ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
|---|---|---|
D3QZA8 | MLKMNPVAKAILQPTICLFVVCLITTFLLAVTNQATEPVIAANTKATAERIYKEMLPEVEEFTAQTTELNGKKYEVQVGKAGGKTIGYVFNTQTNGYGGPVVVLTAIKADGSIAGAQILEMQETAGLGMNASKPEFIDQYKGKKSKLHVVKDGASKDDEIQAISAATITSKAVTKSVNTAMDLFALVNGKEAK | 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: 193
Sequence Mass (Da): 20532
Location Topology: Single-pass membrane protein
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G8NZT5 | MKKLRADLGRRAATFAMMALASLLMAGCHHRTTVAYQPPPPPVNSHRSTTSTASTEPPIDLKKEASSAPKGFFDDTSGRPVFTEEGTASWYGTIYHHHAAADGTIFDQNEMTAAHRTLPMGSTVRVTNLATGQQVLVRITDRGPFAPGRVLDLSMGAAKAVGIYRAGVAKVKVEAFAHASPDPEGRWCVQTGAFKTEGDALDLKAGLLHRYNTAKVTEFSGPTGFWVRIDPVQHSKTQAAEIADWIGTPDPAALPYLVRLD | Function: Lytic transglycosylase with a strong preference for naked glycan strands that lack stem peptides.
EC: 4.2.2.-
Subcellular Location: Cell membrane
Sequence Length: 261
Sequence Mass (Da): 28094
Location Topology: Lipid-anchor
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A0A1Y4BBW2 | MTERLCLVHYHEIGLKGKNRSTFENQLVTNLHRALQAFPVSSIARISGHIAVETSDRRASEELAAAIRCVPGVARVSLAYKCGLDEGEYCAAAIRALGEAGDFATFKVHARRSSTTYELHSLEMNRLVGAALCEAFPDKKVDVHTPDVTVIVHVVQGSVFVYAASAPGVGGLPVGTAGKVVTLLSSGFDSPVSTWMVGRRGATCVPVHFSGRPMTADTSEWLCQDIVEALAPSGVVGRLYVVPFGERQREISLAVPQGLRIIMYRRVMLQVAERIAQIEGAKALVTGESLGQVASQTLDNIAAVNEAVTMPVLRPLIGSD... | Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
Function: Catalyzes the ATP-dependent transfer of a sulfur to tRNA to produce 4-thiouridine in position 8 of tRNAs, which functions as a near-UV photosensor. Also catalyzes the transfer of sulfur to the sulfur carrier protein ThiS, forming ThiS-thiocarb... |
A0A2Z4FR42 | MAKKLIALVERKFSDAVLDVHSRLGQDTVTVEAEFLPAIIQYLRDDESAKMDFLRLVTGVDYLTRTPRFDVVYVLYSTTHKHMLTVRVPLPADNPKVGSIHELYQCAGWFEREVWDFYGIDFEGHPDMRRVLNYEEFEGHPLRKDYDKQRAQPRIDLLDRERDSVEEFYEYSKKHPAAGSRES | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ... |
A0A2M7D9W6 | MNREVFKLNIGGKELKVEFRNLAEQASGDVLVQYGETMVLATAVMSNYEREEIDFFPLTVDYEERYYAAGRILGSRYIRRESRPSDEAILTSRFIDRAIRPRFPKHLKREVQVVVTCLSWDRENDPDIIGCLAASLALSVSNIPWSGPIAVLRVGKNGEDFILNPTYQEREKNDLDLAIAGLESRLAKIAAGEGDDKILINMIEMEGNEVEEDTVLKAMDFAKPILEKLCDFQEEIVMKVGKEKIKIEESPKDLELEKEIKDFLGDRLEKTLYQENKASRMGKENKFSSSSSFPRSGNSMDEVNALKEELIYYIQGKYPA... | 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: 737
Sequence Mass (Da): 82... |
A0A932WGD2 | MIVHAVIPAAGQGKRLGGETKKQFLELCGLPILIHTLIPFQSASIINEITCVVSKEDCSFIEGLVSSHRLDKVKRILHGGERRQDSVWAAVSELCERSDPNDLILVHDGVRPLVTTELIERVAAAAAEVGGAVAARPVTDSLKRVSSGRIISQSLPRENVWAMQTPQAFRLSLLREAYQKAETDRFEATDEAMLVERLGHPIRCVEGSAENIKITTPPDLRLAEILLHARGEERRR | Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 2/6.
Function: Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
EC: 2.7.7.60
Catalytic Ac... |
A0A972RGU3 | MDAAVRRRFTAPLLEWYHSLGRDLPWRRTDDPYCIWLSEIMLQQTQVVTALPYYHRFLETFPTIKALASADLEAVLKLWQGLGYYARARHLHRAAQILVSQFSAKMPESFESVIALPGIGRSTAGAILTIAHGKCHPILDGNVRRVLCRFFAIERDPREKSVDAWLWHCSEMLMPKHNASHYLQAIMDLGATVCVPKQPSCTRCPVEKSCAARKKGLETLLPIRAPSKKVPHYDYFAGVLCVDNAVLIRRRPLKGLLAGLWEFPGERVAENSKQGSIVLAYERFFREHLGLDTCECKPYMTIQHVFTHFKMTLHVFLHHS... | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Adenine glycosylase active on G-A mispairs.
EC: 3.2.2.31
Catalytic Activity: Hydrolyzes free adenine bases from 7,8-dihydro-8-oxoguanine:adenine mismatched double-stranded DNA, leaving an apurinic site.
Sequence Length: 364
Sequence Mass (Da): 41807
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B5HLB4 | MERCSIRQDDHVTDADAVSPDPASMRKQYRAEGLAESDLAATPVEQFARWFRQAATEGRLFEPNAMVVSTADAEGRPSSRTVLLKHFDEQGFVFYTNYGSRKARDLAENPYVSLLFPWHPMARQVIVTGLARRTGRDETAAYFRTRPHGSQLGAWASGQSSVIAGRDGLDAAYAELAARHPEGEQVPVPPHWGGFRVAPQAVEFWQGRENRLHDRLRYVAEADGNWRVERLSP | Cofactor: Binds 1 FMN per subunit.
Pathway: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate: step 1/1.
Function: Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).
EC: 1.4.3.5
Ca... |
A0A850M1F6 | MLKLYNDLTGKKEEFIPLEKNKVKMYVCGPTVYDYSHVGHARSYVFFDIMYRYLKFRGFDVIYIQNLTDIDDKIIKRAREENLTIFELADKYTDLYFRDMKKLRALSADYFPRATQHIPDMIEAIKILIQKGYAYESNGNVYFAVDSFQDYGKLSRKPFEELIDSEDSPDKRNPKDFALWKRKKEDEPFWESPWGLGRPGWHIECSIMSTKYLGSTLDIHGGGQDLVFPHHENEIAQTEAYTGKKFVKYWIHNGFLTVNKEKMSKSLKNFFTIQEVLEKRSPENLRCFLISTHYRKPMEFCEENLDHAQRVLERFYVALE... | Cofactor: Binds 1 zinc ion per subunit.
Catalytic Activity: ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-cysteinyl-tRNA(Cys)
EC: 6.1.1.16
Subcellular Location: Cytoplasm
Sequence Length: 466
Sequence Mass (Da): 54916
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A0A850LVM0 | MKDTDIGQKILQFLNLHQGVTFSSRVIFKELNLPRSKYRSMRIILKDLANKRMIEKVGKRTYRIKKPPHVTIGTIAMTKYGYGFVANHTDKREIFIPRGMTGTAIDGDTVKVEVYASRRGKSLEGEVVEVLERAKNKIIGTYMEAKSFKYVIPDDKKFTRDLYIIKGKNKGAKPGEKVIAEFVKWESEYMNPEGIVKEVLGDPFKHGLDMTLIERAFELPRDFPAKVKREIKSSDFSTPDSEFKNRIELRNKLIFTIDPEDAKDFDDAVSLEMLENGNFLLSVHIADVYYYVRENTAIDKEAFKRGTSVYFPDRCIPMLP... | Catalytic Activity: Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.
EC: 3.1.13.1
Subcellular Location: Cytoplasm
Sequence Length: 705
Sequence Mass (Da): 81617
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A0A4U0X1X7 | MSGQLKSLGLDAFYANLFGICRAASLIDIPSATKNHTNKSTYLPSGVPYAPAGMATRRTVLQEARSFQKEDTSAPRKSDIAPAVPSSVIFKLLGFTFGMITLPIGSYFLTLNTIYGGNTTFAGATAAIVANIVLIGYVIVAMKEDQSDRLEAEEKARKTE | Function: Required for the assembly of the V0 complex of the vacuolar ATPase (V-ATPase) in the endoplasmic reticulum.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 160
Sequence Mass (Da): 17144
Location Topology: Multi-pass membrane protein
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H8WE09 | MNQKGTESSSAPVGPPALGASVQEWLHWLEAIHPTEIDLGLDRVLVVLRRLFPRKPQARIITVAGTNGKGTTVTALESILLAAGRSTGAYMSPHLFRYNERVRIVGQEISDAALVTAFERVEAARRGVTLTYFEFGTLAAFVAFADAGVENWVLEVGLGGRLDAVNVLDPDYAVITSVDIDHIGFLGDNREVIGFEKAGILRPGIPAVCADPNPPSSVLQQAAAQKVALKLTGRDYTLAPGAPGQVLLTIGDEKIELPAGPLPVQSVAAAAVLSRQLVPELSLESLQHAIHSVRVPGRFETIHHDPDVIIDVGHNPHAAA... | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 2/2.
Function: Functions in two distinct reactions of the de novo folate biosynthetic pathway. Catalyzes the addition of a glutamate residue ... |
A0A3G1MZU8 | VGFQAGVXDYKLTYYTPXXETXDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYHXEPVXGXXXQXIAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPPXYSKTFQGPPHGIQVEXDKLNKYGRPLLGCTIKPKLGLSAKNXGRAXYXCL | Cofactor: Binds 1 Mg(2+) ion per subunit.
