ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
|---|---|---|
A7SKC3 | MSFSFGAALKSGFQHAVTRQWQSTNTSLTPHNLIYPLFISDDPDGLEHIASLPGQARVGINNLEKVVKPLVDKGLSSVLVFGVISKLEKDGNASNADSDLCPTILGIKKLHSLFPDLLIICDVCLCPFTDHGHCEVMFTGNKIYSSESCDRTANVSKFSAFVGCHVVAPSDMMDNRVAAIKQIMAANGYGSKVAVLSYSAKFASSFYGPFRDAAKSAPAFGDRRCYQLPPGARGLAMRAVDRDVQEGADMLMVKPGMPYLDIVRDTKNKYPDLPLAIYQILAANGYASKVAVLSYRQFLFLLGADIIITYFVPQLLDWLQ... | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 1/4.
Function: Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensat... |
A0A7X7GFW9 | LWEVHVLTGIRGVTDLPDRATVVALRAHHSVTDGLGLVQMARALFGDADITPSTGRPPSLDLGVVGAIVKLPVALAELAVASVGSARARRSLDALVREGKITEPELHRPRTRFNIESTGPRQFGRVRFALSDVRAVARTTDTTVNQVVMALVSAAMATYLANRDETPVVSLAAQVPVSIADRSDLVSENRTTVAFVDLHTDTTDPLDRLRLIRESAEREKARLDRPETEYLASAVLDRCPAPVLRKVIRRDVGASIEAHGGGTVPSHTIVSNCARGSAVPLRFGDSPAVDGFSAPVLNRTSGLLHMTTSLGEVLNVTFSS... | Pathway: Glycerolipid metabolism; triacylglycerol biosynthesis.
EC: 2.3.1.20
Catalytic Activity: a 1,2-diacyl-sn-glycerol + an acyl-CoA = a triacyl-sn-glycerol + CoA
Sequence Length: 361
Sequence Mass (Da): 38772
|
A0A979FM58 | MKKRYDTSLNFLPLLVLIFHANAVKTDGSSEFKVKFSPNDLSFPVSQTETITLLFYGSKQSDTNLTFSFSESGILEEIPSKTVPAGLNDSLYIVLKPRNVGHTVVFINSTDMIDLSEAYARVSISHTDTLDYVVQCLLFDRGDQKISAATRVILVTIVAFSVFAAIFVFISSVQWLDFLYFVSYVKLFITLIKYIPQAYYNYRRKSTSGWSIGNVLLDFTGGTLSIAQMIIIAYNYNDWTSIFGDPTKFGLGLFSMIFDVFFMVQHYILYRNSRHGVTLVNYPDQSLRDSTSPLITDSVQSSYGAIH | Catalytic Activity: H(+)(out) + L-cystine(out) = H(+)(in) + L-cystine(in)
Subcellular Location: Membrane
Sequence Length: 307
Sequence Mass (Da): 34642
Location Topology: Multi-pass membrane protein
|
A0A238FG24 | MTTSTPPNELLLLVFLHGFKGGADTFAAFPDRLRHNLEQTEPRCEIQSHVYPPYDTRGELTVAVDKHVSWLTHLVATQKGEYTQRGGTGITRVILLGHSMGGLVIADSTLSTLGSLPILGLICYDSPLLGLHPAVFRNTFDKALGYASQGQAALSALTAGYGFIRSTTGNASASSSGSGKNTPPKDGKKSSEKIVSNSASSNASSSKSKSWFSLATVAGVGAAVGAIGAAGAAYYNREAIGNHWSWATSHLSFVGELWKTTEMEQRIHHIVEAQEKGVGFHWSVLPPSSGVVDARQIAQSCRSSRPLHSFYAHLPPKNDL... | Function: Involved in inositol deacylation of GPI-anchored proteins which plays important roles in the quality control and ER-associated degradation of GPI-anchored proteins.
EC: 3.1.-.-
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 413
Sequence Mass (Da): 44319
|
A0A0R1UUI7 | MKILKYKKIVTIMAGLALMGPLAACGNRVMATTSGGKITQDQYYKKLKQSSAGQEVMQQMILDQVLEKQYGKQVTDKKVNAQFNSYKDSYGAAFNTMLQQNGMTAQSFKDRLKSQMLMEAAVRADSKFTKSALEKQWKEFQPKVSTAMIVVNSQSDAQSIIDEVNGASNKLSTFKKLAKSKSIDDSTAANGGVMPAFDNTNSTLPENVRKAAFELQNGEVTAEPIETENGYYVIYMIKHPAKGTYKQHINDLKDQIVTKNMNNQAFAKKVVAKALKNGNVSIKDNDLKGILSGYLTPTTTNNK | Function: Plays a major role in protein secretion by helping the post-translocational extracellular folding of several secreted proteins.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
EC: 5.2.1.8
Subcellular Location: Cell membrane
Sequence Length: 303
Sequence Mass (Da... |
G0WG33 | MCSKASLFKLLILTICPLTLLIGYIISQYLTRSGIIMVNTVDKDGLINTLFVKKGWFWTTLVGWFCIYRYNNRRPDFQKILWKAFKHYCVLTCWWYAFTQSIFIYPPLMDLIFLMTGGLCNFDVFNIASDGKIELNLEFQDNSTRRMKSLNKIYKILKRTQRDATGDDEKELLLHSLNSIGCALEKSCDKINSTISSISSNRKLNEFINTQMNSIRRINTSAQCRMHGGYWTKGHDPSGHIFLLTLMVMFLSGELSTFAPRAFKVLFQRKKIFHLVEYVTKLFDNGLLWDVAKMRDEERKNWKVILHRAVVLQPIICLRD... | Function: Fatty acyl-coenzyme A (CoA) diphosphatase that hydrolyzes fatty acyl-CoA to yield acyl-4'-phosphopantetheine and adenosine 3',5'-bisphosphate. Preferentially hydrolyzes unsaturated long-chain acyl-CoA substrates in the endoplasmic reticulum (ER) lumen. This catalytic activity is required for maintaining ER st... |
A0A2R8C0L0 | MNRSFTMCLRAACLCLVCVVGLAPEGRAQILPAPSRPAMSLPVPPGSAAILSEEGEIIALPSLAEREVEDARIVLLLGTPDTAGSDVIALPGQGPDRQAPQASGQPMHLAALWPRRAGMTAGTRVRLTGERDAVEFLLFVDDPRGVSEIVLTTQSSAYVFPERSRVSVTIGQTDLASFAPGNITEAGRIAFEVPPGALRPGPNLLRVSVDHAHRIFCGAEAAYDLWTEIDLSQSGAQLAGRSIGSGAAGFFTAAGIARGTGDPIHVLGGADRAQVLDVLARLGHVMNGDGLSFSFEAPEGTDAAAPLIRVEPGAQSQVRF... | Pathway: Glycan metabolism; bacterial cellulose biosynthesis.
Function: Binds the cellulose synthase activator, bis-(3'-5') cyclic diguanylic acid (c-di-GMP).
Subcellular Location: Cell inner membrane
Sequence Length: 768
Sequence Mass (Da): 81100
|
A0A6A3CL43 | MLPTVVEGQLAHETQLALVRAYVPFLHLSAASSPLLTGDQGSLSQALPSLPRRCRYNLVPRASKDVPYSFRFPPMTKKPRCISSTPLLGGLLTYPFLGVIGSLPSWFLMAYFFVAYLGIVRRKEWPHFFRFHVVMGMLLEIALQVIGTVSRWMPFAIYWGKFGMHFWTAVAFAYLFTVVECTRCALAGMYADIPFVCDAAYIQIPYD | Function: Involved in protein precursor import into chloroplasts.
Subcellular Location: Membrane
Sequence Length: 207
Sequence Mass (Da): 23388
Location Topology: Multi-pass membrane protein
|
A0A8B7P532 | MDHFRNTYETAKCVRDIANFTRHFATKIYDDPVVKNIIAKRNEFDLVISDQFAFLVTYPFAVNMTHILFTASYLTPLMSAYQGNVFNPAAVSNGVTDYPKPYSFLSRVKNILVTLFFAYIWLWSVRSPAEEAISKIFPGLPSSYEVERNASLVFFHSHLALDGAFPLLPNQIMLGGMVARDPEPLPKDLQDFLAGDIPAVYMSTGTYVTVSNFPDQFKNIFISLFPKLPYKILWRYPSDEVLNSSNLMVRNWFPQQDVLAHPNLRLHISHCGLSSVQESIYHVVPILCLPILGDNFKTAPFVQDEGIGMSLSWLTLTEQT... | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
EC: 2.4.1.17
Subcellular Location: Membrane
Sequence Length: 437
Sequence Mass (Da): 50312
Location Topology: Single-pass membrane protein
|
I6N4E5 | TLYFIFGVWSGLLGTSLSVIIRTELSMPSSLIKNDQIYNTLVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLNFLLLSSMVESGTGTGWTVYPPLASNLAHMGKSVDLSIFSLHMAGISSILGAINFITTCMNMKLKSMKLDQLPLFVWSVMITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFW | 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... |
A0A0E9NKR0 | MITSRTNQRWIEDSRGHRACPTHHQHAHSINPSTTTRSMTSALFGDDDGHRAPSSLFGSSADEHDPWGLPVPKSRKRRHVGSLLDGVTLPDIYEQAYVAANPRPSGILPLSSLRTILDSSHLAPHVLNKLLTLVLPDDGEIGRGEFVVAMALVGLAQEGEDVTLDGVHERRKDLPIPKLDLLKPTPPEPEAKPIPETGVSATLIPDRPTSARPPRTPAPIDNPEHNPFSSSLPNDPLVPPVAPAILQAPPLTSSESQHFVRPLSQPREEEHGEADPWGGNSPGAILSTHHTTTHAAPPPPPIAASTWTSTHDTTPSIQIQ... | Function: Required for vacuolar protein sorting.
