ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
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A0A952PAD1 | MLQVKPIKGFNSFSLIFNAGKKFYDKDLTAVFVHSDAEENNALIKNCNDDKTLYYGVTAGKKFIRKAVVRNRVKRLLRESIKKIFAERYIMLDKPPFKYAVFSWRKAPVHPALINLADVLPSLERVTKSAELYFSSEAESEK | 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... |
A0A1G1LI83 | MLHRLLKGIHWRIVSVAAGLVLIGVVAIYSASFRMGGGFAAKQATWTLIAVCAFFSAAWVGYRFFLNVSYLFYGLTIVLLVFVPLFGETYLGANRWISFGPFQLQPSELCKIATILILAQYLANRTALSEQKRSFFVTLALVAVPVGLILKQPDLGSALVFLPVLFAILFFWGFRIRYLVFLAMLGISMAPFLWHTLKPYQQKRLLVFFNPSVDPIGASYTAIQSKIAVGSGGLIGKGWLRGTQTQLDFVPEHHTDFIFSVIGEEFGFAGSIVIIALFGFLLLYVFEIMEHTTDLKARLLAIGIAAFLFFQVFVNIGMTI... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Peptidoglycan polymerase that is essential for cell wall elongation.
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-... |
A0A1W9UBT6 | MQWRVDEIRDQWGMRGECLVAEPLAPLTTWRVGGSADLLVRPVDLEDVHALFNFLRHNRLPWVVLGGGSNVLIADSGVRGVVIQLTDMNYIIPCGECQLRVGAGCSINHLVAETVRQGYAGFESLAGIPGTVGAAVAGNAGALGQQVGDCVHSGLVAENAAVERWLHEEFAFGYRSSAITTEYVVLEVTMKCQRGQPEQLRQRVKLARQHRWQAQPVVGANAGSVFKNPPRQSAWKLIAESGLQGKSVGDAQVSKQHANFIVNCGKASAMDIVALVSKVQQVVAEKTGFKLEPEIKFIGDFGEAAVQVALMQVNGRV | 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: 317
Sequence Mass (Da): 34219
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A0A2G9P8P1 | MKQKTLTNTMDYQELADVYEQLDKTTKNLEKRDIIADFLKRTPKSELANVILFLNGEIFPSVSEEVLGIADKMVLKALSKITGKNENAITNVWKEKGDLGLVAEQVVKKKTQTTLSQEKLTISYVMEILRAIARFEGENSTQKKTGSLAKLLSSAKPKEARYITRTALGDLRIGVGFGIIRDAIVKAFNVEKEHVQHAYDFRSDLSELVLLAKESGNKGLKNVDLKVGKPLRLMLYQKAQGISNGFTRVGAPAAIEYKYDGMRVQCHFKKGEVTLFTRRLDDVTKQFPDLVGALKEHVSCKECILEGEAVAYNSKTKEYV... | Function: DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.
EC: 6.5.1.1
Catalytic Activity: ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.
Sequence Length: 567
Sequence Mass (Da): 643... |
M2YMQ1 | MPLDMTRSTANALRREIAGNAAHVTSTLNHLTIAVKMAETPAPEHQVPSQPASPLPKRTKYTEPAANLTVASLTFPAMLNDQAPTPTPGTPNQNSLANPLSQMSGPTQATASYPPPAPGSTLPSMSMPMPPMGQMPQIPSMSFEPPPPALQVKLLSESAKPPTRGSEYAAGYDLYASKDAVVPAPSIKLIQASAVLDLTEDDFDFLTRAGVIDADYRGPVKVLLFNLSDVDFQVAVGERVAQLIIERIYTPQVLVVEQLEETVRGAGGFGSTGGFGGSLPPINHPSTAGARQPGKTAWMRSAEPSHLTNHTTFGKEWLPF... | Pathway: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 2/2.
Function: This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA... |
A0A2G9PB40 | MMFASLFKTTLYLGVLTGILLAFGAFFAGTTGLIIAFMFASVINVISYFYSDRIVIALYHGREVTQEQEPELHALVSRLVVKARLPMPRVYLLPTPVLNAFATGRSPKHAAIAVTQRLLDTLPKQHVEAVLAHELTHVKNRDTLISTVAAILAGMISMIGNMAWYSGFLFGTRDRDNALGDMLASLALIIITPILALIIRFALSRTREYAADKGGARLTSPQAMIGALEALEFGPRLRTHGSSATAHLFIVNPFSRGAFSELFSTHPSLAKRVETIRQEFKI | Cofactor: Binds 1 zinc ion per subunit.
EC: 3.4.24.-
Subcellular Location: Cell membrane
Sequence Length: 282
Sequence Mass (Da): 30944
Location Topology: Multi-pass membrane protein
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A0A836D6H5 | MEARRLFQQILSAVDYCHRHMVVHRDLKPENVLLDAQMNAKIADFGLSNMMSDGEFLRTSCGSPNYAAPEVISGRLYAGPEVDIWSCGVILYALLCGTLPFDDEHVPTLFKKIRGGVFYIPEYLNRSVATLLMHMLQVDPLKRATIKDIREHEWFKQDLPSYLFPEDPSYDANVIDDEAVKEVCEKFECTESEVMNSLYSGDPQDQLAVAYHLIIDNRRIMNQASEFYLASSPPTGSFMDDSTMHIPPGLKPHPERMPPLIADSPKARCPLDALNTTKPKSLAVKKAKWHLGIRSQSKPYDIMAEVYRAMKQLDFEWKVV... | Catalytic Activity: ATP + L-seryl-[3-hydroxy-3-methylglutaryl-coenzyme A reductase] = ADP + H(+) + O-phospho-L-seryl-[3-hydroxy-3-methylglutaryl-coenzyme A reductase]
EC: 2.7.11.1
Subcellular Location: Cytoplasm
Sequence Length: 415
Sequence Mass (Da): 47208
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A0A959R6T6 | MVRKSETIDPFVESVRRFMRLHEMSHGGESILVAVSGGIDSVVMLDVIARLSVPLRFSFGVAHFDHGLRESSTVDADFVRELATRYRVKAFVASGDVRRIADEEGRSVEETARRERYAFLERIARRHRYDTVMTGHTADDNAETLMMNLLRGSGVTGLAGIPPTRRLAGGGTVIVARPLLGQSRHQIEEYASASELKWREDESNQSGEFTRNRVRHELMALLRTFNPNVVETLNTTAGLMRDFDRYLSSAVEAALRGTTVEEPVHGERILLDVRQLRHLQPALRGEVVQRAMCETFDIPPISHVAVERGLNLIWKETGAR... | 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)... |
A0A078KEE6 | MENINYIYCWIIQRISAIILTIYTIFIIIYILYHPNLDYTTWSLLFYNFFMRMFTILAIISGVAHTWIGLFTIITDYIKCSYIRLCMNILIIIYLFLFLCGYIEVVYGVFLCNSK | Cofactor: The heme is bound between the two transmembrane subunits.
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle.
Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH).
Subcellular Location: Cell inner membrane
Sequence Length: 115
Sequence Mass (Da): 13793
Location Topology: Multi-pass me... |
G0EDB1 | MSKVHMVDVTHKPVVYREAIAEGAIRLRPETIRAIREGRIEKGDVLTTAAIAGILAAKKTWDLIPLCHPLPLTHVDVKCEVSGEDRVVCRAKVVTSAKTGVEMEALTAVSIALLTVWDMTKKLEKDEEGQYPYTRIEYIRVVSKKKGGEA | Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
Function: Catalyzes the conversion of (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP).
EC: 4.6.1.17
Catalytic Activity: (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate = cyclic pyranopterin phosphate + diph... |
A0A2I0QW16 | MKIGVIGAGAIGMFVSAKLSKSHDVTCYVRRDEQRLIINDEGIRLNDQTYRVASKLFDNLKNEDLLIICLKQTHLDSALKKLSENHPDTPMLFLQNGLSHIDKIKSLSQPILIGTCEHGVLRVSDYEVRHKGEGRIYLSAFEETTKELAKERISPIIDGDDFPVIFKDDLMSMLYEKLVINSVINPITALFQVENGKVLSNSHLKEIAYNLTVEGCEVLNLDENHMWKRVQQVAEHTSSNFSSMVYDIQKGNETEIESMNGYLLNISDQELPNHELIYHLIKAKEIM | Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 2/2.
Function: Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid.
EC: 1.1.1.169
Catalytic Activity: (R)-pantoate + NADP(+) = 2-dehydropantoate + H(+) + NADPH
Sequence Length: 287
Sequen... |
A0A1L0AX97 | MFNKFIRFNRHLPRNFNLKFKRFNSNSSYQKTNYSRKSKYIFGFSTLFIGSTILTFNNPTFLLQSFFKVNDVLVSEDVKLNLIYDYMFNNLHLKNVQIGYAWEQTEQVHIEYDWKNGFIQINNLSIKLDNDNIFFIKKLKFNISLYRYFFKKNEPNSLNLIDMIEADGVKGKMNTNTMLNYNFDMNNNIKVRNCKLAINQRHELVIFQLELNKLSNKSFLLDLMNCEILSGEFDKSLFTIVEKQPHMINDKIQELNEDLKNSWEKISRLQFNKININKLNLDKFDWIYDGDVEFVMDLMIPKMKDTSSANSNNPYLVLDI... | Function: Involved in the organization of the mitochondrial membranes and the global structure of the mitochondria. Also required for mitochondrial distribution and mobility as well as for the maintenance of mitochondrial DNA nucleoids structures.
