ids
stringlengths 6
10
| seqs
stringlengths 16
1.02k
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stringlengths 117
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A0A532UBW9 | MSYKRLMLLVVMMGLLMGGLMVLSTDSASCKSSAAVQGERLEEPIAVLETSMGVIKIKLFAPKTPQTVGNFIKLANEGFYDGTTFHRVIPDFVIQGGDPNSKDDDPDNDGMGGPGYTFADEFHPELFHNKEGILSMANSGPDTNGSQFFITLKPLQYLDNRHTVFGEVTEGMDVVKKISLVDRDERDRPITNVVVNKVAIIEYKE | 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: 205
Sequence Mass (Da): 22594
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A0A968LBM9 | MRFWKSILIAGCLVSVVGLGYAKMVVQSDPFSRLFEGNKVFVGGKPSPEDFSLERRMELAKGQHPLATVLTCSDSRVVPEFIFDKGLGDIFVVRVAGNVVEPTTLGSIEYAVEHLHTPLLVIMGHSQCGAVKATLETNGKPEGNIGAILKKIMPAVKTAKRAHKGPDETLDIAVHENIRNTYNDIMKNSKIIRHLVDEGKLQVMGAEYYLASGKAEPIDLAGPWKTHKHE | Function: Reversible hydration of carbon dioxide.
EC: 4.2.1.1
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Length: 230
Sequence Mass (Da): 25199
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A0A521SIC9 | MKKKKKSRPLRIFLGLFLLILSFSAIYIVYLDYQVIKKFEGQRWKLPSKIYSAPLVLSQGLDIEKSALITRLKRLNYHPVKRPVRKPGEYYLTEGNLEIHLRDFAYPDRLQQGIPVSLSFSSGKRIDRLVDLSLAEDLERIPIEPEVIGGFYEGTWEERTLIRLSEAPPILIDAIIAMEDRRFYEHRGIDPRGILRATWANLRAGGIVQGGSTLTQQLVKNFYLDSDRTLNRKVNEAIMALLLERHYKKEEILETYLNEIYLGQNGIMGIYGIGQGSWFYFGKPPSEMTIGESALLAGVIRSPNTLSPQKNLKKAIQRRNLVLERLFSEQKITLLQYVQARAETVSGRRVRERLNVAPYFVDEVRQRLAAAFPGDLLNSGGLRVFTALDVELQRIAEEKLRNGLQMLERQYPHLKRVEPERQLQGALVAIDPRTGEVRALVGGRDYGTTQFNRVTQARRQPGSLFKPFVYLAAFDQAANGKEPYTPLSQVEDAPITLQAGGRDWTPQNYDRTYLGPVTLRAALERSLNAATVRLSQEVGIEKIITTARGLGVTSPLKDLPSLALGTSEVSPLEMGVAYATLASQGIRHEPLFVSGVIDPANLRLDSSDSEGLPPSETISPQAAFLVTHLMEGVIESGTGQGVRKLGFDRPAAGKTGTTSDERDAWFAGYTPELVTIVWVGFDQNDPVELTGAQAALPIWTAFMKEALAATPPTEFTPPTGIVFKRVNENGKICRDGKEEAFIEGTEPTQSCEGGIFKWFEHLFF | Function: Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross-linking of the peptide subunits).
EC: 2.4.1.129
Catalytic Activity: [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+)
Sequence Length: 764
Sequence Mass (Da): 85465
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A0A521SKP2 | MSDLKPITGQTKLFGIFGHPVAHTLSPFMHNAAFDAVGLPYRYVPFEVPPDRLEGAVKGILPLGIRGVNVTIPHKEAILPFLDQVDEEAKMIGAVNTVEVISGRLIGHNTDGRGFLESLFEMKVALSGKRVILLGAGGAARAVAAVLAQQSIAEMVIVARTAARGKALADRLAAISPGLKVSLWGADWGSPLPADPDRSTLLINTTPLGMKQEDPLPFPIHLIDSRWSVADLIYRPAETALLAAAKRAGAQVIPGLGMLLHQGVLAFEIWTGQKAPLSVMRQALQNALSFQDFRSR | 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-dehydroshikimate (DHSA) to yield shikimate (SA).
EC: 1.1.1.25
Catalytic Activity: NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH
Sequence Length: 296
Sequence Mass (Da): 31681
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A0A4P0TK88 | MLFDGPHLTGLIDFYNACSGWMLYDLAIALNDWCSTADGSLDPARARALLGAYANRRPFTALEAEHWPALLRVACVRFWLSRLIAAEAFAGQDVLIHDPTEFQMRLAQRQKVEIHLPFAL | Pathway: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 4/5.
EC: 2.7.1.39
Catalytic Activity: ATP + L-homoserine = ADP + H(+) + O-phospho-L-homoserine
Sequence Length: 120
Sequence Mass (Da): 13517
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A0A1X6MEF9 | MVKLDRQNRKWYITQILGTLHLNKNDAFRQLFLELHPTDQVDILLNLSKEERKKIYRHLSPDEVANMFKQAEIDEQVRLFAELPSDYAVEVINNMYADDVADFLDALPQEVRQAYLQKMNTESAIEVQHLLTYPKHTVGSLMTTEFLSVWDEHTVQQVMEFLRTEAPNAETIYYLYVVDEKNRLVGVISLRDLIIAQPEQKVKNIMNTNVIFVDAHSHRKEVAEIIQKYDFLALPVTEQGKLVGIVTFDDVMDALEERETESFHKMGTATTISKSLKEATIGYLYRKRISWLVLLVFFNIFSGAGIAFFEDTIAQNIALVFFLPLLVDSGGNAGSQSATLMIRALATGDIRIRDWAKLFVKEISIAALLGVTMALAVSLIGLYRGGIEIAIVVSLSMFCVVIVGSLIGMSLPFIFSRFKLDPATASAPLITSLADMIGVVIYFSIATLLLTM | Function: Acts as a magnesium transporter.
Subcellular Location: Cell membrane
Sequence Length: 452
Sequence Mass (Da): 50930
Location Topology: Multi-pass membrane protein
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A0A4Y6UCT2 | MVLCGAVLALAMPPLCLWPVAFLMLPLLWRAACQAPSWRQAGWFGFCFGMGFYTTSLYWLTNAIMTRLHDFWWVLPFASPGVAVLIAPLVAVPAIMARWPAWESQQRGDAPCPPWRSALLFAAGWTLQDMARTFIFSGFPWNPLGSAFEVPGRVGTILIQPASLVGVDGLTFMLVAFALLFWCGWRWRLALLALALLWVGWGWWRCSHTVSLAVVQPHLVLVQGDVPEEEVLNRSARQLERARQFERYLDLTRQGVQQGVAVPGPHQGGRGGNLVVVWPESAFPGLLDEEPEARSLMSQAAMGHPVLAGSLRRDDKGHWFNSLEAVGQGGTLEALYDKSRLVPFGEYQPWIIPFNLTPAVLTPGPGLQTWNLPEAGKLGPMVCYEVIFSGSVTEPGHRPDWLLTISNDAWYGNSAGPRQHLATGRMRAVEEGLAVAFANNRGPSALYSATGALVGWLPWGHDGVMVKAIPQPLSPTLFSWGGRLLPLALALLACLVALWPWPRLQHGGHT | Pathway: Protein modification; lipoprotein biosynthesis (N-acyl transfer).
Function: Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation.
Catalytic Activity: a glycerophospholipid + N-terminal S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein] = a 2-acyl-sn-glycero-3-phospholipid + H(+) + N-acyl-S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein]
EC: 2.3.1.269
Subcellular Location: Cell membrane
Sequence Length: 510
Sequence Mass (Da): 56038
Location Topology: Multi-pass membrane protein
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A0A0Q5CSQ2 | MSIEIIKHSLSEAQIGLDNLLRNDTVLSNLDRSATMLAESFKSDGKAMSCGNGGSMCDAIHFAEELSGRFRKNRKALAALSISDPAHITCVANDYGYDFVFSRFIEAHGRSGDCLIAISTSGTSPSVLNAVDSAKRLGVFVIGLTGREGSPLDQLADISLCTPAGSFADRVQELHIKMLHIMIELVEHKLKLA | 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-phosphate in D-glycero-D-manno-heptose 7-phosphate.
EC: 5.3.1.28
Subcellular Location: Cytoplasm
Catalytic Activity: 2 D-sedoheptulose 7-phosphate = D-glycero-alpha-D-manno-heptose 7-phosphate + D-glycero-beta-D-manno-heptose 7-phosphate
Sequence Length: 193
Sequence Mass (Da): 20768
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A0A9D6QWB3 | MPNIKLVIEYDGSRYHGWQRQPGLPTVQGALEAAVATIAQQRPTVIGAGRTDAGVHAQGQVANFKINARLTSAAWMRALNSLLPEDIVIVSAQKVSSRFHSRFSAVGKIYRYRILNRRYPPAIGRQYVWTVYSALDIRRMKSAAQVLLGKHDFSSFKGANPSEDRTKGKKRSAVCHLRRLDLVKRYDDLVITIEADRFLQQMVRTIVGTLVEVGRGRRGPREMSILLQKKDRRFSGPTAPAQGLCLVEVKY | Function: Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
EC: 5.4.99.12
Catalytic Activity: uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA
Sequence Length: 251
Sequence Mass (Da): 28187
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A0A5N8YC48 | MESLTRKVIAEKVKGLYVIVDAQVADGRDLVDLTRSALRGGAQVIQLRDKVHDKGDVLPMARRIRGLCDEYGALFIINDHADLAVACAAQGLHLGQHDLPIWEARAILHPSQIIGRSNALLEEALESENQGADYIAVGAIFPTYTKVKTRPAGLETLERVKALVSAPVVAIGGITQGNVRRVVLAGADAVCVISAVIRESNPEEAARRLVDAMNSGDLR | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)-thiazole: step 1/1.
Function: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).
EC: 2.5.1.3
Catalytic Activity: 2-(2-carboxy-4-methylthiazol-5-yl)ethyl phosphate + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 2 H(+) = CO2 + diphosphate + thiamine phosphate
Sequence Length: 219
Sequence Mass (Da): 23515
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E6M2T6 | MSLKIYPSVLNCDQMHFAKALQDIKSADGVHLDIMDNHFVPNLTWGLPTATAVLNSTRLPVDAHLMIENPDRWSLEYAKAGCAIVCFHLEASRAPIRTADVLHSLGAKVGIALNPATPASAIKDILGRFDQVTVMSVEPGFGGQKFIPEVLPKIRQLRAYAEDARLPLDIEVDGGINDDTLPLVLQAGANVVVAGSYVFKRNPEQAIATLRTIGATDHTH | Cofactor: Binds 1 divalent metal cation per subunit.
Pathway: Carbohydrate degradation.
Function: Catalyzes the reversible epimerization of D-ribulose 5-phosphate to D-xylulose 5-phosphate.
EC: 5.1.3.1
Catalytic Activity: D-ribulose 5-phosphate = D-xylulose 5-phosphate
Sequence Length: 220
Sequence Mass (Da): 23824
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A0A7V0IW39 | MTYKPYTEDNLLPLSALQHLLFCERQCALIHIEQAWSENLFTAEGRIMHDRVDTAKHETRRNVRTEFGMPLRSLRLGLIGKADAVEFHKRGNMWHPFPVEHKRGKPKHDNCDKVQLCAQAVCLEEMMNVEIDSGALFYGKTRRRQDVEFDRDLRIETEETSKKLHQHP | Cofactor: Mg(2+) or Mn(2+) required for ssDNA cleavage activity.
Function: CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA).
EC: 3.1.12.1
Sequence Length: 168
Sequence Mass (Da): 19724
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A0A933SLP8 | KFLGIDEPFLYRLVGIVVDLMKVAYPELADTHNYVSRVVLSEEERFIDTLDHGLRMVNEIINKLKAEKQNVISGKDLFRLYDTYGFPLDLAGDIAGEHGFGLDEDGFYSEMNEQKERARRSWLGAEEAKAATVYKEALGNIKSTEFVGYDRLEEDAAVLAIIKNGKIADKAQEGDEAEIVLDKTPFYAESGGQTGDIGTITKKDMKIEVYDVVKPLPLIFVHKGRIQRGGIKIGDRALAKVDISGRTSAARNHTATHILHSVLKYVLGDHVKQAGSFVARDRLRFDFTHFSSISKRDLDRIEELVNERIRQNKGVSVAVMPIDDAVASGATALFGEKYGEKVRVVQVGDFSKELCGGTHCTASGDIGLFKIVSESSVAAGIRRIEALTGEEAYKYVKGQEDTIRYLGETLKTAPSDIAAKVEKLNLLLREREKELEKLKGKLSTSQAGDILSETKMINGIKVLSKKIDQLDMKGLRSLGDSLREKLKTGIIALGSSMDDKVSIVVMVTKDLIEKYSAVEIIKEISDIVGGSGGGRADMAQAGGREAARLNEAMEKVYKVVEKIGAGQVSKTAVE | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.
