ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
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A0A1V0PWK5 | MTARLRDEAGLIRLAALFMTRLPVRVEAEYSPERMRLASAWFPLVGLGIGAVLALAYGLAALVFPPLVAALLAVALGVRLTGALHEDGLADIADGLGGAADRARAMEIMRDSRIGSYGAVALGLVLAVKVAALSHLGSAAMAGLIAAHGLSRLSPVLMMARLPYARSDGKAAFAGTGPGPRGLRIALATSGVTLLGLGLTVGPVAALVTLIALAAVLIRMEAMFRWRLGGYTGDGLGAVQQLSETAVLLAILACV | 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... |
A0A6G1DLG6 | MALRFEVLGRFNRARAAQLTLPHFTCQTPLFMPVGTQGTIKGLTTDQLEEIGCQIILGNTYHLELRPGSQLIDDLGGLHKFMNWKRALLTDSGGFQMVSLLHLADITEEGVTFQSPVDGKPMLLTPEESIHIQNNIGADIIMALDDVVKTTITGPRIEEAMYRTLRWIDRCIAAHKKPDVQNLFGIVQGGLDPVLRDICVKGLVERNLPGYAIGGLAGGEDKDSFWRVVAQCTAGLPEDKPRYVMGVGYPLDIVVCSALGADMYDCVYPTRTARFGTALVPEGVLKLKQSVMATDERPIDPTCPCMVCKNYTRAYLHCLV... | Function: Catalytic subunit of the queuine tRNA-ribosyltransferase (TGT) that catalyzes the base-exchange of a guanine (G) residue with queuine (Q) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis... |
A0A1V0RD32 | MLLEVYNKFGLTLTRGNGVYLYDDKNREFLDFSSGIGVCALGYNHAHFNEALKKQIDKILHTSNLYFNEQVLKATKNLTKASKLSRVFFTNSGAESIEGAMKVARKYAFNKGIKNSSFIAFKNSFHGRTLGALSLTANEKYRKPFKPLINGVKFVSFNDLESVEKLVNEKTCAIVLESVQGEGGINPASKEFYQGLRRLCDERDILLIADEIQCGMGRSGKYFAYEHSEILPDVLTSAKALGNGVSVGAFALSEKVAKNSLVAGDHGSTYGGNPFACAAVNAVFEIYAKEKILSRVLKLTPHLEKVLDEVAGEFDFCGER... | Cofactor: Binds 1 pyridoxal phosphate per subunit.
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 4/4.
Catalytic Activity: 2-oxoglutarate + N(2)-acetyl-L-ornithine = L-glutamate + N-acetyl-L-glutamate 5-semialdehyde
EC: 2.6.1.11
Subcellular Location: Cytoplasm
... |
R6XFU8 | MIYVILGTTASGKTDLAIRLAKEFSMPLISCDAYQVYKEFELGTACPRDEELEGIDHHFFKDYSIDDPIDVKKYQKEVRKLLDEYLEKGQDVILSGGTFLYVRAALFSYEFPDEEENNTYDSYSDEELYEMLKNKDPELAATLHPNNSRRVKRALINLDNNKKANKDDLKLLYPARFFAIDKSIEEVNQNIVLRCDKMFEQGLIEEVKKIVVTHKDLTTAFMAIGYKEVLNGLQENKTIEEIKQDVIVHTRQYAKRQRTFLRHQFKNLIQLKSEEIYKLISLDQKKKTRTIASLGKANYSKIENKKVLVCGLGGVGAIVV... | 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... |
A0A142Y6P9 | MTAIDLATLANRVHGELFARSNESQSNVPLITGASPLADAKPGHITLIDNEKYLPRLENSRAAACVTRQTFPNCSIPQIVVPNPHEAFAQICQIFRPACIVRSATGIHPTAVVAETAQVSLSAVVEAHAHVGDHSQIGDRTHIHRGATVMEGCKIGEDCQIFPGVVLYPGTVLGDRVVLHANCVLGAHGFGYRMVDGKHVSTAQLGWVEIEDDVEIGASTTIDRGTFGATRIGAGTKIDNLVMIGHNCSIGKHNLICSQVGIAGSTSTGEYVVLAGQVGLRDHIHIGSRTMVGAQSGVASDAPEDQILLGSPAIPRMEQA... | 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.... |
A0A2M7H4N5 | MVSILATTAAFLLVLSVLVIFHECGHFLAARLFKLKVDEFGFGFPPRLFGKKYGETLYSVNAIPLGGFVRIKGVAGDDPDMQRDKDDRSSFSSRSPLVKIVVLTAGIMMNLLLSVLLFSGVFMLGVPTTIDQVTEGAVVSDQRLVVTNVGESTPAQAAGVMAGDVVLSVDGAVDPTAAELQEQLGKITDAEVELEIKRGDENIKLSVTPGPIQYGDAGYIGIGVGIEDVVTARYGLVSSVAQAVKTTLVITKQIFVALVNLFLDLFLKAKVSDDVSGPIGIAVLTGQVASLGATSLLQFMAVLSINLALFNLLPIPALDG... | EC: 3.4.24.-
Subcellular Location: Membrane
Sequence Length: 368
Sequence Mass (Da): 39128
Location Topology: Multi-pass membrane protein
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A0A2U9PP49 | MARSRWEGGDEPMTTNTSRVLILLRHGESTANADDRFGGWLDYALTNRGRDQASAAGRMIGDAGLRPTAVHTSLLVRAIDTAKLAMAETNSQVPAHQRSWRLNERHYGVLQGRPRAAVRAEFGDQLYTEWRRSYHLAPPALDADDPTHPRHDARYAALPPDELPSTESLAAVRRRLVPYWQDAIAADLSAGHVTLVVAHGNSLRALCTHLDGLTPDRVRTLEIPTGVPLRYDLDDNLRPLIPGGVYLDTTQASTAPTALAG | Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.
Function: Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
EC: 5.4.2.11
Catalytic Activity: (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate
Sequence Length: 261
Sequence Mass (Da): 28603
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A0A0W0S5E3 | MTQTVAVSKLTLISIKTISYGHLLRAFLFGLILPLSFAPFHIPGAAILSIAFFYAQLIDEKNPHPILNGLFFGLGYFGLGISWVYVSIHEYGHLNSLVSALITLFFLLYLSLFPALMAGICKRLLHPRLPIYSCLLFSALWVLCEYSRSTLFSGFPWLLLGFGQFDAPSKHLLPIIGVFGVGFLTCFAASLLTTFTQFKGKRRFLALTIFVFLLLSPMLLKHINWSKPKAESLSVGVIQANLSMRDKWDESLFWQLLQRYKDETEKLLGTQLIVMPESAIPLPPSYVEDFLLEMHEKAQQSGSAILLGIPKPTMIDENSY... | 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... |
A0A0D8CIE8 | MLSTVRAKQLIAICGVSLMLAACSSNEAPEYVERPVSELYNGAQDLLDAKEYQQAAEAFDEVERQHPYSVWATKATLMSAYSYYQDNKYDDAINALDRFISLHPANPDVPYAYYLKALSYYEQISDVGRDQQMTQHAMDALDDVIRRFPDSKYARDAKLKKDLTVDHLAGKEMDVGRYYQDRNEYLAAINRFKAVIENYQTTTHVPEALARLTECYLSLGLEGEAKRTAAVLGHNFPGSEYYSESYSLMLGEEAPEREEESWWDATTNSISSLF | Function: Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane.
Subcellular Location: Cell outer membrane
Sequence Length: 274
Sequence Mass (Da): 31182
Location Topology: Lipid-anchor
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A0A1V8M1G2 | MHTDFWLERWEQNQIGFHEQEINAHLQKFWETLDIPANSKIFVPLCGKSRDILWLLSHGYQVVGVEISPLAVQSFFSENQLEPIITDCGAFQCWETEGLSLYLGNFFDLSNEHLNDCLAIYDRAALIALPSEMRQEYVQHLNKIAPALEHTLLVTLEYTQYEMPGPPFSVDDNEVHSLFGKTYAIEPLSAEDVLQNNENFRARGLSNLKEKVYRLSKRPDVIC | Catalytic Activity: S-adenosyl-L-methionine + a thiopurine = S-adenosyl-L-homocysteine + a thiopurine S-methylether.
EC: 2.1.1.67
Subcellular Location: Cytoplasm
Sequence Length: 223
Sequence Mass (Da): 25720
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A0A1V8M3K1 | MRRILALLFILGLTGCATLTNMTDSVGDLFKDSDNSEPPAELTEYQPEVKLEVLWDKSDGNGTDDLALNLVPAVADGRVIIADHDGLIQARSLLDGELFWEVETDLPISSGPVIDGDLLFVGTSKADVLALNTNTGEAVWKHQVSSVVLALPVMVGNNLIVRSADGFDVALNREDGTQVWVVEHSIPALTVRGDGAPVAVGNMVIIGYANGKLIALNSTDGAHIWEASVAVPHGRSEIDRLSDLNGTPVLRDDIIFVSSYQSGVNAVMPIDGEVLWRNETISAYQGLSADYSYLYLCDANSDVWQLDQRNGASYWKQTDL... | Function: Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane.
Subcellular Location: Cell outer membrane
Sequence Length: 393
Sequence Mass (Da): 42702
Location Topology: Lipid-anchor
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A0A142Y2V1 | MYHQTIVKTNAEDVALAAKDWLIETIQESIATRGFCSIALSGGSTPKRLYQLLAESSLEELDWSKVTLIWGDERNVPHDHVDSNYKMVREAWLDRIDPRHSRQLPHAFPVQISVNSPDRAAAEYELQIRRAIDPKGEYTNDFPPIDIILLGLGDDAHTASLFPETDALEETSRLFVANYVPKFAAYRLTLTAPMINSARNVAFLVCGISKRPALEVVLHGPRYPSEYPAQLVEPKHGRLLWFLDSAANPDQS | Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 2/3.
Function: Hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate.
