ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
|---|---|---|
A0A1V5LC86 | MIREAVEAFNIKSVELEGYEADDLIATYAKLGIEAGMNVKILSSDKDMMQLIGLGIELYDAFDFSLVDNEKVMQKFGVTPDKVIDVQSLAGDSSDNVPGVKGIGPKTASSLINDFGSLEGIYENLDKISKPRTKALLEEHKDLAFISKKLVTLCNHAPVEVGLKDLEIINPDFDKIMDFMRANEFKSLMNSLPNWQEKREEVIRKVKSESAKYITVDEEKDLKEWVERAINEGVVAFDTETDSLDSFSANLVGFSLCIKEGEACYVPLNHKAKQESLFEETSIKPKQIDFNKALEILKPLLTDESVMKVGHNIKYDMNVL... | Function: In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity.
EC: 2.7.7.7
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Length: 818
Sequence Mass (Da): 92021
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A0A950XUB8 | MPTEETSFLFRHPSRAVLRRELRDFWNDLVRRIPLPGATCLISTDIELRALNKRFRRKDHGTDVLSFPGDHGAPGEIAISLDRARAQALEHGHSVEEELCILMLHGALHLAGMDHESDSGDMARAEARWRRRLGLPRSLTERAGRAGFRTQARLQPRPRAGAPKRPSQAKACSTV | 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: 175
Sequence Mass (Da): 19655
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A0A3S3TSY1 | MGVCKISDPGAVEAFDPARFTEEKVAEIRRFVGDGKAAIATSGGVDSTVCAALAHRALGERLVCFFLDTGFMREGEVEEVKGILTSLGLPLRILAVSDRFMAALKGKSDAEAKRIAFRETFYTVLGEAAKAEGCDVLIQGTIAPDWIETAGGIKTQHNVLEQLGVDTKTSFGFRLLEPLLELYKDQVRRLAVHLGVRLDASQRQPFPGPGLMVRCIGEVTEEKMEVLRKATAVVEGELSRLDPPPKQYFAAVTEDDRREADSRMARSAVGPNGRAWYLGARVTGVKGDERAYGRMVVVEPGDQADPADLLGIVERVIHED... | Pathway: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln route): step 1/1.
Function: Catalyzes the synthesis of GMP from XMP.
EC: 6.3.5.2
Catalytic Activity: ATP + H2O + L-glutamine + XMP = AMP + diphosphate + GMP + 2 H(+) + L-glutamate
Sequence Length: 396
Sequence Mass (Da): 43097
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A0A1V5LAP7 | MANLKQLKQRIAVVNSTKKITSAMKMVAAAKLRRSQDALNATRPYSEGMKYLVGKLIKNVIAHGPTGQEMPLLIKGNGDDKKHLLLIVSSDKGLCGGFNSAIARLAKKTITDLKKQGKDVQIMFVGKKARDALISEFKDLEFKQTSKNDDNQPQKLNFFDETVGAMIEHLFEDNAFNCCSVIYNEFVSTVTQKPTVKQVLPLNIKDFEQEFKNEENQKADYDYEPSEKEILEKVLPDYVQNLISRSILESFVAENAARMTSMDAATRNAKEMINKLALIYNRTRQSMITTELIEIISGAEAL | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex.
Subcellular Location: Cell membrane
Sequence Length: 302
Sequence Mass (Da): 33934
Location Topology: Per... |
A0A2E5FJE9 | MDSHSFRGCRYEIKKAVHTGSSGLVKIAKESRYVTIARLLRPRGNRGELVAENLNSETSEAQDDSLKNFLKLDTVFFWDSNQQRQETAIEQAWVHRGRLILKLRGVDSIGAAERLRNINLQIPQEYLEPAPDNGYYFEDLIGCVVHDIEDGHLIGLVEEILEPGGPLLLQVKMDNHEVLIPFVKDICVEIALGEKTIRVRMPDGLESLNS | 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 ... |
B5Y8Y6 | MGNKGTQQEGVMELKEFVGQTTAVSSVSFSVEAAKKLGKMPDHMLFFGPPGLGKTTLARLVAQEVAANFVETTGNSLTNVKDVLNILLSFSRPTVFFIDEIHRIPKSVEELLYAPMDEQVIRVMVGKNKTARIIKFDLQPFTLIGATTKISFLSKPFLSRFSIKISFNYYGEEEIGKIIKEELAQQGLDISAEALREIAKRSRGTPREALQICRRVVEYAALNHLETLDVGAIIDLFNLLNIDEYGLSPLDKDYIRTLAETFKGGPSGIRVLASALGMDVETLEGVVEPYLMMLGFVTVTSRGRKLTDKGWKAYEKVICS | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an ... |
R5QJ61 | MREDFLSVIAARGDTQIKQNEGLAKYSTFKIGGEARYAIFPENKNALVFAVAACREFDIPCRVIGCGSNVLFDDGGFSGAVIFTKWVNKTEVSENIIRSECGLPLSALSTIAKNASLSGLEFAFGIPGSVGGAVYMNAGAYGGEIKDTLTEVEYFDTETETLHRAPAAELALGYRESIFQHKSYLLLSATFALHRGDRAEIEEKMASNMAARKDKQPLEYPSAGSAFRRPVGHFAAKLIDDAGLRGLSCGDAQVSEKHAGFIINRGSATSSDVLELCRIIKEEVAGRYGVSLETEFIHIKD | 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: 301
Sequence Mass (Da): 32583
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A0A0D2LRU2 | MCSQDHATCACVRCQVVNCVGLLNYKFFLQFLFYTLLASCLAIALMVQPMVAFVTGTDFTGAPGPFIVVVMDGAFAAALIGFLGMHWQLLAHGCTTIEMYEKERANPWPYDRGFRRNFEDVMGRSMQPNALTAAAAICPRLRDSILSRAAIAEQILLHDTDAGTIITRLQPALAAPSADSPAAAAAAAETPALSSPRGAGHSPRHGHSRGARQPSHARPPAGLGALELVVGWAELEQLLLEQLPAGTVEWGSRVTRLQEDAQHVRLTVGRSGDSGSSDSNGGGEGSSEAGVIIIDAEVVVAADGALSAVRQACVGGAEKA... | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 347
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 36131
Location Topology: Multi-pass membrane protein
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A0A4Y3PJ11 | MKPLALEQATINAEGLLLAGSPHLVLSSVHFDTRQLKAGSLFVALTGGARDGHDFLLQAAEQGAVAALVSNQEKIPAGLPEEFGLILVNDTLRGFQKLAAAYRKDFAIPHIAITGSIGKTTVKDIVAHVLEARSPVYKTYKNLNNHLGVPLSLLQMEPQHQAAVLELGMNHAGEIDLLASLVKPEISVITYIGESHLEFFGTREKLALAKAELLPHTAPDGLVLLNKDSEYLPRVAHLYAGEIMYYSVLEPCDIWAEHIQPNDNGTQFDVCFANGERFSAFLPLHGKHSVLNALPAIAIAKRLGMDTEQIVQALSTVKLS... | 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... |
F0S203 | MKLFDIEAEYSVLGSMIVQPSFIFRGVELLQPEDFFKEQNKVLFRFIRDLIAEGYTETQLNEISFKDELIKRNLFEKVGGEEHLGYVVEFALDSYEKFESACKIVKDKALLRKIIDVAKHINEKVEETPDPDTLIDDIEKRVFSLSEERITNTLTPICEVIPEIVKKIEELASRREMVTGLPSGYTELDRMTSGFHDSDLIILAARPSMGKTAFALSIAYNIAVKEGKTVAFFSLEMSKEQIVTRLISQDSGVPLHKIRSGFLFPQEIDKILESADRIREAPIYIDDTPGITILEMRAKSRRLQSEKGLDLIIVDYLQLM... | Function: Participates in initiation and elongation during chromosome replication; it exhibits DNA-dependent ATPase activity.
EC: 3.6.4.12
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 904
Sequence Mass (Da): 104222
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A0A957AY83 | RLEFLGDAVLGAVAAEYLYVEDPDADEGQLTRRRVALVRAETLVRWAREIDLGSYLYLGGGEKPGEGARDRMLAGAFEAVIGAIALDRGFGAARKFVMQLLERDADLLLTQAEGAGNPKGRLQELLQERHRQGPKYRTVGAEGPDHARTFSVEVLFGDEVLGAGSGPSKREAEQAAAAQALRRLNAG | Function: Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the o... |
W4VLV6 | MYEIKQYLQNRDDVYSIINGIESGLKEQLVSGLSGSARSMFTSMLQEASNKKTIIVTHQLTQAQQLYDDMLEFSNEQHVYLYPVNELLASELAVQSPELQSQRIASLSNWLHNKTGILIAPPVAALKRMLPPIEYWEEYQLHFKLTQVIDIEDTIQKLVDMGYARQEMAASPGEFSLRGGILDVYPITEVQPIRIELFDDEIDSIRYYDAESQRTLEKISEITVLPATELLLKDHDIVASAQKLEQSLADMLKKIKNKLDQQNLNESITADIDRLQHCERFQEMKKYISFFYEHNYSLLDYLSKDGLIVLDEMSRIQETA... | 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 ... |
A0A1B1ADA8 | MSLRACFAVLEAGQPLPTETVDGAFREIMDGVAAHDDIKRFLTLTTPLMHDPSLIASGARALRSRMVGLTAPAGAVDVCGTGGDGAHTLNISTAVAFVVAGCGVPVAKHGNRAMSSKSGAADVLEALGVRLTGDIALLERCLREARVAFLFAQNHHPAMRHVALARREIGKRTIFNLLGPLSNPAGVKRQLVGVFSADFVDPVAGALHQLGCEKALVVHGAGGLDELSAAGQDANCVATLDGGQIAHQPATRAADVHPDLRGGAAQENAEEMRAMLSGGGRPGHRAAVLINAAAALFVAGRAAGVVEGHRLAIESLDSGA... | Cofactor: Binds 2 magnesium ions per monomer.
