ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
|---|---|---|
A0A0S8JQT3 | MVIHEDISSFSVQRPVLTVGIFDGVHLGHRYILEKLKERARQLDGETVVLTLWPHPRIVLNQQDDHFKLLNTLEEKKYLLEQAGLDHLIVHPFTTGFSRLSSCDFIREILVDKYRILHLVVGYNHRFGRDREGNFRKLKDCAGKYGFGIEQVEAFQTAGRKISSTGIRDLLLKG | 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: 174
Sequence Mass (Da): 20054
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A0A971BW18 | MQYIFTAILLALCDRFLKLYIIRNIAFGERVPFIRGVLDLTHVENTGAAFGRLQGMRWPLVAISAAAVIVIFALILTRKVRRPFAVWSLTLMAGGALGNLVDRLLYGRVVDMFLLTFVDFAIFNLADCFIDVGGIALCIYLIFISGREDKEAKEAKEAEKASHGGGGDG | Pathway: Protein modification; lipoprotein biosynthesis (signal peptide cleavage).
Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, ... |
A0A829PTM4 | MREFVKAGQVSYQYSTVHTESFSGKALVIGSPTTSKVTALELYLVFPLSNEESTISLVRGTIVTGGVVLLVLLAAAALLVARQVVLPVRSASRIAERFAEGHLSERMPVRGVDDMARLAVSFNDMAESLSREITQLEEFGNLQRRFTSDVSHELRTPLTTVRMAADLIYDNREELDPALQRSAELMVNELDRFETLLADLLEISRHDAGVAELAVEQVDLRDTVKAVVASVQHLADELDTSVELDMPDKEIIAEVDPRRVERILRNLVANAIDHSEHKPVTIRMAADIDSVAVTVRDRGVGLRPGEEKLVFNRFWRADPS... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Cell membrane
Sequence Length: 490
Sequence Mass (Da): 53395
Location Topology: Multi-pass membrane protein
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A0A975H9C4 | MSQNQAAGKWQKYKNVNLRRAIVACAFCVVFGFYLTYDNFSRANQFMGYLSLFTALGAAASMLIMLYSRRDPRKNARLIPLAVILLMLIYGINCAVFVVYGGVGGTSLFILFLVPPVAFYCFNMFYGGIFSALVAIATCVYMWSPLRAFGYQFPDLVFQRAPFIFLAEVIICILAQIDVVRAQSRQDQALQAAEEANRAKSEFLANMSHEIRTPMNSILGFCELILREKGLSKRTREYCMDMRSSGRSLLHIINDVLDFSRIEAGKLTITENNYELSSLARDISNMFAFRAREKGLGWEVEVDESIPDSLYGDVYRIRQV... | 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 some genes that are critical to the sporula... |
A0A0K0E5I3 | MMAPTKKNIDLSALKKANVPIIFIVGGPGSGKGTQCDKIVAKYGFTHISSGDLLREELKSGSERAGELLKIMELGQLVPMEVVLDLIKERILQSIEKGSKGFLIDGYPREVVQGEKFEAEIQEAKTVIYFEVAESTLVKRLLGRAQTSGRADDNEETIKKRITTFNQSTAPVVDYYEKKGKLYKINAEGSVDEIFSKVSTHLDKIL | Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Catalytic Activity: ADP + thiamine diphosphate = AMP + thiamine triphosphate
EC: 2.7.4.3
Subcellular Location: Cytoplasm
Sequence ... |
A0A3D1LGS7 | MSFVYKGLKANFEKLTVTEHELDRQMDRLRQQTPRVIPVTERAAKMGDDVVLDYAGFVDGKQFDGGTAKEQVLTLGSGMFIPGFESQLVGAHAGSDVLVTVTFPKDYRATDLAGKPAEFRCHIVEVREKSAYELDDVFAKEVGGCQTLEEMKQKLRQSLQDYYDERAEMEVQDTLMRQAAATLDYTPSAQELKEGIDAQVELLKAQLGRKGLTLEAYLQFTGKTEQQIRDDAKPEAENSLRIQKSAERIALLEGLTATDEDYANELAAICRQNGLTMEQLKPHMNAQFEASVRDNIRMKKAIAFVRANADVTVVDAPASK... | Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
EC: 5.2.1.8
Subcellular Location: Cytoplasm
Sequence Length: 321
Sequence Mass (Da): 35809
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A0A3D5MME4 | MAEAVQGPAARAERGRPGSLSRCPDSGRDMDAKTEFLEVKGGTEARGLRAASPWEAAPPVGSDRPVAAIGVFDGVHVGHRSLLRRGLVLARERKAPLVAVTFWPHPDRVVRRDGGKGGLLTTLGDKAALLQAAGAQRVLALKFTEQVAAVEPEPFFTETLVETLGCQAVVVGFNFTFGRGARGDAALLAELGKAAGVEVIIHPAVRIRGQVVSSSAVRQALREGDVERATLLLGRPHSLVGTVSRGYGRGQSLGFPTANVEYPGEVLCPATGVYVCSLARGDVAPDDLSQALPSVANLGFRPTFAPPDGEGTPPGLEVHV... | Pathway: Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step 1/1.
EC: 2.7.1.26
Catalytic Activity: ATP + FMN + H(+) = diphosphate + FAD
Sequence Length: 388
Sequence Mass (Da): 41015
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A0A7S2V141 | FFTARPVGVRGGIDFGFTGLVRKVDVTAIRSRLADNDVVVLTSVGFSGSGDMFNVNSEHLAAECAAQLGATKIIYVTEGQQLMDIRTNKQIQSLRIRDAKSFLLHNGIDPKYGLEGAPLPENGDSPGGPRAKVTPTPESAQDYRFATLNIMHAAIQALSKGVTRAHIIGPYSGAMIQELYTRDGSGTLLARDLYEDIRRAEVGDVPGILEIIEPLQEAGLLVPKNREYIEQEMKHYHVYTRDGMVLAVAFLRRFGPHHAEIGSLGVHPRYRKAGRGDTMLGYMERVAAAAGVHTTFALSTQTMQWFVERGYSEGKVSDLP... | Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 1/4.
EC: 2.3.1.1
Catalytic Activity: acetyl-CoA + L-glutamate = CoA + H(+) + N-acetyl-L-glutamate
Sequence Length: 357
Sequence Mass (Da): 39529
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A0A5C6ZWV3 | MRVRFCQTEGTNNVTPCETRPAAPSSARCPGGRRGRARRRSASPPFATATVQRPTRPLMYGARKLPATVMLRTASPPEAGGLARAGRRRRFQPGVGSMVIERHWLRWPAAALVFVAATWLNLQLQPYLNGRGPLLPYFPSLVLVGLACGLGPALAFLAASALAVLYFWIEPIGQIFPVNSPPDATLVVLYLAAGALIASVSAWAGRLMQKERNSRRRLNLALAAGRMVTWDWDMVTGFANTAGGAKQLFGRHWSTMEDMLADMSAEDAERFRERYRYATESGGRFSLACPITRPDNAEVVWTQFDGYVSLDAKGRAAHAY... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 838
Sequence Mass (Da): 91103
Location Topology: Multi-pass membrane protein
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A0A970EYM2 | MRMRKKKNLASRMERVRSLLVENPERFAGSWDKLSSGRPIHLEIGCGKGKFITETASANPNVFFVALEKIADVLVMAMEKASREGLTNVLFIRSDAAMLEEYFSSGEITRIYLNFSDPWPSKRHQKRRLTSEGFLNIYRKILSGDGSVCLKTDNRDFFEFSVRELERCGWRVENVTFDLHGAMQQTAASQGSTDTGGDAGNSNGYQPVFNPEGEAVTEYEQRFASMGVPICRLVAFPADADIDKP | 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: 245
S... |
B5IDU2 | MNLKEEIMKLKKERNAIIMAHNYQIGEVQRIADFVGDSLELARKATQVDADVIVFAGVDFMAETAAILNPDKLILIPSKIASCEMARFLTPELIKEYKKKYPDATVVLYVNSTADCKALADITCTSANAVKVVNSLDADTILFGPDSNLAHYVAERTNKKIIPVPPNGHCYVHTNLNVENVPYDGVLMVHPECPAELQAKADVIASTGGMVKYVAKSNAKKFIVATERDMVERLKMEYPDREFVPAWPYAICLGMKQINLQKIYESLKDLKYEVRVPENIANKARKAIERMLEVS | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from iminoaspartate: step 1/1.
Function: Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate.
EC: 2.5.1.72
Subcellular Location: Cytoplasm
Catalytic Activity: dih... |
A0A927P4J9 | MIPGSNLHTHTNFSDGVNTPEEMVLSAIKKGFHTLGFSEHGYAKHDRFSMKPETEPVYRDEIRRLKEKYRDQINILLGYEHDHFSPLNVSEYDYFIESVHAIPCGNEMVIVDESRDYLLNAMKEYFSGDPYAMCREYFRTVSKSCVNNSALIIGHIELIMKFNENRDIFNDEDPVYLKYAYEMLDTVVKSGMLVEINTGAISRGYRKEPYPGRSILRKLREMGGRIIITSDCHNADWLDCGFEQSVEIAKSCGYKTAWMMKGSELTEYEL | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 8/9.
EC: 3.1.3.15
Catalytic Activity: H2O + L-histidinol phosphate = L-histidinol + phosphate
Sequence Length: 270
Sequence Mass (Da): 31228
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A0A943G9T3 | MNLASLKEIRPILEKNGFNFSKGLGQNFLINESIPKKIAQLCPSSKSSLAIEIGTGVGCLTKELAFRNKKVVAVELDKRLLPVLSETLAEFDNIRIINDDILKVDLKAVIEEEGFKDVFVCGNLPYYITTPIVMKIFESRLPLKSVVIMVQKEVAERFLAPPGTKNYGAITAAISYYAKVAGSFSVSAGNFFPKPNVDSAVVRFDLISPPVSVKDETLFFRVLRAAFLMRRKTLANNLQTAFSLPKNDVVSMLVSLGYSSSVRGEELGISDFARISDVIASFLKP | Function: Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits.