EC: 3.1.1.31
Catalytic Activity: 6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate + H(+)
Sequen... |
A0A1V5UNJ0 | MLDFESVILNSTEILKLAMPVLIVLFGLLVGSFLNVCIYRLAKNESIVYPNSHCPKCWTRLGFLDLFPVVSYVALGGKCRYCARPFSPRYAFVELLTAYVFFAAYMICGFNLKLAVYLYMFSVFIVITFIDFDWQIIPDQITINGTAAGLLLSYICWLRPDSAALTFYTPLNDSIWGVLSGGGILYSISVLSGGGMGGGDVKLAALIGAFLGWKTTLLGLLLACFIGSFFGVSMIILGYKKRKDCVAFGPYIALGTAIVMVYGNQETINLYFKLVDLMTGIY | Function: Plays an essential role in type IV pili and type II pseudopili formation by proteolytically removing the leader sequence from substrate proteins and subsequently monomethylating the alpha-amino group of the newly exposed N-terminal phenylalanine.
Catalytic Activity: Typically cleaves a -Gly-|-Phe- bond to rel... |
A0A2U1LN49 | MEGKVVAKSDKDDQSFSTQTTAEIRNNVPFIIGVAGGTASGKTTVCNVIMSRLHDRRVVLINQDSFYHSLNDEQSANPQEHNFDHPDAFNMELLLSCLETLKKGESVNIPSYDYKINKNSGPGRMVSPSDVIILEGILVLHDERVRDLMNIKIFVDSDSDVRLGRRIKRDTVERGRNIQYVLDQYDKHVKPSFEEFILPSKKHADIIIPRGADNDVAIDLIVQHIRTKLGQHDLCKIYQNLFVIPSTFQIRGMHTIIRDVKTRKHEFVFYADRLIRLVVEHGLGHLPFTEKQIITPTKSIYTGVVFCKRLCGVAVIRSGE... | Pathway: Pyrimidine metabolism; CTP biosynthesis via salvage pathway; CTP from cytidine: step 1/3.
EC: 2.7.1.48
Catalytic Activity: ATP + cytidine = ADP + CMP + H(+)
Sequence Length: 966
Sequence Mass (Da): 107281
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A0A1V5U5X2 | MASVEHKISVSESEANLRLDKIISDKIAEISRSMAAKLISGGNVVSSSCGKLMKPSYAVKESEIITVYIPEARPLDVKAENIDLNIIYEDGDLIIINKKNGMVVHPAAGHQSATLVNAVMGHCDDLSSIGGVIRPGIVHRLDKDTSGIIIIAKNDAAHNGLSDQFRDRTIKKTYYAIVCGEIKKSKFAVDLAIGRSASDRKKMAVIQSDTHKAREAFTEFELVSVRNGFSLLKAMPRTGRTHQIRVHLSHVGFPIAGDVLYTPPAMYKALARKKYFSDRLWLHAAEIEFKHPASGKILKFQTGLPDEFDIFIKNI | Function: Responsible for synthesis of pseudouridine from uracil.
EC: 5.4.99.-
Catalytic Activity: a uridine in RNA = a pseudouridine in RNA
Sequence Length: 315
Sequence Mass (Da): 34708
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A0A7K0K673 | MREPGLAHDLDRAGHGFGDGAVGGRGSRGGDGEGEEHGASLCGARPYTGRVKAGGAERAASTRGAGERIPAWVFIALGGAFGALARGGLDALAAAHPWSLPVPGFLPLMWSTVVVDLVGAFFLGALSAILARRAAPSRGRVNLRFFAATGFAGAFTTYGTLISATRSGMSAAPAIDGILASAAASLLLLVIGVACAGAGWLLLRALLQGDEGDGREGGGR | Function: Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Subcellular Location: Membrane
Sequence Length: 220
Sequence Mass (Da): 21979
Location Topology: Multi-pass membrane protein
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A0A2M7H4M2 | MSKTTYEAIIGLEIHIRLDTKSKIFSGESNAESEQPNTHVSPISLGHPGTLPQLNQEAIRLGMMLALALNCEIPDFMKFDRKHYFYPDLPKGYQISQYDKPLALNGYLEILPDDIHSKRVRIERIHLEEDAAKNKHSHAGDTLIDFNRAGQPLAELVTQPDLRTAQEAKVFAQELQQIARYVGASQANMQHGHLRCDVNVSLRPIGDEALYPKTEVKNINSFKAIERAVEFEIKRQTEMWDNGSAPEITTTRGWDDKRGISIEQRTKEGEADYRYMPEPDLPPVIHNREDIDNLRSRLPELPSARRQRFRDEYNLSYHDA... | Function: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an ... |
A0A0S7ZKD4 | MRTESDYLIIGKVCRPFGVAGELKVLPITDDMRRFGKLKFIYHKRGKSFTKIPIETVRYTKQSVILKLKDYNCRDSVAVFSGSYLYIDRENAIQIDEQSYYYYDLAGCIVVNNEGSVIGKVSDIINAGTCDVYVVSGIGEEEDHRFIPAVKEVVKKIDIKKKEITIDVIDGLF | 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 ... |
A0A0L0DEN8 | MACIPATAAASWYSTTRPPASPQVVQRVDDLRKVVNELDRPLGFVPTMGALHDGHLSLVTAAGEACNSVVVSIFVNPTQFSETEDFSAYPRTLDGDLEALERNGVPVDVVWAPTVDDMYPHLGSVQESGRLPSLATRGGTLVRTEGVSDGLEAASRPHFFDGVCTVVTKLINAVSPDAMFLGQKDAQQCAVLRKMSRDLLLPLEVVVVPTVREPSGLALSSRNAYLTDDERASAAAIYQALEHTRAAHAAAPDKLTPSAIREDVAARITAAGGELDYVAASDPETLQDLDCNTPVERALVSVAVYWGESRTRLIDNMHFS... | Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1.
EC: 6.3.2.1
Catalytic Activity: (R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+)
Sequence Length: 326
Sequence Mass (Da): 34870
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A0A212RQY2 | MASRSPQDTAKHAVAEKAAAMVEDKMVLGLGSGSTMRLTLLSIGRRIQAEGLSLKGVPTSEATAVLAREQGIELVELDARPELDLAFDGADEVVPGSFALTKGLGGALLREKLVAIAASWLVILVDDGKLVDQLGSRSPIPVEVVPFAHKTTARRLAKLGGEPVLRLASDGTPFRSDGGNLIYDLKMPPIGAPEGLAAAIKGITGVVEHGIFLGMAKDVIVGNADGTTRRLPAVLSRVDNGT | Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribose 5-phosphate from D-ribulose 5-phosphate (non-oxidative stage): step 1/1.
Function: Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate.
EC: 5.3.1.6
Catalytic Activity: aldehydo-D-ribose 5-phosphate = D-ribulose 5-phosph... |
L0K9I5 | MQLVVIGASHKTAPVEIREKFSLISSSQEEVITNIKGQVKIKEGVILSTCNRTEIYLVVSDNTIIDKIALKVFKSITDLNVDKLQEYTYVYQGVNVGKHLYKVISSLDSLVVGEDQILGQVKEAFQQANKNNLIGSYLHNLFTNAFRVGKRVRAETNIGAGATSVSYAAVELAKEIFGTLSGETVLILGAGETSELTLKSLVDHGVKGVMVSNRTYTRGQKLAAKFSGEVVKWDMLEKWIQDVDIIISSTAAPHYVLHYDQVKKAMEHRRGPLFLIDIAVPRDIEAEISGIPGVHLYDIDDLEEVIEKNISHRKDAIEDV... | 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... |
A0A6N2T4P0 | MDTKLFVVQDIEKDAPLLQEAADILKRGGLVAIPTETVYGLAADALNPEAVKKIFAAKGRPADNPLIVHIAEFEEIYGLASQVPESAKILAERFWPGPLTMIVPKGESIPDITSAGLPTVAIRMPSHPIAREIIRRSCPLAAPSANLSGSPSTTTAQHCIHDLGGRVDAIVDGGECRFGVESTVITLAGKKPRLLRPGAITLEELRDALGEVEMDKAVLSQIDPGERVSSPGMKYKHYAPKAKVVIVDGDSESFLRFLNEQTGEGIFGLVFSGEEERANKPCVVYGENDEDVTQAHRLFAALRELDERGAKLVYARCPHK... | Function: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine.
Catalytic Activity: ATP + hydrogencarbonate + L-threonine = diphosphate + H2O + L-threonylcarbamoyladenylate
EC: 2.7.7.87
Subcellular Location: Cytoplasm
Sequence Len... |
H0QH83 | MSHESAAAPETGAPAPLVGLVMGSDSDWPVMEAAADALAEFGIPFEADVVSAHRMPTEMIRYGQTAHERGLRVIIAGAGGAAHLPGMLASVTPLPVIGVPVPLKTLDGMDSLLSIVQMPAGVPWPRSPSRGPGTQACSPSACWRRAPMNSPPASARSSWISPRNSMTWRAGRAPTCARK | Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5-amino-1-(5-phospho-D-ribosyl)imidazole (N5-CAIR route): step 2/2.
