ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
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A0A961ZJB0 | MTTRPNQSDGTSVAPSASGHSAGGPSPTGQDEPADPEPKPRIYLDLIDEDEAWGAVPDREMLIRAAVAAVATHPASALTLLSFLTDARPVATDAEAVVVLTTDDEVAALNHQFRGKLGPTNVLSFPAPSPPPGANASASAIASASASARAGAETGPTLALGDIVLAAETVFREAREMATKVEHHLQHLVVHGLLHLLDYDHLTAEDADAMERLETDILAALDVPDPYAGSEPEAMSPVAATRVETP | Cofactor: Binds 1 zinc ion.
Function: Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.
EC: 3.1.-.-
Subcellular Location: Cytoplasm
Sequence Length: 246
Sequence Mass (Da): 25495
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A0A2M7APK8 | MGYSKTGANCRGGYPMKKIVFIGNHPESVPLLENLIQKGKVNFWELSLIITRPDRQVGRKKNLTPSALKNLALEKGIPFLTPLKIATSFDRLATLKPDLILVSDYRQRIPTSILKIPALGCLNVHFSKLPQYRGPSPVPSAILAGEKEIGFSFFLMDESFDTGPLLFTSQFPIDPKDTSGSLIQKLYQKTAQTLPLALKKYFAGRTKPVPQQKKNVSYTRYLNRKDGKINWQKNDGEIERMIRAFSPWPGAWTFWKGKRLKIWQAHLDEKGKLVLDHLQLEGKKMLPLADFIKGYPDFSLANLKAQL | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
EC: 2.1.2.9
Catalytic Acti... |
A0A6P1U5J6 | MKRILINATQREELRVAIVDGQKLIDLDIETTAREQKKSNIYKGRITRVEPSLEACFVDYGAERHGFLPVKEIARNYFREGGKPGNGNLRELLHEGQELIVQIEKEERGNKGAALTTYVSLAGRYLVVMPNNPKAGGVSRRAEGDEREEAKEALEKLQLADNMGVIIRSNGVGRTLDELQWDADYLKDIWQAIEKAAETQKAPFLIYQENNIILRALRDYLRPDIGEVMIDNEQIYTQARTHLEHVMPQNLTRLKLYKDETPLFSRFQIESQIELAHERTIRLPSGGSIVIDTTEALTAVDVNSAKATKGGSIEDTALNT... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Endoribonuclease that plays a central role in RNA processing and decay. Required for the maturation of 5S and 16S rRNAs and the majority of tRNAs. Also involved in the degradation of most mRNAs.
EC: 3.1.26.12
Catalytic Activity: Endonucleolytic cleavage of single-stra... |
A0A7D4ULY5 | MQLYFATGNQHKAQEVEAILRARGADVEILMHKGEEPVESGSTFLENALIKARAAFAATGAPSFADDSGIAVEVMGGAPGIFSAIWSGGRDDKTNRDLLLAQLIDIPEENRAAAFVCTMALVDDAGEVSVTGVWPGKIATQASGEHGFGYDPIFIPQGFSVTAAELEPEVKNSFSHRAMALQQLASLLTSR | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as ... |
A0A1I8JT40 | MSKLWTSGVRYKISSGNVGNVFAIRNTTGALYVAKALDYEKIKKYELRLTASDNFKENYTTVLINVRDVNDNPPVFEKSSYRTQITEEDDRGLPKRVLRVTASDADVERPNNIIYFLTGPGIDIENPSDSNFDINKATGEIFVLKPLNRDPPHGRASWKFTVFAQDEGGEGLVGFTEVQINLKDVNDNAPQFPNGIAYGNVTENGTIGMHVMTIKAEDYDDINEGTNAKVIYSIEKNAIEEDTGLPIFDINPDTGLITTAVCCLDREKTPDYSLQIVATDGGGLKGTGTASIKVKDLNDMPPRFTKDEWFVEVEETDGSV... | Function: Cadherins are calcium-dependent cell adhesion proteins.
Subcellular Location: Cell membrane
Sequence Length: 644
Sequence Mass (Da): 71837
Location Topology: Single-pass type I membrane protein
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A0A7G5ZMR8 | MTTTDEPRRRRNPLRSVWASVALALTLTLLIVAFVGQPSSSSMSPTLQPGDRLIVNRLAYVAADPAPGDIVVFRPDERWGDEPAAPTNWLSAALRWAGETTGIRPYVLVKRVIAGPGQTVECCDADGSVLVDGAPIDEPYVVENLPYTAGEVDCETEPASSRCFPAVTVPENAYLVLGDNRANSADSVYRCRGDADAGDECFRWMMRADAFGKAGPILWPISRWGGP | 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: 227
Sequence Mass (Da): 24523
Location Topology: Single-pass type II membrane protein
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A0A949ZK20 | MCATRCAAEFGNPCEHFCPANVYEMIPAAVESAKIEKNGFMDSGKRLQINFANCVHCKTCDIMDPYQIIDWVPPEGGGGPVYTGL | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Accepts electrons from ETF and reduces ubiquinone.
EC: 1.5.5.1
Catalytic Activity: a ubiquinone + reduced [electron-transfer flavoprotein] = a ubiquinol + H(+) + oxidized [electron-transfer flavoprotein]
Sequence Length: 85
Sequence Mass (Da): 9274
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A0A1H1AU44 | MKLRQFSTQKGMTLVELLASISLFAVLIALSSTVIIQMINSEDNTSRQISLNQETNVLVSELRNEYTEKSDEVEDAEKFNICYQKIDGLDVKQVITFLDDKQQTKQVNNDCIIGITKQEVLPIEITTANEADQTLTIKTSWRNNDEYVIELKNEEDEKYEFTEDGKFANCDYNQNTRFKNADDYKKVMFIDDCKVNGSAWIAGDIEVKNKTKLVVEKNLYISDNVRIVGKGGNDKAGHLCVKGEIHFPDGKSESDYDIDFKCN | Function: Required for transformation and DNA binding.
Subcellular Location: Cell membrane
Sequence Length: 263
Sequence Mass (Da): 29972
Location Topology: Single-pass membrane protein
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A0A8J8GTU8 | MRVPRLHIVTDSVDIARAALSGGAPLIQVRVEDSVSDRALYDLASRIAPLCAERGAICVVNDRPHIAVALRTAAVHVGADDLPVHATRTVLGGSGLIGASARTPERARQVIAEGADYLGCGQVNPSFTKDVATNVIGLGGLTAVVGAAQGVPVIAIGGLTLADVPSVLAAGAYGVAVIGAVRDAADPAYATSALLAAVTPPTLATQDPRQIRDHGRIMAQDSTENPDPAPERAARKGAEPEGAGPEGAEPEGAGR | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)-thiazole: step 1/1.
Function: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-met... |
A0A8S0RZS1 | MFSCAHCCLRVMETIFRQGNGWAYVQIAAYGKDFVKASQDTWELFEKREMAPIVDSDITSAICFLTGVCSGSICVIVVAAWTATVHHGYTATLSVLAAFIGYLMTRIAMALPQACVSCYYVCYAENPENRLFDKTIPDRVNLIKSGRDVVVPTPRIPRRFTR | Function: Choline transporter.
Subcellular Location: Cell membrane
Sequence Length: 162
Sequence Mass (Da): 18104
Location Topology: Multi-pass membrane protein
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A0A8J4PMW6 | MFSRIVVRVQRTAFADIQKRFKYTLPDVPYATTGISNFLSQNSVSEHLKLHKLDVERANNLIQRTPWENTTINQAIVQSSTSREDAPFFEAASSHFNHSFFWRSITDVKQTPSVYMKKAVEIDFGSFKDFQIKFSQNASALNVPGFTWLVFHDKALKIVNTFGNGSPLELRNCHPILCLDLFEHSYISDYQSNKNVNINIILL | Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
EC: 1.15.1.1
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Length: 203
Sequence Mass (Da): 23324
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A0A1F9LQZ7 | MAELPAFIPDVTGVILAGGRSRRFGANKALADLAGRPLIAHVAAVLRGLFASCLVVTDKPTAYAFLGLPTTGDLYPGNGPLAGIHAALRCISTPYAFVTACDMPGLNPELLRFFCTLSANADWQAVLPGLTTGPEPLFGLYRQEAADPIEQHLRAGQYRAALALDDLRVRWVSETELLAVVPSFSVFTNVNRPEDLATIKHGPAPLSAIRREDGK | 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... |
A0A961YEZ7 | MEALAVLPVFFKLAGRRAVLAGGSDAAAWKAELLSAAGADVDVYASEISQEMREVAGNPPGGIIRLIERDWQTDDLSGAAIAIGAISDQQEGLAFANAARLHGVPVNVVDRPELCQFQFGSIVNR | Pathway: Porphyrin-containing compound metabolism; siroheme biosynthesis; sirohydrochlorin from precorrin-2: step 1/1.