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 493
... |
A0A1G1LNE9 | MFILGLKGLSSPKYARGGMQLAAAGMLLAVLGTLFDDHVRNYTWIIVGFIIGTIIGGAMGLQIPMTAVPQRTAFSHSLGALAACLVGVAEFVLYEDMNRVKLTALDFEVVVGGLTFTGSLIAAAKLQELLPGRPLTYKGQNFITIGLLIAVATIGIYLVASQTNSAFFYLMVSLAFVFGLLLVIPIGAADMPTVIALLNSYGGLADAAMGFVLMNKIQIITGSLDGTSGFLLALLMCRAMNRSALNVLFGAFGKVASEDEAAKAAAAKGTVRSISAEESVVLFDMAQTVIIAPGYGMAVARAQYAVAELAGILRERGINV... | Function: The transhydrogenation between NADH and NADP is coupled to respiration and ATP hydrolysis and functions as a proton pump across the membrane.
Catalytic Activity: H(+)(in) + NAD(+) + NADPH = H(+)(out) + NADH + NADP(+)
EC: 7.1.1.1
Subcellular Location: Cell inner membrane
Sequence Length: 446
Sequence Mass (Da)... |
M1WR28 | MKVGLMIQGVDLFFSLFNNLALFIALVVLYRFIHEQFSAWPSSGRQIVMGIVFGFFAIGCMYEKIPVYEGVIVDQRNAVIALSGAFGGPVSALISGMLAGGFRVYLGGGGVLAGVVGVALAAFAGVVINLFFRPFSSLPRAFYFAFFASVLIVPGFLFVQDFKTGWLLTQAIALPYGVAIFCGIFVVGLLLNSQEGQAELDTLFRESEQQYRGLVESSEDLIVNVDRQARFSFVNHMAAMVLGCSPGESVGRSVFDFVLREDRRKTREWFEECIERNVRQAKLENRLVNMKNQSYRVVMWSCSFHYDDQGVFLGLGGIAR... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 842
Sequence Mass (Da): 93057
Location Topology: Multi-pass membrane protein
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A0A445N3M1 | MSLQGASNETIQQVLMMSPLCIAIIEDEIAHLSLMKRAILKAFNSAEIHHFEDAATCLETIDQINPGIIISDYLMPGMNGIDLLEAVNGRGLDIPVIIITGQGGEDIAVRAMKLGAWDYLVKSADFFTLLPSVIEKVIREKETKDLLREAEEKYRLVVDNAGEGIMVEQAQMVKFYNPRFAEIFGYKMEEFTSGSLMDIVYPEDKSMVAEYLVKLITDGHKPVTCDFRIISADGQLKWLSNNAVQINWGGRPASLNFLSDITERKRTEKRIQSLTHELIRAQERERSTIARELHDTTLQDLVALKLKTDMLLFDQEELPA... | Function: Member of the two-component regulatory system NreB/NreC involved in the control of dissimilatory nitrate/nitrite reduction in response to oxygen. NreB functions as a direct oxygen sensor histidine kinase which is autophosphorylated, in the absence of oxygen, probably at the conserved histidine residue, and tr... |
A0A959RIP1 | MFDTSIIELSTSALQYNLKFIKKKLKPGVRYCSVVKGNAYGHGVSQFVQMAMGEGIDYFALYSAEEAFLLKKQLYNIPELFIMGAIENEAVEWVIKNNIEFSVFDFERLETALDYSKKLNTKAKIHLEIETGMRRTGFSYTEFPKLFKWFRKNGEYITLQGIFTHFAGAESRANHFRVSNQINNFDLTLKMFQEEGLRSVYQHSTCSAALLNYPETQKNMVRIGILQYGYWPNKETHVRCTGEKDNLPVMLKRMIRWTSKVMAIKEVNKGCFIGYGTAYLANKNTKLAVIPVGYSHGFSRNLSNVGSVLINGKIAQVVGT... | 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: 383
Sequence Mass (Da): 43459
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Q753R4 | MTTISVWSNSQHRSLFKKPDGYYSDSPPNRLRIMEDPNLSHYLFSDAHIDKNTDPLVWKPELQEEQAQSEDDAGSLHGLLYMLMEYERRNGKKIDADFIASGEHLKHLIYPLLGGPSAHVDIYVRNFDGQIFIRAVQKKHCPLRYENRGKICSCGKRMQEEGRSPSMTINSSYELPFWSKQVVRNGPQYMNVARAGVGEHKMVIGVEADGILASKELKGGNLKHYVELGVCKERWDLDRRLFFVWLHCFVVGIDRITIGFRDDSFKLVDVQEYRTMEILQLFETSALRNDCNSVMNWYGEILKNLSRFFKRRADDFCVYK... | Function: Decapping enzyme for NAD-capped RNAs: specifically hydrolyzes the nicotinamide adenine dinucleotide (NAD) cap from a subset of RNAs by removing the entire NAD moiety from the 5'-end of an NAD-capped RNA.
Catalytic Activity: a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside-ribonucleotide in mRNA + ... |
A0A2Z2NXX5 | MASESAVDGSRSGAHTRVGLFGGTFDPVHYGHLRPAVEMAEQYQLSKLYLLPNHRPVHRGPTAATTDCRIDMLKIALQDAPRLQVDTREALRDKPSYTFDTLCEIHAEQPEATLLFFMGMDAFAAFDTWHDWEGILNLANLVIVGRPEAEHSDFSARLVARQQERCGHKIESGGAGVIELCEVTQMAISATDVRRRIANEQTVRFLLPEQVLEYIGRNNLYRKSQ | 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... |
A0A4Y7RYE5 | MAYRALYREWRPQAFGAIIGQDHITRTLKNAVEAGRVGHAYLFCGARGTGKTTTAKVLAKALNCLQPVGPEPCNRCDNCIAVTEGFSVDVIEIDAASNRGIDEIRDLREKVQFTPSTGRFRVYIIDEVHMLTNEAFNALLKTLEEPPRHAVLILATTEPHKIPLTILSRCQRFDFKRITPAGIIGRLKEVAAGAQLEVEDEALRLIARAAEGGLRDALSLLDQAAAFGSLTITAEDVHNLLGTVRVDALNKMAGYLAAGEAGAALRLAGQLTAEGKDLRLFAREMAAYLRALLLEKIAPGSNAQEAWDTTGLRACMAQFN... | Function: DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity.
EC: 2.7.7.7
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Length: 590
Seq... |
G0EEJ5 | MPGLDAIRDAVRKFLRLSGPYERAVEEFIRDLQRALLSADVNVRLVFDLTRRIRERALKEKPPPGASRRDWFLKIVYEELVKLFGGDREPEVKPPYTPYVIMLVGVQGSGKTTTAAKLALFYKRMGYKVGLVAADVYRPGAYDQLRQLAERIGVMFYGEPGSRDAVGIATRGVKELKERGANIVIVDTAGRHGYGSEVALLEEMKRMSEAIKPDEVMLVIDAAMGQKSFDLAKRFHEATPIGSIIVTKMDGTAKGGGALSAVAATGAIIKFIGTGEDVEEFEVFNPRRFVSRLLGMGDIEGILERIKRLEAAEEFEKTVE... | Function: Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Binds to the hydrophobic signal sequence of the ribosome-nascent chain (RNC) as it emerges from the ribosomes. The SRP-RNC complex is then targeted to the cytoplasmic membrane where it interacts with the SRP recept... |
G4E4N7 | MQRVIDHGFYRGLLGLLALGLSASVSAQGFDPSPAQPLDHIVAVVEEDVIMASELRQRMQLIAQQIQTRGGLLPDEAILIRQVAERLALERLQLQEARRIGIRIDDLTLNNAVEAIARDNQLSLPEFREQLLAQGLNFAQFREQVRDELTIAQLRRRQVENRIQVTEQEIDDLIASESGAIDSGMQYRLQHILVALPEGASPQDIQSARAKAEALRQEAQAGADFTELALRASSSQHALEGGDLGWRGAAQIPTLFARHVVLMRVGDISEVVRSPSGFHLIRLAERRGGERANITQIRARHILIQPSEILSDTEARERLL... | Function: Chaperone involved in the correct folding and assembly of outer membrane proteins. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane-associat... |
A0A078KDR0 | MLPWLSIIGIGEDGLKGLIKAAIIAIAQSKILFGGQRHINLFKIYGKETYNWSYPIEQGIKHLCYFRGNKVAILASGDPFFFGIGTILTQRIPIKEIRCYPSISVFSLVCARIGWTMQDVEVISLHGGRTQECIYPYLHDGARIILLTYNETSPAIISALLVDRGFGKSKFIILEGLNGPYERVRAMTAHSFINYNNNDINPLNVIAIDVIANIEIITLPLTFGRCDNWFDNNGQITKSDIRALTIAKLAPRRMELLWDIGAGSGSISIEWMLIHPSLEAIAIEVNEKRAINIMQNAYRLGVNNLCIVNGDSMDIIYDLA... | Pathway: Cofactor biosynthesis; adenosylcobalamin 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: 412
Seq... |
A0A0T1X7B5 | METAEFEKLAIPIALVVDDDPLILMDTADMIAGEGYAVVEAKTADQAYDFLDRHSSLQLLFTDVQMPGSPVAGSGSHVQWCSERYRTYRAYDDTYVPRAGMRARCMSPYR | Function: Has immunoglobulin-binding and hemagglutination properties, and can bind to mannose. Essential for virulence. May be involved in LPS biosynthesis or polysaccharide transport.
