ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
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A0A2D5ZVB3 | MQEKQVLAKEIADFLAKQYQLELTADEILSKIEKPKDEKMGDLAFPCFILAKALKKGPPVIAKELSEGLQVDPQVFSACIATGPYLNFTLNKADLASKLIPSILSGEFIEARPSKSEKVMIEHSQPNTHKGFHVGHTRNTALGDALVRMYRWAGYEVISATYPGDVGTHIAKCLWYFTQFTDQSAPETHKGEFLGECYTHAERELTFHRLSWFPHAKWVAAKVVSKTLLKKETNLHKVEIQTAKETKTLVCGGTNYNEGDLVVYAPPGSYVKGRLVQSTEKHGVASEGMILSEKEATDRGSKDDILKLNSDDLARVFQWD... | Catalytic Activity: ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg)
EC: 6.1.1.19
Subcellular Location: Cytoplasm
Sequence Length: 730
Sequence Mass (Da): 82596
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A0A2E0WKA1 | MKLRSDNAWHHQPLPWLVLASLALHAGLLAWQAPLQHEVPALSSRSGALAIQLTAPPSPAQQPPAPTATGDAAAATPAGRAATDGDQRQASRPDASAPAQPSVPGPVAAAGTARAEPERQASVERPAPARGGRPAGAEAQQPPRTAAATATAHPEQTRAEAQGSAVLEEIRDALQQHFFYPRLARLRNWEGDVLLGFQVRSDGRIDDVEVLKSSGRAVLDRAALSALRSVRQVAYNAAQPVDLQLPVAYRLH | Function: Interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates. It could act to transduce energy from the cytoplasmic membrane to specific energy-requiring processes in the outer membrane, resulting in the rele... |
A0A534IK13 | MAGTPKARGDSSSVALLDAPAPPHSVEAEQAVLGGLLLDPAAWENVADVVTQQDFYRPDHQLIFDAIGALAGAGKPCDVVTVSQHLESTGKLESAGGLAYLGSVARDTPTAANVRAYAEIVRERSLLRQLIRAGTDIAADVYNNKGESARDLVDRAEQRVFDIAEGSFRKREGAVPVRQLLPGVIDQIDEWHQNPDQLRGLPTGFTDFDKLTGGLRPGDLVIVAGRPSMGKTTLAVNMAEYAAVHPGTRASVAIFSMEMPSEQVITRMLASIGGVPLNNLRSGKISDDDWVRITSATSQLSEAKIFVDETPALNPTELRA... | Function: Participates in initiation and elongation during chromosome replication; it exhibits DNA-dependent ATPase activity and contains distinct active sites for ATP binding, DNA binding, and interaction with DnaC protein, primase, and other prepriming proteins.
EC: 3.6.4.12
Catalytic Activity: ATP + H2O = ADP + H(+)... |
A0A8T7A832 | MTYPKITFIGGGNMATAMLSGLLNNSYPRENFVVIEPDAKRREDLTQRFAITCLAHADSSSIAADFVILAVKPQIIRGVCEDLAKHSSNAQSVFISIAAGTTTQHLMEWLKLLNNTDPVVVRAMPNTPALIGESATGLYSAKQLSNDKQAAIEAIFASIGQAIWLDQEELIDSVTALSGSGPAYFFGFMEALCNAGIQQGLTPDQAQKLVLQTALGAALMAKQYVTGENVNALQELRERVTSKGGTTAAGMASLQTHKFSEIVAQAVQAAKQRATELAKARD | Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-proline from L-glutamate 5-semialdehyde: step 1/1.
Function: Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline.
Catalytic Activity: L-proline + NAD(+) = 1-pyrroline-5-carboxylate + 2 H(+) + NADH
EC: 1.5.1.2
Subcellular Location: Cytoplasm... |
A0A524AVE6 | MLNQSFNGGVVIPNPHPVEAVEIISAPLPDKVVLPLQQRIGDEAIPCVKVGDKVLTGQVIAKTEDHFCVPIHASISGKVVSIDDQTIPHKSGLKSKCITIESDGKDQWAEHEGCGSDFLHCDQATMIEYIQSSGIVGLGGAGFPAHAKLEGIQNCHTLIINGTECEPGIMCDDALMQYHPREVIRGVEILLHICGAQRAIIAVEDDKQEALNSLLMYCHNDRISIEQIRTKYTSGAEKLLIKALLDIEIPSGGFAIDTGVVCQNVATTKAIFDAVVDNKPLISRIVTVTGSAVESPNNYEVRLGSSFEHIVSMSNPNANQ... | Cofactor: Binds 2 [4Fe-4S] clusters per subunit.
Function: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane.
EC: 7.-.-.-
Subcellular Location: Cell inner membrane
Sequence Length: 501
Sequence Mass (Da): 55246
Location Topology: Peripheral membrane protein
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A0A9D8J5Q6 | MITLGIETSCDELGMALIDWRSNRAWHVLRSQIDLHQVYGGVVPEIAARDHVEHMPKLFEKLIRGSGIKRDEISHVAYTAGPGLIGALLTGSVFAATLARSLNIPAIAVNHMEGHLMMGLMGQSVKFPIFVLLVSGGHSQLMLMSDFGKYQLLGRSIDDAAGEAFDKVAKKMGLGYPGGREIQALAMSDHFNEILHLPLPLRGQKGFNFSFSGLKTATVQLLESLEQTPENKARVARAFQGRVVDSFVNVVQRAVENYQVYDLVISGGVSANTELRRRLVDEVGVNLLAPRLDLCTDNGLMIAYCGGLRAMAGDSQMHHY... | Cofactor: Binds 1 Fe(2+) ion per subunit.
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. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, togeth... |
A0A2D8AJD2 | GLLLSTQLGDLSLFRAVGFAILIGSGLFFYQTMVQQTRAPRRLFYQRLFAINAFGFIFLLLSFRFGGHVSVQSLSVQFALAVHFTMFALWIGALYPLLTISRTEQVAELKVSLERFSKHAVVIVSLLLLSGLALMLSLIHSVADLFTTAYGIALILKILLVIGLVAIAAVNKYIIVPRLLLQTDTAQFQRSVRLEIVVAILLLLLTAYLSTVLGPTMH | Function: Involved in copper resistance.
Subcellular Location: Cell inner membrane
Sequence Length: 218
Sequence Mass (Da): 24068
Location Topology: Multi-pass membrane protein
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A0A976JEQ1 | MAPSGYRRLFIALPVPEETNKQLAPYCVSFPHAHWIPTTNRHLTLTFLGHHTEEQTHRAIEVIDRIDAAAFEITLHSMQRFPDDRGRHIVALPTDCMPLKQLHHRVASALTTRGFALKQRDYRPHITLGKIHRGNWSTVAISPAIVMVVKSVALFETVFFDGGVTYHSLATQPLL | Function: Hydrolyzes RNA 2',3'-cyclic phosphodiester to an RNA 2'-phosphomonoester.
EC: 3.1.4.58
Catalytic Activity: a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + H2O = a 3'-end 2'-phospho-ribonucleotide-RNA + H(+)
Sequence Length: 175
Sequence Mass (Da): 19805
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A0A523LDB9 | MIGAFRLLLFACVALLGACATLPRISPDDAEALQRWHEEQLAHFEDWRLSGKISVRDDQDNFSGRLHWRTSSGSYEMLIVAPMGRGSWRLEGSAAGAVLTDEKQQVWRGEDAETLLFQRLGWHVPVDDLVYWIRAMRVPDRVAEVEFDAWGRMGRLREAGWTVTYQAWQESAGLQMPRKMVAASDPYRLKLVINEWALGAGSEAEPEDAPEPGPESGFDSGFEAGPENGPGNGFGPGPEAEKGG | Function: Plays a critical role in the incorporation of lipoproteins in the outer membrane after they are released by the LolA protein.
Subcellular Location: Cell outer membrane
Sequence Length: 244
Sequence Mass (Da): 26986
Location Topology: Lipid-anchor
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A0A2E7LJC0 | MGPCHYEGHATLIDFYTWAAMSGHGLYVWSVYGISIVALVVLGAWPLRAEKKLLVRATERADEEGGS | Function: Required for the export of heme to the periplasm for the biogenesis of c-type cytochromes.
Subcellular Location: Cell inner membrane
Sequence Length: 67
Sequence Mass (Da): 7351
Location Topology: Single-pass membrane protein
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A0A2D9JLJ2 | MTVPPRASIATTEGQHGGNLSWAMTAFGGIADQWLDLSTGINPNGYPVPEMPATVWQRLPDSAAFTQAEDAARKIFGVPSAKAVVVTAGTQAAINVLPRMRPHSRVAVVGKTYSEHALAWAQAGHEVREAESLTDACSAEVVVVVNPNNPDGRVYPRDELCDAARALSARDGTLIVDEAFADSCPDESLAQDGQYANIVILRSVGKFYGLAGIRVGFVICPSALALPLRQLLGPWSVTGPSLAACTVALNDSAWRDDTRRRLFDAGRRLEQTLVAANLTLVGRTDLFALTATPHAQALWQFLADQHILVRRFEQQPLWLR... | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
Function: Decarboxylates L-threonine-O-3-phosphate to yield (R)-1-amino-2-propanol O-2-phosphate, the precursor for the linkage between the nucleotide loop and the corrin ring in cobalamin.
EC: 4.1.1.81
Catalytic Activity: H(+) + O-phospho-L-threonine = (R... |
A0A2E5VBW3 | MPKIYMFDVDGTLTPARSMMDEGFRNFFLRWSEGKKFYLVSGSDLAKIKQQLPQDVMERCAGVYSSMGNSYHERDQVVYSIVYSPSYELLEDLQALVENSEYPIKTGHHVELRDGMVNFSIVGRNADMQQRAAYGEYDKRHGDREGIVETLSHCHPDLDFAIGGKISIDIYPKGYDKSQAVRHLRGEVGNDPEIIFFGDRTEAPGNDYGIVRALDEAPEPSQWHAVEKWADTMSILKESYSD | Pathway: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 2/2.