Catalytic Activity: 2 (2R)-3-phosphoglycerate + 2 H(+) = CO2 + D-ribulose 1,5-bisphosphate + H2O
EC: 4.1.1.39
Subcellular Location: Plastid
Sequence Length: 183
Sequence Mass (Da): 20053
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A0A3G1N1G5 | KDIGTLYLIFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSSVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGISSILGAINFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSFPV | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
A0A2S0LRK0 | MGVVTSSTAIPASTSRAVVDLDAVAANARVLARAAGTPWLAVVKADAYGHGLGPVALACLGAGATWLGVAQLSEALRLRELLDQAGVPRPDAGRSAPTSRAPRLLTWILPVLSPDQAAAPGSPLRVALAAGIDVSVSTPAGLDAVSAAARAEGGAARVHLKADTGMSRAGAVAADLPALAGAARTAQDAGDVVVVGLWSHLSRADEPACGSTQTHLRRLEAAERVLADAGLEVDVRHLAATAGLLWHPAARLDLVRAGIGLYGLSPDPAVATSADLGLRPAMRLEAPLVQVKRVPAGQAVSYGGTWTAPTDRWLGLVPLG... | 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: 466
Sequence Mass (Da): 47068
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E4WX47 | MGWKSIAAWLTVVNSWTLTTEKIRENERYDQTSGEYIKIFSSKEGDKYAISGVDAEPFVVESRRDEDLCSDKVCGILWLKNGITLDREEKELYSVTLTAYDSNNEKKEEDNLIIEVLDENDNKPIFTAASSKLQCEESTKNGGSCGKVEAIDADDGNAGQVEYKILPNTETWKRRGGGLETNNMGIFNIDSQTGEITLNNPGPSYWDAEQYEYVEIEVTAQDAPGKGARNPAVTEKITIFIKDVNDNTPKIVDYEKTIKVGELKPVGSAIGTENFGGAYSFKATDADVDPENNQVTFRLKSASSPFEIVNKLDNTALLQI... | Function: Cadherins are calcium-dependent cell adhesion proteins.
Subcellular Location: Cell membrane
Sequence Length: 780
Sequence Mass (Da): 86507
Location Topology: Single-pass type I membrane protein
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A0A926NHL9 | MQFGRLATALYTPFTKSLDIDWNSLERTIEHLIQTGTDTIVVSGTTAESPTLSLEEKLKLFQFVVKQAQDRVQVIAGTGSNDTAQTIEVTKLAAETGVDGIMLVTPYYNKPSQAALYQHFKSIATHTTLPIMIYNVPGRTAVNMTATTMVQIAQIENVVAIKEASGDIEQITQLIKELPSSVVVYSGDDAVTLPILSLGGVGVVSVASHLVGSEIKEMIDAFITGDVNKAKTINQKLFPVFTGLFMTSSPVPLKYAMSEQGFCEPYVRPPLVEMSESEKKSATEWLGTLV | Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4.
Function: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
Catalytic Activity: L-aspartate 4-semialdehyde + pyru... |
A0A2N3FIT1 | MKARDMMQTIKASADIDSLFSKGQRGTSRRVLVLGLPTPEARDCGTGRVLFVAGKKLGNAVLRNRCKRVLRAACSRLGGPWPGFDVALVSRAGLADAPSSDVDRDVLEALRKAEILQ | 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... |
A0A4Y8IDE2 | MFNRETVPITMKKLTLIASDYNHAPIGELEKLSIKENYIDHIYTELIGSYPINEVVVLSTCNRFEIYFVSEKDEIENLVADYVFKLTGSRLLKQEQTKYVLKGESAVNHLFEVSAGLKSQIIGEPEILGQVKSSISRSRESRASGPFLLKLFESAIKTGKRVRTRTNIAKGNASYASAALSKASEVIGSFEGKKVILLGTGKIGVTVSKYLRSLGLDSYYIASRNKNRAKSLTEKYGGIPISLDKVKKLIPEVDCLISATNVDIKIINRSMLEKLGKFKSPKVIIDLGMPRNVDPGIAEIEGIYLFNISNLDQSIQNSIQ... | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2.
Function: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
EC: 1.2.1.70
Catalytic Activity: (S)-4-amino-5-oxopentanoate + NADP(+) + tR... |
A0A8S1GSG1 | MRLFPKERLQWLGCEMSLTFPGFPDTPNFVRQSEQAYLAVRFSRSDAFQLKRVGELAAIRTNAGAVRIEGASSRRRRTSWCCRQRKKMCKKFTLLLPAGVAWSMIIIGSAIFYYFLAPAVVAKWALWGLAAVIIDGCLFLMVIANLGMAMCLDPGTHPYAIGSEEPTQLDDLRAPLYKNVDINGITVRMKWCVTCKFYRPPRSSHCSVCNRCIDTFDHHCPWVHNCVGRRNYRYFFFFLCILSVHMIYVFSISLFYIWKFRSSDEMLTPAYVCAIILMAACAILSVPVVGLTIFHVVLVSRGRTTNEQVTGKFQSGYNPF... | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 543
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 60225
Location Topology: Multi-pass membrane protein
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A0A0S4LMJ0 | MIVVPITADPKTIGMLLTWAHRSLERAGSTNASQEALWLVAYACGMKHHELASRRDQTVSAEGLALAESVVSRRMAHEPLQYILGTQEFCGLDFDVNPAVLIPRPETELLVQETLREGRFIEGAVVVDVGTGSGCVAVTLATILSDTRIFALDCSWDALTVAKSNAEKHGVGDKITWKEGDLLSPLRECHVDGAVDAIVSNPPYIAEEIWAGLQPEVRDFEPRLALVAGRSGTEFHERLLHDARQFLVPGGLLVMELGQGQAPHVRRAAEQAGGYTRLQTVNDEAGIERVVIARRAG | Function: Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif.
EC: 2.1.1.297
Catalytic Activity: L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-methionine = H(+) + N(5)-methyl-L-glutaminyl-[peptide chain release... |
A0A0A7FZM4 | MYIIYAILAFGLLIIVHELGHFILAKINGVRVEEFSIGMGPKIFSIDGKETKYSLGILPIGGYVKMLGEEEDVNDERSFSAKSPLRRITIILAGAFMNLILAIVIFTAYLNHFGYRLPKVASVIDKSPAYEAGIKPGDKFEKINGSKVFTADDMTFAIALSKGNPVNIEVNRDGKLLDFNVKPSYNEKEKRDMIGFSFDQVKNPTIVQSFKESFNQTGSLIKQTFQGLKMIFTGKADLKTDVGGPVTIIKLSGQAAKAGIWTLLYFTAFISINLAVFNLLPFPALDGGWTVLLLIELITRKKVPDKVAGALNFVGFALLM... | EC: 3.4.24.-
Subcellular Location: Membrane
Sequence Length: 337
Sequence Mass (Da): 37160
Location Topology: Multi-pass membrane protein
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A0A3S5JPJ1 | MESFRTGFEKLSFIFKSSPESRVTIVSPMLREETASFIKGKKINYIQDKYKKSDLENAHIVIATTDSPEVNQKVFADCREKNILVNVADRPSQCDFYMGGIVTKGNLKIGISTNGKSPTFAKRLRQWLENFLPEQIDDILNKLYIYRSQIKGDFEQKVEAMNKVTENLIEEHD | Pathway: Porphyrin-containing compound metabolism; siroheme biosynthesis; sirohydrochlorin from precorrin-2: step 1/1.
EC: 1.3.1.76
Catalytic Activity: NAD(+) + precorrin-2 = 2 H(+) + NADH + sirohydrochlorin
Sequence Length: 173
Sequence Mass (Da): 19919
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A0A6I3J1A9 | MADVPGAPAGPDGTVAPARQDDRQVTLPRGVRLGVDVGTVRVGVARSDPDGLVATPEATVAHVPGRHTDVAAVAALAAEAGASVVYVGLPRTLAGGEGESARRAREFATGLLGSTQTAAGGPGIEVRLVDERLTTVDAARQLRDSGRRARAQRQVIDQAAAVLILQVALDHERSTGRRAGATPAEEPGPVADARRAATPIPDRPRKARHRGRGADARSGATVEPDDKDPSP | Function: Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
EC: 3.1.-.-
Subcellular Location: Cytoplasm
Sequence Length: 231
Sequence Mass (Da): 23725
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E3D025 | MLRTYDPSLVREADRIALEEYRFPGALLMENAGAGAARHLLERYPGARSVAVLCGRGNNGGDGFVVARHLGAAGREVKVYLSCPPEHLTGDAKDAFARYCRFFPEPIPSVTLSDEELRVTLKAQDLLVDALLGTGGGGELRGEILRLVRAAKGLHPLVSLDVPTGVDGTSGATGQDACTAEETLTFLIPKPGLYLPPGYQHCGEIRIQDLGVPADRLLPPQCSCSVFGREDLLGWLPPVPPDLHKGARGLVTILGGSARYGGAPFLACLGALRAGAGWVAVAAPEEGCHTYGSLVPEALLVGGTTDAKGSLTPEILTGPL... | 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... |
A0A2V2XZ54 | MVAGLRISVEISENKSIRIRGPARISIIDGECYISGAKLSKGSQVVISAYKSQAIYSRSRARVEIELGEGAGVDVAKPEEEPLFEWLETAYKLATKGSRVVVIGPTESGKTSFSVLLANIAIEQGLRPCIVDGDVGQEDIGPPGFVALSCPSKQFVWLRDLEPQAMRFIGHNNPLMGSYRLIASIADLVSKASTQSDLIVINTDGWVSSPQAIEMKLDIARYVGASHIVALAGGSFMGHLPRKGFAEIVVLRSPQGVRVRSREERRALRSQAYKKAFEGSVMRSFSISEVIITGSCLFSGSPVSGEELSQLSEALSTKVL... | Function: Polynucleotide kinase that can phosphorylate the 5'-hydroxyl groups of both single-stranded RNA (ssRNA) and single-stranded DNA (ssDNA). Exhibits a strong preference for ssRNA.
