ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
|---|---|---|
A0A4Y7T6Y9 | MESLITEIKKIPPVTRFSVVSLVGLTVPVMLKMLNPEKLIYFGPWVWKGFQLWRLPTSFFFGSTNINFIFEVSMLYRMTNQLESTTFPGNSSDLAWQLFVASGAIILATRPLKSILFLHPLLACLAYVSSALAPPGAQTSIMGLLTIPVTYFPYVMVGMDLLSGGPYAAAQAVAGIIVGHLWWWACMGRRARRRRRCSTGKME | Function: May be involved in the degradation of misfolded endoplasmic reticulum (ER) luminal proteins.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 203
Sequence Mass (Da): 22641
Location Topology: Multi-pass membrane protein
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A0A7X6SL76 | MAKILKFDDEARRALEAGVNKLADAVKVTIGPKGRNVVLDKKFGAPTITNDGVSIAREIELEDPFENMGAQLVKEVATKTNDVAGDGTTTATVLAQALVKEGLRNVAAGASPLGLKRGIETAVAAAVEAIKASAKSVDDDQGNIAQVASISAADSTIGEVIADAIAKVGKDGVVTVEESNTFGMELDFVEGMQFDKGYLSPYFVTDAERQEAVLNDPYILFVNGKIGSVSDLVPVLEKVMQSGKPLLIIAEDVEGEALATLVVNKIRGTFNSVAVKAPGFGERRKAMLADMAILTGGQVISEEVGLKLDSADLTLLGRAR... | Function: Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding.
Catalytic Activity: ATP ... |
A0A7W1Q986 | MKVPPGLLRLALAGIVPYEPGKPIEEVQRELGLDRVVKLASNEGPYGPFPRALEALERAEGELNRYPDGGAYRLRAALAELHAVEFDEIAVGSGADAIIDGLSQAVLEPGNEVVHGWPSFPSYGIYARKLGAQAVKVPLRNDRYDLDALLDAVTERTKLVYVCHPNNPTGTMNTRAELDTYFERVPDHVLTVLDQAYFEYIDDPDYADGIVEYFKAGRSVLVLRTFSKIYGLAGLRVGYGVGPAEIVIALAKTRRAFDLTTPAQEAALASLDFPAELERRRRVNSECRSELVRVLTDAGYRVVGPAVGNFVFVDLGEDAQ... | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
EC: 2.6.1.9
Catalytic Activity: 2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Sequence Length: 372
Sequence Mass (Da): 40592
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A0A538I9T4 | MRRRARRAPATTLRRRTRAPRWPMTVPILNASGCLDALTAAEVAQTLDVFVTKTVTPLPREGNPPPRIAETELGMLNSIGLQNPGIEAFLDDTLPRLARLGVPLWVSVGGFSVQDYAQLCTLLSGREEVTTIELNLSCPNVDEAPETAAEIVAAAREATPKTLYAKLSPATWDIAETARAVADAGADGLSLVNTIRGLALAPTTLEPTLERGAGGYSGPALRPIALACVYACATAVDLPIVGMGGVSSGRHAVALVAAGASAVALGTVLFAEPFAARRVRVEMTEAAVALGYPSAAALRGKAHKSATFANLSAL | Cofactor: Binds 1 FMN per subunit.
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway.
Function: Catalyzes the conversion of dihydroorotate to orotate.
EC: 1.3.-.-
Subcellular Location: Cytoplasm
Catalytic Activity: (S)-dihydroorotate + A = AH2 + orotate
Sequence Length: 314
Sequence Mass (Da): 32655
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A0A538APD0 | MTGRYLIRTFGCQMNEHDSERIAGLLEQDGYAPTPAAAEAEVVVLNTCAVRENADNRLYGALGHLKPVKDANPRLRIVVAGCLAQKDQGRIQARAPWVDVVVGTHALPGLLDLIRAAKRDGPQMDVREYTEVFPSALPSRAGSPYHAWVSVSVGCDNHCTFCIVPLVRGAQRSRALGDILAEVQGVAARGVVEVTLLGQNVNTYGRDLTAPHSAPRPRFGELLRAVNEVDGIRRIRFVSPHPHDFTDDVVEAMAESGRVCEHIHFPLQSGSDRMLRAMRRSYRAERYLGWLDRIRAAIPGIAVTSDIIVGFPGETEEDFE... | Cofactor: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that re... |
A0A538IWB6 | MLELSPLDAQHRALGAKMGAFAGWDMPISYAGTVAEHTAVRERAGLFDVSHLGKVLVSGAGAEPFLDTQLTNRMADLALGRARYSLICNEDGGILDDLIVYVIAENELLVVPNAANRQAVFERLAAAAPASLDVRILDWTTLAVQGPRSRDIVEAMYPSVKGEGYMRVAREGDVVISRSGYTGEIGYEVFTPPELAVETWGRLLSAVGDAGGEPAGLAARDTLRLEMGYPLHGNDIDASTTPAEAGLMWAVRLEDRAFPGRDAIAGAAPTKTLVGLRMTDKLIPRHGYEVRAEGRSIGTITSGTFSPTLRIGIALAYVET... | Function: The glycine cleavage system catalyzes the degradation of glycine.
EC: 2.1.2.10
Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolate + (R)-N(6)-(S(8)-aminomethyldihydrolipoyl)-L-lysyl-[protein] = (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + NH4(+)
Sequence Length: 353
... |
A0A7K0RDK3 | MRLVVGVSGGIAAYKAVGVIRAFVQDGHEVQVIATPSAYEFVGKATLEAISRQPVFDSLYDDVSQVRHVELGQNADAVVIAPATAHTLASLTAGLAPDLLGNAVLARRGPLVVAPAMHTEMWTNAATVHNISVLRTRGVIIVDPATGPLTGQDSGVGRMAEVHSIVAATYAAVGSRVHDLAGVRILITGGGTREYLDPVRFIGNASSGRQAVALAEAARVRGATVRFIAGFMDVDVPSGISVTRVESAEQMHGAVRAELDSSDVLIMAAAVADYRAKQVSDNKLKKLTLGSSPSIELTENADILADAARHSRCLAIGFAA... | Cofactor: Binds 1 FMN per subunit.
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 2/5.
Function: Catalyzes two sequential steps in the biosynthesis of coenzyme A. In the first step cysteine is conjugated to 4'-phosphopantothenate to form 4-phosphopantothenoylcysteine. In the se... |
A0A4D6XZB5 | MVKSIKQSIRGCSDYLPEYMRIWRLLERKIIKVLNSYCYNEIQFPIIENTELFQRTIGLSTDILLKEMYSFKDKKNNSITLRPEGTIGCVRAIIENKLNSITENRLWYVGPMFRYERPQKGRYRQFNQLGIEVFAISEPEIELELLMIFSHLLDDLNLSDSVYLEINSIGSKYTRRLYIKDLVIFLKKYATELDEDSKKRIYTNPLRILDTKNKNIQHLLKEAPIILDYLDEKSKIHFETLCSLMNKFNIKYKINTKLVRGLDYYNDTVFEWKTNVLGSQNTVCGGGRYDTLFQQIGGQSTSAVGCAIGIERLILLIKKE... | Catalytic Activity: ATP + L-histidine + tRNA(His) = AMP + diphosphate + H(+) + L-histidyl-tRNA(His)
EC: 6.1.1.21
Subcellular Location: Cytoplasm
Sequence Length: 426
Sequence Mass (Da): 49888
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A0A7W1JSL1 | MDAHETEKIVAARSAARAVEDGMIVGLGTGSTVAHFLTELAERRPQRLRCVATSPGTEAAARRLGLPVETFDRLERLDLAVDGADQVSPELWLVKGGGGAHAREKVAAAAAERFVVIVGSDKLVEKIVPPIPLELMPFGLLATLRRLSSLGELARREAPATPDGNVLVDLLGRVDDPAALARELDAVPGVIAHGIFPADLVSEVLIGKPDGSVERRSAAAQR | Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribose 5-phosphate from D-ribulose 5-phosphate (non-oxidative stage): step 1/1.
Function: Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate.
EC: 5.3.1.6
Catalytic Activity: aldehydo-D-ribose 5-phosphate = D-ribulose 5-phosph... |
A0A7N0UNT2 | MSSHELDSSTAAATGDPPNPSKPPRPPLSVDRDFLGHLEAYLAKRDGVDKILKICRYATKIILASSAVPEALPIHKRLKSFEASVGLSRKAFRLGKFVQDVNALRASSFRSREDLLLSVVAYGGEGLYYFVEQFVWLAKSGLIDGKHSRGLQTISAWAEFVGYLGSIWLKIRGLRVMLEEEACLISSIEIGNARGVKCGDEELKLSKVREKRMLKSLSTIQDVADLLMALADIRDGRGRLSAPIVVSSAGLLSALISTHKNWISC | Function: Involved in peroxisomal proliferation. Promotes peroxisomal duplication, aggregation or elongation without fission.