EC: 5.4.2.8
Subcellular Location: Cytoplasm
Sequence Length: 242
Sequence Mass (Da): 27550
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A0A8T7HVX6 | MAENDSGERSEKATPRKLQKAKQRGQVPRSKELTTALVLIASPLALMMSSSEVAKGFDAIKQLTFSLSRSQVLDTQFMFYALAESIASVFSALIIFFLAVFLISLFAPMLLGGMSVSAEALAPKGNRMSPMSGFKRMFGTTALMELAKAVGKFSLIAVFAYMVIESNIIQYFMLGRSTPEQEVVAAIDYILAALLMIAAPLILIALMDVPFQMWNHAKQLKMTKQELKDEFKETEGKPEVKGKIRQTQRELAHRRMMEAVPDADVVVTNPEHYSVALKYEQFGNRAPVVVAKGVDQIAFNIRKVAKAHDVVIMEAPPLAR... | Function: Required for formation of the rod structure in the basal body of the flagellar apparatus. Together with FliI and FliH, may constitute the export apparatus of flagellin.
Subcellular Location: Cell membrane
Sequence Length: 375
Sequence Mass (Da): 41784
Location Topology: Multi-pass membrane protein
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A0A9E5ADQ7 | MNSLLEFLPIIAFFAVYKWVGGIEAVYPATATAIGAATLVAAVAWRRQGSLPRRQLVMLAAFLVMGGLTLAFHDARFIKAKPTIVEWLSAVLFLGSQFIGSKTLIQRAFGGSVTLEPHIWRRLNLAWVVFFTLLGGLNLYVARIYSTDIWVNFKLFGVLGLTLVFVVLQGFYLMRYDKSVDSTVNDA | Function: Plays a role in cell envelope biogenesis, maintenance of cell envelope integrity and membrane homeostasis.
Subcellular Location: Cell inner membrane
Sequence Length: 187
Sequence Mass (Da): 20768
Location Topology: Multi-pass membrane protein
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A0A2E0EXY3 | MLRPVSLLSLTSPFITMDLSKAFYTHGSICKPRALASCIIKNYMDSDISQEHIYTVSELNDEVSGLLSSNFGIVWIEGEISNYMKSAAGHAYFSLKDSDSSVRCAMFRIQNQSIGFAMEDGQHILAKAKVGLYQARGEYQLVIEYAEQAGEGLLRQKFELLKNKLQSEGLFDPVHKQSLPYIPNKVGIISSPKGAAIQDIFNTIKRRFSLVELLVYPTMVQGKEASYQICQAIASANQDSQCSVIILARGGGSLEDLWCFNDEEVARSIFNSKIPIVTGIGHETDVTIADMIADVRAPTPTAAAEIVLPDKSEIQKTLSS... | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
EC: 3.1.11.6
Subcellular... |
A0A358XVE4 | MAEATDITAPEDGASNKTTVVRVENKGPLSSVRRIASDPSIRRSAPAIFGVVLAVIGLAAFYFLNKPPVTTLYAGMPEAEKARVVEALTNSGMQVQLDPTTGEILVPTSDYHTARMRLAAQGLPASVPEGYDSISEIPMGSSRTVENVRLKQSQEIELARSISEIEGLVAARVHLAIPEKSVFARASVPPSASVFVQMEDGRSLSRQQISAIVHLVSSSVPSLPKGEVTVVDQYGNLLSQPGRNAASAATDSQLEHRIRLEDIYRQRIISIVTPMVGGGNVMAEVNLGIDFTRSEVTEELVDPERNALRSEQRSSDTSSE... | Function: The M ring may be actively involved in energy transduction.
Subcellular Location: Bacterial flagellum basal body
Sequence Length: 574
Sequence Mass (Da): 61665
Location Topology: Multi-pass membrane protein
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A0A0H5QJQ3 | MLWVDLILAAALRYLLMLTTSHSSESVQIVGASSSYRRVVEAMYLHSQNRSIYDGDIFHQPPLLFAFLSFLNDVGSIHLIHFFFICIDLFIAAMLRNVTMRSRDMGFPFPNSEICIHKQANLHDIVFRMFLFNPLTLLSCASLSTVSLSQVFVIFALYSTYNGHILSLAFSFATSVYLELYNAILLVPILIVLHFKQLDLSSAAKRDAPLNAVPFSLTAKMLMFISLSIGFLASLIALSSHYFGSSRWWSFSYRYLYFVHDLTPNIGIFWYFVTEMFHRFRSFFLICFNSQVFVYVIPLTIRFWHNPLFLFFIFMHLIMM... | Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Function: Component of the GPI transamidase complex. May be involved in the recognition of either the GPI attachment signal or the lipid portion of GPI.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 421
Sequence ... |
A0A2E8NLS8 | MDAPKIDDDRTLVGIDEVGIGCLAGPVVAAAVILNPANPIYGITDSKKISEQRRKXLADQXMXNAVDWAIGQASVSEIDQHNILRASHLAMQRAYGXLKSDATLVLVDGNKSPYFPVESKAVIKGDETVLAIGAASIIAKVFXDGLMEXLGKKYPDYDFEKNXGYPTKSHMQTLRAIGPCAQHRNSFAPVKNWNKKSH | 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.
Subce... |
A0A368C1M3 | MLNKIILKKHSSGFFNETSLLFLFLGASLTLIFPPYNYFFLAPIIMAIIFYACISLKPKQTAIYLFFFGIGFNLFGVYWIYISIHIFGNAPIWVAIILMIALVILMSLYIAIAGLLISWLVGKRKITLIFLGPSVWVLLEWAKGWIFTGFPWLTIGYSQIDTYLAGWAPIFGVYGVSWLLLFSSCSFLFFCVKARFYLAFSTLLAPYLVGYFVSVDFWTENFDKPIAVKIVQGGVSQDLKWKKEQLSKTMNLYRTATFEAEKDTLIVWPEVAIPASLNIIEPFINDISTHIGENNKKLAFGVLEQQKNSNNSYNSLMFLD... | 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... |
A0A523LUI3 | MRVWITRSQPGADRLAAVLQSHGVEVLVAPVLEIEPIAVTPPSISFDAVVFLSEHAAVLGAQNIAIGDSVVLAVGERTGAALAELGIEATVPKLRSSVGLLELPELTEVLDKRILLVAGMAGRDLLSCELTSRGAEIDRLIVYRRVAIDRLSADQRGQLGEVEMIIVASGDGFENAARLWFLANGNADVPVLVPSERVALKGKTVGLANVHDCAGADSDAVLRGLAIFG | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 3/4.
Function: Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III.
EC: 4.2.1.75
Catalytic Activity: hydroxymethylbilane = H2O... |
A0A349X6K6 | MSNFWSIFVIVLVVGNILGMVWLLFSTSKGSDVNEAETTGHEWDGIKELNNPLPRWWLWLFVLTIVYAVGYLYFYPGLGSYEGSLGWSQKGEFEQAIVENNARKAEFYAEFKEMDIPVLATSAKAMEAAERLFGNNCSTCHGSGGGGAKGFPNLTDDDWLYNNDPASLVATLTNGRAGVMPNLNLSPSDVTVMAYYVKHLAGDEVSEHVQLEGKKRFATCAACHGQDGTGNKALGAPNLTDNVWLHGSRIADIEKILREGKRGNMPSFKSILSQDEIRLLSAYVLTLSSSEEASAE | Cofactor: Binds 2 heme C groups per subunit.
Pathway: Energy metabolism; oxidative phosphorylation.
Function: C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex.
Subcellular Location: Cell inner membrane
Sequence Length: 296
Sequence Mass (Da): 32419
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A0A352KIV2 | MSINRRWILPEGIEEILPDQAWQLEHLRRQLLDLFRTWGYELIIPPMVEYLDSLITGLGEDLEQQTFKTVDGMNGRTLGIRPDITPQAARIDAHRIGQEGPTRLCYAGSVLLTHPSALGGSRSPMQVGVELFGHGGVESDIEVLSLLIESLTLTGIDEVHIDLGHVALFHGLAAAAQLSAETEAQIFDCLQRKSLPDLQQLLLNSSLDERYQTWFLELLALSGEATVLDDAKRFYVNAPASIQQALGQLEQIATKIHRRFPQVSLCIDLAELRGYTYHTGCVFAVYVMGEGQAIAQGGRYDHIGEVFGRARPATGFSADM... | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
Function: Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine.
Subcellular Location: Cytoplasm
Sequen... |
A0A9C9GA41 | MTDDRPLRIGLVAGELSGDQLGAALIRAIQATHPHAQFEGIAGAEMRAAGCQALARSERLAVMGLVEVLGILPALLRLRRKTARHFLHNPPDVFVAIDAPDF | Function: Condensation of UDP-2,3-diacylglucosamine and 2,3-diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
EC: 2.4.1.182
Catalytic Activity: a lipid X + a UDP-2-N,3-O-bis[(3R)-3-hydrox... |
A0A2E0GMQ8 | MKFYFDKSESIFFGXGSNLNDPKKQILKAINYIKKEPNIEFVKSSKCYLSPPMGPQDQSHYFNLVIECKSKLNPLDLLNIVKSIESIMGRVENKRWHERIIDIDIIMYGQLEFRSSILTIPHPLAFEREFVMKPLYDINKDIYMPGYGLVKELIKKCKYKVKKSVNLVE | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 4/4.
Function: Catalyzes the transfer of pyrophosphate from adenosine triphosphate (ATP) to 6-hydroxymethyl-7,8-dihydropterin, an enzymatic step ... |
A0A7C3CRR7 | MHFNALIWKNLDTSFIKPRYWPVWLAVGLLRFAIIFPHSQRMYIGKLLGRAVYRFSQKRRKIASINIATCFPGLSKEEQQAIVKKHFDSLGMSVIESAMSWWMDNDRLKSLASIEGIENLEQAVAQQRGVILLSAHFNSLEISSPLMIANTGYAVQAVYQANSNPLLEKIITEGRRNNVEALISHKNIKQMIRALKQKKIVWYAPDQGYAGKFSEIVPFFNTPAASNTAVSRLAKISGAVVVPFFIRQKPDNSGYVLTYLPVLEDFPTEDAVADTQRYHHIVEQEIMKAPEQYLWIHRRFKNRPEEYPDLYKDIVLRK | Pathway: Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis.