EC: 2.7.1.78
Catalytic Activity: a 5'-end dephospho-2'-deoxyribonucleoside-DNA + ATP = a 5'-end 5'-monophospho-2'-deoxyribonucleoside... |
A0A9E9JQW0 | MNWLQKLFFGSLRRQLIIGVAVTNALIMAMFVWDASERQKQMLLDRQTEYAIALTQSVASSSASWLSTRDFQGLQEIIRAQKRYPELQYAMILDKRGRIVAHNDPAHLNQYILDLPAETAEPADVYIQQRSLALVDVVSPIMLSSYRIGWVRVGLTRQTMNARLQSIYRDGVLFALASIVISSLWVGIMGWRLTRRLEIIREASDAIQAGERKRRVHLSGIDEAAALGSAFDAMLDTLAARDLALRLANERLQAATRAGIIGIWEWDAVTDELIWDEVMCRLYGIQVQAFAGTPQAWLNLLHPQDRRAARRDVLKTLSGK... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 608
Sequence Mass (Da): 68399
Location Topology: Multi-pass membrane protein
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A0A6G7VJG3 | MTTPDFPPPVHRQRPSRRQVLTILAGSAAIPLGVAALRMWGPQPVFHYWYGEALGAEASMQLWHSNAGHAKRTLARMVSEVLRLEAVFSLYRPDSEISRLNRDGALADASRDMTNVLERARALADVSGGAFDPSVQPLWTLYENHFRHTADPEGPPPGPLAAARRVVDYRKIDLTGRKVRLASPRMGVTLNGIAQGYVTDVVADLLRNEGFDHVVVELGETRVLGPHPDGRPWRVGLKDSQGGTGRSIDLVDQSSATSGGYGTVFDPAGKNHHIFDPATGLSANSLAEVVVIAPRAMDADALATAIFVAGEDRAPALLAL... | 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: 338
Sequence Mass (Da): 36321
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A0A8D2D9J4 | MAKPAQGAKYRGSIHDFPGFDPSQDAEALYTAMKGFGSDKETILELITSRSNKQRQEICQSYKSLYGKDLIADLNELDMLDIREIFRTKYEKSLYSMIKNDTSGEYKKALLKLCGGDDDAAGQFFPEAAQVAYQMWELSAVSRVELKGTVRPADDFNPDADAKALRKAMKGIGTDEDTIIDIITHRSNAQRQQIRQTFKSHFGRDLMADLKSEISGDLARLILGLMMPPAHYDAKQLKKAMEGAGTDEKALIEILATRNNAEIRAINEAYKEDYHKSLEDALSSDTSGHFKRILISLATGNREEGGEDRDQAREDAQEIA... | Function: May associate with CD21. May regulate the release of Ca(2+) from intracellular stores.
Subcellular Location: Melanosome
Sequence Length: 460
Domain: A pair of annexin repeats may form one binding site for calcium and phospholipid.
Sequence Mass (Da): 51664
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A0A1E5E3Q4 | MLYSQMVETQDSTENEAQKPIPVFLHGFLGSSLDWDGCLSHLDLPHAICIDLPCHGLSKYCEVQNFEEACQQVQLTILSKLKKEKRSLNTPLVFVAYSLGARIAMFGMAKNAFPDLNVQGAIFEGGNFGLNHEEGNVLRWENDKHWSKRFATEAIEEVLFDWYEQGVFSSLNDDQRQELVELRSDNLGSQLGCMLRATSLSKQPYLLDDLKQLALPLLYICGEHDQKFRSIAENSGLAFKMVQEAGHNVHHEQPQAFAALVSDFIDQL | Pathway: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 3/7.
Function: Catalyzes a proton abstraction reaction that results in 2,5-elimination of pyruvate from 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC) and the formation... |
A0A235CL84 | MKLRLSYLALTLAVAILFGSGLSIYLTYRVADHEFRDLLDEDLKHQAEVIARLMAATPGAMSDTELQSLLARTFRHDDEETLLITVTDLQRQQLISNLSYQQWPASIDSGRVKLQFDGHEWSGRQYRHKTILVQLLRRNDLYRELQGEIAEDIITPALAGSGFTLLLLAALVGLILWPLSHLVRQLEQRSANDLAPLRLASPIREVALLSDRINQLMADIADVLERERRFAGDLVHELRTPLTTLKLELACDQPDTPAIRAEIDRMAKVVEQLLLLVRLDQGRWHHQFDCMPVKPILEPVLEHFSRRLAPGQLTLSSRLE... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Cell inner membrane
Sequence Length: 434
Sequence Mass (Da): 48813
Location Topology: Multi-pass membrane protein
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A0A1F2RME5 | MKAVVKIGGTLLETAADRLRIAEMVARQVRAGHRILLVHGGGKQLTQFLDTMGVASRFVDGFRVTTAETLDGVIKVFAGTVNHELLAAFCRVGLPAVGLSGIDAGGLIAEKLQGERGQDWGFVGQIRKVNPAVWETLLEAGFLPVLACLAVGEDGQIYNVNADQAAVACAVHSWRGRADALVFLTDVDGVRDGEGRALARLGAEEIPALLRSGVVTGGMLAKLNAVREALAQAVPSVYIGNGHRDDALDSVFAAGKPSHEAAVAGTVITPSLTASSSEGKCGSHWSEGGHVA | Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4.
Function: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.
Catalytic Activity: ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate
EC: 2.7.2.8
Subcellular Location: Cytoplasm... |
A0A922W8M2 | MRANLLLTTVMGIGALGLAACGDNEPTTPPAASPASSQTAPTPGDQDGVRATTTETGDATLMNNDGEEIGTVTLTQGPTGLLMRVEAEGLTPGWHGIHIHAVGDCSDAAFENAGSHINHSQAPHGLLNPEGPDDGDLPNIHAGENGQARAELFTTSARIAENGPGQWLWDEDGSAIVIHANPDDHRSQPIGGAGDRVACAVVSRS | 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: 205
Sequence Mass (Da): 20961
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E3CZL2 | MTSSGILLLDKADGTRSTACVDRVRTILGRKTKVGHAGTLDSTASGLLVLLVGKATRLASLVMSFPKVYQASIQCGVTTSTDDRSGEVLSRRPFDHVHPEGIRRVLPGFLGWRSQVPPQVSAVHVAGQRAHDLARKGVAPELSPRPVFLRRLDLTGFDPASGRMELRVLCSKGTYVRSLARDLGERLGCGAHLAALRRTHIGPWAADQGLPSDQAFGASSGFLREALLPLDSLQRALPSYRAGAKEAEACLHGAPLRLDRLQAVAPGTCPSTGLVLVLHGHGVSLYRPAYEGDQPILACEANLGEPEALLS | Function: Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
EC: 5.4.99.25
Catalytic Activity: uridine(55) in tRNA = pseudouridine(55) in tRNA
Sequence Length: 311
Sequence Mass (Da): 33095
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A0A6I3IVE3 | MNTPPSPPPTALSIAGSDPSGGAGIQADLKTFSALGAYGMCVITALTAQSTQGVTGVHAVPADFVTQQLETLLGDITPDAVKIGMLADADVTRAVGRVLGRLRAEEDDELPIVLDPVMVATSGDRLLDESAVAAVRELVPLASIITPNLPEAAVLLDAEPATTVDEMVEQARALVTAGARRAYVKGGHHTGTEQATDVLADTHGHVLITAERVPTRHTHGTGCTLSSALAALRPRRPDWETTCRDAKSWLTEALRHADELHVGHGHGPVHHFHDVWSRA | Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; 4-amino-2-methyl-5-diphosphomethylpyrimidine from 5-amino-1-(5-phospho-D-ribosyl)imidazole: step 3/3.
Function: Catalyzes the phosphorylation of hydroxymethylpyrimidine phosphate (HMP-P) to HMP-PP, and of HMP to HMP-P.
Catalytic Activity: 4-amino-2-meth... |
N4UI64 | MNDSISESSVHKSSIPTKVEMSQNEKYSEAPSEPPTIPPPPEQYAWSRVREYCQDAFSEFFGTFILLLFGDGVVAQVVLSRGTKGDYQSISWGWGLGVMLGVYVGGKSGGHLNPAVTLANCIFRGHPWRKFPVYAVAQVLGAMCAAAVVYGNYKSAFDAYEGGPGIRTVIGENATAGVFCTYPAEFMTRTGMFFSEFIASTILQFVIFAMADSANIGAGPLMPLGLFFLIFGIGACFGWETGYAINLARDFGPRLVSYMIGYGSEVWSAGGYYFWIPMVAPFMGCAFGGLLYDVFIYTGPSPINTPGMGLPRLLSPRRST... | Catalytic Activity: H2O(in) = H2O(out)
Subcellular Location: Membrane
Sequence Length: 331
Sequence Mass (Da): 35872
Location Topology: Multi-pass membrane protein
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A0A380MXG5 | MIEPIMTPNTPLHPSDISEPNQPNALMNNYARLPIAFTRGEGIYLYDEQNNQYIDALSGIAVCGLGHAHPELAETLATQAYQLWHTSNLFEIPAQTQAANTLATLSQMDKVIFCNSGTEANEAALKLTRLHARAKGIEYPAVISFYGGFHGRTFGSMAATANPKIRQHFEPQLSEFIHLPFNDIKAVEAQRYRTNVVAVLLECVQGEGGIHPATVPYIQAIRQICDEQGWLLICDEVQVGFGRSGKWFGYQHYNILPDIITLAKGLGNGIPVGVCLAKGKVADYFQPGYHGSTFAGSPLVMTVVNKVLEIYQRENIPENA... | Cofactor: Binds 1 pyridoxal phosphate per subunit.