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 2/5.
Function: Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).
... |
A0A2W4JNN3 | MFYRGRARGGSPALSGEGDERADWVHVDVMDGHFVPNLTLGLPVVQSLIAVSEVPIDCHLMIEDPDRWAPAYAEAGAHNVTVHAEAATDPVMIAKNLRAAGAKAGLSIKPQTALDDFVDVLKHYDTLLIMSVEPGFGGQAFIPHVLEKVRAARNLVDTGHLRLLVEIDGGINADTIEQAAEAGVDCFVAGTAVYGADDPGKAIAALRRKAAEV | Cofactor: Binds 1 divalent metal cation per subunit.
Pathway: Carbohydrate degradation.
Function: Catalyzes the reversible epimerization of D-ribulose 5-phosphate to D-xylulose 5-phosphate.
EC: 5.1.3.1
Catalytic Activity: D-ribulose 5-phosphate = D-xylulose 5-phosphate
Sequence Length: 213
Sequence Mass (Da): 22554
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A0A350UFW4 | MPRIRLTLTGAVQGTGFRPFVHRLAGELGLSGWVRNTAAGVVIEVEGASAEEFRLRLCAECPPAAWIAQLEATQLPPARLSGFKILESEDEDQPVAAILPDLATCPECLAEIRDPDARRFRYPFTNCTRCGPRFTIVESIPYDRPHTTMQGFALCGDCAAEYRDPADRRFHAQPIACPVCGPRLSERLECASEALKSGQIVALKGIGGYQLLVDARNESAVARLRERKSREAKPFAVLAPDLEAVRAVAEVNGEEAGLLESAAAPIVLLRARPDSGLAASVSQGSPWVGVMLPCSPLHHLLLDQFPHPVVATSGNRVGEP... | Pathway: Protein modification; [NiFe] hydrogenase maturation.
EC: 6.2.-.-
Catalytic Activity: ATP + C-terminal L-cysteinyl-[HypE protein] + carbamoyl phosphate + H2O = AMP + C-terminal S-carboxamide-L-cysteinyl-[HypE protein] + diphosphate + H(+) + phosphate
Sequence Length: 712
Sequence Mass (Da): 77066
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W4VQN8 | MFNEHITFPIDTLAVNLAGSFLLAYLTTVVFTKWRIHPLYKTAIGTGFVGSFTTFSTLSVETMDLFQNHYYFLGILYIALSIFGGLWMSRLGFKVRKEVTEG | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Subcellular Location: Cell membrane
Sequence Length: 102
Sequence Mass (Da): 11585
Location Topology: Multi-pass membrane protein
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W4VLM9 | MKNLTSAQVRQMFLDFFKEKNHGVEPSASLVPKDDPTLLWINSGVATLKKYFDGRVVPENPRITNAQKSIRTNDITNVGYTARHHTFFEMLGNFSIGDYFKEEAIDFAWEFLTGKQWIGLNQEKLSVTVHPEDEEAYVLWRDKIGLPEERIIRLEENFWDIGEGPSGPNTEIFYDRGAAYGGEDATDPELYPGGENERYLEIWNLVFSQFNHNPDDTYTPLPKKNIDTGMGLERLVSVIQNTKTNFETDLFLPIIRETEKLANTTYNASEATDVAFKVIADHIRTVTFAVSDGALPSNEGRGYVLRRLLRRAVRYAKQIG... | 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.
Catalytic Activity: ATP + L-alanine + tRNA(Al... |
A0A1H9VMA7 | MKKKLFAAITAVCLLAVAFMGCGFEGTENGDLKGNITLAGSTSMEKLCEAMSESFMEANPGVTVTVEYTGSGAGLESLAAGSVDIGNASRGLKDGEKANGSVENVVAIDGIAVIIDKNNSVTDISSENLAKIYTGEITNWNEIGGEDQPIVVIGREAGSGTRDAFEELLEVKDACAYAQELDSTGAVLAKVASTPGAIGYVSLDVVDSTVIGLKIDGVEPTEEQILAGSYLLQRPFVMATNGEIGEQNELVQAWFAYINSDAGKEVIKKVGLIIPQ | Function: Involved in the system for phosphate transport across the cytoplasmic membrane.
Subcellular Location: Cell membrane
Sequence Length: 276
Sequence Mass (Da): 28766
Location Topology: Lipid-anchor
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A0A4R4YLT9 | MIFAPRREDVIVFDAPAYWHSGGSGRPQVSRVIGVPGAEVECCDGSGRLLVDGAPLEEPYLTEPASKLKFRIRVPQGRIWVMSDHRHISRDSRYHQGDGGDGTIAVSDVIGVVDLP | Catalytic Activity: Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.
EC: 3.4.21.89
Subcellular Location: Membrane
Sequence Length: 116
Sequence Mass (Da): 12652
Location Topology: Single-pass type II membrane protein
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A0A956ZTK6 | MRVGLIGNPIAHSRSPRMHNAAFAALGMNHTYELWETEPDDLAERVATIRQSEILGSNVTVPFKEKVVSLVDEVSETSRRIGAVNTIIPHDGKLIGDNTDAYGYAASIRESYPGYTPERALVLGAGGASRAVIVALQEMGAGEVIIVNRTLARAEELAAELGASAAGWETLPDLMPTASLVTNATALGWYDERVLDESMVAMLPQGAIVTDLTYANTPLLQDAAAHGLHTLDGLGMLVYQGVRSFELWFGITPPVDVMWAAARG | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.
Function: Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydr... |
A0A318N1S7 | MASVVLIINAGSSSLKFSLYRSQNNSDFELYSKGLLEGIGSGPHLKITDRQDKIIHEKNWTNGRYAKLDVRDELLDQVLKWLFDFIKKDRILAIGHRVVHGGMKYYRPVVIDQKIYSYLDSLTPFVPLHQPASLAPMKVIMDKYPDITQVACFDTAFHATMPDKAKRFALPRKYYDSGLRRYGFHGLSYHYIVHYLQKNKSPLIKGKIVVAHLGNGSSVAAINKGKSIDTSMSFTPLDGLVMGTRTGQIDPNVVLYMTREEKRSPDEIEDIIWKQSGLLGVSEVSSDMRGLIHEIAQNGPKSKFAKQALDLFIYKLIGEI... | Cofactor: Mg(2+). Can also accept Mn(2+).
Pathway: Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis; acetyl-CoA from acetate: step 1/2.
Function: Catalyzes the formation of acetyl phosphate from acetate and ATP. Can also catalyze the reverse reaction.
EC: 2.7.2.1
Subcellular Location: Cytoplasm
Catalytic Ac... |
A0A1Y0I4Y5 | MKTVVGLIILAGALLLGTLAGTLMLHDAGYVRVSLGHYMFESSFWFALCLIIGLFATIYLIFALLFRSLRGFQGISQWIDRKSQDAANREVTKGMLEYTEGNWPKALKHLKGSASKANSPIVNYLAAAQAANEQGLVHDAEEMLQKAREVPGSELAVGLTEAQLMVNNNQLESAVEKLKTLHSLAPQNPQILRQLKALYSQLQDWPQLTQLIPELRKKKIFVASELDELEQQCWTNVLQETTESIQKTMGSSYNPAQLEAVWEKIPSDLRKSEPLLLAYSASLRAIKHDDRAEMLLRKTLKQNWNDQLVLEYGLIRFSSP... | Pathway: Porphyrin-containing compound metabolism; protoheme biosynthesis.
Function: Involved in a late step of protoheme IX synthesis.
Subcellular Location: Cell inner membrane
Sequence Length: 414
Sequence Mass (Da): 46670
Location Topology: Multi-pass membrane protein
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R6S2T0 | MIRISSHQQNNPIQGKEEDVRDVAIRVIRILSRSWKDRMLTDEPFVMAARDIYPSEALQFDKAKVLGFVTMYGTINSHTAVLARTKGIPAVIGLGESLKEEYDGKTIIIDGYEGKIYIEPDYATLTKMRERKDANLRHVRNLERLKGKENITQSGQKIDICANVGTREDIENVLRSDAGGIGLFRSEFLYMEMGSKLPSEEQLFQVYKLAAESMGANRVVVRIADFGGDKMVESVDLGEQANPAIGLRGIRIMMEKEELFLPQFRAILRASALGNVSIMFPMVTSMEEVAAAKALLEKAKKQLKDEKTAYNENIEIGVMI... | Function: General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. Enzyme I transfer... |
A0A066TK07 | MKKLLWVLFKSNLIVRMLVCMIIGAFIAAFLPQYGVKLEFLGRVFIQALRAAAPILVFVLVISSIVNNKFDNVSSIKSVAWLYAVTVLISAVLASTVSYLYPLHLVMDVPPISEKPPEGVAEILMNIILKFVDNPVDALANGNFLSILAWSTALGIALRQSSEATKSVIKNWSDATIWVVRLVVAIAPYGVLGLVASHFTSDGLAKLRNYLELIGILLGLMVFVALVINPLIVFLNFRKNPYPLVFTCLRYSGITAFFTRSSAANIPVNIRLAQRMQLPEEIYSLSIPLGVTMSMNGAAITITTLTMATVHTLGMDVSFI... | Function: Involved in the import of serine and threonine into the cell, with the concomitant import of sodium (symport system).
Catalytic Activity: L-serine(in) + Na(+)(in) = L-serine(out) + Na(+)(out)
Subcellular Location: Cell membrane
Sequence Length: 411
Sequence Mass (Da): 44348
Location Topology: Multi-pass membr... |
A0A7X2SUQ1 | MANYFNTLNLRNQLAQLGKCRFMARDEFADGASFLKGKKVVIVGCGAQGLNQGLNMRDSGLDVAYALRAEAIAEKRPSWRKATDNGFKVGTYEQLIPQADLVVNLTPDKQHSAVVQAVQPLMKDGAALGYSHGFNIVEVGESIRKDITVVMVAPKCPGTEVREEYKRGFGVPTLIAVHPENDPKGEGMAIAKAWAAATGGDRAGVLESSFVAEVKSDLMGEQTILCGMLQAGSLLCFDKLVAEGTDPAYAEKLIQFGWETITESLKFGGITLMMDRLSNPAKLRAYALSEQLKTIMAPLFQKHMDDIISGEFSSGMMADW... | Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 2/4.
