ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
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A0A3D1Z1T5 | MGIFSSLFSSALGTIIGFTGDWFVAIALLTIAIKVVLMPLSLKQRRGMLLTQNFSQAKALLDEKFKDKSEKVSTELIKIMGKYRVNPLSSVLVMLVQLPALYSFYISITHLSSTIGSAIIPWVLSVSMVDGLHILPILASAIQGLQGLLAPTAQAGNMLMIILPVGIGLLFLWHAPAGLSVYWACSAIFA | 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... |
A0A1V4YGP0 | MSSINYESIAQKDAAHVMQTYGRQPLALVSGKGAVVCDVNGVEYIDCVAGIAVNNVGHCHPRVVEAIKSQAEKLIHVSNLYYTEVQADLAEELVKLTGMERAFFCNSGAEAVEAAMKLARVTTGKTDFIAAERSFHGRTMGSLSVTYKEMYRAPFRPLVQEEIFVPYDNADAMAEAITEKTAAIIIEPIQGEGGIHVPSDGYLQEVRRICDEHGILLIFDEVQTGFGRTGKWFCKDHFGIQPDIMCMAKAMGGGFPMGGIVAKKGIAFSKGQHASTFGGNPLACAAALGSIAAIKEDGLLERTTELGKYFMDKLTQADIP... | Cofactor: Binds 1 pyridoxal phosphate per subunit.
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 4/4.
Catalytic Activity: 2-oxoglutarate + N(2)-acetyl-L-ornithine = L-glutamate + N-acetyl-L-glutamate 5-semialdehyde
EC: 2.6.1.11
Subcellular Location: Cytoplasm
... |
A0A1M6J6E3 | MGILYVIIGILAFSLLIIIHELGHFAVARLMGVRVEEFSIGIFGPTLYERQGKNVKFIIKAGLFGGYVKLFGEEDEEESKEPYSFASKSPFQKILVFIAGPFMNIVLGILLFAIFTNNIGYGTNEIDKVSDNSPAMISGLKQGDKILKLNNSKISTWDDFSIKMAQTDHKDNVLLQVERNKELMEFNVKPTLQDNRYVIGILFKTIDPNFSQCIKSGVDESISITKQTFAFFGNIFKGKVKKDDVGGPITMVRVAAKSASLGINNLLFFLALVSMQLAIFNLLPFPALDGGWIFIMLFQIITGKKVKEETIGTINYIGMM... | EC: 3.4.24.-
Subcellular Location: Membrane
Sequence Length: 340
Sequence Mass (Da): 37940
Location Topology: Multi-pass membrane protein
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A0A1R4FW36 | MPNGILLVDKPAGVTSHTVVSMARRALGTKKVGHAGTLDPMATGLLVLGVGASTRLLTFIVGADKTYEATIALGATTVTDDAEGDVTASADASHIEFEAVQAAAARLTGDIEQVPSSVSAIKVDGVRSYTRVREGEQVELKARPVTVSRFDLDGFAPGERASVDAVVDCTSGTYIRALARDMGESLDVGGHLTALRRTRVGRFSIDDAVGADSIDAESLMDAATAAALVMPTLELTDEEAEHLKHGRRFATEADGLVAAVHEGRLVGVARGQHGRLVPVANMPEADG | Function: Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
EC: 5.4.99.25
Catalytic Activity: uridine(55) in tRNA = pseudouridine(55) in tRNA
Sequence Length: 287
Sequence Mass (Da): 29823
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A0A1R4G876 | MLCMPLTLLAVALGGAAGTLLRLLADLAMPEQGLPWSTVAVNLIGSLVLGVLAGRAASDRVRWPAWLREGVQTGLLGGFTTYSALALWGASAADAAPTLLSVLLVMGVAVAGVAVAYAGLSIGSRTATKGTR | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Subcellular Location: Cell membrane
Sequence Length: 132
Sequence Mass (Da): 13273
Location Topology: Multi-pass membrane protein
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A0A6L6C543 | MPRLGWSLVNDEQKHHVQKIVDEVHEAVEDASEQIAQTGKTLIRWIVEWLGIILVALSAAFLIRAYVFQTFYIPSVSMVPTLQVGDRIIVSKLSTAFGDINRGDVIVFKHPPREQCGGDTGPNSDLVKRIIGMPGDELTSRNNTIYVNGKKLVEHWQHDPNLGSDIGYVKVPEGQYFMMGDNRPSSCDSRMWGTLPKSLIVGKVVLRIWPLSHFGHP | 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: 217
Sequence Mass (Da): 24326
Location Topology: Single-pass type II membrane protein
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A0A7K1CNR2 | MVKKLTRSASSRRAKVIALIQSGQVHSQSDLVALLEKSGFEVTQATASRDLDEIGAMRGRANDGTSTYVLPESTDNTLARVIALPSDLILSVEASGNLAVVRTPPGGAQLLASALDRASRSGELSSVIGTIAGDDTVLVVSKRSDGGASLAKELSALPNSSGSPKSRLTGIKVQAKRRG | Pathway: Amino-acid biosynthesis; L-arginine biosynthesis [regulation].