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 4/4.
Catalytic Activity: 2-oxoglutarate + N(2)-acetyl-L-ornithine = L-glutamate + N-acetyl-L-glutamate 5-semialdehyde
EC: 2.6.1.11
Subcellular Location: Cytoplasm
... |
A0A1Z8WV17 | MIKIILKKLLMQEHLTEKEASNVFKAMINGELTDAQISCFLSLLASNGESPTEIAAAAKVMRMNCLRVPTNVQNLVDTCGTGGDNSNTFNVSTGAAFIAAAAGVKIAKHGNRSASSNSGSADLLEKAGSEINLPPDKVAYCIENLGIGFMFAPNYHRATKKVVAIRKELGIRTLFNLVGPLTNPAPVYTQVIGIFDSNLIEKYLEVLIKLDCKRAMVIASRDGLDEISVASNSIVGELYDKKYKILELDPEKIGIKKHDKPKIDVKNAEESLRIIRSVFNGEKGAAFDMLALNAAAVIYIGGISEDLKEGVEIAKAVIEK... | Cofactor: Binds 2 magnesium ions per monomer.
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 2/5.
Function: Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).
... |
A0A0X9VJL4 | MFLKDRLLTKPIINLGDWQFDKKVVEVFPDMIRRSIPGYSNIITMIGILVTQYVTPNSIIYDLGCSLGTVTLSILRNIRVNNCKIIAIDNSAAMIKHCKRFINKYRKNTSGINTTVEIIKGNLIDINIENASMVILNFTLQFISPSLRQQLINRIYQGMNPGGILMLSEKFNFENQKINSLLFKMHYNFKRANGYSELEIHQKYNMLKNIMLPDSIDTHKLRFKTAGFNNYDLWFQCFNFGSLIAIKD | Function: Catalyzes the conversion of S-adenosyl-L-methionine (SAM) to carboxy-S-adenosyl-L-methionine (Cx-SAM).
EC: 2.1.3.-
Catalytic Activity: prephenate + S-adenosyl-L-methionine = 3-phenylpyruvate + carboxy-S-adenosyl-L-methionine + H2O
Sequence Length: 248
Sequence Mass (Da): 28677
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A0A5N8TFN2 | MCRWPLPNVTSRHYCTIKTMARFLFCAVGSEECVSERLIIRISDASQPIYWAQVRASDNQVVESGSCQQLSALTEQAQTRRVVVLVDSTWLTLTSVTLPPGSRRQRDKVVPYLLEEALAEEVEAVHVSIVDTQADTAHVAVVAHQQMQAWQHALDEAGIDARQWIPDVLCVPWSSDSLSLLALGEQWLCRFSANQGVVGSADWLAFWGQTWWQHRQDSEETLSPEQADSLTIKGYGDDKPQADNPLSALPLPVEWQSDHAMHLLAVQSHGVTANLLTGGYRPQSQTKQTLRPFLPAACLLIAMAGLLGVEQWLSIRDTQQ... | Function: Inner membrane component of the type II secretion system required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm.
Subcellular Location: Cell inner membrane
Sequence Length: 447
Sequence Mass (Da): 50101
Location Topology: Single-pass membrane protei... |
A0A9D8XW51 | MIFIWLRRIIGFFLFIISLCLAAGCFYYYHVKSTLPDVKQLKEVTYETPLQIYSADNLLIGEYGTDRRIPLEFEQIPQQVKDAFIAIEDRSFYSHFGIDLKGILRAAKVFFEKGKMAQGASTITQQVARNFYLSPEKNITRKLKEIFISIHMEQELTKDEILTLYLNKISFSHHANGIAAAAYIYFGKTVDELTLGETAILAGMPKAPSTNNPISHPDKARERRHLVLLSMLSTGKITQEQFDEADNEPINSYYHVPKIEANAGYVAESIRQTLEATYGDAIYTEGFKVYSTVDSRVQEKANQAVYNGLTDYDMRHGYRA... | 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... |
I5AQU6 | MQEINREQNTEETRDSKDSKEELREETVFHRRSAGSWLMIAVSVAILVALDQFTKYLAVTKLSGEDLRILIDGVLDFVYLENHGAAFSMLQNQQWFFYILTTVFFILAVVVLYRLPQNAKYRPMTISVVVLLSGAAGNFIDRVVNRYVIDFIYVELINFPVFNVADIYVTVGVTILIVLMIFKYKDEDMKVLFRSRKSG | 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-, ... |
A0A1Q7UJS1 | MSRGEQRRRERSTRWAFEHGPPIYVRHQIVHNDHVVRRLERMGAVFVDDEDEVPAGEICVLSAHGVAPSVRENCERRGLRVVDAVCPLVSKVHAEARRYADSGHLVALVGHADHVEVIGTQGERPESTVVVESPDEAAKLDSGGKPIAVISQTTLSLDDVRATVDALETRFGRLRRPAADDICYATQNRQDAVKRLAEEATLILVIGSQTSSNAQRLVEVARIAGAEAELVDGESELPEHVRKHEVVGLTAGASTPEQLVEGTIQRLAALGYGDVEEITVAREDVHFRLPREVAAK | Pathway: Isoprenoid biosynthesis; dimethylallyl diphosphate biosynthesis; dimethylallyl diphosphate from (2E)-4-hydroxy-3-methylbutenyl diphosphate: step 1/1.
Function: Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl di... |
G4QJL6 | MQAYVGRFAPSPSGPLHFGSLVCALVSFLHARQAKGKWLVRIEDVDTTRVQEGADKVILSQLLAHGMQWDGDIVYQTDRQHAYQSALDTLHKQQLVYACACTRQEIKSKGRYYTGTCRQMQLPWENNAIRVINTCQNTYFDDIHLGHVQVDALFCSEDLSIKRKDGLFAYNLAVVVDDIEQHVSHIVRGADLIDTTVQQQHIYSLLGKTSPKYFHLPVICTKSGQKLSKQNHAAAIDNKQASKNLIYAFAAIGLSCQSLTEKMTIEELIHWALTHWSPNLLVKRREILISDINTV | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the tRNA-independent activation of glutamate in presence of ATP and the subsequent transfer of glutamate onto a tRNA(Asp). Glutamate is transferred on the 2-amino-5-(4,5-dihydroxy-2-cyclopenten-1-yl) moiety of the queuosine in the wobble position of the QUC an... |
A0A447LIG9 | MSAAIQIVMLSFACLIVLLCRPPVDQILSGSVFRAGALAIVCAFGLAWMSETFVSSHIDLIKSEVQVLLQEHTWLIAIMMFFVSAMVSSQAATTLILLPLGLALGLPAYALIGSWPAVNGYFFIPVAGQCLAALAFDDTGTTRIGKYVLNHSFYAARPGKRDGFRGDGPDDWQTGVRLMLLPGPLIPGAVFYRLARQSCAKTQCLLTEVHYGAIPHPATILAQRGAALARSA | Catalytic Activity: (S)-malate(in) + succinate(out) = (S)-malate(out) + succinate(in)
Subcellular Location: Cell inner membrane
Sequence Length: 232
Sequence Mass (Da): 24852
Location Topology: Multi-pass membrane protein
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A0A8B8P1Q2 | MEDAYARSVSEVLDFFEVDPSKGLSDSQVARHARLFGKNVLPEEKRTSFWKLVLKQFDDLLVKILIAAALVSFVLAVVNGETGLTAFLEPSVILMILAANAAVGVITETNAEKALEELRAYQADVATVLRNGCFSILPATELVPGDIVEVSVGCKVPADLRMVEMFSDQLRVDQAILTGESCSVEKELACTLTTKAVYQDKTNILFSGTVVVSGRARAIVVGVGANTAMGSIRDSMLQTGDEVTPLKKKLDEFGTFLAKVIAGICVLVWVVNIGHFRDPAHGGFLQGAIHYFKIAVALAVAAIPEGLPAVVTTCLALGTK... | Function: Catalyzes the hydrolysis of ATP coupled with the transport of calcium.
Catalytic Activity: ATP + Ca(2+)(in) + H2O = ADP + Ca(2+)(out) + H(+) + phosphate
EC: 7.2.2.10
Subcellular Location: Membrane
Sequence Length: 1010
Sequence Mass (Da): 110499
Location Topology: Multi-pass membrane protein
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F8KUS3 | MQVMQSNFSMLPFEIESSWQKALEEELKKPYLLELAVFLEKERAMGAQIYPPKNLIFNALWNTPFDQVKVVIIGQDPYHGPGQAHGLSFSVPEGIPQPPSLKNIFKELAEDLGIPAPSHGCLLHWAKQGVLLLNATLTVRQGEPMSHEGRGWEQFTDSIVKALLIQKKPMVFILWGKWAQKKWEHFKNLQDPNQHLVLTAAHPSPFSAHQGFFGCHHFSKTNQWLEKHHLTPIDWKIV | Function: Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine.
Catalytic Activity: Hydrolyzes single-stranded DNA or mismatched double-stranded DNA and polynucleotides, releasing free uracil.
EC: 3.2.2.27
Subcellular L... |
A0A2G2LWL1 | MPDIGFWELLLIAIVALVVVGPERLPKLVRVTGLWMGRATASLQAIRTEISRELRAEELKQALNKTVDLDELISMGSDSIDSEPTKGEAEKSLSEESIKPDPIEKEKP | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. Together with TatC, TatB is part of a receptor directly interacting with Tat signal peptides. TatB may form an oligomeric binding... |
A0A6A4R3E5 | MPPKTYFSISHLIYKYFLSLIIFNSLSLSVSPSSQLSLLSFFTFFAFALMVVMATMSVVNVSPCCMFQPAIQNRSTVATIVKCPFSIGSVKSVSRSFRLKSSSFRVTAMASYKVKLVGPDGKENEFEAPDDTYILDAAENAGIELPYSCRAGACSTCAGKIISGQVDQSDGSFLDDNQLKDGYLLTCVSYPTSDLVIQTHQEESLY | Cofactor: Binds 1 [2Fe-2S] cluster.
