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stringlengths 6
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stringlengths 16
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stringlengths 117
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A0A1E7GKE1 | MAKIILATGGSRSGKSGYTQNIAESLPGKRAFVATCPAPSEEDPEMLERVVRHQQDRFGADWDTIEEELDLQRVLREYTDVNILLIDCLTLWISNLIHQNPDISEDELTAICRELIQLSKQRGGTVIFVTNEVGCGIVPANSIARKFRDLSGRCNQAIAKGADEVIFFSCGLPLFLKK | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 5/7.
Function: Catalyzes ATP-dependent phosphorylation of adenosylcobinamide and addition of GMP to adenosylcobinamide phosphate.
EC: 2.7.1.156
Catalytic Activity: adenosylcob(III)inamide + ATP = adenosylcob(III)inamide phosphate + ADP + H(+)
Sequence Length: 178
Sequence Mass (Da): 19752
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A0A7C8ED71 | MEGSIDKSDFVVIGKIIKPIGLRGEVLIEPLTFDSNRFLNLKKLWIKFSKEMKVQNINTIRLHKKNIALSFHGYENRDAILPLIGALICIHKSESPKLPKGTYYYYQLENLDVFDVQGQYLGKIFQIMKAGEADVYIVKNEDNRELLVPAIKDSILSIDLEQKKMIVRLLEMY | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Subcellular Location: Cytoplasm
Sequence Length: 173
Domain: The PRC barrel domain binds ribosomal protein uS19.
Sequence Mass (Da): 19990
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A0A7C3QCM3 | MSSFELIIAFLLDLVLGDPPRFPHPVRWMGRLIVISERWLRRWSSTPRAEKVAGIILAIGITGIVYATSAGLIWISGGIHPLLGSLLTIYLAYTTLSIKSLRDAAMAVFEHLISDDLPQAREELKSLVGRETAGLNEAGVIRATVESVAENTSDGIVAPLFFMALGGVPAAMAYKAINTLDSMVGYKTPRYSNLGWASACLDDIANLFPARLTGLLIVLAAGLFQNAAGRSVRVMIRDGSKHESPNSGFPEAAMAGALGIQLGGPFAHPDKPGTRAFIGEPLHEPSPDHLRTAISLMVITSTLMLCLVLLSWLWLRS | 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: 317
Sequence Mass (Da): 34110
Location Topology: Multi-pass membrane protein
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A0A1V5WLC1 | MLEAKTFRQPEQETYTHHPGRFFYCKDEETGALFSAPHEPVRAEPDHFLFSPGLSDIRWETEKSGIRIELSVFLPVHDSAELWEVRVFNRSNRKRSVSLYPYIPFGYMSWMNQGASYSEEAGGIIASSVSPYQLLEDWPRIRALKDCVAFLHDRTPDSFETRRAFFEGEGGLSCPDSIREELLAKGTARYEQPAAILQYRMNLDPDESDVFRFLLAPVRDSGEALELRERYLSPDRFRSAREEAEAFATHCVPALHCETPDTHFNAFVNTWLPRQIRYHGLTNRLTSDPQTRNFLQDAMGMTWLDPAAAKESFRYALSRQNPEGSMPDGILLGDATEHAYINRVPHADHSLWLPVCLSAWLDETGDYTFLDEMIPGRDDKRTQTVHTRITRALTSLYSRRDHRDLLFIEQGDWCDPMNMVGPRGIGVSGWLTEAAAWAFSLWADITRSAGKARIANRFQKMSNRLAQAVNTVLWDGDWYARGITDEGTVFGTSGDREGRMFLNTQSWALLAGIADAKQTKAILNAVAANLDTPWGTQLFAPAYTSFREDVGRVSQKYPGAAENGSVYNHASIFWVYALFREGHTDRAWKTLRAMIPGPSHEDLEKRGQLPVYIPNYYRGAWRQFPEVSGKSSRLFNTGTCAWLYRSLVEGLFGLSGCREGLRIHCNLPSDWTRTSLTRRFRGSTFNMEITRDPAVSRMMITFNGERLEGDVITGVSSGAVHAVSIVLPANSTMTPRLSVIMGVAGSGKTTLGRLLAEQTGTRFIEADDLHPPENVAAMRRGIPLNDEMREPWMDRILEELTVATLGGMNTVLACSCLRKKHRDRIRACGCAVRFYFLHADRQRLSARLSSRSGHFFPAGLLDSQLTALEDPREDPDGDVMVLDANLPAAELTALISSGL | Pathway: Carbohydrate acid metabolism.
EC: 2.7.1.12
Catalytic Activity: ATP + D-gluconate = 6-phospho-D-gluconate + ADP + H(+)
Sequence Length: 899
Sequence Mass (Da): 101246
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A0A532UB85 | MNKHREKALWGLIVALILLLDQGSKYLIHSYIGRYRQIDVIPHLLNITYVENRGGAFGIFATSESPLKPLIFSSLSIIALIIIIYFSIKLPLKERWARFGLSLIFGGAVGNFADRLRLGFVIDFIDLHWRRLHWPSFNFADVAICTGVAMLIITTFKPRAEGKATGTL | 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-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or Ala) have small, neutral side chains.
EC: 3.4.23.36
Subcellular Location: Cell membrane
Sequence Length: 168
Sequence Mass (Da): 18973
Location Topology: Multi-pass membrane protein
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A0A6P3IGG0 | MFDVTSRVTYKNVPNWHRDLVRVCENIPIVLCGNKVDIKDRKVKAKSTVFHRRKNLQYYDTSAKSNYNFEKPFLWLARKLIGDPNLEFVAMPALAPPEVVMDPALAAQYEHDLEVAQTTAVPDEDDDL | Function: GTP-binding protein involved in nucleocytoplasmic transport. Required for the import of protein into the nucleus and also for RNA export. Involved in chromatin condensation and control of cell cycle.
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Subcellular Location: Nucleus
Sequence Length: 128
Sequence Mass (Da): 14721
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A0A2N1V750 | MSRKIILPKNSVIVITGPTASGKTSLSIELAHSLKSEIISADSRQVYKLMDICTAKPSQVELNTVKHHLIDFLDPNIEYSAGKFADDATKVIKKLYESDIIPIVCGGSAFYIKALFDGLFDEENKSKPEIRIKLNQELENFGIGYLQEQLEKVDYKSYTIIELDNPRRVIRALEYYYSTCEPISVAYEKRSTIKSEFQPIYFAIDYPREELYDRINQRCEQMWNNGLVNEYKSLISLGYDENLNSLNTVGYKESRDYLKGIYSKEEALEEFKKNTRRFAKRQLTWFRKNKDINWLEGKSESKLDQINDIIKA | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
EC: 2.5.1.75
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(37) in tRNA
Sequence Length: 312
Sequence Mass (Da): 36216
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A0A5C0UEZ1 | MNWLTNWIPKIRSTKSSSIPENLWHKCNKCGEMIFKQQIEDNLLVCTICDHHERMTAKQRLCAFFGSEKCFVVEEPKKYSDDPINFTDKISYKSRLKKYREICDSDDCFLIGIGSVEGKKVVALSMNFKFIGGSMGRALGNAIVYAADLAVENGIPLIIFSSSGGARMQEGMFSLVQMARTTIAIKQVKEAGLPYISVLCDPTTGGVQASFAMLGTITLAEPDALIGFAGKRVIQQTIRVELPDDFQSADFQFNNGFIDKIVHRSKMRSEIIRILDILD | Cofactor: Binds 1 zinc ion per subunit.
Pathway: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1.
Function: Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA.
EC: 2.1.3.15
Subcellular Location: Cytoplasm
Catalytic Activity: acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein]
Sequence Length: 279
Sequence Mass (Da): 31184
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A0A485EDT0 | MSSPLTDRSARLQALQHALRERILILDGGMGTMIQSYKLEEADYRGERFADWPSDVKGNNDLLLLSRPDVIQAIEKAYLDAGADILETNTFNATQVSQADYGMQSLAYELNVEGARLARQVADAKTAETPDKPRFVAGVLGPTSRTCSISPDVNNPGYRNVTFDELVENYVEATRGLIEGGADLILIETIFDTLNAKAAIFAVQGVFEELGVELPIMISGTITDASGRTLSGQTTEAFWNSVRHARPISVGLNCALGAKELRPYIEELSTKADTHVSAHPNAGLPNAFGEYDESPAEMAVVVEEFAAAGFLNIVGGCCGTTPAHIEAIAKAVAKYPPRAIPEIPRACRLSGLEPFTIDRSSLFVNVGERTNITGSAKFARLIREENYAEALEVAQQQVEAGAQVIDINMDEGMLDSKAAMVTFLNLIASEPDISRVPIMIDSSKWEVIEAGLKCIQGKGIVNSISMKEGVEAFKHHARLCKRYGAAVVVMAFDEDGQADTQARKEEICKRSYDILVDEVGFPPEDIIFDANIFAIATGIEEHNNYAVDFINACAYIRDNLPYALSSGGVSNVSFSFRGNNPVREAIHSVFLYYAIRNGLTMGIVNAGQLEIYDEIPKALRDRVEDVVLNRTPEATEALLAIADDYKGGGAVKEAEDEEWRSYSVEKRLEHALVKGITTWIVEDTEECRQQCARPIEVIEGPLMSGMNVVGDLFGAGKMFLPQVGQVRASDEAGGGPPDSLHRGGERRQAGSQGQDPDGHGEGRRARHRQEHRRRGARLQRL | Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-methionine from L-homocysteine (MetH route): step 1/1.
Function: Catalyzes the transfer of a methyl group from methyl-cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate.
EC: 2.1.1.13
Catalytic Activity: (6S)-5-methyl-5,6,7,8-tetrahydrofolate + L-homocysteine = (6S)-5,6,7,8-tetrahydrofolate + L-methionine
Sequence Length: 781
Sequence Mass (Da): 85195
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A0A662R4D1 | MIEKISGLEGCNVVIKLGGNLLNDDIVEDIADDIVRLSRAGVRPVVVHGGGHEISRMMERMGKEPVFVDGLRVTDKETLDIVAMVLCGKENLKLTSLVIKKGGKAVGLSGKDGKTIVGKRIEKLGWVGEVKEVKTELLDVLLERGYIPVISPIAIDDEGNLLNVNADIAAGMIAKALKADKLLILTDVPGILKVRDDHSSRIHQLRLKELSQLMQDGTVSEGMIPKLRAVMQALEGGVKSAHIMNGMEKHSILLELAGEYTGTVITV | Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4.
Function: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.
Catalytic Activity: ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate
EC: 2.7.2.8
Subcellular Location: Cytoplasm
Sequence Length: 267
Sequence Mass (Da): 28793
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Q5KWL8 | MTDKNFFSCRRTLGFTLIETLLSITLLSAVAIGLFSFFTHAMTYTADNERRTVAINVARGTMAYFEKNVLFSSLSNYMTENNLSFLKVEKNSCSHEALSSLLFPSGNQGETISSQQSCTAQLAPTINDVQYETTVYIIRCDQEGWDGFLTSSEFASLPERLKEEIRRERNNMISSEAGIYMAKLYAVVRWGERNGDITWVEGVVTDETIR | Function: Required for transformation and DNA binding.
Subcellular Location: Cell membrane
Sequence Length: 210
Sequence Mass (Da): 23716
Location Topology: Single-pass membrane protein
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A0A1N6LXM7 | MLLYKLVLVVQLAKIAFCDYYKILGVPRNATDKQITSAYRKLAKVMHPDIAPEKEKEFVKITEAYDVLRDPEKRSRYDRFGEEGVSQNFHEPNSNFGGGDHGFFQDIFSQFGGFHFSFNGKDHRQGSGGDHYPYDFHGNIDDYNEHISSTKCITLILLHHPQCGHCLKFKPVFNKLTKKYKTLEFLSVNCQRNNAICQHENIAGYPTLVAYKWPSFDKFTYHGDLSEKSIDNWLHNSVIGIKVKTITTVKQLEDFVANSKILPIVAIVNNPNSLVLPSIAMVLNEKANLAIVLGNNTMIVKRLLPPYTPSLLAVLSVDEIEGEWYNLKNFKFDEILLELRKDVSKFKQSKGGTKGSYKQLTNKLIESGECGPKDGQYCFIALVKDSNAELNNVLKELANKYRNEPVKLRFYPVSGKAPFGLDIRRGIKFVAYRPKRAKFKVLDKILNINSIDEFINGVLEGSVKLDLNAQFFEFRQLEL | Function: Plays an important role in regulating the size of autophagosomes during the formation process.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 479
Sequence Mass (Da): 54639
Location Topology: Single-pass type IV membrane protein
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C5LD13 | MSIFGHTFRVSTWGESHGLTVGCVVDGVPPGLELTEEDVQPQLDRRRPGQSTLTTARSEADQVTIMSGTENGVTLGTPVAMMVKNKDQRKFDYANTTLIPRPGHADYTYQVKYGIKASSGGGRASARETIGRVAAGAIAEKYLYKEFGCAVVAWVDSIMEIRLPEDIRDGFKSRPPTREEVDAFGIIRQAALEDEVYLIDHQDNVYDGISGNPIIGGGVLVGDLTLTNTHYIRCPHGPTAAQMVARLLQVKGANDSCGGSIGCCITHCPVGLGEPCMDKFEAELAKGMMSLPATKGFEIGSGFDGCRTLRGSRNNDPFESGVDGEGLLHTRTNNHGGTLGGITSGMPIYFRVCIKAASSIGVEQVTADFDGHTQTLAVKGRHDPCVLPRAPPLIESMAAIVTMDMVLRQRARGMPMHTLGTVGEEDK | Cofactor: Reduced FMN (FMNH(2)).
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7.
