ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
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N6VF48 | MKARVIVTFKSGVLDPQGEAITSALNSLAFTGIQSIRQGKVFDIILDDIPTETAKQKLEQMCKQLLVNTVIENYTIELL | 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 1/2.
Function: Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent ... |
A0A8T5PFY1 | MESLDYEKLNVKIGLEIHQQLNTKKLFCSCSSEMREDNLIYEVKRKLRPVVSELGEVDRAALFEFFRNREFIYYGYEDECCLVDLDEEPPHEINKDALEIAINIAHNLELWVPHELHIMRKIVLDGSAITSFQRTLLVGLGPAKFNGIRIKSLCLEEDSAKPIKQEGKYVYYSLSRLGIPLIEIGTEPDIKNPEDAKRIAKDLGIFLRTFNVKRGIGSIRQDVNISIAKGARVEIKGWQELRSLDKLIENEIKRQVSLLDIREELRNQKIDVNIREIDEMHILFVKNFERFAQRILCEKKILLDELLDYGGVYNCDLYSN... | Function: Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln). The GatDE system is specific for g... |
Q85I54 | MNLMITLTINFSLSAVLIFIAFWIPQMSIYYEKVTPYECGFDPMSSARLPFSMKFFLVAITFLLFDLEIALLLPLPWALQYSMTYSVVSLTMALILILSLGLAYEWS | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity of complex I.
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NA... |
A0A0L6TWL5 | MCKEPKFLVCKHCGNMVSMIHESGVEMICCGDPMTVMIPNTTDAAQEKHVPVITVNGTTVTVDIGSAPHPMTPEHHIEWIFLETAEGRQRKCLAQDGKPQAVFELTAGDKVISAYEYCNLHGLWKAAL | Function: Catalyzes the one-electron reduction of superoxide anion radical to hydrogen peroxide at a nonheme ferrous iron center. Plays a fundamental role in case of oxidative stress via its superoxide detoxification activity.
EC: 1.15.1.2
Catalytic Activity: 2 H(+) + reduced [rubredoxin] + superoxide = H2O2 + oxidized... |
A0A7T5RA25 | MAKKTTKRAQKKVAAKKADATKREQAAAPKTKIRYDRILVRYGEMALKSDVVRRRMEDRLLGNIRSGLDKMQIKYVLHKEMGRIFVETRQIEETVGVLTHIFGLVSVSPVQTRVIGSSLEKIAETAERIGRTFITSKDTFALRARRTGNENFTSKMIEREAGGRVQDATQARVDLDNPDKTLYVEVRQNKAYFYIEEHACPGGLPLGTQGRVVILFSGSVDAAAAAWLMMKRGCTVVPIYFESSPYTDASTDERAARVFETLREWSHGNKMSLRRVPHGKALFMFTEECRDEHLDVLSKRQMLRVANLIAKQEGARAVVT... | Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
Function: Catalyzes the ATP-dependent transfer of a sulfur to tRNA to produce 4-thiouridine in position 8 of tRNAs, which functions as a near-UV photosensor. Also catalyzes the transfer of sulfur to the sulfur carrier protein ThiS, forming ThiS-thiocarb... |
A0A7T5UJF8 | MDKSALIKELQKDWKKYWKVELFEKEGFARRQCEKCKGFFWTLDASRANCGENPCADYSFIGVRRKDWDYYETWKQVERFFIKNGHTSVPRYPVICRWRPDLYFNIASIINFQRRTPKGITFALPHNPLIVPQVCLRFTDLPNIGVTGRHHSAFVMLGQHAIPEGNGYWKDEAIRLDWEVLTNVLGIKPDALTFKEDAWAGGGAFGYSLEYHANGLELGNTVFTEFLETNGVRERLTRPVVDMGAGFDRWVWYLNGTLTSYDSAFGPVLEKMKKGIEYDGDLFARYSRISGALNFEDVLDAKRAKSDIASALRVSVDNLN... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.
EC: 6... |
A0A972VZG3 | MSISQQSLILASTSQYRREILAKLTLPFIQVQPDFDEIPIPGEAPVSMAERFAAGKALAVASDSLYSASENLVIGSDQVVVVNNQILGKPGNLERARAQLLLCSDQWVTYTSAFCIACGGAILVLEHDDYAVKFRPLSGAEIDRYLALEQPYDCAGSIKAEGLGIALMAETRGQDVNTLYGLPLMRLAQRLREHQIDPLKQL | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes 7-methyl-GTP (m(7)GTP). May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: H2O + N(7)-methyl-GTP = diphosphate + H(+) + N(7)-methyl-GMP
EC: 3.6.1.-
Sub... |
A0A933BG98 | MTVGIGFDTHPLVPGRRLVLGGVEIPFEKGLGGHSDADVLAHAVIDALLGAASAGDIGSCFGTENPEYKDVSSLLLLKQAFQRVNALGYSVGHIDATIIAEAPRLGPYITQMRINLAQIVGGAVEDVSVKATTANGVGVLGAGGGIACLAIALLRRRVAAE | Cofactor: Binds 1 divalent metal cation per subunit.
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 4/6.
Function: Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP... |
Q8D3H9 | MDISLIWAQSKNKVIGHDQYIPWNLPEDISWFKKNTINKPVIMGRKTFESIKKPLENRINIVLSKNLYRNVMSNLKIAKNPKQALFFAKNYNEVMIIGGKQIYKIFLPKATKLYLTVINAEINGNIFFPRYNRKKWILSFEKYFNSDTKNKYSMYFRIFNKI | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1.
Function: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.
EC: 1.5.1.3
Catalytic Activity: (6S)-5,6,7,8-tet... |
Q8D3G7 | MSNKDELEKQEDPTPNRLKKARSKGNIPRSRELTSFSILIFGWILIWFTGNNLLDKIIVELKKNLNFKLYLYEHINYILVNIYLISKKFFFIIFPIIFIIMIITIISSGLLGGWVFSKKSLNIDFSRLNPYKNISRIFSKNVFIEMAKTLFKFFFMLFSCIFYLWHTRFQISDLSDNNYSNAIKNCILIISKCVFVIILSSIPIVFFDSIFQLFTFKKNLRMSKKEVQDENKENEGNPQLKHYIRKKQRHIYNMRMMQNVEKSDVIIVNPTNYAVGLKYEKNMKAPVLLAKGTGNIAIKIKEKAQEKFIPIIAVPPLARA... | Function: Required for formation of the rod structure in the basal body of the flagellar apparatus. Together with FliI and FliH, may constitute the export apparatus of flagellin.
Subcellular Location: Cell membrane
Sequence Length: 385
Sequence Mass (Da): 45234
Location Topology: Multi-pass membrane protein
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A0A2A5B1H0 | MARITVEDCLENVENRFELVMVSSKRARQLQTGGKDALVPEDNDKPTVVALREIAEGHITADILKVKPSIDLGDLGLDIPSDTSTAESTESTAEAKASADSAPEASAEETKTEETTEATPEKPEETPASDA | Function: Promotes RNA polymerase assembly. Latches the N- and C-terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits.
EC: 2.7.7.6
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Length: 131
Sequence Mass (Da): 13926
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A0A918P6U9 | MTSRLCSLKRGAVLSVAILFLLSSCVVRDNPKTAAVPAVRSERSPQAPALPASAHSPVLGRMPSYPFGVPPTGNLTDGPRGAEARALDLSRPGRAGAYPVPHYADCDEGKLGGLAGADLVDYLVTVDGPCVNRLFQSNAVSWHAFAPANVGLVAERANRLAASWDGHTANGLWPLAVYLKAAYYLQYNAPDKVGPLSQSDAAVLRAVDTLLANSALWRAGAEDNGTQEGWLRNTDARGVASETLILIDSVRNTDLALPLIGRFFRNYTLAARGHWAEDGVLPLQIALYNLHYADDFASRIDRGDLNDLLGHLYRLVDAGP... | Catalytic Activity: Digestion of native collagen in the triple helical region at Xaa-|-Gly bonds. With synthetic peptides, a preference is shown for Gly at P3 and P1', Pro and Ala at P2 and P2', and hydroxyproline, Ala or Arg at P3'.
EC: 3.4.24.3
Subcellular Location: Secreted
Sequence Length: 778
Sequence Mass (Da): 8... |
A0A1X4XXF9 | MLKVGIGYDLHRLQKNRKLVIGGVEIDSDIGAYSHSDGDCLLHALVDAILGAAGLGDIGEHFPDTDDAYKNAKSILFVTKTLDLIKKNGFKIVNVDATVLLERPKLASYKLKIKKNMANLLEIDERFVNIKAKTNEKVDEIGKGLAIAAYVVVLLEG | Cofactor: Binds 1 divalent metal cation per subunit.
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 4/6.
Function: Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP... |
A0A4R1QYB3 | MFFKKQTTGADWLVVGLGNPGKKYDGTRHNVGFDAIDHLAKEWGVSVTKAKFEGLCGQAALAEGKVLLLKPQTFMNLSGHSVQAAAEFFKIPPEHVIILCDDVTQKPGKIRIRPSGSAGGHNGLKDIIACLGTDGFARVRLGVGEKPSPDYDLANWVLGKLGGEDRKAFESRLNDVEAAVRLILAGKLSEAQNRFN | 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: 196
Sequence Mass (Da): 21141
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A0A7C0U9W3 | HLLGYESLTKALITVVKEAVENSLTWSTPIFLEVNGKVEIRKIGEFIDEQFEKYKKFVIKERNGNLEKLKKFDPTKVLCFNPRTQKLEFKAVKTLFRHKPNSKIFRITLEGGRYIELTDYHSIFSLRGSEVKAVKTSELRLGDLIIVPRNPWSLCPIEKIDVLEELLRLPEGITRNIRIYGVRNIIRKLKAELKKVLGKEKSYRIQDFKKCDSIPLSLVRKLPPRLIKVFKKCKFGLKFSKYKIPLEIPITEELLAFLGIYVAEGCTLHNLEKVILSFGAEEKELLNYSKKIVKRVWGIDATIKKPHETAVNLIMNSKNL... | Function: Relaxes both positive and negative superturns and exhibits a strong decatenase activity.
