ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
|---|---|---|
A0A6C1T2H6 | MARSTGRAIASAIIALAALAYAAFHLWFATFGTLADSWRNAIHVGGAIAMFFALRGMESGRRMLPWLIIAALCAAIPVYAVVMEQALYARNDRMIPADMWVSGAVLLIVLWAAGLAGGWVLTGLGLLAAAYALWLGPYLPGGWGFRGISTYTFTYRMLWGGEGYFGFLASISATYIYLFVLLGVTLLAAGSGNFLVQASLRLGARLPGGPAQAAVMGSAAMGSVSGTSIGNVMATGSVTIPMMIRAGYRRPFAAGVEASASNIGQIAPPVMGAGAFILAAWTQTPYATVALLSILPAMLYFYSVFIGVALDARKQDWKPV... | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 617
Sequence Mass (Da): 64458
Location Topology: Multi-pass membrane protein
|
E3HCM7 | MNIAVFGYGMMGKFVCEDVASAGLQIAGVIEKRDGAQAMSPVTEDILYKSLNDIKEKVDVIIDFSNPANLDEILEYAIENQIGAVICSTGFTAEQLTKIKQASEKTAILFSRNMSLGVNVISEVLKQITPILADAFDIEIIEKHHNQKVDSPSGTAKLFYDSINESLNGEKEAVYGREGIVGKRTKKEVGIHAIRGGSIVGEHSIIFAGQDEIIELKHEALSKRIFSQGSVKAAKFLAGKAPGFYTMKEVLDIK | Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4.
Function: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.
Catalytic Activity: (S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydro... |
F7UUE8 | MSYLITIVGAGLAGSEAALQLAARGVRVRLVEMRPHTQTAVHVGADCAELVCSNSLKSTKADSAAGMLKQELAALGSFVYAAALRHEVPAGGALAVERAAFSADVTALIEQHPLIDLVREEAHDLQAVAALADALIVATGPLTSPALAESLAGITGNDHLAFYDAAAPIVMADSLDYDKLFRQSRYEDAEQGAGDYLNAPFDRAEYDAFIEALVSAERVIPRDFETRDLFQACQPIEEIARKGPDAPRFGTMKPVGLTDPRTGRRPWAALQLRAEDVSGASYNLVGFQTNLTFPEQRRVFRMIPGLEQAEFARYGVMHRN... | Function: Catalyzes the folate-dependent formation of 5-methyl-uridine at position 54 (M-5-U54) in all tRNAs.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + H(+) + NADH + uridine(54) in tRNA = (6S)-5,6,7,8-tetrahydrofolate + 5-methyluridine(54) in tRNA + NAD(+)
EC: 2.1.1.74
Subcellular Location: Cyt... |
A0A642UZA8 | MAITWRLDDIYTGLWVLHGSIWGVLARKGLIALTSFSSAYLGGVVWANFAACVVMGCLQASTKIWTQVGHPNPIFIGLTTGFCGTLSSFSSVIVESVTLAINIDHVSVPAPGYGTMQVFDVIIGQFAISYVGLLLGGHLGEWLEQTVPKFDRGYRFMVVIGAAIGVGLIIADAIIIGTVASSREWTFSVLFAPLGALIRWQLSKLNNAQWFYGTYIANVVGTVSLSVFSLLQFGLTTHRTPLVTNYTARQVLVGLDDGFCGGLTTVSTFVVELKKSSRGKAYVYIIASVLPSFIMVLLVLGSYHWTKGLAR | Function: Fluoride channel required for the rapid expulsion of cytoplasmic fluoride.
Subcellular Location: Membrane
Sequence Length: 311
Sequence Mass (Da): 33572
Location Topology: Multi-pass membrane protein
|
D8FZP0 | MATDIRHQTENGYQSQITQPSSRENLNRRSLMRLPRSLSAIETSGFGLTGHANWFTIATVIQASMGPSAIFIWLPGILMGMMLNLQVKRIGEYFPDMAGGTPNYTARLLKNYPGLGSYAAIGYLLSWVATLPISAIVLTQLIKVNLNSLGFSCPETLLNITFTLITFILTFSGTRALSILHAFFVLPTVGVLSVFSIHGLFWLAFSPNSPGFFPATWPAFTFIDWAKWFYFGTYIFYCCDSTASFVADSRNPTKTLQFLKISAVAMLPVILGGSWVLMRLATAPGLKDDVFLNVLAACQVLWGPWVPTLVTFLVVASCLL... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 979
Sequence Mass (Da): 108929
Location Topology: Multi-pass membrane protein
|
M4S015 | MSRDWLSVATLKEATIVQRMIGERIETADRLPPAPRVAGADVSMKWRDSMGPVHAAIAPVDGPAATATAIPPFPYVPGYLGFREVPVLAMAWDRMAASGGPVPDLLIVDGHGRAHPRRAGVASHLGVALDVPTIGCAKTLLCGVVEGEVGPDPGDRAPVVHGGEVVAMALRMRARAAPVYVGIGHRVSLETAVDWVLRLGGGRRLPLPVRLAHDAANAARRLAEAERS | Function: DNA repair enzyme involved in the repair of deaminated bases. Selectively cleaves double-stranded DNA at the second phosphodiester bond 3' to a deoxyinosine leaving behind the intact lesion on the nicked DNA.
Catalytic Activity: Endonucleolytic cleavage at apurinic or apyrimidinic sites to products with a 5'-... |
A0A2D9FSN2 | MNKWLENKWAVSITAGILLGLSFPPINLSFLSFPAFILFFHLANKTDSYKQLAYYSYAGFVAWNLIGTYWLMMATVPAGIAAILANSVLMTIPLCLAKYFSQKSRSPVLIAVLQASAWVGYEFLHHHWDLSWTWLAIGNAWSNWIGIIQYISATGFLGISFWVVLTSSLTYQLIISKKRSLAYATLGAFLIFPAWSFVLYSTDNTGSNSQEAVNVAIIQPNHDSYQEYAGMSGLTEVVDSLISLTERTITPETQLIIWPENAIDGAIFANSRTAFRIADSARSWRIPLITGTGLFKTYAPDTDELYRGIYPGTDLPFNYF... | 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... |
W7CQ17 | MTEKSLETNKATSRVTINDLTGLVKMGIVDSNTIAAFAGMWIAFQYTNTPFLQNIVTVIMLVIGTAAIIAGAGCWNNYYDRDIDKKMERTKTRPTITGRISPKMTLVAFIALTVVGEVLLFMINPMTGITGLAGVFLYNVVYTMWAKRNLVSNTIIGSFSGAVPPLIGWFAIAPTLELPAIMLFLFMFCWQPPHFYAIAIRRRADYAAAGIPMLPVVKGVERGRKSILLWVGFLTVLPFFMFDFGIIYVVLATIMNIAWLVLGLRGYKTADPDQWAKSMFFFSLSYLMILFVAMMVLAPFV | Pathway: Porphyrin-containing compound metabolism; heme O biosynthesis; heme O from protoheme: step 1/1.
Function: Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.
Catalytic Activity: (2E,6E)-farnesyl diphosphate + ... |
A0A7L6A2K6 | MIFSWGLYIVLGLNMLFALAVIFAERRDVGATXVWLLVLFFLPVLGFIVYLFLGRQLXKDNFYNLSVEERSFHSLQVEAQLEQIHTRQTQLAQPLFEKYDQLLQMNLRSSKSLISVHNRSLILHDGEQKFKALMDDIRSTETEINIQYYIIQRDALGQALLKELIERAKAGVKVRLLYDAVGSRSLRNSDFKELIANDGEVRVFFPPTLGIINFKLNNRNHRKVVIIDGKIGYVGGFNVGTEYLGLVEKFGYWRDTHLRVEGDVVYNLQHRFILDWNYSGHRKHDPENAFCFARHDIKENSPMQIVTSGPNSDTEHLKNM... | Function: Catalyzes the reversible phosphatidyl group transfer from one phosphatidylglycerol molecule to another to form cardiolipin (CL) (diphosphatidylglycerol) and glycerol.
Catalytic Activity: 2 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) = a cardiolipin + glycerol
EC: 2.7.8.-
Subcellular Location: Cell membra... |
S7T4Y9 | MIDIAIDANVMLSGRLSVERLTSMNDHTILLIEPDQEDARRIISALSTLENVTVRHSPSLDHLLETKEDGPYLAVIVAMGIDAPDSGRLHTRLMSMSLEAPVIALAPEGREDVKTLARALGAGDVLYKDDTLGPELLRMARLLQSRAKARETANAPKPSDHWVERIIANNADGILIMDHEGHLLFANPAAERIFGISSEELVGHGFGFPVIAGESTEIDIFSKTGSKIVEMRVVEIDWDGRMAFLASLRDITERKRMEMELAKAKEDAESANRAKSDFLAKMSHEIRTPMTGIIGMTELALASGLNPQQREYLEMVRQSA... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Cell inner membrane
Sequence Length: 795
Sequence Mass (Da): 87271
Location Topology: Multi-pass membrane protein
|
A0A6B1FRR2 | MMCSMRSVFILGTDTGIGKTYAAVRIIRHLRESGMSVGVMKPYSAGKSVKTGAKSEDAHILAKAAGVIPDSSINPDHQEMEASPYTRCVMGYTAPDPQNIIQQYRALESRFDAMVVEGMGGCMVPILHDYYMMDLARDMGLPAIIVSDNKIGAVNHCIMSVHVCRFRNVQLDGIILNKMHHDGYSIDVLQKSLEGMMDVPIMGIIQNDMLVMN | Pathway: Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 1/2.
Function: Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to form a ureido ring.... |
A0A0N8PWQ3 | MEILEKAQKMLEKHPLCNHCLGRQFALLGYGLDNHKRGEAIKLLLTMRSHRLALLGKKAGVSLLKIIATNGSFDMAAEILKKMRKKVGKKQECYLCQGRFKHLDELVDKSLEKLKAYEYTTFLVGVELPTEVEEREDEFKAEFDVRHGENMRNEFSRDIGKEISEITKKAVDYKKPDVVVILNPFTGQVTLQANPLYIRGRYRKPTRGIPQSKWVCKKCRGKGCPRCNWTGKMYPESIEEIIAGPTLEKTGGEDASFHAAGREDVDARMLGRGRPFILEVKKPKRRFIDLQELTQTINEQAQNKVKVLNLRFADKSAVRK... | Function: Responsible for synthesis of pseudouridine from uracil-54 and uracil-55 in the psi GC loop of transfer RNAs.
