ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
|---|---|---|
A0A3C0P9Q9 | MSAINSRKVQPSSGKNAGKTAKLLESHRIDAVASLRRIRSTPLSSFMTVFVIAVALLLPALLYALNTNLLTVLQRFQHETRISLFLLDSLPDAQGRTVSENLLTDSAIGSVEYISAEQALGEFSASSGFTDIVADLEANPLPATIIITPAATEPSSVEALASRLQRLPEVALVQLDSAWLRRLAAISELLDVMTRSLGLVVIVGLCFIVGNTIRQGVENRKDEIRIIKLVGGTNGFIARPFLYAGFLYGLFGGLVACGLQAAVVVSFSSSLLDLAALYDTTFEPVGLGLGSGFVLVAT | Function: Part of the ABC transporter FtsEX involved in cellular division.
Subcellular Location: Cell inner membrane
Sequence Length: 298
Sequence Mass (Da): 31693
Location Topology: Multi-pass membrane protein
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A0A661FU12 | APAPAPTRTSGSNSGVTASLAAATTVASNVVQGGSVAGATQSIPQTITTTSSQANRVTGNSAFASSEPEMVAVSRLTRTNYVAPKYPRAAHRRNVTGSVDITFTVTTDGRIRDMSVLNSEPGVTFDQAAMDAVEKWRFEPVIENGVAVEKRTAVRLAFTLQ | 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... |
A0A661FRR7 | MRTTCLLSVFCVLLLTACGQDQVRDADITVPLVDAPIPVGKLGDAVRPVAYRLDLTILPDQADFSGNVEIDIDIAAATTIIYLHGSGLEVSAVSLVALSGGVYDAEYLQVDNTGVARLTFPAPVPAGAATLRFEYTAPFKTRSEGLYHTTVAGKSYAFTQFQPIDARRVFPGFDEPAFKTPFTISVTAKSQDVVISNAPVMSEELTGDGHKRVVFETTEPLPTYLIAFAVGPLDVVEGVSLPPNSVRSRSLPFRAAATSGKGDRLRFVLDNTDPIVTYLEEYFAVEYPYPKLDLIASPEFGTGAMENAGAIIYGDALMLL... | Cofactor: Binds 1 zinc ion per subunit.
EC: 3.4.11.-
Catalytic Activity: Release of an N-terminal amino acid, Xaa-|-Yaa- from a peptide, amide or arylamide. Xaa is preferably Ala, but may be most amino acids including Pro (slow action). When a terminal hydrophobic residue is followed by a prolyl residue, the two may be... |
A0A7C1XGW6 | MSNRLRYLLILTIVVVVASLSSWLLRSVEERFVKGPEVVSRSPDYFMENFTATALNTEGEADYTLQASYLAHYPHNDSVLMRKPFMAVFRDDLTPWSMRADEGLVTEHGRFVELGGAVTLQRGKTARHPLLTLNTRDLRIDTRLKTAETEAEVEITQPGTRIRARGMRIDIASGSLELLANAEARYDVR | Function: Involved in the assembly of lipopolysaccharide (LPS). Required for the translocation of LPS from the inner membrane to the outer membrane. Facilitates the transfer of LPS from the inner membrane to the periplasmic protein LptA. Could be a docking site for LptA.
Subcellular Location: Cell inner membrane
Sequen... |
A0A2D5ZYL3 | MSLGPWQIVIIVVVLLVFFGPKRIPGMGKSLGEAIRDFKKGLKEDEIDVTDSVKHEQIEQEKQAEAASQAKTEKEKDKA | 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: 79
Sequenc... |
A0A938Q553 | MCLLPAAWLVAGIIALQSGDATSVAARALGANPVEKIQDTLGIWGLRLLLATLSVTPLRVLLGWPKLYLFRRMLGLFAFFYIAMHFLWYLFVDQAFDWVTLAADVVKRPYVTAGFTAFVLLVPLAATSTARAMRRLGRRWQRLHWLVYAAAVLGCVHFWWQVKADIREPALYAGIAALLLGWRVVQTQLRRRALRVASAIPASIRSPPPTVRSSTDSPSSHQPSIAASTGSPTDATATNSGSRWRSDQL | Cofactor: Binds 1 FMN per subunit.
Function: Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by t... |
A0A8T7D247 | MSEILVSIGSFILVIGVLVTFHEYGHFWVARKLGVKVTRFSVGFGKPVFSWRGKRDDTEYVIAQIPLGGYVKMIDERDEPVDEADLPYAFNRKPLATRMAVVVAGPLFNFILAVFAYWAVFIIGVEGIKPVVGEIQASTRAEQAGLRSGDQIVSINAVKTVNWDSIGLELIEGVLDQADQVTVTVIDENQQEQNHYINLKGLSADLSKGNIISNIGIHPRLPVWSAIIDSVIKGEPAALAGFRPGDKVIAVNEQGIKDWRDWVRYLRKRPGEQVQVSILRDGETRQLSLVVGNKLNDSVSYGYIGAIAKAPEGIPPELRS... | EC: 3.4.24.-
Subcellular Location: Membrane
Sequence Length: 413
Sequence Mass (Da): 45043
Location Topology: Multi-pass membrane protein
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A0A2E4LIH4 | MVKVLLERIKTALILAAGFIIISTQSSILIFNLLISGSMIFVAWEWCSLVGFFNRSSKIIFASGFIAIVIFLYLKLGLAPESTQINEELSLAILSSGVFFWIISTFFLYHYPKYTNSWNGRFKLSIVGLLTIIPAWNGMIILKILNPNGYLLLLIVILVAATDVGAYFMGKSFGRRKLAEELSPNKTWEGVLGGSAACILATILLMPLANVLIPEADGISSLSSLLLVLSIIFFSIIGDLLESMLKRNQGIKDSGDLLPGHGGILDRIDGLLAAVPCFTLILFMITR | Pathway: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 3/3.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphate + CTP + H(+) = a CDP-1,2-diacyl-sn-glycerol + diphosphate
EC: 2.7.7.41
Subcellular Location: Membrane
Sequence Length: 287
Sequence Mass (... |
A0A2D4TTQ8 | MKIEKIRSLEVLDSRGRPTLCTKIHLDDGSVGTALVPSGASTGKLEAHELRDNDVSRYKGLGTLKAALNAESTLSALQEISPDNQLAIDERLIEIDGTENKSMIGANAILSVSXACARAAASSLNTPLYEXLNIIYRNISGKSSXMSIPIPMLNILNGGCHANNDVDIQEFMIIPSSKFSFKEGLAKSVEVYMNLKKHLADEGHSISVGDEGGFAPNLGQSKEVLETIISSIENTGLRYLDDMSIALDCAASELYKDNYYYLEGENKKLXSNEMVEYMSDLAQNXXIKSIEDPFDEADWNSWKSFTSXNNLQIVGDDIFV... | Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5.
Function: Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.
Catalytic Activity: (2R)-2-phosphoglycerate = H2O + phos... |
A0A8T7AEI1 | MNTNTEKAQLSTKACFWFIGFSLLLVVLDQWTKFEIVQRFEYGERLVVTSYFDLYYLRNYGAAFSFLSDAGGWQKPFFISLSAIVCTGIIIWFFRFAKKDQKILALALSLVMAGALGNVIDRINYGYVVDFLSFHYQPFGQIPLLKFLFPNGRYPAFNVADMAIFCGAIFLLIDWWQEVKKEKALAAMKPSVPDES | Pathway: Protein modification; lipoprotein biosynthesis (signal peptide cleavage).
Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, ... |
A0A972LRG2 | MSGNSAKLRTDWLPKILPFYCLEITLEFTESTRLPFFHRGQLTGFIRTLIDARGVSYAGKLLVESAEDGRVFYRSGERYRFGITAFEPGLPLLRVLIQKLEGLPASAQRDKRRNDPFRGNLRLVSIRDRLATGDDFDPERFISYDGERFQHELNLWQAYIHEHPLVWRWTSPLRMLLPAAVREQRESTDGKPRYCSNPGDLDADFLLHRNVEALRALIQHHGHEEPKPTPKAAACNFSECRVFWVEDSYKSGARWKHLSGLLGELQFPPLPDLSTFHIGCLVLGQHLGMGEQPAFGLGRYRLETVDGETANAVPLLRPAA... | Function: CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target... |
A0A9D8A3I3 | MSIPDQTFTKVSYFKISAAQEGQRIDNFLLKTYKTVPKSKIYKIIRKGEVRVNKGRIKPEYKLKIEDTVRLPPIAVSNKDNTPVFIPKDVLDTMEKSIVFENDHFFVLNKPYGLAVHSGTGLSYGVVDVLKRLRPNQMVELVHRLDRDTSGCLMFAKSRKALVMLQNMLKQSQINKTYIAMVVGQWPAKQKVLDFPLKKYLMQNGEKRVRVEKGGQMALTKVLKVQANKKFSLLTLRLITGRTHQIRVHCQSVGHSIINDDKYGNREDDKQLKKYGFNRMMLHAKTLNIESNELCEAVEISAPVPEVFNKKL | Function: Responsible for synthesis of pseudouridine from uracil.