Catalytic Activity: adenosine(1518)/adenosine(1519) in 16S rRNA + 4 S-adenosyl-L-methionine = 4 H(+) +... |
A0A927RYQ0 | MKPIIGILGPTAVGKSKLAIELAQELKTEIISADSMQIYKKFDIGTAKASSQERSQVKHHLIDVVEPDANFSSYLFKKQTQLVLEDFEKRNITPIIVGGTGFFFKNLLYQFDFEEGNNLEEIRAELQAKQKEFGNEYLHNLLKEVDPVSAEIIHINDGKKITRALEIFYTTGQKKSEGKNEQKPLYPYILFVLNRDRQKLYNDINKRVDVMIEQGLLDEVEQLYKSLPEDCQSLKGIGYKELIPYFKGECSLEQSIELIKQHSRNYAKRQITFYKKMDVIWLDAELSSKQLISAIKTEYFKKFNEIL | 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... |
A0A1H0M0B5 | MLGAVAALAALALVGVVIAVTFANRIDGQSMSPTLGDGDRILLEPFFDPADLRRFDIVAARPSPGSPAVVKRVIGLPGDAVKIEVRADGGASVMVRPAGAAGWSVVDAPVWTENWHDARQCCAADGKSGNGEAVVPAGHVFVLGDNPSQSDDSRKYGWIPISEVIGRMAWRLYPLDRLGSLDPGADMRLVREP | 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): 20323
Location Topology: Single-pass type II membrane protein
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A0A1I3K2T5 | MKIYTWNDILAILNGDSNENFPKTGISTGCFDGLHKGHRKLLSALIDACRAKGLSAGVVTFARPLPGIKHSNDYKGDLTTLNQRLNLFEQLGIDFAIIVDFDDSFASMMGADYLNILLNVCNMELLAEGIDFRCGFKGATDAQAIRYWAEKNNVETIFVDPVYFKEGTDEEERISSSYIRTMLSRGFFTTACELLERPYEIDIAALRRDPQSAQLLPPDGLYRTENEKGELVRLKIENGRIKELPVCERVRFI | 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: 253
Sequence Mass (Da): 28547
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A0A3B9I320 | MYEAHRPAWVEVNTDYMAHNIREVKRVIRPETRICAVIKADGYKLGVIKAAEIYLANGADMLSVAILDEALELRKRFKKIDILVLGYTPVELFGQAIENDIILTIYDVNHGILLSKEAEKLGKTAQVHLKLETGMNRLGFLPEKKSVKEIASLYQLTNLKIEGIFSHLARADETDKNWAYKQKVIFDNFYKQLSDIGVTIPIRHLSNSAAIIDLPDFNYEMVRPGIMLTGLYPSNEVSKSNVRLKLAFKLKANLAFVKTIKKGDGVRYGHQFVAEREMIVGTIPIGYADGFTRMLTGKMTVFVKGITCRILGRICMDQCV... | Pathway: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1.
Function: Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids.
EC: 5.1.1.1
Catalytic Activity: L-alanine = D-alanine
Sequence Length: 388
Sequence Mass (Da): 43607
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A0A3D5R8G1 | KAENPKEVGADRIVDAVAAYEIYGGPVIVIDFGTATTYDVVNENGEFIAAITSPGIQISADALWSKAAQLPNIEIQKPKSILARNTITSMQAGLVYGYIGQVEYIVKEIKKELKMDYIKVVATGGLANIIFGETKYIDDYDLLLTMRGLKIIHAKNIDQIKKDK | Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5.
EC: 2.7.1.33
Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+)
Sequence Length: 164
Sequence Mass (Da): 17994
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A0A2N6AKG4 | EKFWPADVHLVGKEIVRFHTIIWPAMLMSLEQPVPKMVFGHGWLLFDGGKMSKSKGNVVDPVVLIERYGVDALKYFLLREYSFGHDGNFNNEVLLNRLNSDLANDLGNLVSRTVAMVLKYNGGVLELPKVKTEFDDSLSEMAVSTGPAVEERMDRLDFSNALESIWKVVRRTNKYIDETMPWVLAKDEEQKDKLNSVLYNLAESIRIISVMIKPFMPHTAAKIWDQLGIAEGESTSWESAGTFGMMEEGTKVKKAAPLFPRIDVEKELEELSAGTAEEVEESPIEPYKPEITLDDFEKLDLRVAEIVKAEKHPKADKLLV... | Catalytic Activity: ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-methionyl-tRNA(Met)
EC: 6.1.1.10
Subcellular Location: Cytoplasm
Sequence Length: 393
Sequence Mass (Da): 43931
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A0A0Q9K1T1 | MNPYPSLKSVTIDCSYSSEVLISGIQFHSGKVGKGELFVAIPGIEVDGHDYIHHAIEAGAVAVVGEKELYHLPVPYYRVSNSRLALAQIASQYYDYPSRRHTMIGITGTNGKTTTAHLLRHIIETAGITCSLIGTVSNLINGVDISSSQTTPDALQLQKWLYESNDQTVIMEVSSHGIDQDRIGGTEYDYAVFTNLSHDHLDYHDSLEDYYLTKARLFNQSKINGAAIITSRGRWGNRLIDQLLTQNKTVYSFGEVGGDKIEIVQIHSESPLYFQIREENRLYDVKMSLPGVYNAWNAAAAWLTAHRMGIESNIIQHALN... | PTM: Carboxylation is probably crucial for Mg(2+) binding and, consequently, for the gamma-phosphate positioning of ATP.
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Catalyzes the addition of an amino acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosyn... |
A0A927RIL2 | DCIVLDVKTGSGSFMKTPEKSRELAEWMVQIGKRAGKRMRALITDMDRPLGYAIGNSLEVIEAIETLNGNGPKDLTELCIALAAHILNLAEKGSYAECEKLAKDAIASGTALKTFADMVDAQGGDKEWILHPEKFPKAKYEYVVTAKKEGYITGVDTESYGVASLLLGAGRNTKEDVIDPAAGIYLCAKTGDFVKVGDKIAVLYSEKESGFAAAEERLLNATRIETNPPKAEPLILDIVE | Function: Catalyzes phosphorolysis of the pyrimidine nucleosides uridine, thymidine and 2'-deoxyuridine with the formation of the corresponding pyrimidine base and ribose-1-phosphate.
EC: 2.4.2.2
Catalytic Activity: 2'-deoxyuridine + phosphate = 2-deoxy-alpha-D-ribose 1-phosphate + uracil
Sequence Length: 240
Sequence ... |
A0A927SMK7 | MHDIRITPADSLQAAIDALPADGSPARILLAPGLYREKVELRRPHTTLQGSGIGETILAWDDGATDIHPDGVRRGTFRSYTLLVLADGCSVRGLTIRNDGGQRADSGQCIALFVDGDGFVCEDCQLISTQDTLFTAPLPPKEVIPGGFLGPTQLLPRKAQRQTYLRCVIKGDVDFIFGGAACWFEDCEIVCILRADRAPGGYCTAASTPEGQKYGYVFHNCRFTGENVPEASFFLGRPWREHAKTVLLNCHIGSHIRPEGWDDWGKERFPRTGFYAEYGCSGPGSDTSARAAFARTLTEEEAADITYEDFLNSL | Pathway: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 1/5.
EC: 3.1.1.11
Catalytic Activity: [(1->4)-alpha-D-galacturonosyl methyl ester](n) + n H2O = [(1->4)-alpha-D-galacturonosyl](n) + n H(+) + n methanol
Sequence Length: 314
Sequence Mass (Da): 34356
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A0A6A6NMH2 | MGVGGGAERHREGHEKLESEASSPREEDEEGRRGAGGEGDATADRDEEDDLDRDVALKKVREREREKVKRQMQLGKNYEYFTGNTVFCWGGRLQNARDRPINIATGILVLAPAGLFFGFSAPWLWRNISPAIPIVFAYIFCVCMSSYFHASVTDPGILPRNLHPFPPPNPREDPLTPGPATTEWTMVISATSPSAAMEVPTKYCKSCNIWRPPRAHHCRVCDNCIETQDHHCVWLNNCVGRRNYRFFFAFVAAATILGLMLFGCSLAQLLVWQRQRRQPGGGGPGFGDALDANRVPFALMIFAVLGTPYPASLLAYHLFL... | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 338
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 37801
Location Topology: Multi-pass membrane protein
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A0A3D4MWF1 | MEKSEVQRKVQLATSEEVFRKTGRIFVPVASSARHVHLCHADVERLFGPGHQLTVFRMLSQPGQYACTEQVTIVGPKGQLAKVRVLGPERSATQVEIAMTDSFKLGIKAPVRMSGKTAGTPGCRLVGPAGEIELSEGVIIAARHLHLSEAQCALFGLRDGQPVRLRAEGERAVVFENVIVRSGKGHDMEVHIDTDEANAIAMRGTPMMEVLP | Pathway: Polyol metabolism; 1,2-propanediol degradation.
Function: Involved in 1,2-propanediol (1,2-PD) degradation by catalyzing the conversion of propanoyl-CoA to propanoyl-phosphate.