EC: 1.3.1.76
Catalytic Activity: NAD(+) + precorrin-2 = 2 H(+) + NADH + sirohydrochlorin
Sequence Length: 125
Sequence Mass (Da): 13162
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A0A961ZBF8 | MLSIGWSEMLVIAAVALIVVGPKDLPAMLRQLGRMMGTLRRMGNDFRAEINKAVAVDEITDIRKSITQPLMTARQEIEREFNKVGPNGSVEPSGKIVPKDPKSESVYEEITAAIAPPGKVTEVPPATSEAKPAAKPAAKRSTKPAGTRRASKAAAAEAKPAAKDSAVKESAAKNPAARKSTAQKPSARKTTATRKSTSAGKSSEATAKADQ | 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... |
G8ZWM9 | MWSLWVLAIAGFIRYTTAILVPIEDIYGSKRYSINYLPFERWEQLIINNSTTLSSGTVMELGDYISCYVPNVDADLDSSVAQYNETELNEMLENGVKIITTVFNGCITYLGGFWNYELCSNTGLSQFDGDPKTSTSNYQLGRIKKSVEDREFQLLYDDFGYYISELVGSGDICDLTGHPRVVEIQYICRPAAGPASIQWVREIKTCHYEIQVAIPELCSLEILSKSEDKIVSRSILCVNKEDSNSGVVDIISSYKPTFLGNEVYLLEPYDKISSHNRTALMFTGNMSSHGSLLEQKLDIKLANAISRMVFQHLLLLPDGL... | Function: Lectin involved in the quality control of the secretory pathway. As a member of the endoplasmic reticulum-associated degradation lumenal (ERAD-L) surveillance system, targets misfolded endoplasmic reticulum lumenal glycoproteins for degradation.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Le... |
A0A1J4WW51 | MKLIEGNLLADKIQLQLKQEVVSFKSKPGLAVILVGENPASLSYIRQKNKAADKIGINFQTIKLPAKTNTAKLIQTIQRLNRDKKIHGIIVQLPLPSQINETLILNAIDPSKDVDGFHPLNRGKVFLNDETGFAPCTPKGILKLLEYSKCSPRGKHVVIVGRSNLVGKPLAVMLINQQATVTVCNSQTRRLKQITQTADIFISAMGQSHFFKNPAWFKKGVVLIDVGFSKVKDKICGDIQLEKFKNLARAGTPVPGGVGPLTVACLMENVIKAWGKNKM | Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
Function: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate +... |
A0A6A1VCD4 | MLLTDIKRKNEICSVAYTEVGGHSRLFPQHIRKTRIYPEALTYSPNSQGAMALLGMLSQLSLRIGATIVAASAASHPNSRCNSTCGSLGIPYPFGTSEGCYLDKYFLITCNLSYEPPRPFLRHSDYHVLNISLDGEITISSPVARDCYGQSGRSDDNGTLFYNDPGWRAKVLSKFRISSKRNKITAVGCDTYSYVQFSNEDKYYTTGCLSLCDPISSVKYGSCTGIGCCQTSIPEGAIDYFLRVGCLENHLTSYNDSPCGFDINECKTSNPCNTTCVNTLGSYKCYYCPKGFEGNGLRNGIGDACTDDVVMFEQNVYEMF... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Subcellular Location: Membrane
Sequence Length: 626
Sequence Mass (Da): 69154
Location Topology: Single-pass type I membrane protein
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A0A2M7F7F5 | MSGRLKRFIRTITLIDLLKGLALTGSVWVRSIITPSRVLVTRPYPEVKRPAFPAFKGHHALLRGEDGAIRCVGCGICAGVCPAKAISVYTEEGDHHEKVVTGYEINAFRCIYCGLCQEACPKDAIVLTRLYEMADYDDRGLYIWKMDRLLKVGDKKPLFRDQIDL | Cofactor: Binds 2 [4Fe-4S] clusters per subunit.
Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (fo... |
A0A5D0MFP2 | MTMFIDEAKIYTQGGKGGPGCLSFRRQKYRPKGGPDGGKGGDGGNVYLVATKSVKTLFEIKNNPHFKAQSGEPGGPNNRYGKSGDDLIVYVPLGTTVYDDEGNLLTDLIEEKDEYLAAEGGRGGRGNKSFLSNTNRAPRIRELGEPGEKRTLHLELRLIADVGIVGFPNAGKSTLLSVLSNANPKIASYQFTTMEPQLGAIVSQKGYSFVIADLPGLIEGASDGVGLGDRFLKHVRRTRILLHLIDMAGIDGRKPWEDYYKIRKELEKFDKEVAKKEEIIVGNKFDIPRAEENYKKFKEKTGKDIIRISAVSHQNIDELK... | Function: An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis ... |
A0A140LBB3 | MRIVDIRALEGPNIYSPKPVVRMLVDVGKWDDVSTKDLGGFKERLLEKLPGLALHHCCFDRPGGFLIRLEEGTYLPHVIEHVALELLNLLGQDVKFGRARWWEKTIYSVVFGYEGKYAALEAGKLAVRLVEDLICGKDVDLPGELSKIERYSAEMELGPSTSAIENEAKSRGIPVTRIGDGSLLILGYGAFQKRVEATLTNRTSSVAVDIACDKILTKKMLSLAGIPVPDGIPVYTEEEAVKAAEEIGYPVVVKPVDGNQGKGVSLNLKNEKEVREAFRIASGYSPKVLVENYIRGRHYRLLVVDGKFVCAAERIPAHVV... | Function: Catalyzes the ATP-dependent polymerization of arginine and aspartate to multi-L-arginyl-poly-L-aspartic acid (cyanophycin; a water-insoluble reserve polymer).
EC: 6.3.2.29
Catalytic Activity: [L-4-(L-arginin-2-N-yl)aspartate](n) + ATP + L-aspartate = [L-4-(L-arginin-2-N-yl)aspartate](n)-L-aspartate + ADP + H(... |
A0A916J5X9 | MKPEKQLVRSAFARAAPHYDAVADFQRETGERLSAQCQMDSLPARVLDAGCGTGHGLQLIAGRWPKAEIVALDFAAPMLHQLPPGTSTLAVCGDIEALPLMNASVDLVWSSLAIQWCDTGRVALEFQRILRPGGHLAATTLGPDTFAELRRAFVGVDEFRHTNDFIDETRLRTALGSAGFDLLTLRRVGMQRHYPDLRSLLASVRELGASHVAARNRRPGLMGKTAWRRFSDNFERMRTSCGLPLTYDTYFILAQK | Pathway: Cofactor biosynthesis; biotin biosynthesis.
Function: Converts the free carboxyl group of a malonyl-thioester to its methyl ester by transfer of a methyl group from S-adenosyl-L-methionine (SAM). It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway.
EC: 2.1.1.197
Catalytic Activity: malony... |
A0A1R3TFM9 | MATHASSCSEKQVDLQRSVRVLRIYLDGAYGIGKSTCASVMTESVLYPTLYAREPMAYWRRFFFPSDIVSDVYSTQERRRTGKISEEDADAVTTSLQVRFASPYLTLHAATRALFGQETYTQQRPDITLIFDRHPIAAILCFPAARYVVGDMSIEAFLALISTLPEDSSGANIVVADITEEEHVRRLQGRNRRGEKIDMNLLRALRNIYIMLINTISYARLRSQVSWRDDWDSIPTFDDTVRDRITSQRSYFISEPPQLRFSLLTLLKTPVICDGDGFVRRIHELAIDNLMNKLALLHVYYADFDNKTPKHCAESIRCMT... | Function: Catalyzes the transfer of the gamma-phospho group of ATP to thymidine to generate dTMP in the salvage pathway of pyrimidine synthesis. The dTMP serves as a substrate for DNA polymerase during viral DNA replication. Allows the virus to be reactivated and to grow in non-proliferative cells lacking a high concen... |
A0A6A1WPC5 | MELSTVLFNQLKIVSESYRVGLPLVFKSSFDKANRTSSKSFRGPGMIEGLKILEKVKIAYDIPTVTDVHESIQCEAVVKVADIIQIPAFLCRQTDLLVAAAKTGKIVNIKKGQFCAPSVMVNSAEKVRLAGNPNVMVCERGTMFGYNDLIVDPRNLQWIREANCPVVADVTHALQQPAGKKLDGGGVASGGLRELIPCIARTAVAVGVDGIFMEENGRWKLGFGEEEKQGFEDEASR | Catalytic Activity: D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + phosphate
EC: 2.5.1.55
Subcellular Location: Cytoplasm
Sequence Length: 237
Sequence Mass (Da): 25799
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A0A2M7FBQ1 | MSYKVLARKYRPQSFEDVIGQEHITRTLRNAVESKRIAHGFLFSGMRGVGKTTMARILAKALNCEKGPTVSPCNICSHCTEITQGNSIDVIEIDGASNTGVDDIRELRENVLYAPASARYKIYIIDEVHMLSKSAFNALLKTLEEPPPHVIFVFATTDPHKVPVTIQSRCQCFHFRSIPVQKITEALLRIAEQEGFAIDQESARLIARASEGSMRDAQSLLDQILSFCGDKITVADIKLVLGIIDPEVLDECSIGLIEQDAERVLNLVEKLNSLGVDLVEFCRELQLYFRNLLMIKILKSPKTVIHIEGEEIDKLRPISE... | Function: DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity.
EC: 2.7.7.7
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Length: 550
Seq... |
A0A961Z879 | AETLAMIETGTAKKGDVLATARIAGIMAAKKTSELIPLCHPLPITKATVDFTISAEPPGLHVAAEVKVAGQTGVEMEALTAVSVACLTIYDMLKAVDKAMHFEGIRLIEKSGGRSGHWRASDPSLLGTRPSAKKAKS | Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
EC: 4.6.1.17
Catalytic Activity: (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate = cyclic pyranopterin phosphate + diphosphate
Sequence Length: 137
Sequence Mass (Da): 14323
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A0A5D0MG72 | MQFLVDTNYKFVTKKRRRIGFVFSIILIIIGIVFYLINGGFNLGIDFEGGATLHYKFKQEVKINQIRKELNEAGYSGAIIQRYGSPKDLLIKIEQGKDLSRLKNYINGKYSNINLESEEKVGPSVGKDLQKNSLYAIIIALIGILIYVSWRFQFKYSIGAILALLHDVLITLGAFAVFQFEFDRSVLAAILMVIGYSLNDTIVVFDRIREYMRTERPRSDEHYETTVNKAINNSLSRTIITSLTTLMVIIVLYLAGGQILRNFSFALLVGVVVGTYSSVFISSPVLIEAHLKVSDN | Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA.