EC: 5.4.99.-
Catalytic Activity: a uridine in RNA = a pseudouridine in RNA
Sequence Length: 312
Sequence Mass (Da): 35794
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A0A7C5N4X7 | MPCRGCWPCWMPGTCPVTAESQGGRLFFALWPDGVLRRQLEIQVRRLPRRLGRPVPLENLHITLLFLGQVPATRLGCVLAAPEEVAAASFELTLDYVGHWPRPRVLWVGPRHTPPALFRLVGALRRALAPCGLDLDRRPYQAHMTVLRKVARAPERQVEIEPVTWQVSSYSLMESIPGEGGVAYRELRRWPLTGDG | 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: 196
Sequence Mass (Da): 22074
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I4ANX2 | MRVIISGGGTGGHIYPGIAIADALKEINQNTEILFVGAEGKMEMEKVPKAGYHVIGLPIRGLQRSFSPKNILENLKFPVRLFGSLNQARKVIKDFKPNVVVGTGGYASGAVLQVATTMSIPTLIQEQNGHAGLTNKILSRQVDAICVAYPNMESYFPKQKIQFTGNPVRSDLKNLPNPVQSDFDYFNLTQSKKTILVMGGSGGAKIINESILNGIETILENDFQIIWQTGKFYIDSIKEKLAQKNLSNHPHIFVSDFIHDMKKAYQCADIVVGRAGALTISELTLAEKPAILIPSPNVAEDHQTKNAMALAKEDAAMLIK... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II).
Catalytic Activity: di-t... |
A0A534CG05 | MMRHIELLPEPLPSEPLVIVERWLAEAWQHRHQPNPNSLVLATSDRAGRPSARVVLCKEIVPQPGYLVFYTNYRSQKGRQLAENPRAAAVMHWDALHRQVRIEGPVAQAPAADSDAYFASRPWQSQIAAWASAQSEPVASRAALEEAVAAAAERFGAPPPRHPGADIDPRIVIPRPPDWGGYRLWAEAIELWVEGEGRVHDRARWTRALTAQPDGLFEAGPWTAARLQP | Cofactor: Binds 1 FMN per subunit.
Pathway: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate: step 1/1.
Function: Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).
EC: 1.4.3.5
Ca... |
A0A0X3NGE8 | MVVPVATTILSGGVETISGQSLSSLIKKTPGSKKSRSAKITPMDNGPDNSYIFNFAENTEAFEGTDEWSVGTTLRCFNNDKKIQETFGVLILESEIQAFERIARRHFLKTRQRYIPEPWIPIQWAVRLVQKAGMHANIADPKIIHDVLKEIGKFRQQLQNLQVYSSLTMPLVYTQVAVIAVYSYFICQILGSQYVERNETVGLSSKSTALPVPVFGVFYFLFLMGWLKVALCVMNPFGDDYEDFECSEILDYNLDVSCRAVLLDEATFPDSLKKATFATTPMAGAENDNLHEFIEKTTEEIQAARSNEEINDIKNLEIRQ... | Function: Forms chloride channels.
Subcellular Location: Cell membrane
Sequence Length: 355
Sequence Mass (Da): 40473
Location Topology: Multi-pass membrane protein
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A0A967SJ84 | LNHIYFGGGARGIEAAARYYFDTRAAELELHEAALLAALPKAPAHYDPHQAPEAARRRRDLVLALMARQARVDSAAAAEARDRDLGVVTDAERDRDGDVIAPYFVQHVRRFLEDSLGERLYETPLRIYTTLDPEAQAAAEEELDLQLERVEQNWYGRYRGARFGDAEAVAAEETEYVQGAVVVLDARTGGVRAWVGGRDFDHSRYDRAKLARRQAGSAFKPFVYAAALEQGLVASQIILDAPYRVPRRGVPDWEPENYSGDYEGRMSMRDALVRSQNIPAVRLAAATGERQVADLARRAGIRGEVPESPVLALGVTAVSP... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
EC: 2.4.1.129
Catalytic Activity: [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate = [... |
A0A920V861 | MSGKTKYIVAYFVILAGESSGDNIGSSIIHELKKSNPNHEFKGIAGPKMIEAGCKPWFDIKDLSVMGIVNVLKHIPRLLKIRKRFEEDP | 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... |
A0A967SQ41 | LVAGGPLVMEALRRGGGELIPVDSEHSAILQCLRRFDDRSAQRLILTASGGAFRTWSATALVDARPEDALQHPTWDMGAKITVDSATLANKALEVIEAHFLFGMAYDRIEVVVHPQSIIHSMVEYVDGSVLAQLGFPNMELPILYALTHPDRVPDDGTRPFDPLAAA | Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 1/6.
EC: 1.1.1.267
Catalytic Activity: 2-C-methyl-D-erythritol 4-phosphate + NADP(+) = 1-deoxy-D-xylulose 5-phosphate + H(+) + NADPH
Sequence Length: 167
Sequence Mas... |
A0A967S984 | LRLGRLLPAMLAFHLTRPHPQAVREALDHGALLRTGVDEINAFVRSAGAEVVAVSEAPVPLAEAADSRFILFREGSGLQEHVAILVGEEADWPDPVPVRLHSACLTGDLFGSLRCDCGEQLRGSMRLFAARGGGVLLYLAQEGRGIGLRNKFRAYTLQEGGLDTIDADSALGFGPDERRYDVAVRILEMLGVERIELLTNNPEKVRAMEDAGITVVRRRPLHGTLNRHNLPYVRAKVQRAGHWLGDMLSQDLSGD | Cofactor: Binds 1 zinc ion per subunit.
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 1/4.
Function: Catalyzes the conversion of GTP to 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate.
EC: 3.5.4.25
Catalytic Activity... |
A0A554JLD8 | MLNKVNVLKNYSRYHFLIFGMTPVEQIKSRLSVVDVVSSYLKLVRAGSNFKAVCPFHSEKSPSFFVSPARDVWHCFGCGVGGDQFRFVMQIEGVDFREALRILADRAGVELVAQNPQERNERARLFALLELATRFYQQELKRHPEVEAYLTKRGVSDESIQKFQLGYAPPEASGWRAFTEHALKNGYKLEELEKAGLSIRKQASSFKFQVSGYYDRFRNRIMFPITDASSHVVGFGGRIFSAEGGPASDGDASMETVAKYINTPQTPLYDKSAVLYAFDKAKVAIRKENSCVVVEGYMDALMAHQAGTEHVVAVSGTALT... | Cofactor: Binds 1 zinc ion per monomer.
Function: RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.
EC: 2.7.7.101
Catalytic Activity: ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.
Sequence Length: 617
Domain: Contains an N-termi... |
A0A7T5RMA2 | MVAIATGLGKNGLQEWVIQRVTAVILSFYCVFIFIFFLFNKDINYENFSMFFDNIFVKIFTLISILSLSAHTWIGLWTIITDYIKNFYLRIFIQIVVNLLLMSYVFVGIEILWRT | Cofactor: The heme is bound between the two transmembrane subunits.
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle.
Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH).
Subcellular Location: Cell inner membrane
Sequence Length: 115
Sequence Mass (Da): 13582
Location Topology: Multi-pass me... |
A0A8T3RZG1 | MFRILDRYIFREVLATWFVVASVLLFVLLTNQFARVLGQAAADKLPKEAVFTMLWLTSVQYLT | 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: Membrane
Sequence Length: 63
Sequence Mass (Da): 7326
Location Topology: Multi-pass membrane protein
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A0A8T7I3W1 | MQLIDFYPLIIVLLIAAVVFLLITFIFNRRISNNSSVKYYRQLTYNLYLVILLIAVIAASPIESELKGQILSLIGIVISGAIALSSTTLLGNTLAGVLLKVTKSFRSGDFISVNDYTGKVASRSLLNIEIQTFDRGLIFLPNVYLIQNPMKVFPKSGLFISVEVSLGYDVQRTKVEKALLSAAEKLGIENAYVEIKGLLDFSVQYALHALVTNLESYMSIKSKLHAMVIDELHHSDIEIVSPNFMNTRALSDTPVIPESIEEKTELEKALDENIDAIIFDKANHADKLEVLQQKKERVLKLLSKESDDSSRAERLRYKLE... | 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... |
A0A1X6PB27 | MDQPSLFLCARSPTASTAGRIFALDGPAPASSEHLRAYLLRPRTLYLRIFYNEADAHVWVANDTLHTTDEEVVLEEPHALTIDSAQAALPLQEALLRTFAAGASPALVDLSNVESTAAFFRALGGSTSDDGVRVVGVPRHTTLSNVIDVDQLQVQARSLDASNGTKRHRASLVRNDAGSDGRARPKLSTKTWGEALCRRVAVRRSVVVQAAEQTPSSVPAWNGQAGGSSSSLPLPRRRHSRASAGCNSAAPVRHRVAWSYGGPGGWRGNDEQLEVAHLPPLRLSDTLGGAALKVCRLLARSTSVFLSGPPGCGKTYLVKE... | Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
EC: 3.6.4.12
Subcellular Location: Plastid
Sequence Length: 711
Sequence Mass (Da): 76413
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A0A833IT55 | MVEPLQPTALPPRPTDTATPVLVLGPDVSPPPSWDSHATALPLRRIRLSKAEDTRHALAQLPHCPGIAGAPLVLLAAEPELLARARALGYALVVGLAGRHARSTLLKAGADLVLRRIEELDPHHLPTRQLPSAFAAIHTLRAELKSATPRLFLDYDGTLTPIVDQPAQARLTEHQRAILRSVSARAKIALVSGRDLADLRRRVALPELIQVGSHGYEALEPAGGHWVHPDAGPATRALAELERVLRFQLPQWPGCVAERKAYGLAIHYRHLPEHRVGALEQWLLGLAGRWPALRPRDGKKVLEFVPDLAWDKARAVKRLL... | 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: 398
Sequence Mass (Da): 43628
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A0A1X6NPU6 | MADAFDDDDFFKDYPPTTAGAAAPSDAGASAPVVGVPDDADVFAMPPPPPPEEEAGGGDGGGDAAAAGGGGGGGDANNPFGDAADFLGVGGGGGGGLATGDASAEGGSSGALGGAAFVMGGDGAAMNGGANGDDAGGEDDGEEELPPRPSTPTAVSNWRREHAARLEERAAREATVVAERRAAATEALTSLHTKWGDRCTRNAEGNKEFEANFLRERDGLIAQFSKPGEPPAWHVVPSLVDMSGKYKEGARDTSRMRSVLMKMKTK | Function: Clathrin is the major protein of the polyhedral coat of coated pits and vesicles.