Function: Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In th... |
R5RGB9 | MGRILSYVMFGFFVCTTIMSASVLRSREKLKINNILFALVCIGSSIWSFCFGFIWIQTDPLRAYYWRCAGMVGTFMYMICAMLVIARWCGQKRLWISAIKGFTFSAILLYPFLMQKSNTVYHMSAIGMTYVFVPGIWNTLYDIYCIVCAIGLCSVCAIGLFALSGFMKKNGERKWERIVGKRLLFCESVIVAGMLLDTIMPVFGFNAFPGSTLSQLFGVLLLYRIYLFINKNKVKLENVSEFVYYSVKSPILIYDYNKKLRIVNKSATDFLKISEQNCENVLFTDLFEMGNEKLKYGGYSNKIDVRCRANGAHCRLDINQ... | Function: May play the central regulatory role in sporulation. It may be an element of the effector pathway responsible for the activation of sporulation genes in response to nutritional stress. Spo0A may act in concert with spo0H (a sigma factor) to control the expression of some genes that are critical to the sporula... |
F0S3D2 | MKHLISAEDISKEQFQEIYELSQQVKKALREDRKKFSVLKGKCIVNLFFEPSTRTRTSFEKAGKFLSADVINISTSTSSVKKGESLIDTLKNLDMMHPDVVVLRHPCEGAPYTVKNYINASIVNAGDGCHQHPTQALLDAVTLTEHLQTLEGKKITIMGDISHSRVARSDAILFRKLGAEVFVYGPSPMMPRFPEAIGVKKLSSFEEVAQISDVVILLRIQLERQSARKVFPSLREYAELFGMNKKRLEMLKPDTVILHPGPFNRGVELNNDVVTSTRSLIFQQVETGLAVRMVVLSLLCGKTEKLKEEIDG | 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: 312
Sequence Mass (Da): 34972
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A0A1F6NVX6 | MLINENRIKIAVQKRGRLRVPSFDYLNSIGLYFGIGESNDLIVSCQNAPVDVLLVRNRDIPEYVRTGAADFGIVGLNTLYERDECYPVTNQFEFGRCSLVIAASINSGINSVTKLQNKRIATSYPNSLRRYLNENGIIANVIEINGSVEIAPLLNIADAVCDITQTGDTLRKYGLKPLATILRSQAVMIEGANRNNVDSFKEKYIYASNKVKTI | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
Function: Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosyn... |
A0A2G2L243 | MLKNTNTKAWHKWIAIIFSLSAIWLTNGVVMAENYGILKDAVPTIVEQPRYPRKAAMEKIEGWVKFKFDVDELGQPYNVELTNAEPRRVFERDARRAIYKWKFEKNKSQKGLTYTMVFKVKSLELLTEG | Function: Interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates. It could act to transduce energy from the cytoplasmic membrane to specific energy-requiring processes in the outer membrane, resulting in the rele... |
A0A0D2M6M2 | MRVACHSEPVLAAIAGDAANDDGGLPSASLACLEQSLERARSLSATPSGSDQDEAQIGSAEYQVWLAQHPCLLTKFEEFQKQLDGRRLAVFLDYDGTLTPIVSNPDAAIMSDQMRETVRQVAGMFPTAIISGRGREKVESFVRLPELFYAGSHGMDIVGPCGATVGSTAGGGVVGGGSGDGGVVEQFRFQAAAEYQPLIDRVYSQLRESLESIPGASVEHNKFCVSAHFRNCHPDSWQRVVSAVDAVVAGAGGGRLHVTRGRKVLEVRPTVDWDKGSALLHLLGVLGLAGQPDVTAIYLGDDKTDEDAFAALAGAGAGAG... | Pathway: Glycan biosynthesis; trehalose biosynthesis.
Function: Removes the phosphate from trehalose 6-phosphate to produce free trehalose.
EC: 3.1.3.12
Catalytic Activity: alpha,alpha-trehalose 6-phosphate + H2O = alpha,alpha-trehalose + phosphate
Sequence Length: 526
Sequence Mass (Da): 55779
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A0A1Q9YB91 | MLSAIDKTQKEELAAYLQNRSQEISADILAKAAAIIDEVRKDKDNALKKYTELFDQVSLDDFEVSKEELEEAASKADADFVAALEDASKNIYEYHEAQKKEGYRIERSNGAFLGQRIMPLASAGIYVPGGRAQYPSSVLMNAIPAKVAGVREIIMVTPPSKSGSINPNIAAAAKVAGITRIFKVGGAQAIAALAYGTQSIPAVDKIVGPGNIFVAAAKKLVFGKTDIDMIAGPSEILVIADENANPAYAAADLLSQAEHDPMASAILISNSKKMIDAVNKELRIQTDRLPKKAIIEESLKNYGKSILTDTLEEAADISNA... | Cofactor: Binds 1 zinc ion per subunit.
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9.
Function: Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine.
EC: 1.1.1.23
Catalytic Activit... |
A0A5J6YU22 | MTFPDAPGRGKPEKQYVEDPAIATLETLGWRLTPVSEVQRVGPRSAILRDRLHAALLRLNPGLSAEALELAVRRVSARERLGLVEGNREVHGVLTHGFSVRLDDDPGGLPSRTVQLADFVDVSRNEYTLIRQFPVVGEGGRRIEFDLSLFVNGVLWAVLECKYARGDLGAALAEGHAQLSRYQALGDYVGRGAPSVFASVQVLGVLCGSEAVSLGVYGAVGASERAFAPFPEAYPQGAAWLADALGLPPGGQPNPQQILLYSVFAPENLLEFARSFTVYEVKEGRLIRKLARHQQRVAVDRVARRVLGLLPVGPEDDPAM... | Function: Subunit R is required for both nuclease and ATPase activities, but not for modification.
EC: 3.1.21.3
Catalytic Activity: Endonucleolytic cleavage of DNA to give random double-stranded fragments with terminal 5'-phosphates, ATP is simultaneously hydrolyzed.
Sequence Length: 1010
Sequence Mass (Da): 112567
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A0A0J9X5C8 | MNTDSTLKNLLWNGSISVRLVLSQDEARNFVDYDYYVSINVPRLSYLHLQLPSALQFFRPLLRHPEDADMLDWWLEFEGVPIKWNWPIGLSFDLLTNHDPNKGPDAYAEIVPWTLILHKKNYPKDRILSLDDGIETVRSYWLNQIKEASYIRYGNSKAVLNLSKDDSDSLWSHLMQTSPRNLPLRIYLPISNSVLQYPLPHDPNQTLGAALNACMPRLFPSKRTCVIARPVMHGVELPLRTPVGALFESGAVFCDGFVHVSLVML | Function: Involved in cytoplasm to vacuole transport (Cvt) and autophagic vesicle formation.
Subcellular Location: Membrane
Sequence Length: 265
Sequence Mass (Da): 30331
Location Topology: Peripheral membrane protein
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A0A1F2PA75 | MIGVFLCGCDGEVSERIELKWLGEVAERDPDVGYLEIDEHLCSKEAVRKIRSIVESKNLDRIVIAGCSPRTHEKIFDDLAPIVEFANIREQAAWVHPEKEEATRVAADILQSAIVRAKLAAELEPVRVPIEPSCLVIGGGVSGMQAASDLSAQGYRVYLVERDERLGGRVKRLSMTFPTISCGFPCRHDCPECELTPKEEELYASEFVEILTSTEVMEVEGRIGDYHVTLRTPEGVREIKVGTVVIATGTKTYDPSRIPEYGYEFEDVITSIELEDLYMKHRFLGGGGELRRPSDDAIPKRVDFIQCVGSRGEKGGNPYC... | Pathway: Cofactor metabolism; coenzyme M-coenzyme B heterodisulfide reduction; coenzyme B and coenzyme M from coenzyme M-coenzyme B heterodisulfide: step 1/1.
Function: Part of a complex that catalyzes the reversible reduction of CoM-S-S-CoB to the thiol-coenzymes H-S-CoM (coenzyme M) and H-S-CoB (coenzyme B).
EC: 1.8.... |
A0A1F2PAR4 | MELDTAHRRMIESLKRLGVKQEVLRAMDKVPRHYFVPENRKHEAYVDHPLPIGDGQTISAPHMVAIMCDLLDIEPGNRILEVGAGSGYHAAVMAELVGEEGKIYTIERFEGLAATARENLRRAGYTNVEIFVGDGSLGLPEAAPFDRINVTCAAPDIPPPLLDQLKVGGKMVIPIGRYVQDLHLIEKRADGISRKIKGGVVFVPLIGEYGFKE | Function: Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins.
Catalytic Activity: [protein]-L-isoaspartate + S-adenosyl-L-m... |
A0A8J6HEJ0 | MYLNGDTAFLVWMVPDPGSLALVLGMVGRSDANGNGRCCSDKAELEQGVDGCSIFDDGADKRVIGVDEGLGGAYTNAVEKVQPVASLLESLLDVEDQGTVLIGHHSQIPNFGTLWDWMTVEMKCLLAEVTAAFDVAGRCHQDAVVFERLYLTPQVSNGRRLQVSPSRWWSDRGCTVWFTGLSGAGKTSIAFELEAYLIQHGIPAYGLDGDNMRTGLNKDLGFSKQDREENIRRVAEVAKLFADAGQICLCSFVSPFAEDRELARRIHRDNDLPFFEVFVDCPLLICEQRDTKGLYQKARQGTIKGFTGIDQPYEKPEHPD... | Pathway: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 2/3.
Function: Catalyzes the synthesis of activated sulfate.
