ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
|---|---|---|
A0A7S2V4V3 | MGTLLDKPITTKETSNVEHNGLTYGASSMQGWRVEMEDQHTIEVHLTGLQDHSLVAVYDGHGGQFAAKFAGKTLVAEFLSSESVAEYNRSGFRETSLLEKALKETFVAVDEKLKTEADVQCGDCSGCTAICAVITPSHIVCASAGDSRGIMVTSGQVRALSEDHKPDGAIERERIESAGGCVSMRRVDGDLAVARALGDFQYKDRPDLPVDRQKVTCVPDVRTTPRSSGDEVLVLACDGIWDVMSNQDCCDCVRQIYQEGETDSGLVCEELLDTCLTKGSRDNMSVVMVQFPAMLEPPPGTAAGAERGGGVMARRSKRAE... | Function: Enzyme with a broad specificity.
Subcellular Location: Membrane
Sequence Length: 333
Sequence Mass (Da): 35984
Location Topology: Peripheral membrane protein
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A0A8B6HEJ9 | MCTHFFLSRPQFLKRLTCCSTQSFRLFCGKATPQIEHYHCLRSNSQVKINQRQCQLINLSKRYFSKQVPKNETKKELDIKRESPYAGLSAAEKVREAGKDASYIAIIVAGIGVIGVVFYTVGKELFSSQSPAGVYSKALKKCQNNDEVLDVLGEPITGHGTSGSRRRKQHVSSQEFMQNGVKHMRVVFKIEGPYRKGTVHVEVFQDESKKYQFKHVICELQGYPTRTIVIENNR | Function: Essential component of the TIM23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane.
Subcellular Location: Membrane
Sequence Length: 234
Sequence Mass (Da): 26639
Location Topology: Single-pass membrane protein
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A0A367K3Q1 | WMRLGKPEKTQIIEFGPGRGTLMCDMLRSLSHFPHFYKTITDVHLIEASTGLRKLQRAALVNGSQDDDVVRFKGNKEEAAYETITREDGVKISWYDGIEVVPDQWSFVMAHEFFDALPIHIFEKNESEWREMLVDIDDTDESERNFRLMKSAHPTVITKAYMDDEKFKTYNDGDRVEISPDSWGLIEKVAKYLERNGGTGLAIDYGQDYIQGHTLRAIKNHEIIHPMRDPGTADLSADVDFSFLKQVIKERSDISSYGPITQTNFLQSLGIQARVEKLFRNAKSSESRKAILDGAERLMDPEAMGRIYKVLAFSKDSHNV... | Function: Arginine methyltransferase involved in the assembly or stability of mitochondrial NADH:ubiquinone oxidoreductase complex (complex I).
Catalytic Activity: L-arginyl-[protein] + 2 S-adenosyl-L-methionine = 2 H(+) + N(omega),N(omega)'-dimethyl-L-arginyl-[protein] + 2 S-adenosyl-L-homocysteine
EC: 2.1.1.320
Subce... |
A0A7C2VPM0 | MIDDILSKLRFRYEQNTVIAVVQDCETKEVLMVGHMNAEALRKTLETGLLHLWSLTRRKLWLKGETSGNYQHVVDLKVDCDADSVLVMVKPLGPICHTGNRTCFYRRLAEL | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9.
Function: Catalyzes the hydrolysis of the adenine ring of phosphoribosyl-AMP.
EC: 3.5.4.19
Subcellular Location: Cytoplasm
Catalytic Activity: 1-(5-pho... |
A0A7C4H4U8 | MMLSKIYRKVYSFWDSHSRLIAAILVLVASIVGFWLRVQQYLNVINIGMGIVYPEAKLDELDPYVNYWIVSYMDRHGLESLLDLTEKNPATCLFWYPECRNLYATELPGHLLTIYFLYQFVKLFGVELLDLMALIPPMLGALGVIFTALAVKELTRSDIASIISAFAYALVFLSREVAGFTVKYSFGLFTAPLVLWLHIRLLKKPNLLNSVLAGMTIAYAASVWTGIGLTAVPIYVTLVLAPIFIDLTQVDNFKKYTLVFAIEIAIPIIAMISMKAYHGGRAIICLAFPIAFAFYIFGALLSLFLGSRARSLYAKKSTKK... | Pathway: Protein modification; protein glycosylation.
Catalytic Activity: an archaeal dolichyl phosphooligosaccharide + [protein]-L-asparagine = an archaeal dolichyl phosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine.
EC: 2.4.99.21
Subcellular Locat... |
A0A3G9ME60 | MQELKGLDLWAKVGFRSFIRDGAVFLDEIRKIDGNFKIFLDLKLYDIPYTMANAALECAKLEIDMLTVH | Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
EC: 4.1.1.23
Catalytic Activity: H(+) + orotidine 5'-phosphate = CO2 + UMP
Sequence Length: 69
Sequence Mass (Da): 7965
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A0A928RNK4 | MKQNQVLLDSEMKTFNIVEIFSSLSGEGSTAGVPASFVRVDSCNLRCSFCDTKYSYNHEFTTMTFKEIVDMLKTFDNKVVVCTGGEPLLNKNNARLLPLLLSNEGFQVYIETNGSVKLYREEELLQGKRENIHYVVDIKTPASQMERFDCIEHNSCLLLDGDEIKCVVASKEDIEFCKNKISKIFNNIKDKKINIILSPVFGEIKLQDLAEYVMQMKSIMKDSCLTVKLGIQLHKLIWPHIEKGV | Cofactor: Binds 1 S-adenosyl-L-methionine per subunit.
Pathway: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
Function: Catalyzes the complex heterocyclic radical-mediated conversion of 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) to 7-carboxy-7-deazaguanine (CDG), a step common to the biosynthetic pathways of a... |
A0A7S3UG44 | ALQGSRRDAMGEGAAKGSEERSEKMEEERIKVNANRFTLLLGMFVWLGGVHLTLFLLVASALTMSWRIFLTCFALLVSLLFVPLFDTDGWKKKFSTFIVKCALAYFPITLEQEEELDDDKRYVIAFFPHSALPVGISALHPSSPLCPKNFKDGKLVGCGSSAICWCPFVRHVWSWLSIESCSRPHVSKRLEEGMSVILIPGGVRECMLLQEDSENVFLSTRKGFIKLALQHGVSIVPTFAFGQSSAYHYARLGPPLLPRRVVDMIARAIGFLPMYIWGAHGSPLPRPVPIHVVLGKPIHIKQKVSNPTYAQLNEIHAVYV... | EC: 2.3.1.-
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 336
Sequence Mass (Da): 37564
Location Topology: Multi-pass membrane protein
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A0A4U8YWC0 | MAQKKEMIGGIETLEEALAFLEARMDAETLAKLKQIRTEEVVKTIANAAKLCTPDSIFINTGSDADGKAVRAGALANGEEDALPMPNHTIHFELKEEQGRITDRTFYLAEPEEKVSSLANRIDRSEGLDDVKTKMGGIMKGMTMIVGLYMRGPVGALGSNPSLQITSSFYVAHSAEMLYRNRFNDFDNEVERLGYFYTNIHSQGLNRTEDLPNARVYMDRNDQTTYSINCTYAGNTLLMKKGNHRFSVDKAVKNRGNELSEHMFITGIEGPGKRTTWFAGAAPSGCGKTTTAMAGHHFVGDDLAQMWIAEDGTVRSINPE... | Cofactor: Binds 1 Mn(2+) ion per subunit.
Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Function: Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle... |
A0A2E6JA56 | MLHPVILAGGVGARLWPLSRAAMPKQFIELNGSRSLFQRALVRLDSLPGLGRIRVLGNSEHRFLIAEQLRQQKVEGSEILLEPVGRNTAPAVTMAALSAVGEDKDAQILVLAADHNIANVSAFEQAVAAAIELASEKFMVTFGIVPGRPETGYGYLKKGAPLSAQGFRVDKFVEKPNLEKAVAYLASGEYFWNSGMFLFSAVELLKEMEVYAPDIVRQCRMASDRISPDLDFLRIPDIEFAACRSESIDYALMEKTSRAAMVPLDAGWNDLGSWQSLWEISQKDNYGNVVAGQVEMIDCRQSYIHAESRMVAAIGLENVT... | Pathway: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; GDP-alpha-D-mannose from alpha-D-mannose 1-phosphate (GTP route): step 1/1.
EC: 2.7.7.13
Catalytic Activity: alpha-D-mannose 1-phosphate + GTP + H(+) = diphosphate + GDP-alpha-D-mannose
Sequence Length: 468
Sequence Mass (Da): 51750
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A0A2E7GF32 | MKIAILGATGAVGQVLLEQLEKRKFQFSDLKLLASSRSVGKQISVFGKNYKIEEVSESSFTDVDLLFSDVPDDVARHWIPLAHKAGCWVIDNSAAFRYETGIPIIVPEVNAEFLNLDSKILTNPNCSTAQLVVALAPLHRKYQLKRVVVSTYQSTSGGGVAAMNELTSQTESFLKNGTYHPPEVFTHPIGFNCIPSIGGLREDDYTSEEMKMIIETRKIMNLPDLKITATAVRVPTYACHGESVNVEFENEFELDELKKALSDAPGIEVLDHPSDNIYPMGNEAQGKDSVFIGRIRRDLSVSNGVNLWIVSDNLLKGAAL... | Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 2/4.
Function: Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate.
EC: 1.2.1.11
Catalytic Activity: L-aspartate... |
A0A2E7DMS2 | MIKLLNKVPKRITIAVSGGPDSMAALDFLTKRRDVTAAFFHHGTKASDKGEKVVTKYCNERDVTLVTEKISCTRRGGESREEFWRNARYEFFEKLNGPVITCHHLDDVIEWWIFTSLHGNPRLIPYKRDKYIRPFLLNRKQTLINWCRRNDVDYITDSTNRNDLYSRGYIRNHIIPTIGRINPGIHKTMKKKIIEEFTREEGYDAAL | 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)... |
A0A8T7BUW8 | MNLASDYSRGRRYQRMRGFTLIEALIAMFIVALALVAVTTKVSLAAKIASRTQQSTYGRWVAMNAITELRLKPGLPATGSSDGDEDMAGQQFRWDMDIKNTPVEGLRRVDVSVASSERPDEVLYEMSAFLGTNNPNANLRPWAGLPDEELQDPNSLTAPGVTIDRPSRTPFDIRDNQVQPNR | PTM: Cleaved by prepilin peptidase.