Subcellular Location: Cell membrane
Sequence Length: 110
Sequence Mass (Da): 12331
Location Topology: Single-pass membrane protein
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B9RGP0 | MRAEAGAAEARAMASSKNMEEEKNKSSTAASTSGISSCRSVSILLACLVHLICGLGLAVSLWVAHNLYSVNLVSDPSDTLLLIWTVETPIVVLLYSWFRLNPKKCSTDTYQRPLIGLFLCHYSQPNGSLEYMICMPAHGAVIAAWFGAWPMPLDWERPWQEWPICVTYGAMIGYLVGMLVSLGFVLARSGQQHPKGD | Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 197
Sequence Mass (Da): 21624
Location Topology: Multi-pass membrane protein
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W5QE45 | NTTGYLKTDHFIYCLPVRGCRPGKIVQMTEAEVRGLCIKSREIFLSQPILLELEAPLKICGDIHGQYTDLLRLFEYGGFPPEANYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECNKRRFNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDTGLLCDLLWSDPDKDVQGWGENDRGVSFTFGADVVSKFLNRHDLDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGGMMSVDETLMCSFQILKPSEKKAKYQYGGLNSGRPVTPPRT... | Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
EC: 3.1.3.16
Subcellular Location: Nucleus
Sequence Length: 327
Sequence Mass (Da): 37298
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M1WL51 | MFKRIFFVVLLVPVTLYYSIRMLLVDPEKAAPEEYDSWGLKWGAAAVWLSGITIETDMGDVDPKGHYVFIGNHQSNLDIPVLFKVLKGNRIRFVAKKSLFDIPIYGKALAHSGHICIDRDNRRAAMQSLNDAVEQAQKGISPLIFPEGTRNDNLDDLMEFKIGAMIIALKCGLPVVPFVMAHTGRVMPKGKMIIDNRPVVRFKALPIIDPSQYTLKEREKFKDDLRAMMSKAYKELLAEG | 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: 240
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):... |
A0A836CSQ6 | MLAWQDGGAKAAPSHHKISFSVLDILDPQKFTRAALPAVRPAPREAKKSLAETEARKDASRDPVPQREAPDAEGRGAGLASPLEGSEAEEAEEEDEDVEDAGRRRGERAVHLRAGLTLSPEARAAASAAGESGAGGLAGSPGSPRPRRRRAEPSSSKPRRARTAFTYEQLVALENKFRATRYLSVCERLNLALSLSLTETQVKIWFQNRRTKWKKQNPGAEAFVQFFMVLKISFPSASQKTQYNLEWSVIFPLEDIMLSKLARLQTVAGLGRGVHSSVASATSVATKKTVQGPPSSDYIFERESKYGAHNYHPLPVALER... | Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-ornithine: step 1/1.
EC: 2.6.1.13
Subcellular Location: Nucleus
Sequence Length: 978
Sequence Mass (Da): 106378
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W5Q4E2 | MRARNRASLIVWIRTIWKTIREHVLVVLVVYLSVKGFHYILNLAILILIQTDPRLHTPMYFFLKNLSFVDLCFSTSIVPQMLVHFLVKKKTISFAGCSLQIVVFLLAGCTECALLAMMSYDRYVAVCRPLHYSTLMTHRVCVQLAMEHWNFTLGSGFILIGILNDSFSPELICATVTVLYMLALASNGFLLLAITMDARLHVPMYLLLGQLSLMDLLFTSVVTPKAFVDYLLSENTISFGGCAFQMFLALTVGGAEDLLLAFMAYDRYVAIC | Function: Putative odorant or sperm cell receptor.
Subcellular Location: Membrane
Sequence Length: 272
Sequence Mass (Da): 30635
Location Topology: Multi-pass membrane protein
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G4E749 | MITLLGFDYGTRRIGVAVGNRYTQSANPLEVVANRASGPDWQALDALVKDWQPEGLVIGWVSYADGREHPLARAIQRFADQLGQRYGLPLYRVNEYASSAEASARLEAARQHTGRKRSKTPALDPLAASLLLEQWFAEHPL | Function: Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
EC: 3.1.-.-
Subcellular Location: Cytoplasm
Sequence Length: 141
Sequence Mass (Da): 15659
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A0A952ICN1 | MRVSLEWLKEYVDLDGLAPETIADALTDAGLEVESIEHIGGNFSGVVVAKVTETEKHPNADRLKLVTVNTGNAESKVVCGAPNVQKDQYIAFAKVGAKVINRKDGSTFELTPAKIRGVESKGMICAISELGLETFYSFEEDGIWPIDEYVSDADLGKDLKTALNLQADVVLDTAPTANRGDLMSMVGVAREVAALFDRELKLPQVPKSVQVPKASFNIRLNDPTACRYFGGMTLEDVTVAPSPDWMIRRLEAAGVRAISNVVDITNYVLLELGQPLHGFDKDKLGLGGDINVRFAKENEKFKTLDDEERTLTEKTAVVTL... | 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: 829
Sequence Mass (Da): 91196
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A0A3N5K3F5 | MRTKLDYILHKNGSEILFEDEAVLVIDKPAGLLVLPDRFDKTLVNLYDLLKEALGAIFIVHRIDRETSGVVLFARTAESHASLNAAFEQRHIEKYYRAIVVGSPSAQSGTIDLPIGENSHGPRKMKIDNQNGKEAITAYTVLEKFDQYAYLEARPRTGRTHQIRVHLNAIGLPILSDPLYGSSGRLFLSKLKRNYKSNGEEKPLIARTALHAFSLTFVHPGTGEKMSIETPLPKDMSMVLKVLRKYQGSRRAGGSSTLIDSDTEER | Function: Responsible for synthesis of pseudouridine from uracil.
EC: 5.4.99.-
Catalytic Activity: a uridine in RNA = a pseudouridine in RNA
Sequence Length: 266
Sequence Mass (Da): 29732
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A0A2R8B6B9 | MGAFWGLLLGGLTVLAGSGLALGAALGLTGFLILQFVAGGATFVAVDAVWNVLNSFTLSAIPLFIILGEIMLRSGVSERIYSALSPLFQHVPGGLLHTNIAVCTLFGAVSGSSLSTAAAVGSVAYPEMTARGYDRKTVVASLAGGGTLGLLIPPSLSLLIYGALTETSIGRLFLAGILPGLLFAAMFMAYIFILCLSRPDLAPSAESKVRLVKSIRNILGLWPFLLLILAIMGSIAGGIATPTEAAGIGVIATILVGRFWGSLSLVTLTESLFAAILLYASIAFVVMGATILAQAVSLLGVPQSILGSVREANLGPLTVL... | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 431
Sequence Mass (Da): 44589
Location Topology: Multi-pass membrane protein
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A0A2G9P9M8 | MILIGLEVHVQLNTKTKLFCACSTNFKDEGKPNTNTCPTCLGMPGAKPSFNRGVFEKALAVSLALNGTISSEMFFSRKTYFYPDMPKNFQTTQYELPISQGGYLIIKVDGKDKKIRLRRVHIEEDPGKLVHVGGDITHSKYTLVDYNRSGLPLVEIVTEPDLSTPAQAREFMQKLRSILQHLGVYEDSFVMKADANVSIHGGNRVEIKNITGAKNIEKALLFEISRQKMLYERKTPIEQHTRHFNAASGITKSLRTKEEEADYGYIFEPDLPLYDINKKAVADAKRALPELPDVRISRFVKDLALNRDVADALVLVDKAL... | 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 ... |
A0A1D2YX73 | MDKFEEILHSYQENIEEDVKKRVEFIRNYVKDANAKGVVVGISGGIDSAVTAALAIIAMGKENVIGVWMPAYSDPIHERDAKALASAIDLNLVTVDLGSTFNNLAKEIEEIVSLNDLAKGNTKARLRMTTLYAIASVKGYLVSDTCNYSEIYVGYMTKGGDGLADFNPVGSLTKHQIRLLAKHLNIPKEIIEKAPSADLWAGQTDEQEMGFTYEDLDRYLLTGEGNKEVIEKIERLHRISEHKRVLMPTI | 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... |
A0A959R4P0 | MAQPKEEEAIVKSEENVGGEPQEEFPEKPTGLYRDRELSWLSFNYRVLQEAKDLRVPLFERIKFLAIYSSNLDEFFRVRVASLRSLLRLRKRSRQSLTIDLGELIEQIRSTVFKYQEEIGKTYRDEILPNLEREGIRILNESEVNAEQLKHLNEWFEEHLLTNLHATFLQQEFAGPFLHNRKLYLIVALQPRLARKFWSEQSEEERVSAPKSEISLAILEVPSGTLGRFHKLPSSNGEHHVMFLDDILRLFLSRIFPGFNPVDAWSVKLTRDAELYIDDEFAGDLLKKIRKGLRKREQGVPSRFLFDKRMPADVLKSLRK... | PTM: An intermediate of this reaction is the autophosphorylated ppk in which a phosphate is covalently linked to a histidine residue through a N-P bond.
Function: Catalyzes the reversible transfer of the terminal phosphate of ATP to form a long-chain polyphosphate (polyP).