EC: 2.7.1.25
Catalytic Activity: adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate + ADP + H(+)
Sequence Length: 395
Sequence Mass (Da): 43908
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A0A508A6G0 | MGAMSTQPHASPEPDDREAARPIDERPTRIRVDLERIAGNLRAIRAHVGVPVMGIVKANAYGHGLVPVARHLQAAGVDQLGVAFVEEGIALRRAGIRAPILVLGGIFGHQIGRFISHDLEITVSSLDKLRQVEAAAEAMGRRAVVHLKIDTGMERIGVHSYSAGPFIEAAVASPWCEVKGVYSHLACADDPASPATAAQVARFAEACEHFTRIGAPMPLRHLANSGGVLHFPDTWLDMVRPGILLYGVLPDPASRPTVAVQPAMSLVSQVVYFKVVKAGHAVSYGGTWTATRDTRVVTVPIGYGDGYPRALSSRGEVLVR... | 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: 400
Sequence Mass (Da): 42639
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C6JR26 | MERTREEKIKRKFIGAHVSTVGGPFNAPKNAKEIGARAFGMFVKNQRRWEAKPLTAEDIEKFKKALKENGYTNEYILPHDSYLINLGAKDEEKREKSLNAFIEEIKRCDQLGLKYLNTHPGSHLNEISEDECINNIADCINKAIEVTENIIIVLENTSGQGSNMGYKFEHLGKIIEKVKNKERIGVCIDTCHTITAGYELKDEVGYKKTMAEFEKYVGFKYLKGVHLNDSKFDTGSRKDRHDSIGKGILGMKFFERFMNDERFDNIPIILETIDSSIWKEEINLLYSLIK | 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... |
F0S3E5 | MEVKKLPAHVLTTIGIGSVYPVYFPENLEELKSILKSEKVYIIGGGSNTVLPEKIESKIVSLRKFKKIKIKRNSIILGAGVSLSEVLKLQIKENFSLFEIFAGIPRATVGGLVAQNAGAFGREIKDFLEKVVYLDLDSYEVATLKNFSSFSYRKSPFPKKGVVLETEFKIEKDNHVKEKIKKFVFFRLSKQPPFYLQTAGSTFKNPLGDSAGKLLDLVGMKGFKVGGVKFSEIHANFCINEKGSFEEFKKLISIAKERVKEKFNVELELEVKIPR | 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: 275
Sequence Mass (Da): 30919
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A0A1W9V5X6 | MTKALKIFSDFDGAISLIDTGDLIVDHCIGRVARRAIDDKIVAGKMSFREGFAAQFAGVHLTWDEAVGRLQLQDGLDAAFPPFVRWTEAANIPLVALSSGFEQFIRACLTPMRLAHLEIRANRALVQGRNWQIAFRDDTPSSHDKSAALREARSQGYRVAFIGDGISDIPAARVADILFAKKGERLAVPRHGRGHRISPTELNSRANIYALKSLGARYIISVSACGSLREDLAPGHIVIPDQLVDRTRLRDLTFFSDGLVAHLSAAEPFSSPLSELLYEAVQETGARPAHLGGTFVVIEGPRFSTKAESKIFRQWGCDII... | Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; S-methyl-5-thio-alpha-D-ribose 1-phosphate from S-methyl-5'-thioadenosine (phosphorylase route): step 1/1.
Function: Catalyzes the reversible phosphorylation of S-methyl-5'-thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate.... |
M1MTM2 | MLRTLLFYSGMILSLVFASIFRIRIKFLTFTNNIKGRNNFIHKVTHTWAKFILKIAGAKVNVIGLENIPKDETVLFVSNHESNFDIPLLLGVIDMPKGFIAKKELENWPFISTWMKYINCIFMDRDNLRKSAEAIVDGINLLKSGHSMVIFPSGTRSKGKSIDEFKSGSFKLATKSKCPIVPLTINGTYKLLEENNNRIKGADIELIIHPTIYVDKLTKDELEKLPNTVHSIIINSCKDY | EC: 2.3.1.51
Catalytic Activity: a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphate + CoA
Sequence Length: 240
Domain: The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate.
Sequence Mass (Da):... |
A0A3M7NSR1 | MDEYRFDDSRLKKQMDDPSKTPLLLVACGSFSPITFLHLRMFVMARDYVKHNTDFEVVGGYLSPVSDAYKKQGLAPAEHRVAMCQLAIDKAANWLMVDTWEAEKKEYQPTAKVLDHFEYEINQVRKGVDCGNGMRKAVRISLLAGADLIQTMSTPGVWSEKDLDHILGRYGTFIIERSGTDIDEALASLQPYRDNIHVIQQLIQNDVSSTKIRLFLRRGMSVQYLIPAPVVEYIEQNHLFGDDGRSSSMTSINLPNAVDKGKDKDKGGDCREQELKGH | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from nicotinamide D-ribonucleotide: step 1/1.
EC: 2.7.7.1
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Length: 278
Sequence Mass (Da): 31430
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A0A444U637 | MAANGNLQKAIDLASKAAQEDKAGNYEEALRLYQHAVQYFLHVVKYEAQGDKAKQSIRGKCAEYLDRAEKLKEYLKKKEKAPAKPVKESQSDEKGNESDEDGDPEKKKRQNQLQGAIVMEKPNVQWSDVAGLEGAKEALKEAVILPIKFPHLFTGKRTPWRGILLFGPPGTGKSYLAKAVATEANNSTFFSISSSDLVSKWLGESEKLVKNLFQLARENKPSIIFIDEIDSLCGSRSENESEAARRIKTEFLVQMQGVGVDNDGILVLGATNIPWTLDSAIRRRFEKRIYIPLPEEHARTFIFKLHMGTTPTSLTEADYH... | Pathway: Lipid metabolism; sphingolipid metabolism.
EC: 1.1.1.102
Subcellular Location: Late endosome membrane
Sequence Length: 772
Sequence Mass (Da): 85592
Location Topology: Peripheral membrane protein
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A0A7V8V254 | MKQQLLPLGRLVVRLNETATLGVFAHLKFPMARTKLKSRSEPENSSPVRGSLAAFQSHVFAWFATHQRDLPWRKSQDPYRVWISEIMLQQTQVATVKEYFRRFTAEFPQVSDLAAANEQKVLRLWEGLGYYRRARQLHAAAKEIVERFHGKFPQTVDEIQSLPGVGRYTAGAIASIAYGHKVPILEANTQRLFARLTGWDQVLTTSASQKRLWQFAEDILPDQDVGIFNQALMEIGSLVCTPKNQSCSQCPLAAHCEAYQQDRQDEIPQPKKKIEFIPITEIALVVRRKNEVLVRQCGQDERWAGLWDFPRFAVADVNEL... | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Adenine glycosylase active on G-A mispairs.
EC: 3.2.2.31
Catalytic Activity: Hydrolyzes free adenine bases from 7,8-dihydro-8-oxoguanine:adenine mismatched double-stranded DNA, leaving an apurinic site.
Sequence Length: 404
Sequence Mass (Da): 45787
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H0QZJ5 | MADIPDVDDAQSVDLAPVTHHAYSAVDDTVEPAYPFDDVDASDHDAPDRRRRRTVVLAAVIVCLLVMVGGVGYYGLRFFGVVGASDYSNAQGTGDVLVTIPENSTLRDFGRILTDKDVVGSVKAFTRAADGKMLSAGIYKMRTQIPASKAVAMLADDQWSYRVGRVVIPEGAQLDSKKGIDGKVTPGVFQRIAEATATTVNGSKVGPTIDELATAAASASLEELGIPQWAKTEVTALNGDHRRIEGLIAPGTWESIDPSASATDILRQLITDSARQYEQWGLLSSNDSGLSPYQTLVAASVVEREVREANDFPKVARVIL... | Function: Functions as a peptidoglycan terminase that cleaves nascent peptidoglycan strands endolytically to terminate their elongation.
EC: 4.2.2.-
Subcellular Location: Cell membrane
Sequence Length: 428
Sequence Mass (Da): 46191
Location Topology: Single-pass membrane protein
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A0A673N0Q2 | MGYDVTRFQGEVDEDLLCPICSGVLEEPVQAPHCEHAFCNACITQWFAQQQSCPVDRTVVTLAHLRPVPRIMRNMLSKLQISCDNAGFGCTATLRLDQLQSHLKDCEHNPKRPVTCEEGCGLEMPKDEMPNHNCIKHLRSVVQQQQTKIADLEKSAAEHKHQLAEQKRDIQLLKAYMRAIRSTNPNLQNLEESIEYNEILEWVNSLQPARVTRWGGMISTPDAVLQAVIKRSLIDSGCPLSIVNDLIENAHERNWPQGLATLETRQMNRRYYENYVAKRIPDAQPYLDLFTVVYIRTVFLSIICHSTS | 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: 308
Sequence Mass (Da): 35152
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A0A673HRZ1 | MKPQSDPASRGPALSSQGVLNPLQKASQFQSLDSRRFVQEPLGFQEKQLLQGPVKPLDWSFPIVPEVQSELAVDFQLRQPVTPSSVAVQCGENRVLVEVKKDLFSNGQLIQPSGLSMGGCPVVGEDSTSRVLNFEYELQDLEDNSHGNDFNLLQMTEDELVYTFALTYPPEAFAGTPISRANRAVVGVQCHYQRFYNVSSNALRPTWVPYTSTEFGEEVLMFSLKLMMDDWSYQRPSNLYFLGDVINIEASVKVYNHVPLRVFVDSCVATQVPDVTAHPRYSFIENHGCFVDAKATASSSRFMPRTQEDQIRFQLEAFMF... | PTM: Proteolytically cleaved before the transmembrane segment to yield the secreted ectodomain incorporated in the zona pellucida.