EC: 4.2.3.5
Catalytic Activity: 5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate
Sequence Length: 427
Sequence Mass (Da): 45771
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A0A524B756 | MRPILTPHEMREVDAAAVARGTAEEILIERAAWAVARRARRMLGGSYGRRVVVIAGPGNNGADGRVAARFLTERGVRVRVIDAASIPERLPECDLVIDAAYGTGFRGVWNAPRTDAPVLAVDFPSGVDGMTGCSHGRPLRATATVTFAALKPGLLFGDGAEFAGDVEIVDIGLDVSSSSVFAVDASDVSVPARAVDAHKWKAAVLAVAGSPGMIGAASLASEAALRAGAGIVHLVSPGSASDHSIPREVVRRPVAPIGWAPEVVEMAGNRFAAMVLGPGLGRDESTMTDVRRLVADATLPMVIDGDALFALGDEFSVLASRRGGSVITPHDGEFARLTGHAPSRDRIAAARSLAHDADCVCLLKGPATVIAAPDGRVAVVDEGDQRLATAGSGDVLAGVVAAFIARGAELFEAAYSAAFVHARAARHDRAIGLLAGDLPLAVADVLAGDFEVDA | 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 is a result of enzymatic or heat-dependent hydration.
Catalytic Activity: (6R)-NADHX = (6S)-NADHX
Sequence Length: 454
Sequence Mass (Da): 46737
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A0A977TL24 | MFKMNISMNNKNFKNKNINFILYLMLFFSTFIVMNSSSWLSAWMGLEMNMMSFIPLMMNNKNHLPTAPSMMMYFIIQSVSSSILIMMMLNMKNIKMSLNNNLITSVMLMSLIMKLGGAPFHWWIPKIMNNLSWMNCLILLTWQKIAPMILMIQVPNLSMIFMSAILSSIYGSLLSMNQTSFKMILSFSSINHLGWLMMSMLFSLKMMMMYFLFYSLINISICLNLNKFNMINLNHMFKINNNKMIKLIMNSTFLSLGGIPPFLGFLPKLMILILMIKNNLFIEAFLMIILTLLIISIYITPFTSSLLLNKMNIKWMNKINKNLNSDKFNFYMINLMLTLMLFLMLMTKMI | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
EC: 7.1.1.2
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 350
Sequence Mass (Da): 40946
Location Topology: Multi-pass membrane protein
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A0A917IEA4 | MRDRPAAASPRPLLPLWAAVPAAAAGGLALDAAFPELGIWPLAFLAVGLSLASLIGRRVGGALLVGLAFGAAFWFPHLDWAARFLGDHPLAWVPWTALAGVQTLFSALGAIPISLAYRWFPDRRVPRLTLLPLLVGAVWTARELVMGNWPYGGFPWARLGMTQSEGPFAAVASWLGVSGLSFLMAVLTAALLELARVRPVRLRSLLPAVALALVLVLTPQWQTGTAGTMRVGAVQGNGPAAYFDERSRGDILAAQLEASQPLRHEDVDVVLWPEGGVDSDPRADRATALTLRVASRAFGAPILLNAASEEGDLVYNTSMLWTEDGLDADGGLQTHAKRHPVPFGEYVPDREFYGAIVPDLIGLIGREYTPGTDAPVVDVDAVRIGLAICFDVIYDDVIREGAREGAQVFMFQTNNADFRGTDENLQQLAFARMRAIETGRTVVNLSTVGTSQVIAPDGTTMSALGVDEAGLLVSELELREGLTPAVVLGPWVQAALLAGSLAALVLLGLARAFRRGGARDGRGGSRRRPRAAPRRPRSDVDRVVAMFR | 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-[lipoprotein] = a 2-acyl-sn-glycero-3-phospholipid + H(+) + N-acyl-S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein]
EC: 2.3.1.269
Subcellular Location: Cell membrane
Sequence Length: 548
Sequence Mass (Da): 58528
Location Topology: Multi-pass membrane protein
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A0A944D3Q1 | MKPSTQHPAKSQFSEMEERVIELWDKNNTFQRSVDERPADQAYSFYDGPPFATGLPHYGHILASINKDVVPRYHTMRGQRVERVWGWDCHGLPIENIIEKDLNLKTKHDIENFGVAKFNDACKATVFTYAEEWKKTIRRLGRWVDMEHDYKTMDRNFMESVWWVFKQLWDRNLVYEGKKSMHICTRCVTPLSNFEVTLGYKDVKDIAAFVKFQLTDCEVPTYIIAWTTTPWTLPGNVALAIGKDVQYVEVECEGARYIVSSHAVEKLFADKEHSITNRYTADQLAGKAYTPVFDFFAKDSELENHSNGWKIYIGDFVSDVEGTGVVHIAPAFGEDDMNLGKQEKLPFVQHVSMDGKFTQELESLAGIQVKPKGEDQERLQADIAIIKALQENGTLFKKENVTHSYPHCWRCDTPLLNYATSSWFVSVTEMKEDLLANNQKINWHPEHLKDGRFGQWLENARDWAISRNRYWGTPLPVWRADDGELMCVGSVKELEQLSGTHATDLHKQFVDEITFEKNGKTFRRIPEVFDCWFESGSMPYAQMHYPFENKEHFEASFPADFISEAQDQTRGWFYTLHVLATALTRGENPAIPSTGGTTPAFKNVSVFGIVLAADGKKMSKKLKNYPDPTVVLEKYGADVLRLYLAQSPVIDMEPLNFDEKDVEELHRKYTNTLWNVYTFFKTFADNEPATITEITNPDELSDPMDEWIMTNLQLLLKRVTAGYEAYHLRDVALPLLDFVQELSTWYVRRIRTRCKSENAADRMMALRTLYTVLKNFVCIAAPVTPFITEEIYQQLRTQSDADSVHLAHWPEVHEAMINSKVMEDMECVRASIEAALALRAEHKLKVRQPLQSVTITGEELAKELQAVIAEELNVKEVHVGSAYAIDTTLTPELKAEGLLRELVRQTNALRKNQKLTLNDRVNITIATQSEAITQMLSVHTDEYLRQVLGLTLTITEAGAGEAMNCDGEQLTMSLTVHG | Function: Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile).
Catalytic Activity: ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile)
EC: 6.1.1.5
Subcellular Location: Cytoplasm
Sequence Length: 978
Domain: IleRS has two distinct active sites: one for aminoacylation and one for editing. The misactivated valine is translocated from the active site to the editing site, which sterically excludes the correctly activated isoleucine. The single editing site contains two valyl binding pockets, one specific for each substrate (Val-AMP or Val-tRNA(Ile)).
Sequence Mass (Da): 111878
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A0A1Y1C2U4 | PTTKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGISSILGAINFITTILNMKPAAITQFQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFF | 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-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
EC: 7.1.1.9
Subcellular Location: Membrane
Sequence Length: 229
Sequence Mass (Da): 24549
Location Topology: Multi-pass membrane protein
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A0A532UL09 | MYQPNVLVLLEPLRKLLHRGAAKRVVHLLSNVRAVDIARIMTSLSDHDRKTLFTILSAQNTKLAADILGEIYPAVGISFLDDCSKEELVSILQELPSDDRAEIMGDMSDEMREELLELMRERESVEVQDLLRYGEKTAGRIMIPEFFALPEDAQVKEAIEYLQKSANVEMAFYLYVVSKYDHLLGVISLRQLLLVPPETKLRDVMSPDVISVHPDTDQEDVARIVARYNLLAVPVADEQGKLLGIITVDDVVDVIREEATEDILKLAGVGAETILDKSTLRNFLTKLPWLFVPWLGQIIAANIINSFQGLLTKIIALAAFIPVVMGMGGNVATQSSTIVSRGLVTGRVNTKNFWKVMLRELMVAVLLGAVYGVMLGFITKLQMGSIPFLSFTVSLSVFCAMIAAAAVGSFGPLALQKMGADPAVSGAPLVTTTADIIGLAIYFGIAYLLLLR | Function: Acts as a magnesium transporter.
Subcellular Location: Cell membrane
Sequence Length: 452
Sequence Mass (Da): 49617
Location Topology: Multi-pass membrane protein
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A0A7C1XTI6 | MTAPISDRPLSPRGCMNLLPVYAEKKRAVETLCLDVMRTWGYREVITPIFEYLDVIARGAGEDLIESGYKLTDRQSGRVMILRPDVTPQIARLAGTALRRARPLRLSYCLNVFRYERVHGGRQRESFQLGAELIGVREPEGDAEIISLFTEVLSSARLNDYRISMGQRDFLRGFWEQERLLPHIGTLKSVFVRKDASGLLDLHRAGVLTGKELGLFEEIMYLYGDEGILDKAESLVDNPVSEAALRNLREVYGFMKTHGVHGKVIFDLSEARGFDYHTGVFFEAFVPDRGLLIGCGGRYDTLVGSFGEDSPATGFSIDLGSLMGVSALAVPERTSVLIVDLTADKALALSLARELRSKGFDAVRDIIRRPLESSFEYARLNGISYVVKIEGAAEGRKLLSLLCTRPGSAAEDPRYEELRTVVESFGG | 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
Sequence Length: 427
Sequence Mass (Da): 47438
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A7HW38 | MAEANNPREMAGAPASCHIEADGNVLRIEAAGDWSIVHLDPVDRQLRAIGARPGTGRAIIGFKDITRFDTAAAAILGRTAAHLGEQGIKVDFEDVSDAQRLLLDKIDSCGMPEPAHVPWRPLHIQIIDKIGATMRDIGAEGLAMLGFVGAVMATAGRTIARPSRLRWTPFVHHMEKAGFDALPLVCLLTFLIGAVVAQQGAVQLRQFGAEVFTVNLIAIIFLREVGLLLTAIIVAGRSGSAFTAEIGSMKMREEIDAMRTLGLDPMEMLVLPRVLALMVTLPLLTFVADIMGLIGGGLVVQVMLDMPPGVYISRVQEAVGFWTFGVGLVKAPFMAVVIALVGCRSGLSVTGSAESVGAMTTRSVVRSIFLVIILDALFAMFFTAVGI | Function: Could be part of an ABC transporter complex.
Subcellular Location: Cell inner membrane
Sequence Length: 387
Sequence Mass (Da): 41224
Location Topology: Multi-pass membrane protein
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A0A1V5WG20 | MKTVAGIDMGTQSMKVILYNWETKEIVAKTQEPVDLIAKNDGTREQKAEWYDEALTKCFAGFTEEQRKSIQAVGVSGHQHGFVPLDKDGKALYNVKLWNDTSTVEECNILTEAAGGNDAVISEVCNLMLPGFTAPKILWLKRHKPEAFAQLRYIMLPHDYLNFLLTGNYVAECGDASGTALFNGIRRQWSEKICNLVDPGLIKLLPDLIESEKPAGKISREAAARFGLPGDIPVSSGGGDNMMGAIGTGTVRDGFLTMSLGTSGTLYGYSDSPVSDPEKGLSGFSSSTGGYLPLLCTMNCTVATEETRKLFGLGVKEFDECASKAPIGSEGVVFLPFFNGERTPNLPNGRASINGLDAANNSRENIARAAMESAIFGMRIGLEAFQALGFRAKEIRLIGGGAKSKIWRSIAANVMDLPVKLPASDEAAAIGGAVQALWCLMNLEGNKISIGELTDEHITINEDQCINPDPASVAAYNKAYAEYNRYLGALAPLYT | Function: Catalyzes the phosphorylation of D-xylulose to D-xylulose 5-phosphate.
EC: 2.7.1.17
Catalytic Activity: ATP + D-xylulose = ADP + D-xylulose 5-phosphate + H(+)
Sequence Length: 495
Sequence Mass (Da): 53322
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A0A9E8NZZ9 | MPIHHLLLASSLAAMTVPMPQAAHAQEVVKPSLTIKAAKAQFRPVSFAATLPAASGTLVLPLGSEADLASRASVLPDAERAAISRALAAAEFDYKTGALSLRGIGGWDRIHVIGTGKDLSAAAVQKLGTIAGRALMKDKGPLAVLATGLPAEAVAELATGMGIGEYRSDLYQAKAREASAMAGTTIVSENGQAARALYEGRGKALIEAMAFARDLSNEPANVIYPESFVERTRAAFAGVAGVSIEALDVPAMEKLGMGSILGSGRGSARPPRMLIVRYTGRGAPSAGPVVLAGKGITFDSGGISLKAGAGMGDMKFDMSGAASVVGAVLALARSQAPVDVVAIAALSENMPDGNAARPADVLQAMNGKTIEINSTDAEGRLVLADAVAYADARLNPAAIVDMATLTGSIMTALGDDYAGLFSRHDPLADQLVKAGDVSGDALWRMPLHPSYAEDTKSTIADIKNSGASGAGAGAGAHFIGAFVKPETPWAHIDIAGMAWGGANDLKPAGSTGYGVRLLEQFVRNFQPVPKVAGE | Cofactor: Binds 2 manganese ions per subunit.
Function: Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides.
EC: 3.4.11.1
Catalytic Activity: Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low.
Subcellular Location: Cytoplasm
Sequence Length: 534
Sequence Mass (Da): 54542
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A0A5S9N4Z8 | MTTTIKIGVILVLCNLGFSVVQAAENTEVCECEEAKTGREVKNGAAGVEPIALGSQVQTTPFSLSTHKPNYLLPISYNRNPNDLGVDLGDKSINHVEVQFQFSLKLLLTDRTAGQPHLYVAYTNRSFWQAYNKGLSSPFRDTNHEPEIFYRLPLNIAFGDWEQNNLDFGFVHQSNGRSLPLSRSWNRVYLNWTTTLDDWTFSFKPWYRLPERSKNDADDPRGDDNPDIGDYMGHFEWLTEYRFEKHILTAMVRNNLSSDNRGAIDLTWSYPLSNNVSWYAKWFYGYGETLLDYNHLNNTFGLGFAISNW | Cofactor: Binds 1 Ca(2+) ion per monomer. In the dimeric form the Ca(2+) is bound by different amino acids with binding of each Ca(2+) shared with ligands coming from each monomer. The Ca(2+) ion may have a role in catalysis.