EC: 5.6.2.2
Catalytic Activity: ATP-dependent breakage, passage and rejoining of double-stranded DNA.
Sequence Length: 1016
Sequence Mass (Da): 116028
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A0A7C0YZ28 | ETTLKSDYTRRIFEQKLVSNIRKGLKSAGIEFEITAEPGRIFVKTKKVNVACDVLKRVFGLVSISPVKEVTVKADIGKLVDYAEKFASNYIKKDDTFAVRAKRTGNDAFTSQMIERRIGARIVEKRGSKVNLTDPDKILYVEVRQNKAYFFREKIKCPGGLPLGTQGNVVALFSGGIDSAVAAWMMMKRGCKVFPLYIDCSPFVESSELEKVKSVFTQLKKWSIGFGMKLIVIKNKALPEIVEKTKENLTCLLCKRMMYRIAEKVCEMKEAKAIVTGENLGQVASQTLDNLYVLDHATHFPVIRPLIGLNKEEIVELAKE... | Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
Function: Catalyzes the ATP-dependent transfer of a sulfur to tRNA to produce 4-thiouridine in position 8 of tRNAs, which functions as a near-UV photosensor. Also catalyzes the transfer of sulfur to the sulfur carrier protein ThiS, forming ThiS-thiocarb... |
A0A497TH97 | MEWFSLIIGISVFFFVVLVMPRYILYAKRRGLIGKDMNKYNKPEVAEAGGVVVFIGFFIGLIALLVYYFLMNNENYLLIAAVTISTSIVSMIAYIDDTGGWKKGIARWKKPLFTFIATIPLIPLVTDRTDIVLLGYPLQLPWLFYPLVLVPIGFIGATNAVNLLAGFNGLEVSLAIVSTLALMYFTQGTPFFSVLLIFLFALMGFFVYNRYPSRVFPGDTLTYLTGSVFAVVAVLGRFQTITILIMMPYLLEGLIKSKEIPYIIKHRKTFKPECFGKVTKDGDLLPPYKSIWSLTHVAIHTIRKIKNKCSENDVVFLLVC... | Pathway: Protein modification; protein glycosylation.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 334
Sequence Mass (Da): 37712
Location Topology: Multi-pass membrane protein
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U3CCN5 | MDIFNQRESQVRSYCNSFPVVFTKAKGCWLETEAGEKYLDFLAGAGSLNYGHNHPILKQALLDYIATDGVTHGLDMHSRSKGDFLKAFQKNILKPRALDYKVQFTGPTGTNAVEAALKLARKVKGRSTIVAFTNGFHGCTMGALAATGNQHHRQGACVSLNDVMRLPFENYADIDGLKLFETMLNDNSSGMDKPAAVLVEVVQGEGGLNVASNTWLKRLSDICQHNDILLIVDDIQAGCGRTGTFFSFEGAEIKPDIVTLSKSISGYGLPMAIVLLKPELDIWKPGEHNGTFRGNNHAFITAAKALDIYWSDNAVFEEHI... | Pathway: Amine and polyamine biosynthesis; ectoine biosynthesis; L-ectoine from L-aspartate 4-semialdehyde: step 1/3.
Function: Catalyzes reversively the conversion of L-aspartate beta-semialdehyde (ASA) to L-2,4-diaminobutyrate (DABA) by transamination with L-glutamate.
EC: 2.6.1.76
Catalytic Activity: 2-oxoglutarate ... |
A0A1I1YKJ7 | MWYNHNMDFKSIGNYIKKHNIINKGDHIVLGLSGGPDSVCLFFVLNSLAKELDLKIYPVHINHKFRPGAAEKDAEFSKSLSAKLGWECRAYEVDCNALAKTEGLSPEEAGRKARYEAFREVYNQVIAEHKGDEVKLAVAQNKDDQVETVLFRIIRGTGLEGIGAMREDSKGIGEMEIIRPLLTYTKKEILDFLHDNEIEYCTDKTNEAEIYTRNKIRLSLIPDLEREYNPNLKDTIFRMSKTAAEDADFISELARELYDKAYGLAEEAVDNNAGSDSDPGERRIILLDRRTIGDAHPAIGKRAIGIALKEMGISRDIAYS... | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34)... |
A0A932UR78 | MRHLDVFITFLVYMVGMWVIGLFCSPLIKSLTDFLVAGRRLGPWVTAMTHEATAHSAYVYQAVPGQAFMKGLQNIWITLPAIAKPYVNFIGLGRRLRILSERLNCLTIPDLLEARFEDPAHSLRILSTLITIFFMEIYVAGQIVGAARLLEQITGANYTVMALVMGGTVVFYCVAGGFFAVAWTDFFQGIIMAIGFVIMAAMVFGEVGLMALTEHLKGVDARMISTTVPFWVAVGWLSIIFGFIGSPHIIIRFFAIQRGFKTLRVATLVSLLWVTVIFYAGTYVGMAGRVLVPDLKNPENVVMELALIKLPGVIAGIIAS... | Function: Catalyzes the sodium-dependent uptake of extracellular L-proline.
Catalytic Activity: L-proline(in) + Na(+)(in) = L-proline(out) + Na(+)(out)
Subcellular Location: Cell membrane
Sequence Length: 509
Sequence Mass (Da): 56053
Location Topology: Multi-pass membrane protein
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A0A833LS99 | MTLRRQNPMICALFFQCSPCHGHQAHLPAQQSQARPRPRFPCAHEDPRWPQGHQRASRQGPQAPRGLTGRAVATPARFPRTARLLAPRDFAALRSGSRRFAGPHLTAQVKPNSGDAARLGLAVSRRVSKLAVQRNRIKRIARDSFRRHRHLLGALDILLIAHPAAAAADNARLHGDLQQLWQRIAALNAGGSTGTMRG | Function: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of... |
A0A0K9EUG9 | MAGLIRREDIDLVRGTARIDEIVSQYVTLKPSGMDSFLGLCPFHDEKTPSFHVRPNHGRYHCFGCGEDGDVISFVQKIESIGFVEAVELLARRYGIELHYEEGGPQRKPGEPRKIRLIDAHRVAIQFYRRQFATPEAAAARQMLAERGFDEAAMDHFQVGFSRNEWDGLTSFLRQSGFSDKEILAAGLASQGKRGLYDRFRGRLMWPIYSITGEPVGFGARRVSEDDKGPKYLNTPETSIYHKSSVLYGLNLAKQEVSRKKEIVIVEGYTDVMAAHLAGIKTAVATCGTAFGEGHIRIVRRLLGDAANPAAGVSLRSGGS... | 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: 727
Domain: Contains an N-termi... |
A0A066VV93 | TNTSNLSRLIQNAIDIFCLAHALGWFGKALILRDYWFCWILSIAFELAEYSLQHQLPNFAECWWDHWVLDVLLCNWLGIYVGMRTCAYFEVKHFTWRSIQSTKGVRRKTKRVLKQFTPHDWTEFHWEGTSSFASYCAVFLLLATFLAAELNPFYLKSLLWMEPSHPIIISRLAGVFMCALPAVRELYQYLNHPEKAVRMGQHAWLLFATILTELLIIFKWSRGMFAEPFPTYIKFAWSVGSALLIVYPSFKFGLPTIRRYLRRAERKRLNRIE | Pathway: Lipid metabolism.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 273
Sequence Mass (Da): 32218
Location Topology: Multi-pass membrane protein
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A0A0C9R3K1 | TFGSKNSQVTMDVNLTKLTFIFMASSVGFVGFLMHAIDDYMPLLIRKTFRYGKSAEKKDHMLVNRLELPKRWFSHFYLFAAPAASISLIIVVNRYFFSGQLPKIVRWLLNFQLGSSRKSLVPAEKCFTAIFLITIQCWKRLYETTRVSVFSNAKINISHYIVGYIHYIGTLTCILGESEGFINASQISFHWSNLTYLDYSCAFGFLSASYLQLLSNYILSNLRKDGKGAVVTKSYKIPRGGLFNYVTGALQFTEITMYFMLTIILWRSSTYHYVFLWVVINQVHCLRFNELVNNIFVHLNILFNFQIQTAVDSDRWYRIY... | Pathway: Protein modification; protein glycosylation.
Function: Plays a key role in early steps of protein N-linked glycosylation by being required for the conversion of polyprenol into dolichol. Dolichols are required for the synthesis of dolichol-linked monosaccharides and the oligosaccharide precursor used for N-gly... |
A0A972VZG1 | MGLAVLGGTFDPVHFGHLRSAVEVRQALGVERVKLIPVGIPAHRERPGSQPEQRLEMLRRGT | 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... |
A0A7J3KE59 | MRTAVIGMQWGDEGKGKVVDYLLDRDYYEYVVRYNGGPNAGHTININDKTYVFHHLPSGVLHKKVENIIAAGVVIDPEILYNELAELYRNNIKPKLKIDYRANLILPYHKILDAEKNKRIGTTKRGIGPAYQSKIGREGLRIGEVISENEEVDEELLHFYLENFLKEYLEPLGLEPKESIDKTEKLLRFYLSQLSKYLADTRKILYKARKDGRCILYEGAQGILLDVDWGTYPFVTSSSTGKNGIYSGTGVDPYLDNVIGVIKAYTTRVGEGPFPSEFKDEYENIGNFLRTKGHEYGSTTRRPRRCGALDLVALRYSKEL... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2.
Function: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.