Function: Component of the zona pellucida, an extracellular matrix surrounding oocytes which mediates sperm binding, induction of the acrosome reaction and prevents post-fertilization polys... |
A0A328R5Q3 | MRDHSAYLDLVERLNAYSHAYYVKDKPLISDHEYDQLYKEVLGFESANPLLIAVDSPTQRIGDRPLESFVPFVHSTKLPSLGNMFSKQDFLDFSKRMYKECVEESILFSIEPKIDGLAVALRYEDGVFVSGGTRGDGVKGETVTENLKTIRSLPMKLSKPVTIEVRGEVYIKKSQFEMIKEDFANPRNAAAGSMRQLDSRVAAKRHLDIFVYQGMDTEFESHCKTLDYLKSLGFPVIPDVFQSSNLDDLYSYIKDYEAKRFSFDWEVDGVVCKVDDYALQETLGFTAKAPRWAMAYKFASEEVITKVLDIDIQVGRTGVL... | Function: DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA.
EC: 6.5.1.2
Catalytic Activity: NAD(+) + (deo... |
A0A8J6HUK5 | MSLDNICYITVLVAVLGLISPALGIRCFQCNSFVNPECADIPVNDTHSPFLHKCEQRDDYQMFCRKVVQTVLDAPQFTRITRTCGWYLNKDNRTNCQVSDTDFKMETTFHCIRCFNCSSRTNMNCVTFEGDNASMIVECPQPNAFCRKTRQIITADSTTIITRACGWIKFEEHSGDYCMVTNTNFKQETSSGSTVVPVARTNDSVGRPCCGDAPDA | Function: Required for homeostatic regulation of sleep under normal conditions and after sleep deprivation. Important regulator of the Sh K(+) channel, acting as a signaling molecule that connects sleep drive to lowered membrane excitability, possibly by enhancing K(+) channel activity and thus reducing neuronal excita... |
C6JLH2 | MITTEYISFLESLMSSLLGMSIVFIALIFLAIFVMIVSRIISVLEKNLIKTTDTKATVSVSTTGANTKKDNKDGVKIAVITAAISEEMKQPVDKFIITSIKKI | Function: Catalyzes the decarboxylation of oxaloacetate coupled to Na(+) translocation.
Catalytic Activity: H(+) + 2 Na(+)(in) + oxaloacetate = CO2 + 2 Na(+)(out) + pyruvate
EC: 7.2.4.2
Subcellular Location: Cell membrane
Sequence Length: 103
Sequence Mass (Da): 11273
Location Topology: Single-pass membrane protein
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A0A5C7JMY7 | MSHTPAITGSTSAFRTIRPLPGRGRHEIGRWWASAKTNSSRDPWFLHVMSDVVHLFESMPESPESPISMSRLQPQPIVQGTASEAVERAVELLREEWRDGFLGRKLERARMLVRQAQDLASDTGISISLARIDVLLARYLDSPEEARKELLSEIGKDLSVVRDRLPSVLAAPVRQTPTAPPVKRVARPAASRQVSLDAPVTLLPNVGEKKAKPLEKLGLRTIGDVLRFLPRRHIDYSKTMTIREAVGFETSGEVTVRGVVRDEAIFDGPPARYTIRLQDATGSIKVTWFNKYLAHQIRAGDEITISGKLDHGYGMPTATS... | Function: Critical role in recombination and DNA repair. Helps process Holliday junction intermediates to mature products by catalyzing branch migration. Has a DNA unwinding activity characteristic of a DNA helicase with a 3'- to 5'- polarity. Unwinds branched duplex DNA (Y-DNA).
EC: 3.6.4.12
Catalytic Activity: ATP + ... |
A0A673N5S8 | MNSNDTVIRVSALVSSMCFCLVSAVELSSALPARVPPAAIPMALRVELSPSLDSTRREQQLQQELLALKHKQQLQRQILIAEFQRKHEQLSRQHEAQLQEHMKVRTVVVKHQQELLALKHQQELLEHQRKMEQHRLEQELEKQQREQKLQLLKNKERGQESAVASTEVKMRLQEFVLNKKKALAQRSLNHCISNNPRYWYGKTQHSSLDQSSPPQTSVSIYNPPAMGVYDSKDDFPLRKTASEPNLKLRSRLKQKVSERRSSPLLRRKDSPISTLKKRSLDMAGDARCMFADSVCSSAPGSGPSSPNNSSHGNLCENGIS... | Function: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events.
Catalytic Activity: H2... |
A0A0Q0RSV6 | MDYDVIILGAGAGGYLAALHLAKKKKKVLIIEKEKFGGECLNYGCIPSKALIELSENIFYLKNMPGMTLDYKLNMKDWQAWKDSMIKKITGGAEGACKASGATVLYGEGKIVNKNTVNVDGKNYTADYLILDTGSVPVKIKGIDDVYYNREILAIDHIPETLVVIGGGYIGIEMGTAFRKLGSDVYIVEMKDRILPEVDEYLSRAVDKRLRDLGIKILTSSRVLGVKKNKNYTVKIENSGDIIAETVLMAVGRMPNTQGYGLENLNLEMDGRFIKTDQHKRTSVDNVYAIGDVSGMPMLAHKAFYDAYVASENILGNDTV... | Cofactor: Binds 1 FAD per subunit.
EC: 1.8.1.4
Catalytic Activity: (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + NAD(+) = (R)-N(6)-lipoyl-L-lysyl-[protein] + H(+) + NADH
Sequence Length: 428
Sequence Mass (Da): 47063
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A0A1A9GJN6 | MGIIGDIFGFIATPLYYAISAVLIGWHKLFTIIGLDPAGGAAWALSIIGLTVVIRALLIPLFVKQIKASRNMQLIQPRVKELQKKYGHDRERLAQETMKLYKDSGTNPFASCLPLLLQMPIFFTLFRLLDQAAKNQTAHGFLTEKLAIQFGDSKLFGHVPLAETFWNNGIWRGDGGDLGVMGVALVLVLAMTATTFFTQRQLMSKNMPADALSGPYAQQQKLLLYVLPVAFGLGGVAFPIGVLLYWTTSNLWTMGQQFYVIRNNPAPGTPAFDAKQEREKAKAAKHGVVLAVDEPTEAPVEKRPAPRQQPKKQTRQQRRQ... | Function: Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins. Aids folding of multispa... |
W4VPL3 | MEVIKITLLPLFINLTDKEIVIIGGGKVAERRLRHLLDYKESLTIISPDVTDIMHEMIAVNKINWINTSFKSNYLAEAHLIIIATNDKKINNQIIQQAPKTAWINAAHHADRGTIHFPIILKRGRLQIAISTDGASPLLAKRIKKEIDSLLPENYESYIDFLYEARQLIKQIKLDPAEKRRLLQDIVEDPIYDKNNQQVFLNKLKNKCKR | Pathway: Porphyrin-containing compound metabolism; siroheme biosynthesis; sirohydrochlorin from precorrin-2: step 1/1.
EC: 1.3.1.76
Catalytic Activity: NAD(+) + precorrin-2 = 2 H(+) + NADH + sirohydrochlorin
Sequence Length: 210
Sequence Mass (Da): 24227
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A0A673KYF7 | MAINVNLLPKECEFTVKNILVGLFCYKTQRGKFKVDSGALWNIIQYMTDRQYNPILRPHLAENPSSVSYKTEMSKRTGDRCFPNYEINNTMPDYAKLPIQMMNFVTTMHCRDYLLIIDPLDVCDAQAKKGAPTLLMAIKTQTANFENREAIRETWGNIKTLGGRQRLVRRVFLLGKSKDLHIEEKLHLESEKYGDIIQWDFVDTFFNLTLKDVLFWDWFSRRCPHARFIFKGDDDVFVRTPAVLDYLLAEETFVVGDVISNAAPIRSNGTKYYIPESFYKGLYPSYPGGGGVLYSGSLAHRLLVVSQRVHLFPIDDVYLG... | EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 392
Sequence Mass (Da): 45186
Location Topology: Single-pass type II membrane protein
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A0A3S3SRA2 | MVEMSKDERTKAREALLSRRVEDLTVADFATVRDLVEGFGRMGGFMAPRLSEATKIMEEMRSEGCVKFLSFTGNIISTGLRGVISDLIRGGWADVIVTTCGALDHDLARSFGARYSSGEFELDDVMLNELEIHRLGNVLIPLEDYGPLIEKVMRRELPEILRGRTSISPSELASEFGRRIDDSHSFLRAAYERGVPVYVPGVIDGSFGTNLFFYAQTNKFNLDLFSDMSRILNTVFDSKKTGALIIGGGISKHHVIWWNQFKEGLDYCIYLTTAQEYDGSLSGALPKEAISWGKVKPRAKHLAVFGDVTITLPLIAGAIS... | Pathway: Protein modification; eIF5A hypusination.