EC: 6.1.1.7
Catalytic Activity: ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala)
Subcellular Location: Cytoplasm
Sequence Length: 574
Domain: Consists of three domains; the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs.
Sequence Mass (Da): 62998
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A0A7E4ZSY1 | MDDQVLATTVMQLYNNMLFPIDDPDWFTFLSNEMQQPYFEKILNSLAQELVEDKKFYPNSTEIFKAFAATPLSKVKVVIIGQDPYPTPDKATGLAFAVPPNLHDIPASLSNIFKSIGRDEEISNVFATGDLTSWAEQGVFLLNTHLTVPANNSLGHSSLGWKTFTDNTVQFIVKNRPKAVFLLMGNNAQIKSKFIPPSRIIQCAHPSPHSAPKFFESTPFIDVNTALMAAGLDTIRWNSVFQATHHA | 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 Location: Mitochondrion
Sequence Length: 247
Sequence Mass (Da): 27516
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A0A520KMP8 | MTHKIPAKEIIKQIKKHDPKVTSLQTPEGLKRKTHKLARKIEEKTDTTVFISGNPCYGACDIEDRELSRVDVDLIIHLGHTEIPIETETPVLYFEIPMELEIDKLVQKAVEKIGNSKVGLLTTAQHHSAIPTIKQKLQKEDIQTVVGEGDRSIKHPGQVLGCNFTAAEIPVDKYLFVGTGNFHPMGIAYSTGKPVLILDPEMNQLREIQDADKFIKKRYAAIAKAQDADKFGVLLCTKPGQLRKNLAIKTKERLAESGLESTIITIDEVTPERLLQLDYDAYVNTGCPRITYDDQTRYRKPILSPTEAKIITGDSQELEYDEIRRK | Pathway: Protein modification; peptidyl-diphthamide biosynthesis.
Function: Catalyzes the first step of diphthamide biosynthesis, i.e. the transfer of the 3-amino-3-carboxypropyl group from S-adenosyl-L-methionine (SAM) to the C2 position of the imidazole ring of the target histidine residue in translation elongation factor 2 (EF-2).
EC: 2.5.1.108
Catalytic Activity: L-histidyl-[translation elongation factor 2] + S-adenosyl-L-methionine = 2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + H(+) + S-methyl-5'-thioadenosine
Sequence Length: 326
Sequence Mass (Da): 36724
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A0A2H0QYG4 | MIKKEDVLKLAQLARIETSEKEAEELAGDLDHILEYVSQVNSLDLSDEKEQTGPIFNVMRDDAHPHESGVHTEELLSASPAREGDYFKVKKIL | 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 activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
EC: 6.3.5.-
Catalytic Activity: ATP + H2O + L-aspartyl-tRNA(Asn) + L-glutamine = ADP + 2 H(+) + L-asparaginyl-tRNA(Asn) + L-glutamate + phosphate
Sequence Length: 93
Sequence Mass (Da): 10491
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E4NEE8 | MRWSQLYVPTLREDPADADAASHRLLVRAGYVRQLAAGHYSLLPLAARVRARIVAVVREEMERIGAQEFLLPALHPAELWRRTGRWESMGEEMFRLTDRKGAEQALGMTHEEVFAHLAEELRSYRQLPQTWYQFQTKFRDEARPRSGLLRVREFTMKDSYSFDLDEAGMARSFEAHRLAYLRIFERLGLPAFGVRASSGAMGGSGSVEFMSPSAAGEDLVVRCPGCGYAANTEKALSALPAVADPAERTERTGPAEQTERTDRSDQAGTFAVEEFATPGARGIEELAERHGIAPERQLKTLVQVVDGALTLVLLRGDHALVEQKLLDALGASAARPATAEEIAAALGASPGSLGPLGGHGLPVLADEALRGRTGLTCGANRDGFHLRGVSIGRDVRVTRWADLREVTAGEPCAECGAALEVLRTIEVGHIFQLGRRYTEALGVAVAGPAGERVVPLMGSYGIGVERLLAALVEAHHDERGIRWPAAVAPFDLVLTVLPDRGGAVAEAAERLCGELGAAGVRVLLDDRAERPGVKFADAELIGVPWRLTLGARGLAAGTAELTARADGSTRELGLDAAVPELRALAG | Function: Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Ala-tRNA(Pro). The misacylated Cys-tRNA(Pro) is not edited by ProRS.
Catalytic Activity: ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro)
EC: 6.1.1.15
Subcellular Location: Cytoplasm
Sequence Length: 586
Domain: Consists of three domains: the N-terminal catalytic domain, the editing domain and the C-terminal anticodon-binding domain.
Sequence Mass (Da): 62966
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A0A1A0JU32 | MSVGHVGTAIARSLELHDVPRIFQVPGESFLPVLDGLYESSIDTIVCRQEGGACYMAEAHGKATGQPGVAMVTRGPGAANAFVGIHTAWQDATPLVLFVGLVPTNDRDRESFQEFDIKAWFGTQAKRVYVLDDASRASRVVAEAFHLATQGRPGPVVIGLPEDVLHQEFTGDLCNPLPASPGAFSDANLDYLASELRTAEKPLIFAGGAHWTPETSAAVQKFAEQQQIPVVHDWRASDRTAFSSPANAGWLGYGRNDAAAELLCEADLVVELGAVLTDVPTDGYTLRQNLDAKNIVITTDTTLLGNSAAVSHHILASPQAFAQVTEELAKRIGSEERVTAGSEASTGTSDSTDAAITATQREWFTAAHRKHLAFSHVGKPEDWPATAKGTAHMAAIMAAIQEQAPHDALYTFGAGNHCLWAQRYLRTETYPSQLSVRNGSMGYSIPSAVAASLQFPERTVITIAGDGEYLMNGQELATAVQAGGAFLVVVMSNAEFGTIRTHQLNHYPKRVSGTQLANPDFAAAAVAFGAHGETVTSDQDATSAVKRALAAVREGKPALINVITDQALSIPTIRQNTEE | 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: 579
Sequence Mass (Da): 61664
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A0A7X0LQU5 | MSAVSRVFVLNGPNLGRLGSREPDVYGATSYAGLVQACQELGKELGFDVEVRETNDEGELIRWLHEAADGSIPVVLNPGAFTHYSYGMRDAAAQRTAPLIEVHISNPYTREEFRHTSVVAAVASGTIAGFGIGSYLLALRALAEERDA | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.
Function: Catalyzes a trans-dehydration via an enolate intermediate.
EC: 4.2.1.10
Catalytic Activity: 3-dehydroquinate = 3-dehydroshikimate + H2O
Sequence Length: 148
Sequence Mass (Da): 15923
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A0A7V4X6W8 | MNFIDKYGIRRIVREALKEDQVSRDITTRLIIPRNLKKEALIVAKESGIICGMDIARMVFKCVDNKIKFKALVKDGRGVKKGDVLAKLYGSVSSILSGERVALNFLGMLSGISTRANQFARKANPYKVKILDTRKTIPGLRALEKYAVRIGGGFNHRFSLADMVLIKENHLQIAKTKDIKETISNIRERLPTGVRIEVETRNLNEFKKVLLAGPDVIMLDNMSPEHIKEAVRLKKNSSIKIKRNLKLEASGNIDFKNIVAYCRTGIDFISLGTLTKDIKSLDVSLDIE | 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: 288
Sequence Mass (Da): 32368
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A0A7C1H6Y8 | MPKEKQKLTKDKDFERVFKSGRAAYAPFLLLKYLKNKIGITRFGIIVSAKVSKKAVLRNLAKRRIREILRLNKEKIKKGFDIIIVVSPKIISQSGEILKYQEIEKTLLNLLKKADLL | 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 the ribozyme.
EC: 3.1.26.5
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Length: 117
Sequence Mass (Da): 13538
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A0A433TCL2 | MTSQTYRVAVIGAGASGLTAIKCCLDEGLTPVCFERSDHIGGLWQYKEERRDDQPCVMKSTVINTSKELLTYSDFPLPAHFSNCMHNSQLVEYFHLYSDHFGLKKHIQFNTQVVSVTKTDDHSTTGRWNVLHRDATTGSERSEVFDAVMACNGYQTFPHVPQLEGLQQFQGKVLHTNDYRTAAGFENKRVLVVGFGNSAGDCAVDVCRVARQVFMSTRGGSWVIKRLNNNGYPMDVTTITRFRLFLQTKCRRPWEKYCEWKLNSHYNHAMYRLKPAHSLFSSQPMINDDLPNRMLTGAIKVRDDVKRFTKTGVEFVDGSYEDLDAVILATGYTTDFPFLRQDILWRENKKVPLYKLLFPPDLEKDTLVVVGCMQPWGSLMPMAEMQSRVATRVFKGLVTLPDRATRWREIDQRYAAVARNAIPTQRYSVMVNQMFYMDELSAIIGCRPDFVALMKQDPIFAIKLWFGPVYPYSYRMFGPGQWAGAREAIDTAMDRVRAPFRTRALPEASAASQPPYWKSLWMYVIILIAAVLVFVLL | Catalytic Activity: H(+) + N,N-dimethylaniline + NADPH + O2 = H2O + N,N-dimethylaniline N-oxide + NADP(+)
EC: 1.-.-.-
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 537
Sequence Mass (Da): 61397
Location Topology: Single-pass membrane protein
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A0A7V8AUR3 | MSSEKFDKQLPLLAVDVGNTSIALGLFLNLTDARLLKTAKIASHPALPASEMKQKFHRFLGRRIARTGVYIVIGSVVPPLAKRLAAATSSVSRLTLSVNARCDFGFQLAVDTPAALGVDRIANAAAAWTLRKRPVAVADFGSATTVSIMDGEAFRGGAILPGVVMMRDALSYRTARLPSASLEADVSAVATHTDAAIRSGIVLGTAGAVEKLISTAERELRLKLSLFVTGGNASLVIPFLSRRHVFAPDLTLQGFRIIFLRRLDLSL | Cofactor: A monovalent cation. Ammonium or potassium.
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5.
Function: Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
EC: 2.7.1.33
Subcellular Location: Cytoplasm
Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+)
Sequence Length: 267
Sequence Mass (Da): 28449
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A0A7Y8HTP3 | MVYKQDGKVALITGGTKGIGKAIALSLADYGAKVIVNYISDAETAEQTRKEIEKINGFALAFRADVSNYEEVQEMIDSIINKTGKLDILINNAGITRDSLLFSMKDDDWKKVIDINLTGVYNCCKAALRPMIAGHWGRIVNIISPSALLGRKGQTNYSASKGGILSFTRSLAREVARLGITVNAISPGVIETDLTKNLDAKVRDDLLNMIPLRRFGTPEEIAQAVSYLVSEKAGYITGTYISIDGGLT | Pathway: Lipid metabolism; fatty acid biosynthesis.
Function: Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP substrates to beta-hydroxyacyl-ACP products, the first reductive step in the elongation cycle of fatty acid biosynthesis.