EC: 2.3.1.222
Catalytic Activity: phosphate + propanoyl-CoA = CoA + propanoyl phosphate
Sequence Length: 212
Sequence Mass (Da): 23027... |
A0A970XJJ6 | MDFSEKWFQDLKEKIDIVNIIQEFVPLQKKGTKFWACCPFHNENTPSFTVNQENKYYHCFGCGKTGDAIKFLQEYQKMSFNEAVEWIAKKIGFKIPVGPESNEAKKRRELKNKILEVNKLTAEYYFSNFQKPEARVALEYLRKRELSDETIVRFGMGCSLDDFGMVKFLKGKGYSEQTIKDAGLLNSNGNDIFARRIIIPIIDKQGDVLGFGGRAIFENDKPKYKNTPQSVLFDKSSILFGINLISKYRKDRVDINALILVEGYMDVISLNQAGIVNVIASMGTSLTIQQCEKIKTIVNNVYVCFDGDAAGQNATWRSLD... | 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: 590
Domain: Contains an N-termi... |
A0A7Y3KJG0 | MDNHHEITFERQERLAFRLPPKVELIKWLVSVIRSEKKQCGKISFFFCTDKYLLELNKKFLHHDYYTDILTFDYSAGKTINGEIFISIERVKENAIAYSQSFRQELLRTIVHGVLHLCGNNDKTAAEKNRMRKKEDTALNLFLKHSWN | 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: 148
Sequence Mass (Da): 17565
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A0A356GGU5 | MPFTKMHGAGNDYIFIDCMSDKTKIKNPAELARQMSPPHFGIGADGIVLILPSSEADARMRMFNADGSEGKMCGNALRCIGRFLYERGYTRKTSLVIETASGIRRLWIKLKGGRFVSALADMGRASFLAADVPVLAAPDREGYITIGGLLGGSCRATCISMGNPHAVFFTDDPEKTDLAGIGAALANHPLFPEGVNAEFARVAGGEIYMRVWERGTGETLACGTGACASAAAAVHHCLLPYDTPIKIHMRGGDFEATVKKNFRVLLSGTAETVFDGTFYDTEDKL | 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... |
E0NNI2 | MLLPIKWLKDYVNINKKPIEIANKLSSTGSHVESINNFAEDIEKVVVGKIVEITKHPDADKLVVCKIDVGNETLQIVTGAPNVFEGAVVPVALDGSTLANDVHIKKGELRGVESNGMLCSLEELGYAQSVIPKEARDGIYIFSSDTKIGSDVKDILDLNDEVLDIEITPNRPDCLSIIGMSRETAATFDLPLIEPKIEFKNETENIIDFIGETVVETKKCSRFYTKVLTDVKIEDSPQWIKNYLMLAGVRPVNNIVDLTNFVMLEYGQPLHAYDLDKLDGNIIVRDAKDGEIIKTLDEEERALTAEDIVITDRSRVLGVA... | Cofactor: Binds 2 magnesium ions per tetramer.
Catalytic Activity: ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + H(+) + L-phenylalanyl-tRNA(Phe)
EC: 6.1.1.20
Subcellular Location: Cytoplasm
Sequence Length: 794
Sequence Mass (Da): 89115
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A0A2N6AUN5 | MRLGELIKENDYVSCFGGKGLNSIVKNISCDSRTAAPGDCFVCIKGFETDGHDYIPQAYKNGSRVFVVEDLSWTSKIATEYPDAAVLLVDDTRSMLSTLSDRFFGSPSKKITVVGVTGTNGKTSVTNYIFNALRKLGLSTGMIGTIEIRMNDEIWPSSRTTPESLELHKIFKTMLDKGIDYVVMEVSSHALTLLRVQDIEFDISVFTNLTQDHLDFHKTMGNYADAKYMLMKKSNKASIVNIDDNYGNEYMNALKKEGKRVLTYGMQNKADIISERNEAHGITTIKSSCGEIEIESSSRFETYNKMAAYAVLKELGFDID... | PTM: Carboxylation is probably crucial for Mg(2+) binding and, consequently, for the gamma-phosphate positioning of ATP.
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in... |
A0A9D5RA69 | MVNRLNREMLLGCEPKEKLSFIDVLLIVVMVLLIVNIFVQSVWLSPVKVDGTSMNNTLEHEDWLFMDKIKQPKRGDVVVFKISETVNYIKRIIALPGDSVRTVKGKVQIKIGKDGEWKEINEPYAYFEPEKVEGTYLLKKIEGVVRIVDIPETEIKEGEMFVLGDNRWGSRDSREIGVVKTENILGIVPRWAIDKKEKYGPYLDYIEQVNKKIRERFGENN | 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: 221
Sequence Mass (Da): 25599
Location Topology: Single-pass type II membrane protein
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A0A2V2E2M5 | MSRTEQIRLVVSGVVQGVGMRPFLHRLANRLSLTGWVRNTAFGVELELEGAPEALRAFEETLRVSPPPLAVVEKITREPLKDPLGVSSFSILPSESGSGATLISPDLAPCSACLAELADPTDRRYRYPFLNCTDCGPRFSILRDIPYDRANTSMASFSMCADCAEEYGDLRSRRYHAQPDCCPVCGPRAYFCTEDGRELPGDPIALAQQALARGEIVAVKGSGGIHLACDARNHTAVVRLRKRKGREAKPLAVMCRHTDAARMFCTVSTEEAALLESPRRPIVLLEKRCPDAFSELSENTRLGVLLPYTPLHTLLLDGSF... | Pathway: Protein modification; [NiFe] hydrogenase maturation.
EC: 6.2.-.-
Catalytic Activity: ATP + C-terminal L-cysteinyl-[HypE protein] + carbamoyl phosphate + H2O = AMP + C-terminal S-carboxamide-L-cysteinyl-[HypE protein] + diphosphate + H(+) + phosphate
Sequence Length: 765
Sequence Mass (Da): 83178
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A0A2V2G5V9 | MRMRKKKNAAKRLDACADIFIADPASQKGAWKKLSGGRDIYIEIGCGKGTFVFENAKRHPELFFVAFEKVKDVIVMAMEKVHAAALSNVLFVCDDAENITDFFEENEVNGIYLNFSDPWPKKKHAKRRLTYITFLEKYKNILVDGGKIFFKTDNRQLFDFSLEQFALAGLEISDVTYDLHNSEYESENIHTEYENNFSAKGFTINRAVATANKKNNFADTGHDIENNKTKSDEISDRSENNV | 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: 242
S... |
A0A2V2E0R7 | MKKFLTTVKDGTRDYMFGECAKIREISTNLCSFVKSRGYAEIMTPTFEYADIFNISNEDLFKFTDGRNRLMALRADCTTPIARVAATKLCDNPAPYRLFYCQSVFNASRKKLEQSDFGVELIGADGIRADVEVLTLASGALQKYFGVGCRIEIGHSKIYKLLCKEYSIDEDTAEKIRLLIEAKNFAAIESLDIPAAIKALPKMFGGIEVLAEFKSLANNEKITEILSYLESLYKILSSLGFSVSFDLGLVRRLDYYTGIVFEGYVDSHGVSILAGGRYDNLISEYGRDLKAIGFSACVDEIFDALDGDLRKITTPDVMIY... | 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... |
A0A970JIW3 | MIFLSPSILAANFTMLGEQVAAAQKGGADFIHIDVMDGHFVPNISIGFPVIESLVKHFSIPLDVHLMISNPEKYATRFCEAGADYLTFHLETMKNPAPLINEIRSRGVHPSLSLRPATPIEAVFPYLDIIDMVLIMTVEPGYGGQSLIPYTLDKVRALRAEADRRGLHDFKIEIDGGVRLENIAVTTEAGANVIVMGTAVFSEHDIPAALDKLRKEAQRGAELRNKA | Cofactor: Binds 1 divalent metal cation per subunit.
Pathway: Carbohydrate degradation.
Function: Catalyzes the reversible epimerization of D-ribulose 5-phosphate to D-xylulose 5-phosphate.
EC: 5.1.3.1
Catalytic Activity: D-ribulose 5-phosphate = D-xylulose 5-phosphate
Sequence Length: 227
Sequence Mass (Da): 24875
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A0A0S8JQB1 | MSHNSFKIWMAQIRAPFLILAVFLVVIGLAFSVKYPQDPGAAFNWLHAVMLVIGVVLSHVSVNLFNEYSDFKTRIDFNTNRTPFSGGSGMMQAGNTRPENVKTVGIITLLVAGAIGIYFAFIAHWMVFVFSIIGAFSVLFYTNFFAKYVLGELFAGLALGTLVVLGTYVAMTGMPGMPVDGLFPREVIWISIPPGILTSLLLLINQFPDHEADKEGGRRHLVIRFGLKGASYIYTAGMFATFGIIVLVPIIGISSFWIYIALLPLPLGVKAAMTAIRHGDDLGKMIPALGSNVMTVLLTDLLLAVSVFIDVL | Pathway: Quinol/quinone metabolism; menaquinone biosynthesis.
Subcellular Location: Membrane
Sequence Length: 312
Sequence Mass (Da): 33968
Location Topology: Multi-pass membrane protein
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A0A5Q2FJM7 | MSHFLDGPDEPGPRRAQRAKERRGSRRAGVILALVTVIVLVALVGGGWYAAGVLGLRAPDYSTSTTAGPPVAVKIPSGATLKEMGQILADKDVVKSEAAFVKAAKANSKASGIQSGDYRLSTHLPASQAVDAMLDPKNRAAKQITLREGLSLAKQLDSIAEQSALPRQQFADLAKDPASVGAPAYAKTLEGYLFPDTYQLGDTTTAKQILVAMVDEYKQAAGQVGLEQAATALHHTPAEVVAVASVVEAEARTPADRPKVARVIYNRLDRGMPLQMDSTVKYLTGLDGKVTTTDKERAQDSPYNTYLHPGLPPTPIDAPG... | 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: 377
Sequence Mass (Da): 40166
Location Topology: Single-pass membrane protein
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A0A2G6GMJ2 | MLPIEEKKCIKIGEIIKPHGYKGEVFIRLNQEIISAKETEYVFLKMEGYMIPFFFASPVKPFKDGFLIHFEEINTPEEARALSNIEVYLEAEKTETDNGDSGMFMEENTEGFDVFDGDKYIGTAGDFLPVPSNPLLVVFGLKNEEILIPYSDRFIRTIDHRERKIIFELPEGLVELND | 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 ... |
A0A8T4WYA6 | MPGYFSKNTDGLKIDGVPAEEIAEEYGTPVYVYSEDRIRDNYRRLRDALKERYEKVRILFSAKSNTNLSILNILKDEGANIDTVSVGEIFLAKKAGFDPDEILFTGMNLGDDEIDHLLGSDVKINVNSLSMLDRLLEKEVPSSISFRVNLQKGAGAHRHLITAGKNSKFGILEDDIIKAYRKALDSGVKNFGIHTHIGSGILDTDHHRRATEKLMDIAGKVKEKLGIGFEFIDIGGGIGIPYEPGEEEMDLEKFSRDVLTAFKEKSAEHGLGDPYFCMEPGRYIIGDAGIILTEVNTVKKTVSRKLAGIDAGLHTFIRPA... | Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; L-lysine from DL-2,6-diaminopimelate: step 1/1.