Function: Hydrolysis of phosphatidylcholine with phospholipase A2 (EC 3.1.1.4) and phospholipase A1 (EC 3.1.1.32) activities.
EC: 3.1.1.32
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+)
Subcellular Location: Cell outer membrane
Sequence Length: 309
Sequence Mass (Da): 35495
Location Topology: Multi-pass membrane protein
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A0A5S9PBN5 | MKWSWKLARIAGIDVNIHATFLLLVLWFAWIYWANFGTVFAAIQGAVYIITLFGCVVLHEFGHALTARRFGVVTKHITLLPIGGVAAMEKMPEKPFEEMLVAVAGPAVNLVIALLLWVWIHLTNTQISAELLMGIDGSFAFRLMVVNIFLALFNLIPAFPMDGGRILRAALATRMSHAAATAKAATIGQGFAILFGILGVFYNPFLLLIAIFLWLGATAENQMEQNRDVLEHMTAEQAMLTEFRIVSPDDVLSHAVEHTIAGSQKDFPVGSRHLLTHVLTQNQLVQALHDHDRSTRIHELDLPTLITVDASTPIKNLLDNMQSHHCNMVAVEKNGELAGIVNLENIMELIRFSQAMQARRR | Cofactor: Binds 1 zinc ion per subunit.
Subcellular Location: Cell membrane
Sequence Length: 361
Sequence Mass (Da): 40100
Location Topology: Multi-pass membrane protein
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A0A931VK37 | MYTLEQLAQHVNGKVLGNPEQTIRGFASADEAGEGEITFLAFPKYLPAVLSTKASCVIVSKPYEEIKKNQLQVSNPYFAFIQIIQLFQKKFLPPPGISSKAEILKNVKIGENPSIASFVFIDEDVMIGARVVLFPGVYIGKGTSIGDDALIYSNVSIRDRSKIGHRVTIHSGAVIGSDGFGFVTVEGVHHKIPQVGIAVIEDDVEIGANVTIDRAALGETRIKKGTKMDDQVHVGHNVIIGENGLFAAQTGISGSVKIGDYAVTGGQTGFSGHVRVGNHVKMAGKSGITHDIEDHQTVAGFPAIPHVQWKRSVILFNHLSNLQKQIQTLKEQIEALEQKIQKLD | 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.
EC: 2.3.1.191
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] + a UDP-3-O-[(3R)-3-hydroxyacyl]-alpha-D-glucosamine = a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D-glucosamine + H(+) + holo-[ACP]
Sequence Length: 344
Sequence Mass (Da): 37253
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A0A9D6Q2K6 | MSVEEIVKDVLINDIGMDDVEVSPNSRLKEDLGVDSTELVEVIAALEKKFKIKIPEGVIGLRSSVKDIVNFLNNVKVS | PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine of apo-ACP by AcpS. This modification is essential for activity because fatty acids are bound in thioester linkage to the sulfhydryl of the prosthetic group.
Pathway: Lipid metabolism; fatty acid biosynthesis.
Function: Carrier of the growing fatty acid chain in fatty acid biosynthesis.
Subcellular Location: Cytoplasm
Sequence Length: 78
Sequence Mass (Da): 8583
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A0A7C5S9A7 | MKRIVLITGGARSGKSDYAIGVVDTGGYRNRYFIATAEPLDEEMRERIEKHRNQRSQEWTTLEEPIRTWDKLQGIDSPDTVAVLDCLTLWVSNLMSKGDVPAVQDCFEKLLQTLKGLRHLTVYIVTNEVGMGIVPADKTTRLYRDLLGQLNRSIASLADEVYLLVSGIALKLK | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 5/7.
Function: Catalyzes ATP-dependent phosphorylation of adenosylcobinamide and addition of GMP to adenosylcobinamide phosphate.
EC: 2.7.1.156
Catalytic Activity: adenosylcob(III)inamide + ATP = adenosylcob(III)inamide phosphate + ADP + H(+)
Sequence Length: 173
Sequence Mass (Da): 19466
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A0A7X8I9K8 | MTHIVPPRKWAYIIFAFFFIGTSILSLIFLYQHFGDGTSFLELRKFRYETLYIIGIMLIMYYVFDALRLFYIIRALDIKISFLYVLKLVFINIFISNITPFATGGGFAQIYFLNKKGISIGNSTAATTIRTVIATVFFLITTPIIIFTEKSLIDIFSKGGGIVYVFLIIFIYFVLIYICYKFIYRTKIIKGIIFSSFNFLERKKLISNRRNKKWSRSLYKEIDTFSNSIKSFAKGEPKYILLSIGFAIIYLFTLFYFSVVLINGLGYHIPVISIISFQVLITFIMYFAITPGASGIAEGGYTLIYSNFIKRGDIISLTFTWRFVTVYIGMVIGGIIFYKEMFKSGFPGGYINAK | Function: Catalyzes the transfer of a lysyl group from L-lysyl-tRNA(Lys) to membrane-bound phosphatidylglycerol (PG), which produces lysylphosphatidylglycerol (LPG), a major component of the bacterial membrane with a positive net charge. LPG synthesis contributes to bacterial virulence as it is involved in the resistance mechanism against cationic antimicrobial peptides (CAMP) produces by the host's immune system (defensins, cathelicidins) and by the competing microorganisms.
Catalytic Activity: 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + L-lysyl-tRNA(Lys) = 1,2-diacyl-sn-glycero-3-phospho-1'-(3'-O-L-lysyl)-sn-glycerol + tRNA(Lys)
EC: 2.3.2.3
Subcellular Location: Cell membrane
Sequence Length: 354
Sequence Mass (Da): 40760
Location Topology: Multi-pass membrane protein
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A0A1F9X5M0 | MNYVLSVLTGILLVLSFPKFNYSFLSWISFIPLLYSARNANKTKSFIYGFLSGVVFFCGLLYWILPTFKTAGEPLLVSLPALLIFSAYLALYFAVFSLLFNAFSKTNTILKTAFLVSCLWVVLEYLRGCLFTGFPWGIIGYTQWNNLWLIQSSDILGVYGISFVIIFANITLYYSILLAKEKYVVKSIVENKKLSETYLLMIISSLLIIVFLRYGDIRLYFISKTPQKNTVKITVLQGNVDQYKKWDEQYVSEILCKYSVLSADAYKKDSPDLIVWPESSVPGYLLENEHLSLWLKNLISKSKTCHLIGSPDYQNGKYYNSAVLISQEGKLKDKYDKIHLVPFGELVPLKSVLSKYISALNSLGDFTAGKKMTVFNISNEPKTAFSANICFEAIFPSLISKFENHEFIVNITNDGWYLKTSAPYQHFVFNTFRAIENRKPLIRCANTGISAYIDKTGRVINKTELFETTFQTYSISPNKIKTIYAIYGDIFVLLSFFYLLYQTNVLIILFKIVKIWLLKISK | 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-[lipoprotein] = a 2-acyl-sn-glycero-3-phospholipid + H(+) + N-acyl-S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein]
EC: 2.3.1.269
Subcellular Location: Cell membrane
Sequence Length: 522
Sequence Mass (Da): 59776
Location Topology: Multi-pass membrane protein
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A0A934ELV9 | MILDRILEHKRAELRHKQSRSYLADLKAAIRDAPPVLGFAVTLDATRSPASPALIAEIKKASPSLGLLREEFSDQFDYLGLARTYQEHGAAALSVLTDKEFFQGDLRYLAEIKRAL | Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 4/5.
EC: 4.1.1.48
Catalytic Activity: 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate + H(+) = (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O
Sequence Length: 116
Sequence Mass (Da): 12968
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A0A660ZM74 | MRCFIAVDIPERVKKEVMRATERARRSHRDLKWVEEENLHITLKFLGEVEKEKIEKVKRVLDMITRAEAPFNLTTSDFGTFPKRGALRVFWLGIEGDLEEIKRLQERIDRELLKIGFDKEDREFTPHLTLARAKRYSRERVSLEDLDLDSVSGRSFRINEVILYESILRPEGPLYRKISVFKLRGR | 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: 186
Sequence Mass (Da): 22088
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A0A223PQR2 | IAAMADDARAYYGVQFHPEVTHTKQGLRILSRFVLDICGCAALWTPSNIVDDAIATVRAQVGSSKVLLGLSGGVDSSVVAALLHKAIGDQLTCVFVDNGLLRLHEGDQVMAMFAENMGVKVIRANAEDKFLGRLAGVADPEEKRKIIGRTFIEVFDEEATKLQDVKFLAQGTIYPDVIESAGAKTGKAHVIKSHHNVGGLPEDMQFELVEPLRELFKDEVRKIGLELGLPYNMVYRHPFPGPGLGVRILGEVKKEYADLLRQADHIFIEELRAFDWYHKT | Pathway: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln route): step 1/1.
Function: Catalyzes the synthesis of GMP from XMP.
EC: 6.3.5.2
Sequence Length: 280
Sequence Mass (Da): 30937
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A0A2H5Y829 | MALHLPRACILLEWASRACHKTMITLHLRFPKPEHSHPILLAPGLLDRCGAALREAGLEGPIALVSDTTVAAYHGARVRRSMEEAGFPVLEILLPPGEKTKTLDTAAALYRRLARGGIGRDGVLIGLGGGVVLDLAGFVAATYMRGIALVSIPTTLLAMVDAAIGGKTGVDLPEGKNLVGAFHPPRLLLIDPMVLSTLPPAEWRNGMAEVVKAALIGDAALWQQLRDHPARWAAMPEIEPLVDLLTRAIAVKVRIVEQDPLETRGEREVLNLGHTFGHAFERVSGYRVPHGEAVAAGMMAAAALSARRGFLEEPRLFQDLEDVLRGLGLPTRWRAWLARYGIDASPEDIIAAMGTDKKRRGGRLRFILIHRPGVVRVHSDVPDEAVLQALEETAGL | Cofactor: Binds 1 divalent metal cation per subunit. Can use either Co(2+) or Zn(2+).
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7.
Function: Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ).
EC: 4.2.3.4
Subcellular Location: Cytoplasm
Catalytic Activity: 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate
Sequence Length: 396
Sequence Mass (Da): 42812
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A0A5C0UH54 | MVIKNKFGVKVYDENSLDKMRIACGLASATLDYLESFVKPGVTTKYIDQMCEEFVRKNGGVPTCKGYKGFPASLCISINEVACHGIPNNTQLKSGDIVNLDVVVEVGGWHGDTSRTFAVGELSKQHKDLVKIAEEAMYVGINSVKANGCFNDIGVAVEKYVASQEGYCLVKEFCGHGIGRNMHEEPLVLHFAVNNQTSPIEPGMFFTIEPIISCGSPHVKQMKDGWTMVTKDKSYAAQFEHTLFVGYDDKIHILT | Cofactor: Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe(2+)-metalloproteases under physiological conditions, and the catalytically relevant metal-binding site has been assigned to the histidine-containing high-affinity site.
Function: Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed.
EC: 3.4.11.18
Catalytic Activity: Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.
Sequence Length: 255
Sequence Mass (Da): 28082
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A0A355FYT2 | MPSAEAKPSAPPPFGMTISGAFARSIVFMAVCRLVFMCETLGKEAIIAEGGRAVKGDSLRVCLVMEAPNRYTGAIMSSEEMPKAYDPQAVEDGIYAAWEASGFFNPDNLPGDRSTPYTISLPPPNTTGTLHLGHAMYTVQDILIRFERMRGKAALWLPGTDHAAIATNAKVERLLKEEGLTRHNLGREKFVERVNAFIKQSQGTINRQLRKMGFSLDWSREAYTLDEPRNRAVREMFKRMYDAKLIYRGHRVVNWDPNLRTNVSDDELEHVEKQDPFYWFQYGPFVIGTVRPETKFGDKYVVMHPEDGRYKDYQHGDTFECEWINGPITATVIKDEAVDPEFGSGVMTITPWHTAIDFEIAERHGLDKEQVIDFEGNLLPIAGEFAGMPIEEARPKIVEKLQKKGLVVKVEEEYVHNIAINSRAGGIIEPQVREQWFIDVNKPFAFVQSKHHPIEGLKSGQEISLKEVMRHVVTSGQITFVPERFEKIYFSWIDNLRDWNISRQIWFGHQVPVWYKGEDIVVGETPEGDGWEQDPDVLDTWFSSGIWTFSTLGWPDDTADLKRFHPTDVLETGYDIIFFWVARMILMTTFALGEVPFRTVYLHGLVRDEQGRKMSKSLDNIIDPLDVAEKYGTDAVRLALIIGSTPGQDKNLSEQKIEAYRNFGNKLWNIARFVLGVVEVVEVVEGVEARTLADRWILSRLGEVTTSVTKKLETFQLSSAAEELRDFTWGDFADWYLEIAKIEKDKDDILLFALERILVLWHPFIPFVTEEIWKRFSAGSRAGETRSFLMVHDWPESGASPLLFSSEGGSASGGKEGKGVVREQMQHLQDVIVAIRNLRSENNVEARKKVVVTLVSQEAAKMLDEQKALIHGLARVESLTISSEKVKPGDSASTVVGTTEVYLSLEGLVDMDAERDRLVGELEEARTFEAKTKVKLDNKEFISYAPTKIVESIKETYAQTQERIQKLESQLARLA | Function: Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA-dependent manner.