Function: Catalyzes the conversion of N5-carboxyaminoimidazole ribonucleotide (N5-CAIR) to 4-carboxy-5-aminoimidazole ribonucl... |
A0A8S2AQX9 | MKVGRVMTQVFVLISLLQGVRSTTSRNNLNVTNPGQKHPSPPVTLRKVGHNQVVVDNGIIQVSFSSPAGLITGIKYNGFNNVLNDQIENRGYIIRSGVSGVYMYAVLERLKGWPDVNMDQTRIVFKLNTTKFDFMAISDGRQKIMPSEADRDIKTRRASPLAYKEAVHLINPQNHILKGQVDDKYMYSMENKDNKVHGWISSDQRVGFWMITPSDEFRSCGPIKQDLTSHVGPTILSMFTSVHYAGVDINTIYKSKEPWRKMFGPVFVYLNSASSRNLLWTDAKRQMVSEVQSWPYDFVKSVDYPLHHQRGIVKGRIFVM... | Catalytic Activity: Endotype eliminative cleavage of L-alpha-rhamnopyranosyl-(1->4)-alpha-D-galactopyranosyluronic acid bonds of rhamnogalacturonan I domains in ramified hairy regions of pectin leaving L-rhamnopyranose at the reducing end and 4-deoxy-4,5-unsaturated D-galactopyranosyluronic acid at the non-reducing end... |
A0A1G0YB18 | MSKIIPKDVIETIRMQNDIVDVLGSYLQLKRAGGTYKALCPFHKEKTPSFNVNPQRQIYHCFGCGAGGDVFKFIMEHERVDFGTAARMLAERVGIALQYTAEDRKEINKDLLYKIHEDVALFYHRCLEQTPEAEKARDYLASRELDAETVKDYTIGYAPTGNPLLKLAKKKGYAYEQLEACGLVMKSDRPEDEGRFFDRFRHRLMFPIRDELGRVIGFSGRILEKNDKLAKYVNSPETILFRKSRILFSLDKARKTIIDTHTAIICEGQIDCIRCQRAGFTNVVASQGTAITEDHAQLLKRYADSLILVLDADAAGQKAA... | 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: 603
Domain: Contains an N-termi... |
A0A3N5CJ96 | MHRFEHKKILILGLGVSGYETAKVLKKYNNDVVLNEQQDLTNHPYKKELINLGVQVIDQHHPLELLEGIDYLVKNPGIPYSHEMIVEANKRQIPVITEVEIAYEIAPCKIIGITGTNGKTTITQWITNMINHDGTYKAIACGNIGHVATKAAYEASENSILVMELSSFQLQGTIHFKPDIAIISNLYEAHIDYHGSIKDYHLAKLNLIRRMDGQGVMICSDQVANTMDKLKDELQINKNLNINVIPNESILKDDSSIKIDGHEIAKIEQMVIKGSHNYENALCVCAVSEQLKLNRQSLSQSIVKFSGVEHRLEVVNTKSI... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).
Catalytic Activity: ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-... |
A0A2M7H2Q4 | MQKIGAHVSAAGGAQNAPLNAKLEKCETFQFFVSSPRTFQFKQPTTEQIAEFKANCEAGGFTDTYVHASYLINLASTNNKTRHGSISLLRKGLDACALLGVTGMMFHTGSAKDYENKADGIKQAAASINKVLDGYKGKTKLLIENAAGAGSTIGMNFTEVGELMKLVDKKYTKHLGVCLDTQHSFASGYDWRTKAGTDAAVKEFDKKIGLDNLVVIQYNDSKTECGSNKDRHEHIADGNMGLQAAKNILGHPKLKNYSFCLETEPEGRAKDIKTLKTIRQK | Cofactor: Binds 3 Zn(2+) ions.
Function: Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate.
EC: 3.1.21.2
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphooligonucleotide end-produc... |
A0A0F6PBV6 | PTETKASVGFKAGVKDYRLTYYTPDYETLATDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYHIEPVAGEENQYIAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPPAYSKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYE | Cofactor: Binds 1 Mg(2+) ion per subunit.
Catalytic Activity: 2 (2R)-3-phosphoglycerate + 2 H(+) = CO2 + D-ribulose 1,5-bisphosphate + H2O
EC: 4.1.1.39
Subcellular Location: Plastid
Sequence Length: 188
Sequence Mass (Da): 20723
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A0A1V5UDF1 | MEGKKNNEKKNGDKLITNSSTAYEHYTHIAMDYISKSRNNLAKFEKRCIFQVHEIARAAADCLKSSNKILICGNGGSASDSLHIAAELVGRFKMERRALPCISLSENISTITAIGNDYGYDEVFSRQVEAFALPGDLFIGISTSGNSKNVINALRKAREMNIKTVGFCGLSGGTMKDENLCDLLLAVPSGETSRIQEMHILAGHIICKLIEEMMFSGGNK | 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... |
A0A0G1GVX1 | MIRLLDQSSKLRVHSEWYRKYLSGLADLWFLSDLNNGTDVTTKIVKGKKDAKANIIVKSNAVLAGVPEIEWLFKNHPRFKGCKIKFHISDGNKVKRGKIIAEVSGKYAVLMRVERIVLNILQRMSGIATETKRLSDKVREYGVKLACTRKTYFGPLDKKACSVGGGLTHRLGLWDAVMIKDNHFDMGFDLSHAKGVRFVEIEVENLRQLDRAILELKVLRPAMRDCALIVMLDNFDIKKIPEAINRLHAEEIAVEISGGINKSNLVKYAKLRPDVISMGCLTQGAKASDIGMEL | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-ribonucleotide from quinolinate: step 1/1.
Function: Involved in the catabolism of quinolinic acid (QA).
EC: 2.4.2.19
Sequence Length: 294
Sequence Mass (Da): 33048
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A0A1E8FCL1 | MEQQSPRYILFDLDGTLVDSVPDLAWCVDVAMQQVGLPARGEAAVRCWVGNGIEKLMKRAVANAMDDEPDEQLFAPAYQAFLQAYKENHAKRSQVYDGVIPALDWLKNHGYQLGCVTNKAEAFTLPLLQEKKLDQYFSVIVSGDTCEHKKPNPEPILFALEALGGKVEEALMIGDSKSDINAARAAGCAVFAVPYGYNHGEDIHAYQPDKVLNTLADLPSILAPHQ | Pathway: Organic acid metabolism; glycolate biosynthesis; glycolate from 2-phosphoglycolate: step 1/1.
Function: Specifically catalyzes the dephosphorylation of 2-phosphoglycolate. Is involved in the dissimilation of the intracellular 2-phosphoglycolate formed during the DNA repair of 3'-phosphoglycolate ends, a major ... |
A0A2R6AJG7 | MEKVIVCDLGYMEYAKAWEIQKALVAKKANDSGFPDYLLLVEHPHVITLGRKGNTENVLEWSLPVYHIERGGDVTYHGPGQLVAYPIIDLTKRTLTLKGYVRMLEELVIQALNQFDIQAQRIEGQTGVWVSGKKVASIGVAVDHWITFHGLALNVNTDLSYFYKIRPCGYSPSVMTSLEVLLGKKVDMERVKHALLQAFSKVFDAELSSIGLQELTELLQKGVTLKNE | 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... |
A0A0H1SC08 | MPLLITLEGIDGSGKTTLINNLKKSGELDLITHNWRDTEWGQKIWHLLNESRGAEKNGLPSDWSYIFLILVAFDELEKKVIQPNLREKKIVVIDRYIDSTLVYQGLAGGLEIGTIQEVAKKTIDLPWPDITFVLDIDPVKAQDRLKKRKLATGEYTNWDKLNLEFHHRIRNHYRELKKLFPERIHIINADRSETEILTEVQDIIKQTRVPKSEAHLPQSVRAIIQNEKGEFLLVKDKWGWNFPGGKIEPGETPEAAACREVFEETNLTIENCQKIAEENVFYANLPPGNQHWKVHFFRTQKYAGEIVIKETEKILGIRFV... | Function: Essential for recycling GMP and indirectly, cGMP.
Catalytic Activity: ATP + GMP = ADP + GDP
EC: 2.7.4.9
Subcellular Location: Cytoplasm
Sequence Length: 549
Sequence Mass (Da): 63218
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A0A0S7Z8L8 | MTLTPRPPWKGKRIVLGVTGGIAAYKSIQLARDLTRLGAEVDTVLTASARKFVAPLSFEGVTGRRALTDLFSAEGAALHVRLGRDADVVCVAPATADFIARAAQGRADDLLCTTLLATRAPVVVCPAMNDRMYAHVQVQENLAHLRDVLGYGIAGPAEGALAVGEGEGPGRMLEPWQIEEAVGRALATSPVLKGRHVLVTAGPTREPIDPVRYVGNRSSGRMGYAVAQAAWRRGAEVTLVSGPSALEPPFGVTVVPVGTAEEMYEAVRSRIDGADVSVFAAAVADFRPIDPRSRKVKRDETGGELSVSLEANPDVAFDTR... | Cofactor: Binds 1 FMN per subunit.
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 2/5.
Function: Catalyzes two sequential steps in the biosynthesis of coenzyme A. In the first step cysteine is conjugated to 4'-phosphopantothenate to form 4-phosphopantothenoylcysteine. In the se... |
A0A8S2ATJ1 | MARLTSFLLLLPLLCFVPLCLCDKSYGGKLFPGFYAHSCPQVNEIVRSVVANAVARETRMAASLLRLHFHDCFVQGCDGSLLLASSGRIVSEKNSNPNSRSARGFDVVDQIKAELEKQCPGTVSCADVLTLAARDSSVLTGGPSWVVPLGRRDSRSASLSGSNNNIPAPNNTFQTILSKFNRQGLDVTDLVALSGSHTIGFSRCTSFRQRLYNQSGNGRPDMTLEQSFAANLRQRCPRSGGDQILSVLDIISAAKFDNSYFKNLIENMGLLNSDQVLFSSNEKSRELVKKYAEDQGEFFEQFAESMIKMGNISPLTANNN... | Cofactor: Binds 2 calcium ions per subunit.
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/... |
A0A1K1X846 | MQINLAIDAMGGDSGPRTNVAGTLLALTQDPLLTVTLVGDKSLLQTLLSQHHLSSVFASRIALLGSDEVIGMDESPASALRNRKHSSMHRTVQLVADGQCQAGVSGGNTGALMLIGRHYLGMLPGIERPAICTAIPTRKGRSYLMDLGANVECNAEHLLQFALMGSEMIRVVEGQASPRVGLLNVGHEAIKGNTLVKLAAHLIDEHPAVNYAGYVEGDEIFAGDLDLVVCDGFVGNIALKTSEGLARFLSGQIQGLFEKSIYSRLVGLMARPVLKQLKQQMDPVRYNGGSFLGLRGCLVKSHGNADAAGFSFAIMRAATE... | Pathway: Lipid metabolism; phospholipid metabolism.