Function: Catalyzes the transfer of an acyl chain from an acyl-[acyl-carrier-protein] (ACP) to a Kdo(2)-lipid IV(A) to form a Kdo(2)-(acyl)-lipid IV(A).
Catalytic Activity: a fatty acyl-[ACP] + an alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IVA ... |
A0A9C7PNW5 | MHEEDYGILWKHTDFGADHSEIRRSRRLVVSSFFTIGNYDYGLFWYFYLDGTIEFETKLTGTLYLRAIHEGEETQYGALVLPVSTE | PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue.
Cofactor: Contains 1 topaquinone per subunit.
EC: 1.4.3.-
Sequence Length: 86
Sequence Mass (Da): 10104
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A0A964LUD2 | MQLPERDEWNLRNPYRNQTTEKRTGNARVKQIIGTFVLLPFEHLLNQIIGRDRLVQQKIRSFSGKILQISSNAPSATLLIRFQADRLSLSALDAAAIHQQATASVTGSASDLFALLLNAAAKPVANPRISITGDALFVQDLLHALRSLDIDWKDYLAPLFGDLITQEAGQIGQQARRWGTQAQANLKRSVDEYVKAEIRLVPARAELELFNEQLDHLKLALDRLDARAQSIQARLDKSLKNQHLSS | Pathway: Cofactor biosynthesis; ubiquinone biosynthesis.
Function: Required for ubiquinone (coenzyme Q) biosynthesis. Binds hydrophobic ubiquinone biosynthetic intermediates via its SCP2 domain and is essential for the stability of the Ubi complex. May constitute a docking platform where Ubi enzymes assemble and access... |
A0A2D7CXR3 | MFRIFLDIVEKLSVGVANLALTLMMLIVTGSVIGRTALNYPIPDDLLLVGLLMVVVIAFPLAHIQRVNGHIAVTIISDLLPFRWRQLQIIIGNILFGLFLGVMGFVIFSKVPRELAQDLYYDGQLEIRTWPMKTMFAIGIGLFVLQICISVYRDFRAMMLGFDQ | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 164
Sequence Mass (Da): 18503
Location Topology: Multi-pass membrane protein
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A0A6L7VKA9 | MSKAKLQSRFAAIDVGSSKIAVCVGESYGGGRLEVAGAARCNSTGVQRGIVVDIERTIAEIAQTTAAAMAKVDAPLDAAVSNLNGDHLQCLNVTGSAVTHKGEVGDKHVKQALHTAQAVNVDAGQVMLHVLPQQYVVDNQGGIVQPLNQAGKRLDAFVHLVMASSNAEQNLSKCITRCKLPNLQLIASPLAAANAVLDDASRELGVCVIDIGHDTTGVVLFVAGELKHTSVLNWGGHQVNQDIAKSLFTPPQAAAQLKERHGSVAGHEMDDSEVVVPGVNGQPDSRISKGALAQIIRAVYERIFTEIEAELARYGLLDDL... | Function: Cell division protein that is involved in the assembly of the Z ring. May serve as a membrane anchor for the Z ring.
Subcellular Location: Cell membrane
Sequence Length: 433
Sequence Mass (Da): 45634
Location Topology: Peripheral membrane protein
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A0A923PZU2 | SWISAVKQKLTRWKEDGYKVFVGIKNQTQMDRLAHFIDRLDFKPLKVDAQEYLWDTWTQDQTSSQNIIHIIPRYLPESLRLEEEHIIFLREVDFFGKKQRAAETSGAEDFQKKAKRLSFGDLKPGDLVVHVKHGVGQYEGLKLMPIGGIDSEFIQVGYKDKDKLYLPVYRVGQLQKYSGASQTTVLDKLGGVGWEKTKSKVKHQLRDIAHDLLALYAKRLELYRPPFVFNDGEYAQFESGFPYEETNDQLRAIRDITKDLTGDKPMDRLICGDVGFGKTEVAMRAAFFAIQNQKQVVVLAPTTVLTFQHLETFKKRFEGW... | Function: Couples transcription and DNA repair by recognizing RNA polymerase (RNAP) stalled at DNA lesions. Mediates ATP-dependent release of RNAP and its truncated transcript from the DNA, and recruitment of nucleotide excision repair machinery to the damaged site.
EC: 3.6.4.-
Subcellular Location: Cytoplasm
Sequence ... |
A0A2E7GC79 | MSLSRTYAKVLFLTTVEKEGNSNSISTYLDHLKEFSGWISENKALKIGLLGPTGSSLEKMKVVEHIGAKANFPQLLTQFLMLLAKKGRLALTKDICVALKEVQLEHEGGVWGQLESADPLSVGEISELRESFGKQIGKKIEFDVTTNPSLLAGLKVTLAGVTYDGSLRAQLERLEKSFLENTTESY | 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... |
A0A2E6YC98 | MQHSEKKLGKVISDLERDQIASIQKTLTSLNPSEIARLLESLTLGKRKIIWQLVDQDDEGDVLKELVEDVRQNLIEEMDTTELIAVTQDMELDDLADLLVDLPEAVTEQVITALDQQDQIRLESVMSYEEDTAGGLTNPNIISVRRGITLEVLIRYLKRLNKLPEHTHYIYIVNKYNTYLGAVKLVDLFLEDKDKPIEAIMDESFKAIPASEDAKQVALDFQDLDLISTPVIDQNNKLLGQITVDDVVDVIQDQANSEIFNMAGLDDEDDIFAPVILSTKRRAVWLGVNLITAFVVAGAIGLFQEILQQIVILAVLMPIV... | Function: Acts as a magnesium transporter.
Subcellular Location: Cell membrane
Sequence Length: 450
Sequence Mass (Da): 49520
Location Topology: Multi-pass membrane protein
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A0A9C8ZXB2 | MKTSQVRIIGGDWRGRKLEFPSTVQQLRPTPARIRETLFNWLSPVIDGARCLDLYAGSGALGVEALSRGAADVTFVESDIVSARLLRQNLAHLGSNSKVYTMDARRFVRQVGGKWDIVFLDPPYRHGMLQQILRFLHDKDSLAKEALVYIEAERELGEVNLPAGWQYIKTRQAGQIGYFLAVYNQEEN | Function: Specifically methylates the guanine in position 966 of 16S rRNA in the assembled 30S particle.
EC: 2.1.1.171
Catalytic Activity: guanosine(966) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(2)-methylguanosine(966) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Length: 188
Sequence Mass (Da): 21265
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A0A948GHW9 | MSDEGINKSAILLMTLGAAEAAEVMKYLEPKEVQKISAAMVTLRNLSRDQIVNVFDEFQQLASEKTTIGMDSGDYIRDMLTQALGDDKAAGLLDRILHNSDTSGIESLKWMDPASVAELIANEHPQIIATIMVHLEPDQSADILALLSERVRNDVMLRIATLDSVQPTALQELNDVLTKLLAGNAVGKKSIRGGIKTAAEILNYMGNQEAVLESVRTHDAELAQKMMDEMFVFEDLLEMEDRGIQLVLREVQSESLIVALKGASEELREKIFKNMSQRAAEMLREDLEAKGPVKLSDVEAEQKEILKIVRRLADEGQVMI... | Function: FliG is one of three proteins (FliG, FliN, FliM) that forms the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation.... |
A0A2D5PRJ5 | MFSTPDLKDKYQKKVFQGFESMKSFGNRDIFFGQIKTVTCHDDNSKVKEILGTNGKGKVLVINSNLISHAAMIGDEIAQKAIDNEWNGIFVAGYVRDVELLKEMDLGILALGSTTTKTNKNNKGFLGEDVIFGGVILSEDSWLYADKNGWLVSKESLEFN | Function: Catalyzes the aldol cleavage of 4-hydroxy-4-methyl-2-oxoglutarate (HMG) into 2 molecules of pyruvate. Also contains a secondary oxaloacetate (OAA) decarboxylase activity due to the common pyruvate enolate transition state formed following C-C bond cleavage in the retro-aldol and decarboxylation reactions.
EC:... |
A0A2E6IXV3 | MDNFNFNKNANLYIISAPSGAGKTSLVQSLCSYFDFIVPSISYTTRKKRDSEVHGEDYFFISEDEFVSKIKQNYFLEYQNVYGNYYGTSKTETSRILDEGNDVILEIDYKGMMQIKRSLPKALSIYILPPSIQSLRDRLRARGQDDQDVVEKRMESSLNELRYSKFADYVIVNDKFDDAQKELFNLVLTLKINSVFNNQWIEKIRDNI | Function: Essential for recycling GMP and indirectly, cGMP.
Catalytic Activity: ATP + GMP = ADP + GDP
EC: 2.7.4.8
Subcellular Location: Cytoplasm
Sequence Length: 208
Sequence Mass (Da): 24278
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A0A3M2C2M6 | MLFLLLAGSVFAQDKPLPTPPTDGDKFSIAPTFIKPSSAVPVFDRQGLLSQFLPISADVEMRPLRSEVDQLGMEHARYQQLYKGLKVEGAVYTTHARGGLLQSMNGYFVSIDEFDVTPAVSEEKALAAAIAHSKGRKFAWEDPGLAPGEDYSYPKGELVVLAMRQFGSSPRLAWKYDIYAVEPLYRAYVFIDAKTGEFIFENLRIHQANVPATGTSLYNGSVNFTADQTGPTNFRLRQTASGGGIETYNMNNGTNYGAATDFTSTSSTFTSDNTGVQAHWGAEQTWDYFMSDHGRNSYDGAGAVIKSYVHYSVNYVNAFW... | Function: Extracellular zinc metalloprotease.
EC: 3.4.24.-
Subcellular Location: Secreted
Sequence Length: 481
Sequence Mass (Da): 52682
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A0A7C1XH37 | WVEMLRRDMARLRDCRVRVNVMPLGAAALAGTSYPIDREFTARELGFDAVATNSLDAVSDRDFIIEFINAGAMIMMHLSRFSEELVMWSSAQFGFIELGDSFCTGSSIMPQKKNPDVPELVRGKSARVYGHLMALLTLMKSQPLAYNKDNQEDKEPLFDTVDTLRGALRVYADMVPHIQVNAEAMRAAALRGYATATDLADYLVGKGVAFRDAHEVVGKAVRFGIEHGRDLAELSLEELQQFSTAIETDVFDVLTLEGSVAARDHIGGTAPAQVRAAIARLREELSE | Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3.