Subcellular Location: Membrane
Sequence Length: 701
Sequence Mass (Da): 77289
Location Topology: Peripheral membrane protein
|
K9SLS1 | MRAIWISFKHKSQLHFRLGIVAIVLISLLTRFWQLEGVAEIVFDEVYYPEYAQAYLNGLPQFDAHPPLGKYLIALGIQLFGYNPIGYRWVTALVGSLVPGLTCCLVYELAHQRRDRHSWALLAGLFTACDGLLLVESRYGLINIFMVAFGLLSQICIFKAMQGWALANQALGDRNIKAMPIELRRSCWWLWLMAAGIFLGAAVAVKWNGMAYGVGILIILAMFWDSAYRSRPTRITDRSINPKLSDRQQLRRSGYKLSQSHSKIDRKTLRQDQVDQQNNQPRQLIGANLIYSQRSLLICIILGLMIMPLAIYGLAWLPHL... | Pathway: Protein modification; protein glycosylation.
Function: Transfers mannose from Dol-P-mannose to Ser or Thr residues on proteins.
Catalytic Activity: a dolichyl beta-D-mannosyl phosphate + L-seryl-[protein] = 3-O-(alpha-D-mannosyl)-L-seryl-[protein] + a dolichyl phosphate + H(+)
EC: 2.4.1.109
Subcellular Locatio... |
A0A6A2XLR0 | MSYSDRKLLQVNPGDITPNIVVAQNGSGKYDSIIKAVAEVPKKNIQQFIIYVKAGVYNERFDIHKHVNYVMIYGDGTTKTVITNNVSVAFVIPKLTTFHTRTFTSSGLNFIAKDIGFENTAEAEGHQAVALRASDDIIAFYNYHFNGYQDTIYSHSCDNSIVIA | Pathway: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 1/5.
Function: Acts in the modification of cell walls via demethylesterification of cell wall pectin.
Catalytic Activity: [(1->4)-alpha-D-galacturonosyl methyl ester](n) + n H2O = [(1->4)-alpha-D-galacturonosyl](n) + n H(+) ... |
A0A6I3B9W8 | MTTRTRIVATIGPQNANADSLKELLEAGMNIARLNGSHNTLKWHEETIKQIQETSANTPILLDIPGRKIRTVLTDKPLIFKRDGLIILTTDVKRTGSNMIAVSFDKLHEFLNPGQVVFADDGTLRFEVEKVSGPEITLRASMDGQLGSRKGINVPGVDLGPVLVSEKDRTMINFAKENKLDFIGLSFVESAKHVQLIRDVIGPSDYPKIISKIENQIGYVNMQEIIEASDAIMIDRGDLSVETDLETVALRQKMIIQTAQKLSKPVIVATEMLNSMIVNSFPSKAEVSDVTNAVIDGCAATMLSGETAVGSFPVESVRAM... | Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5.
EC: 2.7.1.40
Catalytic Activity: ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate
Sequence Length: 477
Sequence Mass (Da): 51628
|
A0A6A8MV19 | MLARENRLRSADDFRSTMRTGRKAVADHMVVYLNRDGSQTQARFGFVVGKTVGVAVKRNLVKRRARSAIRERLQNFNSGEMVVIRALPGSADLDWQEFGAELDYCLNKLSN | 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... |
A0A6G0A9V2 | MSADPDTPEPDGKDATEAPAPAQSTGRSSIAVGAGILLSRIAGFLREAALARFLGIGFAADAVRAAMRIPNLLQNLLGEGVLSAAFIPVYSRIVESEDEERAGEVAGAIAGILIAVTTAVTAVVVVFARPITAVMTPGFDGRTFDLTVTLVRIMTLGLGFLVMSAWCLGILNSHRRFFLPFVAPVLWNAAQIVVIVFVGLLGWTDSSIAVALAWALVVGGLLQLVVQLPAVLRLVPHLRLSLRSKERDVRDVLRRTGPALLGRGIVQISAFADVVLASMLVTGAVAALGYAQVLYVLPISLFAMSVAAAELPELSRESEA... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Involved in peptidoglycan biosynthesis. Transports lipid-linked peptidoglycan precursors from the inner to the outer leaflet of the cytoplasmic membrane.
Subcellular Location: Cell membrane
Sequence Length: 589
Sequence Mass (Da): 62772
Location Topol... |
A0A7V9D8A4 | MRRGRGRAAARRGPGIVQAPPSAILAAGGRGERSGSSVPKQFRALAGKSVLARSLDAVLSSGCRPCVIAVPKDRLDHARAEVEGISEVVVVSGGHTRQGSVRAALELVAAETVVVHDAARPLAPAALFVAVVEALREADGAVPGAAVDETLKRAHAGLIVETVERACLFRIQTPQAFRTAALKEAHFRAHRDGFEGTDDAQLLERLGYRIALVEGAGPNPKLTHPADFELAEVLLRG | 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... |
A0A7V6GJT5 | MILRNILDIDELNKTQILKIIESTGYFKEVLERDLKKVPALRGKTIVNIFYEPSTRTRTSFELAAKRLSADVLNFSPSSSSLKKGETELDTIRTILAMKADLAVIRHKDSGFVKYISENINIPVINAGDGKHAHPTQALLDLFTIYNHFKSLEKIKIAIVGDILNSRVARSDMLLFKKMDFDVSTVSPSMLLPEDMGYFNTVNFNCIDDIVEQYDVIYMLRMQFERQNKKFYPSVREYNRFFSMNLQRFGRMKKGALLMHPGPVNRGIEIDGRILDMEDDHHERIKISEQVENGVAVRMALLHYLLSNQ | Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 2/3.
EC: 2.1.3.2
Catalytic Activity: carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-aspartate + phosphate
Sequence Length: 309
Sequence Mass (Da): 35583
|
A0A7V4MYE7 | FWSRGEVPGDPAAALPGIHRVVVPGASRSGIAAAVALKRLGCDVILSDRREPRSLPGVEQALAAGARLVREEDLSLDWPGADLVVKSPGVPAEAAPVRTARERGVPVWSELELAYALLPNPFLAVTGTNGKTTTTALLGHLLKVAGRPVRVLGNIGVAVTSVVGWADPEEELVVEVSSFQLEDVCRFRPVVGVFLNLTPDHLDRHGTMENYLASKARLFMNQGPEDVAVLNLADPAVAGLGRRLAARLHGPRLAYFSVDPSALAPGLGRGGRGSEDQALHSWVGDGQLVVDGRPLLPISDIRLPGRHNLENCLAAATAAA... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).
Catalytic Activity: ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-... |
A0A0S8AWQ6 | MSRTLFISDLHLTREQPQVSAQLFRFLADPARGAAALYILGDLFEVWLGDDALAAPDGDRLAREVAAALHALHAAGTEVLLMHGNRDFLLGAGFAQACGARLIDDPARLTLGGQAVALMHGDTLCTDDVAYQKFRALARSRPFQDEFLSKPLAERRLLAQHYRAKSEQAKRATPDEIMDVTPSAVQDAFRRLAVTRLIHGHTHRPATHRYEIDGQHCERWVLPDWDRGGGYLVAEDGALRLERV | Cofactor: Binds 2 Mn(2+) ions per subunit in a binuclear metal center.
Pathway: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 4/6.
Function: Hydrolyzes the pyrophosphate bond of UDP-2,3-diacylglucosamine ... |
A0A7V6GJZ8 | MQKQVWTINKLITWAIEFFKRKNISNPRLSAELLLSYVLGFTRMELYLHYNMVPEEKQLKRYRELILKRLENVPIQYLTKEAFFRKLKLFVDERVLIPRPETELLVDEALEKLKILSLKKKIIKILEVGIGSGAVSLSIITEMKKICPEVSVEVMATEISAAAIEVADRNAKQILGEEYPAILKIFNCNILPENNSDHGDEFSSEFDMVIANPPYIKKADFENLPEEVKEHEPREALVAGSAGTEVYSAILERIHDYMNREQSFIIFETDPLVCSDLKKISENRYKNALIEVKNDYNDLARVLIISL | 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... |
A0A2A5FTU3 | MAKDATDTTPNSKSEKVILGRITGVYGVKGWLKVFSHTDPMESIVDFSPWYIRSEGRGQGSQKPXPWTEVKLKAGKRHAKTVVXKLEHCNDRDQAMAYVGTEIAVELQQLEQQREEGSYYWRDLIGLRVTNQQGIELGKVKTLLETGANDVLVVVFEEEGETKERLIPWTIDMAIVAVDIENGCIEVDWDADF | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but ... |
A0A6I2Y627 | MTNHPSTLAAQSRAAESAAALTSLTGVERHDIAVVLGSGWVPAADLLGTTVADLAVTDLPHFAPPAVEGHAGRVRSIDAGGRRVLVFLGRTHLYEERGVDAVTHAVRTAAATGCTTMVLTNGCGGLNPAWSPGTPVLISDHINLTGASPLHGAHFVDLTDLYSARLRELCRQIEPSLPEGVYAQFHGPMYETPAEIAMVRNIGGTLVGMSTALEAIVARSLGMEILGLSLVTNLAAGMSGKALNHAEVLEAGQAAAARMGDLLARVLREVEAVVVDGGIRAHGAAGDLARAQAWVHEDPDDRTRTELRGTIDAARAHDPA... | Pathway: Purine metabolism; purine nucleoside salvage.