Subcellular Location: Cell membrane
Sequence Length: 296
Sequence Mass (Da): 33430
Location... |
A0A1G1N6A3 | MIFYIIALSTCLFAFLTVASRDVFHSAVWLSLTLLSVAAIYFYLDAQFLGVIQVLVYIGGIITLFIFAIKLTAKIGDKTIQQANEQALLSGLAAFVFFIILFKMIALHPWAELQPQAPVFSLEDIGKSMLTTYVLPFEFLSLLLLAAMVGAIVIGKVRK | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy i... |
A0A1G1NAQ7 | MKSNISLQFFISQYTMKRPADWSGHFASAQPVDVEIGFGNGDFLVRTAQTQPQRNFVGIEQQWERVYKTLKKVNRSEIDNVRVLLVDAWVALERLFLPRSIERIYCLFPCPWPKKEHAKHRLFSQSFLKLMNSRLKPHGQATIVTDHQPYYAWVLEQGEGTGFLIEAKEIATQYNTKYERKWVEQGQEHFFELALTKKEHVDVPVKEDVTLQPYFIDTLDPRQFKFEKVSGPTTVVFKELIADEKQKKAMLHLVVAEEKLTQHLWVAIFPIEGRWCIAPALGQNFIPSQGVAEALQAVYQACQGS | Pathway: tRNA modification; N(7)-methylguanine-tRNA biosynthesis.
Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
EC: 2.1.1.33
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
Sequence Length: 305
S... |
A0A924KVE3 | MTPFTAVDHAMMARAIQVAEQGRALATPNPFVGCVIVKHGRIIGEGFTRAGGRPHAEADALANCHESAAGATVYSTLEPCALHANSRGPACSDLLIAAKVARVVSALHDPFEGVDGKGHENLERAGITLDIGLMSAEVERQLKAFLQRVRIGRPYVTVKVAASLDGKTALANGLSQWITSAEARRDVHAMRRDSCAVMTGVGTLLADDPALTVRDVECQRQPLRVLLDSRLDVPDEAKILAGGNTLVVTATGPEARAETLRARGIDVCRVPTEALKGKVDLPAMMQMLGARKLNALLVETGAKLNGSLLAAGVVDEIVAY... | Cofactor: Binds 1 zinc ion.
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 2/4.
Function: Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5'-phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)-pyrimidinedione 5'-phosphate.
Catalytic Activity: 2,5-diamino... |
A0A916M1H2 | MFSFVVCSVDAAKLAVMKPSLAACAGSGRYEVVDIDDAPSLCAGWTRGLERAAGDPVVFCHDDISFVVPDLLARIARHLERFDVVGVVGTDRCAGADWSEARIEHAYGAIVHDRGRSPDFCFYGAGADAVADAVGGIQAMDGVLLAARRAAAERIGFDAATFDGWHGHDADFTFRARLAGLRLGVALDPRSCIARWGAMTGDAAPPPAFRGKTCLEPDSGMRAAGRRVHPDHCARRHRCRLRPREPRPPARVVARRGPASPACGRAAARCRAQRLVPLWRPASVQRVPRRAAFRVGAVESTSRWAPAMPDHADVDTLRLP... | Function: Participates in initiation and elongation during chromosome replication; it exhibits DNA-dependent ATPase activity and contains distinct active sites for ATP binding, DNA binding, and interaction with DnaC protein, primase, and other prepriming proteins.
EC: 3.6.4.12
Catalytic Activity: ATP + H2O = ADP + H(+)... |
A0A8C7DVI7 | MDKLKSVLSGTDGPNENGNILQAANEASTLGWGTRVKGFIICFVIGVTCSILGVCMLFIPKVGILLFIIFYTFGNICSLCSTMFLMGPVKQLKRMCDKTRALATTIMLTCLVLTLCAAFWVWLVIYPFYQRCHPEDYYHVCKVKTPDWPVSLKEQLCLGYKGYLSGLSFMDTCLKLNVVLSITLTRCLRTGQPTPYSKIVLPLYPSI | Function: May be involved in fusion of retrograde transport vesicles derived from an endocytic compartment with the Golgi complex.
Subcellular Location: Membrane
Sequence Length: 207
Sequence Mass (Da): 23123
Location Topology: Multi-pass membrane protein
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Q5H0W5 | MLLFREPTPFQRLLPSHERRRPLVPPTRIAPDLRPFYCALGAVVPCAGRVAVGRGHLAGLVCGTGGLPARRQLPHSLHPCAERLDEPVRVRADGTVRGHRADLADQDLRDPGDGVRADRCGIYRDYPAHRQHLGQADVGRLVGLGPAPDHRIDPAVSLSGRDRPVSRHRRPPSGGTRGGIAGHRRGGAAAGHPLFGGMVEFAASGPEHPPAWPIDDRCQHAAAAVVDGDRHQVLVCRVAADARARRQPAPRGRQGLDRARCAGACGMSYLPYVIAAYAVFVVVLLWDLIAGRWQVRRALKTAQARRLRERKRAVPSDAEL... | Function: Required for the export of heme to the periplasm for the biogenesis of c-type cytochromes.
Subcellular Location: Cell inner membrane
Sequence Length: 322
Sequence Mass (Da): 35012
Location Topology: Single-pass membrane protein
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A0A9E0CER7 | MHKADEFSSVFVFRKVRLGKYFKLHYKPNGLELSRLGFMVSKKVHKRANQRNYIKRTIREYFRTHQDSWLPIDLIVRAQRHFDQRQLEQVLAELEQLCAKFKELNAAQNSRSANSLLSTLP | 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... |
A0A6P1UBE9 | MRVWLVVLLLTLSACTTLPPPPATAPGSAERQWRQHQQSLADIDAFRLQGRLADGSGRSANLDWQQHADGRFTLNLRGPLGIGAVSIEGDAHSVIVHDKQGAHPTDDPQGWMWAHLGWALPLDALRHWALGLPAPGLIDQLTLNAEGQLLDLQQQDWTLRYDAYQTVGLLTLPRRLQAQSQTIRLRLVMDRWAVTEPHTAPSPPAASTTDAPQ | Function: Plays a critical role in the incorporation of lipoproteins in the outer membrane after they are released by the LolA protein.
Subcellular Location: Cell outer membrane
Sequence Length: 213
Sequence Mass (Da): 23435
Location Topology: Lipid-anchor
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A0A3R9PT48 | MRNIWLILTYLYRSKEVLFAVGWFLEKPNGKRLREFCGFCASLLSTLIVPAMAYTMLLRNCGQLLTLAGPATHLPLAGENQRNWRVIPDGYVACVDDRIVATGPMAELDDTLVATATIVLDASGQVVMPGLVECHTHLVFGGNRAHEFQRKLQGETYLDILASGGGILSTVRATRAASDEQLLEQALHHLKGFREYGVTTLEAKSGYGLDAETELRLLQVAREAGRRQPVRVVPTFLGAHVPGPEYRGHPADYLHMLVQEVLPNIYPEEVPFVDIFCEEGAFSVAEARRYLEQARALGFQLKIHAEQLHDLGGCEMAAEL... | Cofactor: Binds 1 zinc or iron ion per subunit.
Pathway: Amino-acid degradation; L-histidine degradation into L-glutamate; N-formimidoyl-L-glutamate from L-histidine: step 3/3.
Function: Catalyzes the hydrolytic cleavage of the carbon-nitrogen bond in imidazolone-5-propanoate to yield N-formimidoyl-L-glutamate. It is t... |
A0A3D3SS72 | MAENLIDEIKRRQLELLRHQRLYHADDAPEISDETYDQLARELEGLEARLEPTHPLKRQSPLGKVGSNPRSGFATVAHERPMLSLANIAGQASVNQFGERLASQLELKGSQAQGLRYAVDLKFDGLALSLRYRAGRLVMAATRGDGTLGEDVTANVEAARIVPLQVNENNSLGNEFEVRGEVFMARSDFKQLNADQQARGEKTFANPRNAAAGTMRQLDSSIAALRPLRFFAYALLGGSPGTAQQLSTHSQQLDALKRAGFPVCDIRCAEASIDQVIAFIDRAETARSDLDFDIDGVVVKLESLTLQEQLGYLARTPRFA... | Function: DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA.
EC: 6.5.1.2
Catalytic Activity: NAD(+) + (deo... |
A0A257FXF0 | MKLADNKATLSFSNGSPSVDMPVYSGNIGPDVIDIRKLYAQTGMFTYDPGFLSTASCQSAITYIDGDKGELLYRGYPIEQLANKADYLDTCYLLLNGELPVGQQSKDFHKLVNQHTMVNEQMQFFLRGFRRDAHPMAVLTGLIGALSAFYHDSTDINNPEHRHIAAIRLIAKMPTLVAMAYKYGVGQPYMYPRNELSYAGNFLRMMFGTPCEEYKVNPVLERAMDRIFTLHADHEQNASTSTVRLCGSSGTNPFAAIAAGVACLWGPAHGGANEACLNMLEDIQKMGGISKVGEFMEKVKDKNSGVKLMGFGHRVYKNYD... | Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate from oxaloacetate: step 1/2.