Subcellular Location: Peroxisome membrane
Sequence Length: 265
Sequence Mass (Da): 29012
Location Topology: Multi-pass membrane protein
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A0A4D6XXP0 | MELKKHYSFIKIRVLHINYNSFKHSSDTVKHCIQLCKKNNLELIIKNIKKIPVKKNFEEVARVIRYNIIKKVLIPKEVVITAHHLNDQCETFFLSLKRGSGPTGLSGMKLNTFLDKDKLLIRPFLDISKKQIEHFANKKKLIWITDHSNNNIYYDRNFLRKEIIPILEKRWPFFLKTCFRSSTICSDYVNIANNLANNFLQKNMLLDSSLNFFNMLFLDVSIRKVILRNWFLKNKLKMPSYSVIEKILKEVINSKKDANPKIIINQFEIRRYKKYIYIFPVLPSVNSLILIWHNINCPLQLPYRFGFLENNSYGMKIPSP... | 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)... |
A0A522TNE0 | MNLIQKEYAMSYHLPEQSAAMVYGDRPIIHQRSMSVFPWPTGATKTFAVIGDPIDHSLSPALLNAAFTAAKLDAVFVALKVDREHLESAAYGIRSMGIAGLSVTMPHKEGVIGHLDRITDRARKLNSVNCIFWDDGELVGDSTDGPALVSSLESDLRESLAGKSVMILGTGGAARAIVLSLEEAGVSEIVVVGRREEAVARVVALGRPVAHAGTIHDAKNVDILINATSIGMAETDGEGRSPLPAELIESRHFVCDIVYYPLMTPLLADAQAAGARFSNGIGMLAHQAARAFWIWTGHEPPIDIMLHVVHSGGH | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.
Function: Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydr... |
A0A523VI08 | MKEYLRILETGSKKLGTVLTDHQVSQFDTYLKQLRIFSEKFNLTAITQRSEIVKKHFLDSLSVLTTKCVLPGKSLLDIGAGAGLPGLALKIVLPGLKLTLLEANKKKSNFLDHITKELKLEDAEVINMRAEEFAKTAGRVKFDLVITRALASLPVNLEYAMPALKVGGYYLAMKGNLAKEPATNNACDELCCSLIESKKLHVPYVEGQRNIVIFRKEKETPSKYPRRTGKPSKYPL | Function: Specifically methylates the N7 position of a guanine in 16S rRNA.
EC: 2.1.1.-
Subcellular Location: Cytoplasm
Sequence Length: 236
Sequence Mass (Da): 26351
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A0A9E4M3R5 | MALSIGVFDGVHRGHQVLLSQLMIDAAKSGLTPAVATFDPHPLEVLAPQRAPKMLTSIEHRLQILEELGMGVVGVMPFPKIR | Pathway: Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step 1/1.
EC: 2.7.7.2
Catalytic Activity: ATP + FMN + H(+) = diphosphate + FAD
Sequence Length: 82
Sequence Mass (Da): 8880
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A0A1M2YFZ0 | MASDGLHELIKKHALKNAMDYGKADPSIVLNKTIASAKKEGVAIPQLRAEIESVVNEVNSMSRDELEKSYEGYSAEFESADREKKEKSAKPRMVLEGAVEGDFATRFPPEPNGYLHIGHAKPLFLEAAFRDIYKGKLFLYFDDTNPKKEKQEYVDAIKKDLEWLGVKFDKEYYASDSVPKTYDLCRKLIREGNAYACSCSAEEIKKLRFEGRACAHRDRPADESLEIFESILANSYTKDDVVIRFKGDMSAANTTLRDPNIFRIVREKHYRQGDKYVLWPTYSFNTPINDSINGVTDVIRSKEYELGDELYRMMLKALGL... | Function: Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).
Catalytic Activity: ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu)
EC: 6.1.1.17
Subcellular Location: ... |
A0A6I3CWB9 | MSTYKDAGVDIDAGDLAVELMKASIAKASRKEVIGGIGGFAGLFDASAMKSMQQPLLATSTDGVGTKTEIARILGKYDTIGEDLVAMVVDDLVVCGAEPLFMTDYIAVGKVIPERIAAIVAGIARGCEKAGTALVGGETAEHPGLLGEDEFDIAGAATGVVDAHLQLGADRVKSGDVLIAMPASGIHANGFSLVRHIIATQKIDITAHNADFGRTLGEVLLTPTEIYALDCLALIRSL | Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 2/2.
EC: 6.3.3.1
Catalytic Activity: 2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ATP = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + AD... |
A0A537YBK0 | LDAAFEITPELVGVNQRDLRTFDVDTGLAIRLRRRIPGDVAMVAESGIADRAGVEALEEAGVEAMLVGETLMRAGDPARAARELLGAPLSPEGTPASGDGEDHD | Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 4/5.
EC: 4.1.1.48
Catalytic Activity: 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate + H(+) = (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O
Sequence Length: 104
Sequence Mass (Da): 10880
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A0A354XT78 | MANAGHPRSRVEAMREASRLAVIGVGGVLGALSRAGVSQIFGQDRLELGDQSANFPWATLAINLSGAFLIGIAAVALITDNSSYRKPFLVTGVLGGFTTFSALALEAVDLFDQGLWVTALVYLIVTVGAGLLAVNIGVRATRRIVRT | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Subcellular Location: Cell membrane
Sequence Length: 147
Sequence Mass (Da): 15370
Location Topology: Multi-pass membrane protein
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A0A538GF90 | MAISRDEVLHVARLARLELSDEELDRFAEQLNAILEAVGKVAELDLEDVEPTSHPLDLVNVWAEDEPRPPLSVDEALANAPDREGDSFRVPAA | 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 ... |
A0A358SM72 | MAPAGAELARARTVFGSALPAAQRYAALLAGAAAERGLIGPAETGRIWERHILNCAAVAELIPRDGTVIDVGSGAGLPGIVLAILRPDARLTLLEPMARRVAFLLECVQILGLDNVTVLRGRAEELAGELTADVVTARAVAPLDRLAGLAAALVRPGGVVLAIKGQSAQAEVARAQPVLRRLGFRDVSVVTAGSGTVIPAVTVVRMVSSRPERLPSARRRVTGRAADRATGRAGSRRAAAGRGRAPRGHSGGTVRDEGRH | Function: Specifically methylates the N7 position of a guanine in 16S rRNA.
EC: 2.1.1.-
Subcellular Location: Cytoplasm
Sequence Length: 260
Sequence Mass (Da): 26870
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A0A6L6R2V6 | MAAPDAHHRSARRLHDVLGVRARDRTSSVGGVHRAGRRVRRGNPGHGPHCRAGRPGAGGRISVTYLAIALAAAVGAPLRFAVDRWVTGRTVRSRPAGGFPWGIYTVNVIGSALAGLVLATTSGTVQVFLLVGFCGAFTTFSGFGWDVTRLWPGNRAAAAATLVVMPASCILAFLAVWHLASAAAS | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Subcellular Location: Cell membrane
Sequence Length: 185
Sequence Mass (Da): 19245
Location Topology: Multi-pass membrane protein
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A0A0H4VF46 | MLKKLLASAAIASILTVAPAHAAEISTHVLNISQGKGGADVPVTLSKQASDGFWQTVTSTKTQSNGRAEDFGNPENLTPGVYLLSFDVAQYYAGKSDTFFPVITVVFNVTEQDGHYHVPVLLSAYGYSTYRGN | Function: Catalyzes the hydrolysis of 5-hydroxyisourate (HIU) to 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU).
EC: 3.5.2.17
Catalytic Activity: 5-hydroxyisourate + H2O = 5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate + H(+)
Sequence Length: 133
Sequence Mass (Da): 14214
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A0A2E5EWP4 | MPDLELAFISLFPQQLSGMLNKGILGRAIDDGRISVRIHDLRQSSHHKRGNVDAPPFGPNPGMLLRADVMATAIRSVPDYEQYQLIYLCPKGDRFDQKRAQKLSQERPLKLMLIPGYYEGIDERIFEMFSIQRVSMGDMVLLSGELPALMITEAVARLLPGVIGNEQSLADESISSGLLEAAQYCQPREVEGKTVPDVICSGHHAKIRQYHHEQALRMTLFQRPDLLAQYPVNEQDKAVITKALLKQAEGPVIDKTEPF | Function: Specifically methylates guanosine-37 in various tRNAs.
Catalytic Activity: guanosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(37) in tRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.228
Subcellular Location: Cytoplasm
Sequence Length: 259
Sequence Mass (Da): 29047
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A0A9D1T8Z4 | MIYLDNAATTRMAPQVREAMLPCLSERFGNPSSLYSLGTKSRETVDEARKAIGQILGADGEEIYFTGSGTEADNWALKSAALDQKERGRHIITSKIEHHAVLHTCRYLEEQGYEVTYLDVDEWGIVKLSQLERAIRRDTVLISVMAANNEIGTIQPLGKIGQIAGKHGILFHTDAVQAFGQIPLPVKKLGISLLSASAHKIYGPKGVGFLYIKKGVGLSSFIHGGAQEKGRRAGTENTAGIAGFGRAAELAGEEMKERGERERKLRDYLIRRVLGEIPYSRLNGHPLQRLPGNSNFSFRFVEGEALLILLDMEGICVSTG... | Function: Catalyzes the removal of elemental sulfur atoms from cysteine to produce alanine.
EC: 2.8.1.7
Catalytic Activity: [sulfur carrier]-H + L-cysteine = [sulfur carrier]-SH + L-alanine
Sequence Length: 400
Sequence Mass (Da): 43602
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G1MST4 | MLFSRCPSSSRARQCFHALKLIKRDCLPSLHTAGWASTAAVPRITTHYTIHPRDKDKRWEGINMERFAEEADVVIVGGGPAGLSAAIRLKQLAAEQGKEIRVCLVEKASQIGAHTLSGACLEPRSLEELFPDWKERGAPLHTPVTEDKFGILTKKSRIPVPILPGLPMVNHGNYIVRLGHFVRWLGEQAEALGVELYPGYAAAEVLFHEDGSVKGIATNDVGIQKDGAPKATFERGLELHAKVTVFAEGCHGHLAKQLYTKYNLREKCQPQSYGIGLKELWTIDEKKWKPGRVEHTVGWPLDRHTYGGSFLYHLNEGEPL... | 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: 503
Sequence Mass (Da): 56199
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A0A3A4PKJ4 | MPESPVESLKKSRDFKRVIEGGNREIMETVTIYRLPNQAGKTRAGISVSKKAGGSVKRNLIRRRIKEAIRRNAPLLPAGEDMVFVARRAIVRASYGDIERDIRKTGGGRRS | 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... |
A0A832VEY3 | MPSRRRGRRTNRMEAIARERIAHLLEQAERWALEGRQRDADRCAQLARLIGKRYRQKLTREQRLRVCRGCNGFLGPATARVRLSRKGWRTTTCLQCGRVCRQPLRSKASAPARRALDER | Cofactor: Binds 1 zinc ion per subunit.