EC: 6.3.4.4
Subcellular ... |
A0A0G0K1S4 | MIKMKKVKDKESGLSKMLLNMQKKISLKNFSSFKIGGNTKYFYEAKTVLGLKKALNWAKKSKIKYFILGGGSNVLFSDDGFDGLIVKLNFNKIKVSGEKIHVESGANLGLVVATALKNKLAGIEDLSGIPGTIGGAIRGNAGIKTCWIGDKIESAKIFDAAQNKIITFRKKDFKFSYRESVLKKHKNLILLNAILKLKRVKDVSPATSQIKELALKRAKSQPKGLSCGCIFMNPTKKYKGKPVSAGELIDKTGLKGKRLGNAEISNIHANFFVNKGNASSKDMLALISLAKSEVYKKFKIRLVEEIEIV | 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: 309
Sequence Mass (Da): 33989
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A0A327X2E3 | MYEIFLVLYLLCAIALIAMILLQRGKGAEMGASFGSGASNTVFGSSGSGNFMTRTTTILAVAFFLLSLILGNMAAGGSQVQDDWSDLSVPTLPDDM | Function: Involved in protein export. Participates in an early event of protein translocation.
Subcellular Location: Cell membrane
Sequence Length: 96
Sequence Mass (Da): 10074
Location Topology: Multi-pass membrane protein
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I2BAJ4 | MLTFNGKEFDTDSEGYLKDSSAWSEGLAEVIAAGEGISLSPEHWEVVRFVRDFYLEFNTSPAIRMLVKAMAKKYGDEKGNSRYLYRLFPKGPAKQATKIAGLPKPVKCI | Function: Part of a sulfur-relay system required for 2-thiolation of 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at tRNA wobble positions. Could accept sulfur from TusD.
EC: 2.8.1.-
Subcellular Location: Cytoplasm
Sequence Length: 109
Sequence Mass (Da): 12209
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A0A1Y3FXA4 | MNVLNQFRQDLACALSLFTRLPVFWLLTRAQRADKRPWPLARSLWLWPFVGAFTGFAGGIVGWFLEAIMHIAPWPAVTLTLAAQVALTGGFHDDGLADMADSYGAHTREHKLDIMRDSHIGSYGVLALCLSVLTKVGALSVLPATALIPALMCSGLLARATMIWVPVVLSPARNNGLARLLSPVPLIPFLFAQACSVMSIACWVYWWNAAYSPVFSTLILPLLMPFFSLGIMVMTAYKNFGGYTGDVLGATATITECLVLAALSASK | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7.
Function: Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-riba... |
A0A8T3XVZ9 | MWLNKSEEKTNSNLGKNPGERTVEELITSSLIILDKHSGPTSHQCTAWVKNIFNVKKSGHSGTLDPAVTGVLPIGLDDATKVMTVLTGLDKEYVGVMHLHKDVTEDVLRNTIAERFLGSIKQTPPVKSAVARREREREIYFLDILEANGKDVLFKVGCQAGTYIRKLVHDIGQAMGIGAHMSELRRTRVGSFNEEISHSLVDVRDAYEFWRNNKEERLLRDMLIPVEHAIPHVKKIVVKDSAIENICNGAPVYVNGICRIQEDIVRGETIAMFSLKEELIALGIAKMTSAEMHKRTKGVAVRNDKLVMKKGTYKIV | Function: Could be responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
EC: 5.4.99.25
Catalytic Activity: uridine(55) in tRNA = pseudouridine(55) in tRNA
Sequence Length: 316
Sequence Mass (Da): 35352
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A0A2A5C860 | MGDGGLGAVAELPNGGARISSRHDGFNNEDESGDEDEYQEYDEDADNYENSQEGDQVVPVLMDTVDIDNDVGTDLAIDDEENSFDEEDYDDDTIEEYEDAEDDELQEISSDGLNADTTSSEDQGYDEQTEDELNDDEEISSVRTSSREDKQGLAKSNIHPPRRGRIEPTLGEMDSFSADELEDKPAHVAQAENQAQAKGWEKEQERVQVDEPTVGQAELFSESPADFIQADDDYDEGEEDYLEPEEVIVINVMAKQGELFAGSDLLPILLQQGMQLGRMSIFHKHADSSGNGPTMFSMANMVKPGTFDVTQMEEFSTPGV... | 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: 3... |
A0A2A5CHT1 | MSQQNTPQLSAFLSPKYWPTWLGLGLLALIAFLPKRLRLFFGAILGRLLYFLAKERRYIVATNIKLCFPELSKPAQAKLVRDCFIENGRGLIDTLVGWFRNPRRFQHMLDIKNMEVLDAAIAKGKGVILLGAHYTTLDFSANLVSLRIPFAVTYRPHKNALFDAFMLRGRLKNTNGVFDRYDIRGTIRHLRKSNIIWYAPDQDYGENHAVYAPFFGNTAATITAASRLAKFNNSSVLLVRHHRNDNANSYEVEFYPFPESYPGDDDVADATYMNQQLEKVIRLYPAQYMWTHKRFKTQAGGKPASPYIGIRTPIQKMNKQ... | Pathway: Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis.
Function: Catalyzes the transfer of an acyl chain from an acyl-[acyl-carrier-protein] (ACP) to a Kdo(2)-lipid IV(A) to form a Kdo(2)-(acyl)-lipid IV(A).
Catalytic Activity: a fatty acyl-[ACP] + an alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IVA ... |
A0A2M7GX30 | MSPNPDQPEPSREADRLCVIKFGGSVLTGLADYSEAASETYRHIRSGEKVIVIASALQGETDALYEESELVGAGASPVARARLVRLGEFRSAALMGLALDRIGVRVIVVDPGEIGLFAEGDPLDAGLCGLDVESLRKKIECADAIVVPGFTASHHESGAAVLGRGGADLTAVMLAAKIGIRRARLIKNVDGVYTCNPAKNPAAVRFDRLDYTAATAASEGLIQDKAIHMAEAAGVQLEIAAMGAVQASCIMPGPAITGALRNNQRKRIALLGCGAVGSGVLDHVVRRPDLFDLNPVLVRDPGARSSDARAAFTSDAAIAL... | Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 1/4.
EC: 1.1.1.3
Catalytic Activity: L-homoserine + NAD(+) = H(+) + L-aspartate 4-semialdehyde + NADH
Sequence Length: 596
Sequence Mass (Da): 62021
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A0A932GIQ8 | MEIVVVGLNHKTAPIELRERLHIPERDLAGPLEALGKEPPILERLILSTCNRVEVYAVAEEVRAARQSIEALLAARAQLPAAAFSGLLYLHTAAEAVRHAFRVAGSLDSLVVGEPQILGQVKDAYQAAAGLGAVGPVLSALMERALRVGKRIRTETALGASPVSVASVAIELARQIFGALAGRSVLLLGAGEMSEAAAQHLKEEGVSAILVSNRRYERALDLAARLGGRAVRFDQFKEEVLSADIVIASTAAPHPILTRADVEQIIRARRQRPLFLIDIAVPRDIAADVNAIDNVYLYDIDDLEAVAAANRKLREEEAVV... | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2.
Function: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
EC: 1.2.1.70
Catalytic Activity: (S)-4-amino-5-oxopentanoate + NADP(+) + tR... |
A0A8T3YFN7 | MGMNTLLVGSGAREHALARSLAASGAKILAYMGNRNPGIAKLSVDSTVGSLADAPAIAAYAQRHRAEMAVIGPELPLEKGVADALWAAGIPCIGPRRLAARIETDKSFARQLLEQHKIDGRLAHQVFADAQAAADFIDAFGKPVVVKPLGLTGGKGVKIVAPGIAGQLKDLEAAKRYARDVIEKAVSGQGKVLVEEKLDGQEFTLQAFVDGRHVVPMPAVQDHKFAFENDSGPFTGGMGSYTGPGHLLPFLTEAEYAHAVAILEQVVAALAEDGLEYKGILYGGFMLTGTGPKVLEFNARFGDPEAMNVLALLETDFLEI... | Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/2.
EC: 6.3.4.13
Catalytic Activity: 5-phospho-beta-D-ribosylamine + ATP + glycine = ADP + H(+) + N(1)-(5-phospho-beta-D-ribosyl)glycinamide + phosphate
Sequence Len... |
A0A933BJV2 | MGDLRRDPVVNRWVIIDGERAEREAIFQMELCAPIPAAECPFCPGREAQDDEVFALGKPGRAANEPGWWLRVIPDKYPILRREGTVERRLEGIFDLMNPFGIHEVVVETPEHHKGWPELDDLQVERVLSTYRTRSLDLRQDDRLRQLLVVKNHGRAVSAFQHPHSLLIALPTVPKGVEEEVQGAAYHFRQSQRCVYCDVIEQEVQMGKRVVLESAQFVALAPFASRFPLEVMVLPKRHAADYETIGDEELLGLAKLLKTVLGSLEEVIQNFSCSIILHTAPLHQDLRAIYHWHLELLPKITKVAGFEWGTGFFINPIPPE... | Cofactor: Binds 1 zinc ion per subunit.
Pathway: Carbohydrate metabolism; galactose metabolism.
EC: 2.7.7.12
Catalytic Activity: alpha-D-galactose 1-phosphate + UDP-alpha-D-glucose = alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose
Sequence Length: 332
Sequence Mass (Da): 37838
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A0A556MPU4 | MADFVLLISDWYRLNARELPWRNTKNPYFIWLSEVILQQTRVDQGMNYYLKFIENYPILNQLANADEASVLKLWQGLGYYSRARNLHQTARQVRDEFGGEFPQTYAEIIRLKGIGPYTAAAISSFAFDLPHAVVDGNVYRILSRYYGIDEPIDTGKGKKIFQELADSLIPTSDPALFNQAIMEFGAIQCTPNNPDCESCVLNQSCGSAFNPELIKKLPVKKGKTKVRKRYFHYLHIEKELEIALDQRTGKDVWEKLYEFPLIESDNDSVPSEFKDSATLCYQTKHILSHQHIYAYFYKTEKSEIEGLDLTFVDKNQLADY... | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Adenine glycosylase active on G-A mispairs.