EC: 1.1.1.100
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] + NADP(+) = a 3-oxoacyl-[ACP] + H(+) + NADPH
Sequence Length: 248
Sequence Mass (Da): 26879
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A0A1B2HPX7 | MTPVFIALEGIDGSGKSSTAAAVAARLRRRADVVRLVRHNAVEPDDPFVAEYLDGLRALQQMSLRGPYFRLGDPHWVLIRASYYALVDRCVITPALERGHVVVADGWFHKFVARIAAGGVRARGDFDRPDQILPLFAPVRRPDLVFLLDTPVATAAARRMATVNPGELGPQNAGTSSPEKAFVSYQSAVRGHLLSMAVAGRWHVVRTAARDVGSVAAEVCADLDVLREVG | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
EC: 2.7.4.9
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Length: 230
Sequence Mass (Da): 24918
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A0A3P7UQQ9 | MEIRNVEQAEKIANTKFDGTFSWSDNVDSILKEVFHLPSFRPLQREVINAVMSELDTLVVMSTGAGKSLCYQLPAIAMKGLVVVISPLISLIEDQLAGLQKLGVEGAALNQSTTKEDVKRIEAQLIQKGSSLRLLYITPEKLAKSKRLMNKLEKAAEVGTLKVFAIDEVHCCSQWGHDFRPDYKFLNILKRQFPNVPLLGLTATATANVLSDVKTMLDIPNAVVFKAGFNRLNLHYEVIQKPDSDFTAELARLIKSRFANQSGIVYCFSRKDCEEVATQLESGIRAAFYHADMESSRRTAVHEKWVSGKYNVIVATVAFGSSFTFESGRAGRDGLPAVCILYFRLSDVFRQSTMVCTERTGIRNLYAMVRYAITCRRKHLADHFEERWTSELCPKACDVCACHTEVADIDITDIVRAMLKIIREVCNSFQKSNDRGSNRITGAKLVELATKQRLGSKVSNDSEPLIKLPFYFLLFKLDRMSVVSSSFSGKVGYGLIFRISLQTIYNVVA | Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
EC: 3.6.4.12
Subcellular Location: Nucleus
Sequence Length: 509
Sequence Mass (Da): 57008
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A0A7V8YJQ8 | MAYDHCHRSRAPGRRSPRRARRARTAYFRGDGWPTQPTRGPARPEWRIDMNEQESGDPSAAAGQRPEVAVLAGGCFWGVEEILRVVPGVLDTDVGYTGGWHPNPTYDDTHESKSGHAEAIRVTFDPSVLSYEDLLERWFFKLHDPTTLNRQGNDVGTQYRSAIFPQTPEQRSAAERVKARVEASGKWKRPITTTIEPASTWHSAEGYHQDYLRKHPGGYSCHFMRE | Function: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.
EC: 1.8.4.11
Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionine = [thioredoxin]-dithiol + L-methionine (S)-S-oxide
Sequence Length: 226
Sequence Mass (Da): 25646
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A0A532UC13 | MPELPEVETILRQLERLIKGRKIKEVQVAVPRILYHLSPADFKKRLRGAVFTSFSRRGKFLLCHMNEGELVMLIHFRMTGSLLYGTPSAISKAHTRISFWLDNDKLLCYNDMRKLGKIELIKGELVDNFHELKSLGPDPLSPDFSPQLLYNILQGSRRQVKELLLDQHKIAGLGNIYASEVLFDCGIHPQKKAHSLSPEEVGGLHRSILKILHLAIESRGCSIANYVDLAGESGAFQELRNVYQREGEPCYRCGELICRIKQQQRSTYLCPRCQQ | Cofactor: Binds 1 zinc ion per subunit.
Function: Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates.
EC: 3.2.2.23
Catalytic Activity: 2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-monophospho-2'-deoxyribonucleoside-DNA + H(+)
Sequence Length: 275
Sequence Mass (Da): 31398
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A0A1J5WLQ8 | MLEFFLNLFGIGSIRRINKKQGVLQILNVFTMFTSAYMGWRLLGSVVNHYSPFVVVLSESMEPGFRRGDILFITMMSDPIECGDIVVFDTQKKQIPIVHRVMNVHAAKKTGKLFFLTKGDNNKGHDRPLYGGKKMWLHGENIQAKVKGYIPFLGNISLIIKEYPAVKTVLISTMCLLTLLTRE | Catalytic Activity: Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.
EC: 3.4.21.89
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 183
Sequence Mass (Da): 20783
Location Topology: Single-pass type II membrane protein
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A0A1G2P857 | MRLHRFYSENVLPAEGEIFRVENFELCHQWRKVFRYNVGSQVVMFDGNGFEALCQIEDFDHAAASLRVGQRRPNRNRPSREVHIFQSLIKKDNLEWVFQKGTELGVSYFHPLISDRSQKKSFNMERASKIVREASEQSGRAAPPNISEVLTMEEAMALTFPAVMAVLHGSGDRFSKFLETLAHCAIGVFIGPEGGWSDRELAWFEKSHIPSFSLGHQTLRAETAAVAVSTLLLL | 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
Subcellular Location: Cytoplasm
Sequence Length: 234
Sequence Mass (Da): 26541
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V5RIB1 | MNKYRVIFCGTPEIAVSILKGLETLNIEIVGVITQPDKLIGRKKELSFSPVKSYSIEKGYKLLQPAKVIDVYDEIVALNADYLITCAFGQFIPSKVLELFKNSINVHASLLPKYRGGSPIQYAIMKGEKKTGISLMKMIKKMDAGEVYVQEEIEIDSNDDSGILFNKMAILGKKMIEEHLFNILEGKIKGMEQDEKKVTFAYNLTNEQEKINWDDTSENICNFIRALSPKPIAFTFLGNERLRIKSARLLDENDIFPMPLKIFQPGEIASVNNKGIVVASNNGFIIILELQIAGKKMVVASSYNQPNSPFKMGLILG | 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 Activity: (6S)-10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) = (6S)-5,6,7,8-tetrahydrofolate + H(+) + N-formyl-L-methionyl-tRNA(fMet)
Sequence Length: 317
Sequence Mass (Da): 35507
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A0A7X8JRM4 | MIKIIPMKEEHIPGIHEIEKSCFTIPWSKEAFEKELRENPLAYYIVAELENTVLGYAGMWVIADEGHITNIAVHPDFQHQGVGTLLMEHLIDEARSKNFFGLTLEVRESNVKAQNLYKKFGFINEGLRKGYYQDTGENAIIMWKYFNN | 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: 148
Sequence Mass (Da): 17166
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A0A1H9GW10 | MPVDILPGDARNVLSRFEIEPAAGERLSVYVELLRKWQATHNLVSHSTLPEVWTRHVADSLQLVSDLPERGLWMDVGSGGGFPGLVLAVVAADKPDLRFVLVESNGKKCAFLRTVARETGARAEIVLGRIEDQAERFGGRADVVSARALAPLDDLCRLTKPLLTPKGALLAMKGQDFAAEEAEAARNWTYDLATRPSLIDPAGCVATLRHLQARTSPS | Function: Specifically methylates the N7 position of guanine in position 527 of 16S rRNA.
Catalytic Activity: guanosine(527) in 16S rRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(527) in 16S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.170
Subcellular Location: Cytoplasm
Sequence Length: 218
Sequence Mass (Da): 23658
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A0A6B2QXI6 | MSLMFTLLLVVQIISSLTIISLVLLQQGKGADMGSSFGSGSAGSLFGATGAANFMSRATKWAAVVFFISTIGLAYVANRGAGGQDTGLMSNFTQTQPAAPAPSGSLVPGSAPAGSASGSSAVPGATNAVPAVPGAPAAVPSAPVPAPSSGVPATK | Function: Involved in protein export. Participates in an early event of protein translocation.
Subcellular Location: Cell membrane
Sequence Length: 155
Sequence Mass (Da): 14878
Location Topology: Multi-pass membrane protein
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A0A973GR79 | MQKLLELVQRINSVQNIETITRTLATVSAAKLSWSRRRAAGLRVYTRKIENILYTQQAYRAGSGMRAGSLSPLLTERQAAHRVAVLVITADRGMCGSYNLAACRLALDFWTKAKKAGQNTLFLVKGRKGERYFRKRGAVIAYAEGWRREGVRSEEVEKLLSRLLDLFLSGTVDEVYTVYTQFYSPIRRLPKIKRLLPVTLELHGHGREATEKWYYEPSFREIIDELLDIHVRVQLYDVLLESYASEQGARMITMEEATERADKTLGECRILYNRLRRESITIDLLGVLFAAKVVEEVKSTPGELA | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex.
Subcellular Location: Cell membrane
Sequence Length: 305
Sequence Mass (Da): 34848
Location Topology: Peripheral membrane protein
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A0A1V5CFQ5 | MRHIISVLVENEFGVLARVAGLFSGRGFNIESLCVAETLDPEISSMTIVTTGSDAILEQILKQLNKLVNVIKVTDFQDADYVSREMVLVKVTADEKTREEILRMTEIFRGRVVDVSAKSYIVEITGNEEKVKAFLTLVKPLGIKELVRTGPVAMMRGEKIMRAREKAAPQRKEETLSDRKAEG | Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 1/4.
Function: Catalyzes the conversion of 2 pyruvate molecules into acetolactate in the first common step of the biosynthetic pathway of the branched-amino acids such as leucine, isoleucine, and valine.
EC: 2.2.1.6
Catalytic Activity: H(+) + 2 pyruvate = (2S)-2-acetolactate + CO2
Sequence Length: 183
Sequence Mass (Da): 20454
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A0A660ZIL9 | MRCFIAVDIPESVKRKIETNFSSVRKRAPDLKWVETKNIHITLKFLGEVNERKLPQIEDALRKIAASTPPFQIQIGSPGSFNAGGGIRVLWLGIQSGQDSLAHLAAKIEDAMHKVGFKRERREFKAHLTLARSRKHGPKIRFSQLGIPESKYPPFTVSEIILYKSTLTPQGPIYEKLKRFALKG | 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: 184
Sequence Mass (Da): 20802
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A0A328FB71 | MLDKNKKRAVYCPDPSFALGRHITIEYYDCASNVLLDKDGVESILLKAARESGATIISSSFHQFEPQGVSGVVIIAESHFTVHAWPEHNYAAVDIFTCADNIDLDTAIHSIEAQLSSQRVFISSDQNRGILQPGFGGCTPNSDEKVMDRRTLPIAWKKVCENAHPWGMSTSVDLYDCSPDKIKDPDAIKNFVGRVCGQLGIVDIENAPLVYYDETETAAGFSMKQSIETSGISGHFAHATNAAYLDIFSCNTYEPRELAEFSLSYFRGSHYKMQVALRQ | 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 in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl group blocking the N-terminus of the alpha chain.
Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Pathway: Amine and polyamine biosynthesis; S-adenosylmethioninamine biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine: step 1/1.
Function: Catalyzes the decarboxylation of S-adenosylmethionine to S-adenosylmethioninamine (dcAdoMet), the propylamine donor required for the synthesis of the polyamines spermine and spermidine from the diamine putrescine.
EC: 4.1.1.50
Catalytic Activity: H(+) + S-adenosyl-L-methionine = CO2 + S-adenosyl 3-(methylsulfanyl)propylamine
Sequence Length: 279
Sequence Mass (Da): 30902
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A0A521LCF4 | MIYTITLNPALDHYLEVDDLTVDDANRVKSECLYAGGKGIDVSRAIRHLGGDSMALGFIGGHNGQVLLDLLKREGVTTYFTPIAQETRRDIIVNNRKAGTQTMLNARGPTVTAEEWRSFLEHLRLLDLRDAYVVLGGSLPRGVALDAYYQIVRLVQRRGAKAVLDADGPCLKAGLKARPFAIKPNVKELQRVSGRPLRTEADILAAATALNRGGVNVVLVSRGRQGLLVVSGTRHRSPLLLRAVPPPVKVRSTVGAGDSTVAGFVFRHAGGKTVEDAVRYATAAGTAATLAPGNQLCRLIDVQRLVPRVKIEQLRSA | Function: Catalyzes the ATP-dependent phosphorylation of fructose-l-phosphate to fructose-l,6-bisphosphate.
EC: 2.7.1.56
Catalytic Activity: ATP + beta-D-fructose 1-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H(+)
Sequence Length: 317
Sequence Mass (Da): 34208
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A0A9D5JR72 | MLGIFDSGVGGLTVVRELLRRHPNAAFEYLGDTARTPYGTKGPETIQRYAVEDVQYLIEQGAHTIVVACNTVSAHAMEVLRTRFTAVRFIDVIEPAVRCVPAAAHVGIIGTSATIRSGVYERLIRERNPAAVVHSVACPLFVPLVEEGWFSGPVVERVVASYLHPLKELDIDTLILGCTHYPMLQSAIRSYLDPKVRMIDSPTAVLNAADLGFEPGRQRYAFTDLSETACTMIKRCNGKCLKPKQILLH | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Provides the (R)-glutamate required for cell wall biosynthesis.