Function: The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate. Cleaves guanosine, inosine,... |
A0A2E6LFN9 | MKGINLNINELVNVKNNAKVQNVNGWVSSIRDHGGLTFIDLRDFYSSIQIVYEQSKNMPSDIKNEYYISVSGVFKERDEELVNKNTQLGKYEIQASEINIINKSKILPFQIDNNIDTDESIRLKYRYLDLRRQSMKSNIVGRSNTFKSIRKIMDKMDVLEIDTPTLIKSTPEGAKDFLVPSRKNNSTFYALPQSPQMYKQLFMMAGFPNYYQIAKCYRDEDSRKDRQPEFTQLDVEFSNANPEIVKKNIETIVKFVFKDAYDIKIDSAFKNMTFSEAISLYGTDKPDLRIKETISDCTEVFKTTEINFLSDILNKEGVVR... | Function: Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Catalytic Activity: ATP + L... |
A0A7K1DHX2 | MKLLITGASGQLGTDLVLSARKSGHEVIAASHNDLDITDKSLVGRVVGEANVDAIIHAAAWTAVDACESDPQKAMAVNRDGTANIVAAARGSGARVIYISTDYVFDGTKSTPYIESDLPNPQSVYGASKLAGEQQLDLTIDQIVRISWVCGEHGANMVKTILRLAASNPTLTFVDDQIGSPTFTSDAAPAIVELATSGGAGIWHLTN | Pathway: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
Function: Catalyzes the reduction of dTDP-6-deoxy-L-lyxo-4-hexulose to yield dTDP-L-rhamnose.
EC: 1.1.1.133
Catalytic Activity: dTDP-beta-L-rhamnose + NADP(+) = dTDP-4-dehydro-beta-L-rhamnose + H(+) + NADPH
Sequence Length: 207
Sequence Mass (Da): 21603
|
A0A537XQF8 | MIAYLDCFSGASGDMILAALIDAGADLAAVDAQLTALGIPFELTFTTVHRCGLRACKVDISAPDGTWTVMRTYEDGLRLVQGAGLDPEVAARATSILGRLARAEATVHGVAVGEVHFHELDGVDTIVDVVGSAAAFASLGAGVVVSSPVATGTGVVPSRHGPLPLPAPAVLELLGGASLYGRTVEAELITPTGAAILAEYAASFGKMPSMTVASVGYGAGSRELEIPNVLRVVLGEPSGDSDVEPADAVEDLMVEATVDDMNPELYPFVLERLTEAGAIDAWLVPVIGKTGRPAQVIQVLAPPHAEEAVRDTLVAETSTI... | Function: Involved in the biosynthesis of a nickel-pincer cofactor ((SCS)Ni(II) pincer complex). Binds Ni(2+), and functions in nickel delivery to pyridinium-3,5-bisthiocarboxylic acid mononucleotide (P2TMN), to form the mature cofactor. Is thus probably required for the activation of nickel-pincer cofactor-dependent e... |
A0A847PK64 | MIDGILIIDKPEGISSARVVFKIKKTLNLKKVGHTGTLDPFASGLLLICLNHATKKAGYFTDLDKTYLGTMILGISTDTQDLTGKVVKVNPIKQNNIEIKDIENAFQKFQGDIWQTPPMFSAIKSRGKPLYQLARKGIEIKVAPRKVIIFKLNLLAMSWNKYPAISFMVQSSKGTYIRTLCQDIGDYLGCGAYLAKLKRIKIGNISIEQSMPLDSFLKLSEEEQKTLILSSNLTALNII | 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: 239
Sequence Mass (Da): 26596
|
A0A7J4HFX2 | MRSSMENATTSRHARSSHPHPRSDPMEILELRALRGPSIWSRYQVIHMLLDLGEMETQPSDKVEGFYGRITALMPTLVEHRCSVGTKGGFFQRIERGTWMGHIVEHVAIELQCLAGMEVGFGKTRKFGDEGSVYTVVFRYRSEEAGLEAGRIAVNLVESLIAAREFDLEAAVFSLKEIREDHMLGPSTRSIVKAAQARDIPFYRLNRDSFVQFGWGSHQRRIQATMTSQTSALGVEIADEKGRTKSLLKDAGIPVPEGYECDSWEATLENALEIGYPVVVKPLVGNHGRGITLGVANDVDLKTAYAAARMRHDYVIVEKH... | 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(... |
A0A7N0TA96 | MHQFHKLIQHLELCVLLMLLAQHIFPGCSSSASAQVLHPNCTARCGDVEIPYPFGTTPDCYLNSDFLVNCTKDSSGSPVLYLRDYGSGQVINISIDGQLRIYTYIGKDCYHQNGNQDEYNSQTASATIPRFPFSNTHNKLTAVGCDTIAGITSIEGINGCLSLCSNDTLQNIVYDGTCAGLGCCQTTIQTNLQDIEVRVTSFSNHRDVWAFNPCSYTFLAEDSYFNFSEGDLRNLNNRTQVPTVLDWAIGNDTCQDAKKNATSFVCQSNSQCVDSTNGPGYRCSCLSGYRGNPYVSGGDGCQDIDECVAIPNPCGDDICT... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Subcellular Location: Membrane
Sequence Length: 748
Sequence Mass (Da): 82671
Location Topology: Single-pass type I membrane protein
|
W3ASW6 | MDLAKMIDHTVLKADATTEQIKHLCDEAKTYGFHSVCVNTCHIDTVVSELKGTDVTPCVVVGFPLGAMLTSAKAFEAAEAVKRGAGEVDMVINVGGIKDGNYDFVRDDIKAVVEASKPAIVKVIIETCLLSDEEKVKACELAEEAGAAFVKTSTGFSTAGATIEDVKLMKQTVGDRLKVKASGGIHTKKFTEDLIAAGADRIGASSGVSIVK | Pathway: Carbohydrate degradation; 2-deoxy-D-ribose 1-phosphate degradation; D-glyceraldehyde 3-phosphate and acetaldehyde from 2-deoxy-alpha-D-ribose 1-phosphate: step 2/2.
Function: Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate.
Ca... |
Q9X0L2 | MMVISEKVRKALNDQLNREIYSSYLYLSMATYFDAEGFKGFAHWMKKQAQEELTHAMKFYEYIYERGGRVELEAIEKPPSNWNGIKDAFEAALKHEEFVTQSIYNILELASEEKDHATVSFLKWFVDEQVEEEDQVREILDLLEKANGQMSVIFQLDRYLGQRE | Function: Iron-storage protein.
Catalytic Activity: 4 Fe(2+) + 6 H2O + O2 = 12 H(+) + 4 iron(III) oxide-hydroxide
EC: 1.16.3.2
Subcellular Location: Cytoplasm
Sequence Length: 164
Sequence Mass (Da): 19379
|
A0A2C8FG30 | MPKTCVLILLDGLGDRAHALLNNQTPLQAAETPCLDRLAAMGSTGLYHAGKLGQPLPSENAHFAMFGSPKSEFPGRGVLEAIGADVELEDGDIAMLAHFTSVLTTLENYLVLKYDRICGTPDEIDALYAAADHYEKDGITIRLHKTGGMFSVLTMHGDVSPYITDSNPMVDGRFVSAVRPLATHRDDPDAIRTARVLTDYISWAYHRLSAVEQNKLRVRQTLPPINGIVTQRAGRMCPRVSMGNRYGMRALSIASGHMYGGMAKFLGMDFHKVRDTRDPGKDIAKRLEYAATRLEDYEFIHVHTKAPDQAAHTKSPKGKV... | Pathway: Carbohydrate degradation.
Function: Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
Catalytic Activity: (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate
Sequence Length: 446
Sequence Mass (Da): 49250
|
A0A3A4WDS5 | MRLFIGIGLPEAIRSRLASLSRSLAPSAPHARWVDEPNLHLTLKFLGETAEESIDRLVDAMRTAAGCVGPFSMRLDRLGMFPSARRARVVWLGVSDGARETTSLAKSLDLELAPLGYRSEARPFHPHITLARLRVPEPLTGLAEDASEQPPPVDASVSVTHVTLFESRLRRTGAQYFVVEEVPLGSD | 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: 187
Sequence Mass (Da): 20491
|
A0A3A5WEC5 | MDVRRVLLVGSGGREHALAMALTQDPRVELHTAPGNPATGRLGTNHPVGAGDVKGLIALTEDLDAHLVVVGPEAPLCDGLADALGDRLCFGPVAAHAALEGSKSFAKAAMEAAGVPTADHVIVRRAGALGDALDRFADHPWVIKQDGLAGGKGVLVSADREQAEAFALSAIATSGSVVIEAFLPGEEASMLVLMDGSGYRCLPASQDHKRVGEGDEGPNTGGMGAYCPAPVVTAEVQAKVESRIVAPMHAHLSAQDVPYRGVLYVGLMIDEHGDPYVVEFNVRFGDPECQVTMPLLGDHALEWFTAVAQDRLADVQHPIA... | Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/2.
EC: 6.3.4.13
Catalytic Activity: 5-phospho-beta-D-ribosylamine + ATP + glycine = ADP + H(+) + N(1)-(5-phospho-beta-D-ribosyl)glycinamide + phosphate
Sequence Len... |
A0A3A4V825 | MSTVIKDSTSIKAYAKALLDIAKAEGKLAEIKNDLFQVSQLFKQQSDLWSFLNDNQMPADKKSKALKEILGDNVQDLTLNQLDFLIDQGKQKLIFDFVEKFNQLVEIEENKVTAEVTTAVPIEAAEQEKIRAKLKKETGKEIELRLIVDKDIVAGLVIKIGDRVVDASVRNRLAQLHGGITSIK | 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... |
A0A538MHG5 | MAAQLRAEHRRAGELALVRLRAARALRGHADRLDAADVRDHGQVAAGDVSGAAARVRLPVHQLPDRPRPLLGDDEPLDGRPGADHAKDDAEGRPSAEALVPDTAEGGEPGPGRRRAGPTAGSGPGGRLVRTAEGAPQEEEGRRAEVTEALQVEASGETVGEAKWTALRELEKLQPGIDKAAVRFQVLTEGERGLLGVGFAPARVIATVDAAAVVAEAPPAEDDSELGGEVREILGRILEAIGIRARIEIREDDETLVATIAGGELGLVIGKHGQTIDGIQYLINAIVWRGQGDDRKQVTIDAAGYRARREATLDSLAVRS... | Function: A probable RNA chaperone. Forms a complex with KhpA which binds to cellular RNA and controls its expression. Plays a role in peptidoglycan (PG) homeostasis and cell length regulation.
