G2F2R2 | MISREQIEHIAKLARMELTEKEKEKFSTELSSILDYIDKLNQVETKAIEPISQITGLENIVREDAPRKEDTRSNIRDKFIKAAPAKKDNYFKVPKILE | 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 ... |
A0A6C2UKG5 | MVFHLISMFFHALEPGRRLSLNRKGHGEPLHPPPPKSFGPWKLISKTEGLYSFCMTHYIHNINPIILQFSDKLAIRWYGISYLLGFLACILLMRNWSKKGEFEVPEAEVSNFVVMLALFGVFLGGRLGYVLLYGLDSFLEDPRYIYQVWEGGMASHGGFIGVILVILWYAKKHHHSFWNLTDNMACATSLGLAFGRLANFVNGELWGRATNVKWGVVFPQEAGLHYGQYDPAFIQKLVEAGELTVRHPSQLYQAFGEGFLVFGLMLLLRHTPWGKRPGALSAAYLALYALARISMEFFREPDNGAFFIGWITKGQFYSAL... | Pathway: Protein modification; lipoprotein biosynthesis (diacylglyceryl transfer).
Function: Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins.
Catalytic Activity: 1,... |
A0A133URA6 | MRKILSEGSGEKSFLLGNEAIARGFLEAGGTLATTYPGTPASEIGDTLHNIAKDAGIYFEYSTNEKVAMEVAGAGAMTGHRTMVSMKSVGLNVAAEPLVTLAYNGVEGGMLIVVADDPFCHSTQTEQDTRYYARLANLPILEPSSPDEAREMASEGIEISEELGIPIILRTTTRVSHVRGSVDLKQWDKRKFEKKRFEKNPEKFAMVPALQRKKHEVLTGEIFEKAKKISEKTKLNKIERVGEEDVLHAVTSGPPFNYLMDVMRDENVPGEVFKLGMSFPLPEDKLLDFLKSKSKVVVAEEVEPILEKEIREIANFYGLE... | Cofactor: Binds 2 [4Fe-4S] clusters. In this family the first cluster has a non-standard and varying [4Fe-4S] binding motif CX(2)CX(2)CX(4-5)CP.
Function: Catalyzes the ferredoxin-dependent oxidative decarboxylation of arylpyruvates.
EC: 1.2.7.8
Catalytic Activity: CoA + indole-3-pyruvate + 2 oxidized [2Fe-2S]-[ferredo... |
A0A444V559 | MAALLRALKVGQVLRALRAAQRSQCDEVKRTFQTAAVLRRVTDDPKQEQVPPSSSSFHQHYQSTPPDSESSRPNTSYADQGGEQAEDYETEEQLQIRILTAALEFVPKHGWSVEAIAEGAQTLGLSPAAAGIFSNGTGDLILHFIAQCNSNLSEKLAEQHKLVQLGQTEPKKTDEFLRDAVEARLRMLIPYIEIWPQAMSILLLPHNIPESLKHLSILVDDIWYYAGDRSSDLNWYTRRAALTGIYNTTELVMLQDSSPDFEETWKFLENRVKDVMNMANTAKQVQSTGEAVAQGIMGAAVTDCTCDEFCPECSVELTLD... | Pathway: Cofactor biosynthesis; ubiquinone biosynthesis.
Function: Lipid-binding protein involved in the biosynthesis of coenzyme Q, also named ubiquinone, an essential lipid-soluble electron transporter for aerobic cellular respiration.
Subcellular Location: Mitochondrion
Sequence Length: 491
Sequence Mass (Da): 55274... |
A0A673J7L0 | MEKVQHITRAAIRRASTMEVPQQAKQNMQELFVNFCLILICLLLIYIIVLLM | Function: Reversibly inhibits the activity of ATP2A2 in cardiac sarcoplasmic reticulum by decreasing the apparent affinity of the ATPase for Ca(2+). Modulates the contractility of the heart muscle in response to physiological stimuli via its effects on ATP2A2. Modulates calcium re-uptake during muscle relaxation and pl... |
A0A5D0ELA2 | MVIKKERIMQRFNAALETYEKNAIAQQHIANDLLKLLLEKGGNRFHRVLEIGCGTGNFTRLLMQNIEAEHWDCNDLCDVSAQLIQNLPLRNYNFYQGCGESLVLSAQYDLIVSASTIQWFSDPLAFLYRCSTHLIPNSMILLSTFAPTNLPEIRALSQIGLDYPNLAQWRETLMGNFHIIHLSQKEIRLEFDSALSVLRHLKDTGVTATNNRIWNREKVARFCEQYHQHYINEQGKVSLTYVPIFMLARKKENA | Pathway: Cofactor biosynthesis; biotin biosynthesis.
Function: Converts the free carboxyl group of a malonyl-thioester to its methyl ester by transfer of a methyl group from S-adenosyl-L-methionine (SAM). It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway.
EC: 2.1.1.197
Catalytic Activity: malony... |
A0A7C3HQI9 | PRLECYGTLDELNAYVGMARLSAEAAAAGMPPLARLGGLLTRIQHELFNLGSILATAPGKAHPKQARVADADVERLEAEIDAMNAELPALRSFVLPGGSRLNAELHVCRTVCRRAERLLVSLARIDEIDEVNLRYVNRLSDAFFVMSRWANVVAGAEEVLWSPNQAASAQRG | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 2/7.
EC: 2.5.1.17
Catalytic Activity: 2 ATP + 2 cob(II)alamin + reduced [electron-transfer flavoprotein] = 2 adenosylcob(III)alamin + 3 H(+) + oxidized [electron-transfer flavoprotein] + 2 triphosphat... |
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