Function: Component of the type II secretion system required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm.
Subcellular Location: Cell inner membrane
Sequence Length: 182
Sequence Mass (Da): 20199
Location Topology: Single... |
A0A971Z1M3 | EFKAWLDELLREAKAAGDSVETADQSPAVEAQYETILDQQRLEHWLQQLRDAPLFAFDTETTSVHAQQAELVGVSFAVEPHKAAYVPLAHSYMGVPEQLDREQVLAQLKPLLEDPNLSKLAQNAKYDINVLAHYSIEVRGVAFDSMLESYVLDSTATRHDMDSLALKYLGIGTTRFEDIAGKGAKQLTFDQIALEQAAPYAAEDADITLRLHQNLWPRLQETTPLTSVLQDIEMPLMPVLARIERTGTLVDARLLGEHSRELGDKLTALERQAFELAGEEFNLGSPKQLGVILYEKQGLPVLSKTAKGQPSTAESVLAEL... | Function: In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity.
EC: 2.7.7.7
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Length: 632
Sequence Mass (Da): 70574
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A0A952NIZ3 | MSNSNKKKILIQMSGSIACFKACALISKLVQAGHHVKVAASKSALQFIGAATLEGLTGEKVHSDLWEEGDAMSHIHLMRWADLIAAVPASAHLINRMAQGVGDDLLTTMFLAHDFKKPYVIAPAMNTSMYLHPVTQKSLELLKGMGIEILEAASGVLACGEVGYGRLLEPDLLLAEIETRLKTPQPPTVGASAPQAQELRKVLITSGGTQENIDDVRVISNISTGRTGAEIVDRLESLGIPTVLVHAASAALPSAEGERLSFVSSKDLEEALKNRLAKGDIAAVIHLAAVSDFIPVAQPGKLSSENEPKIELRKNKKILP... | Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 2/5.
Function: Catalyzes two steps in the biosynthesis of coenzyme A. In the first step cysteine is conjugated to 4'-phosphopantothenate to form 4-phosphopantothenoylcysteine, in the latter compound is decarboxylated to form 4'-pho... |
A0A920JN10 | MAKDGGVLIRAGHTEAGCDLAKLAGLEPSAVIVEILNEDGSMARKKELLKFSRNHKLKIGTIDDLIKYKIANEKTIERIHECEVSTDYGDFNSIYYKDVLTNQVHFVMIKNKIAPNKPTVVRVHVQNTFFDTFKITSDTSWSFENALTKISKSSQGAFVFISSPLDSSHIDQISAIKKNNQSSTSMIKNSWHRAQILNDIGVKEMILLNKPKVYHGINAFGLKVKKYLQKRKKIKQRVNFNQKIKSTGESDLNNYYNTKKPIIFIIKSLYHGDITIALHLIL | Pathway: Cofactor biosynthesis; riboflavin biosynthesis; 2-hydroxy-3-oxobutyl phosphate from D-ribulose 5-phosphate: step 1/1.
Function: Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate.
EC: 4.1.99.12
Catalytic Activity: D-ribulose 5-phosphate = (2S)-2-hydroxy-3-oxo... |
I4AF25 | MNFETTKNFASQLDNNDSLAHFRDKFWIPTLNSISKNTNSSNEKGKEKVVYFCGNSLGLQPKTTKAYIEQELEDWKNLGVEGHFHGKNPWLSYHKLLTNQTAKIVGAKPIEVVVMNNLTVNLHLLMVSFYRPNQKRFKILMEGGAFPSDQYAIESQVKFHGFSPDDAIVEMMPRKNENSEGEETLRTEDILKKIEELGDELALVMFGGVNYYTGQFFDLEKITQAAHKVGATAGFDLAHAAGNVPLKLHDWKVDFATWCSYKYLNSGAGGTSGVFINEKYADDDSLPRFAGWWGHDEKDRFKMKKGFIPMRGAEGWQLSN... | Pathway: Amino-acid degradation; L-kynurenine degradation; L-alanine and anthranilate from L-kynurenine: step 1/1.
Function: Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3-hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3-hydroxyanthranilic acid (3-OHAA), respectively.
EC: 3.7.1.3
Catalytic Activity... |
A0A9E2HXK1 | MNVAVRTLNNLFVPRFLSWLFVTEKQWTVALFLGVPVLLSSVGLIYVKDSNRRLEAHLQSLQVQYGRMHAEWSQLLLEESTWSSDARIANQATHRLQMMIPKTKQIVSL | 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: 109
Sequence Mass (Da): 12596
Location Topolo... |
A0A6L8ELN7 | MMFRRGSLVILSGVAGLLAGNLFAGLSLGFLICLVWQYRILKNISKFLRNGGEQNPPDTPGIVNEIVREIGFLRARHKQREDKLTDHLSRFEEAIEALPDAVIIMDANGHVEWANEKASEYLGIRSSGDRRQRLSHIIRQPELLDFLAQTDKDNPRNSLVIASPVNPDISLEIRITRYAESSLLLVAGNVTDIQRTNRMRKDFIANASHELRTPLTVISGYLEAIDSEANDISTEWQPRITQMRSQTRRMQNLIEDLLKLSRLESKPSADLNNEVDIAELVSVIHDEAQTLSGDQNHTFTLEIQDDLIVKGDQDSLYSAF... | Function: Member of the two-component regulatory system PhoR/PhoB involved in the phosphate regulon genes expression. PhoR may function as a membrane-associated protein kinase that phosphorylates PhoB in response to environmental signals.
EC: 2.7.13.3
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phos... |
A0A6M8UGK4 | MSKNNEILDILRTKKSLFRAVGIFTALINMLMLAPSIYMLQVYDRVLPSANSMTLLMLTLMVLGMYAIMGLLEYIRSMVVICISNDIDRQLNTRVYTAAFRAGLKEGPTDKAGQALGDLTTLRQFITGNGLFTLFDAPWFPIYLLVIFLFNISMGVFAFVGAVLLILLAMFNERWSRRPLLQANQLAIASTQLANTNLRNAEVIEAMGMLSNLRRRWLHLHQGFLASQCRASERAALITALTKCVRLTLQSLILGLGGWLAIEGAITPGMMVAGSILMGRVLAPIEQAIGAWKSWRAASLAWQRLVSLLNAFPRPEDRLA... | Catalytic Activity: ATP + H2O + xenobioticSide 1 = ADP + phosphate + xenobioticSide 2.
EC: 7.6.2.2
Subcellular Location: Membrane
Sequence Length: 553
Sequence Mass (Da): 60295
Location Topology: Multi-pass membrane protein
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A0A8X7NDU9 | MSAMLVTPQAPHHLPSSASENATDAELRQRKTNAAVAAVAVAAAASAAQVPEADQVEDEYDNEQRARDGKPLMGRLKDGRQFEVPSTPDMLTSIFDPRQAKTPLDVLTLVSLAAQIVIYFVTSRQQAQAFFLVYFLFWRAAYNAGLGWVLNAQSKKGWLVSFVDRRGWLDKERCPKTREWIKQQLEVKMRSDYDFEALPNEYNIWLLFRSIVDVILLNDFVAYSLFAFSCTRLPEGHSGWAHIGRWALGWTLIAFNAWVKLDAHRVVKDYAWYWGDCFFLCLQQLVFDGVYNLAPDPMYSIGYAGYYGLSLCSASYAVFF... | Pathway: Phospholipid metabolism; phosphatidylcholine biosynthesis.
Subcellular Location: Membrane
Sequence Length: 367
Sequence Mass (Da): 41651
Location Topology: Multi-pass membrane protein
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A0A9C9G293 | MKLSLHTIPVQVTLNTSQGPIVALSRRTGKGRGKKAKAKSSGNKLPGSVLVVSFTLLALVLTAVVLDQLLDPGVFRIQSVRVVGNFDHLKTSTLKNVVSPLIKDNFFAIDLNHVRQRLLALPWVDDVVVRRVWPRTIELAVRETRILTRWGQRKWLSNRGMVITLPGQVQDGLPMLQGPERTSKQVLAAYLRWDRALGAVGLRIVGLQLRKRGSWTVRVVTSKGQDSELVIRLGRDQVDQRLLRFVHWYSLLLQSLAAKPAYIDMRYPNGFALGPRRTPRQKKG | Function: Essential cell division protein. May link together the upstream cell division proteins, which are predominantly cytoplasmic, with the downstream cell division proteins, which are predominantly periplasmic. May control correct divisome assembly.
Subcellular Location: Cell inner membrane
Sequence Length: 284
Se... |
A0A661EFE8 | MKISENWLREWVNPAISNEKLQQQLTMLGLEVESSKPLDVLDKLVIVAQVLSVEPHPNADKLNLCEVDTGLEKLQIICGAKNVKKGIKIPLAQVGSVLGENFKIKPAKLRGIESNGMICSASELGFENKSDGIMILPDDAPIGTKINDYLQLKDNIIDVDVTPNRGDCLSIRGIAREISAKNHIKFKDFTDNNNYIDNNDIFEFDNMEPDSCPVYSCQIIKNINPTIASPIEWAEKLRRCGLKSINPIVDITNLSLLELGQPMHAYDLDKISGKIEIRFSKKDEKIILLDKKECKLAEKTLVIADDNGAIGIAGIMGGYS... | Cofactor: Binds 2 magnesium ions per tetramer.