Function: Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
Catalytic Activity: a fatty acyl-[ACP] + phosphate = an acyl phosphate + holo-... |
A0A385XWZ1 | MSFESLGLSADILRAVEEQGYREPTPVQRQAIPVVLEGRDLMASAQTGTGKTAGFTLPLLQLLSQRPSQAKGRRPVRALILTPTRELAAQIGENVLAYSQYLRLRSLVVFGGVSINPQMMKLRSGVDILIATPGRLLDLEHQNAVDLSQVEILVLDEADRMLDMGFIHDIRRVLAKLPSKRQNLLFSATFSDEIKELAGKLLTNPASVEVVRRNTPSELVTQHVHYVDKKRKRELLSHLIGKHDWRQVLVFTRTKHGANHLAEQLNKDGITAAAIHGNKSQGARTRALANFKDGDIRVLVATDIAARGLDIDQLPHVVNY... | Function: DEAD-box RNA helicase involved in ribosome assembly. Has RNA-dependent ATPase activity and unwinds double-stranded RNA.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
EC: 3.6.4.13
Subcellular Location: Cytoplasm
Sequence Length: 452
Sequence Mass (Da): 49923
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A0A943UCQ4 | MIVSLLLLGVVLMQRPKQEGLGAAFGAAITDQAFGARTTDVLKKATVYFGSAFMILCLVLGMLINRQHVKSSESLLSPEMMKAAAKQEASVPAKTPEELQQEELRRRAAEAEAASSQAPAPAVPEAPAPVSPEAPAPAN | Function: Involved in protein export. Participates in an early event of protein translocation.
Subcellular Location: Cell membrane
Sequence Length: 139
Sequence Mass (Da): 14595
Location Topology: Multi-pass membrane protein
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A0A4R2R5I4 | MTVGIVLVSHSAALAEGLAELAGQMAPDVRIVPAGGLVDEQGAGLGTDYDAVCAAVARADSGEGVLLLYDLGSARMTAELAVESLAGAQRAFVADAPFVEGAVAAAVAAQSGAELARVATAAAAANAGEESAAGEEPAEREPGAERASGAVRRAEFVLTNEVGLHARPAALFARTVAGLAAEVEVVCGDQRAAGDSVLALMALGAVKGSRIEVSASGADAAEALRRIGDLVDRDFAE | Function: Component of the dihydroxyacetone kinase complex, which is responsible for the phosphoenolpyruvate (PEP)-dependent phosphorylation of dihydroxyacetone. DhaM serves as the phosphoryl donor. Is phosphorylated by phosphoenolpyruvate in an EI- and HPr-dependent reaction, and a phosphorelay system on histidine res... |
A0A1G0YFA2 | MKNPLHTVGVLGQGIWLDYIRRKMLTDGELAQLIEADGLRGVTSNPAIFEAAMSGGDDYDDAIEILAHAGHTAEEIYWELAIDDIRHTADALRPVFDRLDGLDGFVSLEVSPHFARETTDTVRQARELWARVDRPNVLIKVPGVREGLPAIQQLLTEGINVNITLLFGLPDYRQVAEAYVAALEARLARGLDLKSVASVASFFLSRIDVLVDPMLERIMQEPDGKRKKLAASLLGQVAVANAKLAYQIFRNVFHSERFDRLAAKGARPQRVLWASTGTKNPNYSDTKYVEPLIGPGSVNTMPMETLKAYRDHGHPQNRIE... | Pathway: Carbohydrate degradation; pentose phosphate pathway; D-glyceraldehyde 3-phosphate and beta-D-fructose 6-phosphate from D-ribose 5-phosphate and D-xylulose 5-phosphate (non-oxidative stage): step 2/3.
Function: Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.
Catalytic... |
A0A1I2KNA0 | MDWKLWDRIAETHPLIHQLTNVVTVNDCANITLACGASPVMADAPEEAAEMAAASDAVVINIGTLRQDQLDAMARAGESANKHGVPVVLDPVGAGATRLRLEAVDRLLKRVKFSVIRGNSSEIGTLCGRRSGRGVDANLDDLDSLLPSIRNLAKELQTVIAVSGPVDYVTDGKQEAYVENGTPLLTRVTGTGCMLTAVVGCCLGAGIDPFRSAILSLAAVGIAGEKAKASLSEGEGIGTFRIRFFDEMSRMNGETLEQAGKVKLLEKSV | Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; 4-methyl-5-(2-phosphoethyl)-thiazole from 5-(2-hydroxyethyl)-4-methylthiazole: step 1/1.
Function: Catalyzes the phosphorylation of the hydroxyl group of 4-methyl-5-beta-hydroxyethylthiazole (THZ).
EC: 2.7.1.50
Catalytic Activity: 5-(2-hydroxyethyl)-4-m... |
A0A2U1LJ91 | MEKYKVMSFTNNKGSEDRLEKKRKGGFWLRKWDSVDVTYVFLFMGMHILAICAPFMFSWGAIWVALVMEVITALERTNILGERTQVSSHAGESRSGEYSNVPELKAQWFYRFLHSTYIWHKVSLAILLYILGGFPYLAWVMGMREVAIHHFTYFVNSVCHTWGERPWNTSDTSTNNWWVAICTYGEGWHNNHHAFPKSARHGMEWWQFDLTWEIIKFLGTIGLATDIKLPTEADKEKLKVRQHQTNKA | Pathway: Lipid metabolism.
Subcellular Location: Membrane
Sequence Length: 248
Sequence Mass (Da): 29047
Location Topology: Multi-pass membrane protein
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A0A2M7H396 | MHIYSVSEFRDEINELLGQVTVAVQGEISDFRVSQNRFVWFTLVDEDTSVQCFMMAFQLKVSLKDGMEVRLVGSPTTFKKGQYVFRPRQVELVGEGGLKQAYEFLKSKLEQEGLFDESRKRQLPRFPRKIGLITSSDAAAYTDVLRVLKNRWAGLEVLHANVSVQGARAVPSIVKALQQMSEEQKDLNCILLTRGGGSLEDLQAFNSEEIVRAIFACNIPVVSGVGHERDVTLADLVADVRASTPSNAAEIMVPDKRDVTLELAQITDRLERQLREILRRRQDSVASAVDKLDQQTRLQLTQTADLDRRLRIGFERFINS... | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
EC: 3.1.11.6
Subcellular... |
F4GKT4 | MAKISESVIEQIKSRLTISEVVSAYVNLTYRGGRHWGLCPFHHEKTASFSVLNEKGLFHCFGCGKSGSMFDFVMEMDHLTFGESVSVLARKAGVELREETPEDKRKRTESEALQELYDRLTNSFRYILQNSDRAAHARRYLENRGISLEIQEKFGLGYAPAPSQWLYDFLTDKHYSASLLEASGLFSKRNERVSIFRDRLMFPIRTWQGKTVGFGGRDLTGESTAKYINTPETAIYSKRSVVYGLYEALSELKSRKHAILCEGYFDVMAMHQSGFTTAVAPLGTAFTTEQCKQLHRYCDSISTLFDSDAAGQNATGKALV... | 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: 602
Domain: Contains an N-termi... |
A0A917CFZ7 | MHSPSKLLTTLALAAALSACGGKNDGRSVSEVAIDPDAERTAHETALAEYPKARLHTDAGDIVIALHADKAPETVRNFRAYAETGHYDGTVFHRVAGDLLIQGGAYTADYRIKPERGFIRSESDNGLRNLRGTVAAARRANDADSAGAQFFINVVDNPQFDFVSAADAASRGYAVFGEVVEGMAVVDALRKTPVESRPGIGAQVPKAPIVIRRVTVED | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
EC: 5.2.1.8
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Length: 218
Sequence Mass (Da): 23202
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A0A0H1SCB2 | MNNDFLWKEFYLDKSDPSWVPFFQQEAQKDYFFPLLEKLSQEYQNYKCWPRKENIFRLFREIAVHQIKVIILGQDPYHLPEVADGLAFSTQKPNYIPASLKNIFLEFSRDLNCVSPTKGDLLPWVKEGVFLLNTALTVRNGQALSHMSWWKEFIYSLLIYLKNHDQRLIWIFWGQKAKKIGEECQIDSEYSLASAHPSPYSAEHGFFGSCPFSQVNKLLSELGKSPIDWLSILLPKLKKC | 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.
Catalytic Activity: Hydrolyzes single-stranded DNA or mismatched double-stranded DNA and polynucleotides, releasing free uracil.
EC: 3.2.2.27
Subcellular L... |
R6Z097 | MSVEIERVLFLIASFLASLCLSLFFCWGLIQLQKRKKIEQPIHKLGVKSHFLKTGTPTMGGIGIIFSIFLIYILLDWKSLKNYRLLAMVIGILSFSIIGIIDDLLKVIKKNEKGLSAWLRIFLEIEVIIITFIIAGYDDSSTWYLNLYPFNNNLGNNIFFLLIAMFGVIASANSSNLLDGLDGLDGGVFILALLPVLVLAFQQGESDLGLLLLLIIGAVIGFLLLNSCPSKIFMGDSGSLFLGAVLAYSLIYLDKLILLPFIALIYIFETLSVIIQVFYYKRTRKRIFLMAPLHHHFELKGIPEYKIVFSYYFIQSVISL... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yield... |
A0A1V5UFE6 | MSEIRVRFAPSPTGYLHVGGARTALFNYLYAKNTGGKFILRIEDTDLARSTDESINAILRSMKWLGLDWDEGPEKGGEFGPYFQTQRLDTYNKYAAQLLESGHAYYCFCSQQEKKDEPEAQGSKYPGTCRAVSLADAKKRIAAGEKAAIRFKMPAKEIKFKDIVRGDVSFDGSLFGDMVIIRQDGVPTYNYAVVIDDALMNITHVLRGDDHISNTPKQIAIYEAIGFKMPEFGHISMILGPDGSRLSKRHGATSVEEYNKNGILPEAFVNYLALLGWSPEGDREIFPLGEMIKEFSLSRVSKSAAIFDSTKLKWMNGMYI... | Function: Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).