Subcellular Location: Cytoplasm
Sequence Length: 372
Domain: Has an N-terminal Jag-N domain and 2 RNA-binding domains (KH and ... |
F3LBX3 | MNKKSIRILLLGASGQVGSECKKLFQQVGYTVLCITRKELDLSSISSVDEIVERLLCFQTPSLVVNAAAYTAVDKAESEPSLADKVNHTSVGFLAQYCAKGAIPLIHISTDYVFDGTATTAYTESDDVSPLGVYGETKWLGEQAVKSVLAQHIILRTSWVFGISGNNFVKTMLRLSADREQLTIVSDQYGCPTYAGDIARAILCIVKRYASGQSLNWGVYHCVGEGKVSWYEFSQAILNEAYARGFMPNKPQIIPIPSSAYPTPAARPAYSVLSTDKLAREFNYSVPSWRQGLSAFFDGCSPAL | 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... |
A0A3C1P4L1 | MSDGADVVHDSPPAEQRRSFDRLVNFTDAVVAIALTLQLLPLTEIPGPQDGETVWQVLAENWGQIFAFLLSFIIVIVMWTVHNRLFNVLRTYDATILWLNIAWMLAIAFLPWPTAMYGNANSSEVVGGGGVGLLYWANLALISALGSMIAHHARRHPELLEPGALSRGWLAQTSRTRWRGLAFTTYLLMVGVASELLGSHTGWLALGLFPLGRFFSDRTAPAPEPHSAQAASE | Catalytic Activity: K(+)(in) = K(+)(out)
Subcellular Location: Membrane
Sequence Length: 233
Sequence Mass (Da): 25574
Location Topology: Multi-pass membrane protein
|
S7W7X9 | MYTPTMSKYSVLFVCEPIIDIFIKYNDKLMKKYNMSVNGFIFINDYSEFDKCLEIGKNIGGTSLNTFSMIKSNGIFIGAVGKNCTFIENALEKIDKKYFLEKRYKKTMTCYIMIKDCFRSMATTQPLKLSIDFIQERINDILKYNIFYLSLFMYFSNKEIIDFILKLNHHMLVLNLAPIIENYKLFDEIQLIIERSKIIVGNREEFKKLSKLFFKVEENNYTDNILEEYFQVNSKTTFLICTDGDKDIMYTDNNNIYYLKPKKINEKDIFTCGAGDAFCAGVLDAFIEGKSSKNIVENGYKYSYEWIIKKTKEYKDNLKK... | Pathway: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenosine: step 1/1.
Function: ATP dependent phosphorylation of adenosine and other related nucleoside analogs to monophosphate derivatives.
EC: 2.7.1.20
Catalytic Activity: adenosine + ATP = ADP + AMP + H(+)
Sequence Length: 324
Sequence Mass (... |
A0A1M6P9Q8 | MKDNNKKNVNPAPTKGKSLKKRNRKKRVLKIVLISFLIFFAAVFIIGGAIFLGIAKTAPDVDLKVICTFNEPSKFYDDKGVLIDEYLTTEQREPVSYNNIPKLLRESFIAIEDERFESHNGIDFKRLIGATIGNVKSLVTGKKNFTGASTITQQLIKQKYFLQSSLDDRLSFTRKIQEMSMAVELEKKLSKEKILETYMNTIFLGGSAYGVKSAARQYFNKDLDQLTVTECAFLASCAQSPTVSFGAAKYAYDKKELHESPRTKIVLKKLLEKGKITQEQYDKAIVPQLSYSFKDTLRSKMKYEWFSRPVIEQVSADLKK... | 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... |
A0A7K3L212 | MGDAARERFGVIVHEAQPARPGNEGPETARRATIDADGKPGAASADGAGEAGGASETDARDAGADAAERARQARCRACYRLRFEEAAAYAAAHGFDALGTTLSVSPYQYTAVIHEELARACARAGIAARFDDWRPYYDEATRRSREEGLYRQNYCGCRFSDEEAAAERALRKAARAAKRAAERDAHAAEHAAAEEQRAARRAEKEAYAAKRARQRAALKALRAQGGAASGDDPAKPDAR | Pathway: tRNA modification; tRNA-queuosine biosynthesis.
Function: Catalyzes the conversion of epoxyqueuosine (oQ) to queuosine (Q), which is a hypermodified base found in the wobble positions of tRNA(Asp), tRNA(Asn), tRNA(His) and tRNA(Tyr).
EC: 1.17.99.6
Catalytic Activity: AH2 + epoxyqueuosine(34) in tRNA = A + H2O ... |
A0A2G8JI94 | MPKTSHETQPQSLSPEQIQRMQAKKDAALQRLAAKNTTGIPEGINSSWAKALSNEFSKPYFLKLQDFVSKERQSYTIFPPPHQVYTWTQMCDIRDVKVVILGQDPYHNVRQAHGLCFSVPQGIQPPPSLQNMYKELAKDIKGFEHPGHGNLTGWAKQGVLLLNAVLTVRAHTPNSHKDKGWEKFTDAVINWLNKNQEKIVFMLWGSYAQKKGAIINTKRHCVLKSTHPSPLSAYRGFLGCGHFSKANEYLQKSGKKPIDWSSLND | 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... |
K0P9X3 | MLHSAYSFSLLRLLFASKKVTAMEVVDHLLQHIEIQKDLNAFVNVYDQEIIENAVLVNQKIAHNQGGPLAGMVVGLKDMIAYKDHPLQAGSKILTNYISPFHATVTQRLLAADALIIGHQNCDEFGMGSSSENGYFGTVLNPLDKTRVAGGSSGGSAAAVKAKMCHVSIGTDTGGSVRQPAAFCGLVGLKPSYGRISRHGLVAYASSFDTAGILAHTVEDCASVLEVIAGADPFDSTASAREVPCYTSVLHDSARYKVACLAETLSHGGLQPEIKDHTLDGLELLKKAGHQVHNVHFELLKYALPTYYILVNAEASTNLA... | Function: Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln).
EC: 6.3.5.7
Catalytic Activity: AT... |
A0A3P8X594 | MAWKLWGHVPLLRKNLFNCYLRWREAVTTFSSRVGSMFTLSSKKDRNIFLFSLMERKTSQIKHMFVGILGLATIYIIYINTDRRWEMWNRPQVSYVSNNLSENIEEYEEPEFEDPGPYHVAYPKRYPVVMDNTYVCRTKNPFLILIIPVAPSNVEDRDAIRQTWGGEKMVHGQERRRERQRQLRWENEQHHDMIQSNFLDSYRNLTIKTMFMLEWVVENCRNTSYIMKIDSDMLVHVPNLVKLLVDSRTPEENYMSGLVWWHSPVLRDPGNRFYLPPEVITEPEYPPYPLGMAYIMSLDVPGKLLSVSTHIKPIYIEDAY... | EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 382
Sequence Mass (Da): 45077
Location Topology: Single-pass type II membrane protein
|
A0A3E0PWG5 | MLTVVWVAVGGAVGSVTRYWISASLNAFAYPWGTVLVNVVGSFFLGYLVGRWGFGDPTPVRLGLSVGLLGGFTTFSTFTLDVVGLWEAGRITESVFVVAVSLVLGVGAAVAGLVVGRA | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Subcellular Location: Cell membrane
Sequence Length: 118
Sequence Mass (Da): 12198
Location Topology: Multi-pass membrane protein
|
A0A2E3JSC6 | MVSTKKAYSTDKFFILGIGGSGMSSIAKYLIEAGSTVVGYDQRKSQITNQLLKLNIDVTNDVNYEIPEGSVVISSSAITSNNKLLLQANNKGMNVITRPDFLSNLTKQYKTIGIAGTHGKTTTTALLSHIYQYNNIDCSYIFGGMTSYSGIGGHFGNGGELVLESDEAFKTYLNFEHDSLIVTNIDDDHIDHYGSFDLLIESFFSVIEKTKLKPILNIDDKNLYEISQKIDSISYGRNPESEYRYLGNKKIVRNGTEIEMNPRVPGDHFIMNSLAALANADINGFELDKTVDAINTFSGVKRRTELIGTSNGVSIYDDYG... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Catalytic Activity: ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine
EC: 6.3.2.8
Subcellular Location: Cytoplasm
Sequence Length: 444
Sequence Mass (Da): 48857
|
A0A537YSJ2 | MAAEHMVDVEVLTPEGEVWSGEARQVSTRTEVGEIGILANHAPVLAALRPTELRLHVSDSETKTYAQAHGWLQVYGNRARLLLEEAIPPEDLDSGTLKEQLSDAEQRLSECEEGSAEHNRAQKDRDRAQAFLSIAGG | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane.
Subcellular Location: Cell membrane
Sequence Length: 137
Sequence Mass (Da): 15029
Location Topology: Peripheral membrane protein
|
A0A7V9SFD0 | MSDHILIYGLRVEARVGVGEQERSRPQWLVANIDIAIDLAAAGESDDINDTVDYGVLTTEIADLLRGTETRLLEHLAEKVVALIAPNKAVVGVTVEIFKEAPPIAEQLGGVAVRLERAFI | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 3/4.