Catalytic Activity: ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + H(+) + L-phenylalanyl-tRNA(Phe)
EC: 6.1.1.20
Subcellular Location: Cytoplasm
Sequence Length: 794
Sequence Mass (Da): 89975
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A0A3D1EMD8 | MKIIRLPSVLALSILLAACGGEEETTADGSPQSGRGACPVYDAGKKADYADPTKNEDIRLCIPQQTGVILYHEFSEPILVNLKNSRKMMQMKFAAVTKHDNFALAKIASHEMSMRSAFSDRLLQVDEAETGSAGFRTKLQTEFAVAANSIVEKYEAYGFNVVEEVLITDLVVQ | Function: Controls the rotational direction of flagella during chemotaxis.
Subcellular Location: Cell inner membrane
Sequence Length: 173
Sequence Mass (Da): 18948
Location Topology: Single-pass membrane protein
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A0A368C234 | MITLIQRVKEASVSIDSIKISSINAGILAFIAFTPADKEPQLIKMSDKILGYRIFSDDDGRMNRNIVDEKLDLLIVPQFTLAANTKSGTRPSFSCAANPQIGRDLFIQFLEIIKSKYRNIESGKFKENMDVSLINDGPVTFWLEVN | Function: An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active si... |
A0A661DPX7 | QTRELTRECFERGHAVGVLAYDPWKDAIVLLEQFRIGAYIYMADQDNKSARSQSPWLLEIIAGIVEPGESQIEVAHREAEEEAGLTLLALEVIGEFYASPGGTSETIQLYCACVNSNGVGGIHGLEEEGEDIQVRVVSFDEAVQLLENGELNNASAMIAMQWLILHRDQLRDKWQDSAS | Function: Acts on ADP-mannose and ADP-glucose as well as ADP-ribose. Prevents glycogen biosynthesis. The reaction catalyzed by this enzyme is a limiting step of the gluconeogenic process.
EC: 3.6.1.13
Catalytic Activity: ADP-D-ribose + H2O = AMP + D-ribose 5-phosphate + 2 H(+)
Sequence Length: 179
Sequence Mass (Da): 1... |
A0A661EY76 | MKPPTVPRGRFAPSPTGPLHMGSLVAALGSFLNVRQQDGEWLVRIDDIDTPRNVPQMEQAILLTLEQHALQWDGDVYYSSQHLVDYEQVLRALQAAGQVFPCTCSRREISNHPINNQRQTGDTLIYPGTCRAGVTADKPLRSYRLRVPTSAIEFMDLLQGPQADTLAISVGDFVVKDGQGQHHYQLATVVDDQIQQITEVVRGADLLASTARQIHLQNRLGYRQPKYLHLSLVTDALGIKLSKQHGATAVDNTLAGQNLITALTLLQQQPPDELQHVPPAGIIRWAIEHWNREPLKSFPIATLPTTLPD | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the tRNA-independent activation of glutamate in presence of ATP and the subsequent transfer of glutamate onto a tRNA(Asp). Glutamate is transferred on the 2-amino-5-(4,5-dihydroxy-2-cyclopenten-1-yl) moiety of the queuosine in the wobble position of the QUC an... |
A0A920V5F7 | MTQSYISIGSNLDAIKHITIAKRELNNIFTCTYSDNFYSEAEGFKGKDFINLVAGFENSLDPINLTKTLKSLEKKIGRDINQKKVCEIGL | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 4/4.
Function: Catalyzes the transfer of pyrophosphate from adenosine triphosphate (ATP) to 6-hydroxymethyl-7,8-dihydropterin, an enzymatic step ... |
A0A2D6JLY7 | MKNFFSLTMPQLKDYLAELGKEKFRAQQLFRWVYVQGETEIENMTNLSKKFREELPNYLTFELPKVVEQLDSVDGTRKLLFDVGDNMTVETVLIPSEDRLTICLSSEVGCNMACRFCYTGKQKLKKRLSTEQIVGQYVQAAKTLEGEDRRITNIVFMGMGEPLDNCDAVFNSIEIITADYGFNLSRKRVTVSTSGIVPEMHRVWEAKVRLAVSLNAAYDEIRNVVMPVNRRWPLEVLLETCKEFCAQTKDSITFEYVLLKDVTDSLEDARKLPKLLKGIPCKVNLIPFNEHPGSEYKRPNRQRVLTFQKVLMEAGMQTLI... | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs.
EC: 2.1.1.192
Catalytic Activity: adenosine(2503) in 23S rRNA + 2 reduced [2Fe-2S]-... |
A0A9E3M4X0 | MTGNRHIIPTLVRQLIRGERMRTFIALEPPADLRAAIGELSGALDDLMPGMKWVKAANIHLTLRFLGEIETARLEDASVAVAGAAAAISSFDLRPTGLGHFGSPRKPRVVWLGLAHIDNLTELAAGIEERLEESGFGRADKPFSAHLTLARAGRRPGPPPDWERTRAAASPDWPAWTVSEVCVIKSTLTPRGPIYDIISRHELSANP | 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: 207
Sequence Mass (Da): 22518
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I4ALR9 | MKLNYFLLFLFALIILNSCKTSLPSNSTVSYFSEEELKLIYENDSSQAMRVWKINNKEDSIFLRKNCQEVAFNPTDTTIHYFVHRLFKTVRNPNSLGVGIAAPQVGINKRIIWVKRFDKIEEEMPFEVYINPKIIKYSTEVKETAEGCLSIPDRREKVIRPDKITIEYQSLDGKVHQEIVDGFTSVIFQHEIDHLDGILFLDHLKNE | Cofactor: Binds 1 Fe(2+) ion.
Function: Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.
EC: 3.5.1.88
Catalytic ... |
A0A2H0KD34 | MHLIVEQRHKKTTVTCLWLYAILLLMRFLGIDFGTKRVGVALSDETGRLAFPHSVILNDKNLVAEVTQIARDQKVKAIIVGESKNLDGKANSLMKHVEVFVKAIHKEAHKPVYLEPEFWSSFQAGRRQGRRQQGSRGTGVRAEQRRENGMLDASAAAIILQSYLDRRNS | Function: Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
EC: 3.1.-.-
Subcellular Location: Cytoplasm
Sequence Length: 169
Sequence Mass (Da): 19093
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A0A8T7C587 | MSAGWSLLVLIGTIATMAGSAWLLISNRDKKATGERMDHEFDGIEEFDNPLPAWWVTLFFVTIIFGAGYVAYYPALGNLPGAGEWSSAKEWQYRVDQHELRYAPLYEELAAQSPDELIKQPRAMQIGRRLYLNNCSTCHGVTAQGSVGFPNLTDEEWIWGAEFDNIKSGIINGRAANMPAWGEVLSEQQIREVVDFVKVLSRGDTQAAASQPGQTHYVTYCVACHGAQGQGNTLVGGTPLNNDIWLYGGDDAAITASIVNGRMGNMPAQGPIVGEEKAHVLAAYIYSLRTKAQSKAP | Cofactor: Binds 2 heme C groups per subunit.
Pathway: Energy metabolism; oxidative phosphorylation.
Function: C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex.
Subcellular Location: Cell inner membrane
Sequence Length: 297
Sequence Mass (Da): 32416
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A0A8T7IQ35 | MYFDSFAEFINMGGHGPYVWAAYGVTFVSFVIYLAAQRRARKEVERKIRNRIRRELNR | Function: Required for the export of heme to the periplasm for the biogenesis of c-type cytochromes.
Subcellular Location: Cell inner membrane
Sequence Length: 58
Sequence Mass (Da): 6958
Location Topology: Single-pass membrane protein
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A0A8T7C8M5 | MIDTLPRQLHPFSGGLSLDSMKAAALSEPVTQLPTPPEVWVSMHQHCGLAAVPCVNPGQKVRTGELIGRANGTFSANVHASVTGTVGQVCRRPIVHPGGLSEMCVQIISTPEQQHDTAFRISHDYRLADPNMLRQQVAEAGIVGLGGAVFPTALKLAAEADQTLHTLVINGAECDPAISCDEALMREHAPEIVRGIQIMLHILQINIAVIAIEDDKQAAHNSFSAALADAADERLQLCRVPTRYPEGGERQLIQVISGTEVPSGGLPIDIGYLCHNVATAFAIDDAFINGHALTSRIVTVCGNGIATPCNLRVPMGTGVR... | Cofactor: Binds 2 [4Fe-4S] clusters per subunit.
Function: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane.
EC: 7.-.-.-
Subcellular Location: Cell inner membrane
Sequence Length: 516
Sequence Mass (Da): 56374
Location Topology: Peripheral membrane protein
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A0A8T7CBC4 | MTVRLLLITCAALVASCAGAPITLPPPQPEAQPEARRPAGNNAAKTAPYEVLGQRYFPITDATGYRERGVASWYGGKFHGRKTANGERYDMYQYTAAHKTLPLPTWVRVTNLRNGTEIVVKVNDRGPFVKNRLIDLSYAAALRLGMVDAGTTLVEVEMIDPPAEAAVITAASRPAAPAPPPATVTNPPATVTSPPATVTNPPAKVTSPPATVTNPPATVTSPPAGVQDPARRKSDMATSLYVQVGAFGDVANAQRLQASLYNAGLTGVRVNSGYMQEIPVYRVQIGPVTGVVEYDVLMARLDSLGISDTHLVTE | Function: Lytic transglycosylase with a strong preference for naked glycan strands that lack stem peptides.