Function: Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends.
EC: 3.1.26.5
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Subcellular Location: Cytoplasm
Sequence Length:... |
D3UHP7 | MVSELFIEIFVEELPALPFLREFKNFATKWQEALQRHSIPPIQTQFFYTPRRIVLFCEQFPIRTQEEKKEIFGPPVDVAFEKGDKNAPLTAAGEAFLKKNHLQIEQLCYAQKGGKEVLFSLQVQEGVSLTEILPQILKSFLQSLHFGKHMRWGNVTEDFIRPIRNIMIFLGEEFVPFVGYGIEARPQTKLHRDFGLDWQEVKNFADYCKKLNEGGVILDQEERREKILSSIISLEKSQNIAVEVDGELLDEVVAITEYPQVILGHFEERFLELPKEVIITSMKENQRYFAVYQDKSLQHLKNHFVMVSNSTSKDEGIIVL... | Catalytic Activity: ATP + glycine + tRNA(Gly) = AMP + diphosphate + glycyl-tRNA(Gly)
EC: 6.1.1.14
Subcellular Location: Cytoplasm
Sequence Length: 688
Sequence Mass (Da): 78701
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A0A3C0QL71 | MDRRRKNILITGGGTGGHLYPAIAVIEYIQKNHPLANIIFIGSGKGSGKKLIPDMGIEFYTVKARGIAGGSGPLKKIINYILFIIYLIPGFIRSANILRKKKIDIVLGMGGYICAPVMLAAIIRKIPFTLHEQNYIPGRLNRLFSGRAKYFFTSFEDTKRFLGKGNKNIIFSGNPVRASIKDSDNIPSDHKKWGLAEKRFTIIAFGGSLGAKKINDAIMGLYKIFKDNNNIQFLLITGNRFYDSIKDDLEKRRRSDDKIIFNIFPYIDEISQIYRIADIVIARSGASTVFETAAADIPTILVPYPFAIDNHQFYNARYLA... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II).
Catalytic Activity: di-t... |
A0A0F2IYH9 | MIRPQIKTLTAYNAEKTPCKIKLDANESPYGFAIQNDTLQAVKTNKYPDPEAKKLRQRISELWNVDYNCTLHGNGSDELIYYLIAAIGGPVLLVSPSFSMYAVISQILGQDVITAPLDDNFDIDIDKIQQEIDAHKVKLIFLGIPNNPTGNSFSPEKVLRILQNTDTLVVIDEAYIEFSKNGNYLSMLNTYRNLIIMRTLSKIGLASLRTGFIIGDKDLIYEINKVRLPFNVNSFSQAIALQVLTEPQKLDANNKLIIEERDKLYKQMSAIKPIKTYPSDANFILFKAEGADKLHSELLNEGILIKNLNTSLKGCLRVTI... | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
EC: 2.6.1.9
Catalytic Activity: 2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Sequence Length: 343
Sequence Mass (Da): 38689
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A0A6I2WXH8 | MTWLITGGAGYIGGHVVAETLNSGREVVVLDDLSTGIRSRVPELVPFEQVSLQDRNAVCDVFSRYPITGVLHLAAKKQVGESMIRPDHYWQENVGGLINLLEAMSMHHVTNFVFSSSAAVYGEPNISHGELLRETATCNPINTYGATKLMGEWLSNGYVAIDGLTVAALRYFNVAGAGQQHLGDTFALNLVPIVLTALDKNEAPTIFGNDYPTPDGTCIRDYVHVQDLALAHVAAMTFVEKSDPGFESINVGTGIGSSVSQVIQAIAQAKGIDISPSVSSRRAGDPPALAADVTKAKELLAWQSRYDLTDIVTSAVAAWE... | Pathway: Carbohydrate metabolism; galactose metabolism.
EC: 5.1.3.2
Catalytic Activity: UDP-alpha-D-glucose = UDP-alpha-D-galactose
Sequence Length: 328
Sequence Mass (Da): 35166
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A0A7W4WGT6 | MVRGLLFCFVLFLFIGGTTDCFAQAGQLQVSGGGISLSIDPQAAEEDYSAPVQILLLLTLLSVAPAALMLLTAFTRIVIVLSMLRQALAMPSTPPNSVLVSFALILTIYVMLPVFESINAQAIEPYMKKEVSAGEAITLARVPIQEFMINQTQEKNIALILELSEKSAPNFAADLEFSTLVPAFLLSELQSAFEIGFIIFLPFIMIDLIVASVLMSMGMIMLPPTSISLPIKILVFVLIEGWSLLAYSLIGSFK | Function: Plays a role in the flagellum-specific transport system.
Subcellular Location: Cell membrane
Sequence Length: 254
Sequence Mass (Da): 27556
Location Topology: Multi-pass membrane protein
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A0A538LFR4 | MRGRGSREPDAAEGRRHPAEGADVPDRPGVQAEGESHDGRERLQERRLRQLPHARRRALDGHRRAEPRPAEAGLPGRHRPGDERRGADAVLQEEPLDAADRRRLRLRRQIDRRNRSVDLPAGFPRPLAAFAVDLDRTLIGEDAVLRPRTKAAIEGTRAAGVHVIVVTGRMFRAVRPYVKEAGIDDPVICYQGAVVADPVTGEFLRHVPIRGDRRGRRRRLPPQLLRRRPALRRRGDAGGTQLRRLPGTGDPRRRAVARVVARRPDEARRRRRPGRARRTRSRVEAALRRPPVHLQVAAVLPRVRAPGREQGRRAPVRRRP... | Pathway: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1.
Function: Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further conv... |
A0A1I3BCV6 | MNETNEAKKNTYEPRRDKHDPKNKQPQSSRGNEWLSTLLYIGAAVLVFFLIRHFVFAPVSVDGDSMVPTLHHQDRLILNKMSSIDRFDIVVFDAPDDPGKQYIKRVIGLPGDTVEVRDDVLYINGKAYSEDYLDPSQYHLEEWENFTEDFSLSLLTGIQEVPKDDYFVMGDNRLNSKDSRSFGFVSADELVGTTNFRIWPLGDFGKIDQ | Catalytic Activity: Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.
EC: 3.4.21.89
Subcellular Location: Cell membrane
Sequence Length: 209
Sequence Mass (Da): 24002
Location Topology: Single-pass type II membrane protein
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A0A662T9M0 | MIAIPKEDKLIGLEAYNTSTKPINGRIKRRASDFFVEETLKKEFMRKLRSKPSKNFSYPVLRIKKKGKDTLAMISEIASSFNLSPSDLRFLGLKDSQAIVVQYVSISRAVKISGKWMVVGWARRPLLREDMLGNFFRVKVRISDVKRKINTIRKFVEEVEEKGVPNFYCYQRFGSPRGINHLVGEKIVKGDFKGAVLIYLTARSGFEKPEIEHWRKDLRDSLNFRRAYNEAPAQLEYERIMLSRLIKRPNDFKGALRGMPISLRRLFVNAYQSYLFNKALSMRIKLGLPINKALKGEPFYDLKSGRIRINDSEHEWLRVP... | Function: Could be responsible for synthesis of pseudouridine from uracil-13 in transfer RNAs.
EC: 5.4.99.27
Catalytic Activity: uridine(13) in tRNA = pseudouridine(13) in tRNA
Sequence Length: 419
Sequence Mass (Da): 49056
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A0A7K0R821 | MTDEEFAELEDRVDAIEATFETGDQDAIEEAEDELGQDIAARRRERSTAAAAPTRKGGLRFVAFLRASWAELQRVQWPDRRQVGQATAVVLGFVVVAGLYLGLADFVAQKVVDIII | Function: Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation.
Subcellular Location: Cell membrane
Sequence Length: 116
Sequence Mass (Da): 12808
Location Topology: Single-pass membrane protein
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A0A3P8X640 | MLFLRLLVELLAGFTLFSDEQERFICNTIQPGCSNVCFDVFSPVSLLRLWLLHLILLCLPHVLFATYVMHKLMQLHRSHRGSPENTGELSLTKTHLHAPSQEWTSPGFHCSYLLVVFVRLLVEMAFGASQFFLFGLSVPKSFLCYEAPCTSGVECYVSKPTEKTLMLNFTLGVTFLSILVSLVDMVTSMKAMVRWRRKREWLTQEISKGEQNSMFTTATDDNDGLLSRRMSPGVSSGDEKLHHPNNQSNTSGPALKSTGSTNEKTQENVSPPPSPLSPAPTPFVLHRHMKPPLYPRPDCRPPPLNLRVPTPPGVRQLDQS... | Function: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell.