EC: 5.1.1.3
Catalytic Activity: L-glutamate = D-glutamate
Sequence Length: 249
Sequence Mass (Da): 27417
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A0A9D5E9S6 | MSPAPPAPPVPPAPPDAHAASHPDEPGPITPIPLPERCAPPGGGLTLLMLGGTFDPPHMAHALLPLRASEAMGLGDHLLVFVPASRSPHKAAQPLAPADHRLAMLHRLIDDLSLRGRAVAWSDEIDRAAAAGPAAAPSYTAHTLARARRWLDGHGVPAAVMRLVIGADQALAFDRWRDPRAILAIAQPLVLPRGEPPERTLARMSAGGAWSGPEMLGWARGFAPIEPRTGSSTDIRALLAGAGPAGPGGLSPGVLEHIRVHGLYGAGGAGSAAGPQGRSH | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
EC: 2.7.7.18
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Length: 280
Sequence Mass (Da): 28776
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A0A662RD57 | MNKKSVEQPPGAVLVVGGGIGGVQTALDLAEQGFKVYLVERKIGIGGVMAQLDKTFPTNDCSICILSPKLVEAGRHRNIELITNAELQNLRGNAGNFQADIIVHPRYVDLDKCTACGDCAKECPVTRPDLFNENLGDRQAIYRLFEQATPSAFAIEKAGIPPCRAACPIHVNAQGYIALIRDGKFKEALALIREKNPFPGITGRICTHPCEDKCERAKLDEPVAIDSLKRFVADFESEPEWDLTCEPEKDKKVGIIGSG | Pathway: Cofactor metabolism; coenzyme M-coenzyme B heterodisulfide reduction; coenzyme B and coenzyme M from coenzyme M-coenzyme B heterodisulfide: step 1/1.
Function: Part of a complex that catalyzes the reversible reduction of CoM-S-S-CoB to the thiol-coenzymes H-S-CoM (coenzyme M) and H-S-CoB (coenzyme B).
EC: 1.8.-.-
Subcellular Location: Cytoplasm
Sequence Length: 259
Sequence Mass (Da): 28218
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A0A8B9Z474 | MQLNCVCENVVTSVRSELQPYLQTLPVTARIDDKAGIDYSLVAPPTATAQSLDVDLKVRGCPGKA | Function: The cytotoxic action of BPI is limited to many species of Gram-negative bacteria; this specificity may be explained by a strong affinity of the very basic N-terminal half for the negatively charged lipopolysaccharides that are unique to the Gram-negative bacterial outer envelope.
Subcellular Location: Secreted
Sequence Length: 65
Domain: The N- and C-terminal barrels adopt an identical fold despite having only 13% of conserved residues.
Sequence Mass (Da): 6961
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A0A520JSK6 | MKPVLLKIGGSVITDKRQECTFKMQNIKRIAGEIARASVPIVIVHGAGSFGHPQAKKYHIQQNPDTEGLAKTHRAVLELNTVFVETLEEEGVAATGVHPLDCLLAERGVVKRWEIEIIKKMVDFGVTPVIHGDVVMDTVNGISVISGDQILTYLAKKLDVTVIGAGTAVDGVLDKNGRTIPHITSSNFKEVSDYIIGSTDDDVTGGMRGKVLELLKLAEFGIESVIFNAELSNMVFKFLSGEVIKATRISGA | Function: Catalyzes the formation of isopentenyl diphosphate (IPP), the building block of all isoprenoids.
EC: 2.7.4.26
Catalytic Activity: ATP + isopentenyl phosphate = ADP + isopentenyl diphosphate
Sequence Length: 252
Sequence Mass (Da): 27207
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A0A1V4K7M8 | MNTPAAAGGEETGAAGGSGCRGAEGGGEPAGAAGVPEDPGLSAAEESLEEKLRNLTFRKQVSYRKAISRSGLQHLAPVHSVNIAVSNGPVKEPRAALEWTENAVNGEHLWLETNVSGDLCYLGEESCQVKFSKSALRRKCAACKIVVHNACMEQLEKINFRCKPTFREGGSRSPRENFVRHHWVHRRRQEGKCKQCGKGFQQKFSFHSKEIVAISCSWCKLAFHNKVTCFMLHHIEEPCSLGAHAAVIVPPTWIIKVKKPQVVSIPGDEPDWAGDWSPEGETGVSYPYWEGWQNSLKNSTRRKKRTSFKRKASKRGNEDNKGRPFVIKPISSPLMKPLLVFVNPKSGGNQGTKVLQMFMWYLNPRQVFDLSQEGPRDALELYRKVPNLRILACGGDGTVGWILSILDELQLSPPPPVAVLPLGTGNDLARTLNWGGGYTDEPVSKILCHVEDGTIVQLDRWNLQVERNPDLPQDELEDGARKLPLSVFNNYFSLGFDAHVTLEFHESREANPEKFNSRFRNKMFYAGAAFTDFLQRSSRDLSKHVKVVCDGTDLTPKIQELKFQCIVFLNIPRYCAGTMPWGNPGDHRDFEPQRHDDGYIEVIGFTMASLAALQVGGHGERLHQCREVTLLTYKSIPMQVDGEPCRLAPSLIRISLRNQANMVQKSKRRTSMPLLNDPHSIPDRLRIRVNKINLQEYEGLHYDKEKLREASIPLGIIVVRGDCDLETCRMYIDRLQEDLQSVTSTTQRVHYQDQESSFPRVLSVQRLSPRWCFLDATSADRFYRIDRSQEHLHFVTEISQDEIFILDPELVMSQQVGTPPGMPDLVVEQASGISDRWNPAVRKRMLSDSGLGKISPHYEVPDKQKDASQTHMLQSPVSSEDQALLQAVIAGDLLKFIECCKKGANLLIRGPDHCSLLHHAAKTGHGEIVKYILEHGPSELLDMTDSETGETALHKAACQRHRAICQLLVDAGASLRKTDSKGKTPRDRAQQAGDPDLAAYLDSRQNYQMVSHEDLETAV | Pathway: Lipid metabolism; glycerolipid metabolism.
EC: 2.7.1.107
Catalytic Activity: 1,2-di-(9Z-octadecenoyl)-sn-glycerol + ATP = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + ADP + H(+)
Sequence Length: 1019
Sequence Mass (Da): 114057
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A0A3D1CSC6 | MPLFLHNTLTRSADEFIPLVAGKAGLYVCGPTVYGRAHVGNLRSWIFSDTLRRVLQANDYTVTEVMNITDVGHLVGDGDEGVDKLQMAADKVSKTAWDVAVEFTKLFVEDIKRVNIEAPHVMPKATDHIAEQLALIEAMEAKGFIYAIGDGIYFDTAKLPEYGQLSRQKNEDKEEGARVVVNAEKRSPSDFALWKFSPAGEQRHMEWESPWGKGFPGWHLECSAMSEKYLGVPFDLHTGGVDHIAVHHENEIAQTLAARGVLEANYWLHNEFMLIDGGKMSKSLGNVYSLDDLDLKSISPLAFRYFVLGAHYRTQINFTWEGAKAAQNALNNLIDLARDWQKPSNADEVTMGKFMLAVNNDLDTPAALAVLWNFVNDNAVGSDVKAATVLKMDEVLGLALEDVVARPVRVTEAAQKLLDEREVARIAKDWERSDLLRDELFGLGYAVEDKATGQHLRERR | Cofactor: Binds 1 zinc ion per subunit.
Catalytic Activity: ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-cysteinyl-tRNA(Cys)
EC: 6.1.1.16
Subcellular Location: Cytoplasm
Sequence Length: 460
Sequence Mass (Da): 51329
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A0A1Y6K6U4 | MSPFYTSDGDQGETGYLGKGRISKSSLRIESVGSVDEANAAIGLARALCANPKSQMVLLEVQKHLYLLMTELSASPETAAQFDRLNQDHINWLEEQIEELEDAVVLPREFIIPGSSPASGAIDLARTIVRRAERRAVSLLEAELIKKQLLIAYLNRLSSLLFMVEVYEALNTGNDIQLAKET | 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 triphosphate
Sequence Length: 182
Sequence Mass (Da): 20091
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A0A931VKP6 | MENKNPVIAITMGDPSGIGPEIILKALEDVSIYEKCRPLVIGNENIFTRTALNLGKSVKISKIFDLSTLSSKPGHLTLLEPGTASVEFSPGRPTRSGGQAAGSYIEKAAELALSGTIDAITTAPINKETLRNAGYPFPGHTEFFASLSKTENFGMLLVGGPLRIVFVTIHEPISRVSSLITKERVLKTIRLAFHEMKNLFGLSHPVIGVASLNPHGGENGLFGKEELTQIIPAVEKARAEGIPVSPPISPDALFYKAYHKEYDAVVVMYHDQGLIPLKMIAFKESVNVTLGLPFIRTSVDHGTAYDIAGKGVADSSSLKEALLLAARLAGIKKNSEATGLAGDGLGNGRR | Cofactor: Binds 1 divalent metal cation per subunit.
Pathway: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 4/5.
Function: Catalyzes the NAD(P)-dependent oxidation of 4-(phosphooxy)-L-threonine (HTP) into 2-amino-3-oxo-4-(phosphooxy)butyric acid which spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate (AHAP).
EC: 1.1.1.262
Subcellular Location: Cytoplasm
Catalytic Activity: 4-(phosphooxy)-L-threonine + NAD(+) = 3-amino-2-oxopropyl phosphate + CO2 + NADH
Sequence Length: 350
Sequence Mass (Da): 37351
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A0A5N8YBX9 | MRSTSNLCAELVHAQQKGLDSLTPEVFAPQTCLFAQLGQIGYVEAWDTQRAIARRREHGSTPDSLLLLEHPHTYTLGRRGKVSDVLVGDLTLRQMDVQVCQVDRGGEVTYHGPGQLVVYPIVDVRPIGGAVTYVRTLEQILINTLKDFGLTGHREENLTGVWVAQEKIAAIGVKISRGITTHGLALNVSPNLSYFQHIVPCGLKGITVTSMERLLGYPVSLRKVALRLVHHFGLLFDRRMEEAGQAPSTGSEQILHAHLAGIAQA | 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-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
Catalytic Activity: L-lysyl-[protein] + octanoyl-[ACP] = H(+) + holo-[ACP] + N(6)-octanoyl-L-lysyl-[protein]
EC: 2.3.1.181
Subcellular Location: Cytoplasm
Sequence Length: 265
Sequence Mass (Da): 29038
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A0A9D6QUQ2 | MGVAFYNLVLILSLPLTLPVFVFLMITQSEYRTGLSERLGRWPGSWDRPEKIRTRIWVHAASVGECLAVLPLIERWLGDRPEWDVVFSTMTSAGRRLIEQRLGNRVRVGFFPMDFPGLAARLLRRVAPDLILLVETELWPNFLQSASQCDIPVLLVNGRISPRSYRRYQAVRWLFRETLRKIRIFGMQSVQDAQRIIELGAPPERVRVLGNLKFDQAAVPLSEPERRRLLKLLRWGSDEKILVAGSTHEKEEELLLTGFARIKQRWPNLRMILAPRHLNRLSIVTGVLTRHGISYVRYSELDRTTSETQVDVLLVDTLGQLGQLYSLGTVVFVGGSLVPVGGHNLLEPAALGRPVLFGPFVQHVQEMADLLLASSGGRMVRDIDELVREIQALLTESARRQAMEHRARKTVRLHQGASGRAFVMVEQQLKKRFFDRLPRLDFRGALERWFKERMLVSKGGVLTSFAAVGLRGASILYQGWQEVRAAAYSVGLLRSVRVPRSVISIGNLTLGGTGKTPTVMTVCRFLRAQGHRPVVLSRGYGGRIGKAVRVVSDSTGIDRGPDEVGDEPSLMADRVPGVPVVVSSDRVAAARYALEALPSDVLVLDDGYQHLRLKRDLNLLVVDAVDPFGNGYVFPRGTLRESVRQLCRADAVLLTHVGHPAETDELQKFIRRYRSDLPIFTSRHRIVELVPIGPGSSLPFENIKGMRLIAVTGIGQPDRFVRMLQAGGADAAAACLYPDHYRYRLEDLDEIEAEAKRWQAPAIVTTEKDAVRIKKLGRPMEAWWAARLELMIDHSEAFESMLSGVFQ | 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 tetraacyldisaccharide 1,4'-bis-phosphate (lipid IVA).
EC: 2.7.1.130
Catalytic Activity: a lipid A disaccharide + ATP = a lipid IVA + ADP + H(+)
Sequence Length: 807
Sequence Mass (Da): 90651
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A0A7E4UWX0 | MKFTNFQLAKQVLSKLHNAKRPIILGIETSCDDTAVAIVSADKQTLGQRVYVERTGQGQFGGINPAISASQHRGHLDRLIEEVLDEVQCRASDLDAVAVTTRPGLVICLKVGIERALAVARNARLPLLPVHHMRAHALAGRLVDPDLQYPFLSLLVSGGHCLLVLVKGPTDFDLIGTAGKSSPGECIDKVGRAIGVDCRQRHYGAEVERLASLSSPEGPFRFEVKTPITPAADFNFDSLKSSYLQALLDKYKGIPADESDLIDFCASLQYQVTSHICRKLHVALDFLCSKTDIFAQNTPRSLVLSGGVAANRFISTQVGKICAHHGFTVVSPPPRLCTDNAEMIAWAGVEMFNEKNPDIISHLKLPSSIYAVDREPIGTSNLRTAIANYKVSRKLQPRSLFSERLSFYGKPIT | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in mitochondrial tRNAs that read codons beginning with adenine. Probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. Involved in mitochondrial genome maintenance.