Subcellular Location: Cytoplasmic vesicle membrane
Sequence Length: 266
Sequence Mass (Da): 26693
Location Topology: Peripheral membrane protein
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A0A920LYD6 | MKRKTLKGVIEISQVEFKDNRGSFIENFNSKKFKALVRKDINFVQDNLSTSKKGVFRGLHFQHKFPQAKLVSVISGEILDIVVDLRKFSKSFGDWAAFKISSKNKKQIFIPEGFAHGFLSLSDETKVFYKVSDFGIQKTNTHLDLTIKNKYKITFSSKKYFQKG | Pathway: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
Function: Catalyzes the epimerization of the C3' and C5'positions of dTDP-6-deoxy-D-xylo-4-hexulose, forming dTDP-6-deoxy-L-lyxo-4-hexulose.
EC: 5.1.3.13
Catalytic Activity: dTDP-4-dehydro-6-deoxy-alpha-D-glucose = dTDP-4-dehydro-beta-L-rhamnose
Sequence... |
A0A661EMB1 | MAGAAIIAGSAALRAGSGLVSLAVHPSNAAAVVNARPEMMVHGVQGADDLTPLLERADVVAIGPGLGQKSWAQQLWQALEPFKGPMVVDADGLNLLAQSPAQRHNWVLTPHTGEAGRLLSSSVEEIERNRFVAVSALHQKYSGTVVLKGAGTLIQSNETLPTVIDGGNPGMASGGMGDALTGIIGAFLAQGLDTEDAATLGVAAHAWAGDRVASEHGERGMLASDLINDLPETINGTQRFMKSPKSASGKLEYLLSKPEENGSAHSIFSR | Function: Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S- and R-forms, the enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or ... |
A0A2E5VAM3 | MKEKAMYPGSFDPFTKGHEDIVRRISNFFSEVIISVVDKPNKKILFSTKERVEMIESIFDDLPKIKVISYKGLTASFAKNNNISVMIRGIRSISDYEYEYDLAALNKQIAPNIETIFLSTSEKYKSISSSHVKELALLDGDVSKFLHPTVASKLVEKLGQINEN | Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 4/5.
Function: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
Catalytic Activity: (R)-4'-phosphopantetheine + ATP + H(+) = 3'-dephospho-CoA + diphosphate
... |
A0A349SJI5 | VPIIAPILLSDPSANITAVWLGVMIGINIQTSFLTPPFGFALFYLRGVASAVVRTIEIYKGAVPFILLQLVGLAIAGYYPSLVNYLPNRIHLTSETAPPPMNPQLQECLEEYVFTYYDSEGETLLAGVSRAKGLDVSYLPESQQKALLAGFESVMGVSMLVGDVIAARDALDAYIPEYRSLHREVRGVQRRARLSDKRLEELERRIRNWSVEYDGPESEKVKFESEFAVLNEERNTQLSQVPASWQGARDGFVERAKVLKKARVRYRQSVDSAYESVVKLQSLIADADNLAELDKELTNLKRTVQDSSPEAAMAAIKAAE... | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 423
Sequence Mass (Da): 47254
Location Topology: Multi-pass membrane protein
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A0A520TWT6 | MDFVNIILLSLIQGITEFLPISSSAHLIIFSEIINNSNQDITVDVFAHFGTLLAVIWYFREDLIKILRTYKISEVNNLGNCLIIGTLPILFFGFFLRDIIEVNLRNQNVIVFSMIFFGILLLIFEYLRGNRNLEDLTWKDSIILGLFQTFAMIPGASRSALVIMGAFYLGFRSIDALKISFLFATPTLALIFLGENYLINFEYKINILELLLVVFFSFLTACITIHFFLKLVNKIGLLPFVIYRFLLAGILVFT | Function: Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
Catalytic Activity: di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate
EC: 3.6.1.27
Subcellular Location: Cell membrane
Sequence Length: 254
Sequence... |
A0A8T3Q7J2 | MIISEDLQLAIDYLAQDEIIAYPTEGVYGLGCTAFNEETVLRLLQLKNRDVRKGLILIASHWNQIEDLIEPLSNLQHQTVNRTWPGPITWVFPASRKAPEWIRGEHNTIAIRFSNHPLAQALCEGFQKPIVSTSANLTGSTPARNYKEVAIYFNDKIPFILKGEVGGLNKTTSIRDVITGLVIRE | 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... |
A0A2E2ZG30 | MELSVIELFLNASLVVKAVILILILASISSWMLIFERWLYINRVTQEFHDFEEQFWSDSGLESLLIASQEDDHKSIGAEYIFQVGYLDYKRLSKEVDADTVMMSVQRNMRAALSREQSLLEKNLPYLATIASVSPYIGLFGTVWGIMNSFRGLAGATQATLSAVAPGISEALIATAIGLFAAIPALIAYNKFISESDGLSANFDGFKEEFSAVLERDLKSNQS | Function: Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity.
Subcellular Location: Cell inner membrane
Sequence Length: 223
Sequence Mass (Da): 24709
Location Topology: Multi-pass membrane protein
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A0A8S4C1U5 | MLFLRNQPCIKFAFDYKLLLWVCIIVWTTDIAAYFVGITAGGPKILPKVSPSKTWSGFCGALVFSVLSHEIAIRTVVTELFNPKINILIAWSVVILTSLISQVGDFAESAFKRYFQVKDSSHIIPGHGGVMDRMDGLIMVCIIWFIVFILSIIFNF | Pathway: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 3/3.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphate + CTP + H(+) = a CDP-1,2-diacyl-sn-glycerol + diphosphate
EC: 2.7.7.41
Subcellular Location: Membrane
Sequence Length: 156
Sequence Mass (... |
A0A3C0T950 | MSSLPTFKQTCTDPIYFLALGFGSGLSPKAPGTCGSLVALIIYVPLSLLPVFAYLAYILLAFMLGVYICGVAANRLDVKDPGAIVWDEFVGMWIALIIAPEGWSYLVLAFLLFRLFDIFKPWPVDYLDRNIEGGLGVMMDDVAAGIYALAVLQIIALGMRELGLVLL | Pathway: Phospholipid metabolism; phosphatidylglycerol biosynthesis; phosphatidylglycerol from CDP-diacylglycerol: step 2/2.
Function: Lipid phosphatase which dephosphorylates phosphatidylglycerophosphate (PGP) to phosphatidylglycerol (PG).
Catalytic Activity: 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycero-3'-phosphate... |
A0A349X5Z6 | MTSMLTIALSKGRILKQTIPLLKAVGIELLDDPFESRKLIFATNQKDVQAVVIRSTDVPTYVQFGAADLGIVGKDGLMEHGGEGLCELLDLKISRCRLMTARPNNSPELNNSPEPNNSPEPNNSPQLTTKKRIRVATKYPKLAREYYQSKGVQAEIIKLYGAMELAPLVGLADEIVDLVETGSTLKANNLSPHELVADVSCRLIANAASMRTQHTMIQEFTAALGKAIETNKA | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
Function: Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosyn... |
A0A3M1V6Z5 | DPARPIDGLDDSKRLTERRREQLFDEICERALAWSLGRAEVAEIDRLNILWASLLAMRRAVEGLNPAARHALVDGNRIPPEMPCSAEAIVGGDASEPAIAAASILAKVSRDREMVALDARYPGYGLARHKGYPTRQHIEALAALGVSEIHRRSFAPVRRLLG | Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
EC: 3.1.26.4
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Length: 162
Sequence Mass (Da): 17809
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A0A2E1Q781 | MSLKISKSSIRILGLDPGSHITGVGVVDVQGSQLIHQHHQVIRAPKATLEKRLIYLFEALKDLSHSYQPDVVVVERVFLGKNVDSAFKLGHARGVALMALYQGGGQIFEISAREVKKILTGSGSASKEQVRQMVGQWLKIDFQDKEMDVSDALSLAISGSFEYEKRLRLKQLEGEL | Cofactor: Binds 2 Mg(2+) ion per subunit.
Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair. Endonuclease that resolves HJ intermediates. Cleaves cruciform DNA by making single-stranded nicks across the HJ at symmetrical positions within the homologous... |
A0A7C3D7T8 | MATYLIIMGAPGAGKGTQAKLLQKRLAIPQVSTGDLFRYSLKNDTELGQLAKGYMEKGELVPDSVTVAMVKDRLSQDDAASGAILDGFPRSP | Catalytic Activity: AMP + ATP = 2 ADP
EC: 2.7.4.3
Subcellular Location: Cytoplasm
Sequence Length: 92
Sequence Mass (Da): 9784
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A0A965TAR8 | MSAIQNIWTMFTDYLGYLGDNGDMVMFLAVAAIGITAALFVVTDKEAMHSAFYLALVFVVVAVVFLFLEAEFMAIIQLFVYVGAITILFAFSIMLTRRYIMRPGGGNDDE | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy i... |
A0A520TRX1 | MFMNLYSAKEVRKLDSLIIKNQKISAFQLMQKAAEFSFNVLLNHWPNTKRIYVFSGSGKNSGDGYLLAKIAKEHGLESFIITTAKPKVSAGITNKAYKLALKAKVKTISMQSFKKESLKDSVIVDSLIGTGLKGKVRKSISNLINEINAKKKFSSVLSIDIPSGICADTGSALDSYVEADVTATFIGRKKGCFTSTGKAASGIIEFNDLGASYKLKNKIKPNTYKLDMEKGVKKLKTRKEDSHKGNFGHTLVIGGDRGFGGAAILASKAAVYSGAGLVSLATRPVHLEAALSSCPEVMVNGVESGQEVEELLTKASVVVL... | Cofactor: Binds 1 potassium ion per subunit.
Function: Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that... |
A0A9K3DCV8 | GLVFNPSVSWVAFHSISLSLSLSPSLSLSLTPSGLVFNPSVSWVAFHSIYDFGYMAKVILNGSLPNTEADFNEMVGRVFPHIYDIKYIMTTAYEWKGGLQKLAN | Catalytic Activity: Exonucleolytic cleavage of poly(A) to 5'-AMP.
EC: 3.1.13.4
Subcellular Location: Nucleus
Sequence Length: 104
Sequence Mass (Da): 11490
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A0A520U3N6 | MSLSLSENNFNLQKIADLLDGKINGDEKQEVKSLLPLDLAGKEDISFFYNKKFIDKLKTTKAKAVILEKEFEDLFHSNSIVVKDAHIAYAKLTQIFKDQIKKVGVNPSAVVESKNIDPSSYIGPNVIIEKGAVVGKNVKILGGVFVGSETKIEDDTLIYPNVSLYSKTKIGKKCIIHSNSVLGSDGLGFANKDDKWEKIEHLGIVNIKDEVEIGAGCTIDKSSTGETLINSGVKLDNQVHIAHNCVIGENSIIGAKTAIAGTTIVGKRCKIGGGCGIIDNIEICDDVTVTPMSFVTKSISSEGMYSGGSMLMEHKNWLKY... | 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.... |
A0A6N8VJK1 | MATEAHRPAKHCTDTMNDESNKIIKTRWLYTAQQSRDIDRMLIEQTPVSGYELMQSAGCACFSRLIKQWHQAHNIVVFAGSGNNGGDGYVIARLLRLAERNVKVCQLGDANHIKGEALEARTAYLQAGGEIISLDESIKADLFVDAIFGSGLNRDLSEEACRWIDYINTQATAVLAVDIPSGLDADRGCARPIAVKADITVSFITRKQGMYTAAGKDYCGRIFFEALQDIDDIALQFKPTYRLLNHTEALQCLPPRRCDTHKKNFGHVLVAGGNHGMAGAVCLAAKAALHSGAGLVSVLTQTQHITTVTAVCPPLMVHDA... | Cofactor: Binds 1 potassium ion per subunit.
Function: Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that... |
A0A8T6HMK6 | MSLDAEIHSSAELGFDRSAVSPESLEVVRTLKSLGYDGFLVGGCVRDLIMGLKPKDFDVATDALPAEVQDIFSRSRIIGRRFKIVHVVSRRGRFRHVVEVTTYRAASESPNGRAFSRSDHTGRILADNVYGTREEDVMRRDFTLNALYYDPLEEEVIDYLGGIRDIRRRQLRMIGDPDRRFAEDPVRMIRAVRFQARLGFELQDEIESSIRNRFRCLEDIHTSRLYDEVIKLFHQGSAEDAWDRLFETPLGKMLFPHVASPVRHGQPDSCPAFVRGALRNTDNRVRAGMPVIDSFFVAVVFWDEYRKALGRQRAERMAKH... | Function: Adds poly(A) tail to the 3' end of many RNAs, which usually targets these RNAs for decay. Plays a significant role in the global control of gene expression, through influencing the rate of transcript degradation, and in the general RNA quality control.
EC: 2.7.7.19
Catalytic Activity: ATP + RNA(n) = diphospha... |
A0A2D7EWW1 | MSKKVVDPDYEIEALKYAKPIPSRRFILTVIVDHNEPIAFKRLAKELQLDSTDLRQALKSRLRAMVREGQLVVDGRNAFAAPSKTELIRGRVVGHANGSGTLIPDQGKENIFLSPREMQSAFDGDIAEARILRRDRRGRSQGHLVEVVQQNTKTVLGRLYRDNLIWMLDSVNPRITQKILVDETGLEQEGLIVYATITKQPDFEVMATCQIKEVLGHQLSTEVKIAESLRNSAIPRTFSETALSDAANLELQSFNTEFREDLRAYPFITIDGEDAKDFDDAIYCEQSPDEGWRLLVAIADVAHYVTEGSSLDKNAFERGT... | Function: 3'-5' exoribonuclease that releases 5'-nucleoside monophosphates and is involved in maturation of structured RNAs.
Catalytic Activity: Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.
EC: 3.1.13.1
Subcellular Location: Cytoplasm
Sequence Length: 746
Sequence Mass (Da): 842... |
A0A8T6K536 | MTPREGVEGRARDGDALALARLLVAVPSVNPRIEASGSGEAEIAACAAGLLEGWGFDVSLTEPEAGRPNVVGRIGDGARSLMFNGHLDTVGVEGMTIDPFGAQVREGRLWGRGSCDMKGGVAALLSAAAALARRGVPGELIVALTADEEHASTGMAGLTQTGARADAAVVCEPTGLAVMPAHKGFVWVEAAFAGRAAHGSRPDQGVDAILHAAEFLVATAEYEESLFERAPHPLLGWGSIHAGTISGGAAPSVYPEHCEVVVERRTLPHESPEAVMQELAAVVAGLGEEARSGAALRMTLERPGTEVPEASPLVQGLLGA... | Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): step 3/3.
EC: 3.5.1.18
Catalytic Activity: H2O + N-succinyl-(2S,6S)-2,6-diaminoheptanedioate = (2S,6S)-2,6-diaminoheptanedioate + succinate
Sequence Length: 576
Sequence M... |
A0A6L8FG26 | MAADSPLFPAACRVSVAPMMQRTDRHCRYFHRLLAPEAGLYTEMVHAQAVVHSTDGRFLHHHPAERPLALQLGGSEPETLAEATALATQAGIDEINLNVGCPSSRVKAGRFGACLMHEPERVADCVRAMRGEAAGRPVTVKTRIGTNHRQEFSHLLAFARAMQEAGVAALIVHARIAVLEGLSPKENRNVPPLRYEFVYRLKQAMPELPIVINGGICDNSEIASHLQCVDGVMLGRAAYSNPWLLTALSGAPRQPKTRAGVVEAMVEYARREEQSGVRLGAITRHMAGLYSGRPGAGDWRRSLARHAAAPANEASVLLDC... | Function: Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines. Specifically modifies U20 and U20a in tRNAs.
EC: 1.3.1.91
Catalytic Activity: 5,6-dihydrouridine(20) in tRNA + NAD(+) = H(+) + NADH + uridine(20)... |
A0A356K849 | MKANVCWANSMLWQIATSWSPLAEEHFNLTTMTDVFVGIGSNVDPDAHIGSALTDLRERFGAIELSTAYRNPAVGFEGDDFVNLVVRFRTVMQLSEVLGVLHEIEIRRGKDLAAPRLASKTIDLDLLLFGDLVIENDHLVLPRPETTTAKHYLRPLSELEPDRLHPVTGGTFAELWSQLEDGTGLLTAHPLAWSPVSARTIVRPELRVDDLRLAVHLGVPDSERENLQEVSISIAVTFPNVPDACSTDEIDGTIDYGVMCRRVTALVGSRAFRTIEHLAGSCLDELSEMLTESGSELTLEVRKCHPPIPDLHGGTAFIMR... | 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 ... |
A0A924V4X1 | MKKASIIFLILVGIQICAFGAESAHGGAHGEDAIPTKTIMYQAINLGILLIVLFFAVRKTVVALFKARYVDYSSQAAKTEAANRQAQEALSDIKNRINQLQTSEQTAILNAQSDALALKNKMIQETQSQAEKLKADTKLIVAAELNNAKNEIRKEIINASIEIAKGQIKNSAADITKKSEQSFLSDLAKTKQVIL | Function: Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).