EC: 3.2.2.31
Catalytic Activity: Hydrolyzes free adenine bases from 7,8-dihydro-8-oxoguanine:adenine mismatched double-stranded DNA, leaving an apurinic site.
Sequence Length: 334
Sequence Mass (Da): 38689
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A0A7C7NJT1 | MRPYRPKDNVQKKAYYNDRFYVTPQIPKDDPASDEVYSKDIEKLQSKFSISESYIQRGELVIYIDPDSNVEVLEFLKDELDYSFLMEMSAVDFLAQREGFEIFYELLSLSKRKRIRVKTFIKENQAIESVQHLFRSANFAEREMFDMFGIQVNNHPYLKRILMPDDWEGYPLRKTYPLQGDEFAQWYEVDKIFGKEARDIVGPEIRDSAHIDRYDTERFARLGHEVPRGTDISKDEPDTDNHEFQEEGGVFLIKDLNKPQKVLSEKERRER | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ... |
A0A7C3VZ81 | MLHLDTRLPGSESSPCLSQQVSRREESLFSRSTWLGVVLVGPTAVGKTALSLRLAQRWNAEIVVADSLQVYRYLDIGTGKPSLAERQMVPHHLLDLVEPPDPFTAGDFRRLAEVRIKEIRERGRLPLIVGGCGLYIRALVDGLFSGSASSSEVRERLARTVREEGEEVLYQRLLSLDPMMAQKIHPHDSYRLVRALEIFETTQRRPSEVRGVVWPRRKDVPFLMIGLWRPRSSLYRLIEERIENMMEAGFLQEVRMLICRYSVDCKPLGALGYSHLISYLQGRWGLEEAISRWKRDTRRYSKRQMTWFGRDERIQWVSLE... | 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)-dimethylall... |
A0A1I1XNY1 | MSRLGILGGTFDPFHKGHESIGLHALEEGDLDYLYLLPANVSPFKIGKKMAPEEDRIAMLKAYCRSREEFQLSTLEIDTDKVSYTYETMEQLKTLRPDDELFFIMGTDSFLSLEKWYKGKELLESTSIIVGKRNGINDDDLEKLVQHYEKAYNADILIMKNSILEISSTEIKKNISKGESIGHLVPKVIEEYIEKYGLYR | 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... |
A0A497STM7 | MGGKIEKTGLTFDDVLLIPRYTSVLPVDVDVRTSITKNIKLNIPILSSAMDTVTEANMAISMAREGGLGVIHRNMGVEEQCAEVRKVKRSESWIIRKPVTLSPTDKVEKALKIMEESGIASFPIVEGKKLVGILTFRDIRFVKNTNEMVKNIMTTNVITTDENIDMEKAVEIMNKHKIEKLPVVDKHGNLKGLITVRDIEKNKQYPNSVKDNEGRLMVGAAVGPLDKHRIDMLVKEEVDVIVIDTAHGHSKNVIDCVKYIKKNYDIDVIAGNVATKDGASDLISAGADSIKVGIGPGSICTTRVVAGVGVPQITAIMDCY... | Pathway: Purine metabolism; XMP biosynthesis via de novo pathway; XMP from IMP: step 1/1.
Function: Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role i... |
A0A0F0GEF0 | MCRHLAYLGTAVSLASVLYDAPHSLEHQSYAPADMRAGGTVNVDGYGVGWFPGPVRYRRAGTLWSDPNLRQLAATESTAFLAAVRSATVGMPVSDAACAPFTDGTWLFSHNGRVDGWPGTVAGLAKTLDVTDLLTMDAPTDSALLWTVLRRRLEAGKDPAEALVELVREVADAAPKSRLNFLLTNGKVLTGTTWTHTLWVLQEEQGVTIASERLDDDPGWREIPDRHVVTADPSTVEVRPI | Pathway: Amino-acid biosynthesis; ergothioneine biosynthesis.
Function: Catalyzes the hydrolysis of the gamma-glutamyl amide bond of hercynyl-gamma-L-glutamyl-L-cysteine sulfoxide to produce hercynylcysteine sulfoxide, a step in the biosynthesis pathway of ergothioneine.
EC: 3.5.1.118
Catalytic Activity: gamma-L-glutam... |
Q8D363 | MYHALYLANKAKKFGEIPIGSVVILKDNIIGEGWNQSIKKNDPSAHAEILALRSAGKNINNYRLLNTEIYTTIEPCIMCIGAIINARVSRLIFGARKTKKINFFTKDLLNNCNLNHKISLTEGILEENCKKIINKFFSKIRKKNKNKFLCF | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the deamination of adenosine to inosine at the wobble position 34 of tRNA(Arg2).
EC: 3.5.4.33
Catalytic Activity: adenosine(34) in tRNA + H(+) + H2O = inosine(34) in tRNA + NH4(+)
Sequence Length: 151
Sequence Mass (Da): 17217
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A0A0G0JZP7 | MKESFPETLIEKIEQSANKIIFSLKKGKKILICGCGGSASDSQHFAAELVSKYKLERKALPAIALTVNSSIITAISNDYSFKTVFSRQIEALGDSGDILFAISTSGNSEAVLEALKCAKKQAMYLIGLTGETGGKMKGYCDLLLNVPSKETPRIQESHILIIHIICELVEKAFYKK | Cofactor: Binds 1 zinc ion per subunit.
Pathway: Carbohydrate biosynthesis; D-glycero-D-manno-heptose 7-phosphate biosynthesis; D-glycero-alpha-D-manno-heptose 7-phosphate and D-glycero-beta-D-manno-heptose 7-phosphate from sedoheptulose 7-phosphate: step 1/1.
Function: Catalyzes the isomerization of sedoheptulose 7-ph... |
A0A932LVU7 | MYGLYTLGLLVAFLAMLPRLVARYGRGGAFRAGIGQRRGVYTPGDLAAVRGKGPIWLHAVSVGEVLAIRGVVQAIRERWPDVPVLISTVTETGQAVAAERLGGADARIYFPFDLPGCAGRALDAIRPRAVLLAETEIWPNFLRACRERAVPVVLVNGRISPRSFPRYRLARPFLRRVLQDYALCLMQGEADAERLRALGAGAERIRDRGMQPPDLADRLDLRELLVFTIDPADAKDHDDALSIRPLGEDRWEVGVHIADVA | Pathway: Bacterial outer membrane biogenesis; LPS core biosynthesis.
Function: Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of 3-deoxy-D-manno-octulosonate (Kdo) residue(s) from CMP-Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A.
Catalytic Activity: CMP... |
A0A0G1J9J4 | MSIHLGASVNDLPGLGTTAVGDLGRLGVKTIRDLLFYAPFRYNDLSVVKSIPSLQHDDTVTLRGTIKAISTHRSKNGRLNLTEAIFENETGSLKVIWFNQPYLEKTLPVGTTVSLAGQISQKFGATSLVSPVYEKTAVGTHTGRIVPVYGLTGSLSQRRLRGAIKYALKATSKIVDWLPEKILEDEDLLPLSEAISEIHFPSAGESLEAARQRLKFDELFLHQLLFTHMKRDREKISARSLECSTDEIKTWVEKLPFKLTNSQRVSAWEIVKDLSKETSMQRLLQGDVGSGKTVVAVLAAFVALRAGASVAYLAPTSILA... | Function: Critical role in recombination and DNA repair. Helps process Holliday junction intermediates to mature products by catalyzing branch migration. Has a DNA unwinding activity characteristic of a DNA helicase with a 3'- to 5'- polarity. Unwinds branched duplex DNA (Y-DNA).
EC: 3.6.4.12
Catalytic Activity: ATP + ... |
A0A7C7JQH2 | MSKLLVFRNILILLPYRIYSYKFYTKNLNIGVVLKKYSIPAVVFAGGKSSRMGKDKSLLPFGGFPTLIEFQFSKLKKIFNKVYISWKSEKVDLGKDVSIFDIEPNIFAPTIGLLSIFDKLESEYIFIFSVDAPFFGEREIGKVMDTFQNHIGEYEIYIPQHREGLEPMIGIYSRKLYPKIAHMVQDGNHKLKSLISNSKVLKIDFDEVEPFTNLNYWNEYQKARDRI | Function: Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor.
Catalytic Activity: GTP + H(+) + Mo-molybdopterin = diphosphate + Mo-molybdopterin guanine dinucleotide
EC: 2.7.7.77
Subcellular Location: Cytopl... |
V5WG17 | MLSCIMNVPRSHYHKILLFPLLAALLNWLAQPNELFLQGNWLFGLISYIPLYFLVTTAGLTRNQLRLSALIYALSFTLSSYFWLTNFGEYSLWTIGGVTVVYIVYHLGFFRLLYFLLAPGNHTPKSHPFRPLLFALAWTAFEFFKSRGYLAFPWNLAAFPFHNFIFINQISELTGIWALSFTVLFFQAGLAQILLRGRGGFEVQPANARFTGLGRFPSGLRSVAAALLITLCFSAYGVIRHGQISRMEQNAERTELVLLIQQNVDSWAESDPSTGMSIAMELTREGIAEALDQYGRQPDIISWSETSLSYPYTPESSFYR... | Pathway: Protein modification; lipoprotein biosynthesis (N-acyl transfer).
Function: Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation.