Catalytic Activity: ATP + L-valine + tRNA(Val) = AMP + diphosphate + L-valyl-tRNA(Val)
EC: 6.1.1.9
Subcellular Location: Cytoplasm
Sequence Length: 975
Domain: The C-terminal coiled-coil domain is crucial for aminoacylation activity.
Sequence Mass (Da): 110478
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A0A7X8L9S6 | MGTEKILAFDLQFVFETFIMIINPVILFLVLRKLLFTPVHNFMEKRSKTIADELDHAKEQKNQAEALHQEYEEKLTHIQQEADTILETARKRAREQEDYIVMKAREEAEQIRERAEKEIKREQEKVKDDMKKEIIDVASFMTSKMIQKSLDEKNQTQLIDEIIEELEDVSWLN | 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: 173
Sequence Mass (Da): 20612
Location Topology: Single-pass membrane protein
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A0A7C5S9G9 | MHPKTKKTIDRSLPVKKKKVVIGSRGSRLAIWQAEWVKARLLHIAPDLEVEIKKIKTTGDKILDVPLAKVGGKGLFVKEIEEAMLRGEVDLAVHSMKDVPTMLPQGLHLGAVCSREDPRDAFISRKKGEEFTIREFREIPEGAVIGTSSLRRSCQLLHMRPDLKILQLRGNVDTRFRKLDEGQFDAIILATAGVKRLGWEERITERISPELILPAIGQGAI | Function: Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
EC: 2.5.1.61
Catalytic Activity: H2O + 4 porphobilinogen = hydroxymethylbilane + 4 NH4(+)
Sequence Length: 221
Sequence Mass (Da): 24764
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A0A8T6Z5G7 | MSDLMILKLGGSVITDKSTSYATADEKNIELIANEILKCKKDFNFKLIIVHGAGSFGHPLAKKYQNDLKEIDFKGVYEIHESMKILNELIIRSLRRVGIKALPIHPMGLIVADNSRIKLMQTESIYCMLENGFVPVLHGDVVMDKTLGASIISGDQLLTHIGMKLNAKRIGFSSNVDGVFDESGKVIKKITNSNFKNVEMHIKGSKNIDVTGGMREKVIEILNLSKLGFTTYIFNATVTNNISKFLSGKDIGTEIKWD | Function: Catalyzes the formation of isopentenyl diphosphate (IPP), the building block of all isoprenoids.
EC: 2.7.4.26
Catalytic Activity: ATP + isopentenyl phosphate = ADP + isopentenyl diphosphate
Sequence Length: 258
Sequence Mass (Da): 28634
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A0A4Y6U7U6 | MPLPTTQQPAAATTTEGDGVIYALATGPVAGAIAVLRVSGQGCGDMLRHLCGALPPARMASLRSVRWRGELLDEALVLWFPSPRSYTGEDSFELHLHASPAIMARVAEALEGLGARQAEAGEFTRRAVMAGRMDILQAEAIADLVAAETESQRQQALRQKEGVLGQLYERWTEQIKSLLASQEALIDFADEELPPETEQRLQQALHALASEMDAHLSNPLGRLTREGLHVVLAGPPNAGKSSLLNALTGDDTAIVTAVPGTTRDLLHADIVIEGMKVRLTDTAGLRTTTDMVEAEGVKRAKHALEGADLVLRLVPPQAAQHKGSQVEAAEDGDNHFPPERTIMVMSKSDLRPAAPPPPPHALSISTVTPGGLEGLKQCLAQRVRALGAQHQASALLTRARHQAGIQAAKTHLLQAASAPLPELRAEELRMGMEAIGRVTGRVGVEDVLDSVFSSFCIGK | 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: 459
Sequence Mass (Da): 48887
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X0REW1 | MSNRTDLPSNDEDNAKNMTENTELNQNQDNIDTTNDGINQAEDITVDNDMAIEEFFAPSSHAGIADDFKAGYVAIVGRPNVGKSTLMNHLLGQKLSITSRKPQTTRHRIHGILSNHEMQAVFVDTPGIHRNEVRAINERMNKAAVSALVDVDLVLFVVDSDQWRDDDLLVLQKLGDTNLNVVLVINKSDTLKDKGSVLPLIETFNDSFDFADIVPVSALKNQNLDRLQEVIASHLPIAAPIYDTEQITDRSERFLASEIIREKIMRSAGDEVPYDLTVQIDGFKDEPAHTDPKTGRPRKACTFIDATIYVERSGQKAIVIGDKGQRIKQVGMDARKDMEQLFDKKIMLTLWVKVKRGWSDDERALTSLGY | Function: An essential GTPase that binds both GDP and GTP, with rapid nucleotide exchange. Plays a role in 16S rRNA processing and 30S ribosomal subunit biogenesis and possibly also in cell cycle regulation and energy metabolism.
Subcellular Location: Cytoplasm
Sequence Length: 370
Sequence Mass (Da): 41447
Location Topology: Peripheral membrane protein
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A0A1V5WMJ1 | MDILSEQGATYDECLARIREKFGPDVHVLRQKKVKIGGFLGFFEKDGIELYFMLSKNPYRQTIAQNPSSTNFNDERKRILQQAIKNAPSLAGRIPEIPAEPTRQSEEANAAVRGRDQLETILKTVKKLEQRLDKSDMDDADKAGEHETISKIEMLLENNDFSSSYIRKLLTRARNEFTLEDLDNYDLVQETIVNWIGESIQIAQNRSTVRPRIIALVGPTGVGKTTTVAKLAAAYSLAAAKGSRPLNVRVITIDNYRIGAKQQIEIYGNIMNIPVSCAETPSDLQTLVAMYQDVDVILIDTIGKSPKDFSRIAEMRHFLDAAGHCSDVYLALSATTKSSDMREIMQQYETFGYGSVIVTKFDETTRVGNIVSALDEKKKPVAYITTGQRVPLDFEQAAVVRFLTSLDGFRINRARVEERFPVTETTFEWR | Function: Necessary for flagellar biosynthesis. May be involved in translocation of the flagellum.
Subcellular Location: Cell membrane
Sequence Length: 430
Sequence Mass (Da): 48420
Location Topology: Peripheral membrane protein
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A0A522US76 | MKEWLLKKRWRIILSGTLIVTIPLIVLSTYIYLKVTSVLEERLLKENERLAQFTAHTIEEKLRAEIAFGKSYAARPYFLEGLIGGNKKEIRRHLMSLIENSNTIERVFITDHSGAQVDNYPFTPETIGKTFSARDWYKGLSKNWTPYVSEFYMRTAKPQRYLFAIAIPMRYNGKIVGCLVMQPRDDFIKNAVGSVDLAEALQEHMHIGHIYVVDRKGNLVYHPDYKMDRIIDFSNVPPVRNVLKGMEGIEKMIGPVHKLPVLAAYHPVSGWGWGVVVEQQSAAVLAPARKIRLALFIITGFMLLLGGFIAYKASALLASVKMAEENLAVTLHSIGDGVLVVDVDQEIVRLNPVAEQLTGWTEAEARGRKVEEVFRIISEETRLPAAIPIEEVLSTGLITGLANHTVLIARDGTERPIADSAAPIYDRSNEMFGVVMVFRDVTPERDAEKSILKASEQAEAANKAKSDFLANMSHELRTPLNAVIGFSEVLQDEMFGTLNEKQKEYITDILVSGRHLLNLINDILDLSKVEAGKLELELSTFPLKDALNAALCMFKEKAMKHSLKLDLEIEPEAEIEIEADERKLKQIMFNLLSNAVKFTPDGGSVSVQTRLISDVGAIRRVAQEEGRGSASPRQDSDFIEISVTDTGIGIKPEDIPKLFIEFSQLGSAYTKEYAGTGLGLVLTKRLVELHGGMIWVKSESGKGSTFAFSLPVRQASKPLPFAEEHLQMEKKPMTGKRTLIIDDDPKTIELMQKALMTEGYTVLSAPEGKTGVMLAKQEKPDFIVLDLLMPRMNGFETVEALRNTPDTASVPIIILTGMDLSLADKNKLKDQVQRIIEKGHLDKKQFVEMVKETIEGITS | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 859
Sequence Mass (Da): 95874
Location Topology: Multi-pass membrane protein
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A0A2W6CU62 | MAISLGYNQYGKAEVRLVHIDRSTSVHQIKDVNVTSQLTGDFTATHLTGDNSAVIATDTQKNTVYALARLHGVGPIEEFALRMARYFVDKYPQVKGSRQEVEEYSWNRISSAAGGPHDHAFTRGSAEVRTTVVTKHGAGEAIISGLRELTVLKSTGSEFHGFPQVEYTSLIETSDRILATAVCARWRYLGVEHVSIQGS | Pathway: Purine metabolism; urate degradation; (S)-allantoin from urate: step 1/3.
Function: Catalyzes the oxidation of uric acid to 5-hydroxyisourate, which is further processed to form (S)-allantoin.
EC: 1.7.3.3
Catalytic Activity: H2O + O2 + urate = 5-hydroxyisourate + H2O2
Sequence Length: 199
Sequence Mass (Da): 21838
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A0A532U2G8 | MYEKKGEQRMSGYFPREFLTQVRGAADIVEIVSSYAKLRHQGKNEVGLCPFHSEKTPSFTVSREKQLFHCFGCGAGGDVIKFTMLIENLSFYEAVKFLAERCGLRLPAPRKSPDQRDRRKEQLLKVNELALRHFVHNLHQEKEGSRGLSYLRERGLNRETAESFQLGYARSQWDDLYRFLLQQGVEEPTLIDSGLVAKSTQGEGYYDFFRGRLIFPICNSAGRVIGFGGRAIGEEEPKYLNSPETMLFNKSWSLFGINLTHQDIRRKNRALLVEGYFDLMTLYQAGFTNSVAPLGSSFTEGQAKMLSRYTKNVVISFDPDEGGRRATHRAITTLLNQGFRVEVKRLPEGLDPDAFVQKHGPQGFKEELDKALPAIDYLMEETKEMVDLSHPQGRVTALNFVIPFLACIGNQMERVSYVGYLAERFQVEDRAILAELRRAVRGRKSSLGEELTSMKASLKEAEARLLQILICQPEVRDELLPLIDPHCFSQPIGERLLAIIRELHQEGKGVTFDQIFDRLEEGDKSRFTHIALGDNFNWNKEFALECLNAMKRDYLDKEIRGVQQEIERAEADNAPELNRLLQAKLRLLQQRDAL | 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: 594
Domain: Contains an N-terminal zinc-binding domain, a central core domain that contains the primase activity, and a C-terminal DnaB-binding domain.
Sequence Mass (Da): 67885
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A0A2X1XRB5 | MIDYKRDYQFDYFGYKTLERSYLLKVKGVVVERPQDMFMRVAVAVAGDDLEEIRELYDLLSLCYYTHATPTLFNAGCKMQQLSSCFLLAMQEDSINGIYDTLKDCALISKSAGGIGLHIHNIRATGAPIIGTNGVSNGIVPMLKVFNETARYVDQGGGKRKGSFAVYLEPWHADIESFLDLRKNHGKEEFRARDLFLALWVPDLFMERVETDAEWTLFSPHNTKGLSDLYGAEFTQKYQEYERMGLGVKTIKARQLMTQNH | Pathway: Genetic information processing; DNA replication.
Function: Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.
EC: 1.17.4.1
Catalytic Activity: [thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-diphosphate
Sequence Length: 261
Sequence Mass (Da): 29769
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F4LRH3 | MSKPGILYLCPTPIGNLEDITLRALKILKEVDLIAAEDTRVTIKLLNHFEITTPLTSYHEHNKMTKGPKVIELLKEGKDVALVTDAGTPGLSDPGEDLVKDAIEQDIRVVPLPGAAAAICALVASGLSTKRFAFEGFLPQKTKEKKQTLKELADEQRTLIFYEAPHRIIKTLKALKDALGNRQIVIAREMTKVHEEFIRGTIEEVIERFHVKSPRGEMVIVVEGAHSGQKSAKTSVDGISEPELSESHLADKLWLIMQNEMEEGLSKNQAMKRAAKQLGLSRNQAYELLIKKSDAKEKQT | Function: Catalyzes the 2'-O-methylation of the ribose of cytidine 1402 (C1402) in 16S rRNA.
Catalytic Activity: cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = 2'-O-methylcytidine(1402) in 16S rRNA + H(+) + S-adenosyl-L-homocysteine
EC: 2.1.1.198
Subcellular Location: Cytoplasm
Sequence Length: 300
Sequence Mass (Da): 33306
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A0A3M1QFP0 | MESPTLETAAPLAADPRPDLVGRTREELTAFAVEHGMRPFRGQQLTEWLHRHAVVDFAAMTNIARADRERLARIARIGRLRPVREERSADGTRKFLFALEDGRTVETVLIPDEERRTLCISTQVGCAMGCRFCLTAQQGLERHLTSGEIVGQLLEVQRLTGERVTNAVFMGMGEPLHNFEAVVRAVQVLTDDRGVGLSARRLTVSTCGLVPRIRELTERREVRFALAVSLNATTDAQREEVMPVNRRYPIRELVAAIAHYARVRRDMGFVEYVLLGGFNDTPEDARRLARLLRPVRCKINLIPYNAVEGAPYAAPTEEAVETFRRILLDAGYSVFTRKPRGRDIRAACGQLRQAQAAPSTQP | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs.