Function: Specifically catalyzes the decarboxylation of meso-diaminopimelate (meso-DAP) to L-lysine.
EC: 4.1.1.20
Catalytic Activity: H(+) + meso-2,6-diaminoheptanedioate = CO2 + L-lysine
Sequence Le... |
A0A353T3R2 | PDATYQRVRFEGTVYYIEKHLAPRVLGGEYEVLDERKGKDLEYMEYEQLMPFVSTDKKAFYVTVADYVTTEDGTGIVHTAPAFGEDDYQTGRRYGLPVLQPVDDSGKYTCTPWKGMFVMDADREVIQWLAENGKLFRKQKMVHNYPHCWRCHTPLLYYAKPSWYIEMTKLRDQLIKNNNGVDWYPAFVGKKRFGNWLENLNDWAISRSRYWGTPLNIWRCECGNTTSVGSRRELAERAVEDIDESIDLHRPYVDDVHLVCDKCGKAMTRVKDVIDCWFDSGSMPFAQQHYPFEHKEDFNQLFPADFICEGIDQTRGWFYS... | 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 ... |
A0A7Y3HN16 | MSNIQPDSNFTLLKSVKDLTETEQLLITKAKEAAMNAYAPYSEFYVGAALELRSGEILVGNNQENAAYPSGLCAERVLLFSTGANYPSKQIKTLAVLAYKNDKVVAATPCGACRQVMVEYEQKQENPIKIIMYKGEDDIIVSNDAKGLLPFAFDSKSLLNK | Function: This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis.
EC: 3.5.4.5
Catalytic Activity: 2'-deoxycytidine + H(+) + H2O = 2'-deoxyuridine + NH4(+)
Sequence Length: 161
Sequence Mass (Da): 17678
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A0A521AJP7 | MIQLIQTLGTLSRIWFTLVWIMFSTAMALAQDAPIETPETSEQSENFKAPVIIDGESLFFLRGSSALPAPERAETVQNNIIQVALSSENPEVTVTYEDTELGTRILVDGVPVSTVTVADAEMDQMELDVITYLHGSAIHDAIVAYRANRTEQARVSGALEALGWTLGFAVFIAIILWLHRRIRRRTLKFVSRHLKDVETATAKSVQAEAIAALVSYGLNFILLVVFFLGFYYYLSFVLLSFAETRYFAQLLLTYLTEPVLLIFKGVVSYIPNLIMLALIAWLAMYIIKGMRVFFDAVEAGTFELGDFESHWVNPTFNIAR... | Function: Mechanosensitive channel that participates in the regulation of osmotic pressure changes within the cell, opening in response to stretch forces in the membrane lipid bilayer, without the need for other proteins. Contributes to normal resistance to hypoosmotic shock. Forms an ion channel of 1.0 nanosiemens con... |
A0A355V0T7 | MLIGNKNFENYTYVMAIVNLTPDSFFAGSRNTADTVLRTVERAVKDGAAVIDLGPQSTRPGHTPVSAEEEISRLEKPLYLVKKNFGIPVSVDTYFSKTAKAALSMGADMINDVWGLTHDEDMASVIAGCGAAACIMHNAKTPLTGDIWQPVKDFLKNSVNTALAAGIAQNKIILDGGIGFAKNREQNFELVNGYERLSFDGYPLLLGTSRKSMFGGDVEGRLAPTLETTRIAARKKILFVRVHDVKENVQAVKEVYGE | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2.
EC: 2.5.1.15
Catalytic Activity: (7,8-dihydropterin-6-yl)methyl diphosphate + 4-aminobenzoate = 7,8-dihydropteroate + diphosphate
Sequen... |
A0A1W9NY67 | MINNPKQPQLKIIPLGGSSMVNKNMFVYECGKDIVIVDCGIGFPESEQLGVDVVIPDINYLKNKLDKIRGIVITHGHEDHFGALPYLLKDLGNPPIFASKLVRGLIQVKLEEFNLLKGAQINQIDPEDNSFSLGQFEFTPFRVNHSVPDSLGFFIRTPLGNLVHVSDFKFDWTPVDGKFFDVAKLVKLTSQAPVRCLLSDCLGATSRGYTKSERFIQHSFEHELDRAPGQIFISTVSSNISRIQQAINAALKYGRKVAFLGLSIERNAEVAQNLGYLKIPPGTIVNSRTVHKYADNQLLIIIAGSYGQENSALSRLAEGS... | Function: An RNase that has 5'-3' exonuclease and possibly endonuclease activity. Involved in maturation of rRNA and in some organisms also mRNA maturation and/or decay.
EC: 3.1.-.-
Subcellular Location: Cytoplasm
Sequence Length: 556
Sequence Mass (Da): 61663
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A0A9D1RI31 | MYDLIVVGAGPGGYTAAIRAAELGLKVGVVSENIGGTCVNYGCIPTTAYLEASRLAAKIKNAADLGITAKVENIDLKVLKEHKDQITTQLQMGVRSLFKGHKIDLIEGTATVENPQTVVVNDKKIQTKKLLLATGSRPKVVPFKGLDKVDYLTTEDVFSLTELPHRLTIIGGDIFAIDMAFVLAPLGVDVTIVDAAPEILATEDDDARNVIKSELKRMKVAIHSGVKISEIKANQVLSEQGEHFDFDQLLVVTGRQVDLSIATTLGLDLDDWKRHVKVDRHYQTSVKNVYAIGDLIGGYMLAGEAMAEAMKAAGAIADHP... | Cofactor: Binds 1 FAD per subunit.
EC: 1.8.1.4
Catalytic Activity: (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + NAD(+) = (R)-N(6)-lipoyl-L-lysyl-[protein] + H(+) + NADH
Sequence Length: 447
Sequence Mass (Da): 48017
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A0A455U9R6 | MSQTCGFVAIVGRPNVGKSTLMNRILGQKISITSRRPQTTRHQVMGIKTEDETQFIYVDTPGMHIMSKDRNKAINRFMNQAATQALRDVDCVVFIIDRTRWTEEDQAVLKRLEHVKAPVILAVNKVDRLGEKGDLLPWLAEVGARRDFAAIVPISAKHGTQVDTLEEEVAKHLPESVHFFPEDQITDKSLRFMAAELVREKVMRQLGDELPYQMTVEIEEFRETERVTHISALIPCRATGAESYFDW | 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: 247
Sequence Mass (Da): 28163
Location To... |
A0A1W2BER8 | MQFLDVISVNIWAILASLANLLVLTWIIKRFLFKPVKKMLDARRQTIDDYYAQAQAARDEAEENRLNYEAAMAAAKQTGDQIIADASRTAEYRHNEIVAEAREKASEIRRQAEADALLERKKAEDEMKHEIANVSAQLTGKLLQREINEEDHRNLIDSFLNDLD | Function: Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).
Subcellular Location: Cell membrane
Sequence Length: 164
Sequence Mass (Da): 18828
Location Topology: Single-pass membrane protein
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A0A455UDU0 | MTELLIFVGGLLVLMAIGMPVVVAIGVTSFIALVATGTGGLPVELLPLRMVQTLNNFTLLAIPLFILAANIMNIGSTTTRIFDFATALVGFTKGGLGHANVVASSIFATMSGTAVADAAGLGSIEIKAMKERGYELGYSTGITAASSVIGPILPPSIALVVYGWLANVSIGGLFMAGLLPGILMALLLMGMTVLLSASGRVVMPKPTPFDACEVVRTGKRAILPLMMPAIIVGGIWGGFLPRRKPAPLHRFTR | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 253
Sequence Mass (Da): 26220
Location Topology: Multi-pass membrane protein
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A0A972IVN8 | SPIVLFQIWGFIKPGLKVKEKKYVVLALSMGTIFLLMGVIFAYYIIVPMTIKFFTGVTVDKITPSFSFANYISFVSSLLLSFGLVFELPLLIILLTQLGLVAPKTLKKYRKFVILIIFVVSAILTPPDVVSQVLMAIPMTLLYEFSIIVSTIIYRKKKKEKVAQDES | 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.
Subcellular Location: Cell membrane
Sequence Length: 167
Sequence Mass (Da): 18820
Location Topology: Multi-pass membrane protein... |
A0A3C2C4S5 | MAKTGVVAGLDIGNSKVIAFVARAGRPGVITGVGKSASLGMRKGMIYDPQLLASSISRAVEEASNIAGAKIQSVCAGIAGCDVRVITSQSRVSLKKNRQVKKRDIDNLLWHASQVGISDGYQVIQVIPKEFVIDDVLPVKDPVGMICSCLETKIKIVIVNNELIKNLILSLELAGLKVEKVALNLLVAAGEVLGEVEKELGVALVDLGGSTTGVGVFNRGGLVEMAVLPVGGEHITGDLAVGLKTSLTNAELLKRRVGLAGGEEQDREISAMTIQIIRARVEEILALVKEQVFKFTNGSTLPCGLILTGGGALLKEITEM... | Function: Cell division protein that is involved in the assembly of the Z ring. May serve as a membrane anchor for the Z ring.