EC: 2.3.3.16
Catalytic Activity: acetyl-CoA + H2O + oxaloacetate = citrate + CoA + H(+)
Sequence Length: 345
Sequence Mass (Da): 38288
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A0A317D561 | MDKLKSPEKPFEISKWEVWEAFREVKRNQGAPGVDGQSIADFEADLKGNLYKIWNRMSSGTYFPPPVRAVEIPKQHGGGTRMLGVPTVADRVAQTVVARHLGIRVDPIFHEDSYGYRPNRSALDAVQRCRQRCWKKDWVIDLDIQKFFDSVRWDLIVKVVQAHTDAVWVTLYVERWLQAPLQLPDGTLQERDRGTPQGSAVSPVLANLFMHYAFDTWLARTFPDVQFERYADDAVVHCVSERQAREVLAALGNRMDEVGLRLHPDKTKIVYCKDGNRRGSYEHTSFT | Function: Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be i... |
A0A077FHK8 | MESSSKRLSPRYNIVEMEEKWRSNWEQTSLYKWDEHAAREENFVIDTPPPTVSGMLHMGHVFSYTQTDFIARYMRMIGKNVFYPMGFDDNGLPTERLVEKLKKVRAIDLPRNEFIEICKEIVLEAEKEFHLLFKSLALSVDWSLEYQTISNHSRKISQLSFLDLIQKSRAYRQLQPCLWDPVDRTALAQADLVDKELSSHMNEIYFTTEDGEELIIATTRPELLPACVAVFYHPEDMRYKHLQGKHAVTPLFEMKVPIIADNKVIPEKGTGLVMCCTFGDISDIEWWKIYKLPERVIIDHSGRLTNLDNIKFADRLIGLT... | Function: Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA-dependent manner.
Catalytic Activity: ATP + ... |
A0A2T0BFP4 | MKVEIKDVKYIAKLSKLSFTEPEFQTLIGEFESILSHFESIDNFDLSDINLDLNADDLKPVLREDKVKCFEDKKKLLQNVKSMRGTAIIVPKIIE | 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 ... |
A0A2M7FA04 | MRRHKGIARAAGIIGASTLMSRIMGYVRDMVMSGLFGAGMMTDAYIAAFRIPNYLIRIFGEGTLNASFVPVFTETLNRKGREHAWDLANVVITVIFTILSLFVILGMIFTPGLVKAITPGFTKDPMQFNLTVLLTRIIFPVAVFVGLSAASMGILNSLNHFGSPAIAPSFFNLMIILSALFLSPHLPVPITSLAIGVLMGGLLQISVQVPFLIRKGFRFRYRLDLAHQGMRKIFSLMVPGVIGQSVLQINLFIGNLLASFLPAGSITYLFFADRLVQFPLAVFGFSAATAMLPALSVHASNKNIPEMVETLSKAMRMVLF... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Involved in peptidoglycan biosynthesis. Transports lipid-linked peptidoglycan precursors from the inner to the outer leaflet of the cytoplasmic membrane.
Subcellular Location: Cell membrane
Sequence Length: 531
Sequence Mass (Da): 58298
Location Topol... |
A0A0D3V792 | MATYLPIMLDCEDRLCLIVGGGTVAERKAIRLLDAKAKVTIISSELTKKLLELYESGKIHWIRRNFESDDTDGYSLVHATTHNERVNVEIAKEASDKGIPVNVASDSAASTFMNPAVIKRGRLTIAVSTEGAGPAAAVHICSLLEEQFGEEYETYLDFLYSLRTEIKRAVASPAQRHKLLKKLIQCHILDDIQHGRYVEWSQADIQTWIENNEEE | Pathway: Porphyrin-containing compound metabolism; siroheme biosynthesis; sirohydrochlorin from precorrin-2: step 1/1.
EC: 1.3.1.76
Catalytic Activity: NAD(+) + precorrin-2 = 2 H(+) + NADH + sirohydrochlorin
Sequence Length: 215
Sequence Mass (Da): 24115
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A0A077FII1 | MSNIDSIHNRRPLSPHLSVYKIQITSALSILHRFSGIVLFVGALLITWWIILGVYSAFNPTLVKWTFFSTILGKIMLCGWSFALFFHLFNGIRHLFWDAGFGFQKKQFNWSGIVVIIASILSTVLSWSIVLYN | Cofactor: The heme is bound between the two transmembrane subunits.
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle.
Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH).
Subcellular Location: Cell inner membrane
Sequence Length: 133
Sequence Mass (Da): 15224
Location Topology: Multi-pass me... |
A0A5D0MHZ9 | MQELIITKIFSFGAAHNLDSYHGKCENLHGHNYRLEVSVKGVPDNEGMVIDYKVLKEIINKTVIEKLDHKYLNEVLDFSPTSENLLIWMKEKLENKLNSENYKLYKLVLWETESNKASIYV | Cofactor: Binds 1 zinc ion per subunit.
Pathway: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
EC: 4.-.-.-
Catalytic Activity: 7,8-dihydroneopterin 3'-triphosphate + H2O = 6-carboxy-5,6,7,8-tetrahydropterin + acetaldehyde + 2 H(+) + triphosphate
Sequence Length: 121
Sequence Mass (Da): 14146
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A0A7Y3KGR0 | MMRWGALVVAAGEGRRFGGFKQLVEIAGRPMLAWSLDAVAAIAAFSVVTVVTAREAFEDVERVARPMLGERLQPIVEGGATRQASVRNGLRALAGRCDALAIHDGARPCVRVEEIEAGMREVLPGRAALLASRIVDTLKETEAGSLLVRATLPRENLWGAQTPQFATYADLLAAHDRAVVSGVEATDDIALLEAIGVRCTIIPSTAENLKVTEQSDRDLAAAILRARAQRIGEAR | Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 2/6.
Function: Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
EC: 2.7.7.60
Catalytic Ac... |
A0A950XCR4 | MNKTAAETAEYLDIFLAQLPSLPSDVEIVLAPPFTSIARAASKIKGFGVRLGAQTMHWELRGAYTGEISAPMLLEFGVSHVILGHSERRAYCDETDRTVNLKVHTALQQGIVPIVAVGETLAQRRAGITDDHVVAQTKAAFDGVSAGALPGVVIAYEPIWAIGTGENCDPVEANRVMATIRSSLQGLDETPILYGGSMNTDNVGAYAAQPDINGGLIGGASLDPNGFAQLIRSAAVSP | Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Function: Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
Catalytic Activity: D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate
EC: 5.3.1.1
Subcellular Lo... |
A0A0R1V9R5 | MQNYGLQRSYKEENAMADSSARRIEYEPSKQNGSKKHQRIILDPRKVPYSLVEKTLIIVGSVITLGMMIFLVSSSISATSAQHELTKTQQSVTKEQNRVTDLRQEIGELTSTTRLNKIARQKGLTLINKNIRTIR | Function: Essential cell division protein.
Subcellular Location: Cell membrane
Sequence Length: 135
Sequence Mass (Da): 15348
Location Topology: Single-pass type II membrane protein
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A0A916J7C1 | MKLIKEVLLGLALALLVCASASAAGPQSAPRVEMKTSLGTIVVELNPAKAPKTVENFLRYVKSGFYNGTIFHRVMPGFMIQGGGFEPGMKEKPTRDPIPNEGKNGLRNMAGTIAMARRGDPDSATAQFFINHVDNPMLDYPNPDGAGYAVFGQVVRGMDIVQKIAQVRTGNAGMFENVPLTHVVIESVKLLPDSK | 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: 195
Sequence Mass (Da): 20969
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A0A1G9CST1 | MSFADRDGLIWLDGRLVPWRSARLHVLSHGLHYGGAVFEGERAYGGTVFRLRAHTERLRASAAAMGMTLPFSDAEIDAATVEVLAANGIGDGYVRPVVWRGSGQISVSGAGNTVHAAIAPWEWPAVFDGDAKRRGIALTVASWRRPHPSAFPVTAKSSALYSAGTLARGEAEARGCDDALLLDWRGDVADATGANVFLRFGDELHTPEPGTMLAGITRAAVIELAAREGIAVVERRIAPDEIAFADEAFLTGTAYEVQPVRSIDGTAFAVGETTALLMDRYADLVRPKTPAPAVPRPAGPPTVALLGGKLNLVERARALG... | Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 4/4.
Function: Acts on leucine, isoleucine and valine.
EC: 2.6.1.42
Catalytic Activity: 2-oxoglutarate + L-isoleucine = (S)-3-methyl-2-oxopentanoate + L-glutamate
Sequence Length: 691
Sequence Mass (Da): 73380
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A0A9E3DBW3 | MPKAALFSLSDKSGAAELAQVLVRRGTEIYATSGTRAYLESHAVRTRELEELTGFPALFGGRVKSLHPKVFGGILYDRSDPGHVGQAEKYAIPEIVAVVVNLYPFEATVGNAGATLNDAIEQIDIGGVSLLRAAAKNFDDVAVLTHPSQYEEYCHAVEAGEVPPALRRKLAIAAFERTAEYDVAISHYLAAAGEVLPSDLPGALALALPLAKRLRYGTNPQERAAFYLDRVDLLPEQLHGKALSYNNLLDLDATLRLLSRARLGAHFSNERERFVRAAVVKHAVPCGVAQRSNIGIAVREALHTDRVSAYGGIVASDGAI... | Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl THF route): step 1/1.