EC: 4.2.2.-
Subcellular Location: Cell membrane
Sequence Length: 314
Sequence Mass (Da): 33253
Location Topology: Lipid-anchor
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A0A349X6B2 | MTTIDSKETTRQTASPTVSPTPSYNPSIIIGLTGGIGSGKTVASDHFGALGVPIIDTDIIARLVVEPGQAALAQLVEVFGSSILKDDGYLNRDALRELAFSNTENKAKLDEITHPAIRNETMRQLANVTFPYCIVVVPLLTKDSPFQGFMQRIIAVTCSEETRVTRVMQRSKLSREAVIKIISTQLTDQQRLEFADDVIANDGTIDDVKKAVEELHEKYLLLGEPPQT | 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... |
A0A353R047 | DTVTGRTPTQRIEANPAPAAKTNAPQAAPESSLDAVVKAVTPPPAEEPPSPLAKRWQLVAQTDRGPFVITPYRPTYILPLSYAGRRNVEPFQATFGEDEPYDAIEAKFQLSFMSKLWPEFLHPRGDLWFAYTQQSFWQSYNGEASAPFRETNYEPELIYSWKTNFKTLGLNSRLLNVSLDHQSNGRDDPVSRSWNRIIASALFDHGDDFALGLKGWLLRSITA | Cofactor: Binds 1 Ca(2+) ion per monomer. In the dimeric form the Ca(2+) is bound by different amino acids with binding of each Ca(2+) shared with ligands coming from each monomer. The Ca(2+) ion may have a role in catalysis.
Function: Hydrolysis of phosphatidylcholine with phospholipase A2 (EC 3.1.1.4) and phospholipa... |
Q5NVS1 | MAHVRGLQLPGCLALAALCTLVHSQHVFLAPQQALSLLQRVRRANSVFLEEMRKGNLERECVEETCSYEEAFEALESSTATDVFWAKYTACETARTPRDKLAVCLEGNCAEGLGTNYRGHVNITQSGIECQLWRSRYPHKPEINSTTHPGADLQENFCRNPDSSTTGPWCYTTDPTVRRQECSIPVCGQDQVTVAMTPRSEGSGVNLSPPSEQCVPDRGQQYQGHLAVTTHGLPCLAWASAQAKALSKHQDFNSAVQLVENFCRNPDGDEEGVWCYVAGKPGDFGYCDLNYCEEAMEEETGGGLDEDPDRAIEGRTATSE... | Function: Thrombin, which cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII, XIII, and, in complex with thrombomodulin, protein C. Functions in blood homeostasis, inflammation and wound healing.
EC: 3.4.21.5
Catalytic Activity: Selective cleavage of Arg-|-Gly bonds in fib... |
A0A520U9V5 | MREEAIIRTLWLSFQYIKDMKVNKTRFCPSPTGLLHLGNLRTSLFSSLIAKKDNGSFLLRIEDTDLERSKKEFSTAICNDLKWMGLDWDEGPEVGGNEDSYYQSERIDLYEEFYKALLEKNLIYPCFTSEEELKIIRRNQIASGQPPRYTGVWSDATEKEVKEELDKGNKPVYRFRIPKDSKIEFQDLVKGKQSFSTDDLDDFIVRKKDNTPTFMFANAIDDSLMGVDLVLRGDDHLSNTPRQIALLEALGLSLPKYAHVSLFTGSDGAPLSKRNGSISINDLREQGYLPIAVSNYLSRVGHTIVDNDLKTHSELADEFK... | 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: ... |
A0A2E5M3D4 | MNPANGGWLILLSLGLAMALAVLHTPESWPQWLGWLRPAWLALVVFFWVMELPHRLGLISAWVIGLGADVLQADPLGLNGILLAGITYIAWRFYERLRMYSVIQQCGVVFLLVLGSELMRALVQDVAWGRGWSWGVLAPALMSMLIWPLVYLVLQRYRLQFRIE | Function: Involved in formation of the rod shape of the cell. May also contribute to regulation of formation of penicillin-binding proteins.
Subcellular Location: Cell inner membrane
Sequence Length: 164
Sequence Mass (Da): 18642
Location Topology: Multi-pass membrane protein
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A0A2E3U3T2 | MSTISSIKESLKPTDTSANESEWPTFTGAPADDAKDHFIHRNGLEFAGTHLLIDFWGAENLTDLDTMEKAFRDCVDHCGATLLHIHMHHFTPNGGISGVAVLAESHISVHTWPERGYAAFDIFMCGDAQPEKAVPILKEAFRPTRVTVGEQLRGLTQPATEE | PTM: Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme... |
A0A3D5XJM8 | PPGEDGTIQGLLEMLDLPYVGSGVRGSALAMDKVVAKSVFRSHNLPVSAERVVGTGAELKTAVAEIHNTLGSAVAIKPLNAGSAIGVQLLPKGGDLHAALTKGLQFGDCLVEPFIAGKELTVGVLHTSTQPQAHPVIEIRTATGQWYDYENRYTPGQSEHIVPAQLDSKVSAELQRIAVAAHAALGLRDLSRADFILDAENNITLLEVNTLPGMTATSLYPDGAAALGVSFKELVDLLVRTAFARSTH | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation.
EC: 6.3.2.4
Catalytic Activity: ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) + phosphate
Sequence Length: 248
Sequence Mass (Da): 26090
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A0A952HZN7 | MIKPVWVTESDSLALADKLADDVAAHLQHSIEINDAASLVVSGGSTPLPFFKALSHQALRWGKVKVTLADERWVPYASDDSNERFVRENLLVDQASDARFQSLYVDGAEPEEALPKLEAGLSTVARPFSVVILGMGGDGHTASLFPEAAELDDAMALDGTASLAVMRPSSVSQTRITLTRPALLDTEHLIVHITGDKKRSLLEDVLVAVANDCGGDYLPIGRFFEDNNRPVTVYWSP | 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... |
A0A952HTB4 | MINHFYKTYGENSSPVRSFFAPGRVNLIGDHTDYTGGKVFPCAIDSGTTLLLRPSTDGQLHLASTNFSERLSLPITHRDKLPDSHWGNYPLGVISLLAEEGFEIPGLELLYSGNIPNGAGLSSSASILVATAFALSKILTTPHTLIELAHLAQQAEWKFAGTQCGILDQFAVAMGKAAHAIELDCHSLNYRYVPLNLDELSLVVTNTNQRRAVSESAYNERVKECETALTLLQHSSNVTCLGEVSPELLKHHVTAFDDDPIALKRVRHIASENQRVTEAVAALENNDVQRFGELMNQSHTSLQQDFDVSSNELNALVQSA... | Pathway: Carbohydrate metabolism; galactose metabolism.
Function: Catalyzes the transfer of the gamma-phosphate of ATP to D-galactose to form alpha-D-galactose-1-phosphate (Gal-1-P).
Catalytic Activity: alpha-D-galactose + ATP = ADP + alpha-D-galactose 1-phosphate + H(+)
EC: 2.7.1.6
Subcellular Location: Cytoplasm
Sequ... |
A0A9D6MRG2 | MTSIRRRLLFSLLGLFTLGWFVAVAATYVQSRHQIEKLFDAQLERSAKVRVMLWVVANTMDDIEDVKIYEGELARSSRHEKGLAFQVRRRTQEIFHTPESPHFLTPDGPGFSNQVLDGREWRVYTVFQPEESLTVQAGEPYAIRRQLVYEITRNALYPLLLAIPLLAAMIWLGVGGGLRPLKKVSSQVAERSPSHLRPLETKDVPSEIRIFVDELNTLLLRLHEAFEMERQFTANAAHEIRTPLASLKTHAQVALRSLNQGQREERLVQIIHGVDRVTHLVEQLLTLARLDYETQEQKFTPIDLVSLTSEVLAEIAPTAL... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Cell inner membrane
Sequence Length: 450
Sequence Mass (Da): 50537
Location Topology: Multi-pass membrane protein
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A0A9D0QUK9 | MANIRLIPRLDIKGQHLIKGVHLEGLRKLGDPHQFAKRYYQQGADELLYMDAVASLYGRNNLTAIIRKTVRDIFIPITVGGGIRSVADVRQILLSGADKIAVNTAAILHPPLIDKIANHFGSQCMVISIEAKRVADGKWEAYTDNGREKTGRDVVAWAREAAQRGAGEILLTSIDQEGTRRGFDLELITAVTQSVGIPVIASGG | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 5/9.
Function: IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ... |
A0A8T3S124 | MNRLDRYIIRVLLSSTLLVLLVLLALNVFFALVGELDSAGQGNYSYVDIFIYVACSLPRMTYEIFPAAVLIGGLLGLGNLAAQQELTAMRAAGVSVLRIAGAAVQAGLLMIVFSVFVGEVLMPFSAEYAQKMRLSEQNKQVSAGRSGVWMRDGNRFVNVRVIHNDGLLEFVSVMEFDDQSKLHRMLNAHKAQTNKNNNTWVFSGVTQTRFVGDRVEKTSLDTFEYVDFINPDFLRVASLDPRYMSALALWRYVQYQETNHLDSGRYRLAFWLKWALPFSVLAMLLMALPFAFGSTRSGNAGRLLLLGVLVGLSFYILMQM... | Function: Part of the ABC transporter complex LptBFG involved in the translocation of lipopolysaccharide (LPS) from the inner membrane to the outer membrane.
Subcellular Location: Membrane
Sequence Length: 355
Sequence Mass (Da): 39779
Location Topology: Multi-pass membrane protein
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A0A2D8S3E7 | MKMKKVAVIGAGPCGITAIKNFNDQGFEVTAFERCEGVGGNWRFNDPSGHSSVFETTHIISSKYTSFYEDFPLPKDASDYPSHKELLKYFNDYADHFDINRLIKFGTEVLHCKYTDDAKWIIQWRSLDSENINEDKFDALVVCNGHHHEPRYPSYPGDFSGEYLHSHDYKSAKPFADKRILVIGGGNSACDVAVETARVAKKTTISWRRGYHLIPKFMFGLTTDIFSYKSRWLPVPLRVPFMKFMLELIQGKNEDIGLPKVTNSILATHPTVNSELYDAIRHGKVKPKPDIDKIDQNTVHFKDNSHEDFDVIIACTGFKI... | Catalytic Activity: (2E)-geranial + H(+) + NADPH + O2 = (1E)-2,6-dimethylhepta-1,5-dien-1-yl formate + H2O + NADP(+)
EC: 1.14.13.148
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 434
Sequence Mass (Da): 49533
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A0A938Q7P7 | MTLDPAVSWILGLGFALLFGVAAGHKFADRVRFLAVLRNYELIPAGLVPLTAMVIVAAEAAAALLLVPPAVRGYGALAAVALLAAYAIAIAINLLRGRTRIDCGCLGFGRQDRITWTMVARNLVLVALALALLLPASPRGLVALDALTISAGLVAMTLLAAALTRLGTLPAGRKGAP | Pathway: One-carbon metabolism; methylamine degradation.