Catalytic Activity: a glycerophospholipid + N-terminal S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipopr... |
A0A1M5CU05 | MDIDGEISEVIFLCGFMGAGKTTIGQKLAAELGRPFLDLDDRIVEKAGKPIPEIFEASGEGRFRAIERSALLEVARQFNGVVALGGGSLQNQHLLDHLKCNGLLIFIEAPIPVIIDRISQDANRPLLLDEQGEPKDRDTLKKELKMLYEDRLPLYEQAMITLNIKAGESADQQVKTLINKIRNYVAS | 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... |
A0A0G0M4Y1 | MIKRRKTKEVKIGDVKIGGKNEIAIQSMCSTKTVDIKKTVAQILALEKEGCEMIRIGIPDLVSAKAIKQIKKLIHIPLVADIHFDPNLAIASIENGADKIRINPSNIPQKSLIQIIEKAKKFKVPIRIGVNAGSIRPLKEKITAEDLVKEAKKQIKFFGSLNFRNIVISLKHTDVFENIKAYEQISKFCDYPLHLGVTEAGTLFQGFAKNAIAISNLLMSGIGDTLRISLAEDPIEEIKAAKAILSSLNLYKKAPMFIVCPTCSRTNIDIIKISHILEEKLSHIKKPIKIAIMGCAVNGPGEVAQAKYGIIGGNKSAGIF... | Cofactor: Binds 1 [4Fe-4S] cluster.
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 5/6.
Function: Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphat... |
A0A7C3ZW89 | MSKKASTTRVCFLLGYPLGHTRSPSMHNAAFAALGLDYRYVPLEVKPEGLSAVFSALRIMENFGGANVTVPHKVAAMELVDGRTEEAERIGAVNTLFWRDRELWGDNTDAQGFLSSLVEDLGFHPRGRRVMVLGAGGAARAVLCALIGAGVEEIYVVNRTVERAQELAQRYGKVKEAPTLVPLGFFDSRFRSALKGCDLLINSTSVGLSRDDPPLFDYDLLPPGIAVCDLIYEPPLTPLLEAARGKRCRILNGLGMLVRQGALSFHLWTGKEPPLEEMRGAVGNSLDRLGA | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.
Function: Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydr... |
A0A7T5R8C5 | MFSEFREAVLETLKKEVPARAEDLVEPPEPKRFRGSGTSFREPPEGMGELGYPCFGLAKEQKKSPADIAKTLAVRLKTKTPISEVRAVGPYVNFFVDWNAFASSVKQASSKTWGSSSVGKNKTVIVEYSSPNVAKPMHAGHLMTTVVGDSIYRLLRAQGYKTVRINHIGDWGTQFGKLVVAYEKWGDEAALKKNPIKELVRVYVRFHEEAERNDALEEDARKAFALLEKGDKKLRATWKRFVELSLEEFKRTYAELGVDFDAWTGESFYEEMLGDVIEDALKKRIAEEEADGSVVIKFGDLPPMLIRKSDGSSLYATRDL... | Catalytic Activity: ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg)
EC: 6.1.1.19
Subcellular Location: Cytoplasm
Sequence Length: 569
Sequence Mass (Da): 63849
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A0A0C9R2V7 | MITEQTWTMMLEPDVPSCNELRISPTKHLWIKAVKKLTSERLGREGLAAWGSLAAAAAQPQEDSDLPDIEEEEPQGEITIVVAPPEVLLEEKQEKEEEPPVQPDVFKKGLLYKGIFCPSLTTSFHSSSLEKSYFQYSSRQRQKSLIMLNVVDLGLKIALISIWISRRTEKSSGLIETLSWVSCCMLANLVVCILGLWRWFSNNYLYWASIFTWLLINTQGFVVAGLNFYSQQRMMWYILFVVYAPYAMLPLPLRWCVVAGSGTVLTHMIMTIATIFLNQKHLQDLMCILRMLTTNILLYIAVNLVGMYTKYLTDRGQRQA... | Catalytic Activity: ATP = 3',5'-cyclic AMP + diphosphate
EC: 4.6.1.1
Subcellular Location: Membrane
Sequence Length: 721
Sequence Mass (Da): 82131
Location Topology: Multi-pass membrane protein
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A0A9D1PW85 | MSHHASGHSSMQRSPSALTAEAASAVSRLFVALPLPQEIRSALSALQSEWAEPFSLRWTRPETMHITLHFLGNVDNALIEPLAAALSTVTCPAFRLAFTHVGTFGRGDRTVLWAGCAPSKALDGLHDQVLAALATVLPDVCGDKARERSSTAGTARWTPHCTLARVRSMPQKGRSGGRGHEAKALQELVRSLRLPDTLSFAVSSLVLCRSVLSSAGAQHTPLFTRPLA | 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: 228
Sequence Mass (Da): 24376
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V5WHZ3 | MIVTIDGPAGSGKSTVAKMVGSRSRLVYLNSGNIYRAITSGLLKELGVDEVRGSIPDRAQSLVNTASEFHIQVSGGTDDASPAQQGDILFNGTLLGDEELRSDLVDSLVAQVSSIPEIRELVNTILRKEALDKDVVVEGRDMSTIVFPRAELQFYLDASIQARAKRRLDQGTSSLSYEELVDTIARRDRIDKEKDVGALKLSPQARYLDTSDLTIEQVCEIVLRSIREHK | Catalytic Activity: ATP + CMP = ADP + CDP
EC: 2.7.4.25
Subcellular Location: Cytoplasm
Sequence Length: 230
Sequence Mass (Da): 25247
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A0A1M4ZUZ2 | MTKDRSNQSSASNGDFSLPRGKILRGRKNFQRLFEGDVRILRKKHVGLRYHLTDDPSSGCLLGFIVKKSLGDAHKRNHMKRLLREAYRLHQHILTDPLQRIQRTLHGAFMAHTVDASFAEVEHDVTSLLAQVRDQLPTTSPDHS | Function: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of... |
F4KMX6 | MSSHLTNKQLAMKKDQVRIIFYGTAPFATACLERLVDEGYPIVAVVTAPDKPAGRGHRLQPSAVKLCATKLGLPILQPTNLRDEAFVQQLTELKPTLGVVVAFRMLPREVWSLPPWGTVNIHGSLLPQYRGAAPINWALINGESETGVTLFQLRHEIDTGDIIAASACPIESEDNFGTLYDKLMALGAELLAHGLSLLTQHEGRYPQALPQEERSDLHPAPKLTKENTRIDWHQSAHEIHNLVRGLAPQPGAWTMLELPNEEPLLVKIYATTLSQQEAVERPVGQCVSPRKGQLAVQCGDGLLLIEQLKPQGKKLLSARD... | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
EC: 2.1.2.9
Catalytic Acti... |
A0A1V5GJG0 | MQIVTPKQMAKIEERSEKLGVSKKQLMENAGKALADLIDNYCRKENNRTEERSVVFLTGKGNNGGDCYAAANILVYRGYRITIIDIGGQPETDLSKEMYLRLPKERINFIDGYRNKTVDAAIEAAELEYMTVGGDSSLEALENKKDRNPIDNILLHEKRRMQKVTKAVREADVLVDGVYGTGFHGSLDKNVASIFSIGTGAYCIAVDVPSGGNSTEGTVSNGTFKADETLTFGYIKTGMSQFPLKKYCGKVTIADIGLPAGVTDAIDGERKYYRIERNHLAAFPPKRERDSHKGNFGTVLVIAGSSSMRGAAAFASLGAL... | 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... |
A0A4U0PA47 | MSSVLAFDFGEARIGVAVGSTELGIAHPVETIAAEGNDARFARIGQLIAEWQPAQLVVGLPLAESGEEQETSRLARKFANRLNGRFGLPVALVDERYSSAAASAALNDTGVRGRKQKPALDQVAAMQILQGWFDGAAAQ | Function: Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
EC: 3.1.-.-
Subcellular Location: Cytoplasm
Sequence Length: 139
Sequence Mass (Da): 14678
|
A0A4Q3ZB62 | MRLFVAISLPEGLLDRLEALAARLALGRPTPRENLHLTLAFLDEVAETVLPELDDALGAIHLPSVPVAFTGLDLFGARSPEILHASVRQAPGLIQLHESVLRAARGTGLSLARRRYRPHVTLARFNRPPATDRLGAFLADNALAPLPGFEAESFALFRSTLGHGPARHEELARYPLGVLSGTSGPGLPEA | 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: 190
Sequence Mass (Da): 20379
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A0A8H4D327 | MFQKRQGNRTHVSPTYRRVSAKLKAPNLLKHDEASSQRNEQREVPFSVTPVEKSRRHRDAKVKKDTLSQYIKLTKPNLTVLVTLSSICSYAISPNTASVSELALLTLGTALCSGSANAINMGREPEFDKRMLRTSTRPVVRGIITPRQAFIFAAVTGTAGSLILLSGVNPTVAALGFSNILLYGWCYTSLKRKSILNTWVGAIVGAIPPLMGWAASSSLSHPGAWCLASLLYAWQFPHFNALSHNIASQYKQAGYIMTAAENPRLNARVSLRYSLLMFPICFGLSYFEVTDWLFCLDSSLANGWLTILAYRFWRQQNINH... | Function: Converts protoheme IX and farnesyl diphosphate to heme O.
EC: 2.5.1.-
Subcellular Location: Membrane
Sequence Length: 374
Sequence Mass (Da): 41495
Location Topology: Multi-pass membrane protein
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A0A8T4KFE9 | MINIDLPKHIAIIPDGNRRFAKQRRMVPWKGHEEGMKTAKKMLEWWVETDIQELSFWGLSTENLNRSKEEVKQLFRIFRESIKNWKKDIGKLSKKHEVRVRFYGDLEKFPEDMIKSMKEIEKDTEKYNKRFLNILLGYGGKHEIVTAVNKLMKSGRKFVTEKDIQENLFVKNNADLIIRTGGMPRLSGFMPWQTVYAELYITKALFPALTKREFLKAIKWFEEIQRNFGK | Cofactor: Binds 2 magnesium ions per subunit.