EC: 2.3.1.234
Catalytic Activity: adenosine(37) in tRNA + L-threonylcarbamoyladenylate = AMP + H(+) + N(6)-L-threonylcarbamoyladenosine(37) in tRNA
Subcellular Location: Mitochondrion
Sequence Length: 413
Sequence Mass (Da): 45123
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A0A533YZ47 | MLTILLASTSPRRYHILSLLRLPFLMIPPASAEITSDARLPEREVLYQAEKKAASLAAAFPGTVVIGSDTLINLDGQKIGKPRDASDARVILKRLRDREHQVVTGVVILRTGDSRRYEGVEIVRVRMAASSDAQLEAYVSSGDPFDKAGGYSLQGGGRELVAGLTGDYLAAVGLPLKAVAEGLEHLHVPVPVDVAALYRDREFLNWKTFKEC | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: H2O + UTP = diphosphate + H(+) + UMP
EC: 3.6.1.9
Subcellular Location: Cytoplasm
Sequence Length: 212
Sequence Mass (Da): 23080
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A0A7Y8HX11 | MLKSVEDINTTKKRLKIEIPSEVIEREIASSVEKLRQRVKIPGFRPGKAPVNLLEKRFGKEIESEVLEKIIPEYYTMALREADLRPIDFPVLDEEVDFQRKSPLNLSFTIEVLPKIENLNYENIAVKDIPVTVEESDIEETIKKLQDKKAVFEVAEKEIEIDDLVIFDYIDSELISGEKIPSIKEIVTSMGNEIFPPDLMEKVIGKKKGDIIEFQHSFDKMHNVKEIAGKTLNIKVAIKEVKKKTLPEINDDFAKDIGYENLEELREKLKENIYRIKKNYAEKIQKAQIVNKLIEQHKFDIPESMLKKEIDTLLFEANNIKKDTIEENKGTDSEIVDSIKDTESEEDKKKDAEELQSKIHEKASKNVQAAIILQIIGQKEGITVNDEELEERISAIATKLSATPETIKKLYMYREGSLESLRNSILEEKVLDLILSKAKIEKEENA | Function: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
EC: 5.2.1.8
Subcellular Location: Cytoplasm
Sequence Length: 446
Domain: Consists of 3 domains; the N-terminus binds the ribosome, the middle domain has PPIase activity, while the C-terminus has intrinsic chaperone activity on its own.
Sequence Mass (Da): 51308
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C5LPV0 | MMASIVLAALACVVTNKTLPPALASLRRAGICGKDLNKKGNPEIPEAAGVCVGAVYCLALSLFLPFHMMCSTSRGIPMDEAELMSQRKASLFMGSLLSINAMCFLGFADNVLDLPWRVKLIIPTVATLPLLLVYYSSIGNTWVLLPDFMHPYLPDGHGAIDIGVLYYVFLSLLSVFCTNAINILAGINGLEIGQSMVLAVSLILNDLLQLYRHAQQAATWPPYESHLMSLYLLLPFVGASFPLMVANMYPAVAFVGDTYCYLAGMTLAASGILGQCSKTTLLFFGPQIFNFLYSAPQLFKLIPCPRHRLPQYEPKADQLSVSYTPWFNPVEELRPLGQFALMVIQSFHLARVECDEQGRVRVQNLTLINLVLWLKRDTNEKKLNKILLGIQCLWSLCAFFIRYRLAGFVYNVVD | Pathway: Protein modification; protein glycosylation.
Catalytic Activity: a dolichyl phosphate + UDP-N-acetyl-alpha-D-glucosamine = N-acetyl-alpha-D-glucosaminyl-diphosphodolichol + UMP
EC: 2.7.8.15
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 414
Sequence Mass (Da): 45921
Location Topology: Multi-pass membrane protein
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A0A1Q7CJP8 | MPEVRIPAFAKINLRLDILGKRDDGFHELRTIFQTISLHDELRLRASRSPGISLTIQGNQPLSAEPPQKNLVYRAVEALRHELKIASGVEIALQKTIPAGRGLGGGSSDAAAALLGYLRLTKKKLAAARLLEIASSLGADVPFFLLGGRALGVNKGDEIYPLPDIPKSQILVVSPKDIYVPTPDAYGWLEAKPFALTNSAGTSKLFQFCALSCLAGG | Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 3/6.
Function: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
EC: 2.7.1.148
Catalytic Activity: 4-CDP-2-C-methyl-D-erythritol + ATP = 4-CDP-2-C-methyl-D-erythritol 2-phosphate + ADP + H(+)
Sequence Length: 217
Sequence Mass (Da): 23253
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A0A9D6Q3B5 | MMADAIGDTHGIKRSEIDALQERVKAIDRELKNRRKDGTLPFFDLPYQDIKDIIKAADEIKDGFENFVLIGIGGSSLGPKALHAALNSPFYNQLTKKKRKGCPKIYFLENIDPDGLTALLDAIDIKKTIFNVITKSGTTAETMANLLIVRERLNAELGKREARRHLIATTDPKKGTLRRLVEKEGYKSLEVPEKIGGRFSVLTAVGLLPAAVAGIDIKGLLEGAAYMDSLTRSDNIWENPAYMKAGLEYIAATAKGRNITVMMSYADALSVIGEWFCQLWAESLGKRMTIDGKVVNAGQTPVRAIGTNDQHSQIQLYMEGPFDKTVTFICVEKFQNDVLLPRISEDGDALSYLGGHTINELIHAEGFATELALTKEGRPNCRITLSEISPFTIGALLYMFEVQTAFAGGLYNIDPFDQPGVEEGKRMTYAMMGMPGYEEKKKEIQEMVKRERLTIPPQGRE | Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Function: Catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate.
Catalytic Activity: alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate
EC: 5.3.1.9
Subcellular Location: Cytoplasm
Sequence Length: 461
Sequence Mass (Da): 51117
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V5RJB8 | MSSLMIVLGFFVGIFALLALITIHEFGHFIVARLSKAYVYEFSIGFGPRIFVFKGKETWISIRAFPLGGYCSIASDKVDPPKDREDVVVPKERQMDYIARWKRFFFIIAGPLMNLFIALLLFTIIFASTQVKKNDMSYFGAKYDQNKIAYKLIEKEEKKLLKTDKVDINQQYVIWGWTLKDFDTNEFIFDNICDETTKCDDKINEISSQQAVDYKKTVYNFIDNLKRSENHKNVQIMFQYKKVDKFSGLALDGYKDGRITEMSSTDINDNLYYESGQNVGIASPDRFYKSSNEAYLAGWKETFDQSLSIIKSLGMIFTGHFSQLSGPIGIAGQTATMLQSADQFFLYVAMISANLFILNLMFFPPFDGYKVVELFIEMIIRREIPQKYKIIIYTIGGVLFLGLLIAVTIKDFIV | EC: 3.4.24.-
Subcellular Location: Membrane
Sequence Length: 414
Sequence Mass (Da): 47570
Location Topology: Multi-pass membrane protein
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A0A1J5B2V5 | MINTRIAQRYAKALFDLAIEQNIIERVYDDIVLIKGVCETNKDFILLLSSPIIKSDKKQAIIKEIFEKHIHHVTLAFLLIITKKRREYYISQISKKFIGFYKDFKGIEIVTVTSANQLDQTTIQKVLQKLKTFITKEIELVQVINPNIIGGFIIQYDDKKYDASILNKIHALSKNFLTNEYIKEY | 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 catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
Subcellular Location: Cell membrane
Sequence Length: 185
Sequence Mass (Da): 21601
Location Topology: Peripheral membrane protein
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A0A933CEM7 | MSKLYTRGEKIAEGKTKRICRLIWNGDDKPDPSMVVIQHKDDITAGDGAKHFIPKGKGAVSGATNDKVFDLLIRCGLPVAFEFTHASSTEFVARKCAMYPLEVVVRRKAMGSYLKRNPHVPKGALFPRLEAEFYLKTKDKEWRGAKIAKDDPLIRFTETGAELFHPGEPLALQAPFMTLTEELAPAEHRQQMEEIAIKAFLALEKAWSLLGAELIDFKVEFGLDTAGNLLLADVIDADSWRVLKEGDHLDKQPFREGEPASKTLARYRRVKELTDQFQVPKQQVLLFMASERDDAAPFLKSLAHYGFLEDDRNHMIRRIIGSAHKQPEQVLDALFKTVQECPDCVIIAAAGRSNGLGPVLAANTAAPVITVPLNYADFPNDIWSSLRLPSQVPLQTLMPISAVLDPANAVLAAMRILAQRSPWLYMRLGMDVNSRRKNPLI | Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate: step 1/2.
EC: 6.3.2.6
Catalytic Activity: 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + ATP + L-aspartate = (2S)-2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamido]succinate + ADP + 2 H(+) + phosphate
Sequence Length: 441
Sequence Mass (Da): 49232
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A0A532UJM7 | MIKLDISIIFIIGLFLLLVLILNRYFFKPLLKILEERKGMVLGPREEAQQSLKVVEELTQQRERALASTRAESQQLKDERVQEGRREGDKIIASTRTEAERLLSSEEKEIKGMVREVERDLEGMSDKFALKIAENLLGRRLPVSPPDKKGTKGERPHQR | Function: Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).
Subcellular Location: Cell membrane
Sequence Length: 159
Sequence Mass (Da): 18335
Location Topology: Single-pass membrane protein
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A0A2W6DTP9 | MRWQTYATEIFGLWALSRAFFLAYALIARSLGVIHTPRLSPGWHWVFSIYSRADSGHFVRVAEYGYFSRGITDVNVAFFPGYPAVGGAVARVLGLGRPTALDWQIGFTISAWLATFVAACLLYRYIYEESASSDAARVAVIALLFGPCAVFLMAPYSESLFLACALGAWLLGRRERWFLAALLCAAAALVRVNGLFLTVALAAMYLLAARREGRPLLRPSALSFFLPVASTTGYFFWLKLRTGRWDAWFDAEYRGWDRHTVAPWVALANSWRRVIYALTSEERFVLALELAFAAVYILLIIVLARRKQWPELIYVILTGGSLLTSNFYQSVPRSFLTLFPLYLLVAQWWMRRSWSPRTIMAVGSTGTLLILTSLFVRGFPSG | Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 382
Sequence Mass (Da): 42974
Location Topology: Multi-pass membrane protein
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A0A1B8NZY5 | MRKLILIVVVGLAIGALLGQLIMSVPGYWLVRVGDTSFQTTFWFGLVLLFAAFVVLHFLLRLLMRLSRPVSRFKGWSSRSRNRSAMRRTVRGLVALAEGRWKRAEKALVKAADDSSTPLVNYLSAALAAHYQGRYEQADTLLKRAHLSTEGADTAVGMMQAQLMLDRQQYEEALAILTRLDRHLPNHPQVLKQLKQAYLSVSDWEGLRRLMPRLGAQQLISQEEREQLEQRAYRELIAQEAREAGDIEQVRTLWADMPDHLRGNVDLIVLYVEAWCVATSRPSPSACCASRSRITGIAA | Pathway: Porphyrin-containing compound metabolism; protoheme biosynthesis.
Function: Involved in a late step of protoheme IX synthesis.