EC: 4.3.2.1
Catalytic Activity: 2-(N(omega)-L-arginino)succinate = fumarate + L-arginine
Sequence Length: 287
Sequence Mass (Da): 31671
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A0A496VIS0 | MTNPNSHSGKDMPFVQHLLELRDRLLKMILAIVVILLVLMPFATELFELLARPLLLLMPEGTEMIAIDVASPFFTPFKLTLMLSIFLAMPVIFYHLWAFVAPGLYKHEKSLILPLLASSTFLFYLGMAFAYYLVFPLVFGFMISMTPDGVEMMTDISRYLDFVLKLVFAFGIAFQVPIVTIVLVRMDIVSIESLSEKRPHIIVGAFVIGMLMTPPDMISQTLLAIPIWLLFELGLLLSRVAQRKKARNEQDDKPNYPVPTQTEIEDKIARIEDKRNDEK | 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. Together with TatB, TatC is part of a receptor directly interacting with Tat signal peptides.
Subcellular Location: Cell membrane... |
A0A9E5IKQ9 | MAPDDVGEGVWHDGRIGGGFASSVRRVGASRARQLAQPARGKATCVAVFLQPSVIELEEVLHEFDPDLVQLDHESLAEPAIAAALRARAVLPVLRDGRALPAELPVRALFEGVQSGTGRTADWDAARALAPRMELLLAGGLNADNVAAAIATVRPFGVDVSSGVESVPGVKASDKIFEFVRAARDAAREFCS | Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5.
EC: 5.3.1.24
Catalytic Activity: N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Sequence Length: 192
Sequence Mass (Da): 20189
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A0A946YE75 | MFLNSFRILACFIFFAFSSQLSAEWQTEDAAIMGTTIRVEIWHADADVRQKGIDKVLAEMDRVNRLMSPYIEQSQLSKINKYAHEGPIEVDQDLFELIEKSIEFSQLTNGAFDITYASVGHLYNYRKEIKPTEEEVAAAKLLIDYKNLVLDKHQLSISYLKHGVKIDLGGIAKGFAVDQSIQHLRNLGIKHALVSAGGDTRLLGDRRGRAWLVGIRDPANTEEVIVMLPLQDEALSTSGDYERFFIEDGEKYHHIIHPTTGNSASEVRSASILASDSTTTDALSTSIFVMGPDKGLALLNNLEGVEGVIVDKQGKLYYSQ... | Cofactor: Magnesium. Can also use manganese.
EC: 2.7.1.180
Catalytic Activity: FAD + L-threonyl-[protein] = AMP + FMN-L-threonyl-[protein] + H(+)
Sequence Length: 340
Sequence Mass (Da): 37831
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A0A534AAX7 | MAAKPVDFTAAAGAIVAAGRKLGALGLTPATSSNFSMRLDNGNLAVTVSGRDKGALTPHDVMVVDMQGEPIGTSAKPSAETLLHTQIYTRFPEANAVLHTHSRAQTVASRLYARAGVIRFEGWYTTHESQLDLPVFANTQQMPELVAKVGAWIDSGKPLYGYLIDGHGIYTWGRDMAETERHVEAFEFLINCELDLRRLKFSTLEAPL | Cofactor: Binds 1 zinc ion per subunit.
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 2/6.
Function: Catalyzes the dehydration of methylthioribulose-1-phosphate (MTRu-1-P) into 2,3-diketo-5-methylthiopentyl-1-phosphate... |
A0A534D640 | MLCCRLLPRQAAPWRHISGAAISAGPYQRGGSWYAPCAGECSGILTGRITRPRTMSKILPLTGKGAPAPQAPALNSVAEILAELRAGRLVVIMDDEDRENEGDLIMAAERVTPEAVAFMIRHTSGIICVPMEEQHLARLELPQMVPVNDQQQRTAFTVSVDVRAGTTTGVSSADRAATIRALAAEASVAGDFARPGHIFPLRSRRGGVLVRAGHTEAAVDLCRLAGLKPVGVLCEVMNEDGSMARRPQLEEFARRHRLKIGTIADLIRHRLRTERSVERICEHSVQTELGEFRLYAYQDRANLEVHVALARGRLDGPQTP... | Pathway: Cofactor biosynthesis; riboflavin biosynthesis; 2-hydroxy-3-oxobutyl phosphate from D-ribulose 5-phosphate: step 1/1.
Function: Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate.
EC: 4.1.99.12
Catalytic Activity: D-ribulose 5-phosphate = (2S)-2-hydroxy-3-oxo... |
A0A966A8Y4 | MKLNLAIILTLFRIAAIPAVVVCFYSTMPHARPIAAILFGVAAVTDFLDGWVARRFKQTSRFGEFLDPVADKLMVAIVLVMLVQSDPHWHVDIIAMIIIGREIAISALREWMATIGERANVKVTWEGKVKTVLQMFGIAFMVYQNSFMGLDIYGIGFALLVAAAGMTIWSMMMYLIAAWPFIVGNGGEGNQPNKLDLP | Pathway: Phospholipid metabolism.
Subcellular Location: Membrane
Sequence Length: 198
Sequence Mass (Da): 21908
Location Topology: Multi-pass membrane protein
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A0A924V688 | MFFQKTVRNTIEVKGIGIHSGEPCTLKFRPAPANTGVYFIRADLPGRPFLKVSLANVQAVSYQTVLGGELFKVATIEHCVSALSALRVDNVYIELDGPEIPICDGSALAFTEALFKIELVELDQPRKYCYITEPISYTEGDKNAYVLPYHGLRVGVSIEFSHDVIGKQSLDMEITEQSFLREIAPARTFGFLKEAQALKAAGLAKGGGMDNCIVLDDHAVMNPEGLRFKDEFVRHKILDALGDLVTLEMPLMGHVVLHKAGHDIMNKLVKKIINSPQSYKFVELGADVSSEAKKFANWSIPE | Pathway: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 2/6.
Function: Catalyzes the hydrolysis of UDP-3-O-myristoyl-N-acetylglucosamine to form UDP-3-O-myristoylglucosamine and acetate, the committed step... |
A0A920TJG9 | MTVVFGGTFDPVHLGHVHAANVAGNILNSSILMVLSAAPAHRKAPVASIEDRWQMLRAACANEHRLVPSDIEMCREGPSYAVETLISLNATQDRPVIWVFWR | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
EC: 2.7.7.18
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide... |
A0A2D9XSW9 | MKVIHGLTSLNRCKKRCAVSIGNFDGFHKGHQKLINHIISESKKRSLCSTIITFEPLPEEFFKDKKFKRLTRLKEKXKILDXNKIEQVICLNFXSQFSRISAIDFISNILIKNLDTXYXVIGEDFKFGFERKGNYKLLQDCSTKTNMEVVSIESQMLNNKKISSSEIRKALEEGNXNHANEXLGRTYSISGRVTKGDSRGYRLGYPTANIDIYKSYPINGIFVVQILMENNENHFGLASLGNKPTFSGKNNILEAYIFNFDKNIYNEKLKISFITKLRDQIKFKNENELIQQMDLDYKNALQFLEDRSYEV | Pathway: Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step 1/1.
Function: Catalyzes the phosphorylation of riboflavin to FMN followed by the adenylation of FMN to FAD.
Catalytic Activity: ATP + FMN + H(+) = diphosphate + FAD
Sequence Length: 311
Sequence Mass (Da): 35998
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A0A6L7N091 | MSAKVVFAGTSEFALPSLEALASHAGVEVVAVYTQPDRPAGRGRKLTPSPVKTLATALDIPVCQPRHLDKGDAAETLARLEPDLVVVTAYGLILPPAILAIPARGCVNVHGSLLPRWRGAAPVQRAIEAGDAVTGVSLMRMEAGLDDGPVYARSEVAVDARDTGGTLQAKLATAGGQLLRDHLDGILEATLPAVGQDPDQVTYAAKFSPEEARVHWNGSAVDIARRIRAFNPWPMASTSFRGKRLRLLMAWEEPGIGAGGGPGEVLSTGAEGIVIACGRGAIRVARLQSAGARAMEARDFLNGTGISAGERLG | 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... |
A0A6L7VL30 | MPREIVIDHGGFTNLPASETMRGWLELALGDAIGDLYLRFVDERESRQLNSKFRDIDAPTNVLSFPALGDAVLGDIAICVKVLQAEATAQNKSFNAHLAHLIIHGVLHLRGYDHIEDTAANVMEMLEINLLRELGVANPYE | Cofactor: Binds 1 zinc ion.
Function: Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.
EC: 3.1.-.-
Subcellular Location: Cytoplasm
Sequence Length: 141
Sequence Mass (Da): 15620
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A0A2E9FIA4 | MKGVFILGATGSIGENALKVLEQNAGEFSLIGMSFFKNVEKACQISRKFRPKYIFNQHNENKKRFDHGKIVCDQEELLSVLQSEEVDIVISGISGFAGLNLNLVAAKSSKLLLIANKESIVIAGAHFIKACNDHKTKIIPIDSEHNAISQCLDHNYDHHDIYKITLTASGGPFVGKSIGELDKVSIKDALKHPNWVMGKKISIDSATMVNKCLELIEASVLFDIPASKLDVVIHPQSILHSMVTYVDGSTIAQLSNPSMEIPIANAMRSTKRLTIDFKELFIEKTNLEFFPLSLDHNEIIDLAYDVINHGGTRGVVFNAA... | Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 1/6.
Function: Catalyzes the NADPH-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP).
EC: 1.1... |
A0A1F3T6H6 | MLQNKYQDQLFKINDKTYGFIKWNWNYDEALLFQEEARQYIAENRDLKIFIFTSHPRLFTLGRGLQKSKSEDTKALINFDESMEKRLPFPLYRIKRGGGLTFHYPGQWIMYPIVNLNHPGHSLKELIYFMLENVKVTIEEHYHLTELDYNRQLLGLWKEQHKLASVGIEIKKFITQHGLALNVKKDLEMFKELRNVNPCGLSSDIYRSMEDYLNEEIHLEEFTNKFLKTISDRN | Pathway: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 1/2.
Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-A... |
A0A432EI16 | MKVLVVGKGGREHAIAWKVAQSPLVKQVYIAPGNAGTSKVGKNIPISPTDVENLVKFAKEEKIDLTIVGPEDPLAKGIADAFQREGLKIFGPTKDGAKLEASKVFAKNFMAKYGIPTARYGTFDNPQEAKEFIKRLGDKVVVKADGLAAGKGAFVCQSVEEALKVVDDLMVKGVLGEAGKRVVVEEFLEGEEASYMVMVDGTEYVPLPTSQDHKRLLEGDRGPNTGGMGAYSPTPVIDKETEERIRKEVIERTLKGLAEEGIHYRGFLYAGLMLTKEGPKVLEFNVRLGDPEAQPILTRIESDLVQHIMEILEGNIKGVE... | Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/2.
EC: 6.3.4.13
Catalytic Activity: 5-phospho-beta-D-ribosylamine + ATP + glycine = ADP + H(+) + N(1)-(5-phospho-beta-D-ribosyl)glycinamide + phosphate
Sequence Len... |
A0A2E5V951 | MVEICIISVSSRQPDWISDGFTSYATRLKSNYKIQLLDVPILTRSKNMNLETAIEKEGQLVLKKIPNNAFVIALDALGESFDTNQLANNLRSWTEFKKIFFLIGGPDGLSEACLTRADKIWSLSSLTFPHGLVRILVIESLYRAYSINLGHPYHRI | Function: Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA.
Catalytic Activity: pseudouridine(1915) in 23S rRNA + S-adenosyl-L-methionine = H(+) + N(3)-methylpseudouridine(1915) in 23S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.177
Subcellular Location: Cytoplasm
Sequence Length: 156
S... |
A0A2E5NHF6 | MPGRYHSVKRYPYVSHASIDADDPYRNTTFDDYYFAISDPIGERQSVFIDGNSLPTRFRSLQPGSLIRIGETGFGIGLTFIVACINFLNEASSGARLQWISTERFPVKPSDLMQSIKALPLSADMKQIAHELIVGWPDPIPTCHRRFFKDGRIILDLHFNDSIAVVKNLSGTIDAWCLDGFAPDRNPEIWEPTLFKAIAQKSHQETTFSTFTAARRVRDGLISAGFEVRKVPGFAKKRERIEGKFTGNPTVNPWAPASSIHSKHSIAIIGAGLAGAWTAYAFARRRIPVVVFERQTPASAASGNPQAITYAKLSIEATPN... | Function: Catalyzes the last two steps in the biosynthesis of 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at the wobble position (U34) in tRNA. Catalyzes the FAD-dependent demodification of cmnm(5)s(2)U34 to nm(5)s(2)U34, followed by the transfer of a methyl group from S-adenosyl-L-methionine to nm(5)s(2)U34, to fo... |
A0A351MD47 | MSMPSITELLVILGIVALVFGTSRLRGIGSDLGAAIRGFRGAMKDDSSTPGASGQSGMDSGEPDGRGR | 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. TatA could form the protein-conducting channel of the Tat system.
Subcellular Location: Cell membrane
Sequence Length: 68
Sequenc... |
A0A9D8A481 | MIGLLGGTFDPIHLGHLSIATDVQQHLNLNSVEFVPCKVPVHKQQPNVPVDARLAMLQLALQDYPQFNLNRCEVDRESDSFMIDTLKSMASETNEPLVLILGTDAFNGLHLWKQASSILDYCHIVVCQRPGDQMRQKQYDNYWTKEAESLTKQPSSLIYSLIVTPIPCSSTNIRQNVKSAGQYLPQSVLEFIKLNHLYTSNKINV | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
EC: 2.7.7.18
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide... |
A0A8T7DJ10 | MDRLSVNSLLSFTLIDRYLIQELYKTFLGVTVVLVMIIFANNFVLSLEKIVLGQFSSDALVQLMSFELLEMVNFIIPPAFFFAILISLGRLYRDSEIIAMQASGVGPGTFYKSYLLGAIPVIIVTLLMVLYTLPWAQYSMAQLEANQDRDNTTFAAIEVGKFQEIQGGETVFFAASEGDEPGELRDVFIQNRRNGRLGIISAKEAYQLIDKETAQHFLVLKNGYRYTGEPGQNTYTTSSFYEYGIRIRQLEQKQAKVPVKALPTAELWRSGNPLHRMEMQFRYSIPLAVLALTFLAIPLSRSMPRQGIYGRMLVAFVVYF... | Function: Part of the ABC transporter complex LptBFG involved in the translocation of lipopolysaccharide (LPS) from the inner membrane to the outer membrane.
Subcellular Location: Cell inner membrane
Sequence Length: 380
Sequence Mass (Da): 43366
Location Topology: Multi-pass membrane protein
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A0A8T7E2R6 | MKQLLLIGLALVAAVVLGKFIVGDPGYVIIGYGQTTMRTSFVVFCVIAALALLVFYLVIRFLLWLSRLGSGVRQRREMKKQKQLSKGYLALASGDWREAELLLGRDDDDSRVTPVRYLAAAEAAHAQDAVGRRDEYLQRAQQLLPEARHAVELKQAAIHVDEGRLDAARALLMDVLDTDSDNAEALRLLTRVLREQGDWQRLVDDLLPQLKRSRAFNRFRLEELERDAHEQRLRGASGEDVEAAWKAVPRDARRVPALVAAYADARAAGGDTSGAEQLVRKALQRGWHAELARVYGRIEGANPGRQRAVLDSAAAGGHEE... | Pathway: Porphyrin-containing compound metabolism; protoheme biosynthesis.
Function: Involved in a late step of protoheme IX synthesis.
Subcellular Location: Cell inner membrane
Sequence Length: 392
Sequence Mass (Da): 42978
Location Topology: Multi-pass membrane protein
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A0A352KPW5 | MTGDTSFTLATLAERLNGKLSPRASAAEKVTSVATLAEAQPGQIAFFSHPRYRKELLQTRASCVLIHAKDVAGLEVPHMCVADPYLAYARVAQWLNPISQIPSGRGEGCVVAEGSRIDPSVYLGAHVVVGRDVEIHANCAIGAGTVIGDGTVIGANSRIYANVTLYDHTILGQDVTIHSGCVIGADGFGFAPSAEGWVKIPQLGRVRIGDRCNIGANTTIDRGALEDTILGEGVILDNQIQIAHNVTIGDFTAIAGCSAVAGSTHIGKNCLIAGGVRIVGHLTITDSVQIEATSLVTKSISKKGTYSSALAARSATGWKK... | 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.... |
A0A2E1G1J7 | MSTLETVLLSLLVIDALALIALVLIQQGKGADVGAAFGSGSSNTVFGSSGGATAMTRITTWLSIGFFVIAFSLAYTAKERSEQASQLGIPQVVDQATDAANDENDLSPAGDLGEGQQNEDIPEI | Function: Involved in protein export. Participates in an early event of protein translocation.
Subcellular Location: Cell membrane
Sequence Length: 124
Sequence Mass (Da): 12761
Location Topology: Multi-pass membrane protein
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A0A7C5JD14 | MKIKRFFAKDMRTGIRQVREALGADAVILSNQKVVGGIEIVAAIDYDEALLAAEESATRTSLLDTAPAGEPSTDLLSEDSVSLSQPASARQAYVAPVEAPRDSEIPRPQMPAEPPAEIPRREAAPGAGAEAAVEWSQDPTLQQMKNELKDLRGLLEQQLSSLAWSELSHRNPRQAKLIRCLLELGLSPALCQQVADEVGNGHEDFDNVWRHALAWLASRLPLDTADSLDGGGVVALVGATGVGKTTTIAKLAARYALRHGRDKVALITTDGYRIAAHEQLRTYGRILNIPVRIANTREELSEALKLLADKELILIDTAGM... | Function: Necessary for flagellar biosynthesis. May be involved in translocation of the flagellum.
Subcellular Location: Cell membrane
Sequence Length: 450
Sequence Mass (Da): 48722
Location Topology: Peripheral membrane protein
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A0A352KJC9 | GSIEAVKEQVTFLGRSELDISHKSSIGSAINRLAPRLIINAAAYTNVNQAESQSQMAFDINGTGVQYLAELCAERQIPLIHLSTDYVFDGTQSRPYVEEDVTHPLNVYGQSKLQGEQAIMGSNVEAMIIRISWIYSAVGHNFVKTMLKLAQAGKEITVIEDQIGSPTSALDVANMLTMLIKRFARGEPFHSGLFHFTARGETSWYGFADEIFRQAMELDLIASLPDLKPISTEAYGAALARPANSRLDCSHFDTLFAYDRPRWQDSL | Cofactor: Binds 1 Mg(2+) ion per monomer.
Pathway: Bacterial outer membrane biogenesis; LPS O-antigen biosynthesis.
Function: Catalyzes the reduction of dTDP-6-deoxy-L-lyxo-4-hexulose to yield dTDP-L-rhamnose.
EC: 1.1.1.133
Catalytic Activity: dTDP-beta-L-rhamnose + NADP(+) = dTDP-4-dehydro-beta-L-rhamnose + H(+) + NAD... |
A0A948M427 | MKALKIQFSMMLMLSLTVLMGCSTVPSTNVHQPMSVRSAPAPERAASGGAIYQASYSRPLFEDRRARNIGDVLTINIVESTSASKNVSSTAGRTSSIAETAATPTIFGYTPSPSKLGVAGILGGAANFDTSVTASGSQKFEGKGDSSQKNALLGMLTVTVIDVLPNGNLLVSGEKQMGINEGTEYVRFSGVVNPSTISSANVVVSTQVADARIEFKGRGEMDSAQVMGWMTKFFLSVLPF | Function: Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation.