EC: 5.4.99.25
Catalytic Activity: uridine(54) in tRNA = pseudouridine(54) in tRNA
Sequence Length: 442
Sequence Mass (Da): 50365
|
M4SL24 | MSDNPSAPAGVNLTHLQRLEAESIHILREVVSEVERPVMLYSVGKDSAVMLHLARKAFYPSPPPFPLLHVDTTWKFRAMYELRDRMAKESGMELLVYHNPEAMERGINPFDHGSLHTDMWKTEGLKQALDKYGFDAAFGGARRDEEKSRAKERIFSFRSANHRWDPKNQRPELWRLYNARKAKGESIRVFPISNWTELDIWQYIHLENIPIVPLYFSAPRPTVVRDGLTLMVDDDRFPLRPGEVPEMKSIRFRTLGCYPLTGAVESEAKTLPEVIQEMLLTTTSERQGRAIDHDQAASMEKKKQEGYF | Pathway: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 1/3.
Function: With CysN forms the ATP sulfurylase (ATPS) that catalyzes the adenylation of sulfate producing adenosine 5'-phosphosulfate (APS) and diphosphate, the first enzymatic step in sulfur assimilation pathway. APS synthesis in... |
A0A2E3V7F6 | MIEFINESKKQDNTKSVMTANQAVDSTLVHLKLDPDKFEIAILACDDEKIRELNFQFRGINNKTNILSWPEKDLSPKVSGTMPMKPEPINREPVFLGNLAISFDFIVKEAKKLNKDFYNHLYHLISHGTLHLLGFVHDLELDAKIMENKEREILSKVGIADPYSN | 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: 165
Sequence Mass (Da): 18911
|
A0A963XLK9 | MNKTGPDDARLLALVRSAFGTIHPEVIGVAVSGGSDSVALLHLAARFQAERGGLVRAVTVDHRLRPEAADEARFVAGLCETLGVRHDTVEWPHGPLAGNIPDQARRARYDLVTGWAQCHGITHVVVGHTADDDAETFLMELARQAGIDGLASMRRFWHSNGIYWARPLLSVSRESLRQYLRGQNVGWIEDPTNEDETYLRVKARRALAALVPLGITGEGLARVAANLRVAQAELVSLAARAAEEFVTERAGELVMDRLRWRGLGPDTGRRLVIAAVRWVGSAPYAPRGAEVARLEEAIHESHDATLGGCHLRCSPEEIRF... | 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)... |
H2MS24 | MHLGESTRECEYSQISTRSSTPMETPYKKKTPKKRKWETFPGRNRFYCDGRIMMAKQTGVFYLTLVLILVTCGLFFTFDCWFLAEQLTPIIPVIGAVLFLFVIGTLLRTSFSDPGVLPRATPDEAADLERQIDVANGSTGYRPPPRTKEVVINGQTVKLKYCFTCKIFRPPRASHCSLCDNCVERFDHHCPWVGNCVGKRNYRFFYMFILSLSFLTVFIFAFVITHIILNSQRIGFLSALKDSPASVLEVVVCFFSVWSIVGLSGFHTYLISSNQTTNEDIKGSWSSKRSKDNYNPYSYGNIFTNCCAALCGPLPPSLID... | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 505
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 55931
Location Topology: Multi-pass membrane protein
|
A0A2E0UKR4 | MKPKYKKYSVLGSARSGMAAALFLKHKGMDVFVSELQEADHFIESKKQYDEYDIEYEYGKNSNRVLDSDCIVVSPGISLSIPLLETARENGIPIVSEIEVGSWFYDGTIIAITGTNGKSTTTALIGYLLEQAGYNCMVAGNIGYPFTRALYESGPCEYAVLEVSSYQLDSIKTFHPNVAVITNIMPDHLSRYNNNFQEYVSSKARILANMAADDHLVYNADDTNVVTVVEEAETNKHCYSSTVRGECTAYKVDNMLIIGDSSGSILEIDVSNMILVGEHNYQNVMAASIVARICNMSKEVIEAGVTSFKGLPHRLEYIGE... | 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-... |
C0EB00 | MKRLIFLLLPCIVLVSLFAPLTAQAAYTPDFEINSEAAYLVNMETGKVIYEKNAQTQYLPASTTKIMTAIIALETIDDIDNTMVTAPAYVFDQLYGLSASNADLRVDEQLSMKDLLYALMLRSACEGASIIADYIGEGDIQKFVDMMNAKAEEIGCTNTHFVNAHGLDEPDQLTTAYDMYLITNYALTNEQIGARFREIATTYSYTMAATNKHPEPRVISHTNKMMSSNTDLNGGYSRSYVQGIKTGTSNEYFNLVTMAKQDGYTYLLVTLGAHGQNSFVTYSDHAALYDWAFKTFESKVLARPGSKTIPNDVKVEFAKG... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors.
EC: 3.4.16.4
Catalytic Activity: Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanin... |
A0A966KN55 | MSEIKNKFPFITLISDVAMDPYNSYGHDGLVENGQILNDETLPILGKMAVAQAKAGIDVVGPSDMMDGRV | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 1/4.
EC: 4.2.1.24
Catalytic Activity: 2 5-aminolevulinate = H(+) + 2 H2O + porphobilinogen
Sequence Length: 70
Sequence Mass (Da): 7540
|
H2MHM8 | MHTASVGVSKLCFLLSVALCCLLLLLIPALQPPPQVDRPQPRPQVRPGQSRPAEVSAGAYSPGKRPSPLKLSGGSVNEGELVRAKPTQAAKTGPFPRSRPLDKLELKDIFIAVKTTRKYHKSRLELLIQTWVSRAKEQTFIFSDGDDKDLQQRTGVNLINTNCSAAHTRQALCCKMSVEYDKFIESQRKWFCHVDDDNYVILPSLLRLLSSYHHSQDVYLGRPSLDHTIEAAERVKSDGSVSVKFWFATGGAGFCISRGLALKMSPWASLGNFISTAEKIRLPDDCTIGYIIEALLEVRLTHTHLFHSHLENLQKLPVDT... | Catalytic Activity: 3-O-(alpha-L-fucosyl)-L-seryl-[EGF-like domain protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-(N-acetyl-beta-D-glucosaminyl-(1->3)-alpha-L-fucosyl)-L-seryl-[EGF-like domain protein] + H(+) + UDP
EC: 2.4.1.222
Subcellular Location: Golgi apparatus membrane
Sequence Length: 376
Sequence Mass (Da): ... |
A0A368MCQ7 | MTGIAAIGAGLAAIGAGMGIGRIGGSAMEAMARQPEMHGKIQTSALILAAFVEAVALFGVVVAFLQG | 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... |
A0A258BNK9 | MKEHKAKIDAVKRGDQVVTGGGLIGKVTKVEDNVAEIELAPGMKVRAIKSTLTDIVDPLNAKPAND | Function: The SecYEG-SecDF-YajC-YidC holo-translocon (HTL) protein secretase/insertase is a supercomplex required for protein secretion, insertion of proteins into membranes, and assembly of membrane protein complexes. While the SecYEG complex is essential for assembly of a number of proteins and complexes, the SecDF-Y... |
A0A0G1L6X0 | MKNTPRFIAIEGLDGAGKSTLANAIELCFTEKGLDILLTQEPTGGQVGHRVQRILDGKMPLPGTNRELQRLRIEDRFDHIRSIIKPHLQLGNWVLTVNYWLLTLADGMSEGKVEDYERMNDEIIGEHMIYPHIALLLDAPADVCLERLERKGIRFVDWSEKKVLEKIRANYMWLAENGRFGNICVINADRPKDEVLSSAITALGPFL | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
EC: 2.7.4.9
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Length: 207
Sequence Mass (Da): 23477
|
A0A9E4I4L5 | MRDFDTSSGEFSGPSIRPCNIEAEQSLLGAILSNNDVFQEASDVIGPHHFYDPIHQYLFRLISERIERRAIADPKTLKPFIDQEPGFRELGGVNYLIKLQDTAISVHAGRQYAQEIYQFAIRRKLIDLYTELSEAARNPEVDKSAGDLIADAEQKLYAVGESGEGNVGFQSFVQSMSAAVSAAKTAKSRTSGLSGLSTGFVDIDRKLGGLQKADLLILAGRPGMGKTALATNIAFNVAREFKGKGTESPSGGYVGVFSLEMPSSQLAARILAASSRIPISKIRTGDIDTQDFERYTNAARGLQSYPIFIDDSPALPISQI... | Function: Participates in initiation and elongation during chromosome replication; it exhibits DNA-dependent ATPase activity and contains distinct active sites for ATP binding, DNA binding, and interaction with DnaC protein, primase, and other prepriming proteins.
EC: 3.6.4.12
Catalytic Activity: ATP + H2O = ADP + H(+)... |
A0A9E4M2N6 | MRSRRNAAIERGVAAILDLGSAKVSCVLLKFDQLLLNGTGLQPKLHVLGAATIASRGVRCGEIQDRRELEKSIMRVLTVAQGKAHIRVDHAFICTSGGSLESHRPVNTVKINGGRISADDIARVVSTTDLPELAEHRTYISVQPVNYAIDHRHEISDPRNLKGNLLSVDLHAVSADRTTIDAIVNAVEKCNLAVCGIFSSAQASAMSALVESEQDLGAACVDIGAGVISLAVYYRKNVVFTRTVKLGGRHVTNDICGALSVAEPVAERMKTMHGSLFFEPRDDEEMIAFRDVDGRHGTISKAHLNFFIKPRMEEILETVA... | Function: Cell division protein that is involved in the assembly of the Z ring. May serve as a membrane anchor for the Z ring.