Subcellular Location: Cell junction
Sequence Length: 339
Sequence Mass (Da): 37913
Location Topology: Multi-pass membrane prot... |
A0A7K0LMA2 | MFILEWLEVAVSWILVMFHTLLSPILGADNGITWALSIVGLVIVIRIALIPVFVKQIKAQRGMQVLQPRMKEIQQKYAGDRNKQSEEMMKLYKETGTNPLSSCLPLLLQAPIFYALFQVLQGIAQLDSKGVFRWETYAGLTQQAHDALLFGLVPLYATFKDATETPNPTSTRVLCATLVVLMTASTFLTQRQLMVKNMPAGNPMAQQQK | Function: Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins. Aids folding of multispa... |
A0A2E2WYB3 | MRHRLAGRDGYVRPVTDETPHDEVSGPDPAGSGESDGRAWTDDLLARARARSLGQPTESEDPGRPSGEAPLPAGSSHHGPEPNLQPPVVRSPIVTRADLTGGTPPPAASLDGTFSVPTAPLPSEVRVEAPREVDLGIPGRGVSARRSVLEWGSVLLGALVLAMLVRAFLFQAFYIPSPSMEPTLWSGDRILVNKVSYDLHDVNRGDIVVFRAPPGSGTGDDDLIKRVIALPGERVTAEGGRLLIDGGLLIEPYLPYQEGTAGFGMVPWCADGGDGACTVPDGHVFVMGDNRPNSRDSRYFGPVSIESIVGRAFVRVWPLG... | 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: 325
Sequence Mass (Da): 34527
Location Topology: Single-pass type II membrane protein
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A0A2E9CZJ2 | MLVGIGFDIHRHSQEDALYLGGLKIDGPGFEAHSDGDILLHTLCDALLGALSKKDLGHYFPSNSETPKKISSVEMLEEVLRIIDYKKYIVNNIDIIVISQVINVANIRTELVENLGILLNIDTSKINIKGKTTDNIGTIGSKEASACQTIISLSHA | Cofactor: Binds 1 divalent metal cation per subunit.
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 4/6.
Function: Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP... |
A0A836RBZ9 | MKLITPKRMKEWEGGIFSKYGVPSFLFMEQAGASLFYFIVEDMKFERNRKIAVISGKGNNGGDGIVCARYLKEAGYDVVVFTLFEDLPRGEDALLNFKFYRDSGGKIFRVSFENLDLFRDELDKYDLIVDAILGIGVERDLDGLYKDVVNIVNEKRAIVLSVDTPTGINLSNGKILGEAVKADYTITFGIPKIGLYTYPGRYYAGNVVLKRVGFPKKDIDECEVEDYLIDRDLIMGIFPGRAPWGHKGTFGKVLTISGSRGFTGAAYFTSL | 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 is a result of enzymatic or heat-dependent h... |
A0A2K8C5H5 | MSIVCSVVMGLVVLSLGLAVGFRSSKDMKELSSPFECGFDPVGSSRVGFSLRFFLVMILFIIFDFETVLLVPSVLWLKEGLVSNLSMFCFISFLTLLLVGILFELKEGVLQWKS | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity of complex I.
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NA... |
A0A2G8LFS2 | MEPRWYPLLAGLCQFNMRLVFSRNTEQCREHAAIFDVSHMLQSKMYGKDRVKFIESLTVADVEGFKENMGGLSLLLNDNGGIIDDLIISKTDKDYLYIVSNAGCAEKDQAHINERLAEFKAKGHDVTFVPISDRALIAVQGPSAAKVIQEGVSFDMSKLTFMTTAEATIFGIPNCRITRCGYTGEDGVEISVPESEVVSLVSQLLDSKAGSVQLAGLAARDSLRLEAGLCLYGNDIDDTTTPVEANLSWTVAKRRRKLADFPGASHVLTHLKEKPTRRRVGLISTGAPARPGSEVMDEAGVTIGEVTSGGPSPILKKNIM... | Function: The glycine cleavage system catalyzes the degradation of glycine.
Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolate + (R)-N(6)-(S(8)-aminomethyldihydrolipoyl)-L-lysyl-[protein] = (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + NH4(+)
EC: 2.1.2.10
Subcellular Location:... |
A0A7J9X065 | MATVDTTMPKEGHELRRRGLLDYTTTTDHKKIGVLYIFTSMFFFLLAGVLALFMRAELAEPGLQILDTQTYNEFFTMHGTAMMLFFIVPLALGFANYFIPLLIGAPDVAYPRVNAFTYWLFVLGGLTAFSGFLTSGGAASFGWTGYVPLADGTYSPGAGGDLWIIGLALSGVSGTLGAVNFVATVFGMRAPGMTMFRLPIFVWNMLVVSALILFTFPVLTAALAMLFIDRNFGGGFFDPAQGGDPILWQHLFWFFGHPEVYIAILPFFGVITEILPVFSRKPLFGYRGFVLATLLIGAYSFSVWAHHMFTTGAVDGPFFS... | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c... |
A0A662DQ06 | MGRPRFLCLAHRQRGRVSNPGLRSRGCCCGDGHCSVLLRTRPGETPTCTVGVAEQDGRRTCCWCRGRADRRRTPSLPPTFRTDVWPCHWCRRCGLRPHGRSGHVRCETFARSQRHGVGTSGARRLPRQDRWIPVRDTRRVGDLPVGGDTLNPLVVLGATGSIGGQTLDVAARIGVPVVAMASHSASEALHELALAHGDAIVCVADPGEGRDRFEASFGDRVHFGPGAVTEAAALPNTTVVNGVVGAAGLRSSLSALYAGNRLALANKESLVAGGSLMLDALEDGGGELVPVDSEHSAIWQCIVGESRADVARVILTASGG... | Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 1/6.
Function: Catalyzes the NADPH-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP).
EC: 1.1... |
A0A3C1DJV8 | MHRCXTRHDVKARIEEFNALAGHEHIHKGMTSRDLTENVEQLQIRQSLLLIRDKAVATLARLAELAVQNDEVALTGRSHNVAAQMTTLGKRFATFTDELLTAFDRLESLLERYPLRGIKGPVGTSQDMLDLVGGDAARLGELEAKVAEHLGFDRVLLSVGQVYPRSLDHEVLGALVQLAAAPSSCAKTIRLMAGHELVTEGFAEGQVGSSAMPHKMNTRSCERVNGFMVILRGYSSMTAELAGDQWNEGDVSCSVVRRIALPDAFFASDGLFETFLTVLDEFGAFPAVIDRELDRYLPFLATTKVLMAAVRNGVGRETAH... | Pathway: Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 2/2.
EC: 4.3.2.2
Catalytic Activity: (2S)-2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamido]succinate = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + fumarate
Sequence Length: 404
Sequence Mass (Da): 43968
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A0A523VJ70 | MKKERNSKQDKLINPVLPPGVKDILAVEAKELKSIKKRLAKVYESWGYEEVFTPAFEYFDVLSLQAGERIKKEMFKFFDDRGDLLALRPDMTISIARLVSQKVSEESLPLRLYYQSNVFRQQKPLQGQPREFWQSGVELIGGKQTAVDAELIMMLIETLKALNLDNFKIGLGSVGFVKALLSAFNKDGSKLKTYLAQKNLVTVNKMLASNKSAAAKNLKRVLGLRGDKALLQAKKLSLNKKASQELASLNKVANLLKKLGYDKYITYDFSLVPDFEYYTGVVFEVYIEGVGLEVASGGRYDNLLSNLGRPFNAAGFAIGL... | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
Function: Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine.
Subcellular Location: Cytoplasm
Sequen... |
A0A7K1E3J3 | MSILGLVMVFSASSVKALQDSGSSVAIVGRQALLFLVGLAIALFLFRAPFAFLKRMSTLSLVLSLIALALPQLPVIGKEVNGNVNWISIAGFTMQPSEFAKLGMILWLAGVLARHEELKERQAPMGPSALAAQILPGIIAMIALILVGKDLGTALVFAAIAAGVLFVAGIQIRWFVAAIAALTLMAVVLILTQSNRIYRIKALLDPFSEEHYQNAGWQPAHSIMGLASGGIFGSGLGAGKQKWGNLAEAHTDFIFAVVGEEIGLLGTLTLLGLFAFLLLSMFKIALRSQTLLERFFVSGVALWFAIQIVVNIGSVTGLIP... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
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)-... |
A0A7K1DZ31 | FVHVDVMDNHFVPNLTFGPQMVQRIVDVSPIPLDVHLMISHVNRWAPGYAEMGCASVTFHVEASDDPIALARQIRSIGARVGLAIKPGTPVEPYLELLPEFDQFLVMTVEPGFGGQKFMESVMPKLQVLRAEARRIGSDVWLQVDGGVTLDTIVIAAENGADTFVAGSSVYNGTNPEHAIAGLRSAVAHHH | Cofactor: Binds 1 divalent metal cation per subunit.
EC: 5.1.3.1
Catalytic Activity: D-ribulose 5-phosphate = D-xylulose 5-phosphate
Sequence Length: 191
Sequence Mass (Da): 20732
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A0A6I3AP54 | MSKSALASDRRYFPLLLGSSIVLCVIGITMVLSASSVASIKSSGSSFSIVLKQLFFLAIGSAFAFLAFKIPTLIYRKLAPLAVVGSCALQLLIFTPLGVNINGNRNWLEFGPIRFQPSEFGKLALVLWVADALTRGGIPLMDRLVRALFGAAPILILVLAGKDLGTAIIIFATLFAMLFAAGISGRALSFFGMLAMLGTAALVVSQSHRLKRFTALLDPFSVANYQSAGWQPAHGIMALASGGLFGVGLGAGSQKWGNLGPEAHTDFIFAVIGEEVGLFGTLMVVAIFGVVLWCGCSLALRVKDNFSRLIAVGVTTWIVF... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
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)-... |
A0A7J9WV89 | MRVYRTYVRIGGDRAVAQGARELQQVRPNRIPPHNLDAEQSVLGAMLESQDAIANVVEILSADDFYKPANTEIYEAIMGLFNRHEPIDAITIVEELSRRGTLEGVGGRPYILGLIEAYPSASAAARYARIVEELALLRRLVSAGNEVQEIGFSMPSDVADAVDAAEGIVYEVGNRRLRDELHQLKALLGENMEQIEQLYERGEHITGVSSGFSDLDDITAGFQKNNLIIIAARPAMGKSSLLNDFTLAAALRRTDPVPVVIFTLEMSRHELVKRFLSSEAKVDSQRINRGTLQEQDWGKLSGAMGRLAEAPIFIDDSANI... | Function: Participates in initiation and elongation during chromosome replication; it exhibits DNA-dependent ATPase activity.