EC: 2.1.1.192
Catalytic Activity: adenosine(2503) in 23S rRNA + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2-methyladenosine(2503) in 23S rRNA + 5'-deoxyadenosine + L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin] + S-adenosyl-L-homocysteine
Subcellular Location: Cytoplasm
Sequence Length: 362
Sequence Mass (Da): 40579
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A0A1V5CIA6 | MNDFTYKDGTLHAEDISIEKIAKTAGTPLYVYSYATLKRHFLVFDRAFARIPHITCYSCKANTNIALLRLMAGLGGGADIVSGGELFAALRASVPPERIVYSGVGKTEEEISYAVKTGIAMINIESEGELQLIAAIGKKMRKAVPVSIRVNPEIDAKTHPYITTGLRRNKFGILWADARRLYDEIKKSEYLTPVGISSHIGSQITEIPPFIEAVRSLKKMVSELASSGIALHYMDIGGGLGITYRDELPPHPEEYAGAIEKELEGTGLTLILEPGRVIVGNSGIFVTKLLYVKKTPEKTFYVVDGAMNDLVRPAFYDAYHEILPVVPGKKKKIKVDVVGPICESGDFFAKDRKLANVEPGALLAVMGAGAYGFTMSSNYNSRPRVPEVLVKGEDFFVIRKRETHRDLVRGETIPGFLEV | Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; L-lysine from DL-2,6-diaminopimelate: step 1/1.
Function: Specifically catalyzes the decarboxylation of meso-diaminopimelate (meso-DAP) to L-lysine.
EC: 4.1.1.20
Catalytic Activity: H(+) + meso-2,6-diaminoheptanedioate = CO2 + L-lysine
Sequence Length: 419
Sequence Mass (Da): 46029
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A0A1I2XVT8 | MNITAKIPVAILRALEKVPDLYLVLSPDLEVLTASDALLNAMSASRKSMVGKSVVDIFTSTDATAPDDVEALVHDAVQKALSQEESQHISLLQSRTAQPWQVQSSPVTDEAGAILYIILKLTPSGRQEHETLPNTADKYHTLFNSINQGFCILELYFDEHQRPVDYRYLEVNPAFKQQTSIKNAQGKTVRELLPGIEPFWIEQYGQVALTGKPIRLVEEVHSLGIWFDVYAFRIGNPDDRLVAVLFSNITEQREAEKALRESEDRFRTVVNLVPDLLWINGAAGAISWYSQRWFEYTGLTEQDLAGFGWLKVLHPDDQKHVWHNFEKAAEEAGPLRQEYRLRNAAGAYRWFLIQALPIKDTQGKALQWFGAATDIHEHKLAEEVIANHNALLEQEVSERTEAMQESRELLASVLENTSSNIMVLKAIRDSSGEISDFEYVLTNSNLLRGATRDSLVGRKFGEEALGVLPAALLANFKEVVELGQDWTGEAQVRFEHREVWSQVYARKFDDGVLVTYFDITQLKEAEQELRENTIFIEQIMDATPDFIMLFNLQTNKVDFVNRSAYLGNEPCFHETLTLDYAKILERAHPQDRTLLNRYIDRFRTAADGEIYSLEYRVLQEDKTTWYRTRGKVFKRDAAGKPTHYISVVQDISALKQLEAENNRMRLDQQKALLLAILQAQEEERRRISEALHNGVGQQLYAAKIHLDLLHGQRMAPDPKAAAALAQVDHILEQAINQTRSLSHELTPAVLGQFGLEAAFLDIGNSLSSKSLKLQCMVVNLPKELDKNLQIVLYRIAQELANNILKHAKATAASLLLRNEDDTLILTAEDNGVGFNPDKLPAKGIGLSSIQDRVKLLNGSCSLSSSPGQGTSVEVRLPLHPLSLQKV | 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 transfers its phosphate group probably to a conserved aspartate residue of NreC. NreB/NreC activates the expression of the nitrate (narGHJI) and nitrite (nir) reductase operons, as well as the putative nitrate transporter gene narT.
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Cytoplasm
Sequence Length: 886
Sequence Mass (Da): 99759
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M9WHX1 | MKLYDSLSKNLKNLDKKEITLYCCGPTVYNFIHIGNARPSMLMDIFVRFLRSIGYQVNYLQNVTDVDDKIITRAKQENTTEKDLSERYTKAYLQDLTSLNINHPDTLIPISLKMDGMIKFIQQLVDNNSAYIVDGDVYFDIDKYKQQYSKLSGFKLEELISGERVEIDSKKKNPLDFVLWKKTNLGVQWDSPFGLGRPGWHTECVLLIDEFFSGQTIDIHAGGVDLKFPHHENERIQFIAHKNKELANIWMHNGHLQIEDEKMSKSLGNVILVRDFVSQYNPNALRWIFLSSHYRAPLNINKDLINQAHKFIDKLKNLSKKIIDWSIKNDTDIQIINQSQYLDQFTSYMSDDLNTAMVLSLIESMIKEINKKVLDNQDIKLLVGSLKQIIDTLGFTDEIFNYQISQADKQLYIQWKNKLEQKDFLSADVLREHLIKKGIL | Cofactor: Binds 1 zinc ion per subunit.
Catalytic Activity: ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-cysteinyl-tRNA(Cys)
EC: 6.1.1.16
Subcellular Location: Cytoplasm
Sequence Length: 440
Sequence Mass (Da): 51197
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A0A6P3IEU7 | MSMKWLSLLPLLQLTCYFSSGTCGKVLVWPVEFSHWMNMKAVLDELVMRGHEVTVLISSASTITDANKPSAFKFEIFPVSLTKDDFENAIKNLIEKWTYMAKNSFWTNVSSLGELKSLIFEFSGMLMKICKEVVSKKKLMTKLQESRFDVLLADAAGPCGELLAEEMEEFVQSSGENGIVVFTLGSMISNITEEKVNVIASALAQIPQKVLWRYDGKKPDTLGPNTHLYKWIPQNDLLGHPKTKAFITHGGTNGIYEAIYHGIPMVGLPLFADQPDNIARVKAKGAAVRVDLETMSSRDLLNALKEVINNPAYKEKAMWLSTIQRNQPVKPLDRAVFWIEFVMRHKGAKHLRPAAHNLTWFQYHSLDVIGFLLACVATVVFVTTKCFLLCYRKFAKTGKKQKRE | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
EC: 2.4.1.17
Subcellular Location: Membrane
Sequence Length: 404
Sequence Mass (Da): 45575
Location Topology: Single-pass membrane protein
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A0A6P3HPI7 | MSVLLCCPKTLNFLFFQVNPSLISQLEQKDLSFVGQDVDGERMEIIELANHPYFVGVQFHPEFSSRPMKPSPPYLGLLLAATGNLNAYLLQGCKLSSSDRYSDASDDSFSEPRQAVILVQKGASQDSSHRIPGCSCLTGIVSRTNLTADYASGAEHCCSPGKAHPGSEVTEAKMKELSDEITTLVESLCSPPNMGCPASRGI | Pathway: Pyrimidine metabolism; CTP biosynthesis via de novo pathway; CTP from UDP: step 2/2.
EC: 6.3.4.2
Catalytic Activity: ATP + H2O + L-glutamine + UTP = ADP + CTP + 2 H(+) + L-glutamate + phosphate
Sequence Length: 202
Sequence Mass (Da): 21790
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A0A522B2V1 | MTRPARRPGGVFIAGTDTGVGKTIVTAAVAAALNAQGLDTGVMKPLATGSPDQAGALSDTDWLTSVAGLGDPPDLIAPYRFRTAAAPLVAAARDGRTIEPARIIEAFQALAARHDCVVVEGIGGVLVPITPDLFVADLAKQLGLPVLVVARARLGSINHTLMTLECLRNRGVAIGGLIFNHPSPAAAGTDESDTVPTILRLSGTRSFGELPHCEGLPASWIRHRDQLVARLDVQGLLETFGVRGLA | Pathway: Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 1/2.
Function: Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to form a ureido ring.
Catalytic Activity: (7R,8S)-7,8-diammoniononanoate + ATP + CO2 = (4R,5S)-dethiobiotin + ADP + 3 H(+) + phosphate
EC: 6.3.3.3
Subcellular Location: Cytoplasm
Sequence Length: 246
Sequence Mass (Da): 25527
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A0A1F9X1D4 | MKKNKVNVGLVGLGVVGSGVLELFLNNKKNIEQKTGSAIEITHICDSSVARLKESSKGLKVKTSSSWESVVKDPDVDIVVELIGGKGIAKTVIIQSLENGKNVVTANKAVLAENWDEIFNLARKKCKIVYFEASVGAGIPVVQALNEGLAANRVDYIVGILNGTTNYILSKMFKENISFEKALSQAQASGFAEVNPVFDIEGVDTAHKLSILSSLAWSYWIRPEKINREGISHIDPIDIKFAYKEFGYVLKLLGVAKRINNKVELSVRPSLIQKDHMFAAVENEYNAILLHGDASGEILLYGKGAGSGPAASAVVSDLMYLARQVAAGTAGQVPDVNNTSCNLLSFASQQERYGRFYIRVTAVDKPGVLAKISSILAKYNISIAGVFQKDPITSKKAYVPILMITHKLKESDLRKAVDEIDKLPIIKSKTVLIRIEEMAV | Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 3/3.
EC: 1.1.1.3
Catalytic Activity: L-homoserine + NAD(+) = H(+) + L-aspartate 4-semialdehyde + NADH
Sequence Length: 440
Sequence Mass (Da): 47865
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A0A7Y8LAB4 | MPVHVQSHVRRETFNQARLDQLARAILSNVGAASGELGILFVGDRRMRGLNRRYRGKDCTTDVLAFAMRESLTPHPLPFTPVMLGDVVIAVPTATRHAKQGQRSLNEELTVLLVHGILHLCGYDHERNEKEARRMHRRERMILQSLVRWPKLVEKSARTTNTRRGGGRERHDRQDPKNRLGTTGSPVSRMVTLHG | 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: 195
Sequence Mass (Da): 22162
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T0XV92 | MGNGDIYKIFRSKCKAFETISLRASPDESFRSPPKMPERDHRDHCLADPISYNMETILPLTPEQDFPINYGKDTLNQTTREPDISLKGLRHSAAHVLAQAVKRLFPSAQVGIGPATEEGFYYDFHFDRPFSPEDLEKIEAEMKAIIASRSPIVRRALSREEAGDLFSSKGEDFKLEILHGIPEEAEITVYDQGDFTDLCRGPHLSDTGEIGAVKLLSSSGAYWKGIESNPSLQRIYGTAFPTQKELDDYLERLEEIRQRDHRKLGKELGFFRTLDEKGAGMVLWLPRGARIRRVIEDIWKIRHDRHGYQYVYTPHIARLDLWKQSGHWDFYRDSMFSPMEIEGSEFELKPMNCPFHILISRESIQSYRDLPVRLAELGTVYRYERSGTLHGLLRVRGFTQDDAHIFCRPEDIATEIGKVLKLVDEMLLPFGFTNRSVYLSTRPEGSVGSDENWELATRALEEALRTAGIPYEIDPGEGVFYGPKIDMKFHDVLGRTWQLSTIQVDFNLPEKFDLTYRDASGKDVRPIMIHRALLGSVERFFGILVEHFKGAFPLWLAPEQVTILTIGRPAYSLCRENRPLPRGFGAQGVDRLQE | 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: 594
Sequence Mass (Da): 68007
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A0A2N1QW65 | MIRGIGIDVCDISRMRKAVSKEGFCKRVFSKEEIAYAESNADPAAHYASAFAAREALSKATGWGIAGLGINSCSIERTASGPRFIFDENTLSKFSNEGIDNIFLSISHEAGIAVAVVILEKNQ | Function: Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.
Catalytic Activity: apo-[ACP] + CoA = adenosine 3',5'-bisphosphate + H(+) + holo-[ACP]
EC: 2.7.8.7
Subcellular Location: Cytoplasm
Sequence Length: 123
Sequence Mass (Da): 13230
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A0A2S6SXQ6 | MIVIGLTGGIASGKTTIMNFLKKKKFAVHDSDAVVKKIYSKPEPKFLSYLKKTNLKNSIKGNKIDKKTIREEIFTNTEKRKLLEKYLHAKVKKSRDIFLKKNRQKKTQIVFLDIPLLFENKLEKICNYTILFYASLKIRKQRAIRRRGMQKRILVKIIKSQLSDKIKKKKADYIINTSASKDWCFNKILKTIEQIKDK | 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 Length: 198
Sequence Mass (Da): 23266
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A0A2N1V5H6 | MNKNRNKGKVLEKEIKQLDECTRELTITLTTDELQPHYEKAYKAMQPKVKQTGFRNGRVPIAMIKKMYGPGIEADADQDLVNDVFRNYTQEENIQVLGTPTLKDIAKDENGIKYVIEFETLPKITLKDYKGVTIDEPIHAVTDQEVQEELEYILAQNGELDEAEQVTDEHHVIKVEMSEILEDGELSEPNETDVYLADKNILPELKDNILNTKVGDSFDYTPTAADANPTIKDKNFKVTITKIQKLTPAELTDEFVERVTGGRITKADELKDEVNFNLQDEWDRKSRELVENQIVASLVDSNQIPAPEQLVNQVLTQMVQDVKQRYEKSPEQLNMADDELETQLRPNAERSVKWELVRNQIIENESIELEDYDIDPIVEKEAKRYGQDVEQMKKILVQNPNFLTKILSKKVIDFVLDFAIINEVDFETHERIED | 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
Sequence Length: 434
Domain: Consists of 3 domains; the N-terminus binds the ribosome, the middle domain has PPIase activity, while the C-terminus has intrinsic chaperone activity on its own.