Subcellular Location: Cell membrane
Sequence Length: 423
Sequence Mass (Da): 45715
Location Topology: Peripheral membrane protein
|
C0E881 | MKELLLGNEAVARGLYEAGVAVVSSYPGTPSTEITEYAATYDELYCEWASNEKVALEVAIGASVAGKRSFTAMKHVGLNVAADPLYTLSYIGVNAGLVIAVADDPGMHSSQNEQDSRNHAKGSKVPMLEPSNSAECLLFTKLAYEISERFDTPVILRLSTRVSHSRSLCSLSERLEVAAKPYEKNIPKNVMMPAMAVKRHVVVEQRLLDLTEFAETTDLNRVEDNGSKIGVITSGTSYNYAKEALGDNVNILKLGLAYPMPVGLLKEFAANCEKVFVFEELDDFIETHCKKHGIDVIGKEAFSFCGEYSQTIIKEKILGI... | Cofactor: Binds 2 [4Fe-4S] clusters. In this family the first cluster has a non-standard and varying [4Fe-4S] binding motif CX(2)CX(2)CX(4-5)CP.
Function: Catalyzes the ferredoxin-dependent oxidative decarboxylation of arylpyruvates.
EC: 1.2.7.8
Catalytic Activity: CoA + indole-3-pyruvate + 2 oxidized [2Fe-2S]-[ferredo... |
A0A929LKY5 | HKLNVTIDAIPEGELVFPREPMVRVEGSIVDCQLIETALLNLVNFQTLAATKCARVIKAAQGNPVSDFGLRRAQGPDGGLAVARASYIAGASSTSNVLAGKIYGIPVFGTHAHSWVMSFDTELDAFRAFAKSSPTNCSLLLDTYDVHEGIKNAIIVAKEMEERGERLNAVRIDSGDLARLSKEARKAFDEAGLPYIKISVSNDLDEYTIQSLFAQGAPIDAFGVGTKLATCDPQPSLGGVYKLTARRQSSTEPWTPVIKLSEMAYKRTVPGIQHIRRFYDANGCPAGDMIFDPDYLVTKNPESKATVVDIIDPYSTHKLE... | PTM: Transiently phosphorylated on a His residue during the reaction cycle. Phosphorylation strongly increases the affinity for substrates and increases the rate of nicotinate D-ribonucleotide production. Dephosphorylation regenerates the low-affinity form of the enzyme, leading to product release.
Pathway: Cofactor bi... |
F7UWS5 | MQTEDRYNACVSALHAYAENAGFTDVVIGLSGGMDSSLVAVMCVDAFGASHVHGVMLPGPYSSDHSVEDARELADNLGIQAEIISICEPYRAFEQALAKACGGTLSGLAAENTQARCRMVCLMALSNAQGWMLVNTGNKSEAMMGYSTLYGDTAGAFSPIGGLYKTDVYALARWRNDQAIKQGATPPIPEHVFTKPPSAELSPDQEDEKSMGIDYPTLDALLVAHVERGLNAQQLVSEGFAPATVDRVLATIKATAFKRALEPPFPTVRFYE | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis.
EC: 6.3.1.5
Catalytic Activity: ATP + deamido-NAD(+) + NH4(+) = AMP + diphosphate + H(+) + NAD(+)
Sequence Length: 272
Sequence Mass (Da): 29117
|
H0X2J5 | MLATRVFSLVGRRALSTSVCVRAHAHGSVVKSDDYAFPSYVDRRDYPLPDVAHVRQLSASQKALKEKEKASWSNLSMDEKVDGLDPLPGLPGSRELLSTSAGQGEEPSMFSVAVYLVGYDKVTREGPSRTVYGPVPHTFDPDWVAKQTKKMLDMKVNPIQGFAAKWDYEKQEWKK | 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.
Subcellular Location: Membrane
Sequence Length: 175
Sequence Mass (Da): 19546
Location Topology: Single-pass membr... |
A0A3G1KLX2 | METQVVVIGGGITGAGILRDLAMRGIEAVLVEKGDLAHGTSARFHGLLHSGARYAVTDPASAQECIRENLIQKKTAAHCIEDTVGVFIQLAEDDPCFVAQWQKACGDTGIDIKEIDCAELLKREPNLSPVIIRAFQVPDAAVDGFKLIQDNVLAAKQYGAKVLTYGQAVSLAVSSGRVCGVTVRRPSGDEEFISCQIIVNAAGPWTGEIAALAGLKLNLVLNKGTLLAFNHRLTNTIINRCRRPGDGDILVPHHTVSIYGTTSVNVTEPDTDAGVYEEVGRLLALGRQMIPLMEEARILRAFTGVRPLYQPDGEPGDGMG... | Pathway: Polyol metabolism; glycerol degradation via glycerol kinase pathway; glycerone phosphate from sn-glycerol 3-phosphate (anaerobic route): step 1/1.
Subcellular Location: Membrane
Sequence Length: 509
Sequence Mass (Da): 55459
Location Topology: Peripheral membrane protein
|
W4EEW5 | MALHIYNTMTRTKEEFVPQEPDKVKMYVCGPTVYGYMHIGNARPVIVFDMVRNYLETLGNEVRYLTNFTDVDDKMIRKAEELNITVAEVAEMFIAAYQEDLAGLGVKPATMNPRVTESMDTIIEFIKELEDKGYAYENGGDVYYRTGKFANYGKLSRQNLEELRFGIRVEVDSRKENQEDFVLWKAAKPGEVHWSSPWGEGRPGWHIECSAMVREYLGTTIDIHGGGEDLKFPHHECECAQTEALTGEPLSNYWMHNAFLNIGDEKMSKSLGNGLLVKDIRARFKQGAIRYFMLSSHYRNPLNFTEEALLSAEKSVERIA... | 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: 468
Sequence Mass (Da): 53151
|
C7M7R6 | MYGLRVANRYAKALLEYALLQNALEGVFADMTLIDKTIKMNKDLERMLISPIVKTTVKKNVLTEIFTMVTPETQRLFDLLIQNRRLPILGAVAEKFVVLYNDYKHNKTAVVTTASPLNEATRKEILEKVMMLTKNKNVTLENKVDKNIIGGFILRVGDVQYNASVAHKLNRLQQEFQEKLFL | 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... |
A0RUG7 | MCMIPTEVILSFVARPACEAIIMPDPGPAAMEHATFAVDIDGTLTEDGGGGRIHLGALSALRHLATSGHNVILVTGRSSVEAYMLAVYGGITRLAVGENGGCITTGPSEHLLLGDMDVCERAFEVIGPEFGAVRKGTFPRMTEIVLESTFDVGAAREFAKKRGLGIGLADSGYAVHLNPEGIDKESGLRKALDMLGARGKVIAIGDSETDVPMFRTADTSIALGNAPPGVRSAATIRTRAEAGDGVVEALDLLAPMMARSGEWDTGR | Function: Catalyzes the dephosphorylation of 2-phosphoglycolate.
EC: 3.1.3.18
Catalytic Activity: 2-phosphoglycolate + H2O = glycolate + phosphate
Sequence Length: 267
Sequence Mass (Da): 27848
|
W6NBG1 | MFAVAQPVPKEYHVDGNDDGEERNVGIRRKASKLNVFSVNYCNSCRVLKPLRAHHCKICRRCILRMDHHCPLLQVCVHHHNHKFFLLFLFWPCCLGIFVTVITLPYTFRTAYTLWLGGTLSSEHHLLNSAIMNAVVIAVSVGSLLKTQLQSLLSNRTTIEDSQLSFLDEDEMNHEFSIFDLGSRMANFCSIFGKFPLTWLLPVYTTPGDGVNYNYVVRCGREFAAPTPPPRKKRFWKLC | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 239
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 27407
Location Topology: Multi-pass membrane protein
|
B5YGC2 | MDIVSPKGFLYSIAKAQIKYPDRYDIALIYSKKPAQIAGVFTTNQIKAAPVKICMKRIRSGIAQAVVLNSGNANACTGKKGIEDALKITDYLAEKLNINTHYIFPLSTGVIGMPMPVDRILNALNDLIKNLGNAQPMQVAEAIMTTDTFPKITFRQIQTPSPITILGICKGAGMISPNMATMLCTVLTDAKISSDLMKEALKDAVAQSFNSITVDGDMSTNDTVLMLANGESDIKIERKTALWKQFKSALSDLCSELSKMIVKDGEGATKFVTIIVKEAKTTQEARRVARAVANSLLVKTALYGNDPNWGRIIAAVGYSG... | Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; L-ornithine and N-acetyl-L-glutamate from L-glutamate and N(2)-acetyl-L-ornithine (cyclic): step 1/1.
Function: Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of N-acetylglutamate from glutamate and ace... |
A0A2W5CCV0 | MTAPSLTRAVPTLDLELALATRCGPGPRIVVGIDEVGRGALAGPVAVGACAIEVVEGRTLALPDGVRDSKALTARRREQLVEPIRSAARSTAVGWSEPAEIDELGIMRALTLAALRAIDALEVAADAIILDGSVDVLTPDLSRRPGRCPRVELRVKADRDCASTAAASIIAKVARDRRMQELDAVAPAYGWAANKGYGSATHRTAILEHGPSDQHRHSWNLGGREPVLPGVLWDDQSSPQPGKERR | Cofactor: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
EC: 3.1.26.4
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Subce... |
A0A3D3TWW8 | MVVTQADRQATTSAFLEYLHGPQRPVLVFDGATGTSLQGLGLTADDFGGPDLEGCNENLAVTKPDAVKAVHRQFLEVGCDVIETDTFGAASIVLAEYGLEDKAFELNKRAAELAREMADEFSTPEKPRFVAGSMGPTTKLPTLGHIDFDTMRDSFREQAEGLIAGNVDLFIVETCQDVLQIKAALQGIEAAFAATGERRALMVSVTMETTGTMLVGTDIAAVVSILEPFPIDILGLNCATGPEQMKEHIRYLSEHSPFTVSCIPNAGLPENVGGVAHYRLTPVELKMQLMHFVEDLGVQVIGGCCGTTPAHIGSLAELAQ... | Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-methionine from L-homocysteine (MetH route): step 1/1.