Subcellular Location: Cell membrane
Sequence Length: 371
Sequence Mass (Da): 38959
Location Topology: Peripheral membrane protein
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A0A352MWC2 | MSISPYITASIVIQLLGMVIPSLERLVKEGGEEGRAKINKYTKILTIVLALIEGLGIFLSYRTSGIFVDTSFLTGFVVLSSLMAGTALLMWLGEQITNKGIGNGISMIIFVGIISGLPSFIPTIWNLMFQAGAFSTTGLLTALGIVIGAIVLITAVVFVQQAERRVPVQYSKKVVGRKMVGAQSTHIPLKLAMAGVMPIIFASSFMTFPAMIIQMFISDIATQTGFWASIYKFSIATSSSNVPIGYSIANALVYLLLIVGFTFFYTYATFNPAEVSNNIKKNGGFIPGIRAGKPTTEYLSKIISRLTWFGRSIFSNYSYT... | 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... |
A0A357D0E5 | MNKTKKYKISFLILLFLAAFTFYVIFTKFSFYDIIDKVRESSHKHYLLFACVLSVVYIALYGRFINVGISALNEKTSRLKCFVYGCADFFYSAITPSASGGQPVVIYLMTKDGISLSTSAITVIFQTIAFKAVLLFYGILSLFVVWNIVSITSVLFLILILVGVATALISITLCIVSMYRPYLTEKVGTAILRFLTKLRIIRNGKERICSFKDTLTEYHKAATFLNNKKRVLLRMFFITLCQRTAMFSIAYFVYRSFGLCSFGYIDFLCVQALVSLAIDSVPLPGSMGANEYATYFLYGVVYGSNDVMAATAMLLTRGFS... | Function: Catalyzes the transfer of a lysyl group from L-lysyl-tRNA(Lys) to membrane-bound phosphatidylglycerol (PG), which produces lysylphosphatidylglycerol (LPG), a major component of the bacterial membrane with a positive net charge. LPG synthesis contributes to bacterial virulence as it is involved in the resistan... |
A0A1W2B525 | MNTMLNLSAAPHARDKWTTPFIMRMVTLSLLPATIVGILVYGWNAFGIVALAIVSAVASEWLFCKVCKKPSTIWDGSAVVTGLLLALSLGPQTPLYIPVIGSVFAIVVCKGCFGGLGKNFINPALAARCFLLISFANAMAIKPVVDAVATATPVGAMKAGEVVDITKMFLGTADGVIGSSILALLAGGLLLWSMDIIHGQICFSVLIGFTVFLGLFGGKGFDPAYLLAHLCGGGVVMGAFFMATDYVTSPVSRLGQFIYGCLIGVLGGLFRLKGNTADSFSYAIIIGNVCSPLIDTYIVQKPFAYRKIGKTRKTSKEPFR... | Function: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane.
EC: 7.-.-.-
Subcellular Location: Cell membrane
Sequence Length: 518
Sequence Mass (Da): 54135
Location Topology: Single-pass membrane protein
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A0A943Q5M5 | MKRKRHTLILELIQQYEITTQDELLAKLRENGFEVTQATVSRDIKELRLVKAMSPSGQYRYMVSTAPGDEYLAKFYTIFSGSVISVDFAGNTCVLKCYSGMAQAACAAIDAMHFDRSS | Pathway: Amino-acid biosynthesis; L-arginine biosynthesis [regulation].
Function: Regulates arginine biosynthesis genes.
Subcellular Location: Cytoplasm
Sequence Length: 118
Sequence Mass (Da): 13241
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A0A357CX62 | MKSIIILGSTGSIGRQTLEVAHNLGLNVSALSGYNNVKVLEEQCRRFKPLICWVSETKYHELKTALADTGTKVITGNDALDNLSYETEADLLLNSIMGMRGLKPTLAAIDSGKQIALANKETLVAGGEIVMQKVAEKGTTILPVDSEHSAIFQCLQGGVKPKKLLLTASGGPFFGKKRFELNKITPEEALKHPNWSMGKKITIDSSTLMNKGLELIEAVHLFSVAPENIEVIIHRESVIHSMVEYADGAVIAQLAKPDMRLCIQYALTYPNRLQSPVQGIDFLKIGSLTFAEPD | Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 1/6.
EC: 1.1.1.267
Catalytic Activity: 2-C-methyl-D-erythritol 4-phosphate + NADP(+) = 1-deoxy-D-xylulose 5-phosphate + H(+) + NADPH
Sequence Length: 294
Sequence Mas... |
A0A970LUL3 | MEKVLVAISGGVDSSTCLILLKNRGYSPYAVTMKLIGENTNLTGVDTSSPVRDAMKAAEIIGVPFEAVDFTGDFEDRVISPFAESYAAGLTPNPCLLCNKYLKFGKLFEKADSLGIKYVATGHYARVEEKDGKYYLRKAADIKKDQSYVLCNLTRKHLERLMFPLGDLTKDEVRRIAKENSLNTAEKAESQDICFIKEGNYASFVTEYLNLPPNSGRFLDREGKVIGTHDGMIHYTVGQRRGLGMGFGERLYVLSKNPIDNTITLGYDGDLFADELILRDVNIISGEFPSSPFRAAVKIRYHHKEQPATVTPLGEGRLKV... | Function: Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34.
Catalytic Activity: AH2 + ATP + S-sulfanyl-L-cysteinyl-[protein] + uridine(34) in tRNA = 2-thiouridine(34) in tRNA + A + AMP + diphosphate + H(+) + L-cysteinyl-[protein]
EC: 2.8.1.13
Subcellular Lo... |
A0A8T4WWZ1 | MEENIKLIREFISDKVEKTGADGVTLGLSGGLDSTTVLKLSIDALGEERVHGIIMPESASPEEDMKDARWIAEKWDIEYDEIDIDPIMESFPAGPEEKLPYANLKARTRACIEYYIANVEHKLVVGTGNKSELLLGYTTKYGDSAADFLPIGDIYKSDLRDLAEKIGVPERFLDKVPRAGLWEGQTDEEELGHTYEEIDEVLKGIEKQEPLKKIAEKNGVSKETVEDVKEMIDKTAHKRKFPTVLKLRSRTVGNDWREFSR | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from deamido-NAD(+) (ammonia route): step 1/1.
Function: Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source.
EC: 6.3.1.5
Catalytic Activity: ATP + deamido-NAD(+) + NH4(+) = AMP + diphosphate + H(+) + NAD(+)
Sequ... |
A0A971BW44 | MLIFILVAITIIVVLNTTVFPSLFSDKKQKVEVTYSEFLDHIGSGDINEVQVEDDYIYYLLTGDEDTVYSTVRMSDEALVDRLIDSGARFRQVAPAKTPWYLSVIISYVIPIAFFVLVWKFFLSKIISKGVGGNYMDLGRSNARIFAKNELSCKFSDVAGEEEAKESLMEVVDFLHNPAKYEEIGAKLPKGALLVGPPGTGKTMLAQAVAGEAGVPFFSISGSEFVELFVGMGALKVRDLFKQANEKAPCIVFIDEIDAIGKKRDTHGFAGNDEREQTLNQLLSEMDGFDSRKGVVLLAATNRPDSLDPALLRPGRFDRR... | Cofactor: Binds 1 zinc ion per subunit.
Function: Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.
EC: 3.4.24.-
Subcellular Location: Cell membrane
Sequence Length: 618
Sequence Mass (Da): 67746
Locat... |
A0A0T6A7G2 | MWLIVGLGNPGPEYARSRHNVGFVVLDELARRWNRPMTRRRWESLYAEETRRDEPIALIKPLSFMNESGRPVKAWLEGTSVPPERLVVIHDDLDLAFGRIKVVAKGGHGGHRGVRFIQQAIETMGFPRVRVGIGRPEVGDEVTFVLHPFDEAEACLLPDLISRAADAVEEIVERGVASAMNRFNVWKQSGACGEPAETTGEEVDGCQSTR | 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: 210
Sequence Mass (Da): 23413
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A0A9E6DLV8 | MPVSDQLIDMRDPRIALGLLTRLPFGADLRVAADRGPHSAWAFPFVGLIIGALSAGIGALAFLVGLGAGPVAVLVVLTQVMMTGAMHEDGLADSADGLWGGWDPARRLEIMKDSSIGAYGVIALLLVQTLRIMALSALATSGFWSLMAGIVAAACISRTSMVGVMTLLAPARQDGLSASVGQPSPLTLVLAIVIAGLTAVGLIGLYTIPATIAAVVCAFVAMSLAKARIGGQTGDILGGTQQITEISVLLILTIRP | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7.
Function: Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-riba... |
A0A358TY06 | LTVGGGIRSVENVRDVLRAGADKVAINTAAIKRPELIREISKRFGSQCMVLSIEAKKVSEGKWEAYYDNGREKTGIDVIEWAKRGYKLGAGEILLTSVDMEGTAKGFDVDLVRAMSNTVSIPVIASGGMGNIQDLINVINDGCADAVAMAHVLHYKKFTVQEVREKAVSCNVNVRRLKLWSR | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 5/9.