Subcellular Location: Cell outer membrane
Sequence Length: 240
Sequence Mass (Da): 25203
Location Topology: Lipid-anchor
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A0A8T3QC13 | MLTVDSFQKSLRELTQSKTFCVAFSGGLDSSVLLDLLSQLSVIETGISIRAIHIHHGLSANADRWADLCTTYCARYHIPLVIKHINIKRDNESVEEQARNLRYNVFKELLSEKEVLVTGHHRNDQAETLLLQLFRGAGPKGLASMPAATRFGKGLLARPLLGFDKESLKQYAEIQTLNWVEDESNRNLLFDRNYLRNSLLPLIQSRWPAVIENLSRAATHCANANHFIETQIADVFVEAFDPEQLTLSIPAVLKHALPVQNHIIRYWLQQLNLSLPSTQKLALLLKEIMNARPDAVPLLRWKNVEVRRYGDHLYAMRPLL... | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34)... |
A0A2E2HA91 | MSFTDKNEKVSVSFEFFPPADLSKADNFWDSVENLAKLQPDFISLTYGAGGSTRERSLEILKRLVADTSLTPVAHLTCVAVSKDEANEMARQFHEIGIRRLVVLRGDPPEGDNLSTVHPDGYANATEFMHGLNKIADFDMSVAAYPEIHPESPNMEHEIEVLKQKVDAGARRFITQFFFDCDVYLRFVEKARAAGIDIPIIPGILPIVNFNRVRGFAESCGASIPPWLEKLFEGVEPSSTINNMLAASVLIDQCNTLYDAGVRNFHFYTLNKSELTRAVCKTLGIQEKDTK | Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway.
EC: 1.5.1.54
Catalytic Activity: (6S)-5-methyl-5,6,7,8-tetrahydrofolate + NAD(+) = (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + H(+) + NADH
Sequence Length: 291
Sequence Mass (Da): 32451
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A0A3C0I2W2 | IPAITPGSANINVTLGNEWYFRNIYNAKASGQFLANYVKNVFKQDKVSIIRETAPYGSYLAQVFEEQSLKLGMSIQNQWHYDKNNENLDQVFQKIVDELKAKQKEAGVILLAVQANEGVKLVKLIKEASIQNSIIGASSLSEKTFSNGFDKLPMEKEHPGFYTNDIYVATPLIFDTANEKAQNFKELYQKNYDDVPGWAAAYAYDTAMVLVEAMKRAKLEGSKRALKEDRRKIKDALASFNSIYNALEGITGLNYFDENRDAQKPVSIGIYKHKNSVSALTQLQVVRHPNEIADLQNAIKNDRVLLINEKQMYKTNVVYV... | 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... |
A0A976KL11 | GLERRMTVTLPENDISDEVEKRLNSLRKTVRVEGFRPGKVPLKIVRQRFLDQVKDEVMGKVVQSTFGDALKEKDLHPASGPTLQSRELKDDQAFEYAVTFEVYPEIEIQGLDKIDLEKPVVEISDDDVDRMIETLRKQKVTWEEVDRESQADDRVILDFEGKLDGEVFEGGSAKDTPIIIGSGRMLKDFEDNLAGLKTGEEKTFDVEFPDDYHSEDLAGKKAEFSVKVNNVSEPKLPEVDEEFVKGFGVDEGGVDKLRADILENMQRELDQAIRSKVKNQLMEGLLEQNKIDVPNALIDQEVESLRQSAMQDMQASGNAS... | 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
... |
A0A1Y4HIT3 | MLSGLCAPRARPGIFAFCAPFWQKRISCGIKTVKRGMEMEYLRIRGGRALQGSVTIPGAKNSLLPIMAASVLCEKPVTLYNLPDLSDLHTSLDILRGIGWGAEYIDGRVDLFPASRLRARVPKRAAGAMRSSVFYLAPLLHRAKRVELPATGGCRLGARPIDIHLEGLVKMGAIARTENDLLILEAPGGLHGTRFALRYPSVGATETLMMAAVLAKGRTCLSGAACEPEIEDLARFLNSCGARITGAGSPRICITGVERLEGARHTVIPDRIVAATIIAAVAAAGGSAVLREVCPEHLEGVCTVFRRMGMKIARLDLTTL... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine.
Catalytic Activity: phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
EC: 2.5.1.7
Subcellular Location: Cytoplas... |
A0A2E2HFP2 | MSIAISIVLTLLLIALISGILLGFFAEKFRADGDTLVEEINRLLPQTQCAQCGYPGCKPYAEAIARGEAINKCPPGGKQTINDLAQLLDQAYVPLDPDVGSEEIPRTAIIREAECIGCTFCIQACPVDAIIGAAQQMHSVITAECTGCELCVAPCPVDCIDIIPLNTKPPAEMLSKSLSQQECIRCGLCVDACPVDLLPQQLYWFIQGEAYEKAEQYKLMDCIECGLCHAVCPSHIPLVQYYQKGKATLAEKRQQQQQADYTRQRFENRELRLAREKIQAEQRRQERARLADQRSSQDNMIQEALARARARQNQPGEHQ | Cofactor: Binds 3 [4Fe-4S] clusters.
Function: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane.
EC: 7.-.-.-
Subcellular Location: Cell inner membrane
Sequence Length: 319
Sequence Mass (Da): 35454
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A0A2A2B7B7 | MAPLSKSSPAVIKKAPSRSKHERGFTLIEVMVALAILAVVAVAASRASSAYLSSVDTLRTRTLAHFVAQNTAADLHIQKTWLTANRTQTINAQGRDWQVVITVSNAITPALKKVNIAVAPMVDGQTRNVVTDIDVILSNPEQDMGSLDLGNMSSQSADTLGQIGDGL | PTM: Cleaved by prepilin peptidase.
Function: Component of the type II secretion system required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm.
Subcellular Location: Cell inner membrane
Sequence Length: 167
Sequence Mass (Da): 17705
Location Topology: Single... |
A0A661CIY5 | MDKPLLPSDLVESVKRALAEDVGNGDLTAQLIAADTPANAQVISRQPAILCGAAWFEEVFKQLDSRVQITWQAQDGQTISPEQLLCNLTGPVRTLLTGERTALNFLQLLSGTATQTQRYVKAISGTHAQVLDTRKTLPGLRHAQKYAVRCGGGTNHRMGLYDAFLIKENHILAAGDIAHAIAAARKQAAHLPVEVEVEVETLEQVKEALTAGADSLLL | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-ribonucleotide from quinolinate: step 1/1.
Function: Involved in the catabolism of quinolinic acid (QA).
EC: 2.4.2.19
Sequence Length: 218
Sequence Mass (Da): 23495
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A0A2D7FWY6 | MEILQSILALIVTIAILVTVHEFGHFYVARRCGVLVERFSVGFGRPLVVFKRGSSAPSVEQSVVAQQYPGDNQEPLPETEYCIAMIPLGGYVKMLDEREGYVPEHLRDYAFNRQSLLARTAIVAAGPAANFLLAFVLYWLLFTAGVSGVAPVIDTPPAGSPAAELKLGKGSEILTVDGQQTRTWRQVNLALFDRLGESGAILIEVKPFAAGKTQSLSIPIDAFLIQEEEPNPALALGLLLSRPPIPAVLGDILPGGAAETAGLRSGDQVLKIEGQIVSGWQGFVEMIQANPGQRLALEVDRDGQVVYLNVRPEAVVIEGA... | EC: 3.4.24.-
Subcellular Location: Membrane
Sequence Length: 473
Sequence Mass (Da): 51150
Location Topology: Multi-pass membrane protein
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A0A661FGB8 | MNKSGYKLVAFDLDGTLVDSALDLAYAGNEMLAELGLESVTDDQVRHWVGNGAPKLVQRMLTRKLESEQSHPLLEKALSIFLALYEKNICHFSELYEGVNDGLENLQKTGVKIACITNKPLRFVRPILAQLGIEGYFEQVVGGDSYPHIKPHPMPLLKTADYFGCPANEAVMIGDSNNDILAARAAGFGIICVNYGYNQGRRIEDFHPDRVINSVAEIPQYLKVI | Pathway: Organic acid metabolism; glycolate biosynthesis; glycolate from 2-phosphoglycolate: step 1/1.
Function: Specifically catalyzes the dephosphorylation of 2-phosphoglycolate. Is involved in the dissimilation of the intracellular 2-phosphoglycolate formed during the DNA repair of 3'-phosphoglycolate ends, a major ... |
A0A2E1MP25 | MNDGVLIIGAGYVGMSHALGFAKNCEVKVLDIDQEKVNKINDGDLLINEHHHDSSQNLILNVEATTDRTVILEEYKYVLICLPTDLNDESGDLETTIISDYIKYIIDATKSYIIIKSTVPIGYTQSQIDEYGSGRILFSPEFLREDNSYPDIQNPSRIIYGSDSTFGKEYHQLVEEIIQKKEVEVLFMSPSEAEAVKLFSNTYLAMRVAFFNELDNFAITKNLSSKKIIQGVSSDPRVGMYYNNPSFGYGGYCLPKDTKQLSELFKEKKIPNNLISSIDSSNQSRMNFISKHIAEKGISKIGIYRINMKKDSSNYRNSAI... | Pathway: Nucleotide-sugar biosynthesis; UDP-alpha-D-glucuronate biosynthesis; UDP-alpha-D-glucuronate from UDP-alpha-D-glucose: step 1/1.
EC: 1.1.1.22
Catalytic Activity: H2O + 2 NAD(+) + UDP-alpha-D-glucose = 3 H(+) + 2 NADH + UDP-alpha-D-glucuronate
Sequence Length: 390
Sequence Mass (Da): 44387
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A0A920LXF4 | MISGLLVLNKPSGISSGEFIRKLKPFLGDSKIGHSGTLDPLASGVILACLGQMTRFTNFLANERKTYIAEMMFGLQTDTGDLDGKIEREYKKIPTKNDFNKIKKKFIGSLNQEAPKYSSLKYKGKPLYHYARKNKEVPKKIREIEIYKLDLISVDQNKFKFLVECGKGTYIRSLVKDLAKDLNSVAVLSNLQRTISAEHEISEAHEIESINRENIKSKIIQMGDALRSLDKLQCASEIIDRIKKGQKIYLKEAEIKSKYLRLFDEKNKFIGILKNINGLVSPKRLISIEN | 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: 290
Sequence Mass (Da): 32946
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A0A8T7C609 | MNDRIFLEALEIQGVIGIYEWERNTRQTIRIDLEMPANAAAASGSDEIEDTLNYKDVAKRIINYVEDSSYMLVETLAENIAQIVMNEFGVAWIDLSVSKPGAVRGSKNVGIRIHRGVYESSDTDDVFLSLGSNIEPHKHLHEALQLLTERFGPLCRSTVYRNKAMGFVGEDFLNLVVSFPSREKLDVVKAACTRIEDQCGRTRGTEKFAPRTIDIDLLLFGDTIMTTPQTTLPRPEILRFPFMLRPLAEL | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 3/4.