Function: Regulates arginine biosynthesis genes.
Subcellular Location: Cytoplasm
Sequence Length: 179
Sequence Mass (Da): 18481
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A0A2E1CQE8 | MMSDSAEIKEEDARKKTWADLLESTTIALEEKRMFNARVEAHWILEAASGYHREELVMNLKTDAPRLGVKHLNTILDKRLSGEPIQYALGSWSFRKLDLLIDRRVLIPRPETEILVDVAHEYLNQCNQDEPLKVCDLGTGSGAIGLAIAQERDDVEVYLVDVSPDALKVASANLTGLGNHAVKVKVLQSDWFDQIPQHLKDSFQLIVSNPPYIADGEELPPEVANYEPPQALFAGKEGTEDIQSILSSAPTWLSMGGTIILEMAPHQTEYIAETAANQGYSDVKISNDLAGKERIVSCTWKE | 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... |
A0A2E4AX28 | MAIRNILLYPHPILAAKAEPIKEITDEIKTLAADMLETMVAAQGIGLAANQIGITQRILVIDLNPTTDDNEADQINDPALGPHVMINPIITQKNGSIIWEEGCLSIPDQIGAVERSAEIEAVFTNLEGEMCQVQATELMAVCIQHEIDHLNGIVYPDRMHDRTKAREIRLAMKALKSA | Cofactor: Binds 1 Fe(2+) ion.
Function: Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.
EC: 3.5.1.88
Catalytic ... |
A0A2E5HZW5 | MERRRRLRHLHVDYWIEDPASDAGTIWRVLTWIVGALHLTSAFALVGLVLLHSGKGGGVSDMFGGSVGATAAGSTVAEKNLSRITVVVAVTFGFTTLILGLLLA | Function: Involved in protein export. Participates in an early event of protein translocation.
Subcellular Location: Cell membrane
Sequence Length: 104
Sequence Mass (Da): 11044
Location Topology: Multi-pass membrane protein
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A0A7V9V9L3 | MTRARRRALPLMAVGLVFLTACSREAPNVLEPEGPGAKSVASVAYLMFGLATVVYVVVAAFIIIGALRGKKESRISDGAFIWIGGLVVPSLILAGLAVVTVKTTDTLRKPDADALKIEVTGYQFWWGVKYPDEKVATANEIRVPAGRPIEIALQSVDVIHSFWVPQLAGKVDMVPGQRNVIRFTADKPGEYRGQCAEFCGLQHAKMALLVVAEEPGEYERWVIRQQRPRGGPGSEREAAGEQVFMRSSCAGCHTVRDSEAQGTKGPDLSDFGGRRTLGALAAENNRANLAGWIENSQSIKPGNLMPAVQLEPDELLNLLE... | 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
Subcellular Location: Membrane
Sequence Length: 326
Sequence Mass (Da): 35424
Location Topology: Multi-p... |
Q9KCC8 | MEKIDIFKDIAERTGGDIYLGVVGAVRTGKSTFIKKFMELVVLPNIENEADKARAQDELPQSAAGKTIMTTEPKFVPNQAVSIHVDEGLDVNVRLVDCVGYAVPGAKGYEDENGPRMINTPWYEEPIPFQEAAEIGTRKVIQEHSTLGVVITTDGSIGEIPRYDYIESETRVIEELKEVGKPFIIVINSVRPHHPETEQLRRDLQEEHDIPVLAMSIESMGEQDINNVLREVLFEFPVHEVNVNLPSWVMVLKEEHWLRQNYEQSVRDTVQDIKRLRDVDRVVGHFAEYEFIDDARLAGIEMGQGIAEIDLYAPDDLYDQ... | Function: ATPase. Has a role at an early stage in the morphogenesis of the spore coat.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
EC: 3.6.1.-
Subcellular Location: Cytoplasm
Sequence Length: 492
Sequence Mass (Da): 55531