Catalytic Activity: ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu)
EC: 6.1.1.17
Subcellular Location: ... |
A0A1V5UCU8 | MPGVISVDIAPPVLFVYLICYRWIMVEDKIFQQFVVNVKNNNDIVSTISNYVPVKKSGKNFLTNCPFHLEKTPSFNINPEKQFFYCFGCQAGGDVIKFVSMMENISYKEALIKLAGVQGIELPTGLAGSLAPAETDKFKIIYNLLGEASLYFFKVLASASKEAETARNYLYMRGVKNEDIEQYMLGYSFASPAKFHEAVLKSKKYTASDLEQAGLIVKTADGRYFDRFFGRIVFPIFDRSSRTIGFGGRTTQLEGSPKYLNSPETAVYKKNSAFYGINFAHDAIIKTKEVILVEGYFDFISLHRNGIHNVLATCGTALSP... | 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: 619
Domain: Contains an N-termi... |
A0A4U9HK65 | MLRALKLGADQVLQLTPDRVAMLPPDGRCNSWQLGVMEEIALGGRQTWPPRHWTNLTRTRRHVARCGNKSANMNTISSLTTTDLAQAFEIEKRAHAFPWSEKTFASNQGERYLNYRLDVDNTLAAFAITQVVLDEATLFNIAVDPAFQRRGLGRELLEHLIRELEARDVFTLWLEVRASNAAAIALYESLGFNEATIRRNYYPTAEGREDAIIMALPLG | Function: Acetylates the N-terminal alanine of ribosomal protein bS18.
Catalytic Activity: acetyl-CoA + N-terminal L-alanyl-[ribosomal protein bS18] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-alanyl-[ribosomal protein bS18]
EC: 2.3.1.266
Subcellular Location: Cytoplasm
Sequence Length: 219
Sequence Mass (Da): 24727
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A0A1Q1G2B4 | MLIGLTGGIATGKSTAAKLFEQHGIPVVDADVVSRQMVEKGSEGLRKIVNHFGKTILNEDGTLNRKKLGELIFNDSSLRQQLNHILHPLIREEMNRQTTHLLKTNQHVIQDIPLLFENKLEQHFDLVIVVYIDQQEQIKRLQQRDDISYEAALSKVKSQAPIEDKKALAGIVLKNHGTIDALEEQVKETIQNHF | 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... |
A0A328RYF1 | MISLAQTGNVLYTYVFAMVKTSKIKGNIVILSGPSGVGKGTIINGVLKKIASMRVAISATTRQPRREEANRKNYYFMSDYEFDEKIESDSFVEWCNVLNKRYGTLKSEIEDTINEGKDIILEIDTQGAQKIKAKMPDSILVFIAPPTMKDLEARLINRQTEQEIDIKNRLDKAKLEISEIDKYDFVVVNKEINKAIDSIVKILTKSCKEH | Function: Essential for recycling GMP and indirectly, cGMP.
Catalytic Activity: ATP + GMP = ADP + GDP
EC: 2.7.4.8
Subcellular Location: Cytoplasm
Sequence Length: 210
Sequence Mass (Da): 23814
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A0A0L0DK03 | MDSLAHRPPHIPAQLGLLPRLGLGPRRLCPVLRPPPQRQRLGHLPRLHALFVSPRLYGGCATGASVLVPDTASGLRTPPSAGAGGAVNGALAETVRAAPDAVHAGAGVADNEDAARPVVRRASAPPEEAPSGYGSHVVIISVLYGLALNAYVRAATLPPGPVPPALAVAAEKSRGSLRHDKPVAGTAAAEEAIEYFHDWDGSYDEVGPDTEFCGPCGKYKPPRAHHCKRCRACVLRMDHHCPWLGTCVGHGNYKAFLLTCLYFFITSAYNCISLWTFLGSCIGSLGAYNEAYPLEMAAVMGHTALSIFTVCFAALLTGSH... | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 417
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 45012
Location Topology: Multi-pass membrane protein
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A0A1J5HRD9 | MKYGKVAIVGRPNTGKSTLINAIMNQKVSITSPLPQTTRRAQTVLFSDDRGKILFTDTPGLIGKVVDLMSKRVNEEIPRELAKTDLVVAVVDISRPKNEEENKVLGLLRKINTKKILVYNKIDQAVGPANHFPDYNYLEDEFDKTVMVSGLKSKNVKTLVNLIFELLPQKENRGVMKEIEAMSSEVRPLTAMGAREYISEIIREKAYLFLREEIPYTINVKVKEVVDKKKLIYIKAEIITSADRYKKMIIGTGGKKIREIGYNARKELELMSARKVFLDLTVVVDTHWMEGE | 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: 292
Sequence Mass (Da): 33188
Location To... |
Q8NKC5 | MGSLTSPTMRTTRSSSGKSSSMKTSLSAISSSSSSNSDCSDSEAVERLSISSAASVTSLEDSSSPVIAKHIKAIPKITTKNDFSVLYEPWTIGNFYKKLDWVHMLGLVFMPIYGFYMAFTSVPLQQKTAIFAVAYYFFTGLGITAGYHRLWSHRAYAAGPALQFILMIASTGAMQGSIRWWCRNHRAHHRYTDTEKDPYGAQKGLIWSHILWMLVRQDPTTVGWADVADLKANKLVRFQHDHFLWLAPLISLGLPTMVAGFGWGDYWGGFIYGGIIRQVVVHHATFCVNSLAHWLGDMPFDDRHTPRDHILTALVTLGEG... | Cofactor: Expected to bind 2 Fe(2+) ions per subunit.
Function: Stearoyl-CoA desaturase that utilizes O(2) and electrons from reduced cytochrome b5 to introduce the first double bond into saturated fatty acyl-CoA substrates.
EC: 1.14.19.1
Catalytic Activity: 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 + octadecanoyl-CoA = (... |
A0A212R3B0 | MLISGRARLAGVMGWPIAHSLSPLLHGHWFERHAIDGSYIPLPVVPADLDLLFQALPKAGFRGWNVTLPHKERAFALVDRLTPTAERIGAVNTVLVDTDGTLIGDNTDGHGFTANLDDQAPGWQERTQNVILLGTGGAARGVAAALYDRGLRNFRLINRTLERARLLESELRRLGTLNLEIAPWKTRDEALADGDLLVQCTSLGMEGHEPLALDVAALPPHAVVADLVYRPLETDLLARARARNLRTVDGLGMLIHQAVPGFVHWGGQKPLIDATTRLLMRNALGV | 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... |
A0A424R7W5 | MRRIEEAMSRFEAISIAFHKANFETREKFSLSEPXQSSIISXLTKAGARDVMILATCNRVECYWTYLAKKEVESILREFIDVKQNVWKSSCRHMSGPAAXKHLFRVACALESQIVGXTEITGQLKVAFRRTQQLGTPIPFLDRVVSSALKXGKRVKAETGISSGATSVAFSAIHYLRSELSNLEAVNVVLFGLGKLGRNTCKNLAKHARXASITVINRDESKSDSAAAEHGFRSRSIDSLEAXVRGARVLIVATGAQGYTVPREMVGEQQELLILDMSMPRNVDPEVGHLPGVTLLNVDEIXAYAKQQLXARRDHIPQAN... | 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... |
A0A1E8FH91 | MTNSPWLSLSDAITAMLSQARPVSATEQIDVTQAKGRVLATAVTASINVPPSDNSAMDGYALKSMNGNSGQSLIVVGSVFAGASTLPTVKPGQCVRIMTGASIPPDCDTVVIQENVTRQGDTITLHADSPPLANIRQTGSDIAQGDILFNAGHRLTATDNMLLSSIGLAKVTVYKAVTIGLLATGDELIEAGHPLAAGQIYESNRTGVAALLNDWQVNLINFGIVVDQPEVLKTTLAQAQELCDLVISSGGVSVGDADFVKDILDELGEVGFWKVAIKPGKPFAFGQLGKAIFCGLPGNPVSACVTTEQLVVPLLRHLQG... | 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: 413
Sequence Mass (Da):... |
A0A4R2R2T6 | MIGGGAIGGYTAALLAEAGRAVTLCVRSPVERLRLRTPDGSISPELAISSEPAAQRPVPWLLVTTKAQDTPGVAEWLRHLVGPETVVALLQNGVDHAERLDGLVEPAAILPTVVYAPVERVAPGEVVSHADGQLVIPEGVHAARFRELFDGTGLAVQAVPDFRAAAWRKLLSNVAANPLTALTMRRMEVITEPEVGAMATELMREALRVARADGAELTERELDRIRRMWGRMDPAGGSSMLYDRLAGRPLEHEFILGPIVRYAERYGIEVPLARTMLTLLRALDVAPAPQDS | Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 2/2.
Function: Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid.
EC: 1.1.1.169
Catalytic Activity: (R)-pantoate + NADP(+) = 2-dehydropantoate + H(+) + NADPH
Sequence Length: 292
Sequen... |
A0A2M7H4R3 | MAMSSPLKVIFFGTPELAVPCLEVLADPKQTPEISVVAVVTQPDKIGNRGRQAPPPVKLAAQRLGLPVLQPHRIKANNPEGSTFIDEVRSLRPDIAIVIAYGKIVPLELLNIPQLGFLNVHVSLLPRWRGASPIQAALLAGDSETGVTIMKMDEGMDTGPILLQRAINIDQADTAASIHDRLSSLGAAVMIEALTGYVSGALLPVTQPANGITSCGLIKKTNGLIDWSSDPAYIERQIRAMHPWPGAFTDIYGEPIKITEAHLESGRLVIDKVKPAGKGEMEYRAYSNGNRDRPLPPNKA | 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... |
A0A317FIC6 | MGHRRRRGRAARRGRRGGGVGRHADALRQARLAKPALPGAGRRVTRVITDVAEAAALLRAGELVAFPTETVYGLGADALDGRAVAAIFEAKGRPHFNPLICHFWTAEAAFDTEVVADERARELARLFWPGPLTLVLPRRETCRVDLLAGAGLDTLAVRVPDHPLALELLRQVGRPVAAPSANRSGGVSPTTAAHVLESLGGRIAAVLDGGPCAVGVESSVLDLSGGGAVLLRPGGVPVEAIEAAIGRVGRPLPPEAAAATRSLRSPGMLLSHYAPSLPVRLDATEVGPEEALLAFGPAPLPGAGAVWNLSPGGDLREAAA... | Function: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine.