Function: Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
Subcellular Location: Plastid
Sequence Length: 206
Sequence Mass (Da): 22543
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G3YD57 | MPSHSFKRIGIVGAGNMGSMMSFAFTELGLDVSIWDVKRENVDGIKKWYDEGKFSDKGKVEGFYEIDKFTKSLEGQGERKLFIFSITHGDPADSVLDMIQNDLKKGDIILDGGNENYRRTEQRQKRCKELGVSWIGMGVSGGYQSARHGPSLSPGGDPEAIELVLPLLEQYAAKDEKTGKPCVTNVGPAGSGHFVKMVHNGIEGGMLSTTAEAWALLHWGLGLDYQEISDIFEEWNTKGELRKNFLLDIGVQILRTKKTPQGDYQGEGASQNGGYVLDDVLDKVVQDDDDTEGTPYWSVMETANRHVAGPTLATAHYMRI... | Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; S-methyl-5-thio-alpha-D-ribose 1-phosphate from S-methyl-5'-thioadenosine (phosphorylase route): step 1/1.
Function: Catalyzes the reversible phosphorylation of S-methyl-5'-thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate.... |
A0A0H5RY07 | MSAALFYVDALPGAGELAVVDGDEGFHASNVRRIRVGEQIDLSDGAGTLAHCVVEETAKGRLSARLTERVVIAAPRPSVTVVQALPKSDRSELAVELATEAGADAFLAWQASRCVARWEGPKMDKGLRRWEAVARSAAGRGRGVDAGADPAGRRRGVRGSVGAGTA | 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... |
A0A5R9DYU7 | MTANRSCTDDHLSPVNHSACQGGVGVLDTAGAERRLGQVPGWELREGRLTRTFHCSTFRESMAFVQAIADIAEELNHHPNLSLEDKREVRVVLWTHKLGGLTVLDFDLAAGIDAAYLPASSGTSASENPHPLTHLDARGAARMVDVSDKAVTAREAVASTAVVMAPATLSLITSGAAAKGDVLATARLAGITAAKRTGDLIPLCHPLSLDAVRVDLSATAPDRLLITARAKTSGRTGVEMEALTAVAVAGLTVIDMCKAVDRSMQVTGIRLEEKRGGRSGHWRRTTADQDGHVEANAAGSKEG | 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: (4aS,6R)-4a-hydroxy-L-erythro-5,6,7,8-tetrahydrobiopterin = (6R)-L-erythro-6,7-dihydrobiopt... |
A0A3D5ZTQ5 | MAGQYSGEADFRWRGESVSRLENLSDIVFALVLTLAALQSIPSSFSELIGLWRGALSIAICFALVLLIWRTHHVFFRRYGLDDGWVTGLNALLLFLVLIYIYPLKFMTDFVVSYFTGGFDNVEEITGILTLSQVPVLYAVYGGFFGAVYGVFALLHAHALRRADDLELTPVERSWTRFEIEFAIGTVVLSLAVIALAFILPEPLAAFSGMLFAMMGLIAWLCSARAKARIGRQADLPES | Catalytic Activity: K(+)(in) = K(+)(out)
Subcellular Location: Membrane
Sequence Length: 239
Sequence Mass (Da): 26499
Location Topology: Multi-pass membrane protein
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A0A6I3ITP4 | MRLVDTLCLAVGAGLGSMVRYAVALRAPSREDLPRGAVATTAVNVTASLLIGMMLHWFVTGGLAQPLYALVGMGFAGSLGSWSPLAVGCAELVHRREWTLLATYLGGNVLGGVLAATLGWAVAGAA | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Subcellular Location: Cell membrane
Sequence Length: 126
Sequence Mass (Da): 12867
Location Topology: Multi-pass membrane protein
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A0A6L6JMR8 | MKILLLGANGQVGWELQRSLSTLGELSAHGRDTADFENMAGLAALVHKEKPDVIVNAAAYTAVDQAETDEERAYKINTEAVATLADAAKTIDACLIHYSTDYVFDGTKQGRYSEEDITNPQSVYGKSKREGELAIIDSGCHYFIFRTSWVFASRGNNFAKTMIKLACERDELKVVADQIGAPTSAELIADVTALAIYNLSMLGHSDPFDSTQDTSSCHSERSRGIPSFPHRRESSPENSTNDDLSGIYHLTASGETSWHGFAKHVIACAEKLGMKFKVKPENIAPIPTEQFPRPAKRPLNSRMDTQKLQSLLNIELPDWH... | Cofactor: Binds 1 Mg(2+) ion per monomer.
Pathway: Bacterial outer membrane biogenesis; LPS O-antigen biosynthesis.
Function: Catalyzes the reduction of dTDP-6-deoxy-L-lyxo-4-hexulose to yield dTDP-L-rhamnose.
EC: 1.1.1.133
Catalytic Activity: dTDP-beta-L-rhamnose + NADP(+) = dTDP-4-dehydro-beta-L-rhamnose + H(+) + NAD... |
A0A5E7XP71 | MLSIHIPFYNLVLLPFSSLIISAVEIVTSPVECRKKILSLTVEGKNIGFVPTMGALHDGHMELVRQAKLSCDFVVVSIFVNRTQFNNEEDFKKYPKSFDSDAEKLRQSGCDIVFAPSDGDMYPGTPEVKITFPGLQKSMEGHYRPGHFEGVALVVSKLLHVVPAQKAFFGRKDWQQVLIIKQLVRDLHFFSEIISVPTVREPDGLAMSSRNQRLSEKERSLAVIFSKSLYMAREKLLAGESVEGAVASVRQAFDRLPEVRLEYFEIANRETLEPVQSVETNVPVSLFIAGYVGDVRLIDNIFLQEETE | 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)-... |
T0BHR1 | MTIGLEDAHIGGNEHRGQESGKEQDMSAIVWHEQKITRKQHEGLNGHRGLCIWFTGLSGAGKSTLANALEQRLYESGVHTYLLDGDNLRHGLNAGLGFDKDSRRENVRRVAHVAKLFADAGVVVVTALISPFREDRDSAREIVSSDSFIEVYVECPVEVCMTRDPKGLYEKAKSGVIKEFTGVSSPYEPPLQPDITVNTSEMSIQDCIDHILEGVKSKLY | 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: 220
Sequence Mass (Da): 24338
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A0A1Z8WV71 | MKSLVIGLGNKGPNYKNHRHNVGSEIVSKICEIKDIKLIESAKFKARIGLDSNEVYFLVPNTYMNLSGQPVALFLKNKNFDFANVFVIHDDLDLSVGNVRLKKGGGTGGHNGLRSLIKFLSTDTFNRIRIGIGRPKVSEDVSNYVLSSPSRSEKLLIDKTIETVVESIDMITSQDVQLSMNLLNKRK | 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: 187
Sequence Mass (Da): 20807
|
A0A235CJE3 | MTRQTWLFGGLFVVGLITWQWFRNDELVGVNEQDFQPDFVATNLSSVQYNRQGLPYRGMNAQHAEYYDSLSMTLMKKPVILLYSPDGQPQWRLSGDNGTINTGDNAVLTGNVVGRGLQPDALVETLTTEYLEMDFIHNKLQSNQKVTLQSPQYQAEGIGLRGGLDQQTVELLNETRATYFNP | Function: Involved in the assembly of lipopolysaccharide (LPS). Required for the translocation of LPS from the inner membrane to the outer membrane. Facilitates the transfer of LPS from the inner membrane to the periplasmic protein LptA. Could be a docking site for LptA.
Subcellular Location: Cell inner membrane
Sequen... |
A0A831JQH1 | MIIKDIRVYRGRNIYSHRPVIKMVVDIERLDIPTKDIPNFNEKLIKWLPGLSKHSCSYGYEGGFLKRLEEGTYLPHVTEHIILELQNMLGYDIKFGRARNIEGDLYYIIYEYGLEECGIRVGKLAVEMVNKFIQGEEFDLEERLEKIRNIIAEIELGPSTMAIKNEALKARIPVTRVGNGSILRLGYGKYQKMIEGTISQNTSCIAVDIASDKILTKQILKDHGFPVPEGDVAYNEEEAIAIAEEIGYPVAIKPYNGNQGKGVHLNITNREEVSIAYRNAKSYSDLVIVEKHIQGKHYRVLVVGEKVVAVAEKIPAHVIG... | Function: Catalyzes the ATP-dependent polymerization of arginine and aspartate to multi-L-arginyl-poly-L-aspartic acid (cyanophycin; a water-insoluble reserve polymer).
EC: 6.3.2.29
Catalytic Activity: [L-4-(L-arginin-2-N-yl)aspartate](n) + ATP + L-aspartate = [L-4-(L-arginin-2-N-yl)aspartate](n)-L-aspartate + ADP + H(... |
A0A6P1PUS0 | MTRCNGMTLLEVLVALTIFSLASLSLLQSLGQLATGTARLEEKTWADWVAENQLVELRLQKVWPPLRWTMGESEQAGRRWYWRWRGVETHSAEMRDLEIEVSPTPWRENSAPATVLRTYVVRR | PTM: Cleaved by prepilin peptidase.
Function: Component of the type II secretion system required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm.