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A0A537Y9L6 | MFVDEARVQVTAGRGGDGSVSFHREKYQPRGGPDGGNGGRGGSVVFLAGDSVGSLSWLRDHPHQRTADGGPGRSNNRSGADAADLILAVPAGTVVRDDEGRVLADLPAPGDHYVAAAGGRGGRGNAAFLSDSRRAPGFGELGEPGQARWVRLELRLIAEVAVIGLPNAGKSTLVGALSAARPKVAAYPFTTLEPTLGRVESTPSGASLGAAISSGALRGASGFTICDIPGLIEGAHEGRGLGLGFLRHAERALAFVHLVDLSAEGDPLAAYHLVRHEVTAYRPAMGDRPEVVVLNKVDAVDPSVVDRVSRSFAAAGVAPL... | Function: An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis ... |
S7XLL8 | MLSKNYKRSNRKVIVGIDEAGRGPVVGPMVFGALILDISENTKSPLINELKDSKTLTPARRDLLYNKIKTSFDYAYKIITPQYLNKYMHKKNKNQKSLNEISYDAIIELLKDIGKKYTITKVYLDMIGSTNKYLQALHNSLGDKKIDIVTKKSKKIKIKNFSNIIKNTEYIIKTKADSLYPIVSGASIIAKVNRDILVDNKYGSGYPSDPITINYIKNNIDVIKGVVKENNCDQNIRYEWMTIKKYFVRKNEDRLNGKLNSLNFKP | 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.
Seque... |
A0A3D3DI79 | VLCADGKIFTGCNIENASFGLAVCAERVAIFKAVSEGSTKFEAIAVIGDTDKPCSPCGACRQVISEFGEDIPLIMANLKGDFKIKKIKELLPEAFGKNDLL | Function: This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis.
EC: 3.5.4.5
Catalytic Activity: 2'-deoxycytidine + H(+) + H2O = 2'-deoxyuridine + NH4(+)
Sequence Length: 101
Sequence Mass (Da): 10755
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A0A3D5DKH4 | MTVPGNGYMRASDAFSWYMERDPALRSTVVAVIWLGSVPDWDELAALIGRMSRFMPSLRQRVVEPPFRLTTPRWADDPHFDLNWHLRRVTAPAPHTRAVVLQLARLSAMDAFDRDRPLWELTLVDGIEGGGAALVLKLHHSLADGVGGMRMLAVMLDLQREPSDLGEMQSAPLGERLDLRALVAGAVGSVAGRSAYLAQRGAQMAIPALMRYARDPVGRIRGTAAMARSIYRTAAPILDTKSPIMRERAMTRHLAMMEVSLDTLKRAAMTVGGTVNDAYLAAVTGGLRRYHERHDMAIESLRVVMPISLRTESDTSWGNK... | 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: 466
Sequence Mass (Da): 50565
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A0A6I3FE18 | MRYPTMGVASEEEFPDATPSGQFPLIVFAHGYNASTDTYAALLHDIAASGFVVAAVEFPLTSSAYPGNPVQMDLVNEPADISFVIDSLLGATPPAPLVDAIAKTKVGVIGHSDGAMAVLLTAYAPRYVDPRIGMVVSIAGGYDTYGGAWFSASSAPLLVIHGTLDEVTPYSRSEELAAMDPHDVMFVAAEGASHIGPAIAPEYEPVIARVVSESFAWRLLGSTAAAASTLIDADTPPLRIVSVRG | Catalytic Activity: (ethylene terephthalate)(n) + H2O = (ethylene terephthalate)(n-1) + 4-[(2-hydroxyethoxy)carbonyl]benzoate + H(+)
EC: 3.1.1.101
Subcellular Location: Periplasm
Sequence Length: 245
Sequence Mass (Da): 25537
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F2NMN5 | MRELDVWVVGLSHKTAPVGVRECVAVSGERLAVLLERLKPMAAEVVVLSTCNRTELYVASSRVAPLQLFREHLGDFPDRLYAYRGVAALRYLFRVSTGLESLVVGEAQILGQVKEALEAARAARTTGPLLEQAFQAAIAVGKRARSETRIGAGAVSVAYAAVDLARSVFGDLAGRRVLVVGAGEMAELVLEHLAARGVREIDVLNRTRARAEQLAARFGGRAHGMEDLETALERADIVITSAAAPHYVVQARRVRAVVSRRDAPLFLIDIGMPRNVEPEVGRVEGAYLYNLDDLQAVVKRTLEARREELPRVEALIEEEI... | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2.