Catalytic Activity: ATP + hydrogencarbonate + L-threonine = diphosphate + H2O + L-threonylcarbamoyladenylate
EC: 2.7.7.87
Subcellular Location: Cytoplasm
Sequence Len... |
L0KB72 | MQQNHGGNIRAAAKEYNLDPAEIIDFSANINFLGPPESVTKALKNNLKGIKDYPDPECNQLKTIIAKQENLEEDNLVIGNGAVELIYLLATVLSPREALVLAPTFSEYRLAIESVGGSIEEFQLQKEEGFRFNLDDLLPRLDNIDIFFLCNPNNPTGKFITREDIIEIINYAASQDTFLVVDEAFVDFLEEDITVIDLVKQYDNLFVLRSLTKFFAIPGLRLGYGATNKELIKKLNASKDPWNVNCLAQLAGEKALNDKEYIKQTEEAILREKEFLYQKLNQFSKFKVYYPHANYILVDLENSNLTSTRLEEKLAQQGIL... | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
Function: Decarboxylates L-threonine-O-3-phosphate to yield (R)-1-amino-2-propanol O-2-phosphate, the precursor for the linkage between the nucleotide loop and the corrin ring in cobalamin.
EC: 4.1.1.81
Catalytic Activity: H(+) + O-phospho-L-threonine = (R... |
A0A1V5UMH4 | MFDYDSPVAFSRLIAEYKLKFIHLSRAELESCVSFGPAPCEAALGGSVYNYAANALRLEKNEKILLIDGSNSKYYLLAINRIEKKRVTADCRAVEIYDDIIKKEYNCFVGVLKGHANEEIVERLTELGADSIFFFRSRYSQCDIGPEKLERLYKIALSASSQSRRLKAPLIQRLSFEEAVRRLAAPGARSFLMAEPSLCGGLDFAGAPAEAAFEALRKESAGSVNIVSGPEGGFERDEASGILGTAAAIPVTLKNVVLRACFAPQAALAIIKYRCGDL | Function: Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit.
Catalytic Activity: S-adenosyl-L-methionine + uridine(1498) in 16S rRNA = H(+) + N(3)-methyluridine(1498) in 16S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.193
S... |
A0A0S7XZC3 | MFKLYLIVDQLNCHQCDIETVVTEAIKGGVDAVQLREKNASTQEIIELGKKLQVLLYKHNVPLIINDRVDIAMALNANGVHLGQKDMPYHSARKLLGNKKIIGISVSNSEQAHKAQQWDVNYLGIGPVFETSTKLDTSPVIGIEGLRRICSISKHPIIAIGGINVTNAHSVLSAGATGIATVSAICGANNPMLVSKQLFEIVSSYHAQ | 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-met... |
A0A0S7XY18 | MNAVTRVVAQGPLVGSRITLIPFPLPRFKVLILIVMLLISAFVIVYVKDVNRRLFIDYQSLQQRNDSLKTNNEKLLLEKSAWSRQARIQVVAEQNFNMKVPSASNVIVVKL | Function: Essential cell division protein. May link together the upstream cell division proteins, which are predominantly cytoplasmic, with the downstream cell division proteins, which are predominantly periplasmic.
Subcellular Location: Cell inner membrane
Sequence Length: 111
Sequence Mass (Da): 12635
Location Topolo... |
A0A0S7Z8J9 | MGDEDRIRIIPLGGLGEVGKNMMVFECGGDSIIIDAGLMFLEDQKHGIDLAIPDFSYVLERKERVRAIILTHGHEDHIGALPYLLREISAPIYGTKLTLGFAKNRLEEHSLVNLPRFIEVTPRQTVSFGSFAVEFFRVRHSIPDGVGLALHTPHGIIIHSGDFKLDFTPMQAEHFDINKLAELGEKGVLLLMSDSTNAEKEGYTPSEHRLNSALSETITQASGRVIISTFVSNVHRIQQIFDICERDGRKVALFGMSMERQIAMARRLGYLHFEDKNVISSDRVKSYPRERVCILTTGSQGEPMSALARFVNNNYKAIEI... | Function: An RNase that has 5'-3' exonuclease and possibly endonuclease activity. Involved in maturation of rRNA and in some organisms also mRNA maturation and/or decay.
EC: 3.1.-.-
Subcellular Location: Cytoplasm
Sequence Length: 551
Sequence Mass (Da): 61571
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A0A7W7Y345 | MRTGKEFQEVYRHGKVFRNRHFVLVWHEGKPMKVGVVASKKVGNAVVRNRLKRCMREAFRLHRSHLTREGAMVLAARPSARDLKGRQVVESIVGLLRQARLL | 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... |
A0A7S4N112 | MSTLNAYFGTPSAQKQFREWYPTGTEAVEGKAKAGIQEEKSNQNEHSKHSPKSLIIAGPSGVGKGTLIEKLKSEFANVFGFSVSHTTRGMRPGEENGVHYHFSERQAMEEEIEKGNFIEHAEVHGNLYGTSKASVIDVTKQGKICILDIDVQGCRLVRRAKLDGVFVFIAPPSMEDLESRLRGRGTETEEKILKRLEGAKAEMEAKDEPGLFDHQVVNDNLDNAYQKLKEIIQEELAAVLALQEGPSARRRAAVPHKPTVVFVLGGPGAGKGTQCANIVKEFGWVHLSAGDLLREEQQTDSEHSTLIKEYIKEGKIVPVE... | Cofactor: Binds 1 Mg(2+) ion per monomer.
Function: Catalyzes the phosphorylation of pyrimidine nucleoside monophosphates at the expense of ATP. Plays an important role in de novo pyrimidine nucleotide biosynthesis. Has preference for UMP and CMP as phosphate acceptors.
EC: 2.7.4.14
Catalytic Activity: ATP + CMP = ADP ... |
A0A2U1QGX6 | MLYKCIIVESVIYLLLCDMLSLSFISTFLFMTSALKGLYCSPFKDLIRKQSQHNGIPNRVIFSKRRYSCISQCFFNPQKRFISTCDPYKWPNQDKNRSVVVRSEIAGTGSHGASYQLSGFQFGSKIRGICFYTVTSFTAIFLFLFMLVGHPFVLLRDRIQRNFHNLVAKIWASMTIALFYKLKIEGTENLPPKNSPAVYVSNHQSFLDIYTLLTLGRNFKFVSKTSIFLYPVIGWAMFLMGTIPLERMDRKSQLQTLKRCMELVKNGGSVFFFPEGTRSRDGRLGAFKKGAFSIAAKTGVPVVPITLVGTGKIMPTGMEG... | EC: 2.3.1.51
Catalytic Activity: a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphate + CoA
Sequence Length: 664
Domain: The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate.
Sequence Mass (Da):... |
H0QR37 | MTAAPEHRSDDPYSAVEATPARGATAAGGGTASVPDAVPSSDVEPSSDVEPGPDAVPASDAGPASDAGPAAAGQPDAPAKHLAHTWEEARQAAFDCAAPIPAAPVPLRDAVGRTLAVDITAHQDLPHYASSAMDGWAVNGTGPWILAEPGQRLAPHQASVIVTGGLIPPGAKAVLRTESGVISTDDEGLPVLTLGGTARPGEPRNGQHIRKAAEEATAGDVLVRAGVVLNPAHVALAALAGYDEVEVLGKPVVKLLLTGSEVVEQGVPQPGRVRDTFGPQLATVVEMLGGLCREQVRIGDGYAEWLEGLEDSGIAEAHNL... | 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: 519
Sequence Mass (Da):... |
A0A061LYN8 | MSERRSRPGTGEGSRIAATLPDLGVVAVGGAVGSLARHLLSIAIGSSGDFPLAIFVINVCGAFLLGLLVEVVAQAGGEGGRWRTTRLLLGTGALGGFTTYSLLAADLAELLLDGAFGVAALYAVLTLVLGGAASWCGVLAGRMIGPSSARGAER | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Subcellular Location: Cell membrane
Sequence Length: 154
Sequence Mass (Da): 15381
Location Topology: Multi-pass membrane protein
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A0A212LDA2 | MVKSEAEAGSSGNRESFVTAGGVEVARSARPDHYKTAISGYFDRLDTRRGAVLSSNYEFPGRYSRWDIAFVDPPVAITARGRRMTIEALNARGRILLPAFAAAVRGPDLVSLSVDDALISLEVAVPEGGFAEEDRSRQPSVFSVLRRIIAKFATPEDDKLGLWGAFGYDLAFQFDSVDFKLPRPDDQRDLVLYFPDEIVVVDHHRAAATVYSYDFVVEGRLTVGLPRDGAPQPFRESDRDPGRGDHRPGEYAASVEKAVEYFRRGDLFEVVPGQVFYEKPSSPPSAIARRLQQINPAPFGFMFNLGNSEYLIGASPEMFV... | Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 1/5.
EC: 4.1.3.27
Catalytic Activity: chorismate + L-glutamine = anthranilate + H(+) + L-glutamate + pyruvate
Sequence Length: 735
Sequence Mass (Da): 80027
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A0A212RTS3 | MHTERPASHHEGRRALGNPFTSCPAPVRSAKSSLALRVAARAAAPGKTGREPSHDRLGTGIARNERSPSPGSVSAIHVSRPGEGSSRTAADLTGQQPFGDVFASFFRNPSFQGTGGRREDGRTFCGSCLAGGFAIANATPVQPCPRSLMPSSELIVASHPLVQHKVSLLRRKETPTADFRRLVNEVALLLAYEITRDLPLEAVTIETPLTPMQTNMLAGKKVCLVSILRAGNGLLEGMLDLIPSARVGHIGLYRDPQTLRPVEYYYKVPSDIAERPVIVVDPMLATGNSTAAAVARLKEDGVRDIKFACLIAAPEGIKTL... | Cofactor: Binds 1 Mg(2+) ion per subunit. The magnesium is bound as Mg-PRPP.
Pathway: Pyrimidine metabolism; UMP biosynthesis via salvage pathway; UMP from uracil: step 1/1.
Function: Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate.
EC: 2.4.2.9
Catalytic Activ... |
F4GIZ1 | MKNIDAQTTVLYDTPLGVIAISERNGAICGLAFEKGRKADSLPERETPLLREAIRQVRQYLSGTLTIFDLPLEENGTLFQKKVWEALRTIPYGQTRSYKDIAIHVGSPLAFRAVGMANNRNPIAIITPCHRVIGAQGDMVGYGGGLDIKVWLLELEKKSVASH | Function: Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irrever... |
A0A2H0M531 | MKNKELFIFDLDDTLTESKVVIDDEMVDILAGLLSHKQVAIISGAWLPQLKLQVLEKLPQRLDDIRKSRLHIFPTSGAAFYRFENGDWCPVYELRFTDEEKSEIVEKFSDAISKSEIEMPGQIYGERLQDRDTQLTFSALGSEAPLELKKTWDPDRQKRTKVHSIVKELLPQFDIAIAGKTSIDVLRKGVDKAFGVEMMEKHIGILKSEMIFFGDALFETGNDFPVVKTGIECVEVKDHEHTKRILKDFLQNIDGDI | Pathway: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 2/2.