Subcellular Location: Cell inner membrane
Sequence Length: 299
Sequence Mass (Da): 33738
Location Topology: Multi-pass membrane protein
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A0A931Q4P4 | MAKNILIVTGEPSGDLHGGKLVQALIKKDPTLKIFAVGGSAIQAAGGDLIFNIESLGVVGLFEVITHLKVIRKAFQTVLETLRKNSIDHLVLIDYPDFNLRVARRAKQMGIPVTYYISPQIWAWRHGRIHLIKQLIDQMLVILPFEETLYRKERIPVAFVGHPLLEEINPVYQKDPLCKKFGLNPSYPIVGICPGSRESELKRLLPVMLEASEKIRTEIPNVQFILPIAAPFSKEKFLKRLGSYAEKIKAVKGDTSEVMAVCDFLTVASGTATLQAAIIGTPMIIVYKVSPLTYWIGKKLLKIKMIGLVNIILGDKIIPELIQHEATAENIKLEIVKLFQNKEKNRIMKSKLSLIKEKLTEKKASENAAEAILRLLYR | Pathway: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
Function: Condensation of UDP-2,3-diacylglucosamine and 2,3-diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
EC: 2.4.1.182
Catalytic Activity: a lipid X + a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D-glucosamine = a lipid A disaccharide + H(+) + UDP
Sequence Length: 378
Sequence Mass (Da): 42374
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A0A1J5AXM1 | MLKNDCFELGHISKTSGFRGALVFMLDVDVPENYKKLESVFIDINEKLVPFFVKSFHLPKNSRFATVQLENVNDIEQAKPLIHHKLFLPLTLLAPLEGNQFYYHEIIGFDVIDEVNGNIGKVTSIIDMPHYAILQVDANGKEVLIPAIKDIIIKLDRNNKVLSIKAPEGLIEIYTK | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Subcellular Location: Cytoplasm
Sequence Length: 176
Domain: The PRC barrel domain binds ribosomal protein uS19.
Sequence Mass (Da): 19974
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A0A950LRE7 | MLNIFARALFSRVVDPMGGRLARSGIGPDIITLIGTTGTVVSALWFFPRDQLLAGTIAITGFVLLDVLDGAVARARGSGTPWGTVLDATCDRIADGALFAGLTWWCFGLAHDRLLAAAALLCLVSAQVISYIKARAAASGLSADGGIVERAERYLITLVGAGLAGLGVRFALDVALWVLAGLQLVTITQRMLAVRRDSRGAASQRSTLADPGCPIGSRLLRDAPRTPSRQPCPAGADRVGEETPIPEPAPPSPSQPPLPAVVVNPRHITDLPTLHAQITSVCAELSWAPPLWLLTTAEDPGGGQAKAALAAGAAVVLACGGDGTNRHIAQVLAGSGTALALLPTGTANLLARNLAIVPEDTAHATRIALSGTTRTIDVGRVLIDDCAEEQVFLVMTGMGFDAAIMTGAPEQLKARLGSLAYVVSGARALMAPRVPVTLAVDGRSESPRQVRTVVVGNCGKLLGGLTLLPAAKLDDGLLDVVAISPRSLLGWLAVTARVLTRRRRGHRIVQHWQGRTIILSAQAPQQAQLDGDPIGDVRAMRMRIDPGALLIRV | Cofactor: Contains a di-nuclear catalytic Mg(2+) center.
Pathway: Lipid metabolism.
Function: Catalyzes the conjugation of the 1'-hydroxyl group of D-myo-inositol-3-phosphate (also named L-myo-inositol-1-phosphate) with a lipid tail of cytidine diphosphate diacylglycerol (CDP-DAG), forming phosphatidylinositol phosphate (PIP) and CMP. PIP is a precursor of phosphatidylinositol (PI) which is an essential lipid required for cell wall formation.
EC: 2.7.8.-
Subcellular Location: Cell membrane
Catalytic Activity: 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-cytidine-5'-diphosphate + 1D-myo-inositol 3-phosphate = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + CMP + H(+)
Sequence Length: 553
Sequence Mass (Da): 57672
Location Topology: Multi-pass membrane protein
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D2QFV3 | MKVDHETLHKIAHLARLEVKPDEEAALLNSLNGVLTWMEQLNEVDTTGVEPLTHMSAETNVLREDVAGNHLPREQALSNAPQHDEQFFEVPKVLE | 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 activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
EC: 6.3.5.-
Catalytic Activity: ATP + H2O + L-aspartyl-tRNA(Asn) + L-glutamine = ADP + 2 H(+) + L-asparaginyl-tRNA(Asn) + L-glutamate + phosphate
Sequence Length: 95
Sequence Mass (Da): 10717
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A0A931Q627 | MLKRVRENLKNLGVNPGDLLVVAVSGGPDSVCLLHLLSEIGKSYPFKLHAGHLNHSLRGIEADEDAEFVRKFCDVLNIPSTIVKKDIASLAKSMRKSTQETARMARYQALREISRQNEGRWIVTAHHAGDQAETFLMRLIRGSGPRGLSAIPRIRDSVIRPFLNFTKDEILAYLRQHQLAFREDSSNKLPHYFRNQIRQELLPFLEKYNPNILHVLERESDILMEEDRALEAVVNQVLPQIVSFPEKGNAVVAIQPFLNQIPAIQRRILRQVLVQMRGGLLNIHYHHVQNLCHLAKKMGNGKSICLPGGIKAYKSYDRLVFLGQDSIQSGGPVGLSIPIPGHAVSSALKIKVKTSLFEAAPQNKPEKNKEFFDYSKITLPITLRNRLPGDFICPVRLRGKRKKLQDIFVDLKIPRVLRDTIPLIVTPGRVLWIVGMERDFPSQVSSKTNRVLQIEVESTDLA | 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) in tRNA(Ile2) + L-lysine = AMP + diphosphate + H(+) + lysidine(34) in tRNA(Ile2)
EC: 6.3.4.19
Subcellular Location: Cytoplasm
Sequence Length: 462
Domain: The N-terminal region contains the highly conserved SGGXDS motif, predicted to be a P-loop motif involved in ATP binding.
Sequence Mass (Da): 52211
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A0A7V0R0C0 | AVAHHKNDQAETILINLLRGSGMKGLTGISPVRKNIIRPLIDVGKEEIIDYLSNIREGYMVDSSNLGNAYLRNKIRAFIIPELKNLNPGIVETLNRTAEILTQENDYLEMAVTRTMIRLFSRKTESRIEMFLIPMETIPAVLLRRILRRTIAEITELKSLSLRNIEDIIELIKRGKSGDRIYLPNNLRAIRNYSLLVLTTELPSRLKTYSLKAGDDLLLRETGLVLKAQISDRQPDSDGKSIAVFDLARIYLPLTVRARKKGDFFFPAHFGKKKKLQDFFVDEKVPRDERDSVPLICSGDNIIWVVGYRPDDRYIPDKNTKEFLTITSRITMK | Catalytic Activity: ATP + cytidine(34) in tRNA(Ile2) + L-lysine = AMP + diphosphate + H(+) + lysidine(34) in tRNA(Ile2)
EC: 6.3.4.19
Subcellular Location: Cytoplasm
Sequence Length: 333
Sequence Mass (Da): 38170
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A0A973JP39 | MRIGFHVSISGGFSLAVQRAFELGCSTMQIFSRNPRGWTVKPIDPDDVAEFRKLREQYDIGPVFVHTNYLINLASPKPDLYQRSIEQFVIDLERTEHLGAEYLVTHLGSASGQEPEWMIDRVADALNMAMKLHKPQATILLENTAGEKGDVGYTFEQVSEVISRLRNKDKIGICYDTCHGFAAGYDVRTKRGVDTVAKKIEETVGLEKLKGMHLNDCLREFDSRVDRHWHIGDGKIGEAGFKALLNHAAFKDVPKIMETPKETEEDDPRNMKKVRSLVK | 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-products.
Sequence Length: 279
Sequence Mass (Da): 31562
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A0A2W6E9N5 | MVVGEIAEAADFIVIGGGPGGYMAALRAAQLGADVLLVERGGPPYLGGTCLHVGCIPSKSLIELSRLCQSARTSAHRGLVADLVVDLAAFQQHRDDVVKRLCRGISALLRRRRVRVITGEAFFNRPDRIAVRHDNQVSFFDFHRAVIATGSRARQSDVLPVDGTRTLDSSGALALTSLPPRLSVVGGDYIGMEIATAFAALGSVVTVLHDGTPLFPGIDADLLSPVHRRLERLGVTVLPDSTVCGRDDDVLHARTPKGAVEVGTDVTVVSLGRQPNTDEIGLHLADVAVDTDGFISTDTQCLVRPGLAAVGDVTQGPALAHKAYAQALVAAESLCGRPASFQPYAIPVAIFTDPEIASVGMTAEQARDAGAGIQVVNFPLSALGRAATVNASDGFCRLVVDQEQDRILGAQIVAPQASDLIAEVGLAIEMAASPHDLAATVHAHPTMSEGLYEAASLAAGVPLHVP | Cofactor: Binds 1 FAD per subunit.
EC: 1.8.1.4
Catalytic Activity: (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + NAD(+) = (R)-N(6)-lipoyl-L-lysyl-[protein] + H(+) + NADH
Sequence Length: 466
Sequence Mass (Da): 48624
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A0A423PI61 | MFDIGFWELTILAVIGLIVLGPERLPVVARTLGLWVGRAKGYVRGITSELEREVSVDELRADVRRTRERIESETRGAIEPAQDALSPERPSVMPSDDDVARGDARSGAADRGDAPAGAAPTADDGSRKTDRPSE | 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 TatC, TatB is part of a receptor directly interacting with Tat signal peptides. TatB may form an oligomeric binding site that transiently accommodates folded Tat precursor proteins before their translocation.
Subcellular Location: Cell membrane
Sequence Length: 134
Sequence Mass (Da): 14454
Location Topology: Single-pass membrane protein
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A0A1J5WUT0 | MKIPTPLYIALLCCVVHCCVSGICPFAMRLFLCFGIAGVNMNTQQKDVLPEGLGVVAGVSHFAAVAVFLGTSSLAKSRVSRKEKKLVLSTALASLLSCLLGFLDDVLELRWRQKLFLPALALLPFLREFELRKTRLHGTARFFPLHRLASYLLLSLCAVFAVNAINILSGINGIEITQSVIIACGALALPTAPQKGENVAAVLPLALLVATGTALLRLNRYPATLFVGDSFCFYAGTTIALSWFLEDTRGEYILFVLPQTLNFLVSLPQLLKIRPCPKHRLPMFCAESQTLRPSSCDGKTNFTLLNIVLWLREMDERELAATMALVQVLCVSAGILFPLIWDQFIPTQNETEWKNLRQSSPSRLASPRFLEGMASSGPWSTESTSTSSEHRTT | Pathway: Protein modification; protein glycosylation.
Catalytic Activity: a dolichyl phosphate + UDP-N-acetyl-alpha-D-glucosamine = N-acetyl-alpha-D-glucosaminyl-diphosphodolichol + UMP
EC: 2.7.8.15
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 393
Sequence Mass (Da): 43193
Location Topology: Multi-pass membrane protein
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A0A1G1G1V0 | MKLKELASLTDGEIIGPPQSDDIEITGVSGINEAKKGDITFVSSKKFIKDLPGCKASCVIVKEPVSDLDIIQLKVSNPYFAFAKLLEYFYIKPHKCIGISKDAFVSDKSKIATDVSIFPFSYISEGASVGTGTVIYPHVFIGENTIVGERCIIYPNVTLREGIKVGNRVIIHSGSVIGSDGFGYVFEKGRHYKIPQVGGVIVEDDVEIGSNVSIDRATTGNTIIGSGTKIDNLVQIGHNVKIGKNSIIIAQVAIGGSTEIGNYVTLAGQVGVADHAKIASETMIGAQSGIMGNVSKGVYSGSPAMPHREWLKASALFAKLPELYKKIRELEEKIKKLKGGN | Pathway: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
Function: Catalyzes the N-acylation of UDP-3-O-acylglucosamine using 3-hydroxyacyl-ACP as the acyl donor. Is involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
EC: 2.3.1.191
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] + a UDP-3-O-[(3R)-3-hydroxyacyl]-alpha-D-glucosamine = a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D-glucosamine + H(+) + holo-[ACP]
Sequence Length: 341
Sequence Mass (Da): 36489
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A0A5S9QQJ6 | MATVNSTTKPGLAVGAVSKADDVIDLSEIFTLLMRHKWQIVGFTAAATVLVILVVFSMQPIYRASTTLLLEQSENKVVSIEGLYGAEVQNQDYYSTQYEILKSRSIAEKVVHDLNLVNNKLVNPTLAEKGMFDGLFDIRGLLGLTLPTEHLTDEERQAEVLEKTVRVFQSAVRVQPIKKTKVVKVSFDSSDPRLAARVADAIANTYIDSYVGGRLEQSSLAHRWLQEKMGSLEVSLIQAESLLQDYREENNLVDFDGVASLAETELRGLTASYIEASRKRSQSQAAYDQVKKINKTDLNAYADLPEVLNNSLINSLSTQYSKAQGRVAELNMRYGPKHPKMIAALSEREALEVSIQRQVIKIVDGIRTQYRADKEREKILESQIVDAKTNAQAFNRKQFRLMALKRDVRTKKDLHDTFFKRMQESVATEGLETANARIIDKASVPKTPIKPKKKLIVMLGAILAVLFSSGLVVLLDMLNSSIKSMRDIEEKLSLPVLGVLPVLPKSAERIDTGPSAKSPKERDYDIVKVLKEGTDNYAFNEAVRAVRTSISVGALDHPRKVFMVTSTVPGEGKSSVSVALASSLSQLGKVLIVGADFRKPSLVYKMGVKPGSPGLANVLAGSHRIDEVVHSIGALDVIIAGMIPPDPQELLSRGLDKLIEQLSETYDHIIIDCPPVQSVADSLLISKYCDGLIYVVESGRVSASVIQHSVGRLLQVGAPLYGVLLNKHQHAGEKYGSYDYYYEYRSQNAT | Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
Subcellular Location: Cell inner membrane
Sequence Length: 750
Sequence Mass (Da): 82760
Location Topology: Multi-pass membrane protein
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A0A521KU65 | MPLPSADQIRTVVRRALDEDLALGDVTTAALFPKPIPAHGTVTAHQTLVLAGIAVAREVFTVVDPTVRVIRALADGTPVTKGQTVLTVHGDARSLLMAERVALNFLQHLSGIATLTGRFCHAVRGSHATILDTRKTTPGLRTLQKWAVTLGGGQNHRHSLGDGILIKDNHLLLLQGRHIGIAQACVLARKHAPHGLRISVEVQSLDQVREALQGAADVILLD | 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: 222
Sequence Mass (Da): 23710
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A0A7X8LA49 | MISYIKGTLVEIGETWVVVESGQIGYQLFIPTSNFAQLPPVNSEIKLFTHLQIREDIFILYGFLKKEESQLFQLLISVTGIGPKGAVGILSALTPSEVYFAVLGNDIVTLCKAPGVGKKTAQRMILELKDKFKMENIAEICSDGLEKDTSNQSKKEAVEALVALGYQRHDAFRVIQSLDSTDITNTENMIKEGLKRLTMMG | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. HJ branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Subcellular Location: Cytoplasm
Sequence Length: 201
Domain: Has three domains with a flexible linker between the domains II and III and assumes an 'L' shape. Domain III is highly mobile and contacts RuvB.