Function: IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ... |
A0A927ZGN5 | MVKGVHNYSEIGKLNKVLLHRIGCEVDGLVPDNFARLLFDDIPYLKVAQQEHDRFAEILRRNGVEVVYYVDEAAKALEKPEIKDRFIREMLNEVNFSSRGVKEAIYAHLIGMAPYDLVNKVIAGVRKKDITDYKPRTLAEKIDEAYPFYMDPMPNMYFTRDQAACVGNGVTIHHMSTATRRRESLLFQYIYEFNGDFAPAGTEKWFDYNDPYSLEGGDILVLSKDIVAVGLSERTSAAGIETFTKNLLADSEFKKVLVFNIPKKRAFMHLDTVFTMVDYDKFSIHPEIEGPLQLFELSLKADGEIKLNSMTESLKTILAK... | Pathway: Amino-acid degradation; L-arginine degradation via ADI pathway; carbamoyl phosphate from L-arginine: step 1/2.
Catalytic Activity: H2O + L-arginine = L-citrulline + NH4(+)
EC: 3.5.3.6
Subcellular Location: Cytoplasm
Sequence Length: 406
Sequence Mass (Da): 45851
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A0A953GNP0 | MKAQSGRITLEGMRFHAYHGVYPEEQTQGNTFLVDVSFNVSIEKPGISDNLDDTIDYSAVYKIIAEQMAVPSQLLEHLMRRMQLAITGHFPQMADLEICIRKINPPMGGEIYAVSLRTNNSL | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 3/4.
Function: Catalyzes the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin.
EC: 4.1.2.25
Catalytic Activity: 7,8-dihydr... |
A0A3D5R6D4 | MIVDKLYENVEEKGHVCLGLDTDYDYIPKYFAEDFKSKGEAIYNFNKEIIDSTKDSVACFKVQIAYYEALGLEGLKAYKKTLDYIKKNNTMVISDIKRGDIFKTAEMYAKGHFEGDFESDYLTLNSYMGLNDSIEPFLPYVEKNDKGVFVLIRTSNKGANDFQYIKNAKGRPVYEIVGEKLNQLAGKY | 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: 188
Sequence Mass (Da): 21572
|
A0A355V2C8 | MENKKFYLTTAITYTSGKPHIGNTYESIFADAIARFKRMQGYDVFFMTGTDEHGLKVEQKAEAKGLTPKQFVDGVAGEIKGLWDKMNVSYDRFIRTTDEDHVKTVKRIFEKFYKQGDIYKSSYEGMYCTPCESFWTESQLVNGKCPDCGREVKPAKEEAYFFKMGKYATRLVKHILTHPKFIQPASRKNEMFNNFLLADEFIGKSDEELLKACEDNALKTKLQDLCVSRSTFKWGINVDFDPRHVVYVWLDALTNYISGIGYDPETPSEKYKKYWPADVHILGKDIARFHTIYWPIFLMALGEPLPEEIFAHAWLMQGGD... | Cofactor: Binds 1 zinc ion per subunit.
Function: Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation.
EC: 6.1.1.10
Catalytic Activity: ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-methionyl-tRNA(Met)
Subcellu... |
A0A352MWL0 | MLGILLKEEIEGFEFASGIPGTIGGAIRMNAGAHGKEFKDIVVETTYIDYNGNLHTINNNEHIFSYRHSRFFEDNGIILSSKIKLKYGNRQIIKAKMQEYLNYRKEKQPFNMPSAGSTFKRGDDFITAKLIDDCGLKGFSIGDAEVSNKHAGFIVNKGKATAEDVLKLVEYVKRVVFEKTSKNILLL | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation.
Catalytic Activity: NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
EC: 1.3.1.98
Subcellular Location: Cytoplasm
Sequence Length: 187
Sequence Mass (Da): 21014
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A0A367IJV0 | TFIANIFGTIVLSILVLLQSGAVSPAISSCEVIQALADGFCGCLTTISTFMVELNTLGIWDGYVYGISSVVVAQCFVFVILGSFIWSQGINL | Function: Fluoride channel required for the rapid expulsion of cytoplasmic fluoride.
Subcellular Location: Membrane
Sequence Length: 92
Sequence Mass (Da): 9728
Location Topology: Multi-pass membrane protein
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A0A971BIP6 | MRISYTRTHKEAVPMKTSNAAERMPRPVAAAELHGSHLAPGIRGLVRFYPAHSGTMVSIVVSGLPELRLSKDPKNRVGPFAFHIHEGDVCGSPRPPEPFRAAGGHYNPKNRPHPLHAGDLPTVYPNRGYANMTVYTDRFRPDEVIGRTAMLHIRPDDYHSQPAGNAGERIACGVIRAV | Cofactor: Binds 1 copper ion per subunit.
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: 178
Sequence Mass (Da): 19555
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A0A972FEB7 | MSVEERIEALRAEINKHNKLYYENDAPVISDFEYDRLLRELEELEEEYPELIVPDSPTQKVGGTAKSSFAPFEHENPLQSLQDVFSYEELSDFLIKLENGFGELNYCVEPKIDGLSISVVYKNGMFAEGATRGDGSVGENVTENLRAIKSLPKRLNTSIDELVVRGEVYLSDENFEALNKKQEEEGLNLFANPRNAAAGTMRQLDPRIVEARNLDFLAFNIQKISGLSFSTHFETINYLKEQGFDTVDSVLASNPDDCIEIVETIDKNRENYSYGIDGAVIKVNSLSQREKIGTTSKYPRWAVAYKYPPEEKETLLLDID... | 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... |
A0A1W2D475 | MKEVVLGLLGLGNIGGGVWDLIREFGGEVGKRTGVKLRVKKALVLDKKIHGGKEVPDEVLTTDKNDILEDPEINIVCEFLGGEQPAASMMLRALENGKSVVTANKMALSLHFDELREMAKKTGAGLYYEASVGGAIPIINAIQTPLIANHIEQIMGIVNGTTNYILTRMAAEGAEYEAVLKDAQRLGLAEPNPTADVEGFDAAYKLSILGSLAFHSRVLVEDVYREGITKVNSEDIAFGREMGYVLKLLAIGKDNGDSIEARVHPAFLPADHPLARVDGSLNAVYLYGHSFKDMMLEGRGAGDAPTASAIVGDIVQAAQN... | Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 3/3.
EC: 1.1.1.3
Catalytic Activity: L-homoserine + NAD(+) = H(+) + L-aspartate 4-semialdehyde + NADH
Sequence Length: 420
Sequence Mass (Da): 45144
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A0A9E2BLT3 | MIEPSGCLYVLATPIGHLGDLTLRALETLREADAIYAEDTRHTGLLLRHYGISRPLISCHQHNEVKRIPEILERLQRGEQVVLATDAGTPGVSDPGLRVVEAVLKAGGRVSPLPGPSAVTAALSVAGFPASPFAFAGFLPRKKGPQKRALQMWKDVGVTLVLFEAAPRLLRLLENAMEVYGREHQGTVARELTKKFEEVRRGTLEDLYRHYEKEEPRGECTVVLGPISKEIGPNTKGASEGAGGQPGQPG | Function: Catalyzes the 2'-O-methylation of the ribose of cytidine 1402 (C1402) in 16S rRNA.
Catalytic Activity: cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = 2'-O-methylcytidine(1402) in 16S rRNA + H(+) + S-adenosyl-L-homocysteine
EC: 2.1.1.198
Subcellular Location: Cytoplasm
Sequence Length: 250
Sequence Mas... |
I7KGI2 | MVLARELQDEPEKGLRCSACFQLRLDLVAEKAVALGYDYFGSALTLSPQKDSQLINEIGLDAQKIYTVKYLPSDFKKNKGYKRSVQMCREYDIYRQCYCGCVFAAKQQGIDLKAVNQNAKAFLKTKQEVNG | Pathway: tRNA modification; tRNA-queuosine biosynthesis.
Function: Catalyzes the conversion of epoxyqueuosine (oQ) to queuosine (Q), which is a hypermodified base found in the wobble positions of tRNA(Asp), tRNA(Asn), tRNA(His) and tRNA(Tyr).
EC: 1.17.99.6
Catalytic Activity: AH2 + epoxyqueuosine(34) in tRNA = A + H2O ... |
A0A349VRG6 | MAGGFGRVIGIGSYLPDRIMTNDDLAKIVDTNDAWITERTGIKERHISDPEKDTSESMAVEAAKRAVADAGIDPMEIGLIIVASTTPNVLFPVLSASVQAAIDADNAMCFDTNAACPGFLTAFVTAQNYLRSGMVKTALVIGTENLSNYMDFTDRGTCILFGDGAGACVITSDENLKYDAIMRAAGKRGECMHCESYMQKGKEKTPEFLKSNYIQMDGQTVFKFAVTEVPKIIEDLLARTGTDPDEIDYYILHQANRRIIESVAKRLKQPIEKFPMNIEKTGNTSSASIPILLDSMKKEGALGEGKKKVVMSSFGAGLLW... | Pathway: Lipid metabolism; fatty acid biosynthesis.
Function: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the tot... |
A0A943J222 | MKVIVTGSFNPITKGHEDLILRAASIFDEVIVAVFNNVDKKYEFSLTEREKLCRAAFVGVRNVRTVSSDGMVVDLCREENCFLLLRGVRDESDLRYEKMMSEANKRFEPRCETLFMTASEKYERLSSTAVRKIISGNGSFIGLIPEKAEKCLVEILEERKGGKYEK | Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 4/5.
Function: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
Catalytic Activity: (R)-4'-phosphopantetheine + ATP + H(+) = 3'-dephospho-CoA + diphosphate
... |
A0A942ZTZ0 | MKLAMAYFYPGHEQKIQLAQQMGVDRAVVNVCIQKTPMPEEGRWNFTPFRDKVKALLEAGIKPEVVEGPTPLERTKLGLPGRDTEISAFCELLEVMDALDIRTVCYNWMPVIGWFRSRTDIPTRGGATVTGYCHRDMEDAPLTAYGRVSADRLWENLKYFLKAVVPHAERHGIRLAVHPDDPPVKMIRGIDRILISPDSLQKVVEMVPSDYSGITLCQGSVSASGVSVTETIERFARQNKIFFAHFRDIRGTAENFQETFHDNGQSDMYRCMKLYYKYGLDCCIRPDHVPTMPDEICSQPGYSVLGNLFAVGYMKGLMEA... | Pathway: Carbohydrate metabolism; pentose and glucuronate interconversion.