EC: 2.7.4.1
Catalytic Activity: [phosphate](n)... |
A0A1D2YU25 | MNYFYVGIGGFLGAIFRVETGKLLSELYPNHIFPYPTLIINLIGSFLLAYFLTVIRERFSLSPQLILLFSTGFLGSFTTFSTFSVETLRLVQLGAFDQAILYLLSSFILGIFFAWIGVKIALKTTTHDIRANIRRSES | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Subcellular Location: Cell membrane
Sequence Length: 138
Sequence Mass (Da): 15590
Location Topology: Multi-pass membrane protein
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A0A959MGZ2 | MRSLGIDYGTARVGLAISDELGITVRPYSVLTYSKSVVDEIHKVVQTEAVELVVVGMPYDLRGKETETTVRVKKFIEKLRGILPCPVVEWDEALSSRKAVERMVEAGVKKSKRREKGTTDSWAAAIILQEYLSS | Function: Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
EC: 3.1.-.-
Subcellular Location: Cytoplasm
Sequence Length: 134
Sequence Mass (Da): 14928
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A0A2I1HJW7 | QLEAINAYLNGNDTFVSMKTGGGKTLCYALSAVCSEGLTIVFSPLKALMEDQKRELVKAGIPCAVLYANLTQGTRIQEKIFEEIASGLIKVLFVTPEKLVSNEGFCRFITQLYEKKKIRFVIDEAHCIIAFQDFRKAWTQLGMLKQRWRSVPIMLLTATCTRSEVDEILANLTIEKNKFTLIRDSTKIHDQYITNIIDIINRNLHGRTIIYCATRFNCERLHNKLQESLTGISIDYFHGGLRDDERETAMNNWKSNHTQIMVATSAFGXGMGINSNNILVVIHAEAPMSITNLIQEAGRAGRDGNTATHVIFFSKKDIRT... | Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
EC: 3.6.4.12
Subcellular Location: Nucleus
Sequence Length: 455
Sequence Mass (Da): 51980
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A0A2G8Y8E9 | MDQERNSTRPLVIGGVCISTPPEKGWVFDRWLSSQGVLALRSFVQRFTTLLTRAKCSLAPWCTNAPHSAATGSCGESGRTQHRGNAWLSRLFRPTRNSPRASVPFSSSLSSSLSSSLSSSSPPAVENSFGVVAHSDGDVLLHAVCDAVFGAFALGDIGEHFSDSNPAFRGMSSSLLVARALEIVRAKHPDWRLGSVDATVVFDAMKFGRARKQKMRENLAELLQLPAAAVSVKAKTSEGVGPVGRKEAVACHVVLTLFKSTRTDETEKKQETNNAQRLLQNSPQTQA | 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: 287
Sequence M... |
A0A1F8C237 | MIIVVLGPQGSGKGTQAKLLAQKYNLKVISMGDLLRAASKADEGINEIVNKKGGLVPPETTYSVLIEYLKANEINDNFILDGFPRMVEQYELFKTWLVEKGKQIDIVIVLDISEEESIRRLSGRRTDPVGGKIYNLDTSPKPGPEVDVASLVQRDDDKPEAIRQRLNWYKTDVLPLIGHLREANVKVVEIDAARSVDAIQADLIAFLEGLE | Pathway: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from ADP: step 1/1.
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: AMP + ATP = 2 ADP
EC... |
A0A679EQS8 | MRKKRVIAGIVTSALLSTVLIKNIAFAAYTVDGVSMQPTLKEGHHFYINKLTNRFNKIERFDIVVFQMPGEKQALVKRVIGLPGEKIEYRNDKLYVNGKYVPEPFLKKNKEKVYGNPITGNFTLKEITGKEAVPEKCIFVIGDNRLNSRDSRHFGFVHEKNVIGEVKP | 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: 168
Sequence Mass (Da): 19136
Location Topology: Single-pass type II membrane protein
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A0A0T5PP05 | MPDFNNLFINNRNWADRIEREQPGFFKQLSEQQAPEYLWIGCSDSRVPADEIVGLMPGELFVHRNVANLVVHSDMNCLSVLQYAIDILKVKHILVVGHYGCGGVKAALLNQRVGFVDNWLRNVKDVYALHRQQIDCLETEDQRVNRLRYPQK | Function: Reversible hydration of carbon dioxide.
EC: 4.2.1.1
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Length: 152
Sequence Mass (Da): 17592
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A0A934SEV4 | MMAKAMIRRAVGAASGLATAGMVASSALAQDVLGDLPTIGKPHARGTGFQEPVTELAHDQQWLDHFVLIIIAVVTVFVCILLLIVIFRYNSRVNPVPARFTHNTPVEIVWTLVPVLILVVIGAFSLPALFRSQEMPSDPDVVIKAIGNQWFWSYEYPDNGIAFDSIMLNKDQLAEYGYAEDEYLLATDTAVVVPVGQTVLLQVTANDVIHSWTIPAFAIKQDAVPGRIAQAWFNVEKEGIYFGQCSELCGINHAYMPIVVKAVTPEKYAAWVAEQGGTMGEEEQESAAIDAAAAEVELAEAN | Cofactor: Binds a copper A center.
Function: Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).
EC: 7.1.1.9
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(... |
M3AIG2 | MPIAVSPERPRTGVTRLTGGRLVKGDKLIEHDLWISSVTGKILHDQEVFYEHHVTPDEIIDLEGKILCPGFIDVQFNGAFGYDFSTIPEDGMEGYVKGLRKLNRHLIKTGVTSYLPTIPSNNPEIYQKTLPHLRPSGDSRNPLEGSESLGAHVEGPFISPTKNGIHSHDVLRTASNGFGDIEACYGSENLPLGSRGPITKITAAPEVEGVAQLIPEFTRRGIIFSVGHTEATYEDVTNAVRSGATMITHLFNAMRPLHHRNPGPFGVLGKAEETERPYFGVISDGIHLHPTTVKIAYNAHKDGFIIVTDAMKTVGQPDGV... | Cofactor: Binds 1 divalent metal cation per subunit.
EC: 3.5.1.25
Catalytic Activity: H2O + N-acetyl-D-glucosamine 6-phosphate = acetate + D-glucosamine 6-phosphate
Sequence Length: 439
Sequence Mass (Da): 48301
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K0KR38 | MGIKYKVFQWVLNQILEITLVYSKKYQVGRMSEVINPPKVELTEKQRRKLEKDERRKKFADTTIQGTNDYSIVSKRSVEKLYTQKLDQDFGISTPEYFKHFVKKVPRRSPAINRGYWTRMEAIKQSTLKIIQNSLNQGKKITIINLGAGYDPLAFQFLDSRNPDNSTHEGKVSFIDVDYPDLNKMKVQMINNSSEIKDIIGKETESKSSIEGVELQTSNYTVLSCDLKNIELFLKQLNALNLNDDQITKIYIAEVSIAYMAPEFADKVISATSNLPDSHFLCLEQILPAGQYQGFARTMLFHFNKLNSPLKSVETYPTIT... | Pathway: tRNA modification; wybutosine-tRNA(Phe) biosynthesis.
EC: 2.1.1.290
Catalytic Activity: 7-[(3S)-(3-amino-3-methoxycarbonyl)propyl]wyosine(37) in tRNA(Phe) + CO2 + S-adenosyl-L-methionine = 2 H(+) + S-adenosyl-L-homocysteine + wybutosine(37) in tRNA(Phe)
Sequence Length: 725
Sequence Mass (Da): 82658
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A0A0B2V8G3 | MQSIVEYLGPSSGGRCGYCKEEESTKSSIGIWAHRLTVQHYNDILDRGMRRSGRYIYKPIISETCCPQYTIRLDVHKFNLSRTQKRVLRRMNDFLLYDIKPKKSEGEEDLEIRIKHTVSESGTLGNNTGGSVAPSVWSSNSGAVKEDATSGHDEIENNTKPKREPGHKKKIMRRKRAFERMRAKAIDVEEFMKKRAEKEQSRRRTLESFLLPYDEKKFKHRLEIRLVKLLSREFETTVDESFAVFEKYQTIIHKDDHCSRRGYLNFLANSPLFHEEDLSSSPKSVDLGSYHQQYVLDGRIIAVGVIDILPRCLSAKYFYY... | Function: Involved in the post-translational conjugation of arginine to the N-terminal aspartate or glutamate of a protein. This arginylation is required for degradation of the protein via the ubiquitin pathway.
EC: 2.3.2.8
Catalytic Activity: an N-terminal L-alpha-aminoacyl-[protein] + L-arginyl-tRNA(Arg) = H(+) + N-t... |
A0A933YKX7 | MKKKSSENSFLRIGLTGGIGSGKSIVCSQFAQLGRTVLYADEIARELTDTDGAIKTAIRKAFGDAVFLDSGLVNRKALAGIVFGNELRRKKLNQIIHPRVFQAVESAIANLSEARKNPYIVIEAALIFESGMDKQLDYVVVVNADEELRIQRIMARDGISRDEVLARMRSQMDITQKLKLADFVIENDGSEAELLARAKFLDALFSSISTGKR | Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
EC: 2.7.1.24
Subcellular Location: Cytoplasm
Sequence Le... |
A0A1D2YSJ5 | MTRSVVGKLWITIIAIVAVLFLLLSTIVFKYFDNHYYTQQSNSLSALGEEISLIIEKNPNREKAIEIIDDILRAYETNMVIIKKDATGKYPQIEKLFSPEDIKLILENQKNVVRISDVSYKYYLTFDKVDDFLAIAYPLSENGKDIGVIILYQSLERLYEVTNNLKKILLLFVGIASVITTFFSFFLSYKITAPIRQMKKAAVQMARGNFKHKISIRTTDEIGELADSFNKMASQLAETVQALSDEKEKLTNILKSMADGVITVNRRGDIIVTNPPADKLLLWEKELPDSIKEMLETVIKQEVNVKKDINLHGRILSVVM... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Cell membrane
Sequence Length: 574
Sequence Mass (Da): 65021
Location Topology: Multi-pass membrane protein
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A0A952II89 | MSSAKQDFYDILGVSKGASESEIKKAFRKKAKEYHPDTNKSADAEQKFKELGEAYQVLSDPQKRQVYDTYGHDGLRSGGHSTNWDFMDGFPDLSDIFSTFFGGGYGGGGGRRSGPMRGDDLGLELELEFKEAVFGIEKELDINKLDHCSPCNGSGSAPGSGPTVCQQCGGNGQLRQTTQTILGTMAQIVTCPQCQGRGSMILDPCKECHGRGRQEIQKKLTVTIPAGVDNGTRLRVSGEGNAGHLGGPPGDFYVIMRVKPHAQFQRDGYHVLSTQEIPYTTLVLGGNYQVEGLDDVETLKIPAGTPTGHVFTLKGKGVPH... | Cofactor: Binds 2 Zn(2+) ions per monomer.