Sequence Mass (Da): 22262
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A0A8K0VXV0 | MVGLVEVQSPDNFTSKPFRSTYYDDRMRASPALLRARAPYLIKNTITGIAICSLVIGIYTYTINAISQDEFDDVIVPDEPLKRPAQQQPQQLSGGTTLAVQQAVDARK | Function: Required for assembly of cytochrome c oxidase (complex IV).
Subcellular Location: Membrane
Sequence Length: 108
Sequence Mass (Da): 11959
Location Topology: Single-pass membrane protein
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A0A521RTU2 | MGGERRSNSHRDGDLRRSGCFRPGERKVRSLLAAIGTLTIVPFGHSMCAPDRELGRSVLFFPLVGLAIGALLMGTALLLGPVLTPSVVAALLLVVSALITGGLHLDGLADLCDGLGAGGDRRRILSVMKDPHVGAFGAIGLAIVLILKYALFGEMIRRGWTASFLVMGLLSRWAMVLASFIGRYAREAGTARPFIGQIRWPHCAAASALAVGPTWLISKEVGLIAALLVFLSVLIFDRFLESKIGGWTGDTLGALNEIVEVGVLLFVSVAEGFMAGGEPPV | 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-ribazole 5'-phosphate.
Catalytic Activity: adenosylcob(III)inamide-GDP + alpha-ribazole 5'-phosphate = adenosylcob(III)alamin 5'-phosphate + GMP + H(+)
EC: 2.7.8.26
Subcellular Location: Cell membrane
Sequence Length: 281
Sequence Mass (Da): 29642
Location Topology: Multi-pass membrane protein
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A0A2M7QCI2 | MTYTINIATENKPGVLYRITGLLTKRKINIENLNAFETKKPGISQITITADIEPTAIDTLVKQMDKIVEIVNIKYHVAHR | Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 1/4.
Function: Catalyzes the conversion of 2 pyruvate molecules into acetolactate in the first common step of the biosynthetic pathway of the branched-amino acids such as leucine, isoleucine, and valine.
EC: 2.2.1.6
Catalytic Activity: H(+) + 2 pyruvate = (2S)-2-acetolactate + CO2
Sequence Length: 80
Sequence Mass (Da): 9066
|
A0A933SXX8 | MHESDIPEVLEIERMSFTTPWSEAVFYNEIYRPFSITRVAFAGEKLVGYICANQIIDEGHILNLAVHPDYRRRSIASTLVEGILKELKDCECRVLYLEVRISNHAARKLYEGFGFKVVGIRKCYYVSPIEDAVIMMLEM | 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: 139
Sequence Mass (Da): 16082
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A0A520KPA2 | MIWGLVFLYWCFELNSIYFETYGCTTNRADTDVMKGIVEEAEFELACSPDEADFVVINTCTVIDKTEKRMLRRIRELSDKNLIVAGCLASAQPEVIRNIDKSIEILPPSEVGDLLSHVGGTTCFDKWSAPSNLDGVIGRVQIADGCLGNCSYCITKKARGELESSPVELVLQKIEELVFKGAKEIQLTAQDTAAYGKDIESDLPTLIDNIMGLEGDFRVRVGMMNPFSIKGMENEILNMYQHNRIYNFLHLPLQSGSNKILKKMGRPYTQDYYLDFAGKYKEKVGGVLSTDVIAGFPNETQQDFNETISTIKKLEPDIINITRYSPRPGTKASEKNEIKSSEKKERSKRLTKLRKKYGKQNKKPLIGSKRSVLVTKPGKKDTYIGRDKNYNPVVIKNNVSIGQEVEIEIDDYTFAYLEGRKTNP | Cofactor: Binds 1 or 2 [4Fe-4S] cluster. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the methylthiolation of N6-threonylcarbamoyladenosine (t(6)A), leading to the formation of 2-methylthio-N6-threonylcarbamoyladenosine (ms(2)t(6)A) at position 37 in tRNAs that read codons beginning with adenine.
EC: 2.8.4.5
Catalytic Activity: [sulfur carrier]-SH + AH2 + N(6)-L-threonylcarbamoyladenosine(37) in tRNA + 2 S-adenosyl-L-methionine = 2-methylsulfanyl-N(6)-L-threonylcarbamoyladenosine(37) in tRNA + 5'-deoxyadenosine + [sulfur carrier]-H + A + 2 H(+) + L-methionine + S-adenosyl-L-homocysteine
Sequence Length: 424
Sequence Mass (Da): 47812
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A0A7W0J4K3 | YRMRELTGKYRAKLFINDRVDIALSVEADGVHLGQKSIPTYAVRKIVKDKFMIGVSAHSIEEAKQAEKEGADFITLGPVYKTPSKLRYGQPLGVDIIRKTKAEISIPVFAIGGIKKDRIKEVMDAGADGIALISGILGARNIRDKTEEVLGLLR | 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.
EC: 2.5.1.3
Catalytic Activity: 2-(2-carboxy-4-methylthiazol-5-yl)ethyl phosphate + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 2 H(+) = CO2 + diphosphate + thiamine phosphate
Sequence Length: 154
Sequence Mass (Da): 16952
|
A0A081NJL8 | MAIGRVHSMDSFGTVDGPGIRYVVFMQGCLMRCRYCHNRDTWDLREGGELKSHEEVFREIKKVKNFLSGGVTVTGGEPILQAEFVADLFEACQKEGIHTCLDTNGFAKHINDDVVRLLDSTDLVLLDIKHMDEEMHHKLTYVTGSHTQHFAQYLAEINKPVWIRYVVVDGYTVDPQYAGMLAEFIEPMKNVEKVEILPYHSLGVHKWDFLNDTYELEKVTPPTQEQLDLIRDEFTTRGVAAAY | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Activation of pyruvate formate-lyase 1 under anaerobic conditions by generation of an organic free radical, using S-adenosylmethionine and reduced flavodoxin as cosubstrates to produce 5'-deoxy-adenosine.
EC: 1.97.1.4
Catalytic Activity: glycyl-[formate C-acetyltransferase] + reduced [flavodoxin] + S-adenosyl-L-methionine = 5'-deoxyadenosine + glycin-2-yl radical-[formate C-acetyltransferase] + H(+) + L-methionine + semiquinone [flavodoxin]
Subcellular Location: Cytoplasm
Sequence Length: 243
Sequence Mass (Da): 27799
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A0A7W0F773 | MKLGIFGGTFNPIHYGHLRVAEEVKEKLGLNKIIFVPSGNPPLKGTELADAKHR | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
EC: 2.7.7.18
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Length: 54
Sequence Mass (Da): 5940
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C5L3S8 | MASLPSHFSAATSPLPRGIIQAQASPQRGKRRNPISGFTIEEAEDERLKFMRCFTDGIDVTRVRGRSTVSVWEKVADKLSRDGGPAQLLRDTSPAPVDAAYWCGAFPWDNEVRRRNQSVQSLRVLVEADCQIRRFTFGNQGGFRPNQLETINAVLSKRDVFLVMPTGGGKSLCYQIPALVNHEARRGGTTVVICPLVSLILDQEAQLSQCGILCAGLSSSAAHTMPPVETFKKLFSGKLRVLFVTPERLSASKRLLDLLAGLYRNSLLHGFVVDEAHCVSQWGHDFREDYLLLANIRKTFPGVPILAMTATAKPDVMKDIMLQLGMPTSSTVVIRTSLNRTNISYSVVKRPSKGKMLESLAGKIRELSGKDGRGSGIIYCMSKKDCEQVSTGLRAYSIKAAVYHADLPQSIRDTNQKLWMDNEIQVMAATVAFGMGINKRDVRFVIHYSMPKTLEAFYQESGRAGRDGRPSYSVIYYDYYSKNRNQWLIEQGGDRSRAGISTHARHELIGEQKKSLLALVAYCESGTQCRRIILLKYLGTEAGPVATCLDSNSLPCDVCIEQQQVRS | Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
EC: 3.6.4.12
Subcellular Location: Nucleus
Sequence Length: 567
Sequence Mass (Da): 62883
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A0A941UNK3 | MKTPSFKNQLKYIAHLIICHSRNSIPNAFGIGRSGILLLERGSGQIGVTNYSKLISFFIKVIIPCFLFTLSFFYFSLCASASTENTIKVLIVNEVYPKLPAKNERIEKLGTMQGELLVMGSRYAGNIDVWKGENGLYIINELPLEEYIRDVVAAEIVPDWDMEALKAQAVVSRTYALYQKTMNGNSLYHLASSVLHQVYKGKNPDMRITYAVSATNGEVLTFNGTLIEAFYHSTCGGKTEYPEEVFGKSYPYLKSIESSCDLSPYSVWERSIRLDEIAKATGIAGIQDISVKSFTSTNRVRQLSIRTESVTTIMNATDFRKALGWSRLPSTNFTITRVDDGILFQGWRAKEKIIRKFCLFSIPARQYSCMKTVDFDYFLPEPIIANKPLRERTSSRLLVLHRDSTLEHRTFLDLPSYLEQGDMLIINNTKVFPARLTGTKKNGKTLEILLVRENADGTWDVLSQGKFTGRLKISDELEVELQQGISARFQSSLDIMDLLWKYGDMPLPPYIRRAPDEADRLTYQTVYAMKEGSIAAPTAGLHFTDLLLNAISSKGVKIREITLHVGIGTFRPIRTLMVKDHSMDREHFEIEKSIIAEIYEAKALGKRIVAVGTTTTRSLEGYFSGTYTNGSNPFSPPVVRAASPAKKAGTGKMKTSECVRGTTDIFIYPGYTFTAIDSLVTNFHLPRSTPLMLVCALAGREQILTAYNEAIASGYRFLSYGDAMLIV | Pathway: tRNA modification; tRNA-queuosine biosynthesis.
Function: Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA).