EC: 3.6.4.12
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 892
Sequence Mass (Da): 100111
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A0A7W0S9Y4 | MPFGIGIWEVMILGLVVLLVFGPKRLPEMGRSLGKGMREFKESISSTTDAFNLEQQDDPSREPERDERSAKEHRPAA | 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. TatA could form the protein-conducting channel of the Tat system.
Subcellular Location: Cell membrane
Sequence Length: 77
Sequenc... |
A0A7X7E7F6 | MTDPAPSQSSYTRPQNPDERVGDVYLDADTIAKRVRELGAEITADYQGQDLLLISILRGAIFFMADLSRAIDLPLEMDFLAISSYTQEHSDAGAKAIRFLKDLDQPVKDKNVLVVEDMIDSGLTLHYIVRSLQLRRPRSLEICTLFDRPHQRLVEIPVRYRGFEVPDDFFVGYGFDYRQSFRNIPYVAYLQLGPDQPTLF | Pathway: Purine metabolism; IMP biosynthesis via salvage pathway; IMP from hypoxanthine: step 1/1.
Catalytic Activity: diphosphate + IMP = 5-phospho-alpha-D-ribose 1-diphosphate + hypoxanthine
EC: 2.4.2.8
Subcellular Location: Cytoplasm
Sequence Length: 200
Sequence Mass (Da): 22908
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F3LEH2 | MSFSKASLSKVLVSKTIGVLGGTFDPVHNGHIQIALDALEALGLDEVRLMPCHRPPHRDCPALASEQRVELLRLAVKDHPQLSVDTRELLREQASYTVTTLESLRKELGANVSIVFIMGADAFAQLTTWYQWERLRDLAHIIVMARPNSSSPSHPVLQQWVEQAKLSASESEQYGEDLSANIYAQFHQQPAGGFALLERHLMDVSATAIRTELEGVNDSKAAAHLPRAVATYIQENGLYRSGR | 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... |
A0A7X7GBU5 | MKNNSRTTPLHHRHLAAGARMTEFGGWNMPLVYSSILTEHMQVRRRCGLFDVSHMGRFAVTGGDAEASLAKLIPTDLSHLAINQAVYTAFLNEQGGIRDDLIIYRRPDGYLLVVNAGNRIKDWEWVTNHLLPGAQAVDNTSDSCLLALQGPLAFQVLAELSASASGAEAPAGIPHFACAEGVVADIPVLFMHTGYTGEDGVEIMVNSAGIEGLWDALLAVDSPGTVLPCGLGARDTLRLEAALPLHGQDIDETTLPYEARLGRIVNLDKGRFIGCEALTAAHATGPQRLLVGLVAEGRSLLRHQDRILIGGEAVGCVTSG... | Function: The glycine cleavage system catalyzes the degradation of glycine.
EC: 2.1.2.10
Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolate + (R)-N(6)-(S(8)-aminomethyldihydrolipoyl)-L-lysyl-[protein] = (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + NH4(+)
Sequence Length: 376
... |
A0A7C3T395 | MEDENGLLEPPRPVRVRFAPSPTGHLHLGSARTALFNWLFARGQKGKVILRIEDTDPLRSRPEMEADILEDLRWLGLNWDEGPDLGGPHAPYRQSERGEIYREHARLLVEKGVAYPCYCTPEELREKKERALADGRAPIYDGTCRELDPRRREALRAEGRKPALRFRVPDKEVAFQDLLHGFVRFPAGTVGDFIILRSDGSAGFHFSVVVDDALMGVTHVIRGEDHLTNTARHLLLFEALERQPPFFLHHSLLLGPDGGKMSKRHGATSVREYREMGYLPQALTNYLVTLSWSPPEGKEVLELDELVELFDIGDLSASPA... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).
EC: 6.1.1.17
Catalytic Activity: ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-g... |
A0A1Y1LVB9 | MHQYKTGYERAEVLAILSKHETITYDAIQEMPYLDMVIKEALRKYPTLPFLDRECTKTYTIPNTNVVIQKGIAVYISLTALQHDENYFPDPMVFNPERFSAENKSTIVPYTYMPFGEGYKNCLGNVL | Function: May be involved in the metabolism of insect hormones and in the breakdown of synthetic insecticides.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 127
Sequence Mass (Da): 14711
Location Topology: Peripheral membrane protein
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A0A9E4IBV3 | MVVESPTKARSISSYLGPDVVVESSMGHVRDLPKKELGVDVEKDFQPKYVTSPGKGNQVKKLRTALATAESLYLATDRDREGEAIAWHLTQLLKPKVPVRRMVFQEITRQAIRHAFDNPRDLDTALVESQEARRILDRLYGYEVSPVLWKKVKTGLSAGRVQSVAVRLVVERARDRIRFVRADYWNIVGAFHPVDNPDQRFEAPLAKVAGRRVATGKDFTSQGELKNPNTLKLGKEEAEGLASDLAGSPFTVTDLKKRPYRRSPSAPYRTSTLQQDASRHLGMPPARAMRAAQRLYENGHITYMRTDSVSISSDALATTR... | Function: Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is ... |
A0A5N4AVT2 | MYVKIRNISAKPGDKDDMVDLSKKNLIREVKSLICDETGIAVHKQRLYYKGKQLHDDCSVMDYNIQLNDVIQIMELNSPLIPNTPSDENSHDDDSDKENRSSKPEQTNKSPAKSASDVLSEVVDNSPPESAESKYYRVGDAIDFLLEEYGAWFEGEICEILKAESMDPSDKNLEPDIVFKVKHVSDQGTTEEYHVMCFDEIKPRAYHNLNVPEIETGKIVLVNYNVENPTTRGYWYYFKVKRVNRKDLQGTILVGRDAAPLDKCTVRFVDEVLRIEEPVLLENRSDDRKELPPIRKTVYYCEKCKDVDAKPCRDCGCKVC... | 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: Nucleus
Sequence Length: 8... |
A0A537XPP4 | MTEQIPVRPPGPPLEFSKYEGLGNDFILVFVEDVTPELARFMCDRHFGIGADGVIRLVPASNPDYDFHFRLFNSDGGQAEVSGNGLRCVGRFLHEAGLWSQPRIKVETGGQVKVIEVTVAGGEVSSVRVDMGPAEVQGTVELFDRTWYKVVTGNPHAVTMVDDIEAAPVTQLGPKVETHELFPNRTNVEFCKVDGPDLLSVRFWERGVGVTLASGSGSTAAVVAAGLDRATVRTLGGDLLVEKGPGGHLHQSGPVKHIFDGALP | Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; DL-2,6-diaminopimelate from LL-2,6-diaminopimelate: step 1/1.
Function: Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine and an essential component of the bacte... |
A0A7V9J1X5 | MTLIYFDPVSGASGDMVLGALMDAGAPLDSITESLEALGVPGWELAQETVLKGGVRATRALVTTHDGARRSYSDIKALIAGAPLPEGISSRALETFAVLANAEAKVHGQAPEDVHWHEVGGLDAIVDIVASSAAIEHFAPDAIVTGALPLGSGTVTSAHGPLPVPAPAVTEILTGAVVYGAGGAEFVTPTGAALLKANSTSFGALPPLRPASVGYGAGERDLELPNVLRVLVGDALGDDRMEPWPGVVLETNLDDMSPELLPHVVDELLAAGAQDAWLVPIVMKKGRPAFTLAVLTDAGAEDTLRELIYKETTTLGIRSS... | Function: Involved in the biosynthesis of a nickel-pincer cofactor ((SCS)Ni(II) pincer complex). Binds Ni(2+), and functions in nickel delivery to pyridinium-3,5-bisthiocarboxylic acid mononucleotide (P2TMN), to form the mature cofactor. Is thus probably required for the activation of nickel-pincer cofactor-dependent e... |
A0A1C7D7C5 | MKIAFIGLGNMGGGMAANLVNAGHEVRAFDLSPDALAKARDNGCTPCASIPEACEGAEAVVSMLPNGQIVLSAYTGEVIGAAPDGAIFIDCSTIDVATAREVAAKAEEAGYAMVDAPVSGGIAAANGGTLTFMVGGSEEAFKRAETVLSAMGKAVIHAGDAGNGQAAKICNNMLLAIHMIGTSEAFAMAQKLGLDPQTFYDISSVSSGQNWSMTSYCPVPGVGPQSPSDNDYQGGFATGLMLKDLRLAMDAAETSDAAVPLGARAAALYEDFAGAGNDGLDFSAIIRTY | Pathway: Amino-acid degradation; L-valine degradation.