Function: Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction... |
M1WWM2 | MKLEICTWPDEVLSAKAKPVTEVTPELQELIENMIETMYESDGVGLAAPQVGESIRLICVDQSGPKLRGDLRVLINPEIVECDGQVDSEEGCLSCPELNVTVKRKERVKVNALDREGNEICLETDGFLAIILQHEIDHLDGVTLADRTGRLKQTIYRKKALKWKR | Cofactor: Binds 1 Fe(2+) ion.
Function: Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.
EC: 3.5.1.88
Catalytic ... |
A0A136MVP9 | MQLLSKADEVTTLVQVAKSKNLSVGFVPTMGALHKGHISLVRRAKKENDIVIVSIFVNPTQFNDKKDLEKYPRTLDQDIQALKPTKVDIVFAPDVSEIYPDGDKKGSEIDLGGLDKMMEGAFRPGHFNGVAQVVKRLLDIVNPDRLYMGQKDFQQFTIIQHMIDTLHLPVHMVVCPIMREENGLAMSSRNVRLTSTTRSNAGIIYKTLKSAKSKLKTHTIGNINAEAMKSLSTGPFEPVYFEIVDGNTLQPIHDASKHDYIVACTAVWADGVRLIDNHILKS | Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1.
Function: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
Catalytic Activity: (R)-pantoate + ATP + beta-alanine = (R)-... |
A0A0R2JME3 | MNDSDIYIGLDIGTTSIKVIVAQKIDGQINVIGVGNEKSEGVSRGIIVDIDKAANAIKKTISQAETKSGVKISSVVVGLPADMISIDRCSGMTNIDDSSREIDDQDVVAVADSAISSNIPQEREVIDLVPEEFKIDGFDGIPDPRGMVGSRLEMKGRIITGPKTIIHNVRKAVNKAGFDIDMMVVNAEAEGKTVLNDPEQDFGTIILDLGGGQSTVAVIHNYELKYVDVDHEGGKYITKDISSVLNTSLKEAENIKREYGFADVSQASAENEFSVNVVGQSQPVKISEKLLSEIIEARLDQIFGRLKDKLTEANALDMPG... | 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: 450
Sequence Mass (Da): 49098
Location Topology: Peripheral membrane protein
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A0A0K6H2S9 | MPEAGASANLEGAIKPMAPPDSSGSAPQPPRPLERMRPAYPALARERGEEGTVLLGVRIGTDGRVREVRLLRSSGSLVLDAAASRAAEQWRFQPAQSEGRPVEAWLNVPVPFRLEGAGS | Function: Interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates. It could act to transduce energy from the cytoplasmic membrane to specific energy-requiring processes in the outer membrane, resulting in the rele... |
A0A5N0TE84 | MSSPLRVAVLISGTGSNLKSLLDARDAGRLDLDFVRVISNRANAPGLAHARAANIPWSVIDKASAGDVGQDRVVGDTLAADAPDLVLLSGYMRILGAELVDRFEGRMINQHPSLLPKYKGLHTYQRALDAGDSEHGASVHFVTSELDGGPVIAQVRIGVQADDDATSLAARLRPLEHRLLEEVMALFTQRRVTMDGEGVRVDDRNIDQPLQWTPEGWQA | Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide from N(1)-(5-phospho-D-ribosyl)glycinamide (10-formyl THF route): step 1/1.
Function: Catalyzes the transfer of a formyl group from 10-formyltetrahydrofolate to 5-phospho-ribosyl-glycinamide (GAR), produc... |
A0A843HY14 | MTYKPTPKDVLELMWCPRYLWYMRHIPLPPTERMLAGKRAEAAAVRRLSAMLKAEPKLVYVDVGWARGVIDAVAKRRSPVEVKLGPRREIYRWQLYAEAYLLANALRMAVYEAYIYYIDRDQLDKYAIGPDELKTGEILLKKAKKVVEGPPPISSKTPKCGYCEYRNICEIAQA | Cofactor: Mg(2+) or Mn(2+) required for ssDNA cleavage activity.
Function: CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences ... |
A0A2H0W790 | MQTKVEKLKQSKVKLVVSFEPAEMVHYFDHAFEHLAPSVKIQGFRPGKAPRALVESSLGITKILSHALDDAVNESYQKTLIQEKLNPISAPAIKINKYPGYGATAEEIKNGLEYEAEFTVLPEITLGNYSKIKVEKPTKESVKSDDVAKILDNLRKQKASFTAVDRPAKMGDLAEINFDGSIKHVKIEGMASKHHPVVLGEKSLIPGFEEEVVGMKKGEKKSFKIKFPKNYHAKQFAGKEADFDVELLELKEINLPTVDDTFAADFGHKTAAELEKAIEKNLELEYEQKSENEFEQKILDKILPLVKVDVPDEMIEKEID... | Function: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
EC: 5.2.1.8
Subcellular Location: Cytoplasm
... |
A0A1F8QA82 | MFFACLVLLVVSADQLTKWWISSHLSRGEVLWDAGLLQIVRVYNTGAAFGVFQGHSLFLLAVDIIGIVAMLFILFFLRRRWPFLRSLPVISGVAFVIAGTVGNLIDRIRFGGVTDFIDFKVWPVFNVADSSVTIGCIVLAVYIIFSAGRAKKDA | 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-, ... |
M1WU70 | MREILHMLVVLSLICATSGAILVNLKQATHSQIEQQVLTYVQGPALRSVLNDCDNDPIAERKLINDVMVFPAKQDGKLVGIALEAFAPGYSGDIGVIVGFNIENDVLMGVGITTQTETPGLGTKVTKPSFTRQFRNHGIESMDLAKRGGDIDGVSGATFSSIGTVDAVRKAIEIYQGIKPQIATMWQAS | Function: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane.
EC: 7.-.-.-
Subcellular Location: Cell inner membrane
Sequence Length: 189
Sequence Mass (Da): 20257
Location Topology: Single-pass membrane protein
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A0A932DRR1 | MEEKQMLLLVDEKDNFLGKYAEKEKCHLRQGLHHRAFVVLLENKKGEVLLQKRKHKLWDGYWDLSAISHVLHYSTHDETYEEAAARSLKREMGISAVSLKKVGAFNYFAKYGKNCENEYCAILLGEYDGKINPNKDVVYEYAWVKREEFIKDVLKQREKKYTPWVIYTMTNLFLPKHVAMIMDGNRRWARERKLPVFIGHRYGFNRIEPTVSHAADLGIKYLTFWAFSTENWNREKREVDALMNLFRRMFSGSLVAKLKKNNVRVKTLGDISAFPKDIEKDIQEVVEDTKNNTGITVNFALNYGGREEILRAVQKIIAEK... | Cofactor: Binds 2 magnesium ions per subunit.
Function: Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids.
EC: 2.5.1.-
Sequence Length: 397
Sequence Mass (Da): 46711
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A0A0C2IUH8 | MRLSSITLLALATAVVAQESSSTTTKTKTRDASTKTGKNSKGTTTAAANNATDPVAGGSDSGKGNSTAISTAPGGGKKTATTSQASATSFASGTGTVSVNGGDGLIYFIFAVVVFILALTTIYTRPTPAIDSDVLGNTPQSPATMATTRNITWHTGLTRQERNQARGQKGYTIWFTGLSASGKSTVATALEQHLLHLGVAAYRLDGDNVRFGLNKDLGFSEKDRNENIRRIAEVAKLFADSSTVAITSFISPYRADRQLARELHTQSAQAGNAPLEFIEVYVDIPIDVAEQRDPKGLYKKARAGEIKEFTGISAPYEAPL... | 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: 357
Sequence Mass (Da): 37859
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A0A8R1I1E1 | MMNVVKKTFELRQKNAEHVMTPIDRVTMICETQSITQNFLREVYEKGHSRLPVYDIDVNNICGVLNLKDLMLLMDDEGRGLDSDITAGTMLSLLEKRKKNCPESELSCIRTVPNQNCPEAELFVSELSRIRTVRIRTAPNQNYPV | Function: Metal transporter.
Subcellular Location: Cell membrane
Sequence Length: 145
Sequence Mass (Da): 16629
Location Topology: Multi-pass membrane protein
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A0A1F8Q677 | MLMDAVSLRKILDLEKRRGYGDTAVIGGLDRFLAGWVSQAAGLISKRSLLARFRKLFDVSYAAMPGEKRRDWLESAISLLDEIEAKNGNVPGQAVLPAPGKPPRKRVNRPVPPAGDSLDAPVTAVRGISTVLATKFGRLGVKTVRDLLYFFPRRHLDYSHLKFISQLTEGEEQTIVANVWQARETRPGGRRSAEAIVGDETGNIRAIWFNQPYLVKTLATNSRVMLSGRVSLFRGQHVFQSPDWELVEGQDLVHTARLVPVYPLTQGLRPRQVRRLMKDFIDTWAGRLADFLPGDLRQRLDLLELPAAIRQAHYPENETA... | Function: Critical role in recombination and DNA repair. Helps process Holliday junction intermediates to mature products by catalyzing branch migration. Has a DNA unwinding activity characteristic of a DNA helicase with a 3'- to 5'- polarity. Unwinds branched duplex DNA (Y-DNA).