Function: Catalyzes the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin.
Catalytic Activity: 7,8-dihydroneopterin = ... |
A0A976PKE5 | VSIVGDISQVLDQFDVLIDFTAPVATLANAEACAPAGKKMVVGTTGFTPEQRQQLLSAADTTGLCIASNFSTGVNLCFKLLEMAAKVLGDEVDIEVYEAHHRHKVDAPSGTALSMGEVVAKTLGRDLSEVAVYGREGQTGARDRQTIGFATVRAGDIVGDHTVMFAADGERVEITHKASSRMSFARGAVRAAAWLQGQEKGLYDMQDVLGLK | Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4.
Function: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.
Catalytic Activity: (S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydro... |
A0A7C1YAP2 | MFLLAILISLALERLVPALDRLRGILWFRQYADGLRHKLLPEDNRRGALTVLLTVLPPVLLVGLAQHLLDMQLWLFSFGLSLAVLVYALGPRDMDRQVKAYLEARAHDDDERAQVILHEFLPFPVPDNEQARTDVVIDMIFVLTHERVLAVFFWFLLLGPMGAILYRLVSELVSTPPENANEDYWLAATRLHMLLAWLPAHLSALSFAVMGSFMHALQVWHETSLRDMSRVPVVCHQYVIRTGRAALQLDQIDGNQAIEEALGLCSRSLIAWVTILALLTLSGLVM | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
Subcellular Location: Cell membrane
Sequence Length: 286
Sequence Mass (Da): 32331
Location Topology: Multi-pass membrane protein
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A0A966SE38 | MRAVSLDLDGLDADAVEAVFFEAGAYSVVLTDRRDDAILEPKPGEIRLWPATRLQAIFADDGASEDALAAIAGAIGCGRSALHVEEIADRAWEREWLKDFRPMRFGRNLWICPSHASVDERDAIVVALDPGLAFGTGTHPTTRLCLEFLDERHARTRTANDDLVLAEKPAATRVVDYGCGSGVLAIAALKLWPQAEGLAHDIDPQALTATHDNALANDVAERIETFAEADALAARLRTQGGADLVLANILSGPLCELAPILCQLMAAGGELVLAGLLDEQADEVIAAYAPLLALRRWRSLEGWSCLAGCKPR | Function: Methylates ribosomal protein L11.
Catalytic Activity: L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
EC: 2.1.1.-
Subcellular Location: Cytoplasm
Sequence Length: 312
Sequence Mass (Da): 33495
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A0A967CBW6 | MAPPRINPVRFVLVAGEASGDRLGAALISALKARFPEAEFVGVGGAEMEAAGLDAWFGLDAFSVNGFVEPLLKLPSLLSRFFELKRRTISVRPACFIGIDFNVFNLLLAGTLKRQGIKTVHYVSPSVWAWRQGRIRRIKRNVDLMLCLYPFEIDIYRDHGILCEFVGHPQARRLHGPSERVDWLPTKPTLTLACLPGSRRSEIASMMPLFAGTVSDLEHKGYDVRVLIPAPRESLRSDIERLLPSTFGTRRVTLTVGDAEDVMRDADCVLVNAGTAALEAMLLGKPMVVVYQLGALTYRLVKTLVRLERFSLPNILSGEE... | Pathway: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
Function: Condensation of UDP-2,3-diacylglucosamine and 2,3-diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
EC: 2... |
A0A4Q5VD36 | MPLSIFVKKSHNIWLRAWYGDSRWIYCLLPLSWLFAIISSARKFVLTRFFQKKISVPVIIVGNISVGGTGKTPLLIAMAKYLQSQGHKPGVVSRGYGGKVEQYPYLLNEKTKASESGDEPLLIYRAAQCPVCVAPDRVAAALALVQEGCTHILSDDGLQHYQLGRAMEIAVVDGKRLFGNQQLLPVGPLREPCSRLKSVDLVVVNNLINHESLSEFHPVHAMKIQPKAWMHIASRKLMPLNDVFFKTPIHAVAGIGNPERFFKTLDDLSLNYYAHHFPDHYQFSEIDFENYHHDTVVMTEKDAVKCGEFPKSEWYSLVVD... | Pathway: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 6/6.
Function: Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form te... |
A0A7C7XU62 | MFKVEINGQQFEAEPGSTIIEVADNAGIYIPRFCYHEKLSVAANCRMCLVEVERAPKPLPACATPVTDGMVVQTLSDIAKQAQADTMEFLLINHPLDCPICDQGGECPLQDQAMGFGASSSVFDEVKRSVDNVDIGPLISTEMTRCIHCTRCVRFGEEVAGVMELGAIGRGEDMKISTFLGTSMDSEVSGNVIDLCPVGALTSKPYRFTARTWELNGHKGISPHDCLGSNLEIQEIGGVVKRVLPRDNEAVNECWLSDRDRYSYESVNCSDRLTMPLVRRGENYQEIEWTEALELVSSKLLQIKETWSGKEIGAIASPAA... | Cofactor: Binds 1 [2Fe-2S] cluster per subunit.
Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic ... |
A0A7C5PSU0 | MRYPTLQNDSITAGILAGGQGRRMGGIDKGWADFEGKPLIAHVLERLQPQTHSILISANRNLDAYRALGYPVLKDRIDGFQGPLAGLASLLQACPTEWLATVPCDAPGLPNDYLVRMASAAEQTPGTRIVVAHNGDRLQPVHMLVARNLLDDLLSHLQQGGRKVRGWLGQYAYQTADFSDQPQAFFNLNHEADLRQPIRTN | 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... |
A0A2K8P2P5 | MGFWNKLKDKISGNQTEKQNNEEKIVKSKPIVEQKQLTEKEIAKKQKQKAKKEKAEKAIAKSALDFSKDIKKLSKKYKKMDDDFFDELEEVLIKTDMGMKMVLKISNNIRRKVKNTSEANEFREILAEEIYDIYTDGSKKVEELNFEDGRLNVFMVIGVNGTGKTTSLSKIANFYAEQNKKVLIAAADTFRAGAIEQLEEWVDKRLDSKVDLVKGKKQNQDPASVVFDALEKAKAEGYDLLLIDTAGRLQNKVNLMKELEKMYQIVHKFDKKAPHELLLVIDATTGQNGVMQAQEFNEVADISGIVLTKMDGTSKGGIAL... | Function: Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Acts as a receptor for the complex formed by the signal recognition particle (SRP) and the ribosome-nascent chain (RNC).
Subcellular Location: Cell membrane
Sequence Length: 366
Sequence Mass (Da): 41532
Location T... |
L7MJ86 | TGSPALCIASFHPRGLGGAATASFGAVSVRIERRTVEVHLRVEEPRAMTAVVAAARREDPHPIRCSRRQVVTMARCSFLPTGIPFVVCVVFAAFAVVCCGATTDCSAPRDLLSSTLGGGDHRWTEVLAASPTSGGSLTLCPLASGRNTCCTHDTELRLREAAWDHFRFRLRDATAPLRRFLDDSLALFRERLSSLVSEAERNTEVLFSDVYSERVAVEARAPVRQLFRALRHRLGLSSGTSEDAESAREGSQDDPVDVFFGELFPLVYFHTVNPRLADFSDDYKACLRGAQGRLRPFGDAPLRLKGSLAESLGAVRTVLR... | Function: Cell surface proteoglycan.
Subcellular Location: Cell membrane
Sequence Length: 673
Sequence Mass (Da): 71988
Location Topology: Lipid-anchor
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A0A3C0QAX1 | MRLLVTGATGQLGSELARKLTGLGHEVFAPDPDDLDLLDPVRVAATIREQRWDWVINCAAYTAVDKAESAAEQAFVINRDCPGEMARSVAGYGGRMLQVSTDFIFSGDQRCPYTETDIPKPLGVYGRSKLEGEQVVLEMLPDATVLRTAWVYGVYGHNFVKTMLRVAAEGRPLRVVNDQMGTPTWTADIVMAIVALVEQQAGGTYHFTAAGQASWYGFASAILEDAARIGFPVNTDAVVPILTSEYPTPARRPAYSVLDTRKIEPLLPSPPPEWRDSLNNMLKELATCADCL | Cofactor: Binds 1 Mg(2+) ion per monomer.
Pathway: Bacterial outer membrane biogenesis; LPS O-antigen biosynthesis.
Function: Catalyzes the reduction of dTDP-6-deoxy-L-lyxo-4-hexulose to yield dTDP-L-rhamnose.
EC: 1.1.1.133
Catalytic Activity: dTDP-beta-L-rhamnose + NADP(+) = dTDP-4-dehydro-beta-L-rhamnose + H(+) + NAD... |
A0A967ETU6 | MSNPAVVFGGPSPEHDISILTGLQACRTLLDAGRSVEAIYWAKSGAWFSVDPSLEAADFADGVPRRARPLRFMAEAGGGFIARKRPLDISAVVNCCHGAPGEDGTLQAAFDLAGIRYTGPSAAGSALGMDKLAFGAVVQLAGLRSVPRRLLEPRIEWDATPPFIVKPRFGGSSIGIEVVDGMETALALAKSSPHLKSGAVIEPFLEGSRDYNIAIRTYPSLQLSAIGAPVRDAKSGAIYSYEQKYLAGGGLEGSAREIPAKLPAEVAGSIRQAAMIVSDLVGVRSVARFDFLVRGSDVWINEINTIPGSLAAYLWVDPPL... | Function: Cell wall formation.