Function: Catalyzes the sequential condensation of isopentenyl diphosphate (IPP) with geranylgeranyl diphosphate (GGPP) to yield (2Z,6Z,10Z,14Z,18Z,22Z,26Z,30E,34E,38E)-undecaprenyl diphosphate (tritrans,heptacis-UPP). It is probably the precursor of glycosyl carrier lipids... |
D2RLU0 | MTKVFISAGEASGDLHAAALTRAILQQDPTAQVFGMGGDALAAAGGQVVFNYKDYSVMGFVEVLQALPRLLGLKKAFRRLMEERKPDVFVTVDYPDFNMRVAKEAKKLGIPVFSYIPPSAWAWRRGRAKDVARLATRVACIYPFAAKVYQEAGAAVEFVGNPLVDIVQPTLSPQEAEALVGKRSGHPLVLLLPGSRVKEITGVLPVMLQALPKIRARRPDVEFILQKAPSIDAALLQGILETSPVPVKVVEGHNYDVMTACDAALATSGTVTLEAALCGLPSVICYTASPLSMWIAKHMVYVKYIGLPNILAGKEILPEL... | Pathway: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
Function: Condensation of UDP-2,3-diacylglucosamine and 2,3-diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
EC: 2... |
A0A177ZKR5 | MSQLTRSFTNRKVKIKLLGIYLAVTVIPILLIGFYLNYSMRDVVLNNTINEVDANVDKLEMRLNTILDRAISISDQLYISNDLKKVLEQEYESNLEIYNAYAAYPIFDNYLRYYNEIENIRFYMTKEMITNSQFVYADQETRNQEWYQGAVERQGRISWEYIPDKWTKTSYLTLTRSVYGNNRELLGVLAIAISPDNLTSISKSELFDVFVSLDSEKIVHSKDPNYLGEYPFFIKKADIQDQKSIIYDTDFKQENYKIYLRSFKPSKTLENQIQITALIPVEDVIKDSKKVLYNGFLIVMICLLVSITLIGLFIKSFDKR... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 603
Sequence Mass (Da): 69777
Location Topology: Multi-pass membrane protein
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A0A1L8QRJ0 | MKAVDVLTYVQQGVADIGIVGSDVIYEDERDHYEMLDLEIGKCHFCVASTPNYEENDYRRKIIATKYPRTAARYFREKGEDIEIIKIEGSVEIAPILGLADAIVDIVETGDTLRENGLIVFEEMMPISTRLIVNQVSLKRKKQAVCQLVDKLEEHIQQKKVSATNENRSS | 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... |
R6AIY7 | MNSSLTVIKDCPNSHQNIGWSNLTDYIIKKINQKEEPVVFILWGNFAKSKKVFITNPKHLVLTSPHPSPFSARYGFFGSHPFSKTNEFLEKNGEETINWDLN | Function: Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine.
EC: 3.2.2.27
Catalytic Activity: Hydrolyzes single-stranded DNA or mismatched double-stranded DNA and polynucleotides, releasing free uracil.
Sequence Leng... |
A0A8T3XVJ8 | MKLKTEVVVIGAGPGGYVAAIRLGQLGKQVILVEKDGLEGLGGICMNHGCIPSKALIRASKFFHNIKSAGAMGINVSSVSLDASKLQDWKNGILKKLRSGIDFLCKKNNVKWIKGEAYFESSNTVKIRGNEEIDSIEFDYAIIATGAMPNSLPGIEFDGKNIISYNEILDSREIPKDLLVVGGGYIAVEMATCYAKLGSKVKLVHRRDQIFRGYDKDVVSVVQKQMQKDGVELILNSTISKIDKSSSRLKVSINSQEKGEFAVEVDKILVAVGVKPNSANLGLENTKVKVNEDDFIVVDKSMRSNNSKIFAIGDVATQPL... | Cofactor: Binds 1 FAD per subunit.
EC: 1.8.1.4
Catalytic Activity: (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + NAD(+) = (R)-N(6)-lipoyl-L-lysyl-[protein] + H(+) + NADH
Sequence Length: 472
Sequence Mass (Da): 51076
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I6TE69 | SLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLSSNLAHAGASVDLTIFSLHLAGISSILGAINFITTIINMKPPAISQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRXLNTTFFDPAGGGDPILYQHL | 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... |
A0A0G0JN40 | MIKKLVRKNIEKLKPYSCARMEYSGEGLFMDANENPLQSVKIGLKVGLNRYPDPYAMDLRKSLSNYLRVPAKNIFVSSGSDEIIDLLMRIFLNENDEIVIFEPTYGMYRASAEAANAKVKVCLLNADFQIDFRALPRYISKKTKMIFICRPNNPTGNLISEDDVISVCKMFDGIVVVDEAYIEFSSAKSVSRLSPLIQNLVVLRTFSKAWGLAGIRVGYAITSAEIINYLNKVKLPYNVSAVSQYIATLALKEPNQMIKLRDKIVSEREKLKNILEKMGFKVFPSEANFLLIKSEYSDKIFEKLIEEYRIIIRRFKNKPL... | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
EC: 2.6.1.9
Catalytic Activity: 2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Sequence Length: 350
Sequence Mass (Da): 39949
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A0A7J2TZ17 | VFDGKPPEFKKATLEMREEMKKEAEEKMKEALEKGEEAIKYAQATARVNEEIVEDAKKLLELMGIPIVQAPSEGEMQAAYIAKKGDAYASASQDYDSLLVGSPRLIRNLNITGKRKLPNKEVYIEVKPELIELEEVLKTLGITREQLIIIGILVGTDYNPEGVEGIGPKKALKLVKEKKTLENVLKEVEWKFDVRAEDIYNFFLNPPVTDDYKLEWKQPDEEGIIKFMVEEHDFSEERVRNGIEKLKQAFAKSQQKTLGSWFK | Cofactor: Binds 2 magnesium ions per subunit. They probably participate in the reaction catalyzed by the enzyme. May bind an additional third magnesium ion after substrate binding.
Function: Structure-specific nuclease with 5'-flap endonuclease and 5'-3' exonuclease activities involved in DNA replication and repair. Du... |
A0A2A5CII9 | MKKPRYYTAAATRELDRRAIEEHNIPGFELMQRAGKAAFNALLQNWPDIRKTIILCGTGNNGGDGFIIAGLAKTAGLEVDLFVAGDISSIKGDALKALDYALNNGTHTHPATKFYTADIEYKNRKDSGNTILVDALLGTGLSGKVREPFTQLINQINACNLPVLAVDIPSGLCSDTGKILGVAVKADLTITFIGRKIGLIRRSGPELTGKLLFDDLNLPEVIYSNVLFSK | Cofactor: Binds 1 potassium ion per subunit.
Function: Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX... |
I0HQ04 | MPATDVKSVAVAAPCGGTRPVSAPGAAPAAAVTEGWVHSTETCGTVDGPGIRYVLFLSGCPLRCAYCHNPDTWHRHDGTLTSVAEILTDIGRYRGFIQAKGGVTLSGGEPLTQPRFVKALLRGCKAMGLHTALDTSGYLGAKVDDEMMADLDMVLLDIKAFSEKTYHRLTGAELKPTLDFARRLAALGKPIILRYVLVPGWTDHDNEIRALAAFAARLGNVQRVDVLPFHQMGEHKWQERELNYRLAGVSPPSEELVEHTRSIFRDAGLQAT | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Activation of pyruvate formate-lyase 1 under anaerobic conditions by generation of an organic free radical, using S-adenosylmethionine and reduced flavodoxin as cosubstrates to produce ... |
A0A932LYN7 | MTAPAPPSWLEVTLTLPEPLADPAGCALLEWGAPGLVEETDGAGVRLRAYLAEPPRGFGRRLRAYLAALGTASGVPGPVSVRLARRRDPGWARAWRAFHRPLRFGRVVVAASWHRVRPVRGQVLVRLDPGMAFGTGQHPTTAACLGALAAEVRPDRPLLDLGTGSGILAIAAARLGARPVIALDTDPEACGAAAANCRRNGVGSTVRVRCGSLEVLRPRAAFALILANLTAAAHLALLPALRGHLAPRGRAVLAGILAAQAPDVRRAVRATGLAVVGRQRIGEWVALHVARPS | 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: 293
Sequence Mass (Da): 30660
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V5WE21 | MGFRDGCSGTRGVTEARVPQMPRAFIFLLRQVKMIGIIGAMEEEVQQIRQEIHDPRVVEKASYSFISGHVGDLEVVLLQSGIGKVNAAIGTTLMIEHYSPKFILNTGSAGGLLPELSIGDVVLAESAGYHDVDATAFGYAKGQIPRMPLVYAGDSRLLEIAQRCVANGMSFSTVRGLIVSGDKFLAHPDEINNLLADFPESAAVEMESAAIAQTCYQLNTPFLIIRSISDKADSTSPGDFQENLHTASMNSARTILELLRFYREHPGEA | Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; S-methyl-5-thio-alpha-D-ribose 1-phosphate from S-methyl-5'-thioadenosine (hydrolase route): step 1/2.