Subcellular Location: Cell membrane
Sequence Length: 195
Sequence Mass (Da): 21243
Location Topology: Single-pass membrane protein
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A0A9D1PVH6 | MHTIGTKNDICLYGGSFDPVHIGHLNIIHELERLSGIRKLVVIPAYCSNFKQTSHPAEFQKRIEMLTLALSDYRKYYPDSEMEITISDIEGKRKGISYTSDTVRYFLDAYSLNHIYFLIGDDLAADLGKWHDFDFLKEHVTFICLSRYEIESEDSKWIIRVKSRTVDASSSEVRKGNALLLSPLVREYVMKNNLYMTDSDEYRKTIKKEMKETRYLHTLGVEKMALSLARRFALDEKKASLSALHHDRYRYIEKEKAVRELDEASFPIFDEERENDVLLHAPYASLKMSADIPFSSSDMHKAVRYHTLGSSNMGRLGAAI... | 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... |
A0A3D0ZX38 | DDAYLTVADENIQARLRDVYLMHFSNAFGAIPLSTGNKTEAGCGYYTHFDMNFSYAPIKDLYKFQVMDIAKEDPKIPAHIWKKPPSAELSHGQTDEGSLLPYAVLDPIVMAYVEDYVTTFERFCEWIPEQRNTKISGDEKTLSTWLTKDGSEQDYRRIVSLIGKMEYKRRQACPGTKVSKVAFGTGRRIPIVEKWS | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis.
EC: 6.3.1.5
Catalytic Activity: ATP + deamido-NAD(+) + NH4(+) = AMP + diphosphate + H(+) + NAD(+)
Sequence Length: 196
Sequence Mass (Da): 22389
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A0A9K3GI90 | MEAFQNQLISMENRTGVRTTWNVFPNARSDLLRNGVPLGLVYSPLKDIEGIPQLQYSPVKCKRCHSVLNPFSFIDFDQKRFICPFCQQQNALPPNYGDISPQNLPAEVIQSFGSVEYISPAPHQSQESSPAAPAFMFVLDACMPDKEFEAAKEQLLWALSVLPEHTIVGLIVYGTTVQVYELRFEVCPRSYVFRGLKEIPSNQVEEGLGLRNRDLQRQNILRTIGEVELTLPAIVEGLRPDPWDVKDDKRPYRCTGVALSLAVSILGRLLPGVGSRVVLLTSGPCTLGPGQTASIELAEHMRHHSDMEDGDHKMMVSFLG... | Function: Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules.
Subcellular Location: Cyt... |
A0A6P1MCL5 | MAVVMVVLNMFQQQQTEDSRIDYNPTFLQYVKSGKIIQCEIVRGASGNDHVTGELTEIDPSTGKPKAFYVDVVITEDLFKMLQANEVKFKVTPPSTFWPVFWNVAPFFIGFIIIYFFIFRQMRTAGGRAMSFGKSRAKLMKKDDENKITFANVAGVEEAKEELQEVVEFLKNPKQFQRLGGKMPKGVLLAGSPGTGKTLIAKAVAGEADVPFFTISGSDFVEMFVGVGASRVRDMFEQGRKNAPCIIFVDEIDAVGRSRFTGIGGGHDEREQTLNALLVEMDGFDTAEGIIIIAATNRPDVLDPALMRPGRFDRQVFIDL... | 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: 645
Sequence Mass (Da): 71582
Locat... |
A0A975GEW9 | MEIRRSFIAGNWKMFKTVSEAVETAARLLKLVKDAEAEVMIAPPFTAISAVNDVIKGSQVSLGAQNLFWESKGAYTGEISPEMLYSAGCRYVIIGHSERRQYFGETDEGVNKKIRAAINAGLMPVLCVGETESERESKKHFLYLTNR | Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Catalytic Activity: D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate
EC: 5.3.1.1
Subcellular Location: Cytoplasm
Sequence Length: 147
Sequence Mass (Da): 16366
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A0A2E9KRA8 | MNIFIVGPMGSGKTTVGKILANELFLDFYDTDAMIEEKTGVSIDWIFDIEGEEGFRKRETEVLKEMVASNSIVLATGGGIVITEENRELLASRGTVFYLHTPLKTQIERTSKDKDRPLLKNQDPAKILSELQESRLSFYEKVADYIIETENKSGPEVANEIIKLTKNYG | 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... |
A0A933Y7Z9 | MIDHQQLEDLIRSLSQSLPDGAQQFRRDIENNLQAVLSQFFARLDLVTREELEVQKEVLARTRQRLEQLEQQLARLEQSLTDHQP | Pathway: Cofactor biosynthesis; ubiquinone biosynthesis.
Function: Required for efficient ubiquinone (coenzyme Q) biosynthesis. UbiK is probably an accessory factor of Ubi enzymes and facilitates ubiquinone biosynthesis by acting as an assembly factor, a targeting factor, or both.
Subcellular Location: Cytoplasm
Sequen... |
A0A2G6L339 | MARKFFGIGLVWLCFLVARYTFYRFIRLLTSGTGLSRLFDWRYGCDCVCYSCPLYGSGGNKVTEEILVLSPLAQIREALFTDNLTLVRDTINALHPAEIARILESLPPSEREQVWHVVDGDFHADVLANLGEDALEVVIDDTSDERLISAAQDMDDDDLVDFLQDLPADVAIRLLQSLDSAQRQHLSKMLEYDDDTAGGMMATDTITVRKDVTVRTVIRYLRRLDELPDITSKVFVVDRNANLQGELALSRLLTATRGAKIGEVMPKEYTVFHVNDLGHDVVQRFRESDLVSAPVVNDNNQLVGRITVDDVIDFMQEEYE... | Function: Acts as a magnesium transporter.
Subcellular Location: Cell membrane
Sequence Length: 509
Sequence Mass (Da): 55662
Location Topology: Multi-pass membrane protein
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A0A8T7DYR0 | MSRMITAGIAAMLGLLATMPSAAAPATATDGDIETFRSDLQAMKAAQRGPFRRIRWFCKDGSVLPPEPYACKEHGGGTQHGEWSVETLALRDAGYAIATFYTDLDIDGFVPARVASAEFAQMLIEQYLIRADDGWILRRAQFYRGAYQEEGERAGSRKLLLRMVADDELLSRRYLQLRIAASLLRHGKETNLVSRIRQEASSLAVADSAFTPLRNRIHARLSPKDAAAVRDYAAGRSDESDRAALEALAAMIDQAFGAESARTLASLLRVLEPYPQVTEEVGRLQPLLAEDSTASQRFTATASLLQIIREQIGNLRRASE... | Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Function: Catalyzes the phosphorylation of pyruvate to phosphoenolpyruvate.
EC: 2.7.9.2
Catalytic Activity: ATP + H2O + pyruvate = AMP + 2 H(+) + phosphate + phosphoenolpyruvate
Sequence Length: 978
Sequence Mass (Da): 106492
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A0A920RZ66 | MKKLFIVANWKMNGNKKSNRQLIKYINKKVSDNSNIEVVICPPFIYLNQILELKRSSIKVGAQNISENQNGAFTGEVSGSMLLDMDINYVIVGHSERRQIYNDTNDVVARKFELAHKNNLTPILCVGETLNERKTRQTLSIVESQIKSVIESTQLELLAKSIIAYEPVWAIGTGETASPEQAEEVHFNIRNIIEEYDPNIATSIPILYGGSVNGANSKDLFTMGNINGGLIGGASLNEEEFLEIYQQTESLINE | Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Function: Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
Catalytic Activity: D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate
EC: 5.3.1.1
Subcellular Lo... |
A0A3C1N8U6 | MIKPYQSDQLQPRYVDDEAKRARLQVEIRKYAALTISSGAAANAVMLGAGYFTPLTGFMSKADALSVAVSLQTTEGLFWPVPILNLVRENSLEQIGRSVALCDPNIEGHPVLAIQEVDQVEELSDAEMGHIASHTFGTADPQHPGVAALLTQGRYLLSGPIRVLNYSYFEQEFSDTFRTAGQIRSEIKQRGWKRVVAFQTRNPMHRAHEELCKMAADAVAADGILIHMLLGKLKSGDIPAKVRDAAIRKMVEVYFEPNTVMIAGYGFDMLYAGPREALLHAIFRQNAGCSHFIVGRDHAGVGDYYGAFDAQSIFDDAVPL... | Pathway: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 1/3.
EC: 2.7.7.4
Catalytic Activity: ATP + H(+) + sulfate = adenosine 5'-phosphosulfate + diphosphate
Sequence Length: 395
Sequence Mass (Da): 43781
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A0A3C0YG14 | MAYYQAMQSRHAKTLSHLLFSSLVGLCSLCHAAPIDLPNLGDGASRLISPQLEQEIGSAFLKQLHASLPLVGDPILQYYVETQLADLVQYSNLRSPLQAVVIVDDEELNAFAAPGGIIGINLGLMIYARDLDEYASVMAHELAHLSQRHFARRVEAQQAASIPTLVSTIAAILVGVAGGSDAGLAALTTAQAMGQASQLRFSREREIEADRIGLNTLVRANLDPAGMARMFERMQQAYRFTRKPPEFLLTHPLSESRISDAKSQARDYEKTPPRQARPERAEDYQLMRARAESRFSQNPRNEIKTYRKARSKNVDDAAVT... | Cofactor: Binds 1 zinc ion per subunit.
Function: Functions as both a chaperone and a metalloprotease. Maintains the integrity of the outer membrane by promoting either the assembly or the elimination of outer membrane proteins, depending on their folding state.