Function: Catalyzes the transfer of a methyl group from methyl-cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor u... |
H2L9Y5 | MKRVRAYTAMVLVFCVLVIFIYSTLNLEPANTVISTEEGSQRLRRGHDPEGQLKSTHEHTSFTTAEMSTAVLQTVSVSKDLREMIPKNEAYWNRLMHTALKGLDDGDYSFARESPWSLCRVENQELLQLNIHDFSSYPPLLQTFVRGMTCKSPPILIDQPNKCVAANRKEYNQTFLLLAIKSSPRNFEQRQTVRETWGREGVHHGGLTVRTFFLLGNSTQDDPDMSALLSYEAERFGDILQWDFHESFLNLTLKMKVFLQWTLKNCPQVSFIFSGDDDVFVNTPGLLNYLKSLDASKTENLYVGHVISTASPLRDPRSKY... | EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 428
Sequence Mass (Da): 48642
Location Topology: Single-pass type II membrane protein
|
A0A257TDI4 | MARRALRKIDPSLELGRWLRTFDDLPAPWQPEAIFGRQAPLEVEVGTGKGLFLVAAAANAPDRDFLGMEVSNKYARYAAARLAKRGLTNACVVHGDALRVFRERLPDACLAAVHVYFPDPWWKARHKKRRVLNAGFLADVERTLSPGGRLHFWTDVQEYFRSTLDLIERVTRLEGLLEVPEHPAQHDLDYRTHFERRTRLSGEPVYRAEFARTPPMGYAFVTKETSMPPISSLVARDIMRSNLVTAAPGQSLADLRHLLIGSHVSGAPVVDRGKLVGIVSRSDLVRVEELVEALDAEVSEEVWLENQTDGFKHPAPQEFG... | Pathway: tRNA modification; N(7)-methylguanine-tRNA biosynthesis.
Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
EC: 2.1.1.33
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
Sequence Length: 392
S... |
A0A651E8V3 | MRAGYNPKLATGVICASGTLGQILPPSTVLIFMADILQGANSAAQFAMGNFAPDTVSVGDLFAGAFIPSLMLAGLYMAYIGWQAVTQPANCPPVSMTAEERAGLGRRIVVALVPPFVLIAAVLGSIVSGVATPTESASVGSIGALLLAAIRLLADRWFGHDGEAARDERLFWFWLGFLALLGALGLAFGAFGLLTFLVVATIAASVAVLATGALRWSFVDTVKRSCVGTMTITSMVFIILLGATAFALVFTRLGGDVLVRDFLQAMPGGRFGALLIVFLIVFILGFFLDTFEILFIVIPITAPVLLMMDVDAIWLGVMMG... | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 408
Sequence Mass (Da): 43253
Location Topology: Multi-pass membrane protein
|
A0A2D4QUT7 | MKIVFLGSSDFSIPTFKKLIEAGHEIVCVYSQPPRRSGRGKRVNETPVHELALKYGIPIRTPESFKSDEDKSKFFNINADLSVVVAYGLILPPEILEAPKYGSLNVHASILPKWRGAAPVHRAIMSGESETGVCIMKMDIGLDTGPVVAKEIIAIEPHDTTSSLSERLAALGATLLVESIKKIDHLLPKPQSSNEISYAKKIDKQEAKIDWALDFQKIGRQIRALSRFPGAWSYYNGERIKFLNVRIVSSASVDSVKPGTVIKAPLVIACKGGALEIDSLQRPGKSIQTVDEFLRGFPIEIGSVFN | 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... |
A0A2E8PKP4 | MPFAPDVFRHCPGLEGRIQDPETSRFRDMEARIAELDAQIRLDGGDPDWRIPDDMREATRHALLDGRGGEDLWVFGYGSLIWDPAIHAAEFRRARLAGFRRAFCLHLEGGRGSPDAPGLMAALDADPGHVCEGVAMRLPAAIADEETRIMWMREMIAGTYHPAMVPLETPQGPVEAIAFLADARHERYVGDLSQRERASRIAVAEGRLGTNREYLENLLDSLHALGIDDPDMTELLRMVREAAGEAPVA | Function: Catalyzes the cleavage of glutathione into 5-oxo-L-proline and a Cys-Gly dipeptide. Acts specifically on glutathione, but not on other gamma-glutamyl peptides.
EC: 4.3.2.7
Catalytic Activity: glutathione = 5-oxo-L-proline + L-cysteinylglycine
Sequence Length: 249
Sequence Mass (Da): 27604
|
A0A314VUM4 | MPLKIIKLFELLSQRFTVFFLFLSSVFFCGVKLVSANDIFSGLETVGKPIPGGISFQPAVTELARDINWLDQMLFWIILVISIFVVLLLIYAAFKFNRKANPVPQTFTHHPVLEVTWTVVPIFILVFIGIFSLPLLYKQMEIPESDLTIKAIGNQWYWSYEYPEHEIEFDAIMLTKDELSEYGYSQDEYLLATDNPVVVPIGKIVRMQVTGADVIHAWKIPSFGVHTDAMPGRLNETWFKAEREGIYFGQCSELCGMAHSYMPIVVKVISQENFEKWLAYASEEFASLDSEIMLAKAN | Cofactor: Binds a copper A center.
Function: Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).
EC: 7.1.1.9
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(... |
A0A1D6LVA5 | MKGMYRENATANGEVVGGREPAAEPRAHEEYQHYGVKSHEYKAWAEIYLLSLTDMLVTTGKSTFDRLRGPGTRRAEAVGPAQTGQRHSWCSRDMSLEPCFRIAPPYDCKRRHDDSGEIVPHVRHCEDVRAHGAEAC | Function: May be involved in cell wall biosynthesis.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 136
Sequence Mass (Da): 15311
Location Topology: Single-pass type II membrane protein
|
A0A2A4XI12 | MPNKNAAMKFRQALHAEIPLQIAGVINAYSALLAEQAGFKALYLSGAGVANACFAIPDIGLTHFGDILQEAKRITTKCDLPLLVDIDTGFSNEISSPELVSQLIEAGVAAIHIEDQVTNKRCGHLDGKQLVSSEVMQQRIRAMVEHNDKNDLIIMARTDACSVEGLEPAIKRAIEYQEAGAEMIFAEALSSLADYHTFTTALNVPVLANMTEFGVTPLFTQKELARVNIAMALYPLSAFRAMNQAALLVYQTIKHSGTQREVTGTMQTREALYKILDYTSSTTISKDVVSTNSKEKSKDKRKGINTPFAEDSTPSKPRFD... | Pathway: Organic acid metabolism; propanoate degradation.
EC: 4.2.1.79
Catalytic Activity: (2S,3S)-2-methylcitrate = 2-methyl-cis-aconitate + H2O
Sequence Length: 797
Sequence Mass (Da): 88792
|
A0A520P9Q8 | MKQKIILASESSARKNLLQQAGVDFKCVAARIDEGAIKNSLQSEGAKPNEIVDTLAEYKALRVANNFPNDIVIGSDQILVCNNVILSKARTFDEAKKTLNLLKGKSHQLLSAAVIYENNKPVWRTVSRAQLFMRDFSDNYLDEYISTSNENILSSVGCYLLEDKGIGLFNRIQGDYFTILGFPLLEVLNFLRTREILKS | Function: Nucleoside triphosphate pyrophosphatase. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + H2O = a 2'-deoxyribonucleoside 5'-phosphate + diphosphate + H(+)
EC: 3.6... |
A0A3G1L142 | MAEAFISGLLKTDEYLPASLRASDTKEERLAYLREKYGIITVSDNEELVETSDVVILAVKPQNVREVLLHLKDKFTKGQLVISIVAGFSIDSLYQYIPKSVSVIRAMPNTPCLIRKGVSALAFSANITEEQKNLALNIMGSVGAVHILPEKLMNAVTGLSGSGPAYIFLVIEALCDAGVRAGLPREISLDLAVQTVMGAAAMVNSTKTHPAILKDKVITPAGTTIAALHVLERAGVRVAFMDAIMAAAERSQELGSEEGGKK | 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... |
A0A1D6L942 | MVCESDTDELLLEEKLAFVQETRHAFGRTALLLSGGASLGSFHVGVVKTLVEHKLLPRIIAGSSVGSIICSIVATRTWPEIESFFTDSLQTLQFFDRMGGIFAVMRRVTTYGALHDISQMQRLLRDLTSNLTFQEAYDMTGRVLGITVCSPRKNEPPRCLNYLTAPHVVIWSAVTASCAFPGLFEAQELMAKDRFGNIVPFHAPFATDPEQGPGASKRRWRDGSLEMDLPMMRLKELFNVNHFIVSQTNPHISPLLRMKELVRAYGGRFAGKLARLAEMEVKYRCNQILEIGLPMGGLAKLFAQDWEGDVTMVMPATLAQ... | Function: Lipolytic acyl hydrolase (LAH).
EC: 3.1.1.-
Sequence Length: 456
Domain: The nitrogen atoms of the two glycine residues in the GGXR motif define the oxyanion hole, and stabilize the oxyanion that forms during the nucleophilic attack by the catalytic serine during substrate cleavage.
Sequence Mass (Da): 50994
|
A0A0F6W3L8 | MAMVVVVGAQWGDEGKGKVVDRLTAQADVVVRYGGGANAGHTLVVGGEKVVLRLIPSGALHAKAKCVLGPGVVIDPEVLVQEIATLRARGLFGEGRLLISDRAHVVLPHHATIDTLRESGPGAIGTTKRGIGPAYEDKAGRRGIRMADLLDAARFRERLEANLEAWRPVIVALGGEMPAIDEIVKRYGELAKELGPHVGDASAALAEAREQGKHVLLEGAQGTMLDLDHGTFPFVTSSTVISGGACAGAGIAPTHIDRVMGITKAYTTRVGGGPFPTELHGEAGEALRKAGNEYGAVTGRPRRCGWLDIAVLRHAVRVNG... | 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 ... |
A0A961LYD9 | GLERIGALLQGKHDNYDTDLMRGLIEASANATDGAPDGPGKTHHRVIADHLRSTSFLIADGVMPSNEGRGYVLRRIMRRAMRHAHMLGAQEPVMYKLVPALVRAMGGHYTELKTAEALIAETLKLEETRFRQTLDRGLKLLDAELGKIADGSDLPGEAAFRLYDTYGFPLDLTQDALREMGRSVDTKGFDAAMAEQKAKARASWAGSGEAANQAIWFELAEKHGGTEFLGYDTETAEGQVLALVEGDTLVDEAQGEVSVVVNQTPFYAESGGQVGDTGFIRWDGGEAVVRDTRKVNGVFVHQAGVTRGALRRGAAVKLEV... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.