EC: 3.6.4.12
Catalytic Activity: ATP + ... |
A0A2G6EKQ7 | MSEFVISTRYAKALLDNSEKNNSFGKVNEDVRFIFNTLDNSKELRTFLSNPIIKSSVKLNSLKEIFSSHIGKETMDFLRFLIEKERQSALYGICKRFIDLSNGKLNKAEIEITSAIELSEEQKNTMENKLENMINKKLIASYKIDSNIIGGFKAKYNDTVIDASIKYQLKKLKNKLFKEDYLKN | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
M1WM35 | MLKFLFGSKNDRYLKKLQPVVDAINSFESKMEALSDEDFPATIAMWRGQVESGVKTLDDLLPECFALVREAGRRAFDPPMRHFDAQLIGGYVLHQGKIAEMKTGEGKTLVATLPVVLNALSGKGVHVITVNDYLASRDAEWMNQLYSFLGLSVGVIVHGLSDQERQQAYGADITYGTNNEFGFDYLRDNMKFYKEQLVQRPLNFAIVDEVDSILIDEARTPLIISGPGEKSSGLYRRVDAIIPSLTKSSPMDPEDKDAVPDGDFVLDEKTKSVTLSDEGVEKVEAMLGVDNLFDPQHISLQHHVLQALKAHHCFQNDVEY... | Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide c... |
W5P9V6 | NHIRITTGKRKQMQGENLTSWSFFFLEGFSRYPKLEIVLFIFSLLMYLITLLGNSTLILITVVDARLQTPMYLFLGNLSFMDICYTSASIPTLLVNLLSSKKTIIFSGCAVQMYLSLAMGSTECVLLAVMAYDRYVAICRPLRYPIIMNRQVCVQMATISWVTGSLTALLETSFALRIPRCGNLIDHFTCEILAVLKLACTRSLLMDTVMLVISVLLLPVPMLLIFCIFYVYI | Function: Putative odorant or sperm cell receptor.
Subcellular Location: Cell membrane
Sequence Length: 233
Sequence Mass (Da): 26349
Location Topology: Multi-pass membrane protein
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A0A1W9UDJ0 | MPKRLILITMSGQDRPGVFAAVTDLIAQTDGARIRDIEMTVTHPQMVLTLLLDLSTGDSSEKPLIKDLLFAAKEMELHLDFSVVREGDYRRKSAHNRYVVTILGSHVDAAALAQVSKVLVKCHANIERISKLTQGELRCVELLIGSDGQLDIRLLKRQLLQLGGKNVDVAVQKESLYRRAKRLVVMDMDSTLIQVEVIDELARLAGVGEQVSEITERAMNGELDFKQSLAARVALLKGLRQEALMDIYQNIPFTNGARNMVRILRRLGFRTAVISGGFQFFTDRLKEDLGLDYAYANQLEIVDGVVTGRTSGVVVDGERK... | Pathway: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 3/3.
EC: 3.1.3.3
Catalytic Activity: H2O + O-phospho-D-serine = D-serine + phosphate
Sequence Length: 398
Sequence Mass (Da): 43932
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A0A367ZEE7 | MKRILGIDYGDKRIGIAISDPMQIIATALDYIPNNEQAVDNILELTKKYDVDMIVVGLPLNLKGERGVKSAQVNDFIQNLKQKTDLKILEWDERFTTTIARKTIIEMGLKKKQRQDKSKIDSLAAAILLQSYLDSNFKSKNGK | Function: Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
EC: 3.1.-.-
Subcellular Location: Cytoplasm
Sequence Length: 143
Sequence Mass (Da): 16197
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A0A3N5L2Z5 | MLRKNLGILVVLGLVVLFLYYASYFYDPTHDKKNAYINYTSDAAGMEGMVVSASSYASKVGIDILKKGGNAIDASVAVGFALAVTYPQAGNIGGGGFMVLRVHDSIITSIDYREKAPSASTRNMYLDSSGKFDPDLSQFGHLSSGVPGSVAGMLYALEKYGTMSRDEVMQPAIDLAENGFEIEPKFAESLNANFDDFSEFPSTKKIFTKKNSLNFFAGEKFVQKDLASTLRRIRDDGRDGFYKGVTADMIENEMVSNDGIITKEDLANYQPVERNVISTNYKGYDVYSMAPPSSGGIALINLLNMIEHDPVPDTNNSIDM... | PTM: Cleaved by autocatalysis into a large and a small subunit.
Pathway: Sulfur metabolism; glutathione metabolism.
EC: 2.3.2.2
Catalytic Activity: an S-substituted glutathione + H2O = an S-substituted L-cysteinylglycine + L-glutamate
Sequence Length: 582
Sequence Mass (Da): 64344
|
B8DMM6 | MIREVLQYPDPRLAVECEDITEITDEIRQLAADMAETMYRQDGIGLAAPQVGEHCRLIVVDVSGPEKREALMTFVNPRLELTGDKVDSEEGCLSVPGGYRATVTRSDTVRLTARDLDGNEVCMDADGLLAVCLQHEVDHLKGTLFIDHISRLKRTLYDSRVKKMQKNAPRPMPTAAARTRTGAR | Cofactor: Binds 1 Fe(2+) ion.
Function: Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.
EC: 3.5.1.88
Catalytic ... |
A0A7X4CA81 | MHRSLSWLLGASLCLWLLPAGANPAVPLEEATQPLEQPKGTETIVLAGGCFWCLEHDLEKLEGVEEAVSGYSGGHVASPSYHQVSSGNTGHREVVEVTFDSRVLPLEDLLQVFWRNIDPLDDGGQFCNRGEQYTSAIFVATPQQRQVAEASLEAARVQLADQPIVTPVLAARPFYPAEDYHQNYAKTNSLSYRYYRWRCGRDRRLKEVWGDTRPGSGEA | Function: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.
EC: 1.8.4.11
Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionine = [thioredoxin]-dithiol + L-methionin... |
A0A914HEL2 | MEFKCDVCDVLVHSQKHWDDHLKGKGHQQNTELRTKTKSSELAGAMDQFGEVDRVIMDRSGNGAFAIVEFKEEDAAQNLLSSFERLRIGKCNVRIHPRRVDFEGAGTDHHVPEHFGELKSVEVLNCLDENGTSGLENQLNSMIATFSMATTTVNDRAEFAQQLRHFVQPYFASPLQIRVFGSSSTGLGFVNSDLDLNLVFDEDLSESSCGFEDSPSVSSTTSEEMMVEVDKQLTPETLKQNPMNRDTFIRLTKIDCVRLLNRLMNAFRKEKGLITAHVPVPDARTPVVRFLIRHLSTRIPCELSVQNLLGECKANLIRDL... | Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Membrane
Sequence Length: 888
Sequence Mass (Da): 102272
Location Topology: Multi-pass membrane protein
|
A0A1G1LJA4 | MTGKPDAAEALNQVVVTKHNPCQRIRKKNVAALAQLFLKKLGYSKILVSIVFVSDHEMKRLNQRYLNHPWSTDVLAFPLDDPRLAIDTVSRRRRMGRTVFLGEIFISPRRARVQAKHLKVSMSEELARYVCHGILHLSGYSDHTRYGEQRMRRAEDQLLRLVPANTRRIV | 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: 170
Sequence Mass (Da): 19670
|
A0A2X2J0C8 | MSSANIVVLGSSNTDMVVKAAHLPAPGETILGGQFFMVPGGKGANQAVAAARSRSAVAFIAKVGTDIFGQQAIAHYQQEGILVDMIFRDEENPSGIALISVDAKGENCILVAPGANATLTPKELQSVKNTIISGNVLLMQLEIPIETIEQAIDIAVQHDTKIILNTAPAQALTDQLLQQVDILILNTSETQFYTGMTIENWEEAALAADYLYQKCPGIIIITLGAKGSLLKEKDNYIQIPAEEVNAVDSTGAGDTFCGVLAACVAKEMPIVDAVKLASKAAAISVTRMGAQTSIPFWQEYSIL | Cofactor: Requires a divalent cation, most likely magnesium in vivo, as an electrophilic catalyst to aid phosphoryl group transfer. It is the chelate of the metal and the nucleotide that is the actual substrate.
Pathway: Carbohydrate metabolism; D-ribose degradation; D-ribose 5-phosphate from beta-D-ribopyranose: step ... |
A0A2Z2NNI7 | MSSLIDNLETDHEGYLRRHTDWTPELANELAGADGIQLTEAHWEVLNFLQEYYENYEIAPAIRILTKQIGKRYGREKGNSKYLYELFPRGPAKQACRYAGMPKPTGCV | Function: Part of a sulfur-relay system.