EC: 1.1.1.31
Catalytic Activity: 3-hydroxy-2-methylpropanoate + NAD(+) = 2-methyl-3-oxopropanoate + H(+) + NADH
Sequence Length: 289
Sequence Mass (Da): 29291
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A0A2T4KA21 | MDDRMVDQSLHNEESSFEFSLRPTKLKQYIGQTSIKNNLEVFIKAAKLREEPLDHVLLFGPPGLGKTTLSNIIANEMDVNLRTVSGPSLDRPGDLAAILSGLQPGDVLFIDEIHRLSSTVEEVLYSAMEDFFIDIIIGKGDEARSIRIDLPPFTLVGATTRAGSLTGPLRDRFGVHLRLEYYNESDLKEIIIRTAEVLGTQVDDESASELAKRSRGTPRVANRLLKRVRDFQQVNEDEQIYIETTKQALKLLQVDDEGLDYIDHKMMNCIINQYNGGPVGLDTIAVSIGEERITIEDVYEPFLIQKGFIERTPRGRKATA... | 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 ... |
A0A0R2H254 | MKVGIIGIGHMGQAITDGLLNQVSPAEIILGSHRINAAMQSYHEKNKITVTDDYSDIMDANPEFLIFTTPAAKTPEIMDQFKGIDSDVTVLSVASGVSLGDIQTKFPENPSALVVPNTPVSVNHGTLGVAMGPHVTKSNNIESFLGLLGDVYTVPESEFNIFGTITGCGPAFLDVFLSALGDAAVKNGLPRALAYEAAASMAKGSASLLQESGLTPDALKDQVTTPGGSTIRGVVSLEKNAFRSAIIEAVDAANN | 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... |
A0A7V9BYV3 | MALVPLLWAWRDATPRRAALYGFCFGLAFFGVILSWIWYFGAVAYLPLTVAGGAYIAAPGALIAGLARFGIRSPWLTAGTWVLFEQLRGRFPFGGLPWGETGAALHDFPVARSLASWGGIALVTFLVVAVNGLLLDAFMDARTRSWRPLSFAAAGLAGVVVAVGLGHGFRYEPTETGHLRIATIQGNDQNRDITDPIEFEAVVVEQHFELANTIEGKYDLIVFPESSLNRNPEQDPDLRKRITDIGAAHDSAMLVNALLPAPDGRDYNTNLLFDPDGELQGTYAKQHLVPFGEYVPLRRFLDWGGILDRIPYDYAPGKGR... | Pathway: Protein modification; lipoprotein biosynthesis (N-acyl transfer).
Function: Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation.
Catalytic Activity: a glycerophospholipid + N-terminal S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipopr... |
A0A537Y7Z1 | MPDRLTALDAQFLYMERPTAHMHVGGVSIVDPSTKPDGPLLFDDFKAHVLRRMHLVPRFRQKIAFLPFNVGRPMWTDEERFDIDFHMRRASIPSPGGHKELADFVQRVHSRPLDRTKPLWEIYFIEGLEGGQIAIYSKTHHALIDGISGMDIASVLFDFTPAARDVEPEEWTPEKEPTTLELLRHWAVDSVTHPIEAMAHQASGAIGAPKAVLGHVGTVLGALQQQIGSGMAPPSPFNVPIGPNRRFSFTDVPVADTKAVKNALGGTVNDVILAGVAGTLRRALIARGVSTANLSMRAMVPVSTRDESQKMALGNRVSMF... | 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: 790
Sequence Mass (Da): 88175
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A0A2T0TB68 | MGTPDFAVTSLQRLLGAGCEVVAVVTAPDRPSGRGLQLTPSPVKKAALAANLPVLQPERLRDPAFLDELASYKADLQVVVAFRMLPEVVWGMPTVGTLNLHGSLLPQYRGAAPINWAIINGETETGVTTFFIEKEIDTGQLLFSDREPIYPDDTAGSLHDRLMERGADLVLKTVRAIEAGDYTPTPQPESGDLKPAPKLSRDSTRIDWNQSVHTIRNFVRGLSPYPAAWTMINDRFFKVYAVSVANDSPFAADPGQAWTDEKKRILVRAADGWLSIDSLQAEGKRRMTAEEFLRGNRL | 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... |
A0A2D6L0P4 | MQTMEIWTDGSCLGNPGFGGWGAISEAFEISGASSATTNNIMELTAVLRALERCIETDVKDVIVWTDSFYVKNGITSWVNGWKRNGWKTSNGQPVKNKQLWMDIDAVARKMHSVEWRWVKAHNGHPQNEAVDALARGRATALKKSSSPKV | Cofactor: Binds 1 Mg(2+) ion per subunit. May bind a second metal ion at a regulatory site, or after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
EC: 3.1.26.4
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Subcellular Location: Cytoplasm
Sequence... |
A0A7V3J118 | GRLSRLLNDLLVSTDATGNLAVLRTPPGAADYLASAIDRAALPYVVGTIAGDDTIFVAAREPMTGAELAAAIDNLK | Pathway: Amino-acid biosynthesis; L-arginine biosynthesis [regulation].
Function: Regulates arginine biosynthesis genes.
Subcellular Location: Cytoplasm
Sequence Length: 76
Sequence Mass (Da): 7796
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A0A6V8C9X6 | MNPPTKHVFKPHDARTPKEEANPLNPMQWVPEGWRPKLVAVDIDGTLTDANKRLHVGAVEALRALEAAGIPVVICTGNTRPIAYGLWRFIGLSGPLVCENGGVLWYPNGEVVLRAQGSEAEEACRWVAEQLPGIDADGIATNRWRESEWCLKTGEDMEAIQAALSDSRWSHLTVLRTGFAIHVMDPCLSKGQGLAEVLDRLDLSPDDVLAVGDAPNDLSMFELVGWSIAVGGAFPEVAAGASVASPEPHGATFPPLVEAILASE | Function: Catalyzes the dephosphorylation of 2-phosphoglycolate.
EC: 3.1.3.18
Catalytic Activity: 2-phosphoglycolate + H2O = glycolate + phosphate
Sequence Length: 264
Sequence Mass (Da): 28325
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A0A6A8MSG8 | MQGLRLSRSFILRASVAIAAGALSATAFLPIDFGWISLFVLIPLFWAWRDQKILTASLIGFFYGVGFLLVLMFGLHYLGFLAYLSLAFLAALYYAAIGAVVAAFAQRGMRNPWLTAAIWIMSEGLRVRWPLGGLAWGELGGALHDFAVPRSLAGWGGVALISFLVVAINGFLYDFYLGLSSNKKRMRALSGLISILLLVAVGYVARFEPTPTGRIRFALIQGFDKADAELASSAIGPAETQAHFDLAKGLEKNFDLIVLPESALYDDPQVNPELQAQIVSLAEKHNAVVLVNTRHYRANGKLYNTNFAYDPRGEVIGRYS... | Pathway: Protein modification; lipoprotein biosynthesis (N-acyl transfer).
Function: Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation.
Catalytic Activity: a glycerophospholipid + N-terminal S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipopr... |
A0A7C6FNJ4 | MNDMKILVAKHIGFCPGVKRAYTMAIQAFDINYQPVYLLGELVHNHQAVKMLIERGARLEDEVEQIPDKVTVVTRSHGLERKTREKLLEKGVTIIDTTCPRVRKVQSLASELEKKGYTMIILGDPNHAEIKALISELNTKPLVLGKNSTDWENKLNTLPENQPLAVIEQTTFPQQQYLDFCRLLEEKNLTDRCLIYNTLCLETEYRQNELRSHLQTGKIDVVIILGGKHSSNTRGLYLIANDQAPRTIWIEDPNEVEKTWFQPNQTILIVSGASTPDCAVKELMKKLNKGKVYE | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Pathway: Isoprenoid biosynthesis; dimethylallyl diphosphate biosynthesis; dimethylallyl diphosphate from (2E)-4-hydroxy-3-methylbutenyl diphosphate: step 1/1.
Function: Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of is... |
A0A3A4V1W7 | MIITIDGPAASGKSTIAKKVAKKLNYHLIGTGLMYRAAALQALLENIDITQKDQIKELIKRLQVSLSFSWEDGVERVLVNGVDVTKKLSTPEVDAYVSDVAKISDVREMMVERQRKLAKQGDVVVEGRDIGTVVLPDADIKFYVTASTKERARRRCAELAAKGHICDKQELEQDIMKRDKIDSTRKLSPLSKAKDAYPIDTTGKTIEEVVIQIMAIIKEKK | Catalytic Activity: ATP + CMP = ADP + CDP
EC: 2.7.4.25
Subcellular Location: Cytoplasm
Sequence Length: 221
Sequence Mass (Da): 24626
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A0A537VJ70 | MATRWLVAGLGNPGPEYSRTRHNVGFRVADELARRLGARFKRSKHSAQVADARDGDAQLILAKPQTFMNDSGRALAALARYYDVPLDHVIVVHDELDLPFGAVRVKLGGGTAGHNGVNDVARAIGPGFVRVRVGIGRPSGRKDPIDFVLELYGKREEAEVPATVDLAADAVLTVVREGVSSAQTIFNKRTE | Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Catalytic Activity: an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+)
EC: 3.1.1.29
Subcellular Location: Cytoplasm
Sequence Length: 191
Sequence Mass (Da): 20636
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A0A538J3F5 | MARVGEGEAVTAQPAAYPTRRLPSRRRRLLRLIPLGVAVALVWFLVSLFQPFAGSGHGSLDVTIPRGAGVGKIGDILAKKGVVSNGFLFEIRATLAGRRGDLKPGSYVLKRDMSYGAAIDALVKGPGSTLVSVTIPEGLSRREVAARLAPLGLRGSYIRATERSPLLDPRRYGAKTPRDLEGFLFPSTYQIRRGGPVKTLVAKQLAAFKLEIGKVNMRAARHVNLTTFDVVTIASLIEREAQVPSERVLIASVIYNRLRAHMPLQIDATVRFAIGNRTSPLTKAQLRTRSAYNTYLHRALPPGPIDSPGLASLRAAAHAA... | Function: Functions as a peptidoglycan terminase that cleaves nascent peptidoglycan strands endolytically to terminate their elongation.
EC: 4.2.2.-
Subcellular Location: Cell membrane
Sequence Length: 368
Sequence Mass (Da): 39937
Location Topology: Single-pass membrane protein
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A0A0A3IGD8 | MTEIIPEISVLLLIIVRVSAFFVSVPFFSYSRIPPQLRIALSVVFAWMMYYTINVEAIPIDGNYLLLVLKEAIIGVLIGLVAYMVMTAVQIAGGFIDFEMGFAMANVIDPQTGTQTPLMGQFFNFLILFVLLAINGHHLILDGIYYSYQFLPIDQVFPDFGNDNIAEFVIRTFGSVFIIAFQMSAPVVATLFLVTMALGITAKTVPQLNIFVVGFPIKIAVGFLVLIISMGVMIEVMEKVIEMMILSMRDFMQMLGGA | Function: Role in flagellar biosynthesis.