EC: 3.4.-.-
Subcellular Location: Periplasm
Sequence Leng... |
A0A9D6WGJ9 | MSPDLRAVVACAALALLAGCQPARHVEQFRGPTMGTSYHLEVAADDAAPFPRAHLEAGIAVILATLDRGLSTYRPDSDLSRFNAARTREWVPVSADVAVVVAEAQRISALTNGAFDVTVGPLVNAWGFGPVKKPQTVPSEAEIAQAKQDIGFRKLHVRLEPPALRKDDPAMVIDLNAIGPGLAIDQLAAFLEREGHGDYLVELGGEVLSKGRKPDGSAWRIGIENPLATPRALVATAEVEGQALSTAGDYRAYFDAAGRRYSHILDPRTGRPITHALTSVSVVAPSALSANGWDTALMVMGPDEARALAEQQKLAALFVI... | Cofactor: Magnesium. Can also use manganese.
Function: Flavin transferase that catalyzes the transfer of the FMN moiety of FAD and its covalent binding to the hydroxyl group of a threonine residue in a target flavoprotein.
EC: 2.7.1.180
Catalytic Activity: FAD + L-threonyl-[protein] = AMP + FMN-L-threonyl-[protein] + H... |
A0A523LS51 | MKRIAWILVLLLTGCAAGPTRPPLFMAGDGPVYPSEAKAQGVEGYVEVRYAVTVDGVVDALEVVDAQPEGVFEEAALNAVRAWRYKPMVIKGEIQRAENVRSTLRFEIGEPERYEDL | 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... |
A0A7C1A307 | MGERRRGRARCGARGVRIDHGRARHAGRTVEPVPVTDSRGLPVILLLILGAALTGWLLMHAERGLAPSAPQRPELPDYRLSGVRLRVFDATGALHYRLRADRLVHYPTPDRSELSMPLLHWYPQPDAVPWVVRAASGEVLDAGGEVRLLGTVHIDRATHGMRRAVAILTRDLVVWPRRNLAQTAARVTLRSDGIDLSGVGMRADLKRGRVVLLSSVRGTYVQAHS | Function: Involved in the assembly of lipopolysaccharide (LPS). Required for the translocation of LPS from the inner membrane to the outer membrane. Facilitates the transfer of LPS from the inner membrane to the periplasmic protein LptA. Could be a docking site for LptA.
Subcellular Location: Cell inner membrane
Sequen... |
A0A944T7Q9 | MQLIIISGKIGAGKSTLSKCFQRKGYHYINSDMFAKELIASNDSIKKELNNQFTDLNNGNNISVNKLKQIFLSSTIAKDIINKIVHPVFFKKINMVIDHFGKDIVLELPLIETINNIKSKFKVITIEAKLNIRKERYLNRNNKDIKDFMTFNRYQKSNLYYKNNSDYVISNNDTIELLYARFNKLYNQLKK | Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
EC: 2.7.1.24
Subcellular Location: Cytoplasm
Sequence Le... |
A0A2E9FHL6 | MQNDSIFLSEVKDFFHEIHPILSAKVMEIYNSKDFFVXEKKDGSPVTQADLIVNDILIEKLTNKFPDIPILSEENTXPKEIPSLFWLIDPLDGTKEFINRSGEFTINVALVKNTQSIFGYVAAPAIDEIWLSEGQIFKERQKKSICSDSIVIVKSRSHSSKKDDLFEQFLENKGIDYSFLSVGSSLKICMLATNKADLYFRFGPTSEWDIAAANAVLEAHNGGIYDLHTKKKIIYGKADSVLNPXFFAISNRLRYNEIVKLVDEFSEKLL | Function: Converts adenosine-3',5'-bisphosphate (PAP) to AMP.
Catalytic Activity: adenosine 3',5'-bisphosphate + H2O = AMP + phosphate
EC: 3.1.3.7
Subcellular Location: Cell inner membrane
Sequence Length: 270
Sequence Mass (Da): 30649
Location Topology: Peripheral membrane protein
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A0A962UQK5 | MDPDLIRLILVILGVLLVIGIYAWDRYKRSAPPARMGRQAPQAWSDDDMDDDSADSRREPVIESQPDRVPEMTLDEDSVPVASKKVSRESRTSELDPEPVDLGEWSRPSAEGDPQFAMDLDFDVHGDNDYLHTDPALADDVERKIIVVNVVAKGTGQFAGPAIEKACADVDLVLGEMAIYHRHDQRTGKVLFSMASMVEPGSFPVPQLRTFSTPGLSIFTQLPGVRDGVEIYDAMLHAARQLASTLQGEVQDERRNKMTGQMEKHVRESIVEHRRRLKLSRSRH | 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... |
A0A962S061 | MSAHALPADHLLLARRLVDAIEAGDHSGTDELLKALNDGHFEALFKEIGKLTRELHDTFGNLATDERLVALAQEHMPDARERLNYVIAKTEEATDRTLSAVERMQPVNERIASGASALRGELDGAGDLAQLRRQVQAFLDDCEGGCATVRGGLTEVMMAQEYQDLTGQVIKRTIGLVGQVEEKLVGLVSACGAITRGAPSKVAVDPATSHGPAVRADDAVINHQDDVDELLADLGF | Function: Plays an important role in bacterial chemotaxis signal transduction pathway by accelerating the dephosphorylation of phosphorylated CheY (CheY-P).
EC: 3.1.3.-
Subcellular Location: Cytoplasm
Sequence Length: 236
Sequence Mass (Da): 25298
|
A0A963B2H1 | MPGRCREVNLASPRISGGNARASAAKLLQQLEQGRSLSALLDGGLHGITEADSALVKEFCFGVARWRPQLDALSELLLKRPLKEKDQDIRALILLGLYQLLHMRVAPHAALAETVEASRVLKKPWASGLINAVLRRFQREREPLLERIQNRPAARYAYPDWLLQRLRQAWPEDWEQIVVDSLQRPPMSLRVNLSRISRQAYAELLKQKGMEAETIPWVGSGLVLKNAVGVERLPGFRDGLVSVQDGGAQLAAGLLNPASGDAVLDSCAAPGGKSGHLLEWASSISLTTVELDPQRNNRIRENLGRLSFAAEVCQGDASQP... | Function: Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA.
Catalytic Activity: cytidine(967) in 16S rRNA + S-adenosyl-L-methionine = 5-methylcytidine(967) in 16S rRNA + H(+) + S-adenosyl-L-homocysteine
EC: 2.1.1.176
Subcellular Location: Cytoplasm
Sequence Length: 446
Sequence Mass (Da): 49556... |
A0A8T7DZE7 | MSADVDTIAAIATAPGGGAIGIVRVSGPGAAAIAKAITRRTLQPRHAHFAQFHDYGSNEIIDAGLVLLLPGPGSYSGEDMVEFQAHGSGPVLEALLAASLAAGARQARPGEFTERAFLNGRLDLAQAEAVADLIAAGSRQSARAALASLRGVFSDRVAAVNTELIAQRTLLEACLDFPDEDTGALEELAARLAQLHGELAGLRAAAGQGRVLNDGLDVAIIGAPNVGKSTLLNRLAGFDRAIVSELPGTTRDTVEQPITLDGIELRLIDTAGLRDSGNVIEQEGIRRSHAALERAALVLVVDESGAAREGNGAIATRDPE... | Cofactor: Binds 1 potassium ion per subunit.
Function: Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
EC: 3.6.-.-
Subcellular Location: Cytoplasm
Sequence Length: 452
S... |
A0A8T7IAM2 | MIISRSSVSGLKQLQLSLASQINLSKLSAGSWNSDDMCRRFPTVAGVDVGINNESGKLKASAVLFDSQTLQIKELAIFEALPTIPYIPGYLSFRELPVVLGALNKLSELPSMILCDGQGIAHPRRFGIASHLGVELDLPTIGVAKKRLVGDFVEPSNTLFASTPLQFKDETVGLVIRTRVNVKPVFVSPGHLMSVEDAGNWVCYYSRGFKLPEPTRIADQVASSRLSKKMLHELTAVGLQHDL | Function: DNA repair enzyme involved in the repair of deaminated bases. Selectively cleaves double-stranded DNA at the second phosphodiester bond 3' to a deoxyinosine leaving behind the intact lesion on the nicked DNA.
Catalytic Activity: Endonucleolytic cleavage at apurinic or apyrimidinic sites to products with a 5'-... |
A0A3M2DSI3 | MLIDIRDVSLEIGPRVLLHEVNGTLHAGDKWALLGRNGAGKSTFLKLLAGIQEPDSGEILKKQGLQIAYVPQGLPEGLTDTVFSYVASGLRDDGDIVASYRRAILQGDERLDHWHDQMEARSLWTLETKIQRALSEAGLDPNRRLDELSGGWKRRAMIARAIVQQPDVLLLDEPTNHLDIGGIEWLERLLADWQGAFVLVTHDRAFMDRVASQIVLLDRAKFYFFPGNFSEFEARWQAAQEAEARAEALFDKKLAEEEQWLRQGIKARRTRNQGRVRALKALREARAKRLQRQGQMKNVVADFAPGSRRVIEARNLGLKV... | Function: Probably plays a role in ribosome assembly or function. May be involved in resolution of branched DNA intermediates that result from template switching in postreplication gaps. Binds DNA and has ATPase activity.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
EC: 3.6.1.-
Subcellular Location: Cytoplasm... |
A0A7T5RM54 | MNINVILGMSGGVDSSVAAYILKKKGYNVIGIFMINWDEKNVSYCTVAKDLVDTQKICKFLNIKLHVVNFSFDYWQEVFFYFLNEYKIGKIPNPDIVCNSRIKFNIFLEYSKYLGADFIATGHYAMIKYIKNNYFLYKSFDLNKDQTYFLYKLRQWQLKYIIFPLYKYNKFFIRQLAVNVGLYNCMKKDSNGICFVGKADFKNFLKKYISVCYGFITNFYNKQFGIHEGIMFYTYGQKKNLNNKCFLFNLQYIVDKYLYKNELIISNKNRLYTYYCIIKDVNFINKFLFFNIKCYVKLRHSYVMEKCKLKYLTGNLFIIE... | 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... |
A0A6N8VWD7 | MKNMSTIKNKEPLPDFKIIIPARYASQRFPGKPLHKILGKPLIQYTYENALRSGADEVIVASDDERIIDCVRGFGGVACLSSATHKTGSDRSAEIAANEQWRDDQIVVNLQGDEPLLSPQDIRSAVECLAAHPHADVATLAAEVAVEDLAADSVVSVVCDSKHFALYFSRAVLAKSSKTGLHHIGIYVYYCNSLKHFASLAQPEIERSECLEQLRVLWHGGAIYVGVVSPSSHVAIDTEADVLKLEDILRTLNDTPRN | Pathway: Nucleotide-sugar biosynthesis; CMP-3-deoxy-D-manno-octulosonate biosynthesis; CMP-3-deoxy-D-manno-octulosonate from 3-deoxy-D-manno-octulosonate and CTP: step 1/1.