Catalytic Activity: (6S)-10-formyltetrahydrofolate + 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-c... |
A0A926H4P6 | LKVKVWQGIFGKRGDLWIGYTQKAHWQLYNVRYSRPFRELNYEPEVILNFPTNFPLLGFRTRMLGLAFIHQSNGRTLPLSRSWNRLVAHAGFERKQWTVLLRGWYRLPDEEDENPAIADHVGRADAVVIYKRGRSLVSLLGSHSLRGGTRNRGQVQFDYTYRITGNVKANLQILNGYGETLIDYNHNQTTIGLGVSLVEWL | Cofactor: Binds 1 Ca(2+) ion per monomer.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+)
EC: 3.1.1.32
Subcellular Location: Cell outer membrane
Sequence Length: 201
Sequence Mass (Da): 23259
Location Topology: Multi-pass membrane protein
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M6ZEH2 | MKEYQRFSPDSVNGSDSTAGLKRNLEMDDNKIIVTTIQKLNNLIKSESDLSIYNKQVVFIFDEAHRSQFGEAQKNLRKKFKKFYQFGFTGTPIFPQNALGADTTASVFGRELHSYVITDAIRDEKVLKFKVDYNDVRPKFKEIETEQDEKKLTAAENKQALLHEERIREISQYILNQFKQKTHRLQPSSKGFNAMFAVSSVDAAKLYYESFKEVQKDQDKPLKVATIFSFSANEEQDAVGEIQDESFEVSAMESTAKEFLSAAINDYNIIFQTNFGVDSNSFQNYYRDLAKKVKDREIDLLIVVGMFLTGFDAPTLNTLF... | Function: Subunit R is required for both nuclease and ATPase activities, but not for modification.
EC: 3.1.21.3
Catalytic Activity: Endonucleolytic cleavage of DNA to give random double-stranded fragments with terminal 5'-phosphates, ATP is simultaneously hydrolyzed.
Sequence Length: 686
Sequence Mass (Da): 79185
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A0A4Q3UVR6 | MKVCVVGGTNGQVARSLAQLDSPECTIIVRGRPEADLASPATLPAILKALAPDVVINAGAYTAVDQAESDADAARAINAHGVAALGAACANVGIPLVHISTDYVFDGAKTAPYIESDPTGPLTVYGATKLEGEKALQESGARHVTLRVSWVHAPEGKNFVRAMLRLAKTRERINVVADQIGRPTYAPHLAIALRDIAIRLVMDPLAPTGVFHLTGSGGPCSWRSFAQTIFEASRVRGGPTAIADPINTTAYPTPAKRPANSILNCSRMTQLYGLTLPDWRQGVGECVTEIGQRGWE | Cofactor: Binds 1 Mg(2+) ion per monomer.
Pathway: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
Function: Catalyzes the reduction of dTDP-6-deoxy-L-lyxo-4-hexulose to yield dTDP-L-rhamnose.
EC: 1.1.1.133
Catalytic Activity: dTDP-beta-L-rhamnose + NADP(+) = dTDP-4-dehydro-beta-L-rhamnose + H(+) + NADPH
Seque... |
A0A7X8XMU0 | MSDRPHTEKSPDQPSEPPQAPKTRRERIPRRRGPSGGYYLECFLREVLINIRRNPLMSVASISTVMVLTLILGFFVVLVANLDSLSRELAGEMQVKAYMSADFQREDAGAFHASLMKIEHVEGTHFVSKDTAFKRLRERLGSRITLDDLSHNPLPDAFEIRVDQPKALDVVAAKVARLPGVGSVDYGRDVARKLMALNQVVRVVGMVILGLLFASTLLIVSNTIRLTVFARRKEIDIMQLVGAADWFIRWPFILEGVAQGLVGAAMAATVVDVAYRLVVPQLHKTVPFLPILPPGEVLPFLNLGLVGLGCAVGALGSLIS... | Function: Part of the ABC transporter FtsEX involved in cellular division.
Subcellular Location: Cell inner membrane
Sequence Length: 327
Sequence Mass (Da): 35943
Location Topology: Multi-pass membrane protein
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A0A7X9AEK2 | MLDETLAERYSEALYQMAREAGEAGQQFRELQKIVELFADHRELRHALKSPAISRDVKKNIIRHLAEGRVQPRTLHFLYLVVDKGRELYLPAILRLYERKLHSDEGIVEAKVEVAFPLDSTMEDQIRAHLAELTGKKVQMEVRVRPELIGGAVITVGDRLFDGSVRTHLEKMRERLAQA | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
I6PME5 | LYLIFGAWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGXXDMAFPRMNNMSFWLLPPSFILLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGISSILGAINFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQH | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
A0A950F722 | GDTVAIHDGKVAVNGSFVDEPAFVLADHSSMGSLRVPAGCVFTLGDNRAESDDSRVFGPVPESTIIGKAVFVIWPLGEIKRIR | 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: 83
Sequence Mass (Da): 8796
Location Topology: Single-pass type II membrane protein
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A0A418W2Y4 | MFSDVSVRGGAPLSFAGRPSLSRETAPVPHDRSDGACKDAAPDVEVGYPTKRRILELLDLNAKIVARAPVGIIVYAATGECVLANPGSAAIVGGTVEDVMRHPYTELRFWRETGLLQSARDALATGTTRNESVHVVTAEGQDLWLDCDLVPFSSEGNARLLYIMVDVTARRLAEIELVEAKHEAELASQVKSEFLANMSHEIRTPMTAIMGFTSLLEEAPLESRERDYVAKIKTSAASLLGILNDVLDFSKIEAGRLELEQTAFSLQDVMRSIAVIVGANAALKNLEVVYDMAPDVPDGLTGDPLRLQQILLNLAGNAVK... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Cell inner membrane
Sequence Length: 918
Sequence Mass (Da): 97963
Location Topology: Multi-pass membrane protein
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A0A2M7ALI7 | MNIVDHIPVLVNEAIAGLKIKKVGVFFDGTLGDGGFATEILKKLQGGTFVGLDVDPQALERSFNKIRSLKNFSKVSRRKEEFLLEDKNLKVFLLQRNFAQIAEIVQEKNLGGIDGIVLDLGFSSFQLEESRRGFSFLKQEDLDMRFDPRLDNRASDIINQLTKEELNEIFRFLGEEPLSRIIADTLVRQRRLKPIIKTQELVEIVKDVYGKKYRYRSKRHPATRVFQALRIAVNDELRNLQQALNSSGKVLNFGGRLDVISFHSLEDRIVKNFFKRSDFKIINKKPIIPSEDEKRQNPRSRSAKLRIGEKIKNGKKKNL | Function: Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
Catalytic Activity: cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(4)-methylcytidine(1402) in 16S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.199
Subcellular Location: Cytoplasm
Sequence Length: 319
Seque... |
A0A8S0TIQ8 | MAGGGMIAPSVNKGYPGKFTGRVFITCIVAATGGLIFGYDIGISGGVTSMPPFLEKFFPDVYKKEVLNIGGTNQYCKFDSQKLTMFTSSLYLAALVASLIASTVTRKLGRRPSMLLGGALFLAGAIVNGLAQNTTMLYVGRALLGVGVGFANQSVPVYLSEMAPYKYRGALNMVFQLSITIGILAAYVINYFTAKMESGNGWRYSLGCAGVPAIIFVLGSLCLPDTPNSLIERGKNDEARKRLQNIRGVDNVDEEYNDLINASIESQKIKHPWAKLFSRKYRPQLLFVSFIPFFQQLTGMNVFMFYAPILFKTIGFGANA... | Catalytic Activity: NH4(+)(in) = NH4(+)(out)
Subcellular Location: Membrane
Sequence Length: 379
Sequence Mass (Da): 41381
Location Topology: Multi-pass membrane protein
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A0A5M9HY15 | MSEPDKAQTRMTEERNMRLFIAIKLSDEMKKALINCMHNLKKQGVEGNYVPAQNLHMTLAFIGEYDDPEKVKKVIKKVPMPEFRLNLSEKGNFGNILWAGVKGNQKLKAYVKELRSALDEEGIPYDRSSFVPHITLIRKVSAKKPYQVHLGKAVMTVKHASLMKSEQKKGKVIYQEL | 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: 177
Sequence Mass (Da): 20258
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A0A849IML6 | MPDFPDLSGWLRYIEGIHPKTVEMGLDRVRAVKEKMGLSPSFPVIAVAGTNGKGSTCAMLESLLHHAGYRTGCYTSPHLLRFSERIRLDRREAQDVEICSALARVEQARGETSLTYFEYTTLAAVQLFIDQRVDIAILEVGLGGRLDAVNAFDADCAVITGIDFDHMDYLGNTLGEIAAEKAGIFRNGHCAVSATDLVLDPAREAGARLFLAGRDFSWENLGTSWNYHGMKRKLDVLSIPSLEGSVQLSNASVALAALDCLGIFPDEKTASAAFLDLELRGRFQKFGDVTLDVAHNPQAARNLAANLKQNPGSGKTVAIF... | 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 ... |
A0A3N5FK24 | MTRRTYASLRGSCALGAGSVPGFRADRLRARRRGRIIHVTGIRAVSIEVPAGEDAAEPPHRASRLGTHAARGLLVGALYFVAAAFGLQLAFADSNVSLFWLPTGVAVAGLMLWGAPVLAVLVPTVLALHIGLGAPAWAAAAIALGVCSGYWLASRILIRLGLAPDFRSTDDFRTLGLAAVIGMLVPPSAGIGMLALAGKVPADRMLEGWLGWYAGDVLGVLLAAPLLLALHERWRTGTLPWQPAGRAAASSHDMRRDGYAATAVAALLALGVALTLSTASAYATLGIVAMLVLQLATTAASAWLGMLGAWTALVAVALAV... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 1022
Sequence Mass (Da): 108357
Location Topology: Multi-pass membrane protein
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A0A3T1C8S9 | MTSASRPVVIAGNWKMYKTIEEATAFVPELVSLINTPQAQIYLAVPFTAIKATSEAAKDTVLVVGAQNINDASEGAFTGEIAGKMLKDAGAEFVIIGHSERRRLFYETDDLINKKIKRALEDNLQVIFCVGESKKEREAQQTHEVLARQLKEGLADISVEQLRHIIIAYEPIWAIGMPQPAGAETAQDAHAFCRQLINEGWDEKAAEQIIIQYGGAVKPENAKKFLEQPDIDGLLVGGASLSSKDFAQIINCFNSIYEEGITK | Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Function: Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
Catalytic Activity: D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate
EC: 5.3.1.1
Subcellular Lo... |
A0A849IFD9 | MENIEQRVKKIVAEQLGVSEAEVKNSSSFVDDLGADSLDTVELVMALEEEFECEIPD | PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine of apo-ACP by acpS.