EC: 6... |
A0A0G0MTZ6 | MKTNTGPQKIKELLERGVEEVILADRLENQLKSGKQLRIKFGIDPTGPAVHLGNAIPLWKLKQFQELGHQVVLLIGDFTARIGDTSDKQAIRQPLEEEEIQKNLKTYKEQMAKILDLEKTEFVYNSEWLKKMSFEDVLKLSSQFTVAQMIERENFSGRYKSGKPIGLQEFLYPLMQGYDSVAIKADVEIGGTDQTFNMLAGRVIQRAYGDEPQNVLTLSLIEGTDGRKMSKSYNNIIGIADSPKEMYGKIMSMRDELMVKYFNLCTQLPVEKIKAIENALATGKENPRNIKAELAKEITRIYHGEKAATSAEQEFNQIFR... | 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... |
A0A920MN55 | MGLCSSFMLPRNGIGRQSFGKNVKMVDSPSNFRLLASRNEENESSNAVSRIWTMSDLYKNIEAKKVSLAVFSEDSNNNQVTVLDTNGEEHSVNLLQADLPTLVDLFRKNGVRFAVKSHGSKEMTGFLSGLASILIPFTFLSLMFFSFRNGGINPINPGGGMGGLQNMGNLNLEANTGVSFADVAGCDESKLELMEIVDFLKYPQNFTDIGAVSPRGVLLEGPPGTGKTLLARAVAGEANVNFISTTGSEFVEVYVGVGASRVRKMFKDAKKNSPCIIFIDEIDSIGRSRSGGGPGSNDERDQTLNQILSEMDGFSGNTGI... | Cofactor: Binds 1 zinc ion per subunit.
Function: Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.
EC: 3.4.24.-
Subcellular Location: Cell membrane
Sequence Length: 630
Sequence Mass (Da): 68533
Locat... |
A0A7C3Q375 | MAVIEVNINDLFRLLGKNLSEEELKEYLLKIKAELEEREGDNIKIEIKDFNRPDLLSVEGIVRELKGILNIETGIPTYKIENTDYEIIVDKSIINIRPYIACAIVEDVKLGKEGFSSLIQLQEKIMQSFGRKRRKIAIGTHNFDLIEFPIYYKAVYPREIKFVPLYGIREMYLDEILKETETGKKYSYILEGKEKYPILLDSKGEVISFPPIINSNRIGRIDENTKNIFIDVTGTDFNSVIVALNILVTALADRGGKIKSVIIKYPDKIIRTPILKIEEKEFDLNKIKKLTDLDLNNDEIVKLLNKKRIDAEILNGKIIL... | Catalytic Activity: ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + H(+) + L-phenylalanyl-tRNA(Phe)
EC: 6.1.1.20
Subcellular Location: Cytoplasm
Sequence Length: 551
Sequence Mass (Da): 63641
|
A0A257UHV0 | MFAAAVGLVFAAALLAAPKSGKRPPPREKPPAAESAADNERNAADDEEKPVRKTDREWKRLLTKKQYRVTRQRETEPQFSGKYVHTKKEGVYRCVCCGAKLFASQTKFDSGTGWPSFYAPLREKALRAAPDYSDGTPRVEVTCARCEAHLGHVFGDGPPPTGLRYCINSASLKLDEKPGKDGKPAK | Cofactor: Binds 1 zinc ion per subunit. The zinc ion is important for the structural integrity of the protein.
EC: 1.8.4.12
Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionyl-[protein] = [thioredoxin]-dithiol + L-methionyl-(R)-S-oxide-[protein]
Sequence Length: 186
Sequence Mass (Da): 20436
|
A0A6L5EST2 | MARVLFETFPGGVVRLSGLDVAFLCLEQPTRPMHLGALLTFEAPHAVAPERIARLLARRAAATPALTKSVRGTWWPPGGAEWVPAERFATGDHVFTHRLSDPGSAEQLSPLVASLMAPPLPRGLPPWQLHVISGFGQRRNRFAVLAKLHHALTDGAGVPLIAGPLLDGITPLPQRKPATPPAGSPLGRIWDWSRHTLDDVPQRVRDLAGEATTQLRRSGRAAGIASAALAAARPPWPVYPSAAGTGGPRRDWAQLRLDADTLRQVRERHGGTLNDVLLSVIAGGLRSWLSVIGDTAVLTDDRPLRAFLPVDVRSRNRTQT... | 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: 474
Sequence Mass (Da): 50174
|
H2L941 | MGKKEGEEPEHGEPAQFDPSFNGPLKKRSCTDIICLFLFLAVILGYIALGILAWVYGDPRHVLYPRNSTGWFCGVGPNKDKPNLFYFDILKCATSVNVMASALNGLQCPTTQVCVKQCPSGFWVVSPLDFAKSPKEVFDQNLCVPSASLTSGETVKGILDKELCPYYYTPTTPVLGRCLPDVTALGNIPPNFAHTGGLLPSSINDTVSLLKNGTGDILNGFNAKDVAIRIFEDFASAWPWILLGLVIAMLVSMLFLLLLRFTAPVMVWLLIIGLLAAGAYGIWHCYWEYDQYRAQGAKISDVGFTTNVKIYLQVQETWLA... | Function: Choline transporter.
Catalytic Activity: choline(out) + n H(+)(in) = choline(in) + n H(+)(out)
Subcellular Location: Cell membrane
Sequence Length: 714
Sequence Mass (Da): 79468
Location Topology: Multi-pass membrane protein
|
J0IS46 | MKSILLFMIFMVCQLEGKKFLQDNFKVDYNYYLRKQDLHIIKTQNDLSNAWYLPPQKAPKEHSWVDFAKKYLNMMDYLGTYFLPFYHSFTPIFQWYHPNINPYQRNEFKFQISFRVPVFRHILWTKGTLYLAYTQTNWFQIYNDPQSAPMRMINFMPELIYVYPINFKPFGGKIGNFSEIWIGWQHISNGVGARNAISLLIKTAILKTSFQEGL | Cofactor: Binds 1 Ca(2+) ion per monomer.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+)
EC: 3.1.1.32
Subcellular Location: Cell outer membrane
Sequence Length: 214
Sequence Mass (Da): 25663
Location Topology: Multi-pass membrane protein
|
A0A8J7C6R3 | MEKLSLAEVAQVTGAEKNSDAEIYFDGVSTDSRKITTNMLFVALKGENFNGESFAKDALKNGATAVLVSKTAKRVPEGVVLKVDDTLTAYSQIAGAWRNRFDIPIIAVTGSNGKTTTKDLTAAALTGLGNVNKTSGNFNNEVGVPMTLLELNDKHKAAVVEIGMRGLGQIESLAEVVKPTIGIVTNVSETHFELLGSIENIARAKGELVEAIQTGGTIILNADNRHTAAMKKLAGAGVNVVTYSLEGRADLVAKNILIGSVATEFTLSYGGKDYDFEIPMIGRHNVSNALAAIAAGLTVGLSVEEIQRGISTLTTTKMRF... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Involved in cell wall formation. Catalyzes the final step in the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the precursor of murein.
Catalytic Activity: ATP + D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-d... |
A0A832AMI6 | MTQQTSRWFDDVLLCIAFYTIVPLRLTDRQTGHAPADFARAQWAAPLAGIMIGLTGGGVFMAAQLAGLPALVTAVLGVAAGVLLTGALHEDGLADVADGFGGGQDRPKKLAIMRDSRIGTYGVLALIISFALRTGALAALAGQTSIWPGVLALVAAHGSSRAMLPLFVLQVPPARRTGLGAGMSALAPEGAVVALTIGFMALVPCDLLVVVFAIALLSAWFGFMRWLSLRQIGGQTGDVLGALQQGGEITVLLTASVFLVS | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7.
Function: Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-riba... |
A9GWQ4 | MTVLRFREAVRAAMIEEMERDERVYLVGEEVGHYQGAYKVTEGMLDKFGSKRVIDAPITESGFTGISIGAAMVGLRPIVEYMTWNFSAVAFDQILNNAAKLRQMSGGQLSIPLVLRAPNGSAKQVGSQHSHAMEHFYAHIPGLKVVAPAMPADAKGLLKSAIRDDNPVLFMESETLYGVKGEVPDDPDFIVPLGVASIVREGTDVSIIAWSRMVHVALEAAAELEKEGISAEIVDLRSLRPLDEETIVQSVTKTHRAVVAHEGWPYGGVGAEIADRIQRLAFDELDAPVLRATTLDVPMPYNARLEQYVIPQASRIIENV... | Function: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2.
EC: 1.2.4.1
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase] + H(+) + pyruvate = (R)-N(6)-(S(8)-acetyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue acetyltran... |
A0A0F6SFB7 | MKIAIIAVGRVKERGLRDAIDDYEKRIKRYAKLDEIELEDGSTSEVEARFRKAIPARARVVALEVEGRRMTSEKFARYVEQCEIGAVPALAFVIGGSYGLPKSVSDTADLKLSLSDMILPHRLARLFLAEQIYRAFTILRNEPYSH | Function: Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA.
Catalytic Activity: pseudouridine(1915) in 23S rRNA + S-adenosyl-L-methionine = H(+) + N(3)-methylpseudouridine(1915) in 23S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.177
Subcellular Location: Cytoplasm
Sequence Length: 146
S... |
A0A2E6N4E0 | MKKCTVFAPATVANVGSGFDVLGFALCDVGDTVHVKKSSTPGLVIESIIGANNIPSDPVKNVCTVAAQALLDCLEEKQENGYSFIITKEVAAGSGLGSSASSSAAAVVALNELLGSPFSRHDLIPFAMKGEALASGAEHADNVAPSILGGFTLIQSYEPLRVVNLHYPEELVVTVVHPHVEVKTVDSKRILKQNISLKTAITQWANVGGLVAGLAQENFELIGHSLHDVVAEPTRSMLIPMYEQVKIISREMGGLGCSISGSGPSIFVLTDSMEKAKNIADSLESLYMNNFISCDVYLSKINKMGCQVIQ | Pathway: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 4/5.
Function: Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate.