Function: May be specifically involved in the processing, transport, and/or maturation of the MADH beta-subunit.
Subcellular Location: Cell membrane
Sequence Length: 177
Sequence Mass (Da): 18200
Location Topology: Multi-pass membrane protein
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A0A920JM94 | MTINSTSEIINALKKGEMVIIMDDENRENEGDLGL | Pathway: Cofactor biosynthesis; riboflavin biosynthesis; 2-hydroxy-3-oxobutyl phosphate from D-ribulose 5-phosphate: step 1/1.
Function: Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate.
EC: 4.1.99.12
Sequence Length: 35
Sequence Mass (Da): 3894
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A0A920FCJ2 | MKNLILIFLLSFTITSSYGASKIENNKHEDTTLIKIYTTQGEIELKLFDDKAPETTKNFILYAESGKYNGTIFHRVIKDFMIQGGGHLPDLSEIATESPVVNESNNGLSNKKGTIAMARTSDPHSATSQFFINLKDNDFLDKKNAPDNYGYCVFGEVTNGIDVVEKIGESQTGRNGMYDDVPMETVLIEKVEIIKE | 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: 196
Sequence Mass (Da): 21856
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A0A520U3C2 | MENKIIIPLDLEYADAIHIAKILDPEICRLKVGSQLFTSSGPKIIKELHNLGFDIFLDLKFHDIPNTVYQAIKSAADQGVWMVNVHASGGSKMLEASYKALSGYPNPPLLIGVTVLTSVSEESLKEVGLSHLQEQV | Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
Function: Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP).
EC: 4.1.1.23
Catalytic Activity: H(+) + orotidine 5'-phosphate = CO2 + UMP
Sequence Length: 136
Sequence Mass (... |
A0A8T3S0Y4 | MNIKRIHAADIRSGLRKVKEELGPDAVILANRRTATGIEIVAGINLDDPWAMNQANIKSDARPQVNSSAAIATNNNERIMHEAYLGNKPPVSQARILSNATGAYKPQFPKLNSNLDNTVDRIETAQRTQASAIQFSATQASATQQLAAKAKVIALKQHQQSQKLNAENKVLKEAIKKLMLQQKNNAATLSSLTAQASQKQNISSGDIVKLQAPMLRTVQKEIDQLRNLMVNQLDYMGWGKWSEQSPIQSAVLRQLTRIGLDAEQCKRIVNQLGVCTDKSIAWRKALGLWASEIRVNGDDIIQQGGIVALIGPTGVGKTTT... | Function: Necessary for flagellar biosynthesis. May be involved in translocation of the flagellum.
Subcellular Location: Cell membrane
Sequence Length: 549
Sequence Mass (Da): 59924
Location Topology: Peripheral membrane protein
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A0A2E8KBV0 | MPELILASSSPRRADLLSQINLGFKVLVPEVSESVHKNEQPADYVARVSRQKAESVAALLERETGTLSTTRIILAADTIVAIDGDILGKPGGRSDAIAMLQRLSAATHQVITSVTVRCGNRVETALVETVVQFRAISLEECSRYWLSGEPADKAGAYGIQGLGSIFIERLSGSYSNVVGLPLTETAVLLGGFGLECLPQERRPQPTEEQNLDKDVVQNG | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: H2O + UTP = diphosphate + H(+) + UMP
EC: 3.6.1.9
Subcellular Location: Cytoplasm
Seque... |
A0A947XUY9 | MGGTFDPIHFGHLRLAEEMAEGLGLARVRFIPAGQPPHRGAPHTVATHRLEMVRRAIAGNPRFELDAREVESPRPSYTVDTLAALRAELGSEQPLWLLLGADAFLALPTWHEWRQLFELAHIAVAARPGARLLQSDVMPEILKNEVSQRQPVDGPVSGPAGSVLLRKMTPLDISATAIRDTLARHGSARYLLPDAVLDTGKLTSLFERMVIASGTSNRQTRALADNVRIKMKEAGEYVGNTEGEETGEWVLLDLGDVIVHVMLPATRTHYNLEELWGAAEAARARHIQADH | 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).
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NA... |
A0A968NP13 | MAEDYTQAGIEGIFNTVRSGNPVPKADVSKFKTAMLYEFGVMDHEKGWTTQYHL | Pathway: Carbohydrate metabolism; pentose and glucuronate interconversion.
EC: 5.3.1.12
Catalytic Activity: D-glucuronate = D-fructuronate
Sequence Length: 54
Sequence Mass (Da): 6111
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A0A0D8HMW1 | MKEQVSGGAAVVDALAAHGVTDVFGIPGTHNLEIYRYLPASGIRHVVTRHEQGAGYAADGFARVSGSPGVVITTSGPGITNAITALATAYADSIPVLAISPGPLRGTVGRDIGWLHELKNQQAALASVCETSIRVESAEEIPVAIASAFASFATGRPRPVHIEIPVDVLEGSWTRTTVEVQEHPVRAPSSPITGIVDALEGATRPLLIAGGGARRASGPILALANRGLRVLTTVNGKGVLDEGHASALGASIRLSAAHSLANEADVLIIVGSELGDSDLWGGTIAPGGDDRKIIRIDIDRAQLHKNVDADIAVQGDANSV... | Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 1/4.
EC: 2.2.1.6
Catalytic Activity: H(+) + 2 pyruvate = (2S)-2-acetolactate + CO2
Sequence Length: 537
Sequence Mass (Da): 56400
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A0A948GQ34 | MALTLRFKVFERYLAREIYASTALILAAFLALFGFFDVIHELPNVGRGGYTMGHVAAYVALTMPVRVYELMPIAVLIGTLYALTLLARHSEITVLRASGLSTRGLLQALAKIGAVMAIVTFAFGEFVAPPAERQAQQLRLQALSSVVAQEFRSGLWVKDELSFVNVREVLPDASLRGVRIYEFDSSFQLRAISEAEAGRYVGPNLWHLTSVVQTLFEGGRARAVRATEQQWRSSLTPEILTVLMVMFPERMSIASLYSYIRHLGDNQQKTDRYEIALWKKLTYPLAVLVMMALALPFAYMQDRMGAVSVKVFAGIMLGIT... | Function: Part of the ABC transporter complex LptBFG involved in the translocation of lipopolysaccharide (LPS) from the inner membrane to the outer membrane.
Subcellular Location: Membrane
Sequence Length: 364
Sequence Mass (Da): 40662
Location Topology: Multi-pass membrane protein
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I4AKK5 | MKKVIEFLQESRDEMTEHVTWSSFKSLQQTSVVVLVASLIFALIVFGMDQAFQFGLGEIYKSF | 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 inner membrane
Sequence Length: 63
Sequence Mass (Da): 7236
Location Topology: Single-pass membrane protein
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A0A967Z7Y8 | TVTYDQREKRLNINGEAVPLELLGPYDGDPVLQLGEEVLGGKEHELLHMRSRISPGGTYVVPEGHYFVMGDNRDNSQDSRFEGVRYIPEDRMVGRAVRIWMNWRWPSEGGPQWSRIGAGIQ | Catalytic Activity: Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.
EC: 3.4.21.89
Subcellular Location: Membrane
Sequence Length: 121
Sequence Mass (Da): 13794
Location Topology: Multi-pass membrane protein
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A0A963B8U6 | MAEKYGGYLKNSYLLSAVGIIALTIGSIVYLAIQDYLYFVEENEHSIIDQSQRITLVTDKYFEKYRDIFTAIAHSDCVVKRDGAACSRFFARLNGLYPMVENFAAIDRDGRFFASGQPFDRNNPPNVRDLPFFRALESGASSYVMNPHTGPISGARVTGIVIPLLDGAGKFDGLIGVSLKMEEIETLWEGMLNQPNAIYLIIDRNQRLIAASDHAEQLLGQRKISLDLLTKTMQQNGSDRKFEISREFTLHAISSEPSEWMIISLIPTRLPIADYLKDRTFNKVAGTFLILLLGLTIFGLFRDALSRTRLKQTEKKLQAS... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 866
Sequence Mass (Da): 96369
Location Topology: Multi-pass membrane protein
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A0A2D7FWS4 | MTVSGSQFNMSGIATAVHEEETALTTDRLWPSKSLRQVLAIAEEVPVPEVDGIDIDSRRLTEGSLFIPLAPPHAERDGHNFIDAALEQGAAAALSHLPIGQDLGRLPVDDTYIGLQHLARAARSRVAAEAKIIALTGSSGKTTLRSWLQHLLSDVGLTHGSEGSFNNHLGVPLSLARMPSATQFGLFEIGTNHPGEIAPLSRLVDPDVAIVLNVLPVHIGHFESFEALQAEKTSIAEGLDASGQLVVEASIPIRSSQPITRFKVLADGLTSPNPEEEAWDANDRPLYAGQITINEEVHRVLLPAPGSHLLATAAACLATY... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Involved in cell wall formation. Catalyzes the final step in the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the precursor of murein.
Catalytic Activity: ATP + D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-d... |
A0A2E7DKB9 | MMFLEKAWYKKAKWLIILWPLGMLFQIFVFLRRRRQQVLSRPEFICVPIIVIGNITVGGTGKTPLLIALTKYLKKQGMKPGVVSRGYGGSGATYPMLIDEFTSPNLAGDEAVLIAKHCNCPVVIDPDRNSGVNQLLTSEKVDVVLSDDGLQHYKLYRDIEIAVLDGQRLLGNTFCLPAGPLREPVKRLETVDYIVINGREADASFKDAIDMEMEPMFLTNLATGEKRPFSGAPFNIGNTLQAVCGIGNPERFYNSLEKLPYPIKRFTFPDHYNFTLDDFKNMGMEEHQPVVMTEKDAIKCADFAKNNFWFLEATVNLPEE... | Pathway: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 6/6.