Function: Catalyzes the dehydration of D-mannonate.
EC: 4.2.1.8
Catalytic Activity: D-mannonate = 2-dehydro-3-deoxy-D-gluconate + H2O
Sequence Length: 328
Sequence Mass (Da): 36968
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A0A3C1A7G1 | MQRLDVEDILKATNGQLICGEPDFVISEITTDSRKAGVNMLFVPLVGENNDAHDYIGNAFENGASVVITHRDIPPRNDKSIIRVQDTRTALGDIARFYKEKYNLPTVAVTGSVGKTTTKDMISSVLTMKYNTVKTQGNYNNDIGLPLTVFRLEHKHEAVVLEMGMSHFGEIHYLASIAKPNIAVITNIGMSHIENLGSRENIYRSKMQICDFFDENGLLIANGDDEFLQKKQEGIKTITYGIENKACDLVAENVENLGMDGSRFTVLIDGENYEITVKTPGVHNVYNALASICVGRAMGVSMQDIIDGIREFQLTNMRME... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Involved in cell wall formation. Catalyzes the final step in the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the precursor of murein.
Catalytic Activity: ATP + D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-d... |
A0A3D0Y6J1 | MRAFIGMDFGNEVNGQIYEIQEKLRKYARKGRWKDIDNLHLTLKFLDEISPTQKIDIDEVMKEISITRRPLYLTISELGFFKGSGSIPVLWLGLEGDIEELHSLHEETDKALSAIGFLPEKRMFKPHITIGQDIIFTCDFNQICEEIGKIQIDTTNINSIFLFKSMQIHNKRVYFKETEYNFSRKA | 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: 186
Sequence Mass (Da): 21725
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A0A970FY35 | MDYSPLWISLRTACVATVFSVALGLVAAYYAVRLGRVLKGLVDGILTLPIILPPTVCGYFLLLFFGVSGPGGRLFEALFHERVVFSWYAPIISATVVAFPLFYRTMRGAFEEFDRTLIHSGQTLGLSGAFIFWRVILPNCRPSLVAGTVLAFARALGEFGATIMLAGNIPGKTTTISIAVYSAMAAGQTELAKKWVLIDLAISFAAMLIMNFAGGGARRRDTGVAR | Function: Part of the binding-protein-dependent transport system for molybdenum; probably responsible for the translocation of the substrate across the membrane.
Subcellular Location: Cell membrane
Sequence Length: 226
Sequence Mass (Da): 24351
Location Topology: Multi-pass membrane protein
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A0A9D1YT18 | MLEFFDMLMWPIKWLLEAVLVGFHWVIEQAGMDPASGLAWILSIAGLVLVVRTAMIPLTIKQIKSSRKALEVAPEVKKIQDKYKGKKDNLSREAMNREVMDVYKRAGTNPMASCLPLLVQMPIFLGLVQVLNTANQGRAGVGAMAEPLALQFQQASLFDLVPLHMSLEAGVADWNWPVILTAGILTVIMVSAQFYTQLQIMTKNQTPQMKESPMYKQQRIMLYIIPFFLLITAWIFPLATMFYWLVSNIYTLVQQLIIINRMPNPGSDAARAREERMARKRQRLGLPPVDEDGDTAEEENLIQNLQRKQPRRKGSRSDRK | 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... |
N0AWC3 | MSSFFITGTDTDVGKTIVTTLLAAYFQKQGKHVIPYKPIQSGAVEDGGKLVAPDIQLYQLAFPKLNEEEANTYLLKMPSSPHLASREEGVNILSSKIIQHFRLLEQKYDMVLVEGAGGLIVPLQDNGYCMIDLIKALSIPAVLVARAGLGTINHTVLSVMAMRNAGIPIAGIILNQVTDGDSSIEQDNKRMIEHLTNVPIIGMIPCLKNVEELIKNDRLLDRFLASQQFENLKEIEGNESTSTSRK | 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.... |
A0A354MXN0 | MKTERLGVYGGTFNPPHIGHRHAAGAFVEEAALDRLLVIPDYLPPHKEYAGGATAEERLAMTRIAFAGIPRTEVSDLELCRGGKSYTSDTLAALSALGRELFFLTGTDMFLTLPAWHEPERIFSLATIACIRREDDPHLEKEIAARAAEYRATFGAKILLLRASAIEVSSSELRTGLAARDPAALRLLPDGVADYIGTRGLYL | 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... |
A0A355JE68 | MLRRRKKTMIETTNKTKLFGILGTPVAHTLSPVMHSFMAEQNKIDMAYLAFDVPPEKLGDTMRGVKAIGACGFNITAPHKICVMDYLDHICPEAQHMNSVNTVVNRNGVWHGFNTDGNGYCESLLLEGHEIKNKNILMMGAGGSARSLAFTLAKSGAKSISITSRSMEKIHIIGEMVEHYTETIFYDTLDKAKDYDIVINTTPVGMHGAGDSGNPCGFMDLIHENMVCSDIIYNPKETVFLKEAKKRGARIHNGLGMLVLQGILAFELFCEISLDHKRTYEQLMHLFDYYRI | 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... |
F8AB74 | MDAFTIWFTGLSGSGKSTLSRRTYLEIKKRGLKAELLDGDIIRTNFSQELGFTKRERDINVKRIGFLSWLLNKHGIISVVAAIAPYEETRQLNRKLIPNYIEVFCNCPLEVVEKRDVKGLYAKARRGEIPNFTGISDPYEPPRNPEIEVFTDKETVAESMQKIISYLEKKGFLPATENNIDPTVIEEEERLLREHLRQLGFARKSW | Pathway: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 2/3.
Function: Catalyzes the synthesis of activated sulfate.
EC: 2.7.1.25
Catalytic Activity: adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate + ADP + H(+)
Sequence Length: 206
Sequence Mass (Da): 23777
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A0A182C8I2 | MANLTRKILGIPFKNPIIIPSGPGGFGQEINRSLLSKIGAFTIKSITLEPKEGNPPPRLVDAGYGLINSIGLQNPGIKMFLSTIYPKLCPFPTKLFFSIAGNSPREFREMAAVLNGIEGFELLELNLSCPNVKDASTLLGADPEPVAEILKQVKEVFTTRPVSVKLPPEMPDLPSVIKACENNGADALTLFNCITGARFDITTGKPFLKRVYGGYSGPAVKPIYLRKIYLARQLTKLPIIGMGGAYEWEDIFEYLLAGADLVGFGLRTMVDLTEVAELPEKAQKWLFNHGYNTLSEYLQSVRREEIK | 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: 307
Sequence Mass (Da): 33763
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A0A939V4L5 | MKIGLYGGSFDPIHNGHVSMIRGALDSGVVDIVIVIPSARNPFKPGRALTCAPYRYYMVKDVIEDLFDDDVFLSDIEFKIEGISYTDTVVDRISDPAYISAFLEEQGISSKKANASHKFCWIAGSDCLESLATWHNAASLVSKISFLVAFRPGDDCDIPKVAKETSDALGIPVDITTFDIDGVEIASSDIRRTGNFDGIPKAARSFIDEHDLYEACKILEDCSDDACKRFTDAAIWMYGYLRKKRLLHTLNTGLLSAYLAKCHGADIDKALIAGAVHDCAKELPIEDQERMSYARCGDLFVDEKLLHSPAGAVFYSESFG... | 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... |
A0A4Q4VSY3 | MDCWDIFDNCQTFVRNGIWRFFSFSHIWIVLFLVFSAFSNLYYFCWLQLISSAPASLFTPDPTLASDRVLGLSLFVISAFLKATWVGAWVQTLVITWFCDRKWRPPRSSKNIMQVEPSNWNDARESEKGPWIPYDQDRRPRRGEVWGGCNLRISDRVYHCTRLGRCLPVYDHYCDFIKAAVYLRTIKAYLFVLVFLSLDAVFSIAIAIYALARYQLRFAPFAISVIVAALVVIGGVAYFTWDKIWLLACKNCNRVDPEWHLVFKYDHNGQTRLHIQKFHGKHPWDLGIWENLHQVFGRYWWQWLFFWWQPERVSRYGRYA... | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 406
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 47620
Location Topology: Multi-pass membrane protein
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A0A354UQU0 | MYEAFLKELGGVKYERDKPLSDMTTFRLGGKADLVIYPTSTREAAKAISLLKGEAHYVVLGGGSNVLCSDKGFRGVVISTKLMNSMRLWGSILVCGAGVRMKDAVKIACDNTLGGLEFAVGIPGTVGGFIAMNGGCFNKCAADRVCYVVGEGGVYNNETCCFDYRRSRFSDGEAIFEAAFRLKVTEQDLIEAKLTRFKEVRKKSQPKGASSGCCFLNEGFFAGKVIDQAGLKGFGVGGATVASKHANFIISDGGTAADVYKLIQTIKEKVYERAGITLHEEIKFIGEF | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation.
Catalytic Activity: NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
EC: 1.3.1.98
Subcellular Location: Cytoplasm
Sequence Length: 288
Sequence Mass (Da): 31010
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A0A355V3G7 | MIENNNPEIAESALQTPFVFAEHTTYRCGGAAKLAFMPATVSSAVAVYDYLANEKIPFVVLGNGSNVLVSDSGFDGAVVCTKGLTGMYRTSADKIFCRAGTTVGKLLKYCTDNGFGGLEYLAGIPATCGGLAYMNGGAAGKYVADNIVTVKLYDGKIRNFSREMCNFSYKYSTMQDINGLILGVEFKICIKPRDEIKKNIAEVIASRRKLPKGASCGCVFKNPAGCSAGKIIDEAGLKGLSVGGASVSRDHANFIINAGASSRDVRALIEEVRRRVVERTGIKLEEEVVYIGDF | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation.