Catalytic Activity: 7-aminomethyl-7-carbaguanosine(34) in tRNA + S-adenosyl-L-methionine = adenine + epoxyqueuosine(34) in tRNA + 2 H(+) + L-methionine
EC: 2.4.99.17
Subcellular Location: Cytoplasm
Sequence Length: 727
Sequence Mass (Da): 81444
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A0A944D2I9 | MFRETFDDKKRRARKILRILKKTYTEPGEFVHWTTPLELVVGTLLSAQCTDKRVNIVTKSLFKKYRTPKAYASASLDELEAAISSVTYFRSKARYIQGLGRMILRDFGGTVPSTLEDLVKLPGIGYKSAHLVMSKVHAQHTGIAVDTHVKRVAPRLGLTRQKDPGKIGADLEALYPRADFLSVNEYLIMHGRAICAPRNPKCNECPVRSLCPYGRVSRA | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: DNA repair enzyme that has both DNA N-glycosylase activity and AP-lyase activity. The DNA N-glycosylase activity releases various damaged pyrimidines from DNA by cleaving the N-glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The AP-lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate.
EC: 4.2.99.18
Catalytic Activity: 2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-monophospho-2'-deoxyribonucleoside-DNA + H(+)
Sequence Length: 219
Sequence Mass (Da): 24621
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A0A7Y9F1N8 | MTATNEPTTTTPARTTGPAWGHGLATVTGDGTVLDVWFPQPRLGSRPDVEEPAPKVLVDLEGSDHARGVRREVVLVEIADLQQPPADTADVWLRLHLLSHRLVRPHGISMDGVFGKLTNVVWTSAGPCAVADFEMARARMKAGGTHVAVYGIDKFPRMTDYVAPAGVRIADADRVRLGAHLAEGTTVMHEGFVNFNAGTLGSSMVEGRISAGVVVGEGSDIGGGASIMGTLSGGGTAVISIGERCLLGANAGIGISLGDDCVVEAGCYVTAGTKVTMTDPEGGEPRVVKAAELSGASNVLFRRNSVTGAVEAVAWKGEGIALNADLHAN | Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): step 1/3.
Function: Catalyzes the conversion of the cyclic tetrahydrodipicolinate (THDP) into the acyclic N-succinyl-L-2-amino-6-oxopimelate using succinyl-CoA.
Catalytic Activity: (S)-2,3,4,5-tetrahydrodipicolinate + H2O + succinyl-CoA = (S)-2-succinylamino-6-oxoheptanedioate + CoA
EC: 2.3.1.117
Subcellular Location: Cytoplasm
Sequence Length: 329
Sequence Mass (Da): 33995
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A5FW89 | MRAPAFWTTDAFPAPLLAPLGAITRALTARRVARPGFRSGARVFCAGNAGVGGAGKTILARHLLARLADRGETVFALTRGHGGRLAGPLRVDPARHGAAEVGDEALLLAATAPTIVARDRAAGAAFAVAAGATAIVMDDGLQNPDPVKTASFLVIDGGAGFGNGRLLPAGPLREPVEAAARRCAAAVLIGADRTGARAALPPSLPVLTARLVTDAGQLAGARVLGFAGIGRPEKFFESLSDAGAEIAGTLPFPDHHAYRPADLARLDAEASRLGARLATTAKDAVKLPPAFRARCAVIEAGLAFDDPAALDRFLT | 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 tetraacyldisaccharide 1,4'-bis-phosphate (lipid IVA).
EC: 2.7.1.130
Catalytic Activity: a lipid A disaccharide + ATP = a lipid IVA + ADP + H(+)
Sequence Length: 315
Sequence Mass (Da): 32115
|
A0A1V4J4Z3 | MGRPGGLLLLLPLLLAAPGGAGTGSCEHQATCEACVRSHPRCAWCEDPEFPRGGRADAPRCAPREALERAGCPPRAVVQPRGSVRVLRXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXCEDCITRALAVRTACPMCGRFYGTLVGNQPPNGRMLVTRDAGLPLPGYESFGTIIIQYVFPPGVQGAEHPNPGVRYPGTTRVAYLPDCPEGNKVLALFRKAFAQRLTFTVGTSMTTGRANVITWNDIHHKTNCTGGPQLFGYPDPTYLARVQEELRAKGITED | Pathway: Protein modification; protein ubiquitination.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
EC: 2.3.2.27
Subcellular Location: Cytoplasm
Sequence Length: 285
Sequence Mass (Da): 30840
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A0A352PLA8 | MNANEQIMVRMRSHGTLLCAGLDPDLRKLPFEVLKKSGTDEEKVFEFLRGVVNATGTHVCAYKAQKAFFDLLPGGHDVLKEIIRYIHKTQLGVPVIVDCKIGDIDNTMATYIENLFGLINADGIVINPYMGDDVVAPLIELTDKAIIIIVKTSNASGSIVQDIALSDGRLLWQYLLDLVVNRWNKNGNMIPVLSSTAGLDMIKLRSLIPDTMLILLAGIGVQGGNYDDLRSLLNSERVGVFINSSRGLLYPASFEPWQTAIETAAIAMKEALNKAGRIS | 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: 279
Sequence Mass (Da): 30572
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A0A358C2U6 | MNTQFEQSVGALVGDRLKRNESLALHSHYGVGGPATYLVLAKTAEEVIAFVKAATEHNVPWVVIGGGTNILVNDAGFSGLVIKMANRSIKINHQTGEVVAEAGLLSSSLARQTGEAGLTGFEWGIGLPGTIGGAVRGNAGCFGGETKDKLVSVDVLDTQTGEIKTVAKEALEMGYRHSKIKEVPWIVLRATFLFEPRDVVLNRETISEVLRCRLDGQPKNVKCAGCAFKNVDYVDEEDIAKLRTVVKDIPESFLQAKRIPAGWLVDRLGLKGTHVGGAAISEMHGNFITSDGTATADQIMQLIALVKSKVRDAYGIQLHEEVQFIGFDT | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation.
Catalytic Activity: NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
EC: 1.3.1.98
Subcellular Location: Cytoplasm
Sequence Length: 329
Sequence Mass (Da): 35386
|
A7HX16 | MFPRDSTSKGCPQASCLAGPFQTTNKGGPMSVDQKTVRHIARLARIAVRDDELEALAKELNGILDWVEQLGEVDTSGVEPMTSAVAVAMKMRDDVVEVQNLQAEVTRNAPGSEDGFYVVPKVVE | 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 activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
EC: 6.3.5.-
Catalytic Activity: ATP + H2O + L-aspartyl-tRNA(Asn) + L-glutamine = ADP + 2 H(+) + L-asparaginyl-tRNA(Asn) + L-glutamate + phosphate
Sequence Length: 124
Sequence Mass (Da): 13417
|
A0A931MCP6 | MKYALVEVTPVKKTLSVEIPLEVVSKEIAVAYSQLSKTVRLPGFRKGKAPLALLEKKFHEEVKDDVLKKLIPDYYHKAVEESGIDPIEYPKIENIALEKNTPLSFKATVEVRPHFDLQPYTGLPIKIKKLTVTDANVEKSLHSLREMQAQLEPCPDDHIIVEKDFVTIDFESFIEEKPMEGGKAEGYSVEAGSKVLIPGFEENLLGKKKGNKIDFKLILPEGIKPEQNVGKEALFKVAIREIKKKILPEMGLEFAKDFGFYSVEILKEKLKEELVSRFKKERETTLKNELIKALNKRHEFELPSSLITRELVRIIRGLKDEDIKREGLLDIESIKKKFEPLARERVKGALILYAIAQKENIKVSHDEVEDEIHLIARESRMKEEEVKKNILEVEGSFSGIESRLLEDKALVYLMSKAQIEEEE | Function: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
EC: 5.2.1.8
Subcellular Location: Cytoplasm
Sequence Length: 423
Domain: Consists of 3 domains; the N-terminus binds the ribosome, the middle domain has PPIase activity, while the C-terminus has intrinsic chaperone activity on its own.
Sequence Mass (Da): 48428
|
A0A6P3GZI8 | MEPRSNVTHFVLLGLTQNPKEQKVLFVLFFFFYILTMLGNMLIVVTVTFSKTLNSPMYFFLASLSFMDVIYSSSISPKLISSLFVGENTISFQSCMTQLFTEHFFGGSEVFLLLVMAYDRYVAICKPLHYLVIMRQRVCVVLLVVSWVGGFLHSIIQLSTIFGLPFCGPNIIDHFFCDMYPLLKLVCTDTYVTGILVLANGGLIFTEQGALELVSFCWLVEWSGQGVPGGAGLL | Function: Putative odorant or sperm cell receptor.
Subcellular Location: Cell membrane
Sequence Length: 234
Sequence Mass (Da): 26215
Location Topology: Multi-pass membrane protein
|
A0A7V2J5X0 | LIVAAVYCINSCRFAVSWGAEWLEGMRNRMGRYVGSFLNWIEGKIKGPDFESAKRAYSIMIRDGKNHSSPNAGVPEAAMAGALGVRLGGPSTYEGVEVVKPYIGDNILKEGLKPGSAEAYMEAALIAVGIIKLTSFLGLLAAILLV | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
Subcellular Location: Cell membrane
Sequence Length: 146
Sequence Mass (Da): 15578
Location Topology: Multi-pass membrane protein
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F4LWH8 | MSTVVYLNGQRVDYENAKVSVEDRGFQFGDGLYEVVHIYNGRFFYLDRHLARLQNGAKEIYMDLDFGLNNLEKVCRQAVKESGFNDASVYIQVTRGAAVRQHAFPKESSCTWVVIVRESKGNPQEFYENGITCITVPDERWSRCNIKTVQLLANCIAKEKAKKAGSFEAIFHRGGSVIEGSSSNVFIVKDNKLITHPANNKILNGITRGVVLEIADQNDIKYSEEVFCIDDLFDADEVFLTGTTTEIMPVVKVDGKIIGDGIPGKLTKIIQKYYQEHIQTVDC | Function: Acts on the D-isomers of alanine, leucine, aspartate, glutamate, aminobutyrate, norvaline and asparagine. The enzyme transfers an amino group from a substrate D-amino acid to the pyridoxal phosphate cofactor to form pyridoxamine and an alpha-keto acid in the first half-reaction.
EC: 2.6.1.21
Catalytic Activity: 2-oxoglutarate + D-alanine = D-glutamate + pyruvate
Sequence Length: 283
Sequence Mass (Da): 31821
|
A0A931Q573 | MSQASFSVLGVGNMGSILLKSLVSLPFTSPEKISVFDPDPLSMKKAGKYKVRVARHLKEAVEGKAFVVLAVKPQMMTALLNEIRDFLLPEAVVVSVAAGVSIEKIQTVLKRDQKVARAMPNTPAILKKGMTALVYSGRLSSEEKAFVRRIFNRVGKTIVVTEDKMDAVTALSGSGPAYVFTFVEALVEGGVKMGLSEPVAYQMATQTLFGAVKMLIKLDLTPAEQIKKVTSPGGTTLAGLAMLESGRFKEIVISAMEAAAKRSAELGSV | Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-proline from L-glutamate 5-semialdehyde: step 1/1.
Function: Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline.
Catalytic Activity: L-proline + NAD(+) = 1-pyrroline-5-carboxylate + 2 H(+) + NADH
EC: 1.5.1.2
Subcellular Location: Cytoplasm
Sequence Length: 269
Sequence Mass (Da): 28737
|
A0A933S810 | MLFGAALGAMAWPGGPAAADPAPVRVIQLDMGDDAEPPLGLDPVRVPENNPQTPDKIALGRQLFFDPRLSVDGTVSCASCHNPKLGWSNGLSFAFGVKGQTGGRSAPTVLNAAYSDTLFWDGRAPSLEEQAKGPIANPIEMGNTYGQVTQTLKGIPGYVDRFKAVFGTDDITIDHVAMAIAAFERTIVSGNSPFDRYKYGGDRGALSAAQVRGMELFRDKQGPNCAKCHRFDDFTADLTDFRFHNVGVGSDHPTPDPGREKVTGSAEDRGQFRTPTLRNVALTGPYMHDGRFATLEQVVDYYAQGALANPNLDVEIHKFDLSAGQKADLLAFLEALTGDPLVMDPPALP | PTM: Binds 2 heme groups per subunit.
Cofactor: Binds 2 heme groups.
Subcellular Location: Periplasm
Sequence Length: 349
Sequence Mass (Da): 37407
|
A0A9E5AUR1 | MTEPASIGLLASLGINAKLFYAQLINFGIVMLIVWRWVYRPLLKAMDRRNKKIEEGLMQAEQIKKDRLAFDQEHTKLIKAAHEEAHKIMHAADEEAKQQRQTLIMKTQQEIERMERESKTHLEQEQIRMLRSLKSHVAELVIQTTEKILPSVLDKNHRQELMEQAAKEIK | Function: Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).
Subcellular Location: Cell membrane
Sequence Length: 170
Sequence Mass (Da): 19933
Location Topology: Single-pass membrane protein
|
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