Catalytic Activity: ATP + L-homoserine = ADP + H(+) + O-phospho-L-homoserine
EC: 2.7.1.39
Subcellular Location: Cytoplasm
S... |
A0A965FW22 | MTKDLNERFAAAMVAVFDKVPEPLCLAVSGGSDSMALMALIASWQQQHSPATKVSVITVDHRLRPASAGEADFVKSRAKSYGFDHHTLVWTGWDGTGNTQNEARQARYDLINGHLGENATILTGHTLDDQAETVLMRIKRGSGVDGLAAMQPRMTQHNGLTVARPLLAFRRQELRTYLRAHAIDWVDDPSNENTQYDRVAIRALLPELEKAGISAEKFALMAHHMAHAQKVLQHAAQVAFDAIGEQTPIGLAFRETDFWTLERDIQTRLISAAIMWTSNVPFRPRYDTLTKCLGQVQTGHAQTLMGALMFRSRGKICVVR... | 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)... |
A0A3B3IDC7 | MAEVKEAVAELQHREDVGIQPGDGEATENEAESSEAAADAKPSTTTERHISIQTQLEGLEMLADLNGAGRKSCPLCSEEKFKACYSHKLRRHLQNLHWKVFVEFEGFRMCICHLPCRNLKPGISGDQASGRHVAHYHCVVCSVTIARKTDMISHLKRHVNKGETEASYSGSLDVQFEEPTPSGQAYEIMKELGTNVQLLPNYSTPQKSDTYFNRKMKTNRQLVFCSLAVLAEERNPLECLDAFGATGIMGLQWAKHLRNSVKVTITDISDTCVKMIKENCELNNIRVDGGSRTPRGNDAQPIATVEVVKMDANVIMHLRP... | Function: May play a role in motor coordination and exploratory behavior.
EC: 2.1.1.216
Catalytic Activity: guanosine(26) in tRNA + 2 S-adenosyl-L-methionine = 2 H(+) + N(2)-dimethylguanosine(26) in tRNA + 2 S-adenosyl-L-homocysteine
Sequence Length: 666
Sequence Mass (Da): 73860
|
A0A3B3I2X6 | MKKCVDDGGSRRGASLTVHPDLNTSAWPGPSTNVSGQPAVRVTRLSPAQQVLVVMVTASLSVVTVLGNLLVILSIKVNSRLRTVNNYFLLSLAAADLIVGLLSMNLYTLYRVRGQWPLGAALCDTWLVLDYAVSSASVMNLLLISLDRYLCMTRLQSYSAWRTRKMAGLMIGAAWVLSFVLWAPAILCWQSAGSRRVVPEGHCYIQLLVTASHEIRRSVEMEGWRHTDLLSRKDLHWRASEALSTFRCQEGRRQRVMARERRVTKTILAILLAFILTWTPYNIMAVVAAFCHICIPDVVWSLGYWLCYVNSAINPGCYAL... | Function: The muscarinic acetylcholine receptor mediates various cellular responses, including inhibition of adenylate cyclase, breakdown of phosphoinositides and modulation of potassium channels through the action of G proteins.
Subcellular Location: Cell membrane
Sequence Length: 339
Sequence Mass (Da): 37921
Locatio... |
H2M3T4 | MLKPGEKPDGAGRSADREDEESGRHEEELDPRIQEELEQLNQASEEINRLELQLDEARSSYRKILSDSARRLKALSSQLGACTERARPYYEARRLAKEAQQETQKAALRYERAVSMHAAAREMVHVAEQGLLADKNTMDPTWQEMLNHATAKVNEAEEERLRSEHEHQRVTQLCQDAEARVLTLQKALKKVILKSKPYFELKAQFNHILEEHKAEVVQLEKQVTAVKTRYSVALRNLEQISEQIHAQRGRTATCDGRSSPVGAEAEVKGPSTTPASSSTGAAAVEPSWVDMEKTRLWVEKHRESGWGRSESMEDCLSVTN... | Function: Functions as guanine nucleotide exchange factor (GEF) for RAB11A.
Subcellular Location: Cytoplasm
Sequence Length: 392
Domain: The N-terminal half of the protein mediates interaction with RAB11A and functions as guanine nucleotide exchange factor. Four long alpha-helices (interrupted by a central kink) assemb... |
H2MWM0 | MSFTFSFETCLPFCCIFFSEKERLLRANDRSFNLSFHYAKNEIKTSKYNIITFLPLNLYVQFTRLANVYFLLLLILQLIPEISSLPWFTTAVPLVIVLSITGVKDANDDINRHKSDRQVNNRTVEVLVDGKLKEERWKNVQVGDILKLQNNHFVPADLLLLSSSEPLNLVYVETAELDGCEHPNNRLDKFKGTLTVKGQTHGLDNDKVLLRGCTLRNTEWCFGLVIFGGPDTKLMQNSGQSKFKRTRIDRMMNILVLCICGFLVTICVILSIANSIWETNEGSAFTVFLPHLPDISVELSSFFIFWSYIIVLNTVVPISL... | Catalytic Activity: ATP + H2O + phospholipidSide 1 = ADP + phosphate + phospholipidSide 2.
EC: 7.6.2.1
Subcellular Location: Membrane
Sequence Length: 692
Sequence Mass (Da): 79267
Location Topology: Multi-pass membrane protein
|
A0A432YZM1 | MLSVVDTYSDALFAIETASHAFPWSETTLRNCLQQAGYQVVGYYQQHELQGFYVASQVCDEITLMDIAVHPSFQGQGIGRQLLAHLLAQATQSKATVFLEVRVSNTAAIKLYVKLGFQQVGRRPNYYPCGDKREDALVMVWRDDTSPS | 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: 148
Sequence Mass (Da): 16581
|
A0A7Y7DQJ8 | PTYVSATYIFLFILFGSFLEKAGMIKLFTDVSLGLVGHRMGGAAKVSVLSSGLMGTISGSGVANVVTTGQFTIPLMKRFGYRPAFAGGVEATSSMGGQIMPPVMGAVAFIMAETLGVQYVEVVKAALVPAILYFAGAFWMVHLEAGKRDLRGLSADQMPSARKALKEGWYLILPLAVLVWLLFSGYTPLFAGTIGLALTGMLILGAAIAMGMPSTAVRVIFWIVLGLCASAFFKFGIHALLLVIAVMIAACAFFRGGRETLAVCRDSLADGAKTALPVGIACALVGVIIGVMTLTGGANTFGQFIVSVGQNSLFLSLVLT... | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 507
Sequence Mass (Da): 52892
Location Topology: Multi-pass membrane protein
|
C0E9S7 | MHSYTRRTWAEINLDNLAHNYRHITRQLGTTRVIATVKADAYGHGEQHVASTLEKLGAQWFSVSNIDEAMALRRHGIRGDILILGFTPLEDAKELAEHQLTQTIFSHEYARELSSWAQSHQVTLPVHIKIDTGMTRIGFLCNGYENDLEGVRSLYSLPGLRITGTFSHLSHADSTDPDAIAFTQAQARHFDEAVSALKQLGCDPGLTHLQNSAGVICLSGGKYDLARPGISLYGLNPSAEVTDKELRPVLQLKSVISMVKQVGNGIPVGYGRSYVTSAPTRIATVPVGYADGYSRLLSNKGSVLVGGKRAPIIGNVCMDQ... | Pathway: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1.
Function: Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids.
EC: 5.1.1.1
Catalytic Activity: L-alanine = D-alanine
Sequence Length: 388
Sequence Mass (Da): 42213
|
A0A2D7G9N8 | MGQEAVVVGLEAAAAEGDKRITSYRDHGHMLAAGMDPNGVMAELTGRIGGYSKGKGGSMHMFSKEKHFYGGHGIVGAQVPIGAGLALADKYLGNGCVTFTYFGEGAANQGQVYEAFNMAALWSLPVIFVIENNQYAMGTAQNRSTSTPEIYTRGEAFGITGEVVDGMNIFAVKEAGERAVKHCRAGKGPFILEIKTYRYRGHSMSDPAKYRTREEVQKMREERDAIENVRSMLLGKKYASEEDLKVIDKEIKAIVNAAAEFAKESPEPASEELWTDIYA | Function: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2).
EC: 1.2.4.1
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase] + H(+) + pyruvate = (R)-N(6)-(S(8)-acetyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue acetyltr... |
A0A7X3YWB8 | MHFDLVSPEKSVASIEVDAVDLPGVEGDMTAMDGHLPMLTSLRPGFVKARVGGDETRYVVAGGFVEITADSVTVLADEVFPEEEFTTPVLDDLVSRLEETASTKEMQEKDKAEKRLGDAISLRSQISH | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane.
Subcellular Location: Cell membrane
Sequence Length: 128
Sequence Mass (Da): 13908
Location Topology: Peripheral membrane protein
|
A0A9E4I209 | MKHSVAVFFGVGRCPFAPGTAGSLAAALLALGLHELGGASLLLMSAAAATAFGFWSLDGQFEDEESDPPWVVVDEVAGQLIALLPVSLWFDLSETAETEHMIFGWLTGFLLFRILDIWKPWFIGRADKLAGATGIMLDDILAGATAGTILALIGVSGMMLGWIP | Pathway: Phospholipid metabolism; phosphatidylglycerol biosynthesis; phosphatidylglycerol from CDP-diacylglycerol: step 2/2.
Function: Lipid phosphatase which dephosphorylates phosphatidylglycerophosphate (PGP) to phosphatidylglycerol (PG).
Catalytic Activity: 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycero-3'-phosphate... |
A0A3D5PNV1 | MTDEGKVWPTGLTLGEAEEVHSYPIDGTRVFGAIALIAHILVAISTPWLG | Function: Antenna complexes are light-harvesting systems, which transfer the excitation energy to the reaction centers.
Subcellular Location: Cell inner membrane
Sequence Length: 50
Sequence Mass (Da): 5334
Location Topology: Single-pass type II membrane protein
|
A0A642UYY1 | MSSSLRKAVIGLTWLPVAYTVLNHGVSPCRITGRSMSPTFNPGTSTTAEDVVLVTKFGAKTASNIHRGDVIMFRSPRDPEKILTKRVVAVAGDTVYPKQPYPKQKAGVPRNHVWVEGDNYFHSIDSNTFGPISLGLVTGKVVAVVWPPSRWGADLSTGGRNPMDPLTV | EC: 3.4.21.-
Subcellular Location: Membrane
Sequence Length: 168
Sequence Mass (Da): 18171
Location Topology: Single-pass membrane protein
|
A0A7Y0L4K5 | MMTTSWREKVAIVTGGSRGIGRHIALKLAESGMKVAVNYRGNQERAQETEQLIRERGAECLLIPSDVSDIPKAQSLIDAVLEHWGRIDVLVNNAGIARDTLLLRMKDEDWTDVIQTDLTSVFACTRAAIKPMMKQRFGRIVNIASIAGMLGNAGQANYAAAKAGVIGFTRSVAREMASRNITANVVAPGLIDTDLTQHMSQDAFQALVKQVPLGRAGRPEEVADAVWYLVQADYVTGQTLVIDGGLVMD | Pathway: Lipid metabolism; fatty acid biosynthesis.