Sequence Mass (Da): 50039
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A0A7V0JAQ6 | MQKRHNMNILITSSEAVPFAKTGGLADVIGTLVNELKAIGIGSTLILPLYRHIKQSANYLDIKPLDKVISVPLGGRTVKGRLWSGKTLGGADVYFIENDNFYDRQELYGTSEGDYPDNASRFIFYSRGVLETILQLGLKVDVIHCNDWQSGLIPVYLKTIYQKKLAATATVLTVHNLGYQGIFEQSEFPLTGLSNPDGLKFYGKINMLKAGILFADAISTVSGNYAREILTREQGSGLDSVLRLRSDDLYGIINGIDYTDWNPADDAYIQANYTVEDLSGKTKCKEALQRLIGLPKSGSMLIGMVTRLSSQKGLELVGKAMKEIVRSDIQVVILGKGDESLQQGFLKLHKRYRDHLSITTRFDNELAHKIYAGSDIFLMPSRYEPCGLGQLIALRYGSVPVVRKTGGLTDTIREYDPANGTGTGFLFNKYSSGELVKKVKFAHKIFHDTALWRKIRKNAMSQNFSWRKSAEAYISLYQKTLKKKEQKDAGTYRK | Pathway: Glycan biosynthesis; glycogen biosynthesis.
Function: Synthesizes alpha-1,4-glucan chains using ADP-glucose.
EC: 2.4.1.21
Catalytic Activity: [(1->4)-alpha-D-glucosyl](n) + ADP-alpha-D-glucose = [(1->4)-alpha-D-glucosyl](n+1) + ADP + H(+)
Sequence Length: 494
Sequence Mass (Da): 55145
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A0A7C0UEN7 | PQLFLYSQILIALSKNEAKYATTGTPMEFWAFWKEQKDVENKVRDIINTPLASEKKDRLFRDRFKYVRKYFDALEAEGGREVTEQDRVVHALCRPERLLDLTFHYILFDAGEKKIARYQQYFCVKKIMDRITTIDNMGKRLGGVVWHTQGSGKSLTMVMLAKAIALEPTIDNHKIILVTDRIDLDDQIYRTFHHCGKELEQARTGKHLLELIGGHKERIITTIIDKFDAAVGAKDVKNADPNIFVLVDEGHRGQYGPLHAKMKKVLPNACYIGFTGTPVMKKHKNTVATFGGLIDSYTIDQAVEDKAVVPLLYEGRHVEQKVDSESIDIWFEKITEKLSKEQAADLKKKFATTDQLNKAEQKVMRIAWDISEHFRDNWQSTGFKAQLVAQDKATALMYKKYLDEFGMVISEVLVSGPDDREGEEDIYKENKEGIIRFWKVMMDKYGTEKEYNRQIINAFKYGEIPEIIVVVDKLITGFD | Function: Subunit R is required for both nuclease and ATPase activities, but not for modification.
EC: 3.1.21.3
Catalytic Activity: Endonucleolytic cleavage of DNA to give random double-stranded fragments with terminal 5'-phosphates, ATP is simultaneously hydrolyzed.
Sequence Length: 479
Sequence Mass (Da): 55179
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A0A662RWC5 | AAAEMESRIKEVKAAGDSVGGIVEVIALNVPPGLGEPVFDKLDADIAKAMMSIGAVKAVEIGAGFKSVRMLGSEMNDEFFITEGKVRTKTNNAGGILGGISTGEPIICRIAVKPTPSISKQQRSINMRSMEEVSIKIDGRHDPCICPRIVPVAEAMLAIVITDHLLRSKISRL | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7.
EC: 4.2.3.5
Catalytic Activity: 5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate
Sequence Length: 173
Sequence Mass (Da): 18382
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A0A7X8ETU8 | MIYSDYHLHTNFSSDSDTDMEKMILQAIQLGLKEIAITDHIDFDYPDPEFPFLFDYTDYAKKIQQYQQLYGDTIQIRIGVELGLQAHIKESINEFCQKNTFDFVIGSTHCIKRLELYHN | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 8/9.
EC: 3.1.3.15
Catalytic Activity: H2O + L-histidinol phosphate = L-histidinol + phosphate
Sequence Length: 119
Sequence Mass (Da): 14033
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A0A7V0WC07 | MCTKLVNASLKRQGMSDIRESFNNEIGTDFRGEIMYGEMLSGHTSIAVGGPADMYVLPYDAVSLKTCLMFANDRGLAVLVLGGGTNVIVDDNGYRGMVISLKHFNMIKTTDDPDERVDLFVETGVPLQRLINYCIERGYAGIEGLTGIPGTVGGAIIGNSGSFGQEIRDVVESIVVINLSGMIKRLERDEFSFGYRRSSVEQGLIILSANMRFKKSEPEVLSGKASECISRKKNTQPLSERSAGCVYMNPEGRAAGMLIEEAGCKGMRAGDIEVSRVHANYFINRGNGTASDFLKLMKMVEARVFEHSGVSLEPEVRVIAGKHE | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation.
Catalytic Activity: NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
EC: 1.3.1.98
Subcellular Location: Cytoplasm
Sequence Length: 324
Sequence Mass (Da): 35324
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A0A972R0T2 | MVSLRNKIITVMVVVILLFGLGMMLFTQIKLTRILTQERQHWGIIVSQDISLRSVDFLLKGDLPGLQRFIEDVESKHAEHFAYIFVVDKEGRVLAHTFKEGFGEELVRANKISPDQSSNIQLLETKQGWVYDIAIPIFKEGGVIGTTRVGINEKYIRKAVTNIVGAVMGVTALAMGIGIVVALGLASFITRPLSELTEAARAVGGGDLERQVDIRTNDEIGQLGKIFNQMTADLRKATELTATVTQNLMEGVMLLSKDFRILWANKKIKEFSGLEEKDIIGNFCYRVTHGRKDPCQPPHDVCPVNKLMETGKPTVELHIHFDKEGNEHHVEVTVEAVRDEKGDIVQFIHVTRDVTEIMKAKKELEKAYEEIKELNAGLEQKVEERTRALKQAQAQLVQSGKLAAIGQLGAGVAHELNNPVGGILGYAQYLQDKINKPGFQGEDFKTCKKYLGYIEKEAERCKTIVENLLKFSRRSPERFEPLNINQVLEDTLAITAHQLMMKKIKLKKELASHLKPVEGNANQLQQVFINLILNAQQAMTEGGELTIATRLKVKSQKLEVRDEKCLPETNFVEIVFRDTGCGIPPENLDKIFDPFFTTKMDWRGTGLGLSVSYEIVQHHKGWIEVESEVGKGTTFTISLPVKA | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 643
Sequence Mass (Da): 72049
Location Topology: Multi-pass membrane protein
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A0A2N2E481 | MKLRLAGILSESIVDGPGVRFVVFAQGCLHHCPGCHNKATWDTKGGEVATVKEILKKIKRRVKYIRGITLSGGEPFLQAEEMAQLAYAARKLGLDIITYTGYVYEELLQIDLPGSKDLLGATDMLIEGPFILAKKDISLQYRGSSNQRIIDLSKNKEQRQACNISYMTMLYSS | Function: Activation of anaerobic ribonucleoside-triphosphate reductase under anaerobic conditions by generation of an organic free radical, using S-adenosylmethionine and reduced flavodoxin as cosubstrates to produce 5'-deoxy-adenosine.
EC: 1.97.1.-
Catalytic Activity: glycyl-[protein] + reduced [flavodoxin] + S-adenosyl-L-methionine = 5'-deoxyadenosine + glycin-2-yl radical-[protein] + H(+) + L-methionine + semiquinone [flavodoxin]
Sequence Length: 173
Sequence Mass (Da): 19243
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A0A3M2CXS3 | MNRRQLLNVQPLCGSRRQLIVTIDGPAGAGKSTTAKALAARLGYTYLDSGALYRAVAWKMALRGIDPIDEREVRDLLATTTIRLSKTNDHLSVMVDAQDVTDNLRAPDVGRLASVVATNPLIREWLLPLQQEWGRRGGLVAEGRDMGTRVFPLADVKFFLDADVEIRAQRRLKDETQGAGSQSLDAVRADLVERDVRDSSRDIAPLYPASDAIMIDTSTRSLEQVVEEMVAAIAARQ | Catalytic Activity: ATP + CMP = ADP + CDP
EC: 2.7.4.25
Subcellular Location: Cytoplasm
Sequence Length: 237
Sequence Mass (Da): 26082
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A0A972H3R2 | MKRVKLKLCYDGSGFSGWQIQPDAVTVQGVLEEAIERVTGQRSRVTGASRTDAGVHALEQVAVFDTESALPPLVIVRALNANIPVQVRVLEASYVDGDFHPRFSARGKIYVYIIENSQIRSPFLVNYAYHNPRKLHVDAMKEAASYLIGRHDFKSFQGSGCSARTTIRDLRKLDIQIVSEVGFGPVRLTGRFILFEFEADAFLRYMVRNMVGTLVEVGLGKLRPVDIKEILRACDRTRSGPTAPGQGLYLKKILY | Function: Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
EC: 5.4.99.12
Catalytic Activity: uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA
Sequence Length: 255
Sequence Mass (Da): 28490
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A0A3M1XPE6 | MRGPERYLKTKVNYYPIFLDLRDRLVVVVGGGKVAERKVRGLLEAGARVRVISPELTEGLRRLVQKDKIEHIGRDYQRGDLKGAFLAIAATSDMEINRAVSADATSIPVNVVDVPELCSFIVPATVKRGELCIAVSTSGASPKMAGSIREELEEMFKEEVAEFFSLLKELRERLKETALEPSAREGLFKELGSRRVLRVLLDAGMDEARKEIKRVLSKWGQDEIGKSL | Pathway: Porphyrin-containing compound metabolism; siroheme biosynthesis; sirohydrochlorin from precorrin-2: step 1/1.
EC: 1.3.1.76
Catalytic Activity: NAD(+) + precorrin-2 = 2 H(+) + NADH + sirohydrochlorin
Sequence Length: 228
Sequence Mass (Da): 25441
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A0A3M1G1B7 | MSEIIEQLIQKNQTKILMVVLDGLGGLPLNGKTELEAAKTPNLDSLAKQSAIGLHIPVSYGITPGSGPGHLGIFGYDPLKYQIGRGVLEALGLGLKLTPNDIALRGNYATKKDGLIVDRRAGRPPTEESRKLTEALQKAIPEIDGVEIIFAPGMEHRFAAVMRFPEALPEEAAEVSDADPQKEDLPPVPPKALNPKAEQVAEIARKLIDKAEEVLKDQPKANTLLLRGFSKVPHIPGFMERFGLKALAVAVYPMYRGLASLVGMDTPALQGDIKEQLQMLKEHWHEYDFFFVHVKKVDSYGEDGNFEAKVKKIEEFDSYLPEFLALEPDVLIITGDHSTPAVLKSHSWHPVPLLIKGPYVLGGTSDGFSERECLKGELGILPAIHILPIALANAGRLKKFGA | Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.
Function: Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
EC: 5.4.2.12
Catalytic Activity: (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate
Sequence Length: 402
Sequence Mass (Da): 43900
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A0A7V1I002 | MKITGGAKAKSVEAMFSSIAHRYDFLNHFLSLGFDITWRKKAIACFSDLRGKKILDVACGTGDLAITIAKAGDETTRITAGDFSREMIEIGKTKIKEADLDSAVTMEFSDALNLTYHDNSFDGVTCAFGVRNFAGLNRGLSEMTRVLKPGGRMVILEFTQPSNPVFGALYKFYFTQMLPAVGGLLSGNKDAYKYLPDTVYQFPAPDKLSAMLEGLGLERVEFNPLTFGICGIHTGIKK | Pathway: Quinol/quinone metabolism; menaquinone biosynthesis; menaquinol from 1,4-dihydroxy-2-naphthoate: step 2/2.
Function: Methyltransferase required for the conversion of demethylmenaquinol (DMKH2) to menaquinol (MKH2).
EC: 2.1.1.163
Catalytic Activity: a 2-demethylmenaquinol + S-adenosyl-L-methionine = a menaquinol + H(+) + S-adenosyl-L-homocysteine
Sequence Length: 238
Sequence Mass (Da): 26052
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A0A4U0VQW4 | MSSINEPKTAVSDALAGLGFLNPHTKVVNRTTLILRQPAPDRVHLLCGGGGGHEPAHAAFVGQGMLSCAVSGQIFASPNAAQVEDALARLDLAGQSRGTLIVVKNYTGDVLQFGLANERWAATHLATSEDGQGSTQPHQVRLVVVGDDVSVPREQGALTGRRGLAGTVLVYKLAGALAADDGSSPSLDEIEHLARTVAESCGTMGMGLEHCHVPGTDKAEAYLGENEAEIGMGIHNEPGIRKVSPVPSAAKLVDEFLSTITSTTDSERSYLPFKNDGQDEVILLVNNLGGLPEVELSIVAKEAAEWLKRKRIIVRRAIAGSFMTSLNLPGFSLTLLLLPREPVPLPPSAAASSSSFAVTSDLLVELFDAPTEAPAWKWSFKGEPEMLVEEGEKEGKKRKEGSVGEKESRVKGPRPSDPKLFLAALESALKSVIAAEPEITRYDTIAGDGDAGLTLKAGAQGILDAISENRIPDDDVVAAMVACSEVVEREMGGTSGGLYAIALSGLSKGLVEAAKDKESEVATAEVWARGLELALNTLYRYTRARPPSRTLVDPLSSFILTFASDPSRLSHAIKAAQEAAEATRDLDAKAGRAAYVDQDKIREASVPDAGAWGVWKLLEGMQKALLLRVEYDPYERETDEDEEYDFDYEPDPVEVFIRTVDIKIINQAGKQVGRALFWLIDRDDLVEVGENFVALLDDHSSELSDFAATLFDGRGRIKSSVAREGEEVWGRELDADATVAYLQEFRVDKDLRSQGIGRWALGEILKHTDVYIDGVQFVYTFPCAINSEWPRPASWSEPDPYVAEKEAVTVRLVGFYRRLGFRRVGTTAYFCCAHSLLHPSHAVPANQDADRVKPADPFAEMDPTMARTMTVLSRQNLI | Pathway: Polyol metabolism; glycerol fermentation; glycerone phosphate from glycerol (oxidative route): step 2/2.