Pathway: Glycolipid biosynthesis; KDO(2)-lipid A biosynthesis.
Function: Carrier of the growing fatty acid chain in fatty acid biosynthesis.
Sequence Length: 57
Sequence Mass (Da): 6330
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A0A1Y2T1H5 | MQVYRGMDIGTAKIRPEEMGGVPHHLIDIKDPDEEFSVAEFQARVDELIPQICARGRLPMLVGGTGLYVRAVVEKYTFTPMEPDPELRARLRQEEERHGPGYLHARLAEVDPVSAARLHPNDLFRIIRALEVYERTGIPISATQIAAQSEPRYDDLMIGLTMDRQQLYARIDERVDAMLAAGWVDEVRRLLSRYPPNLRSMQALGYRELVLYLRGFLTWDEAVALIKRNTRRFAKRQFTWFRR | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
EC: 2.5.1.75
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylall... |
A0A961ZYU2 | TMFLMWLGEQITQRGVGNGISLIIFAGIVAALPSAIAGLFEMARTGALSTFLLIALIVLMLAVVAAIVFMERAQRRLLIQYPKRQVGNRMFQGDTSHLPLKLNSSGVIPPIFASSLLLLPITAASFTAGANNQGPEWLNTIVAALGRGQPLHLIVFVALIVFFAFFYTAVVFNPKETADNLRKYGGFIPGIRPGEKTAEYIDYVLTRITVVGAIYLAAVCVLPEFLISYAAVPFYFGGTSLLIVVSVTMDTVAQVQSHLLAHQYEGLIKKAKLRGASSNRGRK | Function: The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring compos... |
A0A1Y2T7C7 | MAHLALYREYRPQRFGEVVGQEHITRTLRNAIVQGRLHHAYLLSGPRGTGKTTVARILAKAVNCLNPQDGEPCNECEACRRITSGEALDLIEIDAASNRGIDEIRDLRDKVNFAPVELKYKVYIIDEVHMLTEPAFNALLKTLEEPPAHVLFVLATTEKQKLPITILSRCQPSTTGGCPRTRSWHGCGRCAGSRDSRPARKPCRPLPATPTAACATPCRCWTR | Function: DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity.
EC: 2.7.7.7
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Length: 223
Seq... |
A0A962FNM8 | ILRVPVAVAIFAASYFYATFTGLLPQLSLASLAVNGVGGFLLVSIPTFILMAELMNRSTITERIYSFANGLVGHVRGGLAHVNVLTSLIFAGMSGSAIADIAGLGRIQIRAMTQAGYSLPLSAALTAASATIGPVLPPSIIMVVFASMAQVSVGAMFLGGVVPALIMAAAMSITVALLSLRHGEWVKQPRATWNERGHRLMQALPALLTPAILLVGFLSGYWTPTEAGAVASLWAFLIAKYYYRDLSWRDVGDVLKRTAVSSGNILLIFAAAHMLSQIVALEGLATDLSRMLQTFTDSPTVVLLLINALMFIGGMLMEPT... | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 414
Sequence Mass (Da): 44147
Location Topology: Multi-pass membrane protein
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A0A9E0Z3S3 | MVESVQNLFGTRKIRRKPRILTKEEHQIDINKVSPFAVSVCQKLKDAGFKAFIVGGAVRDLLIDHTPKDFDVATDATPEQIKKITRRAIIIGRRFRLVHVTRGAETIEVATFRGLRQDGVEKDGQGRVIDDNVFGEQFEDAARRDFTVNAMYYDPLEEEVYDYHNGLLDIKKKRIRMIGDPELRYREDPVRILRAIRIGAKLGFKIDPKTSKPIREMQKLLLAVPEPRLFDEIMKMLMSGASVECMRLLDEEGVNVNIPLLKEYLSAKNDPFLLKAMEKSDARVAHGKPISQSFIFATLFWSLVKKEVEKVKKEVPDVTI... | Function: Adds poly(A) tail to the 3' end of many RNAs, which usually targets these RNAs for decay. Plays a significant role in the global control of gene expression, through influencing the rate of transcript degradation, and in the general RNA quality control.
EC: 2.7.7.19
Catalytic Activity: ATP + RNA(n) = diphospha... |
W8EZH4 | MERLFITGIGTDVGKTFVSAILTEALQADYWKPVQAGLTPTTDAATVRGLVQNPISHFWPERYRLQLPASPHAAAAAEGLTLRPEDFQLPQTDNHLLVEGAGGLLVPLAPGFLLADLARQFDLDVVVVSRNYLGSINHTLLTLEALQARGLRVRGLVFNGEPTPATETFIAEYTGVPLMPRILPEPEVAPAVVSRYAAEFRAWFGL | Pathway: Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 1/2.
Function: Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to form a ureido ring.... |
K6XN79 | MLGLKIDLRIAPEAQRNGPYVFIANHQNSFDIFTICAAALKGTVTVGKKSLKWIPIFGQVYWLSGNIMIDRKNSGRALDTLKNTVRKMQKRKLSVWFFPEGTRSYGRGLLPFKSGAIRIAKLAKRPVVIVAASNLENKIKLNRWDNGTLIIDVGKPYDLSGERTTKEWTEHFHALMAEKIAQLDSEVAAGNR | EC: 2.3.1.51
Catalytic Activity: a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphate + CoA
Sequence Length: 192
Domain: The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate.
Sequence Mass (Da):... |
A0A8H3ETA6 | MAGEFAGTFLFLFFAFTGTQVANSQTQGATSTTIAQGSNPAQLLYISLCFGFSLAVNAWVFFRISGGLFNPAVSLGMMIVGAVPWPRGCLVIISQLIGGIASAAVVSALYPGQLNVRTTLGAGTSHAQGLFIEMFLTAELVFTIFMLAAEKHKGTFIAPVGIGLSLFIAELSGVYYTGGSLNPARSFGPCVVVRTFEDYHWIYWVGPLLGSLLASGFYKFIKMLEYETANPGQDFDENETQLFDPERDTNRPMVNFSTASESGSQAITKSRPISGDTFAEYRREEIPLQQVRKQHSRSKSGEEENHIQDRPSSNPTKQQP... | Catalytic Activity: H2O(in) = H2O(out)
Subcellular Location: Membrane
Sequence Length: 412
Sequence Mass (Da): 44502
Location Topology: Multi-pass membrane protein
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A0A0Q9U2I0 | MKLNRWVTSSLRTKMLIMFVMLTAIPLIAVGIISYTKSYNTVSQHSIATTELVAEHLKNEMDVLFSDNRKFLDISKNSSVLRFLLIQNETYEEAKDILKTFSLYRDTYRFSNGITNIMLFNQYGKGISEKKGVFQMDGDPFQYGTFKNLLNYPDEILILPPSETDGFNNLDHAVQDSPFIISIVATVKQEITDEVIGFMVINLDATVIENFCNNTKMGDNGFFYVTDSYGQPIIVPDKLKSAGRAAGLTKQQLFAPSGNDIRHFNNRDQLVVYATSDLTGWKIVGEVPLSEVVKDAKQIETLIFVSVVFTIVFTITLYAF... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 605
Sequence Mass (Da): 68403
Location Topology: Multi-pass membrane protein
|
A0A133VPW0 | MSITRENFLQHELIGLKAEVLKAKNTSLEGKEGIIMKERKNVLTLEEDGDLKILPKSGVTLSITLPDGEKVKVDGKSLVARPQDRTKKFR | Function: Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
EC: 3.1.26.5
Subcellular Location: Cytoplasm
Sequence Length: 90
Sequence Mass (Da): 10073
|
A0A5F7ZIG2 | MAHSHWPRLGHVLGHQAVTGQKEEMLSLAGPGHMFFLSQGAGSALSEELGLRRGGCYPRRCRGSRGSHLLLGGSSSTALGWGVRAEVVSKPPHSTGRETEAQRQTVPTQSPSRVIFGSSPQRLDGVCVQQWAGRECSGILGGGNLGAKVGGEPKVSVFRGPWRAADRLRLTAGAVSPQLQAFIRPFREHHIDPTAITRHDFIETNGDNCLVTLLPLLNMAYKFRTHSPEALEQLYPWECFVFCLTIFGTFTNQIHKWSHTYFGLPRWVTLLQDWHVILPRKHHRIHHVSPHETYFCITTGVKVPRNFRLLEELEEGQKGV... | Pathway: Lipid metabolism; fatty acid metabolism.