Function: Catalyzes the irreversible cleavage of the glycosidic bond in both 5'-methylthioadenosine (MTA) and S-adenosylhomocysteine (SA... |
A0A191T4D3 | MSLDDSLERTEGFYFENNLIDSSKEGFDLITSDPKQTNFLIEKSSIEDIVVDKNQSLENDVEDELEEYEPPNKPTTPGAGLWLFCETCKQMLFIKHIKLRVCPGCNHHFRMRSTERIEMLIDEDTWDPINEDMMPVDMVELATDSYKDRLEEEQEWAGMPDAVQTGFGELRGIPVALAVMDFEFLGGSMGSVVGEKITRLIELATFYKLPVILVCASGGARMQEGALSLMQMAKISSALRVHQLINKLMCISILTSPTTGGVTASFGMLGDLIIAEPGAYIAFAGKRVIEQIYKVEVDEQRQRAENVFDHGMIDLIIPRT... | 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... |
D2RNT4 | MSYFPLMIQLDQAPVLLVGGGRTAFHKARILVDFGACVRVVAPEVLPELEQLPVQVERRPFSGADLEQSDWTLVVAATDCRTVNGQVSRLCRQRRIPVNVVDDPELCSFYFPALLREGEVVCAVSSGGRSPLVTQYVKEKIRQVLPAGLGWINEQMGAFRKQLKGEETNPDKRKKRLQDKLRSLLESQEHTL | 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: 192
Sequence Mass (Da): 21556
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A0A0F0GQI9 | MTSLFDEPRRLPGTLITLDGPGGVGKSTAAKLVAETLTAAGVPVHATVQPSRAPLGELARHGTDTFRGMALACLCAADRHHQLDAEIKPALRDGQIVICDRYVASSLVLQGLDGLSAETVWQLNHGVYRPDLSVILNGDPAVIDHRLRTRGGHSRFERAEDNSDMESGLYVHAVVDLQAKGWLVETLDCTTDDAATIAARIVSLIHRVIEEKIAVCR | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
EC: 2.7.4.9
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Length: 217
Sequence Mass (Da): 23359
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A0A0C9QEK2 | MFTTLRNAAIMSDDEHDLFPANLLDRLPNQRQENGLLVRPLRTTDYDKGFIQLLGQLTDVGHIGRDQFLNRFHSMKSAGGHYVIVVEDLEVGKVIGSSTLVVEQKFIHNCALKGRLEDVV | Pathway: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route I): step 1/2.
EC: 2.3.1.4
Catalytic Activity: acetyl-CoA + D-glucosamine 6-phosphate = CoA + H(+) + N-acetyl-D-glucosamine 6-phosphate
Sequence Leng... |
A0A1N7C8E5 | MDRLAKLPIFLDLAGKRAVVVGGGGGATWKVELLAAAGAKVEVFAHDPAPALSELAQAQPSSVTLRGERWEGADFTGVVIALLEPEHGDGEITAFRAKAKAAGAVVNVIDTPHACDFQFGTIVNRSPTIIGISTDGAAPILAQALRRRIEAMLPPGLAAWTAAAKAFRDELAARLPGKPARRRFWERFVDLLFAHDRQEEAGSAEALRRIADAVAAGDPAMAGPHLTVLTVDPLDPERLTLRDIRLMQGADLILHAADIAPAILDLARREARRMPLPADEAEFIAGLDPETPLAIVKLAAAPAAARPASSGGRTRR | 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: 316
Sequence Mass (Da): 33390
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A0A932LWE2 | MKIYTRTGDKGKTGLFDGTRVSKADVRVEAYGAVDETSALLGVAAANTTDVELQGILQDLQRDLFAVGAQLADPKWGVKARKEKTRLSQSRVAELEALIDRAEAELPPLKRFILPGGSPAGAVLHLARTVCRRAERRIVALAATVTVSPVLLAYVNRLSDLLFVLARLASRRAGTEEIPW | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 2/7.
EC: 2.5.1.17
Catalytic Activity: 2 ATP + 2 cob(II)alamin + reduced [electron-transfer flavoprotein] = 2 adenosylcob(III)alamin + 3 H(+) + oxidized [electron-transfer flavoprotein] + 2 triphosphat... |
A0A842Q781 | MVEIRKDYLLNRWVIISEKRKFRPKPKDEPKKKKLPKKSKNCPFCPGNEKMCPEPIIEKPNKNWKIRVIGNKYPAVSKEEKFREKFGRLTTKKTGYGSHYLIIDTPKHNSYPANYKKKEWRLWFETIKDVFNEEAADENIQYILAFKNRGPEAGASQPHPHTQIISLPAVPHLINEEMSGADDYYTFNGKCIFCEIIKMESKFKKRVVFENKDVIAFCPYAPLWPFEVWIFPKEHTPSIQMSKSSEDGILKALSKVLKTYYKVLDDPPFNLYMHTAYLRMKDHVPQKYHFHIEINPRLEKDAGFELGAGMNITTISPEEA... | Cofactor: Binds 1 zinc ion per subunit.
Pathway: Carbohydrate metabolism; galactose metabolism.
EC: 2.7.7.12
Catalytic Activity: alpha-D-galactose 1-phosphate + UDP-alpha-D-glucose = alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose
Sequence Length: 328
Sequence Mass (Da): 38430
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A0A1X4XX03 | MKNVLLEKIEKEPLSHKEALELFQNADLLDLALMAKKIKFLKSGNKVYFTINKHINYTNICSSKCLMCAYYRNEDDKDAYTMSFEQVEKELSNIEDLHEVHIVGALNPKLDFSYYITLLETVKKATPNANIKAFTAAEIDFFSKISSLSHKEVLEKLKAAGLQTMPGGGAEVFSERVRKKLYPKKIGFEEWAQIHALAHSMGIKSNATLLFGHIETKEEIIDHLFKLRNLQAQTKGFLCFVPLLFHPENTIFEKHIQKQSAVFQLKVLAISRIILDNFDHIKAYWVMMSDSISQVGLHFGADDIDGTIEKENIFHAAGAT... | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Pathway: Quinol/quinone metabolism; menaquinone biosynthesis.
Function: Radical SAM enzyme that catalyzes the addition of the adenosyl radical to the double bond of 3-[(1-carboxyvinyl)oxy]benzoat... |
V5WG69 | MNSFVDEMKIGVASGNGGPGCVSFRREKYVPKGGPDGGDGGRGGDVIFRVKDNLKTLTHLRPNKTYRAQNGLPGEGRKKHGKDGEDLVVLVPPGTQVKDAETGDILLDLVENNSEHRFLIGGIGGQGNTHFATSRNQTPRFAQPGMPGETRKIRLELSLIADIGFVGYPNAGKSSLLGVLTSAHPKVGAYPFTTKIPNLGVLRAFNRDIILADIPGIIQGASEGAGLGYRFLKHISRTAALLFLVDLSDYQDPVEVFENLKQELHAYEPELLKRPHYILATKMDIPEARERLDEFRSKVSEEVLPVSSATRDGIDELIKK... | Function: An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis ... |
A0A1F4VRR7 | MLVLYCYLQPMTDLKDRAKAILASYNIENLNSRKVELEKESLSPTLWDNWEHAQEIMKELDQVKKELDEATLLELMLEEQNETELAKEITRLETKLFISGPYDKGPAILSIHAGQGGTEAMDWSGMLKRMYLRYCERMGWKAEITDETVGEEAGIKAVYIHIYGNPAYGFLKGESGTHRLVRQSPFNANDLRQTSFAGVEVIPLIEKDISGIEIKDDEIEVTTFRSGGAGGQNVNKVETAVRIKHLPTGLVVSCQIERTQHRNREIALNMLKGKLIALREAEALAKEKTLKGDYIIAGWGNQIRNYILHPYKLVKDLRTQ... | PTM: Methylated by PrmC. Methylation increases the termination efficiency of RF2.
Function: Peptide chain release factor 2 directs the termination of translation in response to the peptide chain termination codons UGA and UAA.
Subcellular Location: Cytoplasm
Sequence Length: 355
Sequence Mass (Da): 40212
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A0A6P0YD26 | MWVTSSLATVLTPTTVALGNFDGLHRGHRQVVQPTLKLDTRKNSLYVYPSQTDTEVDKDTKLQLLNSSWYYQGELDKNDDCQEPKIYSTVVTFNPHPQEFFSGKPKKLLAPLDEKLALFQQMGVEQVVLLPFDQELANLTPTQFVEKILVKHLKASKVSVGWDFRFGRNRAGKATDLQTIAANYDIEAAIVPLYTCENGERISSSIIRQALEQGDLKKSNRLLGRPYSLVGQVVEGQKLGRTLGFPTANIQLPPQKFLPRFGVYAVEVYIFEQKQLQENDSGDRPYFG | Pathway: Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step 1/1.
EC: 2.7.1.26
Catalytic Activity: ATP + FMN + H(+) = diphosphate + FAD
Sequence Length: 288
Sequence Mass (Da): 32513
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D3RQ52 | MESSFSPFAFPALEPERLRILVASSEAHPLIKTGGLADVSASLPAALRQLGHDARLVIPGYPLAMRQLREPKPLGEIRVPGYRTAIRLVEGRHPDHDLPVYLVDAPEYFAREGNPYCDPTGRDWGDNPDRFMLFCRVLALMAQGLPAIGWRPDVFHGNDWQTGLAPTLLQEAPWSPARVFTIHNLAYQGLFDRATFDRLELPPALWNLAGLEFHQRLSFIKGGIVFSERINTVSPTYAEEVRTARFGCGLDGLLRQIGQRFSGILNGIDYQVWNPAGDPLILQNYDAERFGLKTENKLDVQRELGLPRSEDAFVLGYVGR... | 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: 511
Sequence Mass (Da): 57012
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A0A410UGT9 | MNPFFGSVFWLAVTLGVLVTFHEFGHYWVARRCGVKVLRFSIGFGNAIWKHIGRDGTEYQIAAIPLGGYVKMLDAREGEVDLALRDQEFTTQPIWKRIAIVAAGPGFNIIFTVVAFWLMFVLGRADYAPVVTAAPQSMAAEAGIQPGDRLLTVGGEPVTSWSGSIDAIANALLSRTPLAITVSDRNGAQRSLVLPLNRLPAGEDIGHYMGKLGLQLAPPPAIVDSVSPSDPASLAGLRAGDKILSVDGIAVKDSSDLGKQIGIAAAKSPQLTLEVERHGKPMPFSMTARMESPDGGAPRWVIGVTQVAPEAATQHYGPLK... | EC: 3.4.24.-
Subcellular Location: Membrane
Sequence Length: 449
Sequence Mass (Da): 48117
Location Topology: Multi-pass membrane protein
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A0A2A5AUP0 | MSANSLKSQQRISNISRRNFLTRTSLLPLGVGLGIIPVLAQSAESGVASNIKALTFDVFGTVVDWRASIIREGQLLAARKSFDVDWAEFADRWRSGYGPAMSKVRSGELPWTKIDDLHRMILDDLVVEFNLEGLTEAELVNFNHAWHRLSPWPDTVAGLNKLKTKFIITTLSNGNVSLLTNMAKNAGMPWDAILSAELSGHYKPDPEAYLKAADLLSLAPEQVMMVAAHPGDLRAAARAGLRTAYVIRPLERGPGRPVNTNPDGEFDYTANDFLDLARQLGA | Function: Catalyzes the hydrolytic dehalogenation of small (S)-2-haloalkanoic acids to yield the corresponding (R)-2-hydroxyalkanoic acids.