Function: Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form te... |
A0A523LK73 | METRTFVLVALLAALAAASFFVVRQNGADEEEPGVGVIGNADYTMTGFTLTTMDEDGATQYRLTSAQLIHYEGDATAQFEQPDVTIYGKGLPVWHIVSDQGELTAAGDEVHLLGNVTITKINQDGTQPAVTIFTKNLWLYPEQELAQTDEGVEIKQPSGTLWGTGMRANLAAQQFELLSDVRGWYVPPTP | Function: Involved in the assembly of lipopolysaccharide (LPS). Required for the translocation of LPS from the inner membrane to the outer membrane. Facilitates the transfer of LPS from the inner membrane to the periplasmic protein LptA. Could be a docking site for LptA.
Subcellular Location: Cell inner membrane
Sequen... |
A0A2E7GHP3 | MSHSPAILITVSGPDSPGITSALTKVLSDSQAKILDIGQSVIHGLLSLSILFESKEGGHNTLKELLFKSTEMGLKMDFKLIQSQETKNAPKTRYAITLIGDDISASALHEVTEVLAQTTTNIDTIERLSQSDFGCVQMLLSSETPINQSDLRKKLLEIARIQKVDIALQTEGLFRRAKRLVVMDMDSTLIQNEVIDEMAKHLGVYDEVASVTEKAMNGAMDFDESLKLRVSKLKGMKESDTHEVFQKLKLTSGAEDLIRVLKKLGYKIALISGGFSIVADQFKEKLGIDYAYANQLEMINGICTGNVIPPIVNAQRKSDL... | Pathway: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 3/3.
EC: 3.1.3.3
Catalytic Activity: H2O + O-phospho-D-serine = D-serine + phosphate
Sequence Length: 394
Sequence Mass (Da): 43222
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A0A2E2WSH0 | MARQEVIKKYAVFGNPIEHSMSPLIHEYFAKNLKINLSYVPILGSLGKFEKEAKIFLGNGGSGFNVTLPFKEDAFKLAETKSKIARITGSVNTISIKNGIIHGDNTDGIGFVKDMKNNIEYDFNDKKILVVGAGGAAMGVIPSILNENPSELKIYNRTFEKAKALSDSFENIGPVEAVSQDKIHKHNFDLIINATSIGINNIKFELSKKILNTETVCYDMSYGKISNSFKMWSNENNLKFHDGLGMLLEQAAESFYIWELQRPVITEELKNNLKQRL | 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... |
A0A2E7GBQ6 | MKNMDLDKLYVIHLPKNEGSKDFAQWAALIQKQHSQSFFTETCQRYLWVIHSNSPIIESELPVEILSKNDAYQFLLELTTGLKSEIAGETDIFGQYKKSWGEYESQYEPEKALRTLMQKLFADTKEIRSRYIQRIGGSSYGTLARMALQIQPADSCLLLGAGKLAHSVSPFLNGKELYVWNRNSERLQKLITHLHSHPRFETKITEVPTNDLPELIKRVNKIVICIPTSENDSKWIQLVNKENPNASLLHLGCLRNESEIWKKIKNFQCLTDLFDLEKSQTKKRWFQIERARTACRARSWHRSFRAPKRMNSEDTHVLTL... | Function: Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
EC: 2.5.1.61
Catalytic Activity: H2O + 4 porphobilinogen = hydroxymethylbilane + 4 NH4(+)
Sequence Length: 805
Sequence Mass (Da): 92090
|
A0A098E6A6 | MENKKINIGIVAAEFNYDVTYAMVELAKEHAKFLNAEVVEVMKLPGTYDIPFGVKILLSKKNIDCIVTLGAVIEGQTDHDEIIAQQASRKIMDLSLEFNKPVALGISGPGMSRLEAHERVDYAKRAVETAVKMCKIKFANEEEKKEEEEVTKEQKIEEPEKKKGDLMGAEEFMNKITEGKREKKKAGRPKKKKTFEVMANKTKKGEEISGPAKLKKIKDEEKKKIIEEIKKKRNITTKDVMNMFNVKRITAWSAMKELIKEGWVKTEGRRNKTRYILA | Pathway: Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2.
EC: 2.5.1.78
Catalytic Activity: (2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2 H2O + phosphat... |
A0A8T6I595 | MTSLSDWLDRIGVEHPRGVRRGLEHVRDVAERLDVLPPAPCCIVVAGTNGKGSTAAFVESLLLAAGRTVGTTTSPHLHRFNERIRINGREADDANIVAAFEAVEACRQGAGLSYFEYAILAALKVITEAGVDHAVLEIGLGGRLDAVNVVDADVAVITSIGLDHQDYLGATRELIGAEKAGILRSGIPLVYGERVPPRSVTARAHDLDVPVYLAGRDFGHVGRSLWFRDRDQRGSLELPESAVDPVNAATAVQVTRLSGCPLDQSAVAAAAGRVRNPGRFEVVRRDDRVWVFDVAHNPDGAEFLAGQLRERFAGRIAGAV... | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 2/2.
Function: Functions in two distinct reactions of the de novo folate biosynthetic pathway. Catalyzes the addition of a glutamate residue ... |
A0A2E0GSS7 | MSINKDQIKYLSLLSRMDIQDSEINDVEEKLTKIIDFVDELQSIDTDEIQPMAHPLNQSQRLRADEVVEENNRDKIQKNTKSTERGMYIVPKVID | 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 ... |
A0A2E0GST2 | MKFGFYIILTILLGALLAXNLIDFPGHISIYYKDFVIDISLIFFLLCFSXFLILIYXLSKVLXAPSFLXNKAKNSKRXKSNKLLENSILAMSKGDYHDAQRNALKALPFCDNPILAYTQIIQAYXSQDKYKERDEWIKKAYEKLSHAETHILLIQANTQLKSSDYENAKATLEKINEIEPDNTIAAELLADMQIKFSEWXQLENNLXXLKSLNRSKEEKLIELELISIAELIKDAKNFDLLKKIWKGASNSVKESSYLVDTYCKKLKELNENDVAEKILLNFLKKTFDEILVYNFISLNQDQPEKVIKKISQWQKRYENN... | Pathway: Porphyrin-containing compound metabolism; protoheme biosynthesis.
Function: Involved in a late step of protoheme IX synthesis.
Subcellular Location: Cell inner membrane
Sequence Length: 389
Sequence Mass (Da): 45321
Location Topology: Multi-pass membrane protein
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A0A969HXV4 | MTHFDYSFGLEEEFFLSRADTGALAVDVAGALLNEARSTLGACVTAEMLQSQIEIASPIFRHVHEAHERMITLRQGLANVAACLGLTPIAAGTHPLGVWQEQLVADDLRYEQLMADFRIVGHRNLVCGLHVHVSVPSCVDRVDLMNRVMRWLPLLLALSTSSPFWNGSVTGLLSYRQALYDEWPRSGIPDFFESEADYAAFADRMTRAGAILDSSQLWWAIRPALRYPTLELRLTDACTLVEDSVAIAALFRCLVAATVKSPRAGVRHTTHTRRIIDENRWRAKRDGIRAQFIAEASSDVLSVAQVLHAARAFVADEADR... | Function: ATP-dependent carboxylate-amine ligase which exhibits weak glutamate--cysteine ligase activity.
EC: 6.3.2.2
Catalytic Activity: ATP + L-cysteine + L-glutamate = ADP + gamma-L-glutamyl-L-cysteine + H(+) + phosphate
Sequence Length: 392
Sequence Mass (Da): 44172
|
A0A9D8A1Q4 | MKSNSVKGFTLLEVMVALVIIAITLGAIIENNTASTRNALHLKNKTIAYLVANNQMVKTRIARTWPQSSAMSGVVENAKQEWLWKQKLSKTDDSALRRIDITVSLNEKPDAILYQLTGFMTSP | PTM: Cleaved by prepilin peptidase.
Function: Component of the type II secretion system required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm.
Subcellular Location: Cell inner membrane
Sequence Length: 123
Sequence Mass (Da): 13677
Location Topology: Single... |
A0A2D7G684 | MRGMAEQWSFHSTPRRIGFVLALILCVSALRSTFFDWHHVPTQSMVPTIFPGDRIIVSKSFYRVRLPFSSVTVLERNSPERSDVVTFLDPEEDLLMVKRIIGIPGDRVEMDDNQLIINGIEASYIGTQNSKDKDLADSKFSHLREFNETISEKSRDIAIFSIKPKWSQRSFESKTIPTSHYLVLGDNRDDSSDYRTFGLIREDRIMGKVLRVGISQKI | Catalytic Activity: Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.
EC: 3.4.21.89
Subcellular Location: Membrane
Sequence Length: 218
Sequence Mass (Da): 25044
Location Topology: Multi-pass membrane protein
|
A0A2E9KPZ7 | MKYIASNLGMPRVGRKRELKFIIEKYWRGEASISELTSTAEEVVTLNNTLQAQAGINPTTVNDFTLYDRMLDMCCLTGLIPSRFNNLNKLSFTDSYFRFARGEGNVAAMEMTKWFDTNYHYIVPEIEETSAPNFNREFFENQILPNGDRNNQKFTIIGPLTFLTLAKASKGSINKYAIYFELKKTYDELLKYVLSLGYINLQIEEPALGTDLSDEQVTIFSDFYSNLKARLDIPTNILLATYFGNVEDNISIVKNIEVDCLHLDIFTDESNIDNLSTLNESYDSISLGVISGRNIWKINLNETIEIVNRALQNLNFDTVF... | Cofactor: Binds 1 zinc ion per subunit.