Subcellular Location: Cell inner membrane
Sequence Length: 123
Sequence Mass (Da): 14284
Location Topology: Single... |
A0A2A1ZU97 | MENNVKIKIRKMDISDIPFVYDNEIKIFGRSLGEKTLYNEILYNDLAHYYLAVIDNQRAGYIGSWFTLPNAEILNVFVLEQYQKRGVGNALLCKVIDLCKELDIIYLSLEVRESNLSAINFYKKLGFKREAIRKGYYENKEDALLMVLDIGGKK | 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: 154
Sequence Mass (Da): 17885
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A0A2A1ZR87 | MNVLFVGSEAIPYAKTGCLADVLGSLPKALGNRNIDVSLVLPLHGIIKQDVEKNIRLISSYDIEIGSRVEKINLFSLFKDGVCIYFIDNHNYFGNRDTLYGHHDDGERYYFFNKAIIKSLSYFYSYPDIIHLNDWQSGFVPYLLRKNNIKIKTLFTIHNLTFQGIFPIELMEYLKEEINDVFILNDQVNFLKTGIMLSDFVTTVSKTYSTEILSAEYGYGLNNILNQKKDKLSGIINGIDYDYYNPKTDEDIYFNFTLNNYVKGKRINKEKLLEEFNIIKQRGPLVSIISRINDIKGFDLLKEIIEELITTYKINFILLG... | Pathway: Glycan biosynthesis; glycogen biosynthesis.
Function: Synthesizes alpha-1,4-glucan chains using ADP-glucose.
EC: 2.4.1.21
Catalytic Activity: [(1->4)-alpha-D-glucosyl](n) + ADP-alpha-D-glucose = [(1->4)-alpha-D-glucosyl](n+1) + ADP + H(+)
Sequence Length: 469
Sequence Mass (Da): 54299
|
A0A2S6MXE3 | MLRAVVMPHSAIRPLVAVLNGPNMNMLGLGQPDVHGRATLDDVEALCAEAAEAAGLAIDFRQTNGEGELVTWVQECRGRAAGIVIAPAGFATTSVALMDALLATDLPVIEVHISNIHRQEPFRRNSYVSLAATGVICGLGVRGYAMALQAMADLLEDLR | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.
Function: Catalyzes a trans-dehydration via an enolate intermediate.
EC: 4.2.1.10
Catalytic Activity: 3-dehydroquinate = 3-dehydroshikimate + H2O
Sequence Length: 159
Sequenc... |
F8KZC8 | MQNVIDILQERGFIEAMTSNNLKEITSTPLKVYCGFDPTAESLHLGNMVAIMGLAWFQRCGHTPIAIVGGATGMIGDPSGRSKERNILDDDSIQKNLYGIRKNIEAVLKHSSKDVELIILNNYDWFKGFSLVDFLRDVGKYFRVGTMLAKDSVKIRLESEEGLSFTEFSYQLLQGYDFLHLYDHHGVTLEMGGSDQWGNITAGTDLVRKVRGKAVHGLTFPLLTRSDGKKFGKSEQGAIWLSSEMLSPYEFYQYLFRVADADVIKLMKILTFMEMDEIRIYEKMMTQSDYVANTAQRKLAEEVTRIVHGEEGLRIALKVT... | Function: Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr).
Catalytic Activity: ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + H(+) + L-tyrosyl-tRNA(Tyr)
EC: 6.1.1.1
Subcellular Location... |
A0A427Y7U2 | MAPSLAVATGGVLRVALSRPMHHAHSPTLANAIAGPSRLPLPATAAPAQVLRQFVISVRSAHQYTRGELKRILPTLSDLGLKSGDHVTVAMSGGVDSSPLKLNVVYMRNWDPQLSESQPESVPSAKSRAVPSLSYPSSEARSSAGSSSVPPSACQWERDWKDVQAVAKYVGIPEDKVKLVDYSKEYWSKVFEPSVEVWQAGGTPNPDVMCNREIKFGTLVDQVATKPRHFLATGHYARCMRKQHATRLCRANDMDKDQTYYLSSISEDQLKRAVFPLANLTKPWVRRLAAHFGLPTADREESMGVCFIGERGNFGDFVSQ... | Function: Catalyzes the 2-thiolation of uridine at the wobble position (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln). Required for the formation of 5-taurinomethyl-2-thiouridine (tm5s2U) of mitochondrial tRNA(Lys), tRNA(Glu), and tRNA(Gln) at the wobble position. ATP is required to activate the C2 atom of t... |
A0A1F7Z1G6 | MAILLVFQIVISVLLVIVVLLQVKGTGFGRVWGGLSISSTRRGLEGVIFKFTFVLTFLFISVSLASLIF | Function: Involved in protein export. Participates in an early event of protein translocation.
Subcellular Location: Cell membrane
Sequence Length: 69
Sequence Mass (Da): 7532
Location Topology: Multi-pass membrane protein
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A0A2G2LSP5 | MSSNHACLNASVEAIISLATSKQIWVAYSGGVDSHVLLHLLATAEHMPLVSLHAIHIDHGLHADSSSWTQHCKIVVADLGIDLSSIKVQVANIEKMGLEAAARAARYNAFEQYLTENDVLLTAQHQQDQAETLLLQLFRGAGPKGLASMAKQFQLGKLSVARPLLNSKQSDILAYAQQHNLKWIEDPSNVETRWNRNYIRHNVLPEIEKRWPSAAKTISRSAENCAEASELLTELAQHDLMAIEADSASDYLAIPKLLALSAARCRNLIRHFIELKGLALPSAAVLQGVIDEVCLAKQDSVPMIAYADVEIRRFQGKLYF... | 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)... |
G8P0Y7 | MSTGRMRGEFAEPVRHDSPRLASLQEMYRPPAREHSISDYWHILLKRKWIVIVSVAIVLITTALISLHTTPIYEAVTKITISPPTSNPLNFKDNNSSSSALEDPQAGINTQVKILQSDTMAELVIHRMNLDTRADFAGRAQTQSNGGIAVSQSPAEESFRLESLIRKLQGNLTIQQIPDTTLVQVGYSDPSPALAAEIANGITAAYIEQNVKSRYDSTMQAADWLSKQLADMQIKMETAQAKLVQYQKEHAIVGTDDKQNLTTEKLDELNRELTSAQADRIQKESLYNVAKRGDPSTLSVILQDPILSALRQRQSELQTR... | Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
Subcellular Location: Cell inner membrane
Sequence Length: 779
Sequence Mass (Da): 85740
Location Topology: Multi-pass membrane protein
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A0A8B8NXF0 | MSSTRSIILKSSDGESFEVEEAVALESQTIKHMIEDECADDGIPLPNVTSRILSKVIEYCKKHVDADRASSVADDDLKAWDAEFVKVDQATLFDLILAANYLNIKGLLDLTCQTVADIIKGKTPEEIRKTFNIKNDFTPEEEEEVRRENQWAFE | Pathway: Protein modification; protein ubiquitination.
Function: Involved in ubiquitination and subsequent proteasomal degradation of target proteins. Together with CUL1, RBX1 and a F-box protein, it forms a SCF E3 ubiquitin ligase complex. The functional specificity of this complex depends on the type of F-box protein... |
A0A380N0D7 | MIQKILRHLLLLTFLMLLGLGGIGYFIYQQTLQTPIQAQNNTIIHIPKGSSVTSIARILEQDYGLKNSWVVPLYARLNGSAQKIQAGYYRLEQNITIPVLLHKMIKGEVATFSFQLVEGKTAKALLEQLSNTPDITQTLQNKTPEEIAKALNINGSLEGQFLPETYHFPYKTTDLALLKRMHQALQSALSEAWSKRSNNIALKTPYEALILASIIEKETAIPSEREQVSGVFNRRLQKNMRLQTDPTVLYGLSSPKQILTKKDLQTDTPYNTYTRNGLPPTPIALPSKASIQAAVNPDNSNTLYFVANGAGGHSFSVTYQ... | Function: Functions as a peptidoglycan terminase that cleaves nascent peptidoglycan strands endolytically to terminate their elongation.
EC: 4.2.2.-
Subcellular Location: Cell inner membrane
Sequence Length: 337
Sequence Mass (Da): 37730
Location Topology: Single-pass membrane protein
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A0A2Z4FN12 | MSDAPTGHISQRKLDHIDLCAQQQVEYRGKSTLLEEVEFLHDSLPELSLDAIDLSSEVMGKRLAAPLLITGMTGGAERAQEINLTLARVAQELGIAFGVGSQRAMMRHPDLAQTYRVREVAPDVLLFGNIGAVQVAESSTAELEDLVGAIDADALCVHLNPGQEMIQPEGDRDFRGCIDGIARLVDALSVPVIAKETGCGIGPRALDKLKQTGVQWVDTSGAGGTTWVGVETLRTTPEKAEIGDMFWDWGVPTGAAIGYAAERGFQVIGSGGLRTGLDAARAIALGANLAGMALPWLKAAYNEGPEAALKYGHTTLHALR... | Function: Involved in the biosynthesis of isoprenoids. Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its allylic isomer, dimethylallyl diphosphate (DMAPP).
Catalytic Activity: isopentenyl diphosphate = dimethylallyl diphosphate
EC: 5.3.3.2
Subcellular Location: Cytoplasm
Sequ... |
A1ZPM6 | MMRSFYQYLLYHPSFFAKQLQFLVCLCLYFTTYIHSLLLIVMKKPQFIVAAPTSNAGKTSLTLGLLRACKNRGIDIQPFKSGPDYIDPMFHQLACHKTGINLDLFMMEQAHLQANYTHCMQVPEVACIEGVMGLFDGSIKAEGSTAALAKLLDIPVILVVDAQAVAYSVAPLLYGFKNFDPDLNLAGVVFNRVNSESHYQFLIDACHDVGVVPLGRLPFLSNCEIPSRHLGLSIDQLPQYNGAIDELAKAVEQHVPIDPLLDLCMRAIEPLQTTPPPPLVSTMKIAVARDEAFNFCYQQNIDAFRQLGKIVFFSPLHDSA... | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 10/10.