Function: Catalyzes the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin.
EC: 4.1.2.25
Catalytic Activity: 7,8-dihydr... |
A0A7V9EK81 | MAASVRTRIAPAPSGSIHVGNARTALYNWLFARGQGGVFVLRVEDTDQSRVSEESYQAVLEDMRWLGLAWDEGPEAGGEFGPYRQSLRSDRYDAAALSLVDAGHAYRCYCTPAELAERRKAARGSQAAPGYDGRCRDLTERQRSAFDAEGRSWSLRFRVPEGRTITFDDVIRGTIATPTSQIPDFVIKRSDGSPTYMLAAGIDDALMAITHIIRGEDLIAATPRQLLLREAMAIEDVPVFAHLPLLVQPDGKPLSKRWGDVSVGAYRKGGFLPEAMVNYLALLGWSYDDRTNIFTVDELIDRFSLERVARNPAAFDVAKL... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).
EC: 6.1.1.17
Catalytic Activity: ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-g... |
A0A4P5RYW6 | MEPPSTTQPRIVLASRSPRRVELLTKLLDEAFGEGEMPFDIEPADIDETPLEFETPIAHVQRLAQGKAHVIAQQYKDLDVIVIAADTTVDVGGEIYGKPENLEDARRMLGEMSGRTHRVHTAISVVRGDRQAHTVDTASVTLVHITPELMDWYLGIGESLDKAGAYALQGDGRKLVETVQGSFTTVVGLPLEPLSDLLEKCGLSWKIGA | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: H2O + UTP = diphosphate + H(+) + UMP
EC: 3.6.1.9
Subcellular Location: Cytoplasm
Seque... |
A0A6I3GW78 | MIEQEVIELLAERVGLRDQVKILTDQAMAGEIDFREALLKRVGLLEGLNAKVLEELLAEIRITHGVPELISAVHNSGGLVGAISGGFSQVLELLSAKLNLDFFKANNLEIENDVITGKIIGEIVDAEVKARTLLRWAGEYGFDLSSTVAVGDGANDIQMLKASGFAVAFRPKEVLRDHADLIIEGDSLEPLISVLELRPS | 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: 200
Sequence Mass (Da): 21683
|
A0A521XND3 | MVARAVDRRVGRRRPRPGGALGGRVNPSTAFAQVVLDELIAQGIDHVVLSPGSRSGPLALALAAAEAAGQVQLFVRLDERSAGYLAVGLAMSSGSGRPVAVVCTSGTAAVNLHPAVVEASYAGVPLVVVTADRPPALRGVGASQTIEQRELYGGAVRSFVEFAVPVRAVGQVGQWRSTVAEAVRVATGFPPGPVHLNCPLDEPLVPQLRPDGSGDPDWPEPLSSGQADDDSSTRDRPAVRDRRPVRDRVDLAQWCRLFGLPAVPPRGVVVLGRGSDPDGRRDAVALAGRLGWPVLCEPPATPPEDAGDPQAPGQGQVIRH... | Cofactor: Binds 1 thiamine pyrophosphate per subunit.
Pathway: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 2/7.
Function: Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting s... |
A0A7K1D926 | MIDVSNLSSINIDEKSVIHYVNQMLKFLKVNPKSDVSILFVDEDEMTKQHVRWMNEDGPTDVMSFPMDNVLLANSKSLKKQATLGDIIICPSVALKDARKQSINPAYHLVFLLAHGILHLLGLDHQEKSQRGVMQKKEQGIMNSLRTVKKH | 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: 151
Sequence Mass (Da): 17120
|
A0A3P8X2L8 | MRRTRTSRNKSQCVKETEESRLKTVWQWRGDDGQWEAYSPSASAMLDSAVSSGQTSFTLTLDSGASYNVDLKKMVQINPVTKYKRKIRCQKVKQEVLNESSDLTVSHDTVVQIKEELKEEEREEEEKEQPAAKRKRSQKNEKTPDGETECDAVRTVVMKGKAPVDPECKSKVGKAHVYCEGSDVYDVMLNQTNLQFNNNKFYLIQLLQDDSSKVYSVWMRWGRVGQPGQNSLVACGSDLLKAKNVFKKKFSDKTKNEWEYRETFEKVPGKYDIVYMDYNTDEKKEEKLGSTSSTEVQKKPSRLNPKVQSLLQLICDLKAL... | Pathway: Protein modification; protein ubiquitination.
EC: 2.4.2.-
Subcellular Location: Nucleus
Sequence Length: 653
Sequence Mass (Da): 74190
|
A0A7V9NR68 | MPSRRVTAGLVVGVGILSVAVDQIAKTIAENNLRDHSIDLVLGARFVLTYNSGAAFSVGTGRSGVFTVLASVTVTLLLVYALWARQSRLRAVMFGLIVGGAAGNLFDRLFRPNGGRVIDFVEIARWWPVFNVADVSLFFGIVLMLFVSMREPERSRS | 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-, ... |
A0A7V9NSX4 | MSRTGVLVLAHGTPARPEDIEDFYTRIRRGRPPTPVELAELTRRYEAIGGLSPFAERTTVQVDGLRAALDAERFEVRLGQKFVAPFIPDAVEDLIAADVDRIVGIVLAPHYAPPSVGDYTKRARDAIAERVPVDVIASWHNEPALIELLAERVRDAWIDDAVLIVSAHSLPLAAIGDDTTYGDALEETARLVARSLGVTNYRVAWQSAGVSGGAWLDPSLLETIREEAAEGATAVVVCAAGFVSDHLEIAYDLDIEAKAVADEEGVAFARTRSLDGDPAFCALLADLVTRAASGASSPPLVS | Pathway: Porphyrin-containing compound metabolism; protoheme biosynthesis.
Function: Involved in coproporphyrin-dependent heme b biosynthesis. Catalyzes the insertion of ferrous iron into coproporphyrin III to form Fe-coproporphyrin III.
Catalytic Activity: Fe-coproporphyrin III + 2 H(+) = coproporphyrin III + Fe(2+)
E... |
A0A7W1RVS6 | LILVTLALVAFGLVMVYSATSASATVGGSDPGYYLKRQAIYAALGIVLMMVAQRWDFRRLRALAPILVVGSLGLLAAVLVIGPPINGARRWISLGPAVFQPSEFAKLALAIWASAYYARHPAPRDLRELWRPVGALSAVFCLLLVVEPDLGTTIALTLMLVGILVVSGTPGRTIGAALGLVSAAGFAAIWTKPYSRERFFAFMHPTHDAQGIGYQILQAKIGMGSGGLFGRGLGNGVEKIFYLPEAHTDMILANIGEELGLVGVTAVILAYAVFAFSGFRISMRCKDPFGKRLAAGLTTLVAGQAAVNIAAVLGVAPLTG... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Catalytic Activity: [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-... |
A0A6I2YAM2 | MARLGILGGTFNPPHNAHLGLARAARDQLDLDRVLMIPAHVPPHKPVEDEPGAEVRYELCVAACDGEQGIEASRIELDRDPPSFMVDTLEQIAAENPGDELFLVLGEDAAAALASWKNPERIIELTTLAWAARPDHVVPEAEERVLSALEPFGPTQTPIRLEMAPDSASSTQVRELCQQGASLGDLVPGSVEKLILARGLYRGVLQMSSTTSSNPVLDGPAMAAEIVRFAHDKKAVDVLELDLRGIVDYTDGFVIATARSDRQAKAIHDGILAGMKKEHGISARRIEGLPEGRWVLIDFIDVVVHIFQAEARELYRLEKL... | 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).
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NA... |
S4SML3 | YLALFWAFLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAA | 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... |
A0A926HVI9 | MTRTTALTENREFKRAYARGKTRAGKYLAVYCFRNRRNAGVNRYGLTVSKKVGNAVQRNRAKRLLRESLRLLEPRMKTGYDLVLVARTRILGARCQQVQSAMEEIFTEFGLIEGPRHD | 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... |
B5E7Q4 | MQLRFGIRTKLLLSILAILFVSYSTLLYSSMKTLNASLQTELDRNLATNLKYARSQYLDQAEIAKFSMMQAVVSQTVQQRLRERDSAWFSTRIKRWHDVLPFVDLVVVVDPQEKVLATLQGPEKNGPMELPAMVKQALASKRAILSTELLSGEFMCRAGVPGYCERPGSEALVATVAVPVIGTDGSVLGCVVTGDILNHHPNLPGKLQEVTGNNVEVTLTQRGLRVASSLPARVRESYILSPKVLDVLERGEVYRGRTDMGAKSYETIIDPLLNSRGEFVGSLSVAISTETVTNSRRENLQYILASAFLGIICSFAMAYF... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 754
Sequence Mass (Da): 83748
Location Topology: Multi-pass membrane protein
|
A0A7K1D819 | MDVVVGRLGRPHGVHGEISVEVRTDDPENRFAIGAKITLKETNQVLTVAATRWHLSRLLIKFEEIQDRTQVDKVRGKLLVVEVDPSQTPTGNNEFYEFQLIDLEVFNQKNEKLGVVKEVLPGSAQALIVVKTPENKEVMVPFVNQLVPEVNIKNKRIVMNPPSGLFDEENAEDAR | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but ... |
C8XAL8 | MPLPTVDHPTQSGQPSRPHRRGRLTRWRRDLLGPGGLRILAAAAGGYALYQAFAPSTRWWLAIVGFTLLGLALDRRGWRAGLGLAFVFGLTFYIPLLSFTNIYVGDFPWYALSVAEAVLTAPVGALVAAASRRLPLWPAWAAAAWITGEALRGRIPFGGFPWGGIAFSQPDGPLLPAASLVGSVGLAFLTALAGFALAALIGELIGELIGALGARPRPPWRSVAVLGSGALLLVPFVLGVLGLSTMQRGTDAPTETIAVIQGNVPRPGLDFNAERRAVLDLHAQQTHQLAAEVRAGRTPAPTLVIWPENSTDIDPYRNAD... | Pathway: Protein modification; lipoprotein biosynthesis (N-acyl transfer).