Subcellular Location: Cell membrane
Sequence Length: 258
Sequence Mass (Da): 28639
Location Topology: Multi-pass membrane protein
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A0A6A8MNG6 | VMGVLKNNFSVVFHESSTHKFSNTVIPSELEKIYVIIGPEGGITQEELEAFKSAGAGVARLGEPVLRSAHAGFAALSALQTKLGRW | Function: Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit.
Catalytic Activity: S-adenosyl-L-methionine + uridine(1498) in 16S rRNA = H(+) + N(3)-methyluridine(1498) in 16S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.193
S... |
A0A7V2VK28 | MEGPLPPLNSSEPERKPGLVPRAGRFLLRLVREIVETVLPALLIALLINLFLAQATVVEGQSMEPTLHDHERVIVEKVSYRLHPPRRGDVVVLRNPGGEGLLIKRVVALPGEEVAVQEGHVIIDGRPLEEPWSVQVGGADLPPTTVPPDHVFVLGDNRPHSNDSRTFGPVPIDQIVGRAWLIYWPLDQVGRVD | 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: 193
Sequence Mass (Da): 21275
Location Topology: Single-pass type II membrane protein
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A0A2E7UI21 | MIFEPVIGLEVHIQLSTKSKMFCGCSASYQEQEPNSLVCEVCLGLPGTLPSVNQEAIRSAIKLGLSLNCRIANLTKFDRKNYVYPDLMKGYQISQFDLPIATNGTIMVDDNINKSETLIRINRVHMEEDVAKLTHDDISNSVIMDINRSGVPLLEVVTEPDFSSARQAEDYLVQLQSIVRYIGIGTANMEEGSFRCDANVSIRKKGTQKLNEKVEIKNMNRIKAVSRAIEYEIKRQKEATKNGERIVQETRGWDDIKSKSIPQRSKEDAHDYRYFPEPDIPALQISEKFIEGMRSKLPELPKSKLQRFIDELGLSEYNAS... | 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 ... |
A0A5C7P6T2 | MSAATPFGDGASGAGSAIQRLCPARSGPPRLADVTTAQTPALPGSLGDLSVLVLGTGVSGRSMASWCRRQGARVVVADPRGAGPEVPCLAGIDAVLMSPGISPRGPDAAPVLAAAAAAGIPVASELDLFAAALAKLAASSGYAPEVVAITGTNGKTTTTALTAALLNASGRRRARVAGNIGPALMDELSAALDDDALPDTWVLELSSFQLSYGRNFAASVGVLLNVTPDHLDWHGGFADYERVKLTVLTTSAKAIVCREDVAGPRPPASTGTAPTTTTFGIGVPHAVGDYGVSSAGPTRWLVQRGTDGRLDPIVAVESLR... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).
Catalytic Activity: ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-... |
A0A537YWQ3 | MRRQLYPAVVMVLVMTLLTGLVYTFAFTGFAQLVFPGKADGSMIEVNGKEVGSKYIGQAFVDTHGKPLRKYFQSRPSAATGPDGKTEAGYDPRLSLGSNHGPTNPCFVPDPKVPCRDDHGKKIPPIVIERVRAYRKLNGLAPNSKVPVDAVTASASGLDPDVSIMNARIQARRVADERGLSLARVRKLVDHYTSDRWIGIIGEKRVNVLELNLALDRIATRGT | Function: Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit acts as a catalytic chaperone that increases the ATP-binding affinity of the ATP-hydrolyzing subunit KdpB by the... |
A0A538CM62 | MIALASQSPQRRAILEALGVPFRIVDVDVEEIEAGEPQEVARDNAVRKATAGASAAQSGEVALGVDTLVALDGRIWGKPADEDAAAESLRALGGRTHDVVSCVALVRDGKPATAIEVTRVTFHPLDAATIRWYVASGEWRGRAGGYAIQGRGGALVSRVEGDYLNVVGLPVGALAGLFGGFAAFLAEGN | Function: Nucleoside triphosphate pyrophosphatase. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + H2O = a 2'-deoxyribonucleoside 5'-phosphate + diphosphate + H(+)
EC: 3.6... |
A0A538BCD4 | MTTIWRIRDRATFVALRRSERRVRRGPITVTWAPGDPAEPPRVAYAIGKHVGGATVRNRVRRRMRAIIRDLERPLGPGAWLIGATPEVAKLSYGELKAVVAEAVGALDREQGGA | 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... |
A0A3P1X084 | MNPNSGEGGLRRLIRFWWSSLPLRVLATTFVASCVILVLAGLLLTQQTATGIVDAKRASAVREAAGMQRFMQEQLMLPEMRGVATYEQLSRLAELAGAQAGQFQVIIQGPASRVYSATGILYESIPVEMAERVRTADGMFIVPTRLRATSAALQGQPGIIVGSALLSPVGERFPVFYVFPMTSEVATLVDVQRAVVSTGAALLIGLTAIAYLVTLQVVRPVRKASRTALRLASGQLDERMTVRGSDDLASLAVSMNTMASDLQQRIRELEHLSAVQRRFVSDVSHELRTPMTTIKMASDLLYEGRQDLGPQDARTVELMA... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Cell membrane
Sequence Length: 520
Sequence Mass (Da): 56558
Location Topology: Multi-pass membrane protein
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A0A538KHQ4 | MPSPGCSRLAQASLTSSASRGEATRIWPRRSLCSAKKAGPNREPSGADAVSGVERISEAFASARADGRRAALMPYLMGGFPDLNTSFEIARACVDAGGSLLELGIPFSDPLADGPVIQAAGTTALNAGVTLEDVLGLAGRLSHDGVPVVIMCYENQILARGVERFADMLQAAGVSGLIVPDLPLEEADATVAACDECDVALVPLVAPTTPDERLEQIASRARGFLYVVSLTGTTGADGVIVGSRLVRAAEEAMDPPAAV | Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5.
EC: 4.2.1.20
Catalytic Activity: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan
Sequence Length: 259
Sequence Mass (Da): 26646
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A0A2E5EVK3 | MSYLRFFLFEACIGIKRSFLMAFITVCTMAFSLVMLGVFLMISFNLSQLSEYVTSKIEIRVFLKETLTVREVQQFQRELQQEPHVDSVTFVNRDRAWRQFKNDYESLHLANYLDQNPLPHMFKVSLTDNEFIIPVGEQIQNRRQKVEKVFYGGDVAGRIHQFSKFIRWFGLGLGSVLTLFTLLIIVNTIRLTIMSRQTEISIMKLVGATDRFISGPFLIEGCLFGVFGALFSVAFLNSVYVFGTQFVLQKMPFVPVLLEASEMRSVYVILGILGVLLGVLGARISVSKSLKVTI | Function: Part of the ABC transporter FtsEX involved in cellular division.
Subcellular Location: Membrane
Sequence Length: 294
Sequence Mass (Da): 33549
Location Topology: Multi-pass membrane protein
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A0A7V9IHB8 | MRPVAQPVSTQTGRREPRERGRFVKEAWAELKKVEWPGRSQVIQGTIVVLIACVIVGAFLYGADQAFKPFVRAVLLGE | Function: Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation.
Subcellular Location: Cell membrane
Sequence Length: 78
Sequence Mass (Da): 8709
Location Topology: Single-pass membrane protein
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A0A0F2J3B0 | MNYQEIIQEIKDRIDIVDVISQYVTLKKAGSNYKALCPFHNEKSPSFVVNPQKQIFHCFGCGAGGDITTFIMKHEAMSFWDALNLLAKQAGVAIDRSSLNPNARSNTKAVMDILNHSLEFYTKQLYSNQLAKQYLTQRGISKDTIEKFSLGYAPSGRGNLYTSLKKAGFSDNDIMSAGVVNRSENGFYDIFRERILFPIFNLQSEPIAFGGRIIKDGQPKYLNSPETEVFKKKKTLYGLNAAKDNIKKQGYIIIVEGYVDFLMCYQHGIDNVSAPLGTSLTEDHIKIIKRFTSNLITLFDADEAGIKATKRTIEIALQNN... | Cofactor: Binds 1 zinc ion per monomer.
Function: RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.
EC: 2.7.7.101
Catalytic Activity: ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.
Sequence Length: 564
Domain: Contains an N-termi... |
A0A239ISU4 | MNPPDEPPYRSGFACLVGRPNAGKTTLTNALVGEKVGIVSNRPQTTRHAIRGVVHRPGGQLVLVDTPGLHRPRSLLGRRLNDVVRDTLSDVDVVVFCVPADQPVGTGDRYIARQLAEVRAPVVVVVTKTDAASRKQVAEQLLAASSLVEAAEVVPVSAVRGDQVELLEDLLVGLLPEGPPLYPPAQTTDEDVERQLAELVREAALEKVFQEVPHSLAVTIEELIRRPDPKRDGGELVEVHALLHVERPSQKPMLLGRGGSIVKAIGTEARQGMEALLGARVHLDLHVTVLGEWQDDPKKLNRLGY | Function: An essential GTPase that binds both GDP and GTP, with rapid nucleotide exchange. Plays a role in 16S rRNA processing and 30S ribosomal subunit biogenesis and possibly also in cell cycle regulation and energy metabolism.