Function: Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source.
EC... |
A0A933DML0 | MKYVFFGTPEFAAIVLERLIGAGMPPATVVCNPDRPVGRKKVITPPPTKLLAQKYNIPVLQPEVLSTSNLQLLTSNCDFFVVAAYAKILPREIIELPRLGTIGVHPSLLPKYRGTTPIQSAILAGDEETGVALYCMDEKVDHGAIIAKSKAQMANSNYEMLLKKLAALGGNLLIQTLPKFVKGEIRPVPQDESQATYTKKFATEDACVGEKDIEDAQAGDAEKAIKIDRMIRALNPEPGVWTFGSALANRPPALTPTRFESPAGQDVVSGRRSESGRSSMRSRAGKSQIAGGKRVKLLEAEIRDGKLLLKKIQVEGKTSQ... | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
EC: 2.1.2.9
Catalytic Acti... |
A0A8S1GPW3 | MALARVNRKLAKLGDFLLDWGGSCFVSMMLIGIYYSCLYVAAPMLYDEEATIQFLRFLANFIVFEIMINLACFHYYSRYNSVTHWHRESCVLDLRSFAEENNENGRQYFALDNLENHLNGVTEDESGSRFCITCNREAPIRSHHCPLCKMCVLRKDHHCFVTGACVGLGNQRYFIVFLFWCTFGLIIAVPHLFWLLTQTIGPWYPFGFTLYIGPIAIFRWIFSYSPFSEAVYATIFSFSVAGFFSAAGFLGMQIYYTTHGYTMYEYHNLTVRASFPGDGKNCGERFRLVFGKNWLLNFVLPMPWNMPLLTQDISNSLFRF... | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 830
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 95164
Location Topology: Multi-pass membrane protein
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A0A6A4P180 | MIAINTYNNPGFAHANAVGILPALAAKVEGNRSAFYNCSFKGVQDTLWDRSGLHYYYNCYIQGAIDFIFGDGQSIYEKCAINFTTGIDGPTIDGVITAQKRESTDSTSGFVFKECTINGINGKAELGRAYGPYSRVIIANSYLSDIVRPEGWSTWDKPEENIIYVEVNNTGPGANNANRVKWMKTLSEDELNSFLHISYVDKDGWIHKQRNANNF | Pathway: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 1/5.
Catalytic Activity: [(1->4)-alpha-D-galacturonosyl methyl ester](n) + n H2O = [(1->4)-alpha-D-galacturonosyl](n) + n H(+) + n methanol
EC: 3.1.1.11
Subcellular Location: Secreted
Sequence Length: 215
Sequence Mass (Da):... |
A0A933DQ53 | MKRRVFVALGISHELAKVINAWKERYSRLPVRWLSSKNLHITIIPPWYEGNVRRLVETLQSLENHAKPFQIEFKKVSFGPSQRSPRLVWAKGDTPHRIVALRDGIAAALGIHPEPRPFTLHLTLARFRLEEFRSFPIQRLSQEVDWSDDVTSFRLMESHLSPGGADYTIVEQFPLHWRDE | 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: 180
Sequence Mass (Da): 21014
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A0A9D0KYA1 | IRDFPASLKILEKCRPVYKTLKGWDKNTFGLKDKSQLPEEAWEFIKTVEEETGVPVVMLSTGPERSEYIWLK | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2.
Function: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.
EC: 6.3.4.4
Subcellular ... |
A0A1Z8WXB7 | MNSNYNRFFIPTPISTGQVIELPNYVINKLVNTLRQKQGDKIRIFNENKEFSATILELKTGRIKIIANKELAVIKEPAVKLHLFQCILKNQNMDLVIQKITELGATEFTPILSKNALVKLQSNKIEKKMAHWFEISRHATEQCGRIKLLKLNHPIKLDQVFVENNVASCFVLNSKDGKRLLDQKKIKRKVAICCGPEKGFDASEVEILAQKGFRNLRLGPRTLRAETAAISAISSIQTVWGDH | 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... |
A0A916WMY5 | MTVETLPTRPDWLDVLIQRATRADGQPPFSDGSLVELATGARELLVIGDVAAALVRDGEAEFVVDPDARRHGHGTALLEELLTRSPRLRVWAHGDHKAARALAASHGLEAVRELLQLRLGGVDFDTAVDGRVNQQNDIDAFRRGTDEAAWLALNARAFAAHPEQGAVTRADLDVLMAEPWFDAEDFLVLRDGDELIGYCWLKVEHGIGEFYVVGVSPDRQGEGLGRRLVEAGLSRLAARGIRISSLYVEADNEAALRLYRSFGFGDHAVDVQYAKA | Function: Catalyzes the transfer of acetyl from acetyl-CoA to desacetylmycothiol (Cys-GlcN-Ins) to form mycothiol.
EC: 2.3.1.189
Catalytic Activity: 1D-myo-inositol 2-(L-cysteinylamino)-2-deoxy-alpha-D-glucopyranoside + acetyl-CoA = CoA + H(+) + mycothiol
Sequence Length: 276
Sequence Mass (Da): 30185
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A0A2Z4FLM4 | MTIDTTQFRKGLKIEINGEPFVIVEANHVKPGKGVAFVKTKYKSLETGRQQQENFRSGDTVDTPNLESREMQYLYKDESNHYIFMDNETYEQLRVSETAVEPVLDYLKDNMTIDILFHNGRAISVDAPNFVELIVAQTDPGVKGNTAQGGTKPATLETGATIMVPLYLEQGELVRIDTRTGEFVERVNK | Pathway: Protein biosynthesis; polypeptide chain elongation.
Function: Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increa... |
A0A2Z4FRT9 | MLSGALTPHLINLHLVRVRPLSNQTPNAFKDLHETAARVRRSARVLAYQSAAAKNDALAHVAASLRASAPSILEANQKDLVRGREKGLDAAFLDRLELTTERIEGMAAAIEEVIALSDPVGRVDSTWVRPNGLRVGKRRIPLGVIGIIYESRPNVTSDAAALCLKSGNGVILKGGSDAFESNRAIYAAIRAGLEASDLPAEAAAAVGFVDTTDRAAVGELLKLEKFIDVIIPRGGHKLIRYVTENSLIPVIKHDHGICHGVVDGSARAEVVDAVILNSKVARPGVCNAMETLLVLENARQTHLPRLLGLLADAGVRLHLC... | Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 2/2.
Function: Catalyzes the NADPH-dependent reduction of L-glutamate 5-phosphate into L-glutamate 5-semialdehyde and phosphate. The product spontaneously undergoes cyclization to form 1-pyrroline-5-carboxylate.
... |
A0A1E5E056 | MNELSIGVILLIVLFTLLASGTWVALSLISVAAVGMLLIGNDSFGLIYATTTWGTVSDWSLAALPLFIWMGEILFRTRLSKDLFEGLTPWLSRVPGALLHVNILSCGMFAAVSGSSAATAATIGKMTLPELKRKGYDDQMAIGTLAGSGTLGLLIPPSIILIVYGVSAEVSISRLFIAGALPGMMLILMFIGYTIFWSIKNKTRMPVDDTYYSTATKFQALLKLIPVACLVVFVLGSIYAGITTPTEAASFGVLGSLILAITSRSLTWDTFKSSLLGAVKTSCMILFILAGAAFLTVAMGFIGLPRMLAEQIAIMQLSPY... | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 434
Sequence Mass (Da): 46583
Location Topology: Multi-pass membrane protein
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A0A9E4K8V6 | LQALPGIGRSTAGAIRSLGFGHYAAILDGNVKRVLARHYAVEGWPGQAAVMKRLWQLSEHLTPQRQCADYNQAMMDLGAMVCVRTKPLCGTCPLAHSCVARARHEIERYPGRKPKTSKPERSAQLLVVLDGADNVLLQKRPPSGIWGGLWSLPECPVEQRGEHWCQANLGLRVKQLRQLAPRRHTFSHFHLDITPVLLKMEKPLKAVMDENSLVWYNLSEPEDLGLAAPVSTILQQIDSKPDRGKQ | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Adenine glycosylase active on G-A mispairs. MutY also corrects error-prone DNA synthesis past GO lesions which are due to the oxidatively damaged form of guanine: 7,8-dihydro-8-oxoguanine (8-oxo-dGTP).
EC: 3.2.2.31
Catalytic Activity: Hydrolyzes free adenine bases from 7,8-... |
A0A7X3DGE7 | MDTEAQPTERDRSLPPDPEDSSGAPGPEGRSRSALVSRFADGLPGGRITLTLLLCLLFLLAVNVFVARPFEIPSGSMEKGLRVGDRVLVNKLAYTFGDGPARGDVIVFDGIGYFGDADYIKRVVGVG | 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: 127
Sequence Mass (Da): 13525
Location Topology: Single-pass type II membrane protein
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A0A448PFT2 | MFETTSAWWDIDYHLLLPAPADLIWGTVAFAVVAFAVYKYGWPAFKETLDERAEKIDAGLKAAELARAEVADQRAQIEEEIRQAQREATGIRELAQDNAKAIVAEAQTRANTEAENTILKAQRRIDADTISAMRTLEGDIGELATDLAGRIVGEAIQDEALAHRVIDRFIDELAQNTPEYAKGAEA | 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: 186
Sequence Mass (Da): 20542
Location Topology: Single-pass membrane protein
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A0A6G7VHP0 | MDQDEDYKDLFFTECDELLAELQDHLTLMSSGEHGRDIVDATFRAVHSVKGGAAAFGLDALTGFAHRFEAVMDACRAGRLDVDDTTLPILFRASDMMQELVEHSRSDAPLRDEVLQQITRSLDALVGIEPEPSAVATADTTGQTPPAADGEPIVVTFRPEPNFLACAHDPLRMLRGARRIGLTEVRVAGDLPPLEDLDPMVCPWTWHLTFAQAEPSVLRDFFSIYDLSARIDGVPTADAPATLPLRTSQPSEGARVPTTDGGTGVGYVKSLRVPLDRIDRLVNLVGEIVITQAAVAQVLSQPRHGVEDTLAHSIEALSRQ... | Function: Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. CheA is autophosphorylated; it can transfer its phosphate group to either CheB or CheY.