Function: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
EC: 1.2.1.70
Catalytic Activity: (S)-4-amino-5-oxopentanoate + NADP(+) + tR... |
A0A7K1B8J6 | MTGRRPSTLLASLAALALVAGACGGDDDASPATTAAAETTTAATEPAPETTEAPATTEPAPTTTEPAPTTTVDLAELASTYAEPGPYPVGVSTYTLAKGPSVEVWYPAVEGTTGEVTYDVRDFTPPAIREILTADVPATFTFVGARDAEAAEGTFPVVLFSHGFTGIRLQSSFLTSHLASWGYIVAAPDHPSRDLPNVLSATASGDRADSVDDLLQTLDLVVAEGAAADGLLSGRVDAENVVAVGHSAGGGTIVGAALDDRIDGYVSMASGVALGDPAATTTTAADGASGLPDKPSFFLAGSVDAVVSPEERTRPSFEAV... | Catalytic Activity: (ethylene terephthalate)(n) + H2O = (ethylene terephthalate)(n-1) + 4-[(2-hydroxyethoxy)carbonyl]benzoate + H(+)
EC: 3.1.1.101
Subcellular Location: Periplasm
Sequence Length: 429
Sequence Mass (Da): 43723
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A0A2E5EWM5 | MSGRVILTGSSTGGHLYPLIAIAQEFGSDRCLFIGSERKMDVGIVQEYGFRHLGIPVTRFHPLRWCRALWRSRRYIREFRPSVVVGSGGYVTVPVLVMAWLLRVPILLLEQNIIPGRVTRFMSKVAKKICVSFDQNKGYLPSEKMVTTGNPLRKYWLKDAAYKAFSSVRIQTDRVLLVLGGSQGSLAINRFLEANYEVLMGKGYTVIHLVGRAYYKSHYDQDYYTMISAKDGLAKVYVMPYFENMAYLYGLSDVVLARAGATTLAELSYYQIKAILVPYPYATEDHQRSNAEAIVQQKMAIMLDESLLSWSALSSALLQL... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II).
Catalytic Activity: di-t... |
A0A7K1D6U7 | MSSVLDEIIVGVREDLALRQEKVTIDELKAQAEKTSKAIDPFPIFDEAGVAVIAEIKRSSPSKGELSKIVDPASLAKKYEAGGASCISVLTEERRFKGCLADLAAVRKVVDIPVLRKDFIVSSYQLWEARAYGADLALLIVAALDQEALVSLIERSKSIGLTPLVEVHTEEEIKRAADAGAKLVGINARNLKTLEVDRNTFAKLAPLVPSGCIMVAESGVRDKHDLITYANAGAHAVLVGESLVMHEDPQAAVHELVTAGAHPATNHGR | Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 4/5.
EC: 4.1.1.48
Catalytic Activity: 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate + H(+) = (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O
Sequence Length: 269
Sequence Mass (Da): 28817
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S7QPQ6 | MKSLPTAFTSPPLMEGLVSSLHRVLGPRSSPTAIQALSIKHIVSTLQVHVPDREQARRWREFLLASETGSGKSFAYLLPLLQDLKMTESNPFPDQVRETRSRASINPRAIVLAPTHELSRQLTSFAKSVSHDIKLRILSASRSNVPNISSAKSASQMARDLDRIFGEGEAGSELELKGRGNAQDRDVDVLVSTPMKLLEMLRGRYWREERPRFPGQNNEKKPEVGFERVEWVVVDEADVLFDPDFRTFTQDLLSDISKQRGHPVSHILDPKANIAAGPVHYPFHLLLTTATIPAMLNSYLEKFHSSMTRLASPNLHRLPR... | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 492
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Sequence Mass (Da): 54902
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A0A1H3SQG4 | MHRVRRVGGYDTFPDRGVPTVPRCESPNVTRVATRFPIGRWHATLRGMSSPSRIQATSEPTTTPAGRTRPTAAEALAELLAGNERFVTRRPRHGHSVEAAASGDQEPSALVVGCIDSRVPLEAIFDQTFGSICVARSGGQVLDRAVLGSVEFAVAELKVPLVVVLGHERCGAVAATVTALRTGERPGGALGYLVDEIAPAVTEVGLDEPDVVALALRRHTVRTVRAVADAERVAERVATGAVEVVGAIYDLDTGRVALLD | Function: Catalyzes the reversible hydration of carbon dioxide to form bicarbonate.