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-methionine from L-homocysteine (MetE route): step 1/1.
Function: Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation.
EC: 2.1.1.... |
A0A9K3CTS3 | MDKDRDESQILGMKRMLEQRDLYEAAYGVTRMIKGTRSGWLYNVQESKTEDTNVGIVKSCLDCYLMDSVGEQFKVSIPFCPFLLLSAEPAAFSQIETELGRMFPDCICGVSIVKKEDLEVPNHLIVHTEFMKVEFHTQDDLRTCARAMRARLPDKDTYTKQSDTLIHDLEDAAGTNSHYLSATSGLFGLLRDVVEWDVPYTTRAMIELDVRCALWYKVTVKPGVVSVSQLKDKVTHNTPRVLAFDIETTKQPLRFPDAETDEVMMISYMVDDQGYLIVNRSIVSADIPDFEYTPTQEYKETLDVFFRHCREVKPTIYVTY... | Function: DNA polymerase II participates in chromosomal DNA replication.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
EC: 2.7.7.7
Subcellular Location: Nucleus
Sequence Length: 583
Sequence Mass (Da): 66622
|
A0A6N9AV38 | MNTHRCGLRGVNLLNVHQIIVRKLGRVDYQKTVEEMQEFTRCRHSEVRDELWLLEHHPVYTQGYTCNQLPFGTSNIPIVSTDRGGQITYHGPGQLVIYLLLDIKRRNQGVRNLINSIEAGIIATLQHYRIEGQVRPKAPGVYVKERKVASLGIRVSRGCTYHGLSLNVDMDTSPFESIDVCGYKDLEVTTMHETGANCDLNEIATRCAEELAQELGYLQITYVSGVNSVKE | 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... |
A0A3D5Y4E0 | MKTGCASLLVLALALAGCGTGPVHFAREGPQAADSPNLRTSAEVTRRWKRDTGAGYADSSTLLLPMAADDRIFVAEPAGLIQALDSASGKPLWQVDLEEPLAAGIGGDNSILVVATGEGTVVALGRDNGAVLWRTAIGSEVLARPVVTEDKVLVRSGDGQVIGLNAQTGVVGWRVRRAVPSLSVRGLSTPAIVEGVLVVGFANGRLAGIDVHSGQELWNVLIARPRGSNEITRLTDIDADPYRVGKLLFVAAYQGRISTLSLGNQSVLWRSDISTLKPMGSRARVLLVTADDGTIIGIDQSSGATLWTQTALRGRGVTGP... | 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: 386
Sequence Mass (Da): 40094
Location Topology: Lipid-anchor
|
A0A946VWZ7 | MASLQRHSDNNDWYILGAGAIGCLWAAMLAKLQLNVTLLHRRTGTVGIEPVTLKYASGNSSESYPVYSTTAPDLREQQCQINQLLVATKSYDVVAAINDILPLLGSQAKVITLCNGYGMHSEIVECLNKQKPEIELYAAASSEGALLQAPLHIRHTGRGVTRIGPLQGVSSKNPLPPQLALNVEYVNNIEFNLLQKFFINCVINPLTAIYDCNNGFLLSDQNAYADFCQLCSELQTVYDAVVLHLGDFGMVPHGIDFDLHENALDVAKSTADNLSSMLQDYRAGRQLELRYLNREASAMARRMGIACPLNALILNKLG | 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: 318
Sequen... |
A0A3D0SUV2 | MAKSYWSHALLYSSLAAALAGCGTVPENSAPLGSPVADIPATPPKSNLESALRLEPASRSGNPDTYVVFGRRYRVQETSEGYRERGVASWYGKGFHGRKTSSGPLYNMFDLTAAHKSLPIPTYVRVTNLENGRNVVVKVNDRGPFVGQRIIDLSYAAADRLAMLGKGTAQVEVTALEPYQLLPKLAARRADARRQLAGQPSKSASDGPATPRSAREEPKAPDSAALSVVASARAEPPPASPPLPLTFASVPTEPSKRSIAEPARSVTPPRGAAPPMVRVEPVPPAMSEPPRSELIAVRAGPPGPVASPPQTLAGDDASAG... | Function: Lytic transglycosylase with a strong preference for naked glycan strands that lack stem peptides.
EC: 4.2.2.-
Subcellular Location: Cell membrane
Sequence Length: 426
Sequence Mass (Da): 44755
Location Topology: Lipid-anchor
|
A0A2E8I2I9 | VLETLKSNEVFLWSVVDDLGVWKACLIAQLNVDQVDLLFIYVRPNFRKEGVGHLLMNELIKWSGHTAKANDIFLEVRESNIAAIQLYKRYHFEQVGVRKSYYQDGENAIVMKKSLV | 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: 116
Sequence Mass (Da): 13429
|
A0A6L7VUT3 | MWLGVVTIFPDLVKASFKEGVVGRAIERGDISLETINPRDYPLNSYGSVDDRPFGGGPGMVMAAEPLAACVQAARETVRPHTLKTALLSPQGTLFSQSLATELSQLDALLLVAGRYEGVDERFITNYVDLEISIGDYVLSGGELAASVVVDVIGRYVEGTVNNPESIECESFTDDLLDCPQYTRPRVFEGLEVPEVLLSGDHGAVEHWRHQQRIEKTWTRRPDLLVQRVNRETETTELRNCMLNAQPASLETVEEESCAKQQNN | Function: Specifically methylates guanosine-37 in various tRNAs.
Catalytic Activity: guanosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(37) in tRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.228
Subcellular Location: Cytoplasm
Sequence Length: 264
Sequence Mass (Da): 29194
|
A0A2D5PRT9 | MKLHRVYYKEFSRIDKISIDNKSKINHLRNVLRLTEGSKLDVFDGEGNSSIYKIVSLEKKKIVLEQVGDIEFQQPERINLKVLMPYIKKENLFFAIQKVTEIGVSNVSLFRPDNIDQSIKNKDLSKISEKALSIITQACEQNGSNIVPDFQIYEDLSSAIDHDSFSIFFDLDATNDFQSIENVEDSITLITGPESGFSKKEKEFLNATTSHNISLGKNILRAETAPITALSVIKSNLGLL | 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... |
A0A2G6EIP9 | MVPNSSEFGKPMVDDQAWLDGAAGSNRQSRIVVSAEALRHNLAVARRFSPGSRFLATIKANGYGHGAVAVAQVLSTPPGPNDTDGYRPADGFNVVTLAEALALRRAGIDAPIMVLQGLREEGDLVHFVEHHLWPVVHASEQWAWYRKAPLARELFTWLKVDTGMGRLGVPPEEATAILADTPASDRVRGVMTHLACADVPGNAHTREQLERFAAIRSLAGEARADSIANSAAVLAWPEAQADWARPGILLYGANPLVEPLPAGVKLVPAMTVTAPLVSVREFRQGQGVGYGQHWHAPEAMPVGHVGIGYGDGLPRLLGED... | Pathway: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1.
Function: Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids.
EC: 5.1.1.1
Catalytic Activity: L-alanine = D-alanine
Sequence Length: 393
Sequence Mass (Da): 41978
|
A0A389M204 | MPRLYIDAPIIPNQSFILKDAPFNHAIRVLRLQIKDEIVLFNGTGGEYLAIITSIDKKHAVLQVLDFNPIERESSLNLHLYQALAKGDKLDYILQKATELGVNSITLLISKRSIAAIAEERLDKKMAHFRSIIISACEQCGRNTLPVLELPLKLHKLNLSSELNYLTLDPKAEDKLSDSIKVSTKGATHKNIALIIGPEGGLSPDELDLLSKKGCQSINLGARILRTETAAIAVIAALQALFGDW | 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... |
A0A3C0YJI7 | MNSSRASGPTKGAADHALIFMLRLYFQLLRWLLIKTTKPSISGEENLRFPHPDLVVDPQSRKAPWQVVYVIQRRSVLDLLALETALIKGGLAPELEENMPLSPLELGTWRTSRRSLALERAFRGRITMRRHSRRLRKLIAAPMAVQENVLLVPVSIFWGRSLAPRGSWIKALTSDQRSATAGFKRMVTLILNRGDIHICFGSGIALSELATHPRGEDYALRRAARLLRVRFKAQHRATLGPDFSHRRTLLNSVVASAEVQASINALVEEGGNRWRLERQANKMVRTIASDMTYSIIRFFLIFLAWFWARIYSGIDIRGLT... | Pathway: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 1/3.
EC: 2.3.1.15
Catalytic Activity: an acyl-CoA + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-phosphate + CoA
Sequence Length: 839
Sequence Mass (Da): 94290
|
A0A520TTZ3 | MDQDLTKLINPSIEGLTPYEPGKPIEDLEREFGINKAIKLASNENPIGPSPKVIESINKEVFNIHRYPDGNGFRLKEAIASKFKIKSSSLTLGNGSNDIIEFVARCFLNTQSSVVFSQYAFAVYPLVIKALGAKPIEVRAKDWGHHLQAMLEAIEEDTKIIFIANPNNPTGTFIKRQEIIRFLEKVPSNKIVFLDQAYFEYSDYEEEDVTLDIVDNFENLVISRTFSKAYGLAGLRVGYSVSSEPIANYLNRIRQPFNVNSLALKAAEIALSDDEHLERCLSSNKKEKIKLYNFFKDNNFEYIDSLANFICFNCKDESRD... | 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: 366
Sequence Mass (Da): 41723
|
A0A9D8J4A1 | MLNPILTVAVTGLLGSINISLKLLGTEFHQKRLNKAFYVLLLITYINLFNVESLFVIITAISGIVKFNRFLQKTLANSVIKEFSNQYFIPLFIIAMVRFFIIQPYQVPTGSLEPTVMPGDFLLVNQYAYGLRLPMTQTEILPIGKPKRGDIAVFQSPVGEEKLVKRVIGLPGDHLVYKNKQLIINGIPVSQEATADQNASSAQMRLTEYLPGKTHDILIIPNRANESIDLSIPENHYFMMGDNRDSSGDSRIFGPVDAKYLIGKAFFIWMNWNPQNGEIDSERIGKSL | Catalytic Activity: Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.