EC: 2.7.13.3
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Sequence Length: 667
Sequen... |
A0A1N6M543 | MKKLLNQSIARKLVFMFVTASFVVLVVFALTIQHAIKNHFNEQDYRHLETKLRPLIGTVERDLDLFHSWDISAWVLNNKQVVKTNNETIDFPSELIGRSSYEWSVGNNRFHAFKFDYPEIKGGEIVLAMDVTHHKVFFDKLNTILFWTLVLTLSLSGAYALIIVRNGLQPLKQLKEYIAQVNTSNLSMRIPSDSLPKELSSLIISQNEMLERLQEGYLRLSEFSSDIAHELRTPLNNIQTQTQVALGIERSVEEYQDILVSNVEELERFNKTISDTLYLAKSENQLLHKTESELELKEVITPLLEYYEALAEEKNVRFTL... | Function: Member of a two-component regulatory system.
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Cell inner membrane
Sequence Length: 442
Sequence Mass (Da): 50467
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A0A0U2RS00 | MATWLNMSLQDGASPIMEQLVFFHDHVLMIMLMITTTVSYMMITLIRKQTNQTIHTSSTNNWNHMNHCTCNHPCIHRHTIPTTSLPNSRSPQPSINAKSSWTPMMLKMWMLSLHKASVRLMYNPASSTTSKNIPTTSHGQPNRPTYKLTYPINRYSSSCPTLMNNPKTGGKNSRHTSTTKPNKILNQSSWYPLRTVLSNLRSKPQIHAHYNWKSTSKKLHYWVSKMSE | Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
Subcellular Location: Membrane
Sequence Length: 228
Sequence Mass (Da): 26227
Location Topology: Multi-pass membrane protein
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A0A7C8TZ50 | MEGLKAAFAKCKAEGRNALVAYVTAGYPTVELSVPILQALQAGGADVIELGLPFTDPIGDGPTIQGSNTIALQNNVNVPTVLSITKQARAAGVTVPIVMMGYYNPMLIYGEERLIKDCAEAGINGFIVVDLPPETEALQFRDHCVKGGLSYVPLVAPSTSEARLRKLCSIADSFIYLVSRMGVTGATGKLNDDLPDLIKRVKQASGNKPIAVGFGVSTRAHFQLVGAAAEGVVIGSQIVNVIRENPGNETLALRKYLYEVLGRSDLGDLSKPNGENVTFANGENRAVDGSKVTVDGVIREGPYGTEPGLADQIEALNMEH... | Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5.
EC: 4.2.1.20
Catalytic Activity: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan
Sequence Length: 539
Sequence Mass (Da): 58009
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D3PZ12 | MSLGDTLAPVLRRNGGSAVGFEPPTIRDGERLWQLALDSRTLDVNSRYSYLLWCRDFAETSVVARHDGEAVGFITGYRRPGSPGTLFIWQVAVADSHRRQGLARRMLDNLAARLIPQGITALEATVTPDNLPSTRLFTSFAEARGAELTRDELFSGQLLGEGHLAEILFRIAPLSPASE | Pathway: Amine and polyamine biosynthesis; ectoine biosynthesis; L-ectoine from L-aspartate 4-semialdehyde: step 2/3.
Function: Catalyzes the acetylation of L-2,4-diaminobutyrate (DABA) to gamma-N-acetyl-alpha,gamma-diaminobutyric acid (ADABA) with acetyl coenzyme A.
EC: 2.3.1.178
Catalytic Activity: acetyl-CoA + L-2,4... |
A0A2M6YPA4 | MLRFFRHFDWLIFFLALIIALLGLVVLKSIAPSLITQQIIWLVLGLFFFFIFSQIDYQRYPRFAWIFYFGSIFFLLLTFIFGRVIRGSTRWLEIGGLGLQPSELVKPFLILFFASFFASGEEMNLKKILTGFGLLLPPFLMIFFQPDLGNSLVVLFFWLGIILAKGMKSKWLALSFSLFFFILPLFWFFLKDYQKQRLFTFLNPQSDPLGSGFNVLQSMIAVGSGQFFGRGLGRGTQSHLSFLPERHTDFIFSSLAEELGFIGSFLLVGLFFLLLWRILNLARNSRDQLAFLIYIGVFTLLFSQIFVNLGMNLGLLPVTG... | 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-... |
A0A836K7M6 | MVAEKYNKLEPELKEELRTIAQQIVTPGRGILAADESTTTIGKRLQDIKVENTEENRKAYRQLLFTTAKQTKSILKPTNPLPPRLYRLPKVHKPNIPLRPIVSAIHSPTYNLSRFLQSLTGKSESHITNSTDFIQKIRFYEQTLGAAMGSSVIANIFMKHFEKEVLQKNTQKIRSLVSLCIDDTFVMWSRAELRKFLIFLNNQHSNIHFTINIEKNRKFPFLDVLVSKKDKKDITKIINKHANKTTVTISDIQPDERILSILSYIKGITNRIDRILNKYNIRIIFKPPKKDVIGQHISGVILFHETLYQKADDGTPFVEL... | Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4.
EC: 4.1.2.13
Catalytic Activity: beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate
Sequence Length: 587
Sequence Mass (Da): 65748
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R9PJ05 | MLNFLSSMPYQRKPWFLLFIGSLSLELCALFFQHVMKLDPCVMCIYERVAMFGLMFAGLIGWIAPQNLIIRLTAFGMWIVSAAWGLQLAITHTDYQMNPNPFATCDFFANFPEWAPLDKWVPWLFNPTGFCDKISWMFLGWSMPQWLILIFAVFLAAGVIFFGLQWRKK | Function: Required for disulfide bond formation in some periplasmic proteins. Acts by oxidizing the DsbA protein.
Subcellular Location: Cell inner membrane
Sequence Length: 169
Sequence Mass (Da): 19683
Location Topology: Multi-pass membrane protein
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A0A926RT71 | MLHRKLKQMIIKNEWFGATDHLLVGVSGGPDSMALLHALLRLRADFKWKLTVVHVNHQLREYESDEDATFVKEICRTWDVDCHVIYVNVKQELQEFGGNKQQTARNLRYDAFAQVGEQVGAHKMLLAHHADDQVETIMMRLLRGTGMQGLAGMKPQTRWKKLSLIRPFLFVSRAEIEEYCRHEHILFRTDSSNQTLTYTRNRLRLELIPQLETYNPHFKKALQHLSEVIHEEELIWDELTQEALTKVIQYKSERKYLVKVSSFLHLPIALQRRAVKLILKYLAPTGEQLDSFERIEEIRRLAMHTSPSVSIDLPHGLKIS... | 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)... |
A0A926NEM5 | MKSEDEKKEAPRAKARPSKRPVTKKEEVPLEPSPKQPVLDQYVTLIKGAVGEQAVSEYHINREAGHLPTIVIRKEDWLATARYLKRSDELSFDYLQSLAGVDYASYFEVVYVLLSMSTLQKVMIKVKAEREEASVPSVSDVWAAANWNEREIFDLFGIEFTDHPHLKRILLPDNWVGYPLRKDYEPLDKEV | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrog... |
A0A932WHS0 | MVEGLLKTEEPKGESGFRPPKVTLKRLTRPEIRNVFEKGRKVLSSAFVLFFIESRASTPPSYSIQVKKKLGTAAERNRTKRIFREALQRHKLLLKGYQLILIPRSDSKGIGLNDAVDQVMKIFLGMQRKK | 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... |
H3KBU9 | LCEDVLSPFDVPRFNNSAMDGYAFRGSELKGERVTLALCGTSYAGTPFEGEVPVGACIRIMTGAAVPEGLDTVIPFEDVEATDAAVSFSADAVKPGANVRLLGEEIRRGQVVIPKGAMLTPEALGLAASFGRAALPCASLRVGVFSTGDELREPGEPLGPGQIYASNGYLLEALITRWGHEVVPLGVLPDDETVLEKAIRAAMAECDVLVTTGGVGEGDHDLISRVLGRLGSIEHFHVRMRPGKPLAFGYLDAGHPVFFMGLPGNPVAAAMSSRLFLRPTLARLSGLTDKVERPETVRVVCGKDVRAKASRTDFVRGNFV... | Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
Function: Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP.
EC: 2.10.1.1
Catalytic Activity: adenylyl-molybdopterin + H(+) + molybdate = AMP + H2O + Mo-molybdopterin
Sequence Length: 365
Sequence Mass (Da):... |
A0A836FQ97 | ILINYIFNELKILINYSLKTLGTPFILLPFIVIIESIRLIIHPFTLTIRLTANIIAGHVLLILLGSSGINIFNFFISVCLIRLYNIHFSPYHQFGFEAAS | Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramemb... |
A0A177WB83 | MSKSIAVKFLGNAVSYRKAMEVQSYLLQMRTKKCISDPANIDILLLLEHVPTFTAGRRIKGTDDTEGARLRNLNAEYFQTLRGGQTTFHGPGQLVGYPILNLKTMKIGVRCYVDRLEKVLIDACSHYNIKAGTTHDTGVWVDNRKIAALGIHVSHHISTHGFALNCNTDLKWFDHIVPCGLPDKKMTSISQELMSRGRKEIVTVDTVMPVVIESFGKLFEANMSPLYQVLPEVDDHITAILM | Pathway: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 1/2.
Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-A... |
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