Function: Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation.
Catalytic Activity: a glycerophospholipid + N-terminal S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipopr... |
A0A538HZN5 | MAGPATLTERIIHDHLVAGTDEELALRVDQILLEDATGTMACLQFERLGLDRVAVPTVSYVDHNILQFDNKNPEDHAYLRSFASRYGLRYSRPGNGISHYLHLERFARPGQVLVGADSHTTMAGALGMLAIGAGATEVAVAMAGHPYVVERPRVVAVELRGRLGPWVQSKDVVLELLRRRDVRGGRGCIFEFFGDGVSSLTATDRGTICNMVMETGATTGIFPSDEQTRRWLAAQRREDEWVALAADDGAVYDEVETIDLATLAPLIALPSSPGRVVPVTDVAGTPTRQVCIGSSVNSSYEDLALVAAILRGRALPAELD... | Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate from oxaloacetate: step 2/2.
EC: 4.2.1.3
Catalytic Activity: (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = 2-methyl-cis-aconitate + H2O
Sequence Length: 649
Sequence Mass (Da): 68455
|
D7DR03 | MKRLVIAGTSSMVGKTTVSTGIMATLSKKLNVQPYKIGPDYIDPTYHTTATNNHSRNLDSFFMNDVQIKKLFAKNSKRADISIIEGVRGLYEGLSPYNDVGSTASVAKSLKSPVILLIDARSLTRSAAAIIKGFKSFDEDINIQGVIFNKIRGEKHYEKLKDAVEYYDKEIKIIGAIPRSEELTVSQRHLGLVPTPEKKNEMASQIGLWAETIENNLDMELLKEISDVDFEADFEFDNLIPDSEENILWDINKNKCKIAIAHDEAFNFYYWDNVDALKDNGAKIEFFSPLHDSEVPDSDIIYIGGGYPEIFAKELSENKD... | 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. In... |
A0A538IDB8 | MPLTVQVVTPEREVTVCDDATFVLAHGIEGDVGILPGMAPMLIALGVGPMKIEEGERDSQLLLDGGFLQVKDDRVIVLAEYAILPEEANAQQVSDRIEDLKRKITAEAEDEHAKRELARQEALHRMLRM | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane.
Subcellular Location: Cell membrane
Sequence Length: 129
Sequence Mass (Da): 14286
Location Topology: Peripheral membrane protein
|
A0A2G8KDP5 | MMNQATAELYYTTNYVEDYFDCIESLPNDLQRNVSQIREVDSTFRSILKQTRQYYEELTTKELDPQSRKRVLLQLHRSLLRSQELGDEKLNLASQIVEVVENRLRQIDVHKGHVEMAEKPKPVLESNKDKSHKAKREVENGADRSSKRPRRHRNDNEKEKEKEKEKEKEKQKVPVTTTSTENIKSKKKKRSKKIERDPSPINVPIDPNEPTYCLCNQVSYGEMVGCDYKDCLLEWFHFGCVGLNHKPKGKWYCPSCAPLVKKK | Function: Component of an histone acetyltransferase complex.
Subcellular Location: Nucleus
Sequence Length: 263
Domain: The PHD-type zinc finger mediates the binding to H3K4me3.
Sequence Mass (Da): 30839
|
A0A7C3U9A4 | MAADGAGRVRRFSDRLADSILRRRSVVCVGLDPVLERLPPQVRPQAAATAAAEAAAAVAAAFREFCCGVISAVADVAACVKPQAAFFEQYGAAGWQALADVVRCAREHDLPVIVDAKRGDIASTAAAYAAALFDGAPGPQGPLAGLGADAVTVNPYLGEDALEPFVARCAGGHGVFVLVRTSNPGAAGLQELDAGGRPLYLRVADLVARLGAAHVGEHGYSDVGAVAGATAPTSLAAVRQALPQAFLLVPGYGAQGGGAAAVRGLAAGDAAGLVVNASRSVIYAWQQDGGDYRRAAARAAEAMRDELARVVW | Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
EC: 4.1.1.23
Catalytic Activity: H(+) + orotidine 5'-phosphate = CO2 + UMP
Sequence Length: 312
Sequence Mass (Da): 31678
|
A0A7V8WN41 | MRVVVKNVFKRKDTIAYPEVRRRPYPRFKGRHILDRHPDGLEKCIGCELCAGVCPADAIFVVGAENSPGQRFSPGERYAQIYQINYLRCIFCGLCVEACPTEALLMTTEFELSSYSRAESILTKEQLIVDEPIRRHWPTTKELPPDVNVLAEMAKAGYQANDETNVADEHSRAAAGTGSSQSGDEAKR | Cofactor: Binds 2 [4Fe-4S] clusters per subunit.
Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (fo... |
A0A3P8VF40 | MPQSLFFFPKCPHLIPRHQIQGQRRKKSATPVLRITQLDALELDSSLEQLVWTQFSQCFQNFRPGILTPVEPELRTLLHLLLWRFTLYSKCASVGQSLLNLHYHNTLFLQQGLRCLTLVSGIAQLANLVNFLIFIRKGRHPVLAERIVGAQAVSTQPNMIRDIDYQFMNRELLWHGFAEFLIFLLPLINTRKLKATVSSFVFGGDRARGEGTTEGQQLWKECGLCGEWPTMPHTVGCRHVFCYYCIKSHSIADTCLTCPKCGAEAGQPQPVKMNVEMTEM | Pathway: Protein modification; protein ubiquitination.
Catalytic Activity: [E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-cysteine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-S-ubiquitinyl-L-cysteine.
EC: 2.3.2.36
Subcellular Location: Membrane
Sequence Length:... |
A0A926DG25 | MENKTLERVQAASPAEVKHPRKRRPARGGQTDALGSLRALWKRSEPLRLSCLLGGITFVVALLLGIVNAVTAGPIAQHAEQRKQAALTEVFPEADRFAVVDIDLPRSVSEIRSVYAGDELLGYGVSAAANGFGGEIEMLVSVDAQGQVAGVSVLKLSETPGVGTNAAAEQQLALYNGKSGTIITEKITHNQPNEVLAVSGATITSKAITEGVNAALEAVRLAGREVS | 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: 227
Sequence Mass (Da): 23760
Location Topology: Single-pass membrane protein
|
D3UFP8 | MIVATHLLEEFIDISHLDIQEICKVLDNIGLEVESLTRVQMPRNVVVGKVLEKNPHPDADKLSVCQVDVGKECLQIVCGAKNVDTDQFVAVALKGARLEFDGRVLEIGESKLRGVNSYGMLCSSTELGLGKINEGIMLLDHSIGELDLGRELCDYESFQGYNLEISLTPNRGDCLCVLGIARELKAYFGLKLKKSREYMSTNQIGVGRKFQVAMENKISASLFYKVVDFESKTLPLKLGLALANAGILKKGILENYLAYITYMTGVILNAYEADALRKDQNQANEILWLHVREDEKGFETIYAEERLSNIGIGNVIHQDI... | 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: 782
Sequence Mass (Da): 88349
|
A0A920L8X7 | MISVSKESNNLVQDLIDNFETYNINLLKGFDDCTIIDAGINCPGSIECGRVVSEICLGGLGRVHLLNTFQSKSWPFSIHVNTKHPVISCLGSQYAGWNLKSNLKSEKFQALGSGPARALAQKEEIFDHINYKDKFSRTALVMEVDSIPPEDVVKKIIQDTGVEGKNLTIIITPTTSIVGNIQVVSRVLEVALHKSHELGFDLSKILDGVWKRTYTSKFQ | Pathway: One-carbon metabolism; formaldehyde degradation; formate from formaldehyde (H(4)MPT route): step 3/5.
Function: Catalyzes the hydrolysis of methenyl-H(4)MPT(+) to 5-formyl-H(4)MPT.
Catalytic Activity: 5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O = H(+) + N(5)-formyl-5,6,7,8-tetrahydromethanopterin
EC: 3... |
A0A7X7E7Y1 | MSHRLQGTVVLGIGTDVLSVQRMRSCIDSPAFVNNTFTEAEVEMGVSRGDPAAYYAKVFAGKEAVFKCFGMEADALRSWTEIEIVDGGQGQPVVRLRGQLEALAEAREVREVLISLSYDTDYAVGFAMLTGEAGHGD | Function: Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.
Catalytic Activity: apo-[ACP] + CoA = adenosine 3',5'-bisphosphate + H(+) + holo-[ACP]
EC: 2.7.8.7
Subcellular Location: Cytoplasm
Sequence Length: 137
Sequence Mass (Da): 14808
|
A0A7X7PNL3 | MSGARRFCPSGPLRGRVRVPSDKSIMQRALVIGALCDGPVEIVTPVWAGDPLTTAGMIADLGVRVDGLDAGTGPAVIHGVGLRGLRAPDRPLNAGNSGTGMRLLAGVLAGQHGRFVLDGDQSLRRRPMGRVVEPLRAMGVRIAAREGQFAPLTITGGSVTPISYRPPVASAQVKSCVLLAGLYCDGETTVAEPLPTRDHTERMLAAAGVPVRCRDATVSLTGVPALHLDRVAVPGDPSSAAFLAAAALVVEGSEIEIADVGLNPTRLGLFEVIRRMGGRVSWEATSSVGGEPRGVLCAAFSRLGAVCVTAQETAAMIDEV... | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7.