Function: Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP substrates to beta-hydroxyacyl-ACP products, the first reductive step in the elongation cycle of fatty acid biosynthesis.
EC: 1.1.1.100
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] + NADP(+) = a 3-... |
H2LGI3 | CRSLFQNVIWKHKGDRPSTLGDNTLIVDWMPQKDLLGHSQVKVFVAHGGTNGVQEAIYHGVPVLGIPLFFDQYDNLLRLQERGAGKILQLADLNGRTFEEGLKEVLHNISYRQNIQRLSCLHKDKPMSPMDQAIFWIEYVIRHKGARHLISEAYKMPWYSYHSFDVVLLVLAVETVLLYAIYAVFRFLCCRRKRKTKTKQN | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
EC: 2.4.1.17
Subcellular Location: Membrane
Sequence Length: 201
Sequence Mass (Da): 23342
Location Topology: Single-pass membrane protein
|
H2MLP7 | MLKKQERMSFGSTLWMLLFLICGVSLQESDYDHEYYEELEPTNCSVEEKIKGGYVTFSQGGLPGSLLTYHCGPGQYPSPVSSRLCEDDGEWTPMRLATGRLTSSATCKNILCPGQLQLDNGDFWPRNQWFRVGATQSFTCQDGFRLHGSPERNCTVSGDWTGSSPVCDKHEDDCDDPGIPPGAERSGGQFDIGDKVTYQCQAGLNLLGSSERVCMEQREWSGSTPRCQGPNTFDSPSYVAAAMAGSLAGVMDVVSPDFKKQKEGISFGRTIRVGDVSRMHIYILLDTSGSIKKKDFNLSREATIALIKKLDSYDIQLNFH... | Function: Component C2 which is part of the classical pathway of the complement system is cleaved by activated factor C1 into two fragments: C2b and C2a. C2a, a serine protease, then combines with complement factor C4b to generate the C3 or C5 convertase.
Catalytic Activity: Selective cleavage of Arg-|-Ser bond in comp... |
A0A2J9DVX8 | MPTQQNTPAPHNNSNSDSVDNIDNIDALDNSHHDQSLRQRLAQVRIVMINTTLPANIGSAARAMLTMGLTDLVVVAPKHPIDDESVSHAAGAQSVLNNCRIVDNLEQATADCQLVFAASSRQRHIPRPVVTPDQAAKLVLARPTHDTKVAILFGREDRGLTNDELALADYHIQIDANPDYPVLNVASAVQVIASFFYSRFLQHSQQPQGLTNTNEINNTDDSNQAIYNQALDNDLNSDLDNDLNSENLLMPVMLRQIWDSPAISHEQKLKLQLRIIELMYQLQLLEDTQTDKLRDLPSRLSRLLSRLQLDQKEYELLNAI... | Function: Catalyzes the formation of 2'O-methylated cytidine (Cm32) or 2'O-methylated uridine (Um32) at position 32 in tRNA.
Catalytic Activity: S-adenosyl-L-methionine + uridine(32) in tRNA = 2'-O-methyluridine(32) in tRNA + H(+) + S-adenosyl-L-homocysteine
EC: 2.1.1.200
Subcellular Location: Cytoplasm
Sequence Length... |
A0A2D7AFB6 | MDLFETPQQNIPKVSELTQRIKVLLEQHFTNISVLGELSNVKKSSNGHIYCTLKDSEAQLPCVMWRTQAQRYASLFEDGKEVILRGSIQVYKPQGKYQLIIDEVEAVGVGKLQMEFERLKKKLAAEGLFDASHKKPLPRFPTKIGVVSSRTTAAFQDIISTLSTRWPLAEISLYHASVQGERAAGEICEALEFLGKSNDIQVIIVSRGGGSLEDLWPFNEESVARAIYSCPIPVISGVGHEIDFSISDFVADQRAATPTQAAVLATPNRDDVLAGLDEYAERLHRRLEQRWNQAKQRVDYLAKSYALQKVQERLHISTMK... | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
EC: 3.1.11.6
Subcellular... |
A0A3C1B4Q7 | MTTSIENTKGASGKIVLSIDAMGGDRGPAAVVAGIARAAKQNAHLHFILHGKKSVLDLQVSKRRALWGRVDIRDTSDVVSMDDKPSQVLRLGKNTSMWSAIDSVRNGEAEVCVSCGNTGALMALSVIRLR | Catalytic Activity: a fatty acyl-[ACP] + phosphate = an acyl phosphate + holo-[ACP]
EC: 2.3.1.274
Subcellular Location: Cytoplasm
Sequence Length: 130
Sequence Mass (Da): 13828
|
A0A2D5BGR8 | MDALAERRQVALSVLPQPTGLNALDAGARLGRNFAPERQNEALSLFGAVSDHIKKMGAIKPVVITSYSSGARERLSGLLQDEGHGELREIRNIKDLRGAGTYLAVSQLEHGFETEDLVVITEQDILGDRLVRSTKKRKRADNFLTETQSLSPGDLVVHVDHGVGRFKALEIISAAGADHECLLLEYAENSKLYLPVENIELLSRYGHDEGLLDRLGGGAWQAKKARLKERIREMAEKLIRVAAERALRQAPLVDPPLGMWDSFCARFPYQETDDQSNAISDVIEDLGTGRPMDRLICGDVGFGKTEVAMRAAFVAACSGL... | Function: Couples transcription and DNA repair by recognizing RNA polymerase (RNAP) stalled at DNA lesions. Mediates ATP-dependent release of RNAP and its truncated transcript from the DNA, and recruitment of nucleotide excision repair machinery to the damaged site.
EC: 3.6.4.-
Subcellular Location: Cytoplasm
Sequence ... |
A0A4Q0IAU2 | MAMPALLAEGLCVAAGGAIGSLGRWGLMATGWFDSGRIWHTVTVNLIGAFLIGALWQICSSTTVTRHIQPFLFTGILGGFTTFSTLALDTTRLLSAGDALRAAIYLAISLAGGIAACIIGIWAAKTILT | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Subcellular Location: Cell membrane
Sequence Length: 129
Sequence Mass (Da): 13355
Location Topology: Multi-pass membrane protein
|
A0A966XH65 | PFEPPYMTAAGMSCDFVGHPVVEEPVASENAASAFRERYGLGNNPVVLCLPGSRISEVTRLAPVFMQTLSKIKERRPEVRFVLPAATEVVSELRAIISDWQEDIIFLDPRDQSPEQGLAHKRAAFRAADGALAASGTVSLELAASETPMVIGYDMSWISRQIIGRLVRTDTVTLVNLVSETREVPEFIGPSCTPSNLAKAVLEVLESPEKQLGAMRNTMQRLGKGETAPGERAAQSVLNFISQRK | Function: Condensation of UDP-2,3-diacylglucosamine and 2,3-diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
EC: 2.4.1.182
Catalytic Activity: a lipid X + a UDP-2-N,3-O-bis[(3R)-3-hydrox... |
A0A2E3AGR9 | MSQFETMKQIGDVXMSEKPKIAFAVLSTVLVVFSLYTAMFGVFPDMIQRGAHISAVIGLVYIRLFGLDGAXGLSWSRIKFFGLGVFGSAVLGYQFFFYEDVVSRFGSITSYEMPIAILAIILLLDATRRTIGWSMVGLAIFFLVYAFYGRYFPGLLAHRGYDMVRILEQVYLGADGIYGTPLGVSSTFVIIIVVLGALLXKTGASGVLMDIAVSMTRNSRGGPAKAAVVGSSLMGMISGTAVANVLTTGTISIPLMRRGGYRPAVAGAVEAVASTGGQLMPPIMGAAAFLMADIMEVPYLDITKAALLPALLFYIAVFAS... | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 632
Sequence Mass (Da): 66582
Location Topology: Multi-pass membrane protein
|
A0A0D1YDW0 | MLSYDKAPTAYHGTVLPYNNSNSNSASSSSSSPTTPTQRLARKMSQRDRHVFVVYGPAGCGKTTIAQYISKAFNFTYIEGDNYHPQSNVEKMSRNIPLQDADRWDWLINLREAAVAALEQDVDGVVLTCSALKKKYRDVIRIASINEHSVHVHFLCLQADRATLIKRVTARKDHFMGQKMVDSQLRDLEPIGSRETDVVPIDVRGTQAENEKLAEAAVVSILS | Pathway: Carbohydrate acid metabolism; D-gluconate degradation.
EC: 2.7.1.12
Catalytic Activity: ATP + D-gluconate = 6-phospho-D-gluconate + ADP + H(+)
Sequence Length: 223
Sequence Mass (Da): 24867
|
B5YFZ1 | MDQLAYDEYFMKEALKEAEKAYEKGEIPVGALIVVNGEIISKAHNIKETTFDPTAHAEILAIREAARILGAWRLTDATLYVTKEPCIMCSGAIVNSRIKRLVYGCNDPKGGAVVSLYNILNDKRLNHQVEITNGILEEECRVILKRFFKELRED | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the deamination of adenosine to inosine at the wobble position 34 of tRNA(Arg2).
EC: 3.5.4.33
Catalytic Activity: adenosine(34) in tRNA + H(+) + H2O = inosine(34) in tRNA + NH4(+)
Sequence Length: 154
Sequence Mass (Da): 17400
|
H2L8S0 | MAAADPRYSRGGFPAGESSNDRDGPGGGSGESERDRATFECNICLDTARDAVISMCGHLFCWPCLHQWLETQPSRQQCPVCKAGISREKVIPLYGRGSSSQEDPRLKTPPRPQGQRTEPESRGGMFQGFGDTGFHMSFGIGAFPFGFFTTVFNANDPFHRADQYAGDHQGNGNGNNSWQDSLFLFVAIFFFFWLLSV | Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.27
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Length: 197
Sequence Mass (Da): 21735
|
A0A7C2IP48 | MTPPYGLVLAGGEGRRMGGPQKALVRLGGRTLLDRAVAALGPQVTRLAVSWNGDPADLAGLAPDVIADAPAAGGRQGPLAGVIAGLRWAGARGARLLATAPVDAPFLPAGWVAALAAEAGPGPVLARSSAGRVHPVVALWPVSCLAALEADFAAGTRGVMAAADRLGGRPATLEAPEEAFMNVNTPEDLRRAEAMLGRRD | Function: Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor.