Function: Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria.
Catalytic Activi... |
A0A2G6L0I3 | MATCGCILLALFLDALLGEPKRHHPLVIFGNWAQRIETALNHQQRSGTHVFRGVLAWVIAVIPLVIFTGLTACLTYQISPWLHGLFAALVLYLAIGWRSLKEHMLAIYFPLTNNQLPAARHACSMIVSRNTDTLDETGIAKAAVESTLENGSDGIFAALFWFALLGAPGVVLYRLSNTLDAMWGYRTERFESFGKFAAKTDDLLNWAPAKITAWLYIANAFTVKRKAPEQETPRQLAQQAIINWKEQAPRLASPNGGPVMVTGATVLGVKLGGPTRYHGEWLDKPFFGGEATVEPNDIQRALTLIDTTLIGWVAIATVIS... | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
Function: Converts cobyric acid to cobinamide by the addition of aminopropanol on the F carboxylic group.
Subcellular Location: Cell membrane
Sequence Length: 332
Sequence Mass (Da): 36494
Location Topology: Multi-pass membrane protein
|
A0A2D4PF84 | MNKLNIFFKKINPDPIFHCHSVKDTLLLVNIHWLYLRCFHLLHILLNSQFLSFQGGDITKHDGTGGQSIYGNSFEDENFEIKHTGPGLLSMANCGRNTNSSQFFITLKKAEQLDFKHVVFGFVKDGMDIVKKIESFGSPEGIVSKRIVITDCGQIQNYSANILEA | 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: 165
Sequence Mass (Da): 18636
|
A0A2D8DMA4 | MYMTKKNLNFEDSLAKLESIVDALEDNDVSLEESVKKFEEGIKLVKDCQKQLQEAELKVNKLMSDGEILDQEN | 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... |
A0A9D6QQX5 | MGIGIDTDVKPRDDIHNGVLRQVGISGMGFYVPERAITNQELSTMVDTTDEWIRHHIGIETRHIAADDQALSDLAIEAGRKALTAAGLDASDIDMLIITGQNHDYKAPATSCIVQHALGMRKIPAIDLAIGCSGFIYGLAVASKFVADGSAKHVLLIGAEIHSRMMSWKDRTTCVFFADGAGAVVLSPAASGYGLLGFDLGTDGSGSQTIIIPAGGSRTPVTEQALQMLEDDSHQIRAMTHVRMDGKAVFAFATHIFPATIRACLDKLGLSTKDLDFVIAHQANRNIISEGMKALDLPMDKTYINLDRYGNCSSASIPIA... | Pathway: Lipid metabolism; fatty acid biosynthesis.
Function: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the tot... |
A0A9E5AHI4 | MPEGNAAQTIGEVLGVAVAQSGHGQRLDLELLLGLATGLNRAGLLRESKTQLSPAAHAQFNALYAAYRGGRPVAQLLGEREFWSLALLVDEHVLIPRPETELLVETAVELAHLAPPGPLIDLGTGTGAIAISLSRELPERTVFASDDSHAALRVAARNVARHAPARVHLLAGRWLHAVGPARCALIVSNPPYVSAQDPALQATGALRFEPHHALAAGPEGLDALTEILALAPARLLPGGWLALEHGATQALAVQQLMASGGFRAIATHRDLAGLERVTCAQRPPDA | Function: Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif.
EC: 2.1.1.297
Catalytic Activity: L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-methionine = H(+) + N(5)-methyl-L-glutaminyl-[peptide chain release... |
A0A7C7WA89 | MVSLKTTTIGDSLVHEVEVSRSTERLSGEPDEAQVAFWLEFVLDRLDRQSSEVSVRIVGEEEIASLNAQYRGLEKATNVLSFPAGISVEEVELLGDIVICSKVVKLESDLYGRGFADRYAHMLIHGLLHLLGYDHMEEGARTRMEQLETDLLSRLNMWNPYE | 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: 162
Sequence Mass (Da): 18312
|
A0A3M2C2N5 | MDSQSGFLLERSLVKRSFNQAAETYDEVAVLQREVGQRLIERLDYIRMKPQILVDLGCGTGEGIKLLKQRYSGAEVLGIDMAHAMLKVSKKKWPRWSLASKPKLVCADVEQLPLAEQSVDMIVSNLTFQWLNGIDMVLQECRRILRPGGLLMFTTFGPDTLKEMRECWHQLDPDGVHVNRFLDLHDIGDALLANRFMDPVMDMEMFTLTYSDVRKMMQELKALGAHNVNRGRSAGLTGKNRLQSLVSAYEKFRNAGRLPATYEVIYGHAWIPEQASVLTNEGMRETRVPLTAIQKTS | 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... |
A0A496V9Y4 | MLTRWGTWIVLIGFALATTWLVHSLEEEFSAPNKNSPHVPDYTMKNFKTLQMDEHGRLKNQLTAETMTHYPDTNTALTTPYMVFYKDNLPTWTVRAEHGEVSPDGNQVWLLGNTVIQQHTQSQQKALKIFSRDMWIKLDTEYAETAAPTTILSNSGETHSVGMRVFLPTERIELLSQVRGRYVHP | Function: Involved in the assembly of lipopolysaccharide (LPS). Required for the translocation of LPS from the inner membrane to the outer membrane. Facilitates the transfer of LPS from the inner membrane to the periplasmic protein LptA. Could be a docking site for LptA.
Subcellular Location: Cell inner membrane
Sequen... |
A0A1P8MTR9 | MRARRFALEGWMLDVGDGHRLWFEQAGQGVDALVLHGGPGSGCRPGHYDLFDLSRYRVTLLDQRGCGRSTPRASATLDALEANTTAHLIADIEALRARLGVEAWVLCGGSWGTTLAMAYAQAHPDRVRAMVLAGVATTAARDLQWLYGDVGAMFPEAYAAFCAHVPEVSDDAAATPQRIAAYADRLRDTGRAQAAADAWCQWETAIFGGDIRDPASRYADPGFRLGFARIVTHYFAHQAWLGDDELLKNVAAIAHIPCTMIHSRFDPSCPLRGAWALAQAWPAATLRILGGTAHSALDADMSAAIRTATDAVLPER | Catalytic Activity: Release of N-terminal proline from a peptide.
EC: 3.4.11.5
Subcellular Location: Cytoplasm
Sequence Length: 316
Sequence Mass (Da): 34112
|
A0A6N9AS53 | MLTVHEAAESVDGRHIGDNPMIDSVSSDSRTIESGALFVALRGERFDGHKYVEEAVNKGAVGAMVDTESNLPTPQIIVDDTEYALGQLAAGWRRRFDIPLVAITGSNGKTTVKEMIGNILRANDNALISKGNFNNLVGLPLSLLKLRESHRYAAVEIGMNQVGEIERLASIAQPSVAVITNAGAAHLEFLVNIDQVATEKGKIISSLRDSGVAVLNADSSHYSAWRRTAGSHRVISFGFSSDADVSGTCTTLTFGSQISMKTPLGEFQVDLQLAGEHNVINALAAAAASVALGLTPSSIKTGLENMSAVAGRLQPRKHLK... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Involved in cell wall formation. Catalyzes the final step in the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the precursor of murein.
Catalytic Activity: ATP + D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-d... |
A0A2D6JEA4 | MLSSGNLIRSKNLTTKKSKTVWTNLPRIFDKTLRYLAIFLISFYQSVFRFWFGGRCRFEPHCSEYGFSAFKTYPFLTALKLTFNRIMRCRPGQEFGYDPLPKEKCCGK | Function: Could be involved in insertion of integral membrane proteins into the membrane.