Function: Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-ph... |
A0A0J6CTH7 | MNYATFAAGCFWGVEALFQQLNGVISTSAGFTGGETINPSYEDVYTELTGHAEAVRVEFDPSLISYEELLEVFFDNHNPTSLNRQGEDIGTRYRSAVFFHTEEQESAALIAKGKLSSSGRFKKPIVTQVVPATTFYRAEEYHQSYLAKRGQSSCKIS | 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... |
A0A7C3BRY3 | MMSMYDDVEKILYSKESIQKRLQAVAKEMNALYSDADLPLLICNLKGAFMFLADLVRYLDFRHELDFIETSSYGAGTASSGDVRFLLDVGESITDRNVIIVEDIVDSGVTLSCILERFEARHARSVRVAALLNKPSRREIEVPIDFCGFVVPNEFVIGYGLDYDQQYRNLPFIGVLKPAVYQGS | Pathway: Purine metabolism; IMP biosynthesis via salvage pathway; IMP from hypoxanthine: step 1/1.
Catalytic Activity: diphosphate + IMP = 5-phospho-alpha-D-ribose 1-diphosphate + hypoxanthine
EC: 2.4.2.8
Subcellular Location: Cytoplasm
Sequence Length: 184
Sequence Mass (Da): 20748
|
A0A2E5EUB8 | MKKFNVQNTYQLPISGKPSTQVNVLADPDVISVSPESLSLIKPKLLKKQGEKVQIGTPLFFDKRNPDAIWVSPAAGVIKEIVYGPRRVILRVDIERDKKEAVVQHETLDDAALVAMEREALVDRLIQGGLWSSLMVYPFKVAPKKEVVPHNIYVTVDQDDPFLPESDVYFDGQTEAFLLGVTALKKLTTGQVFVGVSNENQVVYPKVSSVVTHIIEGAYPANDPGVFIYHNKTDQKDNSAWGLRAQDVIRLGQFLSTGTYPIDRIYTVGGPMVKSPCHVKSREGVSVEHLLSGFSLTKGKTRFILGGILTGRQADKASAL... | Function: NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE are probably involved in the second step, the conversion of ubisemiquinone to ubiquinol.
EC: 7.2.1.1
Catalytic Activity: a ub... |
A0A7M3WS36 | MIPSSTFEPRARQIRPASSTSWLPPSPQNSPAPPSEEDAPVSASGQHHAEAIGLTGYATVADGIGGLVKTRVEDFRVEELSTKLSMDQRGRFTVASITLRNWETNRFIARLAKALGIPKERIFFAGTKDKRAITRQLFVIDAPANKVNGVELTDVDIEVLGRTHQKIGFGNHRGNRFTITVRGCAHPDGRPMTDQEAMEEIGKIHATLEATLGAERFPNWIGPQRFGSGRPVTAEVGRHVIAGRFDEAVMTYLSMPGDGEAPDVAAFRKRIREEGISEEVIESCPDWMDFERRMASHLLEKPDDHVGAFRRLPNNLQLMT... | Function: Could be responsible for synthesis of pseudouridine from uracil-13 in transfer RNAs.
EC: 5.4.99.27
Catalytic Activity: uridine(13) in tRNA = pseudouridine(13) in tRNA
Sequence Length: 508
Sequence Mass (Da): 55734
|
A0A3C1DPL8 | MTAVAIIGGGKMGEALLAGLLGANHSVVVCEPDELRAASLRKMYGISTGDPRIAVENSDVVLLAVKPAMVGEVLGSVGDAIPVEALVISVAAGITTAALESGVAHGIGVVRAMPNTPALVGQGMTVLSAGRSCTPEQLEQAQELLAAVGKVAVVPEAQQDAVTALSGSGPAYVFFVVEAMIDAAIALGLDSETARELAIQTAYGAATMLRETGDDPVELRENVTSPGGTTAAALERLEAHEVREAFIAALTAAKLRSAELASE | Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-proline from L-glutamate 5-semialdehyde: step 1/1.
Function: Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline.
Catalytic Activity: L-proline + NAD(+) = 1-pyrroline-5-carboxylate + 2 H(+) + NADH
EC: 1.5.1.2
Subcellular Location: Cytoplasm... |
A0A7W1GML4 | PEGRATIHAVLPRQTKISRKVNLTETEEQVLAANVDTIFLVSSLNRDLNVRRIERYLATAWESGAQPAIILNKADLCPVDERAGLVAEVEGVAFGVPVHTVSAFTGEGIDELRPYLGPGHAVVLLGSSGVGKSTLINRVLGVEQLETQEIRSGDDRGRHTTVHRELIRIPGQGLVIDTPGLRELQLWGESDGGIAEAFEDVAELAATCRFADCLHETEPGCAIRAAIEDGSLPAERLESYQKLQRELARLERRRDGRLQSLERKKWRQFSKQQRHNPKTRRR | Cofactor: Binds 1 zinc ion per subunit.
Function: One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Helps release RbfA from mature subunits. May play a role in the assembly of ribosomal proteins into the subunit. Circularly permuted GTPase that catalyz... |
A0A6L6E7T8 | MFQTSLRPTACPSVAGSRLTIGVLALQGDVREHERVLDDLGVAHCQVRSPVDLKGIDGLIIPGGESSVIDKLSRIFEVREPLISAIADGLPVLGTCAGLILLSSTVIGAIEGQQTFGGLDIAVERNAFGGQLESFETSIEMPLISGGPVNVAFIRAPIIRDVRGCSIIATLPNGEIVGVRSGNCVGIAFHPELVGESRVHEWWLDSVVTGAQR | Pathway: Cofactor biosynthesis; pyridoxal 5'-phosphate biosynthesis.
Function: Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS.
EC: 4.3.3.6
Catalytic Activity: H2O + L-glutamine =... |
A0A6L6C7I7 | MTTPPRVIALVGSTASGKSSVAHSFALQRGDVEILSVDSMTVYRGMDIGTAKPTTAEQREVRYHLLDLVDASESYSVAEFQRTAREALTDIASRQKIALLVGGTGLYGRAIIDNFTMPGEYPELRASLTVRAETELATMFQELTELDPSAAEKIEPTNARRVVRALEV | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
EC: 2.5.1.75
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylall... |
A5D2F8 | MAGLIDHTLLKPEATPEDIVKLCIQARHYGFATVCVNPCYVYLAARELKESPVKVCTVIGFPLGASDSAVKAAEAAAAVRAGASEIDMVMNIGFLKGRLLKEVKEDMEGVVKAARKEKRETVVKVILETGFLSDSEKIEACRIAVAAGANFVKTSTGFGKGGAEVSDVILLRRTVGQEIGVKASGGIRDLSTAIKMIEAGASRLGTSSAVSIIEELNK | Pathway: Carbohydrate degradation; 2-deoxy-D-ribose 1-phosphate degradation; D-glyceraldehyde 3-phosphate and acetaldehyde from 2-deoxy-alpha-D-ribose 1-phosphate: step 2/2.
Function: Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate.
Ca... |
A0A7C1GK48 | MDIIIVGLGNKGDKYQFNRHNIGRFFLERLITNQPADFQFPDFWQDSKKFLAKEIGGEIGNKKVAIFLPETMMNLSGRSVRKILDFYGRDNLLLVVHDDLDLTLGQMRLSFGSGSGGHKGVESINKELANKNYYRLRLGIGRPDDKDLNYNKDIRDFVLDDFNPEEKDKVESLFADFCSCLEVLIKEGPQSAMNIFNSSNRL | 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: 202
Sequence Mass (Da): 23091
|
A0A538B029 | MSAPPSSDESLATLDRELARGLDLVARASSVEDVEDAQTSLFGRKAPFAVVERALGSLPEDERRRVGQRTNEVRARLKAAITERRQALESERETAVLELDRIDVTLPGRRLRAGSLHPLTIVQQEIVEIFTRMGYRVVEGPEVEDEWHNFDALNIQPDHPARTMMDTTYLSVPGHPELLLRAHTSPMQIRTMQAEPPPVYVVVPGRVFRNEAITAKNMPVFHQVEGLAVDKGIRFSDLKGTVESFLRELLGADLRVRMTPSFFPFVEPGAQFDVSCFVCGGSGCKTCAFVGWIETMGAGMVHPRVLENVGYNPERYTGFA... | 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: 356
Sequence Mass (Da): 39834
|
A0A7W1E277 | MSKVWEDLQWRGLVHQVTDPALGPLLDDDFLTVYCGIDPTGPSMHPGHLIGVLTLRRLQLAGHQVVPLIGSGTGLIGDPSGRDEERLLLSEADLEANVVAIRHQVERLLDADGRAAKLAPIVTDNGQWLRKLTLTDFLRDVGKHFSVNEMIRKDSVRNRLEGREQGISFTEFTYMLLQAFDYLHLYDEHHCRLQIGGSDQWGNITEGIDLIRRLRADTAYGLTWPLLTTDNGSKMGKSDARTTVWLDPTRTSPYQFFQYWVRTDDADVGMRLRWFTFLDRERIEELDEATASHPERREAQRALAWEVTALVHGAPEAGRA... | 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... |
A0A3D3DBS9 | MNMLKEIIKQKQEETRKDKKNFPFKFLLQLIDEGLPPTRGFFQKLNSSSTISVIAELKFASPSKGIISDKKKNLEKIIQIYTTNGASAISVLTEKNFFKGDPGYIRQAKRVTDLPILRKDFILDEYQIFQSRCLGADAILLIARLLDELTLIRFQKIASSLGMDSLVEVHNKEELIKATTAGSKIIGINNRDLMDFSIDLSVTTRLSSLVPQDCLLVSESGIKYHEDIRRLSLYGIDAILVGETLMTAHSPGDKLQKLTGVEKKRREKQVYVG | Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 4/5.