Function: Catalyzes both the phosphorylation of dihydroxyacetone and of glyceraldehyde.
Catalytic Activity: ATP + D-glyceraldehyde = ADP + D-glyceraldehyde 3-phosphate + H(+)
Sequence Length: 878
Sequence Mass (Da): 94955
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A0A944D3N4 | MHNLWLIVGLGNPEKKYDRTRHNVGFRILDALASDFREEKKFNALVTKRDNIIYCKPLTYMNDSGDAVQPLAHFYDIPVERIVVIYDDKEIPFGTLRLRSSGSDAGHNGIKSIIERLGSKEFPRIKIGVGMMPEQWDAADYVLAPFTADEEKVLPEILQAAEEAIRDIVVRGLNPQTHRDITVQSEK | Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Catalytic Activity: an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+)
EC: 3.1.1.29
Subcellular Location: Cytoplasm
Sequence Length: 187
Sequence Mass (Da): 21263
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A0A8C0BRB6 | VPGTAGCQAARGGASSAPAPLSPGASPGAGLVLQGTFPHGQRRESFLYRSDSDYDLSPKAMSRNSSIASDLHGEDMIVTPFAQVLASLRTVRSNLTHLQDRTPR | Pathway: Purine metabolism; 3',5'-cyclic AMP degradation; AMP from 3',5'-cyclic AMP: step 1/1.
EC: 3.1.4.53
Catalytic Activity: 3',5'-cyclic AMP + H2O = AMP + H(+)
Sequence Length: 104
Sequence Mass (Da): 10891
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A0A944D3Y2 | MKYLGIDFGTKRTGLAIAPDGRVAVLKETIRSQSQNATIKRVKEIVENDAIECIVVGHPLHLDSSHTEMTEQVERFVEKLRNHVSVPVQLFDERMTSEMAATLLRGVKDAERDQVAAQIVLQNFLDQLPKE | Function: Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
EC: 3.1.-.-
Subcellular Location: Cytoplasm
Sequence Length: 131
Sequence Mass (Da): 14753
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A0A9D6QUB1 | MKPSNPTGLYLILDHDLLAGRSLTDIAAQAMAGGVKSIQYRAKNLSKREAYFNALQLRALSRQSGVTFLINDGVDLALATEADGVHLGQEDLPLSAARALLGSDRLIGISAHTLEQAKEAEAGGADYLGIGPIYSSTTKQDRPPLGCEALKQFRKHVRIPLVAIGGISPLNVRQVMTTRVDGVAVVSAILSRSDVTRATADLVAILQTRRI | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)-thiazole: step 1/1.
Function: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).
EC: 2.5.1.3
Catalytic Activity: 2-(2-carboxy-4-methylthiazol-5-yl)ethyl phosphate + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 2 H(+) = CO2 + diphosphate + thiamine phosphate
Sequence Length: 211
Sequence Mass (Da): 22480
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A0A497IPQ1 | GLKEALDPDLADKLFDLISSRSCDEISEIIGETPELDHLRKVLLLLDCYGVEYQLNPGVARGLEYYTGIVFEIYAEGLGAENQVCGGGSYRLIPLFGGPDIPSTGFAIGFDRIMEIFEPEVEKKLRIAVVPTDDVREEGVRISKILRTRDKTYLDIMGRNLKSQLNFADKWNADYAIILGSKEVAAGKVTLKSLAKGEQQTMTFDECLEILDQNA | Catalytic Activity: ATP + L-histidine + tRNA(His) = AMP + diphosphate + H(+) + L-histidyl-tRNA(His)
EC: 6.1.1.21
Subcellular Location: Cytoplasm
Sequence Length: 215
Sequence Mass (Da): 23869
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A0A081NHY1 | MEPPGIQLIDILSVTIPSTVVGLSLAVLITNKLGNELSDDSQYQKKLEDPECRKNLSCSVDAPGGRPGIAFRFTDSNVPCCEWVFFCAQLRTDHYGPIIASLDFDRTGTIRIGRYVLNHSFMLPGLMSISFSVVVGFFVVDLVL | Catalytic Activity: (S)-malate(in) + succinate(out) = (S)-malate(out) + succinate(in)
Subcellular Location: Cell inner membrane
Sequence Length: 144
Sequence Mass (Da): 15827
Location Topology: Multi-pass membrane protein
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A0A9D5ZZ26 | MQLNVLENYPLSELTTFKIGGAARFYVKAESLISVFESIEFAKLNSIPFYVLGGGSNLLVSDKGYGGVVIHMSNTDSETISDGESVYKTCGAGVLWDNFVSECVSENLFGVECLSGIPGTVGASPVQNIGAYGQSVDNLISEVIALDANTGEVVKFNNAECKFSYRKSLFNSEGFGRYIIISVKYILKRVGKPNVKYHDLEKYFLKDIDITLKEVRTAILKIREYKGMLQMEGYRGFKCAGSFFKNPVVSAGHFDEILDGLNGAKSDRNWYWPQADSEVKISAACLIENCFGKGYRAGRVGLSPNHTLAIVNYDSATFTEVMDFAKLIEDTVYERFKVTLDREVQIL | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation.
Catalytic Activity: NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
EC: 1.3.1.98
Subcellular Location: Cytoplasm
Sequence Length: 347
Sequence Mass (Da): 38426
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A0A933FLT4 | MTTDAESAYAKAGVNYKGIDAFKRNCQAKGRLTDDNARRRGLEPMEWSRGETAAVKRLPDGTYLATVNEGVGTKPVATGDFYKLTGWSRYKEIAQDTAAAIFNDLVAVGAQPSGTMMHLAVGSSAFFDDEPRLNALIEGWFEACQTAGCRWDGGETSVLVDNVESPTFMLSGSAEGLIRNPRRLIKPAIEDGDAIVVLPSTGIHVNGLTAARKLADALPDGYRAKIDDGREFGAALLDATPLYGPLIENLQEAAVRIHYAVPVTGHGWRKLMRAQLDFSYVIEKLPPVPPVLQFMQRVQRLTDAEAYSTYNMGAGFVLFVPPSDVGIIRNVAALQGMTAMLAGRCVSSPGGKSLTILPLNVTYQGDSLDIR | Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 2/2.
EC: 6.3.3.1
Catalytic Activity: 2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ATP = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + ADP + H(+) + phosphate
Sequence Length: 371
Sequence Mass (Da): 40030
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A0A1E7LCN1 | MSFFASFVTELSDVLGPFFGSSATAAAIVAFTLCVRLVLHPLARAAVRGERVRARLAPRLAEARRRYGSDPQRLRRELEKVQAKEGASPAAGCLPTVLQLPVFFAMYHLFTTDESLLGHTLLGAPLGGRWRDALAAGGAFGDQGLVYVGLFVLVAAVATWTYVRTRRLMAASPASVPAGLSSSSGAPSPSVPGAAAMGRMLPLLSFGTLLTVGFVPLAAGLYVVTSTTWTAVERAALRAGRPAKQEEQAEEQAKGRGGGRRDGASGKPSRGRRSTT | Function: Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins. Aids folding of multispanning membrane proteins.
Subcellular Location: Membrane
Sequence Length: 276
Sequence Mass (Da): 28996
Location Topology: Multi-pass membrane protein
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A0A6N7ANJ7 | MQKNKLSSGRLNDNEIMQRLMHNVWDKKIIITPLISLKDQLGSNSLDLRLGTEFIVTERPNYTHIDPLDAKIEEQEIKFRLIKRLSPLKPFILHPREFALGSTLEYIKIPNDLVGHLEGRSTWARMGTLVHLTAGLIHPGSAGTITFELLNAGDVPIKLYPGIRIAQLVFYTLNEPLKSYEIKFGAKYSGNLRVSKPIYWNDMEIDILRDSRDKGKTNLENLKLKEMEIENRRLRFKSSGSGL | Pathway: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 1/2.
Function: Catalyzes the deamination of dCTP to dUTP.
EC: 3.5.4.13
Catalytic Activity: dCTP + H(+) + H2O = dUTP + NH4(+)
Sequence Length: 243
Sequence Mass (Da): 27837
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A0A0D0PTR3 | MTVTSDPGDRGHLAARARLLADPGPARTGRERRAALARLTDDWLTGLYRAAGAPAGTALVAVGGYGRGALSPRSDLDVLLLHDGPLAAEVAERIWYPVWDSGVALDHAVRTPDGARKVAAADLRAGLGLLDARHLAGDARLTADLRTRVLADWRAAAPDRLPELRALGRARAERHGELSFLLEPDLKEARGGLRDLVALDAVAASWLADAPRDGLDAAATTLADVRDALHLTTGRATDRLTLQDQDQVAERLGLPDADALLRQVYRAARTVAYASDVTWRAVDRVLAARTRRGRPFRMTRRAAPAERRPLAEGVVEQDGEAVLARAARPAADPVLPLRAAAAAAQAGLPVGHATVRRLAAETGPLPVPWPDEARDRLVGLLGAGEACLPVWEALDAEGLIGRLLPDWEQVRCRPQRNAVHRWTVDRHLIETAVRAAALTRRTGRPDLLLVAALLHDLGKGRPGDHSETGELIVRELAVRMGFDKPDTDTLALLVRHHLTLVDTATRRDPDDPATADLIAGIVGNRTHLELLHALTEADATATGPAAWSAWRASLVDQLVARTAARLTGSPPAAGGGPGDDAPGADGPTVEQERLAVEAARTGGPALALRAELAADGTESVGVELTLAVPDRPGLLGTVAGVLALHRLTVRKAGLRELDPVGTGPVLLLGWTVAAEYGDVPEAARLRADLRRALDGSLDVTRRLAERDAAAPRRPGIRTPPPVVAVAPGTASRSATVLEVRAHDAPGLLHRIGRALDTAGVRVRTAHVSTLGAEAVDAFYLTAEDGRPLAPERAQQVARAVQDALGTG | Function: Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen metabolism.
Catalytic Activity: [protein-PII]-L-tyrosine + UTP = [protein-PII]-uridylyl-L-tyrosine + diphosphate
Sequence Length: 807
Domain: Has four distinct domains: an N-terminal nucleotidyltransferase (NT) domain responsible for UTase activity, a central HD domain that encodes UR activity, and two C-terminal ACT domains that seem to have a role in glutamine sensing.
Sequence Mass (Da): 85228
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A0A7C1XUF7 | MDIRGYIERAVRELGAEVPFVELEVPRVAEHGDLSTPVAMVLAGRLRRPPREIAEEMASMLRAESPFERVDVAGPGFINFTFRRGFLYEGLRNLLGDPARCLRRDLGGGQKVQVEFVSANPTGPLHLGHGRGAAVGAALSNLLARAGYEVEREFYINDAGRQVRLLGESIFARYKELLGVACRFPEEGYRGGYVVEIARQLLGEAGDRFRDAGFEGEAAEYFVRFGVGRMLGVMKEDLGGFGVEFDRWQSEKALYDEGLVRRCLDELREKGMLYEREGALWFRATEFGDDKDRVVIKSDGSHTYFASDIAYHWYKIQRGFDELIDVWGADHHGYVPRIKAVIRALGHPEERLSVLLVQIVTLLRGGKPVQMSKRSGEFVTLREVTEEVGADTTKFIFLTRSHDSHLEFDIETAKKESSENPVYYVQYAYARINSIFRKARQQGVEPGGAVDLGCLKEEAEAGLIKKLLFYPLMFEGAVRAREPHRVTFYLQELAGLFHPYYNTHRVLGLDPSLTLARLALCEAVKRVLEEGLSILGVTLPERM | Catalytic Activity: ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg)
EC: 6.1.1.19
Subcellular Location: Cytoplasm
Sequence Length: 543
Sequence Mass (Da): 61164
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A0A7C3QET1 | MSSKIGFTLLEVLVALAVLSLALVILLGLRNRDVELVNTTRDLTTATALARMKMEETQMEGFPELGEATGEFGEGYPQFHWQRLVSSTPFDYVREVRVSVKWGQANPDGVELVKYVFQEQ | 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: 120
Sequence Mass (Da): 13479
Location Topology: Single-pass membrane protein
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A0A1E7GH93 | MIKILIYGCGGTMGQVLANMAQAASDIEVVAGVDPVADATAFPFPVYAELDSCDKTFDVIVDFSRPESLGDLLKGALKKKGPLIIATTGHTTEDKASIKTYAESLPLFQAANMSLGINLMSDLIHKAASVLGEHYDVEIIEKHHNLKKDAPSGTAYQLAETINQAFMNSKNYVFDRHTNTEPRSIHEIGIHAVRGGTIVGEHQVLFAGTDEILEIRHNAYSKQVFAAGALQAVRFMVGKSPGYYTMKDMIAEESTITHMYTSDEEALVSMDHIPYDPVKITRIFKTIGEQKINLDMISQTAPVQEKVSISFTIPRKDVEPTMAILKSFQSSWPKLQVDVLTEITKITVQGPGMEVQSGVAARVFEVMTSKGIALKAITTSETKISYIIPEKDRLVAIEAIKTTFGI | 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-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH
EC: 1.17.1.8
Subcellular Location: Cytoplasm
Sequence Length: 406
Sequence Mass (Da): 44414
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A0A7U7G633 | MAQEPASDTSRKQGPEEESGSRARKRFRLLTKGRVFALLLAAAGGTVFAGYGHYTDPGPLQTERVVVIPKGGTGRVIEALQENGILARGGVSSLFFKVAMYATRSQGAIHAAELKFPERVSMAHSLEILRHGHPVTHSLTVAEGLTAKRIRTLLMQAPALQGDLPTIGEGQVAPQTFFYVWGMERQALLHHMTELMGKTLQAIWDQRDQAALQGVITTPEQLLILASLVERETSLAEERPQIARVFLNRLKQGMKLQTDPTVIYGLSDGDGVLPRPLTHEDLQTESPYNSYLHPGLPPGPICSPGRESLEAAAHPASGNALYFVATGHGGHNFAHTLAEQTDNVRAYRRMKKAAAQ | Function: Functions as a peptidoglycan terminase that cleaves nascent peptidoglycan strands endolytically to terminate their elongation.