Subcellular Location: Membrane
Sequence Length: 397
Sequence Mass (Da): 44417
Location Topology: Multi-pass membrane protein
|
A0A961UUS8 | PAIPPAPTWLKTALYPEAKTVVIPLPDGISQFGSIRLDGVADNEISEVWEEMKLQFAILAGFFTLILWLVSFTLDRALRPLDKLAAGLGEVRRGNFNAQVAENGPQELNIIYREFNRMAQGLQEAERRNKLLSTQLSAVQEEERKELARDLHDEVGPFLFAIDVDAQTIPEFIERGTLGDVTARVGAIRQSVAHVQAHVRAILGRLRPSQFLDLGLTHAVDYLTAFWKRRHSDLTIQADFDQSSYGPEVDDVAFRIVQESLNNAIRHGEPTHIQIKGNAVCDRDPAVLELSIVDDGGGISPMAGAGFGIAGMRERAEAIG... | Function: Member of the two-component regulatory system NreB/NreC involved in the control of dissimilatory nitrate/nitrite reduction in response to oxygen. NreB functions as a direct oxygen sensor histidine kinase which is autophosphorylated, in the absence of oxygen, probably at the conserved histidine residue, and tr... |
W7V0H9 | MENERIKVLIGDDSASNGVKAAVTLRECGFIAYTRRKNGKAILDSILKDSPDVVLLDLTLPDTDAISLIERARASSGNVPAFIVVSDINNSFIERQVIENGASYFLSRPYEVGAIASIIKSVCKRSPDRSCTDTEIIVTDIIRRLGVPAHIKGYHYLRTAILSAIDNQKLMDCVTKLLYPRVAQKYDTTSSRVERAIRHAIEIAWDRGNAEMINDFFGYNVDSYRGRPTNSEFIALISDRIRLQLKSAHA | Cofactor: Binds 1 Ca(2+) ion per subunit.
Function: May play the central regulatory role in sporulation. It may be an element of the effector pathway responsible for the activation of sporulation genes in response to nutritional stress. Spo0A may act in concert with spo0H (a sigma factor) to control the expression of s... |
G2FLC3 | MPEVILEAVDLKYSYPDGTNALRKVCLQVEKGERLAILGSNGAGKSTLFMQFNGIYRPNSGCIKYQGRDITYSNKALIELRKKVGIVFQDPDSQLFSASVYQDISFGPLNLGLSEEIVAARVKQALIDTETTDLVDKPTHLLSYGQKKRVSIAGVLAMEPEVIIFDEPTAGLDPRHALEFMQLLKKLRDSGKTIIISTHDVDLAYSFSDRIAIMCSGEIIGHGEPSELFLQSDLIQRADLALPWLIEMHSELVKKGWLPPSTPLPKTKEDLLRNIPPKSDQQSA | Function: Part of an ABC transporter complex. Responsible for energy coupling to the transport system.
Subcellular Location: Cell membrane
Sequence Length: 284
Sequence Mass (Da): 31496
Location Topology: Peripheral membrane protein
|
F6TUB8 | MALTSNYSFTKPLTSAKFALGCEEDCCEMNSGCIRLRGRLKSRDPPTLFPRSLMGSLLRFQAQTRAPGAERGGPARPSAHPIGQTSARVGGAAAGAEESSEAAFGGRGLHGGGGGPWGSCFRASSPAPMWDPEGQSRRQRWWEQLPGALREADRACSQHPRSPWFQPSDAPVPTGSRHAAPVHSAQWLLPPTASGLADRHHHPQCLQPHLPHLCHALGLARQGSQTLDPTLLPPSPRPYFFPASQPSLSGTPSPLALPTATNPYPTPNSCRDVPDDVQPIASLPGVARYGVSRLEEMMRPLVEEGLRCVLIFGVPSRVPK... | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 1/4.
Function: Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensat... |
A0A1F1Z1V5 | MTELFWPRKSPHFLACRRAVREVWQTSKIGLVDGPVDRPVVIGFSGGPDSLALVAAAAAENVPALAVVVNHNLQEGSAQIAGEAAVQARALGVDTKVVHVDVDLEAGGGNVEAAAREARYAALFRVAGQVAGQVAGQVAGANGEVWVAHTADDQAETLLLGALRGNPSGMLQRSGNLVRPFIYLRRADTVGACRELHLHPWHDPMNEDLAFRRVAMRTEIIPALSELLGGDAVPALARTADRIAQSNEVIRELATPTGGCDELACADLDCAELAALPAVVRRSRIHAWLVNKDIHPNGAQLDAIERLVTHWRGQVGVELA... | 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)... |
A0A1F8MDF0 | RLDSVLPLRCISSKPAFLLAWTTTPWTLPGNTALAVAPDAEYSVMEGDQDYLVLARELTGRVGLERYTEAGVVLGEDLVQLEYDPLFNPHAFGVQRLALPTLCVEEARKDLTYSVIGADFVSLDEGTGMVHVAPAFGEIDFGVGISNGLGFVQPVDLEGKITGTYSFAAKFVKDADPFIVDDLKSRGLLYRSEKVVHTYPFCWRCDAPLLYYAKPAWYIRTAAVKEQLILGNSQINWYPDYIKHGRFGDWLENNVDWAFSRERYWGTPLNVWHCSSCGNDECVGGVEELRARPGLDGLTMPLDLHRPYVDEITFACSKCD... | Function: Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves ... |
A0A952H5Y9 | MERLEQLPAFRSVSIRRTALPTSDWIDVSTLCFDEAAFTPAHFAEAGMPCPDSIARSVRKRQAEFFFGRLAARRAIERAGVDRAVAQADIGIGASREPLWPRNVVGSISHTAGIAAAVVASSQAYGGIGIDVEQIVSASTRPAVLEMALNGAEVHMLQACPGPMSLDEKVTLVFSAKESLFKAAFGSVRRYFDFSAARLSSIDPDSGRLALTLVEHLNEEFTLGRCCELSFTRLDGGTILTICAFRPRPGSAAVELASRSLHSRLHSA | Pathway: Siderophore biosynthesis; enterobactin biosynthesis.
Function: Involved in the biosynthesis of the siderophore enterobactin (enterochelin), which is a macrocyclic trimeric lactone of N-(2,3-dihydroxybenzoyl)-serine. The serine trilactone serves as a scaffolding for the three catechol functionalities that provi... |
A0A978SSM4 | METPQVKWYHSLIFQGTLGSLLLLLLLVVGIVLVMKTKGQQIVLAESSRLTEQTGNNAVSHLLARSQEIAALARSLATLVEILPKSEKTFKQIIPEIINFHGDQAVAGGGVWPEPYTFDPKLARRSFFWGRDAKGILQYYDDYNQPGPGYHNEEWYVVVRYSQPGRCFWSRSYMDPYSYQPMVTCTVATFKSQQFTGTVTIDLKLEGLHDFAESWRQQTGGYIFIVDRNNKFISFPKPELVKHFGKDNKGKKTEEFIFAYEFAKKEPLFAPIAMALDEMNKTILSQAKLLAGKRKEIIEKIDADSYQINREEAELINAII... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 740
Sequence Mass (Da): 83592
Location Topology: Multi-pass membrane protein
|
A0A2W5XCC0 | MNETELIAALSALSESSTNRKILVGIGDDAAAWRPSRSRLSVISTDALIEGVHFTRALGNEAIGHRAMAANLSDLAAMGARPVLCTIALGVPRDELHEGVLEMYAAGARLAREYNLTIVGGDVARSPVLMLCITVVGEVRPTRMKRRAGAKPGDLIATTGALGASRAGLDVSQGRVHLRDGLQDVALRAHCFPQPRLAMGAWLAASQSVHAMTDLSDGLSTDVLHMARSSGRRAILERVPVSSSALAAASAQGMDATEYVLAAGEDYELLVAIAPRAFRYLNSRFTKRFGSGLECVGRFEAGEGGAIVGSSGEVPLKASG... | Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine diphosphate from thiamine phosphate: step 1/1.
Function: Catalyzes the ATP-dependent phosphorylation of thiamine-monophosphate (TMP) to form thiamine-pyrophosphate (TPP), the active form of vitamin B1.
EC: 2.7.4.16
Catalytic Activity: ATP + thi... |
R7Q265 | MRDQSAPTITDADRLLKERFGHDEFRPGQRRVIEHILATAATPSSPDISHHRAGRALAIFPTGAGKSLCYQLPGLLFQDGLTLIVSPLMALMKDQTDSMVQKGLSAACLDSSLTASETRDLFQRVRDDDLRILFVSPERFKNSRFLRLIQNTRIALFAVDEAHCISEWGHSFRPDYLRLSRWADRLNCQRRLALTATATPRVAEDICAALNIPFPSAQVRLASVRRNLTLRVSSIPPAPHDGYQSLTDKLQTRMDVLVERLRSRDPGPTIIYVTLQATATFVASELRRHGFIQAASYHAGMRQDDRKQVQDDFMANKKDA... | Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
EC: 3.6.4.12
Subcellular Location: Nucleus
Sequence Length: 683
Sequence Mass (Da): 76414
|
R7Q1E8 | MALAHPFVMWRDKATRRFHDFIAMAWMKCSFGSVLVHPNIVNAHNLPPKGTPVVYVANHSSYLDIFSFAYLRRRIKYVSKAEIFKLPIVGWAMEMAGNIALRRMNRRGQMEAYRKMVAVVKNGLSLVIFPEGTRSASGKMRKFQSGGFRAAKKQNAPIVPVTILGTREVMPAHAWVPLRYPTKPISLVVHPPLDTANRSVHELQDCAYEAIDSALPPEAQTRPLIKHAKNARRNF | EC: 2.3.1.51
Catalytic Activity: a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphate + CoA
Sequence Length: 235
Domain: The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate.