Subcellular Location: Cell membrane
Sequence Length: 108
Sequence Mass (Da): 12744
Location Topology: Peripheral membrane protein
|
A0A6N9B1M4 | MLISFTMCIAEEQRIHYSKSFYSPFWILPIAALLTACDFAGYESYGGSTMGTYYRVVADCQKTLSLSKITEALSSVDEEMSNYRIDSTVQQFNRSPTESWFGVDESLVHVVSVAYDVSRLSSGRFDISIEPLVSAWGFGATKVSSRPSNETIETLLKQVDYRALEFRSSPPGLRKKRPLTIDLSGIAKGYGVDVLAELLDQSDCDNYLVEIGGELRVKGVNQANRAWKIGIENPSGGGVQTKILMPRGSLATTGDYRNYRVFDGESYPHVLDATTGYPVDHNVASVTVHMPTATEADAIATALFVLGEEGLELATAHDIA... | 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: 347
Sequence Mass (Da): 38291
|
A0A2E0GRC5 | MTXNNDXYHQIEFNIAKDDLXETEKILXXYXPXSISIQGFGEEKIYEPLPGEMPIWEKIRVKAMYQNTKNLSELENEIINKTNIKIFNNKVIKAIGEKDWQEEWVQSSKPMRFGEKLWIYPDHLIDNLEGKVCVNLNPGLAFGTGSHPTTRLCLEWLEKSNLDQKSVLDYGCGSGILGISAIKLGAKSVTAIDLDPQAVIASKNNAEKNHVQQEIEITDNNKTIEKNFNIIVANILAKXLIELAPYFYKKLNLDGVICLSGILEGQINIIKDAYLKYFNLSEIKIKDGWVMMSGIKL | 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: 297
Sequence Mass (Da): 33669
|
A0A3M1WP99 | MPDPLDQTRQCVFCGLCLPHCPTYALHEDEAESPRGRIALMQALQEARLTADDPALARHLDRCLGCGRCEAMCPSRVPYLSLLDTARNMQQQARPRRLPHAARALLQATRTPARLRLAAAGTRLLRRLPGHPRLLDVLSRRDRVVPERRPETEEPVWLFADCMSGLLEDERLPAARTLLQALGHAVRLPSGPSCCGALHQHAGLPQAAADWQRRNARAYGTSGPVLSLASGCARQLATDPELGPRHQAITAFVAEHPHLDRLRFRPLEASVLVHTPCTDPNGEAATALLARIPGLNVRPLPMAHGCCGAGGLNLITEPEQ... | 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: 383
Sequence Mass (Da): 41445
|
A0A9C9G5J5 | MKVRNRRPDLPVSSHVKLDKQDKALITLIQAGLPLSSTPYTDLGHDLGMTEREVIERLKHLMQDNIIKRFGVVVRHHELGYRSNAMTVWNVPDEQVSELGHCIGQFDFVTLSYRRPRRLPDWPYNLFTMIHGQNRGHVLKNIQFLIERCNLDRVEHQVLFSTRRFKQRGAIYHPFNKGLSDDPQTAG | Pathway: Porphyrin-containing compound metabolism.
EC: 4.1.1.111
Catalytic Activity: 2 H(+) + siroheme = 12,18-didecarboxysiroheme + 2 CO2
Sequence Length: 187
Sequence Mass (Da): 21792
|
Q8M1C2 | LQLIIFANQSMIFAMSSISLLGGLVWGHHMYTVGLESDTRAYFTGVTILISLPTGTKIFNWLFTYLSNPPLLHLRITSVFLSHLFLLMFTVGGSTGIILGNGAVDLGLHDTYYVVAHFHFVLSLGAIIAIFSGIILNGEKIVATKNLLLSSSCTLSLYHLHLIFIGILLTFSPMHFLGFNVMPRRIPDYP | 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... |
A0A0D8J174 | MKILNFGSLNLDKVYKVAHFVREGETISAQEQNQFLGGKGLNQSVALARAGIFVEHAGAVGRETTEFHALLKAEGAGTTYLRVLETVSGHAVIQSCAGQNCIIVYGGANRMTRPQDVDAFLKDYGPGDLLLLQNETSCVRYAMEQAREKGMTVAFNPSPIDGSLTQDVLALADVLFVNETEGGLLSGTPANENEAVLTALAERFPHVAVVLTVGGEGALYRKGGVLLRQRAYPVKVVDTTAAGDTFTGYFLAGMIRGFDPGKCLRCASMAAALAVSREGASASIPTWREVLDFSAAQGEPLESLRGTGAAAL | 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 ... |
A0A6P2BA91 | MQARPAWLRDGYGEDGAVTIDRLDQGGRWLLPDGVEEILPPRARQIEALRQRILQRFDLWGFELVFPPLLEFLDSLLVGVGGDLDLQTFKVTDQESGRLMGIRADLTSQAARIDAHSLRSEGPTRLCYAGTVLRTRGQGLFGSRSPVKVGAELYGVPGPEGDAEVLALMAETLAVAGLGTLHIELGHVAIYRALANAAGLPPAAQDTLFDAVQRKAAADIRALLHGQDVPADIAKMIITLPSLLGNASVLPRARQTFAAAPPAVTVALDELEKTAELARQRCPALDLGFDLSELHGYNYHTGTVFSAYAPDHGQALARGG... | 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... |
A0A6M8UF16 | MDRFTLLAALSGTMAGSFTGLVIDRFQPQQTAQQWFSVLVKPRSYCFHCHRILAWRDLLPLISWCSSGGKCRICRAPIPRFLPACELFTALLFVLLAALEPRPAPLLALTLFSLLLVLLSEIDRRHCLLPDVLTLSLLWAGLLFHTFFPTFPLHDAILGAVAGYLYFWLPGWLFLLYRGEEGIGGGDMKLFAALGAWCGWQTLPVMALLAALIGILCWLYRSQRGVGQQKTIPQPFGPSLAIAGWLVFIAQHKGYNVMTILL | Function: Plays an essential role in type IV pili and type II pseudopili formation by proteolytically removing the leader sequence from substrate proteins and subsequently monomethylating the alpha-amino group of the newly exposed N-terminal phenylalanine.
Catalytic Activity: Typically cleaves a -Gly-|-Phe- bond to rel... |
A0A348UQX7 | MNALLDLLPIAIFAAVFFASDIYVATAALMIAVTVQVAAVKLMRRPLSRELLLTFWMSIIFGSMTLIFHNEIFIQWKPTIVNGLLGLSLIASEYVGQHNLLKRLLGAQLELPDAIWTRLNLGWAIGFLFAAGLNLVVAYSFPMAFWVTYKLVGGFALTLGYVIATLAYLGSKGLLTTESLSTQRTERS | Function: Plays a role in cell envelope biogenesis, maintenance of cell envelope integrity and membrane homeostasis.
Subcellular Location: Cell inner membrane
Sequence Length: 188
Sequence Mass (Da): 20719
Location Topology: Multi-pass membrane protein
|
A0A920S7S8 | MTQFRTRNRALLVVGALVLAGCASQQEPEPVAQEESPVDVAPVESQAVQAEPTPSDFDNRSRPLTPSGRILATKFYFELDQARLSARDLRLLEMHANILTRNRDRRLVIEGHCDERGTREYNLALGERRANAVSSFLTSAGVRRSQIETVSYGEERPDDPGHDEAAWGKNRRAVVIYR | Function: Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity.
Subcellular Location: Cell outer membrane
Sequence Length: 178
Sequence Mass (Da): 19973
Location Topology: Lipid-anchor
|
A0A4V2U4X0 | MTQSTLDRAASGPAPAQAGAAPGWPARLIGAVTWLVRGGVILTLAAVLILTVLQVVDRHFLRHGFAFDQYSRVGLVWLAFFGIAMGFRERANIRIDLLDHFLPKRLVAPQQFLLNLIILAVAAALIWFGWPLLEVGTFQALMDTPLSYDVMYGAGLAGLILICLFLVLRLADVLTGGRYGLDEKASDDHDHY | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 192
Sequence Mass (Da): 21013
Location Topology: Multi-pass membrane protein
|
A0A9E5AE40 | MNLNRAPLCSLLVVLLVAGCTQQVDSVKDTMGNMFKAKDEQSEALKKAAEPTPLDEEFKSSIAIKKVWSGRFGKGYEKLYLKLLPSWYGEHVYVADRDGRVMAVDVATGEKTWEERDKKRLISGGPGAGEGKVFVGTSEAQVVARDAKTGQKIWIAEVSSEVLAAPRAGGGVVLIRTGDGKLYALDAATGVQKWVFDRTIPTLTLRGSAAAVIHEDKVLAGFDNGRFSALELATGKELWETRLGEPKGRSDLERLIDVDSEPVILDNTAYIDCFQGRVAAVSLDNGSLEWTRQISSYEDLAVDTDHVYVTDEHSVVWALK... | Function: Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane.
Subcellular Location: Cell outer membrane
Sequence Length: 404
Sequence Mass (Da): 44178
Location Topology: Lipid-anchor
|
A0A9E5ACD2 | MRISRSGWPGLGAVGWGLLLLGALVCGAVGVGWARPSLAVAGRSLAAVRAAHPPSEARLLDRHGVVLQTLRTDLVRRRGPWVALADIAPGLQRTVIALEDRRFESHAGVDWWAVLGALRDGWHGRPRGASTLTMQLAARLDPALRARGARSLGQKWRQLQAALALERGWSKAEILEAYLNLASYRGEVAGVEAASRVLLGRAPAALDHTDALVLAVLLSAPNATLERLSARGCALGQRLPTRIDCAAFSARAHRALTPHAAPPGAAELAPQLARAALDGSTRNVSSTLDATVQRLARDSLQRQLALLAERNVGDGAVLVV... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
EC: 2.4.1.129
Catalytic Activity: [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate = [... |
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