Function: Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine resi... |
A0A4Y3PLP4 | MRFHSKLMLIICSLLLGVIVILGITFELMLADALEKEIGRRALDTAKTVAQMEEIKQAFYTEDPAKIINPIAEKIRVSTNAAFITVGNLQGIRYSHPDPDEIGKPMVGGDNETVFEGNSIISETVGSLGPGLRGKTPIYNEAGQVIGVVSVGFLFADINETIESYRDRIVLVGIITLLLGVVCTMLLARNVKKAIFGLEPASIGRLYQENQAVLESIREGIVAVNETGAITLANQTAQRLLGQKQEKERDCLTEKQDDLVHALGLTEVIETGEAEFDREALVNEQVLIVNRVPIKDANNQITGAVASFRNRSELFEVTQE... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 528
Sequence Mass (Da): 58177
Location Topology: Multi-pass membrane protein
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A0A7V9A8C4 | MPIQPLPTGLPIIAPRAADSHKGTYGRALLVGGSVGMPGSISLSGQACLKGGAGLVTLAVPDAIINTVANFEPSYMTWALPTDRSGHIPLHAKSRLREKLEASSCLAVGPGLGQSQGLFHLVGHLYETFTGPMIIDADGLNLLSLRSAPLAGRAGPRVITPHLGEFRRLVGKPHLSMEDARDMASELAGRQKITVVLKGPKTLVTDGQRHWHNPTGNPGLATGGTGDVLTGLITALLAQSLDAYEAAVLAVFLHGLAADLAIETTTQAGLTATDLLSFVEAAWRDYESRRDHLST | 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 ... |
A0A3S3SSL1 | MESIKTVSKERTERLAWLSKIALTPEEVDRFTDQLNRILEFAGALDSPEVEGVEPTFHVLDLVNTFREDREEKGLEREGALATAPKVKDGFIVAPKIV | Function: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an ... |
A0A3E2TJJ4 | MDLKSIYEGKKFGEILFCEPLKDYTTWGIGGPADVLVKPHNEKELQDLLIFNNENKIHTTVIGRGSNLLITDKGIRGCVLVLADNYDCISLEDTELTVLAGTKLNKAALYAIENKLTGMEEVSGIPGSVGGAVAMNAGAYNREIKDICINVKAFDLSGNEYNFTNDEMNFSYRHSKIFEQDLIVSSATFKLFYDTENKAEEKYDDYTNRRETKQPLDKKSAGSTFKRPEGSYASKLIDECGLRGYRVGDCQVSEKHCGFIINTGDATSREMLDFIEEVAGIVKEKTGFTLEREVKLIGDL | 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: 300
Sequence Mass (Da): 33428
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A0A4W2I5P7 | MTPRARGGGRTYGAVGSTIRSAGEGKRSRPRPRAREWRGETRSLRPRPLHPTAGGDARGLLFGARRGRLESGMARSRAALLLPSLMLLLLVTPAQVSPDYQYFGQQGEGDTWEQLRLQHQEKGPMVYAICYCPLSRLEDLEALKVADSKTLSESERDRLFAKMEEDGDFVGWALDVLSPNLISTSMLGRVKYNLNALSHDTATGLVQFALDQGVNVAQVFVDTVGLPETYQERLQQRFPGIEVTVKAKADALYPVVSAASICAKVARDQAVKNWKFVEKLQDLDTDYGSGYPNDPKTKAWLRKHVDPVFGFPQFVRFSWR... | Function: Catalytic subunit of RNase HII, an endonuclease that specifically degrades the RNA of RNA:DNA hybrids. Participates in DNA replication, possibly by mediating the removal of lagging-strand Okazaki fragment RNA primers during DNA replication. Mediates the excision of single ribonucleotides from DNA:RNA duplexes... |
A0A9E8ATU3 | MRLSNLGLAFLGGTFGTAAREAVSLGLPAVSDVPWAIFTVNILGAFLLGLLLDALARSGPDEGWRRRARILVGTGFMGGFTTYSALAADTAGLLGADPGGASSPGIGLAYAVGTVLIGGLATFAGIATATTLRRGGAEVDEVADDLPIEPDAWDEDTADAGPDASADRHPGSAR | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Subcellular Location: Cell membrane
Sequence Length: 174
Sequence Mass (Da): 17484
Location Topology: Multi-pass membrane protein
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B0CDY1 | MSVSLSRPPLWFWIGISCVWIFALAFRFWGLERFNTLVFDEVYFAKFGHNYLTQTEFFDAHPPLGKYLIALGIALKGFNTWGFRWMNALIGATIPLILSGIAYQLCKRPSYALITAVLASLDGLLLVESRYALLNVHILFFGLLAHWLVLISLNHQGMQRNGWLAAAGISFGAAIAVKWNGLGLLLGLYLLWLVAKGGQIWLGSSETPKRRLPLQKLSELSWLQMFVYLPAIALFVYGILWLPHLAQNPEFNLWQVHQEIFNYHRRVGGDEVHPYCSSWYTWPLLLKPISYFYQVTQSTLEPLPVTGPPLPQDAVKWIYS... | 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... |
A0A956W9C9 | MTITAPKRFLESVEQSSEDRDSLVCVGLDPDLARMPDTITRGRSAGDAIFEFNKQIIESTIEFAAAYKPQLAMYMQYGPAGYEALLRTRELIPSTTPAILDCKIGDISTTMEPYARAYLDEADFDAITVNPYMGSECLQPVFDRAGKGAFLLCKTSNPGSGEIQNLTLENGQPLFVEIARKVAAWNAGSAASLGLVVGATYPAELIVVREAVPDLLILVPGIGSQAGDLAAAVDAGIDGQGRGLLINSSRSITFASAEKDFARASATAARTLRDQINAIRG | 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: 281
Sequence Mass (Da): 29943
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W4VK85 | MITVIGIVMYLNNVNEMKNQTQSMSKVLSTQFSRTIDLYFEDIERLSLAIFTDSVIQDTLSNYEEDLLYNDISIRNSLYPRLFNQVYPQSDVAAVTIHTDSGTIFDYEKSGDMEVRYATEDPEWVQLLKAANKNEFLILPTSEVEQLNGQKKQVVSLIRDIYKIPQRNRIGSMKIDIDVTIFEKLLEMDNVDELEEHMRIFVMSANESVIYDHRKELIGENNVGLNLPTVTVNEPEDGTLSWQSDSYLYANDHSDFTNWNTVVLIDNEFIIYERNQILLFIAISGLVAFSVIGVISYLLSYNITKPFNGIIQKMRRVEKG... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 571
Sequence Mass (Da): 65682
Location Topology: Multi-pass membrane protein
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B5Y9Z3 | MRKIRLFYSFLWLVFILLSAYVFTFFPGTKTIPNKLGPFQLYAIMITMGAIFAYLAALLLGPVKGIEEELIDKFALVAIPFGLVGARLGFVLQNAEYYQNHPLEVIGITPDGFGLSGLSIHGVIVAGVLCLLLFYGWVGLRTLDLGDLGATILLIGQAFGRFGNFFNQELYGYPTSVPWKMFIDPAHRLAGYYDQAFYHPTFFYEGFLCLLGATILAYRFLHKRRFRGQIVLEYLMLYSLIRFVVEFFRIEPPSLWGLHTAQLLSLVIIVLCGIMYVLTLRFGQKLFVGEARQTP | Pathway: Protein modification; lipoprotein biosynthesis (diacylglyceryl transfer).
Function: Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins.
Catalytic Activity: 1,... |
A0A5C7JZX5 | MREGTGGAMHRGSTGGRRRTLTRLVTLLALVAMAAGVLLPAVGAQSPYTTLSPQSPQADDIQWLYKLVFFLALIVFIGVQIAIVYTVLRYRRRVNDERPEQLHGNKTLEVIWTIIPAIVLLAIFIPTVRTIYAHADQVEEGDFTVQVYAKQWWWEVHYADDTGEAAGVITANDIVVPQGKNVVFELYSNNVIHSFWVPQLSGKLDVMPGHENKLPIDTDNVGLYFGQCAEFCGDSHALMRFKVIVQPQETFDQWAASWKAGPSDASASFVPDGDLTKVPAAFGLCLACHQVEGTNASIAPEGLEEAPLTDTGEMGPAKYA... | 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(... |
B8FLB7 | MPFFSIFKREIFRKLTGKAKDRENAAFQALHQPQSWLVAGLGNPGEKYSQTRHNIGFMAADLLGEKWRLGFETHGASLFGAGLIGETPAGVIKPQSYMNLSGPPIWEIAGKFGIDRERVLVIHDDLDLPFGKIKIKKKGGHGGHKGIQSLIQSFGDGDFPRLRVGIGRPPAGQSVVDHVLGRFDAEENLVLGKVLALSGDAVETVLREGISKGMNSFNNQQITA | 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: 224
Sequence Mass (Da): 24385
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A0A359LYH7 | MLRMSFLEHLEELRSRIIKILMGFGVAFVASLTFTAELWNAVRAPAAAALTSLGLKPDLVAIEPMEQFNIIWLKLPILTSIFLASPWILYQVWSFIAPGLYKRERRWAAPFVLCSAGLFIGGGLFAYYVAFRLGLRFLLGIGTGMGVTPMISISFYFDLFVNVILGVALVFELPVLVFFLTLLRITTPKFLLANSRYAILIIVVVAAILTPTPDIFNLTIFAAPMVVLYFGGVFASYLLVLHRENKRFPWALTLGIVLLVLLLLAAGAYIAVSKYGYTLTGSWPFLTR | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes.
Subcellular Location: Cell membrane
Sequence Length: 288
Sequence Mass (Da): 32057
Location Topology: Multi-pass membrane protein... |
A0A379AIG7 | MKRMLINATQQEELRVALVDGQRLYDLDIESPGHEQKKANIYKGKITRIEPSLEAAFVDYGAERHGFLPLKEISREYFPSSYNAHGRPNIKDVLREGQEVIVQIDKEERGNKGAALTTFISLAGSYLVLMPNNPRAGGISRRIEGDDRTELKEALSALELPEGMGLIVRTAGVGKSAESLQWDLSFRLKHWEAIKKAAENRPAPFLIHQESNVIVRAFRDYLRQDIGEILIDNPKVLELARQHIAALGRPDFSSKIKLYTGEIPLFSHYQIESQIESAFQREVRLPSGGSIVIDSTEALTAIDINSARATRGGDIEETAF... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Endoribonuclease that plays a central role in RNA processing and decay. Required for the maturation of 5S and 16S rRNAs and the majority of tRNAs. Also involved in the degradation of most mRNAs.
EC: 3.1.26.12
Catalytic Activity: Endonucleolytic cleavage of single-stra... |
A0A1A9GPE0 | MGVSATGKSSVARRLAELHECDFIEGDDLHPRANVAKMEAGDPLTDEDRWPWLARVAQTMREQADAGRSSVVTCSALKRAYRDRLREDVADVWFLHLHAPAAVLEDRMSRRTRHFMPVSLLASQLATLEPLAPAEHGRVVDVTPPLDDVVAAASRALAELLNESPGA | Pathway: Carbohydrate acid metabolism.