Sequence Mass (Da):... |
A0A7C6HXB3 | MKIGKYELKNKVIIAPLAGYTNYSYRKIMREFGASLCYTEMISAKGINFKNKKTLDMTKVKEDDHLVSMQLFGGTKEDLVKAAIYLDKYSDCDIIDLNMGCPVKKVLKAKSGSYLLKSPENIYEIVKGVVESVSKPVTVKIRLGITKNTINVIEVAKQIEKAGAAAICIHGRTQSDLYKGKANYDYIKLAKESIKMPVIANGDIKTIEDAEYVLEYTKCDAIMIGRSSIGNPWLIQNIVNHFEGKEVKEPTAIERIQMVQRHYELLKAELGTKLAILNLRSLFSRYLKGLDVKEYKIRLMGITEDKKMLEFFKEMEEKYE... | Function: Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines.
EC: 1.3.1.-
Catalytic Activity: a 5,6-dihydrouridine in tRNA + NAD(+) = a uridine in tRNA + H(+) + NADH
Sequence Length: 322
Sequence Mass (Da): ... |
A0A4R1S4I8 | MRKLVLATTNKGKVAELRELLAGLPVCVCGLDDYPQAPEVEETGVTFAENAALKARTIGEYTGELTLADDSGLEVDALGGEPGVYSARYGQPGWNDRQRYEYVLSKLAGVPENERAARFRCAVALFDPVANRMELADGAVEGRILDEPRGANGFGYDPVFFLAEYRKTMAELGPEQKNRLSHRARAIAAILPTLRQHLG | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as ... |
A0A931LYJ9 | IILAAAGLKRLGVPARIRPRLDPEESLPAAGQGAMAIEIPDNRRELQAMLMALNHTETAQAVTAERTVSKAFGGSCQMPLAAFATVSQGQMQIRAMVATPDGTRIARAEAAGDADKPQELGLKLAQALSAQDAEAILAVCKAEITE | Pathway: Porphyrin-containing compound metabolism.
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: 146
Sequence Mass (Da): 15259
|
A0A9D5GBH1 | MSFGRFGPVVTAMITPMRADGSVHYDEAARLSRWLCDHGSSALVVAGTTGEAPTLDDHEKTRLFTTVVSAVGDRVPVIANTGGNDTRHSVELSRKAASCGVHALMAVAPYYNKPPQAGLIAHFIAIADAGGLPVIVYNIPGRTGVNVLPQTIVAMSSHPAIVAVKESSGDVNQIAEMAAAVPAEFDVYCGDDYLALPAASVGARGVVSVVSHVAGDALRSMLRAFDEGDVERARHIHRSLLPLFRALFAVTSPIPVKAAMRSFGFDAGACRPPLCELTPEQEAAVAREIAVWKPVAVTGVSS | Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4.
Function: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
Catalytic Activity: L-aspartate 4-semialdehyde + pyru... |
A0A956TC78 | MAEIDRLTISDGLPGRVLMETAGRAVAREAAWFGARRILVLCGPGNNGGDGYVAARHLHQHGFEVRLTRFGAEPQGQDDAARNWELLAPLCLPCDDWSSLDLSEVDLVIDALFGTGLTRPLQGELAQGVDRLNRSGLPVLSVDIPSGVDSATGQVLGAAVAATRTVTFGLPKFGLLIGAGAALSGQVVVEEIGFSRRRLEGGAWRIGPDWVSNRLPQRPLDAHKGTCGRALVVAGSERYPGAAGMSALGALRGGAGLVTVAVPQVVKGWLESALLEAMFMPRTAEMPLHADALCLGPGLDESDEASALCEYVLDSFYGPM... | Cofactor: Binds 1 potassium ion per subunit.
Function: Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that... |
A0A3S0K8J2 | LFSFVLTNENLPHQLADWLLSMNLGQNGFLFVVNLVLLGAGNFMDPSSIILIMAPIFFPAAMQLGVNPVHFGILIDVNMEVGLCHPPVGLNLYVASGISKLGITELTKAVLPWLATMVVFLIIVTYWPWLTLVVPRMMGML | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 141
Sequence Mass (Da): 15509
Location Topology: Multi-pass membrane protein
|
A0A956QBQ3 | MTALTRADAAWLHMEEPTNLMTITGLFLVEGRLDQVWLEHHVVRPLMEHHRFGCKVVDPTVGSPRWVEDTDFEMDHHLVLSESSPERLFELVGQLMSQPLDRSRPLWQIHSVWLGQDSALVIRVHHTLGDGVAMMKVLSSLADNPPEPSHSRTPRTSFGKLGAWLAALGELVFGVLLSPEPRTSLKAPLGRAKLAAVSPPIALSEVKRVEKKIAGTVNDVLLATLTGALRRHLKKTAGSVPANLRAVMPVDLRRADDLTLGNQFGLAFATLPVGLDDPLERLRESRRRLLKLKSSPHAAILYGILRLAGCLPVSLELALV... | Pathway: Glycerolipid metabolism; triacylglycerol biosynthesis.
EC: 2.3.1.20
Catalytic Activity: a 1,2-diacyl-sn-glycerol + an acyl-CoA = a triacyl-sn-glycerol + CoA
Sequence Length: 406
Sequence Mass (Da): 44224
|
A0A852UPP6 | MKNTKILATLGLACSIFLAACGGADGNTSAKTSEGLSGNVAGDGSSTVAPIMEAIVEEYAQAEKDVKVSVGVSGTGGGFEKFIAGSTDFSNASRPIKDEEKAKLEEAGVDYTELKIANDGLTIVVNKENDWVDSLTVEDLTKMWTEDGTTKKWSDINPSWPDEEIVFYSPGTDSGTYDYFNEVVLEDADLVKSATLSEDDNVLVTGIKGDKNAIGFFGFAYYESNKDALNAVLIDGVQPNAETIESGEYTPFSRPLYVYVSNAALKEKEEVRNFMEYVIDNSADMADAVGYVRLPAADYDAAREQLKAVK | Function: Involved in the system for phosphate transport across the cytoplasmic membrane.
Subcellular Location: Cell membrane
Sequence Length: 310
Sequence Mass (Da): 33378
Location Topology: Lipid-anchor
|
A0A1D7YZ55 | MTDSTPFAPTAQRLGLYPVVDSVEWIERLLGVGVKTIQLRIKDRSDEQAEADVIQAIALGRRYQAQLFINDYWKLAVKHQAYGVHLGQEDLDTADLSAIKQAGLRLGLSTHDDRELARAVAVNPSYIALGHIFPTQTKDMPSAPQGLAELTRHIADLQGRFPTVAIGGIGIDKVPAVLETGVGSIAVVSAITQAPDWQQATATLLKIIEGREA | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)-thiazole: step 1/1.
Function: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-met... |
A0A949Y4I9 | MDSISHAPVMLDEVLALLSPAAKQSPLPVFVDCTFGAGGLTRSILERIPGSRVIALDADPAAVARAEALREQQPRRVTPVHANFAQLADALASVGVGSVNGVVYDLGLSSLQLADAARGFAFAGEGALDMRLDPTSDAATAAQLLATAKEGEIADIIFEFGDERNARRIAREIVKRRTRSPLRTTSDLVAAVLAAQPRGARGKRGTIHPATRTFLALRMAVNAELDGLARSLEAAIACVQPGGRIAVISFHSGEDRVVKHQFAAWRRTGVAETLTRKPLTPTQTEIAANPRSRSAKLRGTQRTRAPLPRSA | Function: Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
Catalytic Activity: cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(4)-methylcytidine(1402) in 16S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.199
Subcellular Location: Cytoplasm
Sequence Length: 311
Seque... |
A0A950UME3 | MSLYRTWRPLTFADLVGQDAVVRTLSAAIENGKLAHAYLFSGPRGSGKTSAAKILARCVNCASGPTVTPDNTCENCTAMLAGTALDVLEIDAASNRGIDEIRRLREAVKFAPATMRMKIYIIDEAHMLTREGANAFLKTLEEPPAHALFILATTEPEKLPVTILSRCQRYAFRRIAVPVMIARMRDIAAQEGIAVEEDALAAIAYRADGGLRDALTMLEQLAAFSQGTPIDAAMLDLAFGSSGRSFAQALIEAIVARDAAEALRTVERAGDAGIDFQVLIRSLIAGFRNLLIARIDPDLLARDLAPDDAARTAAAAQGLS... | Function: DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity.
EC: 2.7.7.7
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Length: 383
Seq... |
A0A950MTT1 | MANETLARRYAQAVFSLAQEQGVVDRVGRDLETLRDAILLDAQTRAFFVAPVIDRKGKECALTASFSGKTEELALHAVLLLVRKRREPLLAEVVKQYGELEMQARGARPLTITSALELSPRQLDELVKELEQHYATHFEVKHKVDPQLIGGVRIMMGDRRIDGSVAGRLDELSRVLFGATT | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
A0A950IK84 | MRIGVVGAGALGLTFAAGLAAAHDVVVLARRADVADALARDGVTVDDERGTHRIRLHASADPRALAESDAVVVAVKAYATVDALTPLRAILGAGTLIASVQNGLDAAADARAALPDARVVAGSTTQGAIRLGETHVQRVNDGTTVFARPRHPELVEGRASPTSDDLVAAFTAAGLDAHVADDIATILWRKLIVNAAINPLGALARATNGAIAT | 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: 213
Sequen... |
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