EC: 6.3.2.4
Catalytic Activity: ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) + phosphate
Sequence Length: 362
Sequence Mass (Da): 38175
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A0A965TBE8 | MNEDIEKMSFEECITALEALVKELESGTLDLDKSLEVYERATVLRDRCKKILEESERRVQKITENSEGIRRSDLKIE | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
EC: 3.1.11.6
Subcellular... |
A0A938Q4T6 | MHGLDFSSDHCPIALRKDGRIVDLAYKNEQDTIPNEQSIVYTTDTDGLEILRHSCAHLLAQAVLELHPEAKLAIGPVIEDGFYYDLDLASTLSENELDLIEQKMREIASRNLKVQRHEYDLKDAIALFQKQDQIYKVEILESLDGADPVSCYQQGDFIDLCRGPHVPSTALLKHFKLIKVSGAYWRADSSNKMLQRVYGTCFATAQELDAYIKRIEEAKKRDHRLIGNAMDLFHMQEEAPGMIFWHPRGWTLFRLVEQKIREFISDDYLEIKTPQIVHRSLWERSGHLAMFAQNMFQTQIEDDFFAIKPMNCPCHIQVFN... | Cofactor: Binds 1 zinc ion per subunit.
Catalytic Activity: ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + H(+) + L-threonyl-tRNA(Thr)
EC: 6.1.1.3
Subcellular Location: Cytoplasm
Sequence Length: 619
Sequence Mass (Da): 71485
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A0A520TKM8 | MIVSNWKMNGTKSDIEHWVNEVSNKIDYKSHIKCIICPPSCYLDSTRQIISKIDSPIKLGSQEIDSTNSGALTGGINSQMLKDFSTEYVLIGHSEQREHLNEDNITLRFKLDSAIQNGISAIFCIGEPAEMKLAGNTENFLLEQLDLLTPDDLDFITIAYEPIWAIGTGLNADNKYIESI | Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Catalytic Activity: D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate
EC: 5.3.1.1
Subcellular Location: Cytoplasm
Sequence Length: 180
Sequence Mass (Da): 20113
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A0A9D6WGP5 | MNLRLRLTLLLTSIFVITLGVGAGYVMKNARAAVTDELLSSLDLASSLIGLMVAQEASETSAPDPVRLARQLTGLGHPRHLHIELSSSPEALVLALPAAGGNRARAPDWFIRTIEPDRLDLLRSVRVPNSGLHVIVRADPAAEISEVWSETRLMLGVLVAFGVVAVALVSLVVGRALRPLYAVAAALERVERGEYASRVAGSGSSEVDAIAERFNHMASVLERSHREMTALATRSLAIQEEERRNLAHELHDEMGQSISAIKALAVSIGQRAPAADGTLATSAATIANVCTDVYDRVRHMMMRLRPIILDELGLVTALQN... | 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... |
A0A937I972 | MYSFENIQANLNNRIDLSIEEAYFVSEKMFEGSLDDNQIKEILILLNKKNICSAELIGFATAMRKISTKVEINEKVIDSCGTGGDGIGTFNISTCASFIAAACDVKVAKHGNKAITSSSGSADLLHDAGAKINLEPEHVSKCIRHVNFGFMFAPLHHMAMKNVANSRKSLAPEKTIFNMLGPITNPANAKIQLIGTYNKEAMNLIANALLELGTKSALILNSRDGMDEASIYDVTDVLEIKNNNITSFTIDPIKYELVGEDLENIKTNTERSSLDIIYSVINNLDSDARKISVLNAALLVMIYKEIDLKDAISQCKDSLD... | Cofactor: Binds 2 magnesium ions per monomer.
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 2/5.
Function: Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).
... |
A0A2G6KU62 | MAVRFETVDENSDGQRLDNYLARVMRGVPKGRIYKALRKGEIRVNKGRAKADYRLKHGDQVRIPPVRQADPRAPQPVPAHWKDTLEQAVLASFPGVLVVNKPSGLAVHGGSGLNFGLIEALRQQRPQERYLELVHRLDKDTSGCLLIARKASALKDLHRQLREGTMSKRYLALVAGRWPARVRQISAPLEKNVLSSGERMVRVSAEGKPSLTEFSVVKRFHGATLIEARPVTGRTHQIRVHARHQGFPLLGDSKYSTEHTEQVAKSLGLKRLFLHASELHFDVEGKRRSVSAPLDSHLQHIIDRLEY | Function: Responsible for synthesis of pseudouridine from uracil.
EC: 5.4.99.-
Catalytic Activity: a uridine in RNA = a pseudouridine in RNA
Sequence Length: 307
Sequence Mass (Da): 34554
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A0A2G6KRK7 | MSTSSILIFLRSTLFYIVLIIFTVVFSTSCKIISPAMSYRTRFRFIIQGYTGFITQWLRICCGVDYQVTGTENIPDTPCIIASNHQSTWETFFLQTRFAPQTQVVKKELLSIPFFGWILSLTNPVAIDRNNRKQAMKQILMQGREKLRRGIWVLIFPEGTRVNPGQTKCFSKGAAALAIHAGVPVLPVAHNAGEHWPNNGYMKYPGTIKVVYGPLIQSDNKTTEELTRETEQWIGNKVREIGNQPIHKEGIVPLQP | EC: 2.3.1.51
Catalytic Activity: a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphate + CoA
Sequence Length: 256
Domain: The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate.
Sequence Mass (Da):... |
A0A2A5D2H7 | MKIRRFFANDMRTALKQVSNELGPDAAIMSTRKTKGGVEVVAATDYEAAITQHNQQRKKQVETKRAISVTVGDKLDVSTLSSTSVQAEPVKKSAVDIEWHQEPDLMAIKQEVGLMRELLQDQLGELAWHDKSRRSPIQAAILRKLINMGFTPSLSNDFAKTITVFDDFSTGWQQLKNNICYAMPRTENSILQKGGVVALIGTTGVGKTTTIAKLAARYVLKHGADSVALVTTDSYRVAAHEQLRIYANIMGISMRVADXADSLAVILDELANKKLVLIDTAGISQRDQRLAEQMSCLVNSGKSIDCYLVLSTTAQTRVLE... | Function: Necessary for flagellar biosynthesis. May be involved in translocation of the flagellum.
Subcellular Location: Cell membrane
Sequence Length: 403
Sequence Mass (Da): 44218
Location Topology: Peripheral membrane protein
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A0A964PLP7 | MKRNLSTRYAIPRQEMSLTRPNSFLAIALSVMLLVGLGYIAKAVSGTDYPIRKVSVEGDFRFLTPTYIQALVTKSLDGGFFQVDVQKIHRELLEEPWIFDATVERLWPDVIRVEIKEQIPTARWGENALLNSDADVFAPHVASIPQALPRLSGPVGTEIEVLRAYKKMAERLDALGMKVGSVSVSQRGAWTLTLTDNTQLIFGRDDIWRRLHRFCASFDVLLKEGWTRIAKVDLRFTNGFSVTERRRPELRSELQKNG | 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. May control correct divisome assembly.
Subcellular Location: Cell inner membrane
Sequence Length: 258
Se... |
A0A6N8F9H2 | MQIISSLSELRTWRQQCYKDGKTVAFVPTMGNLHEGHIELVQQAHKYADFVITSIFVNPMQFGENEDLDAYPRTFDADCKKLEAVNNHVVFYPTVADMYPNGLKAQTVVSVPNNELEHCAEATQRPGHFDGVATVVTKLFNMVQPDTALFGQKDYQQVRLIQTLVKDLNMPISIVPVPTVREVSGLAKSSRNGYLSDDQKATAAVIYQTLLAVQDALKSGARNINEMQTFALEMIELAGLKPDYIEIRDSSDFGKVTDSSLQAVILVAAFVGKARLIDNLTVELS | Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1.
Function: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
Catalytic Activity: (R)-pantoate + ATP + beta-alanine = (R)-... |
A0A1X6PCW3 | MHTLRFLGSGARLLRGSVYGARGSGVAGAAGPCLRPPRAGPATGSGSWGFLPRTATAGARAMSTEILPEHRRITMPKLSPTMEVGTIAGWRKAEGDAIDENDVLAEIDTDKASMEYNYSDVGFLAKIVLPEGTSDVKVGELIGIYVEEEKDIAAFKDYDPLSESLVTEASSKELADVAAQPVDQDFESATTPAKQASTDAAVQASAANVSTSKPAPGGDGRIVASPAARVRAAETGLSLPEIDGSGPDGRIVVADVLRAMESTDSRSGGAPSPSSSSPAPSPIVAVMEGGVGMYEDVEVNRFQRVTAARLLQSKQTIPHY... | Cofactor: Binds 1 lipoyl cofactor covalently.
Function: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2).
EC: 2.3.1.12
Catalytic Activity: (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + acetyl-CoA = (R)-N(6)-(S(8)-acetyldihydrolipoyl)-L-lysyl-[protein] + CoA
Subcellula... |
A0A2E5J9J6 | MSPSINHLILNAIQKKPINRTPIWIMRQAGRYLPEYNKIKDKAGGFINLLRNPDLACEVTLQPLKRFNLDAAIIFSDILVVAELLNLEFEFIEKKGPVFFNTITTKKDLGIVPNKFDISKLNYVFEAIKLVKNELNNSKPLIGFIGSPWTVATYVVEGNSTKKFNKINKLVDEENPIIDDILSLITNASIEYVQKQIDAGIDIIMIFDTWSNLLTKNNYQRYSLSYINKINEVIRKTKTPIIYYSRNTYENLNLLKHLDVDVVGINSDVDIKIVKKNIGERFALQGNLDVKILKEDNNTIKNEVKKILNNYGIESGHIFN... | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 4/4.
Function: Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III.
Catalytic Activity: 4 H(+) + uroporphyrinogen III = 4 CO2 + ... |
A0A7C7JBK6 | MPSSLRPELKNAKKSFVLRKGRTTSAQRRALKYLKKQHTIQLGEDKVDFSAAFEGSPKKLIADVGFGSGESLLYMADRFNEVNFVGIEVYPPGIGSALNQIEQNKLTNLKIIESDVFDLLETKVTNETFDAMIFLYPDPWPKRKHLKRRLLSEDFLNLLYDKVVIGGLVFCKTDWGDYYTQVKEAVASDNGWLREDLTNLPEYLKSLPQTKYERKALIEGRESRELIFRKTPR | Pathway: tRNA modification; N(7)-methylguanine-tRNA biosynthesis.
Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
EC: 2.1.1.33
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
Sequence Length: 233
S... |
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