EC: 4.1.1.48
Catalytic Activity: 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate + H(+) = (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O
Sequence Length: 273
Sequence Mass (Da): 30780
|
A0A350MT97 | MGVLDRVFTRFERELKGKAIRNRPLAKHTTLRVGGPAGIFVIADSINELRLVLQTALDFGLPYFVLGKGSNVLVSDEGFDGIVIELGIDFRRIVVDGGYIQAGAGVALPVLVQVACKRGLEGLAFAVGIPGSLGGALVTNAGAYGRTIGDVVRKVTVYNTLDHQLRSVDHSEIAFRYRNSSLLADGIIVEAVIKLEESDPDCVAGEMEKLFRKRKRSQPLNLPSAGSVFKNPPGLFAGKLIEEVGCKGLRVGDAQISQKHANFIVNLGNATANDVLTLLKKVQDEVYSVKGIILEPEITLVGEFPPSLIPRGRAGEDYEV... | 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: 324
Sequence Mass (Da): 34859
|
D7DRY6 | MNNLRPRIIPTLLMENNRLVKTVKFKNPNYIGDPINAVKIFNDKEVDELIFLDIGCSKKHTSINYNLLDKIASQSFMPLCYGGGIKTFEEASKIFELGFEKISLNSVLFEKPSLLTELSQSYGSQSIVASVDVKKNLFGKLKVYNGSKNNSINDKILDYVKNLENLGAGELLINSVDLEGTYKGYNLSLINELSNALTIPLIALGGASSTKDFKDALQAGASACAAGSLFVYYGVNKAVLINYPTDFINEL | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 5/9.
EC: 4.3.2.10
Catalytic Activity: 5-[(5-phospho-1-deoxy-D-ribulos-1-ylimino)methylamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine = 5-amino-1-(5-phospho-beta-D-ribosyl)i... |
A0A0A3IIJ8 | MEWIIVAIGGGVGATLRYLVQLLVKRMMASYWATASVNVLGSLLLGFASHEAIDSSSMMTFLTVGVLGAFTTFSTFAFEMVNLMDTKKWGTACLNLSTNLIGGIMAFSMGWIL | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Subcellular Location: Cell membrane
Sequence Length: 113
Sequence Mass (Da): 12169
Location Topology: Multi-pass membrane protein
|
A0A7K0TPX4 | SKVLEVGPGLGSLTLALLEPGATVVAVEIDRVLADQLPLTVQAHLPESAGSLTVIHGDALTLHELDFEPDALVANLPYNVSVPVLLHLLRTLPSLRSILVMVQKEVADRLVAGPGSRTYGVPSVKIRWFGDPQAAGNVGPKVFWPEPNVDSGLVRITCHEPPKCNSSRAEVFAVIDAAFAQRRKSLRAALSQFAGSPALSELALVAAGIDPGARGEALAVADFARLADALGQSAQSARNT | Function: Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits.
Catalytic Activity: adenosine(1518)/adenosine(1519) in 16S rRNA + 4 S-adenosyl-L-methionine = 4 H(+) +... |
A0A4Y7TJK7 | MDTDNTIPPGLRNPADLFFQKDGVRRAIVAAYWTVIILAIPLWWHTTSIERLPLPDARVSHQVSKSISIPVQVCIEGASEGLVSQVEGAGGGGYWGSMRWCVVLVSPALASKDAYVVTTTGPERVLRSRQLTYPVDESHHLQSTNFEGKDKQNRVVQFSSRYRLAFSLLNEDASAGNAVMAWNVQKGIQEHIQPVLDILKPLHNFTIESQVQYYAPLAFGVQPTEDRIYGLSYEDLTVFVNSAEWTLSSSASNDPVLHFLLFIPSASHTPLKILTSKSDAFLLPQWGGISIYNTPHLASFAHLSDRTLHRTFTTFSTQLL... | Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 432
Sequence Mass (Da): 47311
Location Topology: Multi-pass membrane protein
|
A0A1V5FWF0 | MKTVSCVPAVLVLRANDLAGILPARDHDAHKGRFGHVLLLGGNVGYGGALILAAQAALRVGSGLVSVVSRQATVDALLARQPECMGVALESSMDWHRAEFIRMQRRANALVIGPGLSNDRWARKLWDRFIDDVRPRVIDADGLNALARSPRALQGAVLTPHPGEAARLLGREAADIQADRVGALQCLIERFGAVVVLKGADTLVSGPGSPIFRIHAGNPGMAVGGMGDVLSGVIAGLLAQGLGALDAARWGALLHAVAGDHAASVGQRGLLPSDLLPYLRAGCNR | Function: Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S- and R-forms, the enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or ... |
Q0S4U6 | MTGRLVLAATPMGDVGDASPRLRTALGTADVVAAEDTRRTKALASALDVTITGKVVSFYDQVETARLPALVADVASGKTVLLVTDAGMPSVSDPGYRLVSACVAEDLAVTCLPGPSAVTTALALSGLPVERFCFDGFPPRKQGQRKTWLRALVAEQRACVFFEAPHRLADCLADAVEVLGGTRRAAVCRELTKTYEEVRRGTLAELAEWAADGVRGEITVVVEGATLVASDPADLVDEVERLVADGTRLKDACALVATTGVSKRELYETVLASRKD | Function: Catalyzes the 2'-O-methylation of the ribose of cytidine 1402 (C1402) in 16S rRNA.
Catalytic Activity: cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = 2'-O-methylcytidine(1402) in 16S rRNA + H(+) + S-adenosyl-L-homocysteine
EC: 2.1.1.198
Subcellular Location: Cytoplasm
Sequence Length: 276
Sequence Mas... |
A0A2E6XUI9 | MHSSPSGNFEYRPSLSGPASTRLEGSWLLRRQGRSTSRPPRRPLWRSSGEMLLSALLAATEQSVSASSKPGEDPDIGRIVHDSRVVSSGDLFCCVPGQNSDGHAHAREAVEAGAVAVLAERSLELDVPLIVVPSVRRLMPLLASELTGRPSAELDVIGVTGTNGKTSVVHLLGEILEHAGRSPATIGTLTGTLTTPEAPCLQRQLAAWVAEERGAVVMEVSSHALDQHRVDGTRFSAVAFTNLSRDHLDHHQTMESYAAAKERLFTSSFTGRAVVVVDSAAGRRVADRALEEGLEVVEVSVADVDRKVWVDRVAFRWAGL... | PTM: Carboxylation is probably crucial for Mg(2+) binding and, consequently, for the gamma-phosphate positioning of ATP.
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in... |
A0A537WL73 | MVPGSGVQRRHGRQPAARRGDQGPSRFHRNDLRGVRIGAHVPTRGGLLSAIRAARECGADAIQVFLSNPRAWAPPRISRKEADAFRQAWGESGLGPMFVHAPYVVNLASPVPEFLERSIDVIRQAVAAASSVGANGYVVHAGSGGPGEPAESFRRTVSALRAVPAQGGCDVVVELTAGTAGSVAATFPEAAHLFEAVGDPRLKLCADTCHLFAAGYALDEPDGVAACFEELHASGLGDRLVLIHANDAKYERGARRDRHEHIGQGGIGVEGFFEILHRPEVQELALVVETPGRLEDHARNIATLRRLAAD | Cofactor: Binds 3 Zn(2+) ions.
Function: Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate.
EC: 3.1.21.2
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphooligonucleotide end-produc... |
A0A1C3E4I9 | MRTADPQWPTRTSQLLGFQILGVGAYVPDQVVTNAELQERCGIDPDWIEQRTGILARRYVAEGQATSHLCIMAAQRAMADAGVTAEEVDLVVIGTFTPDHLCPSTANLVQAHLGIEAPAMDLAAACSGFTYALATAAQFIVTGNSRRALVIGGDCNSRIVNPQDPKVAPLFGDGAGAVVLGRGDEKQGLVRYQLGSDGSGASLLDRPAGGTLHPFTESDLRDGKTYLQMDGRNVFKWAVKAVCNSILVTLEQAQVSIEQVSMFILHQANLRIINHVAEDLGIQQDRIYNNLDKYGNTSAGSIPIALAEVIASGRLQRGEL... | Pathway: Lipid metabolism; fatty acid biosynthesis.
Function: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the tot... |
R7I2Y4 | MLLAASGAAGLPQAFAAAKAGKRMLLANKESVVCGGALLQQAIREGGAELLPVDSEHSAIFQSLAAATPAQREKVVIWLTCSGGPFLRRMDLTGVTVEEASTHPRWKMGRKITVDSATLMNKALEVIEARWLFDIPPERIRVVIHPQSILHSGVAFEDGAVMAELGVPDMRTPIAVTMAWPERTESGAAALDFTKLKEPLTFEAPDLERFPQLKLAWEALEAGGSATIVLNAANEAAVAAFLDRKISFLGIGRACREALSGLVLPAPKSLSDIYAADREARSYVDSLIRSGRIS | Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 1/6.
Function: Catalyzes the NADPH-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP).
EC: 1.1... |
A0A6L6E7P5 | MTSLTAKLWATDTSTLAIVHTSLKPVIAVFVGGIAGSAARIGIALVAGRFDDYWWPYPTLVVNLVGSFVLGYLVARRMSSAPTWMRLGVTTGFLGA | Function: Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Subcellular Location: Membrane
Sequence Length: 96
Sequence Mass (Da): 10202
Location Topology: Multi-pass membrane protein
|
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.