EC: 3.4.21.89
Subcellular Location: Membrane
Sequence Length: 288
Sequence Mass (Da): 32365
Location Topology: Multi-pass membrane protein
|
A0A965TAA9 | MHPAILLQAETPRSRSMISEKVVKAVNDQINMEYYSAFLYLGMSNEMDAKGYRGYGKWLFLQYKEEMEHAEKFIGFLQTRGAEPVLSTINAPGKVPSVPLDVAKAAYEHEMKVSASIDKIYELANKEGDHASASFLKWFIDEQVEEEENTRNIIDMFGAAGKDVNALFAIDHHLGKREDE | Function: Iron-storage protein.
Catalytic Activity: 4 Fe(2+) + 6 H2O + O2 = 12 H(+) + 4 iron(III) oxide-hydroxide
EC: 1.16.3.2
Subcellular Location: Cytoplasm
Sequence Length: 180
Sequence Mass (Da): 20394
|
A0A3M2DZI3 | MRTALTLVSKELGPDAAILSSGAVAGGVEIVAAIDYDEALLAARRQKNDAQPTSQHHPGALDNASEQEAEREKTKSLDERASTKPLVSPDSAMDRLAEQSPWQNKTDSPSRQRTRSVSSGTSAKETQWLEDPSLARLRESLTEEMQALRHLLETQMADFGWQRRAKQTPVYCEMMRRLVNLGLPVSLANHFASQVHSEEIGDAWYKVAALAAKAISITDKDLVQQQGVYALVGPTGVGKTTTLAKLAARGVLQFGPDAVALITTDGFRIGAHEQLQIYAQLLGVECFITQDAAELNQILERLLDKKLVLIDTAGVAHRDE... | Function: Necessary for flagellar biosynthesis. May be involved in translocation of the flagellum.
Subcellular Location: Cell membrane
Sequence Length: 444
Sequence Mass (Da): 48616
Location Topology: Peripheral membrane protein
|
A0A1F5DRC9 | MGFWFPVEEVDEGTARLLVPTIDRGKGEPLDHARSRAAVFYNPLMRLNRDTAVLAVSLRGDHLGRTVEACEPMCGCGVRGIRLALEAGAVRVLMGDLNPSGVQISEENVRRNGVSDRVRVRFMDANLMLNLHSSPRNRLDYVDIDPFGSPSELLDSALRATRDGGLIALTATDMAPLCGVSPSACLRKYGGKPLRTAYTHEVALRLVIGAAVRAAAVHETGIKPLFGYYADHYVRVYLSLRHSAKPADAALAEMGYIVHCQRCLYREAVKGAYLKASRTCPVCSSQLTVGGPMWLGDFADNSFAGGMLEKAVKIRGWEPR... | Function: Dimethylates a single guanine residue at position 26 of a number of tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.
EC: 2.1.1.216
Catalytic Activity: guanosine(26) in tRNA + 2 S-adenosyl-L-methionine = 2 H(+) + N(2)-dimethylguanosine(26) in tRNA + 2 S-adenosyl-L-homocysteine
Sequence Length... |
A0A2D5ZUR8 | MKIYTKTGDEGKTSLVNGERVSKTHKRLAAYGAVDELNSRLGLLILSLQQNALLEDLSPTLVEIQNQLFNLGSHWACPPSDWVQKLPAIKAENISSLEAQMDQWNTELPALREFILPGGSEPAAHAHLARTQCRLAERLALEIEDLADEQKGGLVFLNRLSDYFFVLARYINLRLGRPEQTWQK | 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... |
A0A525C937 | MAEEPLIEHQRDLQEMLNQIQFLMERQKLVSQLLKKQKGSNELLQTLLEKQQNTELQQYLRRLHPADIAYVLESLPMAKREEVWRSVDKNSYGEILLELSDAVRERIIPFIQNDDIAQIARKLDSDEIADLFPDLPSDIANDLMDSLQQEERQQVHSALSFPDGSVGALMDFEMITVKEDNSLGDVIDILRKRGEMPSQSNMLFVVGVNKELIGGLEINELLINDSKLLVCDVISQGIPTFHTNDEAKEAAQAFERYDLISAPVINAHNHLVGCLHIDAVVDFINESSQREILSKSGLSEEEDLFAPVLQSGKNRWPWLG... | Function: Acts as a magnesium transporter.
Subcellular Location: Cell membrane
Sequence Length: 482
Sequence Mass (Da): 53728
Location Topology: Multi-pass membrane protein
|
A0A849WWG1 | MKEAILVINAGSSSIKFSVFFNEEGELNLQSRGQIDGIGVSPKFIVKDDSNKILESKEWMNEKAINHEFLLKFLIDWLNQNLKGAKVKVAGHRVVHGGSDFTKSVLVTDEIIFKLEKLIPLAPLHQPHNLAAIKALKKVYPDLAQIACFDTSFHTTNPDVLRHFFIPRELEKEGVKKYGFHGLSYEYIANTLKESYPDIANKKVVIAHLGSGSSMCVINKGFSVFTSMGLTALEGLPMGTRPGNLDSGVILYLMREKKMTADQIESFLYKKSGLLGLSEISNDMRVLEESSDPKAKETIEAFSWRICQMVGSLAATVGGI... | Cofactor: Mg(2+). Can also accept Mn(2+).
Pathway: Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis; acetyl-CoA from acetate: step 1/2.
Function: Catalyzes the formation of acetyl phosphate from acetate and ATP. Can also catalyze the reverse reaction.
EC: 2.7.2.1
Subcellular Location: Cytoplasm
Catalytic Ac... |
A0A6L7N0Z4 | MKPSAKTSRNAVAADHGALLRSGAGFIDVRAPVEFAKGALPSAVNLPILNDSERAAVGTRYRQRGQQAAVALGEELVSGDVRATRIEAWAAFAHSHPQCTLYCARGGLRSRIAQAWLAEAGTSVPRVEGGFKSLRQFCLRTIDEAAASLKLIVVGGRTGSGKTAVLAHAPASIDLERLANHRGSAFGEQPSPQPPPVGFENALAVEMLRLSAPGTTVALEDESRQIGRLAVPATLYQAMQAAPIVVIEASLETRVENILTEYVLEAPNPHEHLPASFARIRKRLGGTRHQEIGELLTNALSQGDPDLHRQWIRRLLTDYY... | Function: Involved in the post-transcriptional modification of the uridine at the wobble position (U34) of tRNA(Lys), tRNA(Glu) and tRNA(Gln). Catalyzes the conversion of 2-thiouridine (S2U-RNA) to 2-selenouridine (Se2U-RNA). Acts in a two-step process involving geranylation of 2-thiouridine (S2U) to S-geranyl-2-thiour... |
A0A938TRD0 | MNQFLVLRLANPVSWLIAGGDGGRPGPVVTGEFADAVPVARERQVVVIAPGSSVTLAQPELPVKGGAKLAQVVPYAMEDSLAGEVEQFHFAIGAADTGQSTLIAAVRREELRGWLEALEAAGVEPMSVVPDTLCVPDNPGKTVAVIDSGQLLVRAPGSLPVALDAEPLTEAFTLAGLEGEDRHVQLFVSQQDWQYSREMIEALREVTGSLDLQILPDGALPLLAAGAVRPGTLSLLQGEFARRTGWRAEWQRWRVAALLAAAAIALFIGVRGYDLVRLHAEQGRLDIAIEQAARIAMPDVERIEDARIQVEQRLRGAGAN... | Function: Inner membrane component of the type II secretion system required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm.
Subcellular Location: Cell inner membrane
Sequence Length: 404
Sequence Mass (Da): 42781
Location Topology: Single-pass membrane protei... |
A0A938TT00 | MNIKCYGIGTDLVEINRIEQLLMRHPKRFIEKILTPKEQIAFSKAPYPARWLAKRWAAKEAVAKALGVGIGAQCYFKDIEISKTPLGQPIAQYHGSLSQTNSNQNFTIHLSLTDEKLWALAYCVIFMESQAEVDYPRI | Function: Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.
Catalytic Activity: apo-[ACP] + CoA = adenosine 3',5'-bisphosphate + H(+) + holo-[ACP]
EC: 2.7.8.7
Subcellular Location: Cytoplasm
Sequence Length: 138
Sequence Mass (Da): 15699
|
A0A962GW08 | MSPDHASARQWASSLAPDAPVADPQLRGSGTPHSAGSEPPECASLAQILDTRNHRPMLRLQALQIIEGVCRSLDHTHRNGSAHGDIQPAKILVTAEGHVRLIDHGTTPTPAYASCEVLEGETPAAADDLFSAACTGYQLLAGEPAFGGRTALQAEAAAQRPVRIPNLSPGQWRALDRALAFRRAERQPDVETFLNELRSQYPGQAEVEATASVPALPIAHQAENRSLRRPVLAAGVAGIVVISIAIGWWWLRAPEVPASAAPTVSATGPGTGGLIIRGEESAPVTSVAPPSLTADTPTAPTTAPLSVPVARPDAASSPRP... | Function: Interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates. It could act to transduce energy from the cytoplasmic membrane to specific energy-requiring processes in the outer membrane, resulting in the rele... |
A0A6L7SUP9 | MSNDAMTESSITGLVLAGGQARRMGGVDKGLIDIDGQTIVERITRKLKAQCADVVINANRNLEQYRQFGYAVIEDQIEGFQGPLAGMLSVLKSIRTEWLITAPCDGPFLSSTYAESMFQAAWSIGAPIAVAKDQERLQPVYMLLHISTRDSLEAFLNSGERKIDKWFSGFRFAEVLITDCDDMFENINTPEQLEACRKKLSGGQSGY | 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... |
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