EC: 3.8.1.2
Catalytic Activity: an (S)-2-haloacid + H2O = a (2R)-2-hydroxycarboxylate + a halide anion + H(+)
Sequence Length: 282
Sequence Mass (Da): 30967
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A0A6N7SJE6 | MDKKTVTVIGGGPGGYVAAIRAAQLGAEVTLIEKKRMGGTCLNIGCIPTKALLDSAHVYHEAGASAGIGVVASPHLDWEMVQERRKSVIDRLVSGVEGLMRSNRIRVLYGSAGFLDPHTVCVNMADGQKQRVSSDFFILATGAEPLVPPIPGAGGDICIDSTAALSLEKVPDSMLIVGGGVIGVELATAYHEFGTKITIVEMAGNILPNMDRTLSEKLKADMEHRGMRIMTGAKVCKFEKKGDMAACCVEQENTQITLEAEKILLCIGRKASLEGLNLEKAGVRVERRILTDSFMRTSAKHIYAVGDCNGQLMLAHAASE... | Cofactor: Binds 1 FAD per subunit.
EC: 1.8.1.4
Catalytic Activity: (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + NAD(+) = (R)-N(6)-lipoyl-L-lysyl-[protein] + H(+) + NADH
Sequence Length: 467
Sequence Mass (Da): 49686
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A0A257GTI4 | EHKQVAHLIEDLQSGKAAIAAGRLLRPSDLGLAASLGIASLKVHRKLKVAILSSGDELRPLGQPLDAGSIYDSNRYSLTGLLNRLNLEIIDCGIVRDDPASLKAAFLEAAAKADVLISSGGVSVGEADFTKQIMQELGDVGFWKIAMRPGRPMAFGMLKPVEGSQRKTLFFGLPGNPVAVMVTFYQFVRSAL | Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
Function: Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP.
EC: 2.10.1.1
Catalytic Activity: adenylyl-molybdopterin + H(+) + molybdate = AMP + H2O + Mo-molybdopterin
Sequence Length: 192
Sequence Mass (Da):... |
A0A4U1BPU1 | MRYFPLFFDTQNQSLLIVGGGEVAARKLTLWRRTQMDIVLVAPFLCQSLQLAQQRGDFHWFNGEFTDELVAGKAGVIAATNNEALNVHISHLAKAEGAWVNVVDNPEACTVITPAIVDRSPMVVAIGSEGGAPVLVKELRKRIETWLPNRLGKLAQFMAERRYRVPLSERKAVWERFLNSNGLTLEPASEQRFEAALAADSSTLKALFLSAETDSQMLPIAAVNEMQEAESVIHSRALPKAIDELCRRDAERHQLDLHQALAQPGWPKVVVVSADELPHWREQFQLQGVTTAVARCGSLETV | 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: 302
Sequence Mass (Da): 33528
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A0A7S8HEV6 | MRRLKRIASRKKNTTLKPVHSGPTAIHMIEVEGGDFHSHTAERIEEVEKHLQDTPVDWIHIDGVHDVNTIEKVGGILNLHPLVVEDILNVDHRPKLEVKENHLLVILKRLAFHPEKVEVLEEQISIVIFDKVIISFGEAGSSFYERVITQAEEQRQDHLLDQSDGLFHTMLDVIVDEYMKVTEEMGDDMEELEDRLIMHPRQNDLQTIYEYRHAVLSFKKRALPVQDMLIKLLQQEFDMIQVNMREYFNDIYDHMVVVADAYEAHRGQVASLVDLYYSSISNKMNEIMKVLTIVSTIFIPLTFIAGIYGMNFAHMPELDE... | Function: Mediates influx of magnesium ions.
Subcellular Location: Membrane
Sequence Length: 348
Sequence Mass (Da): 40597
Location Topology: Multi-pass membrane protein
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A0A932MFQ4 | MGSVTVEPRARLAWQVLDLGLQPFGAVLRQQEELVRQRLLGTIPDTLILVEHPPVVTLGRAKQRGNLRLDPETLLARGIEYFEITRGGDVTYHAPGQVVGYPIFDLRQHGRDVLRFCRGMEAALIAALGDFGILAGAVAGKAGVWVGEK | Pathway: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 1/2.
Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-A... |
F7RYI5 | MKHIHILGICGTFMGGIAALAKALGYQVTGSDSNVYPPMSTQLEKLGINLFQGDDLQQLQPTPDLVIIGNALSRGNPVVEAVLERKLAYQSGPQWLGEALLRERHVLAVSGTHGKTTTASMLVWVLEQAGINPSFLVGGVVQPYNETARLTDSPYFVIEADEYDTAFFDKRSKFLHYFSDTLVMNNLEFDHADIFSDLAAIQQQFAYVLRTVPRNGHVIYPPAVKALAEVVAKGCWSERVCTGENEAWDTKLLNSAGSTFAVLHNGAEVAQVTWDLIGKHNVENGLMALVAAAQVGVEPKLAAEALSRFTSPARRLQLRG... | Pathway: Cell wall biogenesis; peptidoglycan recycling.
Function: Reutilizes the intact tripeptide L-alanyl-gamma-D-glutamyl-meso-diaminopimelate by linking it to UDP-N-acetylmuramate.
EC: 6.3.2.45
Catalytic Activity: ATP + L-alanyl-gamma-D-glutamyl-meso-diaminoheptanedioate + UDP-N-acetyl-alpha-D-muramate = ADP + H(+)... |
A0A1C7DF57 | MTKLKYVYEALKRASSYLDENGREEGAARILLQHELGLTYSGLIASMHDEISEQQFGEFWAKVEQHAKGIPVQHLTGSEEFYGRKFLVNPDVLIPRPETEELIEETLKLIDRYMTKKELAIADIGTGSGIIAITIKCELPEARVTATDISQLALQTAAENARRLNSKIDIRLGDLSKPLKGEKWDVILSNPPYIAHAEAPGLSDSVRDFEPHSALFADKEGLALYEKMALELPELLNKPGIIGFEIGYQQGQEVQKMLQDAFPDALVYSKKDINKNDRMVFAIIT | 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... |
A0A7V4UZP5 | MFKNGYIITGSIATGKSSVCGILRSKGYVVVDADKIAHEELRNSKDEVQSLFGTKCIRNGDVDRKALGRIVFNDVEARKKLENILHPKIKKVIMDLAVKLEAEGNLFFIDIPLFFETNNYDFDKVVLVYTTRDLQLKRLLTRDCIGEADAKNRIAMQIDIEEKKKMSMFVIDNCGNYIDLQKNVEDFLQKIKG | 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... |
A0A8T4KSG8 | MFGFLKDKIKKAVQSISDKFEKKEEPVQEPQEIKPVVEEKIKPQIEIQKEVEEIKKIEPEIVEEIKEEVLEQIPETEEIEKTLAPELVEETEKISPEIPSEKPIEVKPEFAVVEKEVEKPKKKGFFEKVFEKVVKKVVEKKLSEKDVVPVLNDLETGLIESDVAYEVAEKIKNDLKNNLLDREIKRGTENKIVTESIRNSLMEILNVPAVDLASLAKQKKPFLIVFLGFNGSGKTTSLAKVGKWLIENGYSCVFAAADTFRAAAEEQLEEHAKRIGVKVIKHQYGADPAAVIFDAVEHAKANGIDFVLADTAGRAHTNKN... | Function: Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Acts as a receptor for the complex formed by the signal recognition particle (SRP) and the ribosome-nascent chain (RNC).
Subcellular Location: Cell membrane
Sequence Length: 415
Sequence Mass (Da): 46727
Location T... |
R6B107 | MNIVIGKIVNTFGIKGELKIVSNFEMANRAFKKGNKIIINNKERLITNSRFHHHNYLVEIDNIKNINEVTYLIGAKVSINKDELKLEENEYLMCELDGYDVYNGDKYVGNVEEVVINEVNPLIKVNGHYIPLQKNFIKKVDVNSKKIICQNIDELVREG | 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 ... |
A0A1M4WD95 | MINIVVFASGSGTNFQSIINATEDGQIEGQVRGLVTNKNDIQAIRRARKHDIAHVTIDPADFTDRSDYVGELLDQLAAWETDLIVLAGYMIKIPAELIKKFENRIINIHPSLLPKYGGKGFYGHNVHRAVLDNNETESGCTVHIVTREYDEGPILAQKKVPVYESDDPSTLAKRVQQQEHLLLPEVIAKLANELKQKNNS | Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide from N(1)-(5-phospho-D-ribosyl)glycinamide (10-formyl THF route): step 1/1.
Function: Catalyzes the transfer of a formyl group from 10-formyltetrahydrofolate to 5-phospho-ribosyl-glycinamide (GAR), produc... |
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