EC: 5.4.2.8
Subcellular Location: Cytoplasm
Sequence Length: 257
Sequence Mass (Da): 29387
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A0A8F6TV98 | MNPLAFIVSLPIRFYRLVISPMIATNCRFTPTCSTYAMEALRKHGAIKGTWLASRRILRCHPWGGSGIDNVPD | Function: Could be involved in insertion of integral membrane proteins into the membrane.
Subcellular Location: Cell membrane
Sequence Length: 73
Sequence Mass (Da): 8191
Location Topology: Peripheral membrane protein
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F9Y9E4 | MKRLKLDRGRAMRAVAWMALGALAGFGIAPFGLWPLTILALAIFFAKAGSGFRRFWLFGFGYFALTLWWIVEPFLVDIARHGALAPFGLFAMCGGMALFWGLGGWLMRRLHLSGPFAAAAVIALAELVRARIFTGFPWAMPGEIWIDTPIAQYGAWGGPLGLTFLTLGLAAALAWLGPRARTMAVPGGIAALWAASLALFPALPDPTGGPLVRMVQPNIAQADKWRPETVETLIPLMRDLSVGGATPDLVVWPESATPWLLEDARGLFEAIAEESGAPLMVGAVSLRGEEFFNSLALVEPDVPLQVYDKVHLVPFGEYIP... | 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... |
A0A1V8M7M1 | METSEITQKLLAAKNKKEKSFADLGKLINRDEVWVAALFYRQASASEEEASIISVALELEQDIFNKLTEYPVKGLGPLVPTDPLIYRFYEIMQIYGMPMKEVIQEKFGDGIMSAIDFTLDIDKVEDPKGDRVKVTMNGKFLPYKKW | Function: Catalyzes the reaction of cyanate with bicarbonate to produce ammonia and carbon dioxide.
EC: 4.2.1.104
Catalytic Activity: cyanate + 3 H(+) + hydrogencarbonate = 2 CO2 + NH4(+)
Sequence Length: 146
Sequence Mass (Da): 16702
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A0A1V0RE31 | MKQDCILVLDFGSQYTQLIARRLREFGIYAEIVPYFESLDSIKSKNPKGIILSGGPASVYEEGAYKPDDGVFSLGVPVLGICYGMQYIAHFFGGKVVRAQAQEFGKAVLELVESSLRADETSTTIQPSFDTSELKFVSFSEKELEDVQGALVDLWEDSVRASHHFLSEEDISEIRVEVEGAFYQVANLLVATYENDFVGFIGVQDDEIPMLFVSPKYFNFGIGKALMLEALERYLKGFDAIRLDCNEQNPNALIFYQKLGFSQVARSEKDSAGRDFPILHLSVRREILLQTLKNPSQKSVKFQASNKLFAGVKQDSIVWM... | 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
Catalytic Activity: ATP + H2O + L-glutamine + XMP = AMP + diphosphate + GMP + 2 H(+) + L-glutamate
Sequence Length: 903
Sequence Mass (Da): 101637
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A0A7K7U835 | HWQHIASLFPNDVDRLRRMSLIEEGGTKRINMAHLCIVGSHAVNGVAKIHSEIVKTQVFEDFAALEPEKFQNKTNGITPRRWLLLCNPGLAELIAEKIGEDYVRDLSQLTKLHEFVDDDLFIREVAKVKQENKVKFALYLEKEYKVKINPSSMFDVHVKRIHEYKRQLMNCLHIITMYNRIRRDPAKLFVPRTVIIGGKAAPGYHMAKMIIKLINAVAHVVNNDPVVGSKLKVIFLENYRVSLAEKVIPATDLSEQISTAGTEASGTGNMKFMLNGALTIGTMDGANVEMAEEAGEENLFIFGMRVEDVTELDKEGYNAQ... | Function: Allosteric enzyme that catalyzes the rate-limiting step in glycogen catabolism, the phosphorolytic cleavage of glycogen to produce glucose-1-phosphate, and plays a central role in maintaining cellular and organismal glucose homeostasis.
EC: 2.4.1.1
Catalytic Activity: [(1->4)-alpha-D-glucosyl](n) + phosphate ... |
A0A8F6U0B7 | MMVDLGQYTAVVLSAYAGTIVCLLALIFASVARSRRVARRLTEVEARRGKGAGKSPAEGSLT | Function: Required for the export of heme to the periplasm for the biogenesis of c-type cytochromes.
Subcellular Location: Cell inner membrane
Sequence Length: 62
Sequence Mass (Da): 6540
Location Topology: Single-pass membrane protein
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A0A0N0Z6X6 | MKKKVIYFLCTGNSCRSQMAEGWAKQLLGEEWEVYSAGIEAHGLNPNAVKVMKEVGIDISNQTSDVIDPDLLNRADLVVTLCGHAADHCPVTPPHVKRVHWGFDDPAKAEGTEEEKLAVFRRVRDEIGERICRFAETGE | Function: Catalyzes the reduction of arsenate [As(V)] to arsenite [As(III)].
Catalytic Activity: [thioredoxin]-dithiol + arsenate + H(+) = [thioredoxin]-disulfide + arsenite + H2O
EC: 1.20.4.4
Subcellular Location: Cytoplasm
Sequence Length: 139
Sequence Mass (Da): 15493
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A0A356VVL3 | MSNNAIPPNKKNTAEMSLVQHLLELRNLLTKAILAIIVLFIILFPFANELYIYISEPLSRFLPEGTSMIATGVASPFLTPFKLSFVLAVYLAMPFLLLQIWRFISPALYKHEKQLIGPIMFFSSFLFYAGGLFSFYVVFPLIFGFLSQSAPEGVTIATDIALYLDFVIKMFFAFGLAFQVPVVVVILILTGMSTPKKLYHARPYVVVGAFVIGMLLTPPDIISQTLLAIPMWILYEAGIIVGAFVKKCRKTPEQREEDADAEAKKTADDNFNERMNSLDDGDIDDDIDYNEQFDETIEYDNRYADQVNDDKDWDAEFDNI... | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. Together with TatB, TatC is part of a receptor directly interacting with Tat signal peptides.
Subcellular Location: Cell membrane... |
A0A7S4JNX0 | MTKGGEDIELQSHDEERERLLRQDALMHDMSDIMIDDVDDTEGLGIESLEYFRWSLGLWFLSVLLMVVTCGFILLLFRWMPILALKCRYRRVARSRATHVLVSCTDGTKTIVEIESRSAEGFEDQLPRMFVFRHFMYFETSNGFSPITYKSGQPFSALVKHSSVGLTGSEVAKRRALFGNNL | Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
EC: 7.2.2.-
Subcellular Location: Membrane
Sequence Length: 182
Sequence Mass (Da): 20881
Location Topology: Multi-pass membrane protein
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L0K9D0 | MEKLIKNIDYVIPLITLVLIMMGLVLIGSATHVNEGSFWNNIFLQKQLIATLVGSIAIGIILVFDYRILQDYVNVIYGGIVLVLVGILFVAQTIQGGQSWIRLGPFSFQPSEITKIAVIITLADVLTKRKRRIKYILGLIVPGIYIGVPFILILLQNDLGTSLVLLAIFIGMIYVAGANSKFLFGSIFGVIAVTASWVSAHLYLGVPIPLQRYQLNRFLVLVNPQFDPLGAGYNVIQSKVAIGSGGIFGKGLFAGTQNQLNFLPERHTDFIFSVLGEEFGLIGTMVVLVCYFILIWRGITVAKNAKDSFGRFLVIGVLCM... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Peptidoglycan polymerase that is essential for cell wall elongation.
Catalytic Activity: [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-... |
A0A0S7ZFB4 | MEVSRELIRNAERVVIKVGTKVLTENDNILSQSIIESLVRQVTEADERKRFIIVSSGAIALGLSRMGLTERPKEINLLQAAASLGQSRLMHAYEMEFKKSRYETAQILLTYEDIQNRQRYLNIRNTIFTLWSFRTVPVVNENDSVAYEEICFGDNDLLAAHLSVMIDADALIILTDTDGVYDRNPGHGDAKILREIPSITEEIKQGAQGKGSSFSSGGMESKLKAAEIATKGGVGVIITNGKRMQMKGLLDGKAIGTFCVPSSRRMRGKKKWIAFGSKVEGRIYIDRGGERAIVEKKKSLLPVGVVDVSGIFKVGGNVSI... | Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 1/2.
Function: Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate.
Catalytic Activity: ATP + L-glutamate = ADP + L-glutamyl 5-phosphate
EC: 2.7.2.11
Subcellular Location: Cyt... |
A0A0S7Z7X9 | MTSSPFASITGWGACMPPAVLSNDDLATFLDTSDEWITTRTGMKERRVSHVSATELATLAARRALACADLDPSELDLVIYGGVSNDELCPNSASGVQFNLGATHAAAIDLNTACTSFCYGLVAATAMIRTGVVRNAVVIGVELISRYMDWSSRNVAVLFGDGAAAVVLQASDEEVGLVGSVVGCDAEARQTLRVRGFGCGYAGLGITLGDTFWDFDGPQIFKRAVKAMAQASQEVLEQAGVHADDVGLVVPHQANLRIIESVAKYAGIPMDRVMLTVEKYGNMSAATVPVALVEALEEGRIRPSSYVLMPAFGGGLTYCS... | Pathway: Lipid metabolism; fatty acid biosynthesis.