EC: 2.8.1.-
Subcellular Location: Cytoplasm
Sequence Length: 108
Sequence Mass (Da): 12422
|
A0A8R1IE80 | MVETDGAEKRTSWKQNILNFVWGAAEAEEEPGQITESFITHVRAERPFKLAASFAFFILVFVIGMPMWHLTTSSYRAPFATFSANRSISVPIRVLFVTTTTSDEMQADVTSLMEELKENVTSKEVVKPLDFQWTTQFLGVR | Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 141
Sequence Mass (Da): 16015
Location Topology: Multi-pass membrane protein
|
A0A935W785 | MENLREQFLTNRNRLFNDEELLKNSYKFCVRYSLLVEEYILRTIKPKSVDCVMVAAGGFSRRELSPFSDIDLMFIIPKTETHEQNIREAVTKLWDTGIEVSHTVRTFSDIQKFMNEDLHAFTQFFETRFLIGSKLLYDDWNKKVFEVIEKTDKKQLIFDLFEDVVQRYQKYGSSPKVLEPNVKFTGGGLRDIHCVEWMYSIKNNVLLSNQDEITHTEIFLKTILENGTINRKAYKRLFESYQTILNARNHLHLVEGRKNDRLEFEQQEQIAERLGYKKNDWKEFMYSYFKASTILNRFSKTMMKRYKQAYATTISDFLSI... | Function: Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher ... |
A0A959RXH9 | AEMPGLYAEKDYDLSGTIVGIVDKNKIVDGSKIEKGDVLIGFESNGLHTNGYSLARKVLFEKYTLDENIEELNSNLKTELLKVHKSYLNVIQNLISKSEVKAFSHITGGGIIGNTKRVVPNELKIKIDWNSWKVPEVFNLIQKTGEIEDDEMRMVFNMGIGLIAIVDKNDVSNVEEICKKINENPIIIGEIE | 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... |
B6YRN0 | MAKQLNEKNSVFIFDTTLRDGEQVPGCQLNTIEKIQVAQSLESLGVDIIEAGFPISSPGDFNSVIEISKSVTWTIICALTRAIEKDIDIAAESLQYAKRKRIHTGIGTSPYHIKYKFNSTQDEILERAVASVKYAKKYVEDIEFYCEDAGRTDNVYLARIVEAVIKAGAKVVNIPDTTGYCLPEEYGAKIKFLMDNVKGIQNVILSTHCHNDLGMATANTISGIINGARQVEVTINGIGERAGNTSLEEVVMIIKSHKELNIGTNINTKHIYPISRMISSLMNMPVQPNKAIVGRNAFAHSSGIHQDGILKNRENYEIID... | Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 1/4.
Function: Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-ketoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate).
EC: 2.3.3.13
Catalytic A... |
A0A2Z2NQU8 | MKRRSFLKSSLMLSGGIFLPPAVLALVGCSGTAREPELAGFEGLVMGTGYSVRYGGESIENLDQEVLAVLQNVDTHMSTWRPESELSILNRSVDGDWQVVSSATARVIAHAMTLSEQTDGAFDTTVGPLVDLWGFGAGAAPSADGSRGHRPAKQAISQTLAQIGHEYLEIDLGANAIRKRKPEIQLDLSGIAKGHAVDRVVAALDARGLDSYLVEVGGELAAKGRKPDGSAWKVAIEKPEVGRRDVFRVLELEDKAIATSGDYRNFFDDGGQRYSHAIDPRTGQPVNNGLASVSVVADSAMAADALSTSLMIMGADKAMA... | Cofactor: Magnesium. Can also use manganese.
Function: Flavin transferase that catalyzes the transfer of the FMN moiety of FAD and its covalent binding to the hydroxyl group of a threonine residue in a target flavoprotein.
EC: 2.7.1.180
Catalytic Activity: FAD + L-threonyl-[protein] = AMP + FMN-L-threonyl-[protein] + H... |
A0A061Q6W4 | MPFEPLITAVIETTLNTLIKDDPELGRRLSRLKGQVIQIHLKEINKTLTFIFSQQIDVLGNYEGQPDCYLSLNLSVLPELRDQANITRLIKQDKLELEGDIQLAQKFSQLMVDCKPDIEEWLSRVTGDVVAHTFVQGTKNVGGFFASQAEKHQRHLAQVVTEEWKLAPAPLEIAHFCDQVDDVRSQASRVEARLNALLNKFDSDKPALETHDASRNKALIHIIKVQLEYGLDELLPDHQLTKAPLLMRKSLFWMKNKHPEKPLGERLRLALQELGPVWIKFGQMMSTRRDLFPPHIADPLALLQDQVAPFDGQLAKEQME... | Pathway: Cofactor biosynthesis; ubiquinone biosynthesis [regulation].
Function: Is probably a protein kinase regulator of UbiI activity which is involved in aerobic coenzyme Q (ubiquinone) biosynthesis.
Subcellular Location: Cytoplasm
Sequence Length: 717
Sequence Mass (Da): 82027
|
G0EF11 | MSAPCIEYDAGVIRELKRVARNDKALELLLSSLCEPPRRLYVRVNTMRADPGEVLDELREQGLRAYRDEHLEEAIWFPVEGPFRVPRVDKRVVVDKRTAESVLLGAHVYAPGVIDMEGVSKGDEVNIVAENGVVVAYGVAEMSWDEVREKRRGLAVRVVVSRFRAPSTRELSVWKRGLIYEQSLPAMWASRLLEPQPGEIVVDMCAAPGGKTGHLVELTRGKARIVAIDHSRSKIRRMVEELGRLGHLDLVHIEQADSRYLDLDYPMLRADRVLLDPPCTALGVIPKVYDRKTWRDVRNAAEYQWQFVKVAAKILKPGGR... | Function: S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the C5 position of cytosine 72 in several tRNAs.
EC: 2.1.1.-
Catalytic Activity: cytidine(72) in tRNA + S-adenosyl-L-methionine = 5-methylcytidine(72) in tRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Length: 386
Sequence Mass ... |
A0A2L2BP47 | MDFSASTLNPADEAVLAAVIGDGTTPVVHSRPFKAMGANASITLVGGHPHLVDDAIGLAAELEGLWTRFSPDSDISLLNWSEGTPIEVDPRTATLVDYMQRAWKDTGGAFDPTLLPQLLLEGYTHSVVDATRGTTLPDSARAPGQLGDIIIEGNIITVPKGTTLDAGGIGKGFAADLIVDFCRSAGAMGAMVELGGDLRVDGFSPRGRGWRIGVENPLNLDSHVSVVEIESGGLATSSQLKRRFHNAQGKETHHLIDSHSGESLESDSLSVTVLAPTAWQAEVMTKVGFQKSPADFLHVSRRKGLRVGVFTSDGSWTRSS... | Cofactor: Magnesium. Can also use manganese.
EC: 2.7.1.180
Catalytic Activity: FAD + L-threonyl-[protein] = AMP + FMN-L-threonyl-[protein] + H(+)
Sequence Length: 327
Sequence Mass (Da): 34768
|
A0A975FW99 | MTLRPALPEDTPALAALHAASFVAPWGAQEIADLLAGPGGFGLVIEAANGSPAGFILCRVVVGEAEVLTLAVAPETRGQGLGRVLMQAALGLARTAGAETMFLEVAADNAPALALYRGLGFERIGLRPGYYAHGGRGPIDALVYRLSLNAPT | Function: Acetylates the N-terminal alanine of ribosomal protein bS18.
Catalytic Activity: acetyl-CoA + N-terminal L-alanyl-[ribosomal protein bS18] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-alanyl-[ribosomal protein bS18]
EC: 2.3.1.266
Subcellular Location: Cytoplasm
Sequence Length: 152
Sequence Mass (Da): 15561
|
A0A1G1LJM8 | MNLLIKQVHIIDPKNEVDGVFDLSIENSVVREINKEISSQVGEVIDAKGLYLFPGLIDLHVHFREPGYEQKETIQSGAKAALKGGFVAAVTMPNTNPPCDHQSVIDNMIRKANEVPFYIYPAATLTKNRAGGELSEMADLRKAGARAVTDDGDWISDSLLMRRAMEYASMLNLLVVSHAEDKRLTAMGAMNEGIMSTQLGLKGIPNASEDVAVSRDILLAELTGVRLHLTHISTRGAVEQIRLAKKRKISVTADVTPHHLTLTDEALAGYDTNFKMMPPLRTEADRKAVVDGLIDGTIDAIATDHAPHTEEEKMAEFQDA... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3.
Function: Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate.
EC: 3.5.2.3
Catalytic Activity: (S)-dihydroorotate + H2O = H(+) + N-car... |
A0A959M083 | MPRFFMIDGMSLVFRAYHAMYRTGLTNNSGEPTGAVFGFANILTSLLDKYDPKHILVVYDTSAPTFRNDMFEEYKANRAEFPEDLGPQLLKIKQMMNLFGIPQLELDGYEADDLIATLADKASEQEIDSYCLTSDKDYYQLVTDHIKILKPATKGGALEVIDYPEVREKFGVRPDQVIDVQALIGDSVDNIPGVKGIGIKTAYPLIEQFDSLEGLYENIDQVKSKSVKAKLIEHKEMAFLSKQLVTLKKDCPIEFKFDDYEFKNTKFEELDQFFAHEGFRTLRGKWFERSGKASLLNSTEFDKESDLENIESVDNDYKMI... | Function: In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity.
EC: 2.7.7.7
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Length: 940
Sequence Mass (Da): 106787
|
A0A952P8S6 | MNLILLAPPGGGKGTQSSLIYNDFGIHRISTGDLLRKHKEQRTKIGKEARKYMDAGELVPDYILTEILKTELIKEKYKSGFLLDGYPRTLAQAIELESLTENINSKIDLVIILDVPAEELLNRLGARRICKICERVYNLKFHPPDNPNKCNEPCGGKLYQRDDDKPETIINRLKIYESKTRELLEYYSKMPVTQTLDGTGKVQRVYDRVKDLIEKVRQDD | Pathway: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from ADP: step 1/1.
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: AMP + ATP = 2 ADP
EC... |
A0A3N5JQN6 | MISNPLSVKILKTRSDLEKFTSHEIIEVIRKSVKEKSRCSIALSGGETPKNVYRQMGLDAAMSHADWSRVHIFFCDERSVPPAHPDSNYGMADRVWFSRSAFPHENIHRIKGEIEPHSAAREYELEIKKYFGSNPVVFDFILLGVGEDGHTASLFPGSEAAAEKQALVSAVPVQSLNSWRVTMTFPVLNNARDIMILAAGSRKANVIQRILDASAPDLKLPAAGIRPGKGTVQWMIDEEAGSLLKDHSGILIKRISLTE | Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 2/3.