EC: 2.7.1.12
Catalytic Activity: ATP + D-gluconate = 6-phospho-D-gluconate + ADP + H(+)
Sequence Length: 167
Sequence Mass (Da): 18314
|
G2KPF0 | MIDLQITSENPGWNTDLPDYESVIERTVHAVFSTCPVAAEIKGSVPSIEISITLSDDESVRILNRDYRGKDKPTNILSFAMQDTEDGWEYPTPGLPCTLGDLVIARETLIREAEDEAKSFADHFTHLIVHGTLHLLGYDHIEDEDADEMEALEINILNELGIKNPYLLPGGD | 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: 172
Sequence Mass (Da): 19165
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A0A1B1AIY1 | MISNAITIFRTLLTIPLFALLAYGAGDFGWTPLALFLGAGLLDMVDGKVARARNETSAFGAMIDLVGDRLLTFAAVLGLIVGGDVAGVQLIAGIIIVARDLVVASLNEALPGKLGPRVGTLEKIKIAAAFAALTLLIAPSTFEQQQMAGIAALWLAAAFTVLTVAGYWMAALREFAKS | Pathway: Phospholipid metabolism.
Subcellular Location: Membrane
Sequence Length: 178
Sequence Mass (Da): 18518
Location Topology: Multi-pass membrane protein
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W4VIG5 | MPELPEVETIRQTLKQLTIGKTIQTVDIYWPKIIQEPDDYHHFIDLIKNQTIHDIRRKGGKFLLFDLNQHVLVSHLRMEGKYGGVYPQREELMAHTHVVFHFTDGTDLRYRDVRKLGTMHLQERGTELTKKPLLLVAQDPLEADFSLQTFQKKVQKSERNIKNILLDQSVIAGLGNIYVDETLFMAGIHPLTKGLSVTDEQVIQIVEASVATLKDAVKQGGTTIRSYVNSQGQIGMFQQKLNVYGQNDKACRKCEDTIMKIKVNGRGTHYCPSCQPI | Cofactor: Binds 1 zinc ion per subunit.
Function: Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase... |
A0A673MS37 | MYTHYTHIQCREKVFAPFLFQILIHFMHAFLIWTFRFSLSATPGSREHDPSSQQVTKRHRKLLKTSPVRRPHTNSSHSPSSSSSSRRLSDVQESRRRIIREVCGKYRSNISRTITPHHVSRIYVEDRHKLLYCEVPKAGCSNWKRILMVLAGVANSTREINHVAVHYDNHLKRLDSFDHQGISKRLETYTKVLFIREPMERLVSAFRDKFESPNSYYHPVFGKPIISKYRVNASQTALKTGSGVTFREFIHYLLDVHRPVGMDIHWEAANQLCSPCHLHYDFIGKVETLEEDANFLLRKIGAPENLTYPSFKDGNPKAAR... | EC: 2.8.2.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 362
Sequence Mass (Da): 42488
Location Topology: Single-pass type II membrane protein
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F0S058 | MSKFCEVVNELYKIVEERKEKLPEGSYTAKLFRKGEDKILQKVGEEAVETILAFKSGDKNHTVYETADLIYHLLVALVNKGITLDEIGEELQKRMK | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9.
Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-ATP + H2O = 1-(5-phospho-beta-D-ribosyl)-5'-AMP + diphosphate + H(+)
EC: 3.6.1.31
Subcellular Location: Cytoplasm
Sequence Length: 96
Sequence M... |
F0S3Y3 | MLLSCGVDIVSIKRVEKLLERYGDRFIKKVFPEGIEYCYQKRKGELAGCIAARFALKEAIIKALSGIEKKVTLSEIVIIGGGKNLEVKLKNHKEIQLIYSISHEKDYAVAMVNVIKLK | 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: 118
Sequence Mass (Da): 13295
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F0S460 | MHSSERIGKLYIVATPIGNLEDITFRALKVLKEVDLIACEDTRRTIKLLNYYKIPVKKLVPYHEHNERKVSKKLIKELLSGKDIALVSDAGTPCISDPGYRIVSLAREKKIDVIPIPGASAVIAALSASGFPTDRFLFVGFLPKKELQLKKTIKEISKLPYTVVAYESPHRLEKTLKILKEMIPEKKIGIYREITKLNEEFLEGNPGKLLNELTLEDKLKGEFVLLFYPSKEEKENENEKSLDEILLQLKEEGNSLKTTVKEACQRTGLPKNEVYKRALELFSRD | 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: 285
Sequence Mas... |
B8FEA1 | MAPETWTIQKILKWTTDFFSEKQVEAPRLSAEILLSHCLDYPRIHLYTRHDQPLNPEELGRFRELVKRRAAREPVAYIVGNRDFWTLELDVNPSVLIPRPETETLVETALEVLNAAQAPMRVLDLGTGSGAIILALASEKPEHHYMAVDYSPQALETAKANAQKHNLNVDFYKGSWFEAVRCLDRFDLVVSNPPYIPSRDIPGLMPEVARYEPMSALDGGPQGMDHLALIIERAPEHLKPGGWLMLEMGFDQKELVEQVALETQAYENVRFVRDLAGHFRTAVMQRPAP | 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... |
A0A1F3JPG0 | MRIHKAGFSVITVALLISGTLMTVLVLTKMPTWVLGGFGLIFFLLLAFIFRFFRFPNRKIEFDETMVVSPADGTIVAIEEVEENEFIKEKRIQISIFMSVWNVHINWYPVVGKILQSIHFDGKYMAAWLPKSSHENERSVVVIDTPKAGKILVKQIAGAVARRIITYAKPELECHAGDQLGFIRFGSRVDVLIPIGSEIKVQLNQKVTGGLTLLAKLPHS | PTM: Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme... |
A0A7X2TSG4 | MARQRLGQHFLRSQTVLERIALSVCPEPQPLVIEIGPGKGALTAHLLRRAERVIAIELDRALAVELRQKYEDEPRLTIIEGDALAADLAQWGPAVIAGNLPYYAATAIIERVLDSGAGLRWAVFLIQKEVAERMAASPGGREYGFLSVRTQLAADCAVLFRVKPAAFQPPPKVESAVVRLRPRPGVAPDPEFLAFIGHCFRQKRKMLRNNLSGLYPKDLIEAIPEGFQRAERLTLSQFAQTYRRLVAYSKETIMFTPEQAQGLAMFLAMGLEKEQQTTKKVLAAVPAESLDFKLGDKGRTAGALMAHIVSSELWFADGIE... | 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(+) +... |
A0A1Y0I6Z8 | MTDKRSLIRTFALAITCTALVALLYTSDEPELPENYKATDENEPDAFVVNGSYLEFDETGNLALQLESHQGVHFPNADQSIVGTPSVKIYQENQVPWVVNASQGQYFQEDRKLILSGDVNITRSNSNDPPLRFSTEELTLYSDTQFITTDKPVKLEDRLGTTEATGMNAWVKERRVELLSKVRGTYAQDPTHAQEPKE | Function: Involved in the assembly of lipopolysaccharide (LPS). Required for the translocation of LPS from the inner membrane to the outer membrane. Facilitates the transfer of LPS from the inner membrane to the periplasmic protein LptA. Could be a docking site for LptA.
Subcellular Location: Cell inner membrane
Sequen... |
A0A1V5L8B6 | MSNSFQKNKMVCVCQVASAHGVKGEVKLFSFMEDRLNIKSYPVLFDEDGKSYEVKVTGLFKEDLLIARLNDNMDRNVAEELRGKKLYVNRDNMPDLEEEEYYHADLIGLEVVTTDGENLGIVSAIHNFGAGDILEVKKGQNSLMLPFTKKVVLKIDFDNGQMISIPLKEIFLEQENDKEGEEN | 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 ... |
A0A4U0FGM0 | MSIRLKLLFSYAAMLVVPLVLIVLTALLLVFVFRGDLQNLRSFYETQIEGIDDHDYHQLINHTIARNPALVTDPGFLTTLSDEMKTGDQFVIVLIDGNPYFVSKAIQTRTQLISRLPAFHHSGYRHEWSTKSYGNEFFSLSQYDFVPKSGQSGSLYVVTQVQPLVYFSRKYLPILLTSFLVILILTNSLLTYFMSKSIIRPLRKLHKATRKIKEGDLEFQVGVGGKDEIGQLGVAFEEMRSQLEKSIRLQLQYEENRKELVSNISHDLRTPITAIRGYVDGILDGVADSPDKIEKYVRTISAKAAEMDRLIEQLFLYSKL... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 488
Sequence Mass (Da): 55765
Location Topology: Multi-pass membrane protein
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A0A4U9KTN8 | MGVGAFTGAFFHVLTHAFFKALLFLGAGSVIHAMSDEQDMRSMGGLKKYLPITYATMLVGTIAIAGIPPLSGFFSKDEILAHAFVSSPVFWVLGFLGALCTAFYMFRLLYMTFFGEFRGTENQKHHLHESPVQMTIPLIVLAVLSVVGGVINLPEALHGGTWLANFLSPVFAQTNQVVEPFHLSHSTEYVLMGASALGAIIMAFIAYNKYVKKSEIPQGDGASEESGLYKLSYNKLYIDELYDTLFVRPLNSLSKFLHSVVEKAGIDGLINGIGDLFVSSGKGIRQLQSGNVGFYIFMMVIGVIAFMLYGLFTI | Catalytic Activity: a plastoquinone + (n+1) H(+)(in) + NADH = a plastoquinol + n H(+)(out) + NAD(+)
Subcellular Location: Membrane
Sequence Length: 314
Sequence Mass (Da): 34315
Location Topology: Multi-pass membrane protein
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M1MY49 | MKKKGKSSAGFIAIVVVILFLAFAGFKGFVVGGWQVKSFDKVITRGLDLQGGVSVLMEIQQDKVTKEELESAKQHISLRVNKLGVAETVVTTEGEKRIRVDVPGMSNSNDIVQSLSKSGNLVFKGPNGDEILTGKDVKKATAQLNQQQGGYEIGLELNDEGTKKFADATGKYIGQNIGIYLDDEQISNPRVQVQINDGKASITGKYTLEEAKSQAGLINSGALPLPVKAVTVSNVGAELGATAFPNSIKAGVIGVGLVFLFMLINYRRQGLMADIALTLYIVLTLLVFVEVGVTLTLPGIAAFLLTIGVAVDANILTFER... | Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA.