Catalytic Activity: NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
EC: 1.3.1.98
Subcellular Location: Cytoplasm
Sequence Length: 294
Sequence Mass (Da): 31441
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A0A356XHX0 | MFDFVGKRKIFMGISLAIMTVGLIFFLMFGLNLDIQFEGGTVMQVNTGTVDFASAEIQTVVQDTVGKSASSIQKLTGSENGDKINIILLKFTKSSALTQGETQQLVAALKTHLGSDDLDVSYETVEPFIGRELLNKGLLATLIASILIFLYVWWRFSVMSGIPAAVTALIALLHDSLIMLSFYAIFRLPVNEAFIAAILTVLGYSMNDTIVVYDRVRENRILIRKAHTYELMNRSIQQSLPRSINTVVSTLIAVITIYIFASIFNINSLKEFTLPLMVGFIAGVYSSIFIAGPLWAVWKERQENSRPAGKKQLKRA | 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: 316
Sequence Mass (Da): 35064
Location... |
A0A923ZWX2 | MPKTSIYTYLFMLPRVIWKLFFIINFIIGLVVLYPLFYLLLQGNAPYTKAFALMRFWACWILHVPGIFVHTKGNANVATTPCVLVANHASYLDIIVSYVVFNFYFVFVGKSEIRSAPLFNVFFKRMNILVDRGNASSGATAYKACSERLQRGESVFLFPEGGIRANSDMRTFKNGAFQLAIDNQVPIVPVTFRNNWKLLQTGAFFKCYGTPGIAQVVVHNSVPTLGLTKEYVPQLKKTVFDVIKNAL | 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: 247
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):... |
A0A3D2KL56 | MVRLFTAAEMREADRLAVEAGVPSLILMENAGRAVARLATRLLEEVPPGRRGSLLVLAGKGNNGGDGLVAARLLAGLGLPVEVVLAGSEDSFTGDALTNLRALEAQGLVRPRVFGRELEGPAFSALVKEAAVVVDALLGTGVSGAPREPVATLISLLGAVPEACVLAVDLPSGLDADTGRAPGQAVRARATVTFGGVKLGLALPGAAAFTGRLYLADIGLPPSCLERAGRARWWLLPREAAAWLPARPADGHKGTFGHVWVAAGSPGFTGAAVLTALGALRAGAGLATAAVPEGSRALVAGSFPEALTKGLEEGPDGRVA... | 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... |
A0A3D0YAU1 | MISIIVAIIVFSILILVHEFGHFIVARMNGVFVEEFAIGMGPKLISKKMGETIYSIRILPLGGFCKMTGEEENSDDPRAFCKKSVGQRMAIVVAGALMNFIYAIVAIIIAVSLMNNVTLPIVDTISPNSPAEIAGLMKGDKILYINDTKVGIMEDILFETALLNTPEKKVNLIIERNGEKKNITTSLNAGIIISAIPQELEGKINLKVGDFVVNIAGKDVYYIKDIEKELMNKNKVNVQVLRNDKIETLIDENTKTLVINQTRIKRVMGFSPLEQKLDFMESFDYSVKKFGYFIRTTWVSLSKLVTGQVSFKLVSGPIGI... | EC: 3.4.24.-
Subcellular Location: Membrane
Sequence Length: 425
Sequence Mass (Da): 47248
Location Topology: Multi-pass membrane protein
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A0A8J9WR15 | MPVCAKQAMALLHDAVPVMLGWLQRFRRPAPDRGAAVEVPRARGGGPGRAAIAVAGVADIEESVWAPRYGLKGMIDASVQLLMQPVPEGPWQAQHAMEACTAPLEFKTGKPHQSHRAQVTLYQLLMEERYGEPIEAGLLWYLNQSSPEIVTRSPYEVAGLMMQRNALAARLGRARSLPPMLREERSCSNCFQRSNCSLFHKASAPLLHTPYFPPLSSLSGVPRLATLGALEGGCAESAGMGPTFSELTGHLSAVHAQFLAHWLHLVDLEEGDTSAKRSEIWAMPGEEREALGRCVAGLRLTAERAKPPESPRDRGAWLLD... | Function: Key enzyme involved in DNA replication and DNA repair. Involved in Okazaki fragments processing by cleaving long flaps that escape FEN1: flaps that are longer than 27 nucleotides are coated by replication protein A complex (RPA), leading to recruit DNA2 which cleaves the flap until it is too short to bind RPA... |
A0A9E2BKQ1 | MEKPEALLEEAARRGFLPRGARLGVAISGGRDSVALAFAARSLAPRWRWSLILFHYDHRLRPESGQDAQFVRELARRWRLPLVVGRAPRQKKSWSEARARSRRYFFLRRQARRHGVEAVLLAHHGGDQLETLLLRLFRGSGPDGLAAMAPKRGRWIRPWLSLLPEELEAYVRLHQLPYREDASNRDVRYVRNVIRQKILPHLSAIHPAAWKSALQTARRLREERVYWQREARRALWDQAAEGGWRTKAMAAWPWPLFVRASQMIYERLRKEEALSRRRLLLLRPRLPERHLRTWRRMVTLGKPRAWEGPRGVRVAVTRGI... | 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)... |
A0A965ZB52 | MRLFIAFPVVRSEALDALMAAFRQHLAGDKITWSDLQNMHLTILFLGETDQVLLPDILSIMDAVAYDTDPFIVHYARVGLFGSRYDPRVVWMGAEPVDVPGALHRRLAEALQPLGFTPDRQNFVPHVTLGRIRMCRDKARLTQVVQQYQGLKLPEQKLSDIVLYESKLLPSGPQYITKGISTLGC | 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: 185
Sequence Mass (Da): 20833
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A0A923ZX23 | MNNNDFLQIGYISKLHGYRGELKIKPSSVVLINAQAIKYVLLKNTAGETPYKIEQLSASGETYVIKLMGIDSDLQAKSLIGCTCSVAKEYVQINEEEAMAGELVGFTVIDATLGNIGIVKELDTNAPQPLLYVTHPSNIEILIPFIPQAIVIDINEELKQIHIDAPEGLLALYLDEN | 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 ... |
A0A316M7P0 | MASTPLFFVTRDSIENDRVVITGADASHIVRVLRLREGAPLLVSDMQRNEYTVTITCASPQRVECAILSQRVADTESPYRITLYQAFPKADKLELVVQKAVELGAAEVVPVLSERCVSRPDAKSMENRLTRLNRIARAAAEQSGRGVLPAVSPPVPFPQMLEGLLAADLGFACYEGEREYKLRDLLADVPQPRTIAFFIGPEGGISEPELELLRRHGLPAVSLGRRILRTETAGLYVLSAISAILE | 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... |
A0A924ABP7 | MSRILALDYGLQRVGVAVTDPLRMFAQPLTTVDTRLILDYLKDYLSKESVDIIVLGLPTRFDGSDTHATSFVNVFAEKLRTTFPAVNLVMADERLTSRMAKASLLASGMKKNQRKDKKHLDTVSAALILQTYLETYS | Function: Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
EC: 3.1.-.-
Subcellular Location: Cytoplasm
Sequence Length: 137
Sequence Mass (Da): 15328
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A0A972C5H4 | MSHATRVEKKKSKAAKNKNKNIFKSVALITLVILLIAGFFAAGVVKSIIDSAPPLDLTKIEEQSQTSFFYDQDGNPVTEYFGFENRVWASLDEIPDMLQKAFIAIEDKRFMEHQGIDILRIGGAFINNLKGGYIQGASTITQQLVKTLYLTPERSYNRKIQEAYLAIKLEREFTKEQILEAYLNTINFEEGNYGVKAAAKDYFGKELNELTLKEMAVLAGLVRNPSGYNPRRNYHGEEDRRHITEDRAQLVLKAMLENEFITQQQYEEAVAEGLHVVKEATRLKLYDMAPFIEYAIYEVRDAIIKLKGWQDHKDGRQKAD... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-term... |
A0A3B8V7D8 | ERGRILSYPDRSRTYRIQTPQGFYRDELSSAYEAAYRDGKRDFTDDSSVYAAYVRAPKLCDGDESNVKLTYAEDFRAAFSRTGIGVDTHAFGKKQDYILLGGVKIPSESGLIAHSDGDVLAHAVCDALLSAAGLYDIGHYFPDTDEQWKNADSMKMLGNVLCLVKEQGFAPANLSVAIQAEKPRLARYIDEIRSSLASALSLPVSAVGISAGTNEKLGYIGEGKGITVNAAVLLKNI | Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 4/6.
EC: 4.6.1.12
Catalytic Activity: 4-CDP-2-C-methyl-D-erythritol 2-phosphate = 2-C-methyl-D-erythritol 2,4-cyclic diphosphate + CMP
Sequence Length: 237
Sequence M... |
A0A943J1R0 | MKDKVVVVVGPTASGKSSLAIDIAEKKNGEVVSADSMQIYRGMDIGTAKVSDTRGVKHYLIDIVEPSETFTLSDFLLEANKAVKHILSKGKLPVIAGGTGLYVSSFMDNISLSEVRIDENYRRQLRDFAAKNGNKKLHELLKDVDPESYKILHPNDEKRIIRALEMVHLSGITVSEQNKISKLIPSPYDFYVIGLNFKDRSVLYDRINKRVDDMIAAGFIDEVASLDFESLSQTARQAIGYKQIFEYIKGT | 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... |
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