Function: Hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate.
EC: 3.1.1.31
Catalytic Activity: 6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate + H(+)
Sequen... |
A0A3A0B634 | MRNFVVAIDGPSGTGKSTTARILADKLKVLYIDSGAMYRAITYLVLKKKINPTDSSKIIELTKSADLKLEGENVYINGEDVTKQIRSLEVTNRVSAISKIREVREILVSKQREFANSQSVIMDGRDIGTVVFPNADFKFYFTCDIKTRAARRQQDFRDHGLKIPLDKIKLELKKRDDIDANRKESPLRKAKESIEVDTTNMIIEEQVDCLYKKIISQLDN | Catalytic Activity: ATP + CMP = ADP + CDP
EC: 2.7.4.25
Subcellular Location: Cytoplasm
Sequence Length: 220
Sequence Mass (Da): 25060
|
A3D7Q0 | MNTPSVDSQFAAQLTTQLTLGLPVELVALTPTDVPKMAQLESMAHSHPISEGNLADCFGHLYRVLGLKLSAGSDANTDAVSDFASDPDSVDGLLGFAIVQQIVDEVTLLDICLLPSQQGKGYGKLLLNAVVASAKASAAVVLMLEVRESNLAARALYQKAGFIESGRRKGYYPIAGGKEDAILMDLAITQE | Function: Acetylates the N-terminal alanine of ribosomal protein bS18.
Catalytic Activity: acetyl-CoA + N-terminal L-alanyl-[ribosomal protein bS18] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-alanyl-[ribosomal protein bS18]
EC: 2.3.1.266
Subcellular Location: Cytoplasm
Sequence Length: 191
Sequence Mass (Da): 20162
|
A0A959P0Z4 | MKIIRDIKSEFEIEQSAVTIGTFDGLHVGHNKIIESLKKKAKDLNIYSVVITFYPHPRVVLNQGYDIKLLTPLEEKIKLFEKLGI | 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: 85
Sequence Mass (Da): 9767
|
A0A183VD04 | LCNVNVNAGGDDGRESRGSSQQSDRRYWSRLLNVFIVYWSQTIFAAAFGLALLYMTVLGFDGIAIGYGKSQGLSATWLGILRSIGSACGIAGVLTYTTLETNIGVRRTGLIGLLTQQFPLYVCIASIWLPGSPFDPFNYFEELTLPMWWKQFKDAFRFTPTNRTETVTIDWSTWTSNGHSIISVFALLMGIAFARFGRLYMADLSITQIMQEMVPERQRGTVFGVQDSACQFFSVLKDLMVIILPDPRTFGVLIIVSVLFVIFGFIFYICYLIKTRHHSTGYKRSSNAIVESSPLMQSGKDDEISAEQRENKTNT | Function: May be involved in iron transport and iron homeostasis.
Subcellular Location: Membrane
Sequence Length: 315
Sequence Mass (Da): 35321
Location Topology: Multi-pass membrane protein
|
A0A078KBJ8 | MIINLENCFKRIKNRFQLIYISCNRSRELSKGSSYSKLPNENNKPIIVALKEISRGYIHGSIPKNYKFNLKSEFGQNIKVQKLKLLEIQFQHLMSFNLIK | Function: Promotes RNA polymerase assembly. Latches the N- and C-terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits.
EC: 2.7.7.6
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Length: 100
Sequence Mass (Da): 11790
|
A0A7W9BRN4 | MTETPQDLLAAYADLVRDEATRQNLVSAASLDAFQTRHIDDSAQLLDLAPPGGRWLDIGSGAGLPGIVLAILGAEVRLVESRRLRAEFLAHCIETLGLKDRATLHAGRIETMETERFDRITARAYAPLPKLLDSAVRFSDRNTVWILPKGRTASSELDTVRGTWQGEFRVVPSRTDADAAIVVATNVRQNVRRKEPR | Function: Specifically methylates the N7 position of guanine in position 527 of 16S rRNA.
Catalytic Activity: guanosine(527) in 16S rRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(527) in 16S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.170
Subcellular Location: Cytoplasm
Sequence Length: 197
Sequence Mass (Da): 21... |
A0A1J4VTK6 | MSKSLHTLGEFGLIDEIKKMTRTDASVLLGIGDDAAVLAFAAGGKILFTTDMLIEGRHFCRSQASGFEIGRKAMAVNVSDIAAMGGMPTHAVVSVGLPKDLNVKYVKRLYAGIQDVARRFRVNIVGGDTNASDKLVIAIALLGTCGKHPPVTRSGAQAGDVIFVSGDLGGSYASKKHLNFTPRIAEAQYLVKNYKINSMMDLSDGLSSDIYRLTKASHVGAAILQEAIPVSAKAKHLDAALSEGEDFELLFTLSSKEAARLTLADKPKILATFCPIGKVMPQKYGVQLIKSDGQRKVLFEKGHDHFRG | Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine diphosphate from thiamine phosphate: step 1/1.
Function: Catalyzes the ATP-dependent phosphorylation of thiamine-monophosphate (TMP) to form thiamine-pyrophosphate (TPP), the active form of vitamin B1.
EC: 2.7.4.16
Catalytic Activity: ATP + thi... |
A0A932JGV4 | SKDTESIDGTELPVYRGHLVNGPEPDPESRRPDPVRMLIGFLAAGEREVPCAWMTRWFRDVIFAFRIGF | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 1/7.
EC: 2.5.1.54
Catalytic Activity: D-erythrose 4-phosphate + H2O + phosphoenolpyruvate = 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate + phosphate
Sequence Length: 69
Sequenc... |
A0A395HB69 | MHGPLSRGLWCYRAALRAPVLHQVNRSFALVSCLRSGQPAFSPTTSLKGPASIPSHLQGETPVAESQDTSSTDGLFDHLSKLSDDKVRSELGEGPEDRDSTLFLRLLYNQLSTSSAEEKAIARINLSCSAISRQHPGYTKNDLYTAFMECASSGYSVSDDLGFAVVSALLAPQPAGQVSNSDKEIALRVLEYLSLRGTNVVNMKVFNMIYQAAANAPSALSRVSRLIDTLDLPFDPLQSRSLMASLFQHGDYNGFWKLWRKLPLNGSPRTAADYEMLFRLHADLGNELRARDCISTWMPMMSREQPPIPLRGKLLVDIKR... | Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Membrane
Sequence Length: 856
Sequence Mass (Da): 95269
Location Topology: Multi-pass membrane protein
|
A0A2H0W5I6 | MIKKLEFKTRTYEVDFGGKKLTLETGKFAGQANGSITAHYEDTIVLATVCLNPEPKEGMDYFPLMVEFEERFYAAGKISGSRFIKREGRPSDRAILAGRKIDRPIRPLFPKSYRNDVQIMVTALSYDGSIDLATIGTVAASAALMQTNAPFRGPIAAINVGLIDGQFVINMTEDEIEKSALNLNFAANTERIMMIETEANEVPEEKIFEAMEYGHKAMQAAIEIQHKIAEDHQRQVAEAAEEKIVGVHAEVYNLVADKIKDALAEMDEAARKLKLKAFEEEALSQLEGNYKQVEISGAFTKVVEKEIRSLILVKGIRPDN... | Function: Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
Catalytic Activity: phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate + RNA(n)
EC: 2.7.7.8
Subcellular Location: Cytoplasm
Sequence Length: 714
Sequence Mass (Da): 78... |
A0A2H0YBQ4 | MEKIVVIDFGSQYSHLIASKLRKLKVFSEIKSPELRPEELKEVKGIIFSGSPLRIVEPTAPGIDKRIFKLKIPILGICYGHQLLGREIGGKVRESKIKEFGKTVLKTQDKSGILEGLKDDELVWMSHNDEVSKLPRGFKISAQTENCQIAVMENPKKKFFGVQFHPEVSHTEGGLKIFDNFLKICRVKRDWEIPGLIEEIIKDIREKVGKRKVFLLASGGVDSTVTLAILIKALGTERVFAFYVDSGLGRKNEAEEIKKLFRKSGFKNIGLIKAENRFLKNLEKISDPEEKREIIGRLFIELWKEKIKNFAPEDWLLAQG... | Pathway: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln route): step 1/1.
Function: Catalyzes the synthesis of GMP from XMP.
EC: 6.3.5.2
Sequence Length: 613
Sequence Mass (Da): 70010
|
G4E427 | MLSLHTLVIVLFSLLALGSATLMLTQTHPMRVALALIATMLSLAALYAALYMHVVAIFQVLIYVGAVMVFMVYAIMLLDRQDRVLRLPLSKMKWPGILGFVAVLLVLSVHLQPSLHEGLGTLSSEEHPFALAQFAQVFLNDYWLYFELASVLLVVAVVAVVAVLKAPAVSHDG | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy i... |
A0A0H5BX30 | MTIKIHKLYAEEILKFLPHRFPFLLIDRVLNFTKGRYLCAIKNVTFNEPFFQGHFPKKPIFPGVLILEAMAQASGILALKSEIKLLPEEYYYLAAINEAQFKQTVQPGDQIIFEIKFVKKRKKITKFNGIAKVDGKITCQASLMCTKQIKK | Function: Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O
EC: 4.2.1.59
Subcellular Location: Cytoplasm
Sequence Length:... |
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