Subcellular Location: Cell membrane
Sequence Length: 421
Sequence Mass (Da): 44860
Location... |
A0A5B8UTR0 | MEKFIKKFSQTGINDIAEVGGKNASLGEMFSHLTARGLLIPNGFAVTASAYRYFITCNDLEDKLGELMKGLNRKDFSNLSETGARARKLIMDGHIPSDLGFAITDAYDYLFDNDDQPVAVRSSATAEDLPDASFAGQHESYLNVQGHTHLLYSVKRCYASLYTDRAIKYREDKGFEHSKVFLSVGVQQMVRADIGCSGVGFTLEPESGFRDVVHLAGVWGLGENIVQGTVTPDEFLVFKPALKNKKRAILQKNLGSKSKMMIYADESDEANSTINKDTPRDMQEKFVLNDREVEKLANWALIIEEHYQKPMDFEWAKDGC... | Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Function: Catalyzes the phosphorylation of pyruvate to phosphoenolpyruvate.
EC: 2.7.9.2
Catalytic Activity: ATP + H2O + pyruvate = AMP + 2 H(+) + phosphate + phosphoenolpyruvate
Sequence Length: 809
Sequence Mass (Da): 89492
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A0A2S0R4Z8 | PRMNNMSFWLLPPSLFLLIMSMIIGSGSGTGWTVYPPLSNNMFHSNMSVDITIFSLHIAGISSIMGAINMISSIMNIRSMMMNMNKISLFSWSILLTSILLLLSLPVLAGAITMLLFDRNINTSFFDPSGGGDPILYQHLF | 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... |
A0A455XGQ9 | MGKTAKSLVHLSAQQEGDHIIIRITDDGKGMRPEVIRNKAIEKGLINAESVSSLDDEQSLGLILLPGFSTKDEISSVSGRGVGMDVVKTNIEKLSGKISITSVPGKGSEFTISLPLTLAILPVLLLRLCNQSFAVPLSLVREILSVPPSDLQQIAGKATMVVRGEVLPVLSLASLIGWEQTDKPEVGVLMQIEKNSFILSADGFAGHDDVVIKSLDTFRPKGVAGVTMSSEGEIILILDIKELLGELCR | Function: Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. CheA is autophosphorylated; it can transfer its phosphate group to either CheB or CheY.
EC: 2.7.13.3
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Sequence Length: 249
Sequen... |
A0A444L6F3 | MEGDLWFALLQIFKMGGHTRQILLGTSDFGRMIGVSQQTASRRLLELVESGLITRELTPDGQLVMITEKGMDAIREVYNALKMGLEGIDNVKFLNGYVFSGFGEGAYYVTKSGYREQFSEKLGFAPFPGTLNLKLRSSADIRARNELEALPGIIIKGFTNSERTYGDVKCFLAKVNDTADGAILMIHRTHYGKEVLEIIAPENLRKKFGLRDGDMVQLKVFLNRDHAAQSHLG | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin (CTP route): step 1/1.
Function: Catalyzes the CTP-dependent phosphorylation of riboflavin (vitamin B2) to form flavin mononucleotide (FMN).
EC: 2.7.1.161
Catalytic Activity: CTP + riboflavin = CDP + FMN + H(... |
A0A3D8HWY7 | MKKIVLICAYICEILIANSLRQELNYLQYNDIAYIRAHLDQYKSQCENGNGNSCQIIGSYYKRIYQISGYKDAEIEKASLMWFIKGCNLKSGSSCYLASLGYGNISKLPTHLPKDEKKAFELHKKGCDYGHSVSCNYVGYYYEELSNKESDENIKNEYQIKAKLFHQKASELKKTAK | Function: Hydrolyzes 6-aminopenicillinic acid and 7-aminocephalosporanic acid (ACA) derivatives.
Catalytic Activity: a beta-lactam + H2O = a substituted beta-amino acid
EC: 3.5.2.6
Subcellular Location: Secreted
Sequence Length: 177
Sequence Mass (Da): 20362
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A0A7C3C800 | MTVRFYKAHGAGNDFLITWAEDVPSGDRADLARAICARHTGVGADGWYVVERPGDGVDARVHLYNSDGSEAELSGNGTRCVAAVLCRLGLAGEELRIETGAGLRTLRLLGRSGETFRFEMAMGEPVIRDEDVDVELALSRGLCRATILDVGNPQCAVFVDRFPDDWREIGAEIERHPRFPNRTNVSFVRVIGRHAVDARFFERGAGETLSSGTGAVGAAVAAIVRGEAESPVTVRTPAGELDVRWDGEVRLTGPATVVASGEFFYSQGGG | Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; DL-2,6-diaminopimelate from LL-2,6-diaminopimelate: step 1/1.
Function: Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine and an essential component of the bacte... |
A0A8J6HH62 | MPPLSILNKPGKLSIPVDSGLSSIILNYRLKGFLSLDVDVSHLEVNQCEPAAPAANEISIFHGTHKCHNTTSQCLYRAQATSSNWSRGKYQCLCRPGFYSPHYDGVFNGTLVEVSWQDQEENNTDTWRTVFQCKQCAPGCHFCTDPSPCLATYHWPFRITLLVFSISCALCTMIINAYMFKHRKLKVFKVASPIFLSITLFGCATMYLEMAAIFPVLDRYSCIATKWSRHLGFCVTYTALLMKTWRVSLTYRVKSAHKVKLTDKQLLQWMVPILLVMLIYLGTWTLSDTPTAEEIVDNEDLRFKQCVYNWWDHSLAIGEV... | Function: Required for homeostatic regulation of sleep under normal conditions and after sleep deprivation. Important regulator of the Sh K(+) channel, acting as a signaling molecule that connects sleep drive to lowered membrane excitability, possibly by enhancing K(+) channel activity and thus reducing neuronal excita... |
F0S3U8 | MRVVEGKLKAEGIKFAIAVSRFNSFITERLLEGAIDCIVRHGGKEEDITVIKVPGAFELPLVAKKLAKMDFDAVIALGAVIRGETPHFDYVAAEVSKGIANVSLEAEKPIAFGVLTTDTVEQAIDRAGTKAGNKGWEAALSAIEMVNVLRELK | Pathway: Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2.
Function: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This ... |
A0A2T6D4K0 | MGGPESPGSWQAPGHKYLCGSLLEGCDFMGDSARLVLVLREALEKGSLPVSAMVGVSGGIDSCTLVHALVAAGSRPVVTHYDHGWGPAAAEDPAFVGELAARLGLQFRSGAAHPAPARQREDEARRQRYAFFAQQAVELGCEDLVLAHHADDQVETLLLQMLRGGGSGAVGMRETSTMRVTTDGREVVLRVHRPWLGVWRREIEAYAQLQRIDWKEDATNLDGAHLRNRLRHDLVPLLEAIGGPHVRGKLLDFAATRRDEQEWLDAICKPWAMCEKLSVKDLRAQPEFALRRIIWAWLLARGVAGLRRRHVEEVAAMVAV... | 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)... |
E7H310 | MEQFNLPVSMLRQHCFCPRIPFFQLMRGIQPVGPMWLQQGLNHHVREEMLAKRRKLSRFGISPQSFRFLEDIKLYNDSLGLHGICDGAIFTAKEVIPLEFKLSEVSPPMGARLQLAAYAMLLEYQEKRKISRRFVLYGQKGHTLEVIVDIKLRAEVHTVANLIREACKKAIVPHTAATESQCAQCEYQNFCADRF | Cofactor: Mg(2+) or Mn(2+) required for ssDNA cleavage activity.
Function: CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences ... |
A0A916QS45 | MNNTKEKFVVTAAQMRQIEERIFVAGMPVAALMEKVAGLVTRKIVKLLNPNISKIGILVGPGHNGGDALVIARELHFQGYEIIVYCPMQKLKELTNAHSKYLQSLGVNFVDNISPVKNCDLLIDGLFGFGLEREITGYLAKAINEINSWKKHIFSIDLPSGIHTDTGAILGTAISANHTFCLGLWKQAFLQDQALEYIGTSELIDFDIPLADITAILGEFPTIERITKTSATANFPLPLSPITYKYKNGNLLLIVGSHRYSGAAILTGLGARATGVGMLSIAVPKSIKPILNNHLPEALIIGCPETETGTIKQLPEDIDL... | Cofactor: Binds 1 potassium ion per subunit.
Function: Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that... |
A0A7X2TTR7 | MGSALMEGWARSGIKGIVSTRSTGGNREAAAAADIVIVAVKPHVVQVVLEEIRDVLREGQILVSAAAAIPLAAIEKIVRVPAFRVLSNLPAAIGKGATAIATHAADRTRVVSLFARIGSVELVDEAVLHAVTALSGSGPAYAYLVIEALASGGVKQGLKWDVALRLTAQTVLGAAAMVIETGVHPAELRDRVVTPGGTTIAGLHELEKSGVRGALMAAVEAGAKRSEARAQELS | 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... |
A0A318N079 | MTKTGLILAIDTKDYDLAEQWAQIADLTGQMIKIGMEFTYACGFDAVRKLARGRQVFLDLKLHDIPNTVASAIASLVSVKPAMLTIHTLGGKDMIKAARKAIDVNFPENQKPLLLGVTVLTSMDQENLNSVNLHTTPLEQVMKLAGMALDAGVDGLVCSPEEVATLRKFYEDKVVLVVPGIRLENAKTDDQKRIMTPALAHKAGANWIVVGRPITQSANPQQVAEEIICQLQD | Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
Function: Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP).
EC: 4.1.1.23
Catalytic Activity: H(+) + orotidine 5'-phosphate = CO2 + UMP
Sequence Length: 233
Sequence Mass (... |
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