Function: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the tot... |
A0A2U1KJD4 | MISLSLLGLIGVFGTAALVVGVFGTAALSKGLAGKTFCSVGVCTYPLSDAESRSHVKEERVGVLLLNLGGPDTLHDVRPFLYNLFADPDIIRLPRLFRFLQRPLAQLISVLRARKSKEAYASIGGGSPLRKITDEQADALKSELEAKKVSANVYVAMRYWHPFTEEAAHQIKKDRITRLVVLPLYPQFSISTTGSSIRALNDIFRKDNILSKLPVAIIKSWYRRDGYIKSMADLIEKEMQSFDTPQEVMIFFSAHGVPVTYVVNAGDPYKDQMEECIYMIMQELKARGIDNNHRLAYQSRVGPVQWLKPYTDEVLVELGQ... | Pathway: Porphyrin-containing compound metabolism; protoheme biosynthesis; protoheme from protoporphyrin-IX: step 1/1.
Function: Catalyzes the ferrous insertion into protoporphyrin IX.
Catalytic Activity: 2 H(+) + heme b = Fe(2+) + protoporphyrin IX
EC: 4.98.1.1
Subcellular Location: Plastid
Sequence Length: 438
Sequen... |
A0A2U1QD99 | MSRSYSNLFELASGDAPLPSSGFSRGAKKLSRVATVPGILSELDDEGFSSDAPSSVTQERMIIVGNQLPLRVNKRPDGSWVFSWDEDSLLLQLRDGLGEDVEIMYVGCLREDIDPKDQDDVAQHLLENFKCVPARYALGLSYQSKAEVIIGLVLWSLLLASNILPVGLHLATTTKNVVDDMDIFKGISLKLLAFGEFADSSIREKRVNVVLGSNANRSGSREGCSGGIAYYVNSGVVCDSCPGRENFDTYEYIICRQGNAKLDETLGLNPSFPKKEYVMVSNSWGAPLPDFYWKQIAEPVMKLYTETTDGSTIETKESGL... | Pathway: Glycan biosynthesis; trehalose biosynthesis.
Function: Removes the phosphate from trehalose 6-phosphate to produce free trehalose.
EC: 3.1.3.12
Catalytic Activity: alpha,alpha-trehalose 6-phosphate + H2O = alpha,alpha-trehalose + phosphate
Sequence Length: 473
Sequence Mass (Da): 51968
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A0A2U1Q140 | MNNLCLLVLISLLFIVPRSSCSSIINPSKVKQVSWKPRAFVYEGFLTEEECDHLVSLAKSELKRSAVADNVSGKSQLSEVRTSSGMFIHKNKDPIVAGIEEKIATWTFLPKENGEDIQVLKYESGQKYDPHFDYFSDPVNVARGGHRIATVLMYLSDVEKGGETVFPSAEENSRHKTPKPDDLSECAKKGIAVLISLLFIVPRSSCSSIINPSKVKQVSWKPRAFVYEGFLTEEECDHLVSLAKTELKRSAVADNVSGKSQLSEVRTSSGMFINKNKDPIVAGIEEKIATWTFLPKENGEDIQVLKYESGQKYDPHFDYF... | Catalytic Activity: 2-oxoglutarate + L-prolyl-[collagen] + O2 = CO2 + succinate + trans-4-hydroxy-L-prolyl-[collagen]
EC: 1.14.11.2
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 475
Sequence Mass (Da): 52766
Location Topology: Single-pass type II membrane protein
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A0A3P1XUQ1 | MGSASREALARTAKLLEGPIAANVGLQLLEVAQHASEQPQLAAALSDPAASESAKAALVAKAFGGITQGARTVLTEAAVNRWSSQQEFVSGIEELGIRATAATSVALDDELLQVAALVDSNHELELTLGSKLVNPAHKAEVLQKLLSGKVSDATAAVATHLVSYPRGRRFSTSLRDAARVAADQLGNTLAQVTTAAPLDGTRTERLRQALSKIAGRSVKITTSTDPSLVGGIRVQIADEVIDGSVRTRLEDLRLQLAG | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
A0A259LNF6 | MSDDPNRATPATSTATASQPASQSPADGLSQDELDALVAAADTGGRTPSGPVGLFIMLVALAWSLFQLWIASPLPFMVGFGVFNDTEARAFHLAFALFLAFAAYPAAKGATQTGLAIGVPVALSALFIYGSREGDPIWWIPLVGAAMVVAVLLGSPRNRVPVWEWALAIIGAAAALYVYAFYDEIGRRVGAPITQDFVVSVIGILILLEATRRALGPALMIVASVFLIYTFLGPMMPQIIAHKGNSLAEVVNHQWITTQGVFGIALGVSTSFVFLFVLFGSLLDKAGAGNYFIQVAFSLMGHMRGGPAKAAVVSSAMTGL... | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 477
Sequence Mass (Da): 50191
Location Topology: Multi-pass membrane protein
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A0A0S7XX76 | MEDISAKAVPAEFIEAIPATYAQQHFLIGIRSQADDSELTVVLSKPLDANALDNVSKMTGLPVKAAISTRAAITAVIDIAYEQRTTVIEEVAEELDSQNLDQLVDEVATSDDLLDVVNRPPVIRLVNDILFRALQLRASDIHVHPYETKIQIRYRIDGILYDTLSLNRNVLPLIISRIKVMAGMDIAERRLPQDGRCSVRLGQREVDLRVSTVPTSYGERSVLRLLDKSTGLFGLDELGLWEDDLKKFDSLLTRSHGVIFVTGPTGSGKSTTLYACLNRINSAEKNVMTVEDPIEYQLEGISQMQVAAKKGVTFVNALRH... | Function: ATPase component of the type II secretion system required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm. Acts as a molecular motor to provide the energy that is required for assembly of the pseudopilus and the extrusion of substrates generated in t... |
U2TIR2 | MAKKERQRRSARQARQRERVAREAQEAAATSDESKGSKRVATSEGKSLAAGSAKGGKEAPRRKGRIRTYLGAVGSELRRVSWPSRSELTNYSVAVIVALVVVGAVVWLVDTGFLNLMFQFTKLRG | Function: Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation.
Subcellular Location: Cell membrane
Sequence Length: 125
Sequence Mass (Da): 13706
Location Topology: Single-pass membrane protein
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A0A142XZE1 | MENTTNTVDGWPDSGRLAGVDYGTVRIGVALCDPSRTWTNPLETYTRKGPEQDRQYFLRITKENQIGGWVLGLPIHCDGRESVKSKEVREFAKWLRDETDRPVRFIDERYTTALANRMLRDLELTHKQRKKQLDKIAAHIILESYLDSTKQPHFEPLPLEDV | Function: Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
EC: 3.1.-.-
Subcellular Location: Cytoplasm
Sequence Length: 162
Sequence Mass (Da): 18811
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A0A1E8F8K2 | MAARLLKKLTGVVVVIAATTSYAQAASVAVDYIRGEGDVEGIKVAYQYYQQVLTDYSPDLHFYVETSVNFWEYGAERQHDTNFIIALSPVLRKTFSPSATGRFFGEFGIGLSLLDDTRFAGKNVSTHYQFEDRLGLGYEFGRTYQYRLALRYFHYSNGGVKKPNPGLDFISLSFAMRL | Function: Has lipid A 3-O-deacylase activity. Hydrolyzes the ester bond at the 3 position of lipid A, a bioactive component of lipopolysaccharide (LPS), thereby releasing the primary fatty acyl moiety.
Catalytic Activity: a 3-(acyloxy)acyl derivative of bacterial toxin + H2O = 3-hydroxyacyl derivative of bacterial toxi... |
A0A0W0SLU3 | MFLDILGTVTSLLATYYFIQLNNKAWLSSLFATLANSWLYWQKGIYADMLLESFYFLSTCYGWYLWRTSTQKEVIIIGKLSIKQWFVLLGLIAGLFVLIVNLLVTFTHSDIALLDALTTSLSLGAQWLMCYKIIATWILWFITDAIYAFMYIQKEIPFHSLLMVVYTLMAIIGYRTWAKQRGIQLLSRTKSCLQ | Function: Required for nicotinamide riboside transport across the inner membrane.
Subcellular Location: Membrane
Sequence Length: 194
Sequence Mass (Da): 22525
Location Topology: Multi-pass membrane protein
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A0A0P0CHQ6 | MMKMMFCLFSMFFMLMINKLEMLIFLIFISLMLLSFILLINMNYNDYWMNMYSWMGMDNYSMILMYLSLWIIMLMMMVSFKVKNKKYFVFILMMLMISLMMSFSMMNYLMFYLFFEISLIPTFMLIMGWGYQSERLNAGMFMFLYTMFASLPLLVLIYYLYNYYDSLNYMIMFLYNLNLLNLNIFVIYFYLFFAFLVKLPMFMFHMWLPKAHVEAPVTGSMILAGVMLKLGGYGIIRSMMIMLNYCVKFNNIFFVMSLFGMLMLSLVCLRQLDMKVLVAYSSVVHMAMMLMGLLTLSYWGLWGGMMMMIGHGLCSSAMFV... | 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... |
A0A3S7EBV2 | YIAYVAYPLDLFEEGSVTNLFTSIVGNVFGFKALRALRLEDLRIPPAYVKTFQGPPHGIQVERDKLNKYGRSLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFISR | Cofactor: Binds 1 Mg(2+) ion per subunit.
Catalytic Activity: 2 (2R)-3-phosphoglycerate + 2 H(+) = CO2 + D-ribulose 1,5-bisphosphate + H2O
EC: 4.1.1.39
Subcellular Location: Plastid
Sequence Length: 106
Sequence Mass (Da): 11857
|
A0A7W7Y396 | MDSRMVFAIVLSAIVLIGYQVFFFDDMDSVEKAIGDAPTEVEERAPSPESEQHQVAQETLPQMEFGSLPAGPPDATAPTQPLTVMEGGEDIVLQNEHIIATFSTHGAHLKSLLLKHHREDGRDGGMVEMLRPGYPAFSTVIITSSGSTDLAAQPFEVENLQAKSATFRTQLASGEELRKHFQLSHDYQFTIRYEMDCPNSNCASLTTLPTEIVENVAGDMFTFDGIIHGNQDDGLEKIKYDDIKSVRDIPNTQYAGVMDKYFLMAFLTTPQDTFRLFPDIPQRGASLVSPIHQEITVFTGPKIKDYLDCYDVGLHRTIDY... | 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 multispa... |
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