EC: 4.2.2.-
Subcellular Location: Cell inner membrane
Sequence Length: 356
Sequence Mass (Da): 38744
Location Topology: Single-pass membrane protein
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A0A1F9WZ29 | MIELKTKPEILILKETGDIVSEILSEIVSNIKPGITTKHIEEIADKLFKKNNVQPAFKGYLGYPGSICVSINEELVHGIPSRNKIVKDNDIVKIDVGIKHKGFYGDVAQTVSLGNTIKENKDLLQVTYDSFENIKKYANKYCKLGDISASVQEHVESYGYSVIRDFVGHGIGRNLHEKPEIPNFGKHSTGPNLMPGMVFAVEPMVTIGSWEVNILEDGWTVVTKDKKCCAHFEHMLAITENGCEMLTKITNKF | Cofactor: Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe(2+)-metalloproteases under physiological conditions, and the catalytically relevant metal-binding site has been assigned to the histidine-containing high-affinity site.
Function: Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed.
EC: 3.4.11.18
Catalytic Activity: Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.
Sequence Length: 253
Sequence Mass (Da): 28238
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A0A520JVX7 | MKWLIDELKRIKREHLYRKLRILETGQVSRVRVGGRQLLMLSSNNYLGLTEHPLVKMATVDAVKKYGTGSGGSRLVTGTNDLYISLEKTLADFKGVERCLVFSAGYLANIACLTSLMKKGDVILSDSLNHASIIDGCRLSDADVKVYAHRNMEHLRCLLKESTQYRHRLIVTDGLFSMDGDLAPLPEIVELAEDFDALVMVDDAHATGVFGKKRSGTVEYFGMHDKIDIQMGTLSKALGSMGGYVAGREELIEYLINIARSFIFTTALPPAAVGAAIAAINVVQQEDPAKKLWKNVREYTTSLNNGGLSLATNSQIIPILIGETVCSTYGKKAGALIRNEDVTCAVAERLFERGLYVTAIRPPSVPKGKERIRTTLMSTHSRQDVHTAADIILETLGEYGLL | Pathway: Cofactor biosynthesis; biotin biosynthesis.
Function: Catalyzes the decarboxylative condensation of pimeloyl-[acyl-carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON), [acyl-carrier protein], and carbon dioxide.
EC: 2.3.1.47
Catalytic Activity: 6-carboxyhexanoyl-[ACP] + H(+) + L-alanine = (8S)-8-amino-7-oxononanoate + CO2 + holo-[ACP]
Sequence Length: 402
Sequence Mass (Da): 44191
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A0A5E4PYU6 | MALKYIFVFMFILNYISVGLSIKCWNCRSSNDPKCADPFDNSTVPITDCDQERGLSHLVGIRPSMCRKIRQKVNGEWHYFRDCAYLGEVGIQGDERFCLMRTGTYNIFEEYCTCKSKDGCNSASLNFSKISLCVSILTALSFCCLV | Function: Required for homeostatic regulation of sleep under normal conditions and after sleep deprivation. Important regulator of the Sh K(+) channel, acting as a signaling molecule that connects sleep drive to lowered membrane excitability, possibly by enhancing K(+) channel activity and thus reducing neuronal excitability.
Subcellular Location: Cell membrane
Sequence Length: 146
Sequence Mass (Da): 16580
Location Topology: Lipid-anchor
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A0A2W6D2R9 | MGILSGWHLVILLVVVILLFGATKLPTAARALGQSIRIFKAEIGGSRSEREADAPAPEHQSLPQSGPAASGVSEAGVNEHRRDNDTVR | 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: 88
Sequence Mass (Da): 9296
Location Topology: Single-pass membrane protein
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G3XCM7 | MLTSFSLTQLILISVTYLSTLFGIAWITERGYVPRRLVRHPLVYTLSLGVYASAWAFYGTVGLAYQYGYGFLAIYLGISGAFLLAPVLLYPILRVTRAYQLSSLADLFAFRFRSTWAGALTTLFMLIGVLPMLALQIQAVTDSISILTRDPAQERVAFVFCTLITLFAILFGARHIATRERHEGLVFAIAFESLVKLVMLGSIGLYALYGVFGGPEGLEVWLLQNQTALTTLHTPLAEGPWRTLLLVFFAAAIVMPHMFHMIFTENLNPRALISASWGLPLFLLLMSLAVPPILWAGLRLGASTTPEYYTIGLGLAVDSPALALAAFIGGISAASGLTIVMTLALSGMVLNHLVLPLYQPPAQGNIYRWLKWTRRLLIVAIIMASYAFYLLLGAEQDLSNLGIVSFVATLQFLPGALSVLYWPTANRRGFISGLIAGMLVWAITMLLPLMGNVQGLYLPLFDVIYVLDDSNWHLAALSSLAANVLVFTLVSLFTEASDEEKGAAEACAVDNVRRPQRRELFAGSPQEFASQLAKPLGAKTAQKEVEQALRDLHLPFDERRPYALRRLRDRIEANLSGLMGPSVAQDIVETFLPYKTSEESYVTEDIHFIESRLEDYHSRLTGLAAELDTLRRYHRQTLQDLPMGVCSLAKDQEVLMWNRAIEELTGVGAQKVVGSRLSALPEPWKGLLERFIDAPDEHLHKQRLVYDGHTRWLNLHKAAIEEPLAPGNSGLVLLVEDLTETQLLEDKLVHSERLASIGRLAAGVAHEIGNPITGIACLAQNLREEREGDGELTEISEQILDQTKRVSRIVQSLMSFAHSGSHLQALEPVCLSEVAQEAIGLLSLNRRSVEVEFFNLCDPAHWVEGDSQRLAQVLINLLSNARDASPPGGAIRVRSEASEHTVDLVVEDEGSGIPKAIMDQLFEPFFTTKDPGKGTGLGLALVYSIVEEHYGQITIESPTDHQREGGTRFRVTLPRHPGPTAEL | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 983
Sequence Mass (Da): 108381
Location Topology: Multi-pass membrane protein
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A0A2N1V3P2 | MSEEIKKMFSSISKHYDYMNNVMSLGLHHIWRKRLVKLSGAKPGDNILDTASGTGDLAIEFKKVVKDGRVLATDFCSDMLKHLPMKAIKKDVEIDAELADILDLHFESKSFDIVGISFGIRNVDDMYRGIAELARVVKPGGKLMILETGKPKGFLKKIYDYYSKIIMPKLGRMLIDEEAAYTYLPTTIDGFPYGQKFVDILKGTERFTEVKCYPQFFGVSYIYKCTVK | Pathway: Quinol/quinone metabolism; menaquinone biosynthesis; menaquinol from 1,4-dihydroxy-2-naphthoate: step 2/2.
Function: Methyltransferase required for the conversion of demethylmenaquinol (DMKH2) to menaquinol (MKH2).
EC: 2.1.1.163
Catalytic Activity: a 2-demethylmenaquinol + S-adenosyl-L-methionine = a menaquinol + H(+) + S-adenosyl-L-homocysteine
Sequence Length: 228
Sequence Mass (Da): 25922
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A0A7C8EB70 | MSNFELITPFKPSGDQPKAIEELTEGVLKGLEHQTLLGVTGSGKTFTIANVIANTNKPALIIAHNKALAAQLYGEFKELFPNNAVEFFVSYYDYYQPEAYIPSSDTYIEKDALVNEDIDRLRHSATISILERKDVIVVASVSCIYGIGSPDEYLGMHLFIEKGLLIKRAELLKKLTEMLYLRSDNEFKRGTFRARGDIVDIYPAFFYDDAIRVEFFGDMIDRIIKIDVLTGKKTSKELEKIVLYPNSHWITSKSNLQRAQEKIEEELGERIRYFKQRNETLFMHRIEQRTLFDLEMLSEFGFCHGIENYSRHLSGRNPGEPPYTLIDYINRGPSEGDYLTIIDESHVTVPQIGAMYEGDKSRKQTLVDYGFRLPSALDNRPLKADEFRQRTKQVIYVSATPGDYEIKVSKGRVIEQVIRPTGLVDPPMIIRPAKNQVEELLEEIQKRTSVNERILVTTLTKKMAEDLCDHYKELGIRVRYLHSDIDTLQRIEILRDLRLGVFDVLIGINLLREGLDLPEVSLVAVFDADKEGFLRSERSLIQTAGRAARNVNGLVILYADRVTKSMDKAIKETERRRKKQIKYNEQMGINPKTISSAIKDILNSIYQSQTEPEYLSVAEDNKSYEGIEETIKKLEIDMKESAKDLDFEKAAKIRDKIKYLRQLILKI | Function: The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate and the UvrB-DNA preincision complex is formed. This complex is subsequently bound by UvrC and the second UvrB is released. If no lesion is found, the DNA wraps around the other UvrB subunit that will check the other stand for damage.
Subcellular Location: Cytoplasm
Sequence Length: 667
Domain: The beta-hairpin motif is involved in DNA binding.
Sequence Mass (Da): 76598
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A0A0S7XBD0 | MAPQPVVTYGNPTLKRRATEIEEIDDSVRKLAAEMFETLDASQGVGLAAPQIGVSRRLIVLSIPLEDNTRWKFVVVNPEIVTKKGKSALEEGCLSVPGVYEEIVRSEEVEVRGLNLEGEEITIEGKGLLARALQHEIDHLEGVLIVDRLSSAKRHVLQKKLRELEETGGANR | Cofactor: Binds 1 Fe(2+) ion.
Function: Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.
EC: 3.5.1.88
Catalytic Activity: H2O + N-terminal N-formyl-L-methionyl-[peptide] = formate + N-terminal L-methionyl-[peptide]
Sequence Length: 172
Sequence Mass (Da): 19002
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A0A847WDC3 | MTDKLILASASPRRKELLGLIGLNDFEIIPADSEADFPSQLPIEQAVEYIALKKAEAVSEKAGKAAENAIILAADTLVWLEGRVLGKPADEAEAAQMLKALSGKKHTVYTGMALIKGKTVIKSHAVTDVWFREMTDREIDTYVKTGEPLDKAVAYGAQGLASMFISRIDGEYYNVVGLPLCTLGTMFKSLGSPVIDEI | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: H2O + UTP = diphosphate + H(+) + UMP
EC: 3.6.1.9
Subcellular Location: Cytoplasm
Sequence Length: 198
Sequence Mass (Da): 21402
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A0A952WZZ5 | MGLVQEFRQFAMRGSVVDMAVGIIIGAEFGKIVNSLVSDVLMPPLGKLIGNMNFNDLILPLGAAGADGKVAELKYGNFLQAVVNFVIIAFAVFLIVKARNAAEARVRGPVDPKAPPPPPEDVELLREIRDLMKADRAA | Function: Channel that opens in response to stretch forces in the membrane lipid bilayer. May participate in the regulation of osmotic pressure changes within the cell.
Subcellular Location: Cell membrane
Sequence Length: 138
Sequence Mass (Da): 14799
Location Topology: Multi-pass membrane protein
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A0A973GRB0 | MAASSDSASAPIADRLSVLFRLAVGGIFLVSGLAKIADPVRFLLTLREFQLLPGVLESFLAVYLPWLEFLLGLCVVLGILHRTSALMIACLNGFFIVAIGSVMARGIVVDCGCFGLLADVLHLPDMADGKAIVRNLILMGICIYVFCSDARAWTLEEYIRR | Pathway: One-carbon metabolism; methylamine degradation.
Function: May be specifically involved in the processing, transport, and/or maturation of the MADH beta-subunit.
Subcellular Location: Cell membrane
Sequence Length: 161
Sequence Mass (Da): 17449
Location Topology: Multi-pass membrane protein
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A0A1V5WNR8 | MGNERILMTVEELTQATGGSCPGNFAPDSGCSSVVTDSRSVIEGALFVPLMGENQDGHRFIPEALDSGARVVFVDAAHGEGSANMFSLLAKQHGAAIIMVENTLTALQDAAKAYVRKFPGLRRVAITGSSGKTTTKELTAAIFSRKYRVVANAGNLNSETGLPLSVFRIRDEHEVGIFELGMNRRGEMREIAEVLDPDTALITNIGTAHIGILGSREAIAEEKKAVFSLFSGESSGFVSETDDFRDFLVSGVPGSFSFFGPSSTQGILGTESLGLEGWIIRYETEEIHFPMPGPYNLENAFAAISLARSFSIDPATIREGLESIQTLFGRTEIVRGAVTTIFDYYNANPQSMEEAMRFCDELPWQGEKIFILGSMLELGETTNAAHRAVCEIADRSTAAHILLFGEDMIRAGKSMNWNHDSVYFAETMEDLAEKVSSILQKGAMVFIKGSRGMALERLRPVLEHFSSGEARS | 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-diaminoheptanedioate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine
EC: 6.3.2.10
Subcellular Location: Cytoplasm
Sequence Length: 472
Sequence Mass (Da): 51269
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