Catalytic Activity: GTP + H(+) + Mo-molybdopterin = diphosphate + Mo-molybdopterin guanine dinucleotide
EC: 2.7.7.77
Subcellular Location: Cytopl... |
A0A2D9IQJ4 | MELNDFILELISEEIPAKMQTPAIRQLERLTLKKVGENGLIVEKMKPFVTPMRLGITLENISTKVNESIQEIRGPRLGAPENAIEGFLRKNKIGRGELKEKKTEKGDFYFYTVKASAQSLSKILSRIFTEIIQEFNWPKSMYWGDNYSLKWVRPLRGIVAVLFQNETRERVPLSVRGIDSGIVTRAHQVMHPEFFEFDSIDDYREKMLKGKVILQPQDRRKSVVQEGKKQAEARGFYLVEDDKLLDEIVGLTEFPIPILGEIPKELLSIPEEVIITSMREHQKFLSLRSSASRKVEGFLVVADLQTNDKQKTILSGNMRV... | Catalytic Activity: ATP + glycine + tRNA(Gly) = AMP + diphosphate + glycyl-tRNA(Gly)
EC: 6.1.1.14
Subcellular Location: Cytoplasm
Sequence Length: 687
Sequence Mass (Da): 79061
|
A9GLV8 | MKTWIDGRIVDAADATVNVTDHGLLYGDGVFEGMRVAAGRVFRIERHLARLEIGARALGIALPRSLDGLRAVVEETARAHGQPEAYVRLVVTRGVGPLGVDPTTCERPGLFCIVGAIRLFDDEQRRRGLELITSSHRRPNADALDMRIKSLNYLGSALAKLEARQRGADDALLLNARGHVAEATVANVFALRGDVLATPPATDGCLEGINRAAVMELARGIGLTVVERSIGRLDLFAADEAFLTGTGAGVIAVRSLDGRTIGRGERGPVTARLTSLHRQLAETEGAPFITAPGGPG | Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 4/4.
Function: Acts on leucine, isoleucine and valine.
EC: 2.6.1.42
Catalytic Activity: 2-oxoglutarate + L-isoleucine = (S)-3-methyl-2-oxopentanoate + L-glutamate
Sequence Length: 296
Sequence Mass (Da): 31420
|
E3H7G6 | MERIGVYGGSFNPVHTGHVNIIKYVLENMKLDRLIVIPVGCPSHKDNLLLNGNKRIKLLEVACKDIDKVTISDIEIKNKGVSHTYDTLLNLKKKYKDAIFYEIIGEDSADYLHEWKDYEKMVKECKFVVLKRNGYAYRAEHENIIVLESPLYRYSSTEIRERLKKGLDITGMVPRKVHEIIIKEKLYR | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
EC: 2.7.7.18
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide... |
H0XBC8 | GRKRRGLVPDAAAATATATAAAICHLSSGTSPVASAPSAASAEPPSGPATSLRYLRPPMDLVGVASPEPGPAAAWGPSKCPWATPQNTISCSLADVMSEQLAKELQLEEEAAVFPEVVVAEGPFITGENIDTSSDLMLAQMLQMEFDREYDAQLRREEKKFNGDSKVSISFENYRKVHPYEDSDSSEDEVDWQDTRDDPYRPAKPVPTPKKGFIGKGKDITTKHDEVVCGRKNTARMENFAPGFQVGDGIGMDLKLSNHVFNALKQHAYSEERRSARLHEKKEHSTAEKAVDPKTRLLMYKMVNSGMLETITGCISTGKE... | Function: Involved in regulation of type I interferon (IFN)-dependent immune response which plays a critical role in the innate immune response against DNA and RNA viruses.
EC: 2.7.11.1
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Length: 577
Sequence Mass (Da): 64423
|
A0A4Q0I9D0 | MNQPNRQISMTFLLLAVTFCVCLITANLMEIKTVPLGPFTITAGVVVFPVSYIIADCVVEIYGLRRARQVIWLGFAANLFVSVMLQIGILLPGTDSWHSQEAMTTMFGAVPRIFAASFIAFLAGSMVNAYVMHRMRLAHPDGSRFSLRAIVSTLFGEGADSLIFFPIAFAGELPAGVIISLIATQALLKTLYEIIILPVTIQVVRLLRRTEDRHIHTEEA | Function: Involved in the import of queuosine (Q) precursors, required for Q precursor salvage.
Subcellular Location: Cell membrane
Sequence Length: 220
Sequence Mass (Da): 24242
Location Topology: Multi-pass membrane protein
|
A0A8J7C839 | MRVAASLMSADFAHLADEIRHVTDAGIEQIHIEVGDGVFSPNITVGAPVVKSLRKVTEAIFEAHLMTIKPEDKIVEFAQAGADLITFHIEATEQAQSVIHKIKGAGSKAGIALNPATPLCMIEELLYDVDVVLLMTAIPGSAGQPLLKHSLDKVKRLHNIIRENDYGCLLEVDGGVTIENAQALREAGANILVSGTAIYESTDVWASVSMLKGE | Cofactor: Binds 1 divalent metal cation per subunit.
EC: 5.1.3.1
Catalytic Activity: D-ribulose 5-phosphate = D-xylulose 5-phosphate
Sequence Length: 214
Sequence Mass (Da): 22904
|
A0A0F6YM51 | MDESTPRYPTVHVEVPENDVDEASAMLWELGASGVEERDASTLDKPVEGGALLVAHFDDEDEARIATEALIGEERGWSARIEHIVGDEWKHRWREFFKPTRIGNRLVIRPSWEQVDAREGDVVLTLDPGQAFGTGTHETTRLVLAELEWWVRGGEHVLDVGCGSGILSIGALLLGAADAVAIDNDELAIDATNENAEANGVADRVKASTTPIEQIEGRWGLVVANIEARVLLPMAEALMARVAPGGMLVLSGLLLQDEDEIRRAYAAMEPVARRQERDWIALTFRAPEARARERSDDVQDANGHGSQAQGATTAEIDELA... | Function: Methylates ribosomal protein L11.
Catalytic Activity: L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
EC: 2.1.1.-
Subcellular Location: Cytoplasm
Sequence Length: 576
Sequence Mass (Da): 61007
|
A0A963XBX9 | MKLVVTTPMAVIVEADGVTHVSAEDETGRFGILDRHADFITALAISVVTWRGSDGGESHIAVRGGMLEVRNGNLISIATRDAVPGDDLRQLESDVLEGFRQRVEAERISRTESQRLYLAAIRQICRFVRAERTPGYPDTSASQSNDGFSA | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane.
Subcellular Location: Cell membrane
Sequence Length: 150
Sequence Mass (Da): 16374
Location Topology: Peripheral membrane protein
|
A0A3B3HSL6 | MSHLRPRLCLMEKGVAGYGFHLHGDKGKSGQFIRLVEPDTPASAAGLLAGDRLMFVNGENVEGESHQQVVSRIRATSGALELIVVDDETAELLKKHNLQCRREFVTEGIPVPGRDSDSDRGDAQSNGTPREASPQPASQPASQPASQPASQPASQSASQPVSLFLPSDLPDGLRPRLCHMKKGQSGYGFNLHSEKSRPGQFIRAVDDHSPAQRAGLRPLDKIIQVNGVPVAGMQHSEVVAAIKAGGDETRLLVVDAETEEFFKKCNVTPTEEHVTGERFHIPIHVCVFQAAAELKPKESVSSRASSVSSSSSLQQAAPSS... | Function: Scaffold protein that connects plasma membrane proteins with members of the ezrin/moesin/radixin family and thereby helps to link them to the actin cytoskeleton and to regulate their surface expression.
Subcellular Location: Endomembrane system
Sequence Length: 373
Sequence Mass (Da): 39922
Location Topology:... |
A0A966NDA9 | MSRLLSILTLFCFVLLSLYPFAWMFFSSFKTNKEIYQPSQLLPEKFDAQAYGMLLDGKFVDFTGSLWQSVMIATLQALLATFVSALAGFVLARYSFRLKAFLIGAALLIILIPRQALVVPVFEWFHWLGWTGNSFSLVLCGIASGLGVVFFSQSFRQLPVELMEVSRLEGFSPLRSFLLVIPLFAPSMVTYFLLHFALCWQEHLLALLLLDDSSLTLPLALAKLSDVSHRAPESIGMAAATLSFLPIVFLFALFFRKMRTALSQLSLS | Function: Part of the ABC transporter complex UgpBAEC involved in sn-glycerol-3-phosphate (G3P) import. Probably responsible for the translocation of the substrate across the membrane.
Subcellular Location: Cell inner membrane
Sequence Length: 268
Sequence Mass (Da): 30049
Location Topology: Multi-pass membrane protein... |
F7UV47 | MADSKDIEEAARRVTDAHAYLHVDEKRAELEKLDAESAKPGFWDDAAHAQSVSKQASVLRDTIAEYEDAATLLDDARAAFDLASEDEAFAEEADEALDKLDGLLDTLEINSWFSERFDSGDAILTVNPGSGGLEAQDWTDMLYRMYTRYAEKKGWKVTILDVVPGEGIGLDKATIQVEGRNAFGMLKSENGVHRLVRISPTDDKKRRHTTFAGVEVLPVLPDDIEVDLNPADVRVDVYRSSGPGGQCVNTTDSAVRLTHMPTGIVVTCQNEKSQLQNKEAAFRVLKAKLYELEEQKRAEELAQLRGERMDSTFGSQIRNY... | PTM: Methylated by PrmC. Methylation increases the termination efficiency of RF2.
Function: Peptide chain release factor 2 directs the termination of translation in response to the peptide chain termination codons UGA and UAA.
Subcellular Location: Cytoplasm
Sequence Length: 362
Sequence Mass (Da): 40366
|
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.