Subcellular Location: Cytoplasm
Sequence Length: 305
Sequence Mass (Da): 33065
Location To... |
A0A7V9RXR6 | MGLVGKSHGLQGDFVVERGSEDPDRFAVGATLLVDGVPARIVGSKRARGRPVIRLDREVSRGAELQVDRAELPVPEDGSYYVFQLVGLAVEEEGGRSLGQVAEVTPGPANDVLELDTGLALPLVDACVQEVDLDSGRIVVRRGFAGAE | 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 ... |
A0A7V9T8I3 | LDPRLDLLPMELRGEAVLGRAAAASAVARFCKGIVGAVGPYVVAVKPQSAFFEALGSDGMRALEDVCDYARSIGLLVVVDAKRGDIGSTARAYAAALLEPRDGSAPLADATTASPYLGQDSVEPFLAACRRHGAGIFFLVRTSNAGAAEIQDAILSDGRPLWQYLAELVHEWGQPLVGERGLSSVGAVVGATHPRAVSQARKLMPQTLLLLPGVGAQGATPADVARAFTSGPASALVTASRSVIYAFRGTEEDWRAAAASEAERLATQVWAAAGW | 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: 275
Sequence Mass (Da): 28596
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A0A1G9L722 | MDWVGWILALVLAGAVVFLLLRRRDSRAALDAETSRLRQHEDRLLTDSEGLQARAEKLDAQRSELKRKQASIQAELERVAGLTREQARAEIIEEAERTAKLQAAQLAREIEQRARRDAEREARNIIVGAIQRIAAEQTSESVVTVVQLPSDDMKGRIIGREGRNIRAFEQISGANLLIDETPETVLISCFDPVRRETARIALEELVADGRIHPQRIEEVYAKAERTIDEEIRHAAEDALTEVGIVDLHPNLVPTLGSLAYRTSYGQNVLKHLVESARIAGLMAAELGLDVATCKRAAFLHDIGKALSHENEGPHALVGAD... | Function: Endoribonuclease that initiates mRNA decay.
EC: 3.1.-.-
Subcellular Location: Cell membrane
Sequence Length: 452
Sequence Mass (Da): 50057
Location Topology: Single-pass membrane protein
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A0A7X7E8H1 | MAEHTYDAGDIQVLEGLEPVRKRPGMYIGSTGHRGLHHLVYEVVDNSVDEALAGACNQIDVTIFPDCSVRVVDNGRGIPVKVMPQFDRPALEIVMTKLHAGGKFGGEGYKVSGGLHGVGVSVVNALSEWLTVEVCRDGYRFRQSYARGVPTSEVEKVGKSDGQSGTSTHFRPDPEIFNDLNYNFTTLSQRLREVAFLNRSLRITLVDEREDDGDGDGQSSDSDDDYAAHDDLDLTVERVFSADSLTATGEGETGAGEVMARKRLEPRSVVYCYDGGIVDFVKHINKHKDAIHPKVIHFEGQEADQTVELAMQWNAGYNDN... | Cofactor: Binds two Mg(2+) per subunit. The magnesium ions form salt bridges with both the protein and the DNA. Can also accept other divalent metal cations, such as Mn(2+) or Ca(2+).
Function: A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modu... |
A0A2E7UK98 | MINHFKNKALTIAGSDSGAGAGIQADLKTFSSLGVYGTTVLTAVTAQNTIGVQGVEMLPVKIVESQIKSVLSDIGTDSVKTGMLGNAEIIHTTARTLEYFTYNNLVVDPVMVAESGDPLLEDSAIEAYVNHLFPMASLVTPNIYEAEKISGIKITNEKSLIESGNKILDIGSKKVLIKGGHFNGEFSEDVLFTSSGITKLREKRVVTNNTHGTGCTLSAAITAFLAKGDNVEFAVRKGKEYVTKALQESYDIGKGTGPVNHFFGT | Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; 4-amino-2-methyl-5-diphosphomethylpyrimidine from 5-amino-1-(5-phospho-D-ribosyl)imidazole: step 3/3.
Function: Catalyzes the phosphorylation of hydroxymethylpyrimidine phosphate (HMP-P) to HMP-PP, and of HMP to HMP-P.
Catalytic Activity: 4-amino-2-meth... |
A0A7K1C477 | GLAALACGAFHIRTGGKVYFNTTPLGRVVTGTLLVRAMHADGVEIWGDGSTYKGNDIERFYRYGLLANPNLRIYKPWLDSDFVAELGGRKEMSEWLAARNLPYRSSIEKAYSTDSNMLGATHEAKLLENLDESYELVEPIMGAKFWDPSVAIEQEDVSVTFRQGRPVEINGKDYTDPVALVDEANRIGGRHGLGMSDQIENRIIEAKSRGIYEAPGMALLHIAYERLLSAVHNEDTLAAYHNEGRRMGRLLYEGRWLDPQTLMLRESLTKWIASAVNGSVTLRLRRGDDYTILDTRGEGFSYHPDKLSMERTDDAAFGPA... | Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3.
Catalytic Activity: ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-arginino)succinate + AMP + diphosphate + H(+)
EC: 6.3.4.5
Subcellular Location: Cytoplasm
Sequence Length: 357
Sequence Mass (Da)... |
A5D5Q7 | MKGVEAAAVGAKPEGLKKLTVKIAGMSCAACASRVEKALSKIPGVEDARVNFAAETATVDYHPELVSPATIFDKIKETGYRPVMGRAELKLSGMSCAACAARIENGLNKLPGVARAAVNFATEKAIVEFDPAEIDVPRIKKAVADIGYRAYEVDDRTTAGLEREEREREIRRQKSLVIFSGILSAPLVVYMLAMVFNLHHKIPAFFLNPYFQFALATPVQFIAGANFYKEAYVALRGRSANMSVLVALGTTAAYLYSAAATFFGGRIGVSEVYYETGAIIITLVLLGKTLETIAKGRTSEAIKKLIGLQARNARVIRNGQ... | Catalytic Activity: ATP + Cu(+)(in) + H2O = ADP + Cu(+)(out) + H(+) + phosphate
EC: 7.2.2.8
Subcellular Location: Cell membrane
Sequence Length: 820
Sequence Mass (Da): 87379
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A0A3C1DNA9 | MTSRIGSWTVIVPMKAPEQAKSRLRETRQNGPRLPDATELATAFLLDVVQAASRATRVAEVLVISPDTAVAAVLHNQSSRFLVQDHDPTRAPAVTGINHAITQATLAIRATNPGTSVAAITGDLAALSSDSLDAALALADAFATTCFVADRQDTGTTALLLPRGTWTAPQFGAGSATAHRAAGIREISDDVGLDLRTDVDTADDLAEAIDLGVGPNTARLMS | Pathway: Cofactor biosynthesis; coenzyme F420 biosynthesis.
Function: Guanylyltransferase that catalyzes the activation of phosphoenolpyruvate (PEP) as enolpyruvoyl-2-diphospho-5'-guanosine, via the condensation of PEP with GTP. It is involved in the biosynthesis of coenzyme F420, a hydride carrier cofactor.
EC: 2.7.7.... |
A0A6I3X9N0 | MSRTSGVVLVDKPAGWTSHDVVAKMRGILRQRRIGHAGTLDPMATGLLVIAVGPATRLLRFATDTQKTYIGTVKLGEATDSLDADGVVIATAPIPELSPLEAQAIAATFLGPQQQIPPMVSAIKVDGKKLYELAREGKEIERKPRDIVVSKFEIAESEVPGSWAFEVTVTPGTYVRVLLADWAVQAGTLGHLTALRRTASGASLVDAAHTIESLQEAVAQGESVLAAPLEMTKQFPVVVVDDATVLAIRQGKTVAFDTPLDGDYLNAVDGTGELVAILRPKDDRWQPDVVLAIESTVKDS | Function: Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
EC: 5.4.99.25
Catalytic Activity: uridine(55) in tRNA = pseudouridine(55) in tRNA
Sequence Length: 300
Sequence Mass (Da): 31950
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G1NN33 | MDAAGSCGLQRKETLFGDGRAAARTEVEKQNHRMSQIGRATHGSSSPTPGCTQDPSQVQNSSSRLRHAVCIFYLVLRALDTIEDDMTISLDVKVPMLIEFHSYLYQPEWKYMESKEKHRQVLEDFPTISMEFRNLAKVYQDVISDICHKMGVGMAEFLEKKVDSQSEWDRYCHYVAGLVGIGLSRLFSASELEDPIVGQDTELANSMGLFLQKTNIIRDYLEDQLEGREFWPREVWSRYTKKLSDLTKPENIDMAVQCLNELITNALRHVPDVLTYLSRLKNQSVFNFCAIPQVMAIATLAACYNNKQVFRGVVKIRKGQ... | Pathway: Terpene metabolism; lanosterol biosynthesis; lanosterol from farnesyl diphosphate: step 1/3.
Function: Catalyzes the condensation of 2 farnesyl pyrophosphate (FPP) moieties to form squalene.
EC: 2.5.1.21
Catalytic Activity: 2 (2E,6E)-farnesyl diphosphate + H(+) + NADH = 2 diphosphate + NAD(+) + squalene
Sequen... |
A0A2S6SH45 | MKNYPLWKSVTVIFVVILGIIFTIPSIIYSEDSSNWYLQNKINLGLDLQGGSYLLLQVESDVLLKEEFENISDTVRIISRNEKTNFVNIVSKSDYIEFTYENSQSINEIRNELISNYRDIDVVINNNKMKVILNDNFKKRIQESAIKQSLEIVRKRIDESGTKEPLIQKSGKSRILLQLPGVKDPERIKDLLGKTAKLTFHMVDDENTAALKTNKAPFGKIIVSDYENPDIQYLVEKKSSVGGENLVDANPSFDPSEGHAVSFRFDTTGAQKFGKATTENIGKRFAVILDGVVITAPVIRSAITGGSGIITGNFSSQEAT... | 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: 517
Sequence Mass (Da): 56725
Location... |
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