EC: 4.2.1.1
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Length: 260
Sequence Mass (Da): 27496
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A0A5N4AZT3 | MFIRRVFALFIQLPNKSSAQFLVKRSIPIVQQNRILSKVVNSKIGEQQTQISGYLTESPLISSHLNGDGTAANREAAWRTIKYTLLLSATAVLGTGIYLVVKFGKPQAAENGLLIPDEFYAQPTPLQYIRRALKVLEGYVRLISEPSREKLLPDELNPPYYQPPFTLVLELTDVLVHPDWTYQTGWRFKKRPGVEYLLETLSGLYEIVIYTAEQGMTVFPIVEALDPKNLIMYKLVRDATNFVDGAHVKDLNKLNRDLSRVIVVDWNANSAKFHPDNVFQIPRWDGNDNDTSLIDLTALLVTIAHSGVEDVREVINYYKD... | Function: Essential component of the TIM23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane.
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 366
Sequence Mass (Da): 41612
Location Topology: Single-pass membrane protein
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A0A0F2IW47 | MSTIAVSFIVLCGIGIMSAVLLGVASNVFAVKTDLKIAQIEELLPGANCGGCGSPSCFVCAQKMAVGDVEPNVCVLSPAEKVKQIGKVLGLDVEVKVRRIAAINCVGGMSAKKQYDYAGTRSCRVCALYGLGDSFCQWSCLGFGDCASVCSFGAMKIDGRGIPVIIPDKCTGCGMCASVCPKDLITLVPVNAVPYVACNTKDKGKFVVKNCPDGCITCKKCVNGCPESAINLVFGRIKIDYNKCTKCGLCIEECPRKIIKNFQETQKLAIEHK | Cofactor: Binds 3 [4Fe-4S] clusters.
Function: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane.
EC: 7.-.-.-
Subcellular Location: Cell membrane
Sequence Length: 273
Sequence Mass (Da): 28878
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A0A2E9W316 | MAEGLVACSDDRREAGGSLPGDRPSLDVRAFRGIRMNCSRRGDAVGVIVVDVALVVGSYIIGMLPSAHYVAGRKGLDPTREGSGNPGATNVFRVAGRRAGIMVFAADMGKGAVATGVGLAVGGRSLAAVCWAAAVVGHVLPAARRFRGGKGVATAGGGACVLFGYLTILGTAIFLLVARLTRKASLASLSMAVSMACLILLSGVPLLEAVVVVCLTVLLIVRHQANIRRLLAGDEGTWKPRS | Pathway: Lipid metabolism; phospholipid metabolism.
Function: Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
Catalytic Activity: an acyl pho... |
A0A2A5G3E9 | MSHSRGVTHELRRMNRYGVLAAYIPAFDSIVGRMQYDLFHAYTVDQHILFVIRNMRRLSVPEFCGEFPLASGVFQHLPKPELLYLSGLFHDIAKGRPGDHSDVGAVDAKDFCILHGLSEDNSELVSWLVKSHLIMSFTAQRKDISDPDIISEFARHVKTIEHLDYLYLLTICDIRATNPKQWNNWKDKLLAELYNKTASLLNKGLDSENIDQHSDKEINILKIQTDSLRQLEKQGINSHQANRLWNTLNEEYFQGHTPGEIVWQTSLIHASRKNKKLGKPLIQTRVAPSGDNIELFVYMKSRTRIFYDIVTVLRNSEVDI... | Function: Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher ... |
A0A2D5C7X8 | MKKSTVFRYLFLAIFNSFIVYAVPLTITFESWFLLSLILIIGLLVNIVYFSDRFLPMKWILPGMIFLISFVVFPAVYNTFVSFTNWSTGHILTKSQAINILESRTFTPEDQQGIEFDLYVFQNQELQFYYLADIDEQNILFGKAVTNENIPTSNFALHEPSLKQNGEIVPPDGFNLLTGKDQIANSTTLQDLSLVIDQNTRAQLFKISVFGASTGLLSSTSQLYTFDESTDSITNNSTNVTCLAEIDNFV | Function: Part of the ABC transporter complex MalEFGK involved in maltose/maltodextrin import. Probably responsible for the translocation of the substrate across the membrane.
Subcellular Location: Cell membrane
Sequence Length: 250
Sequence Mass (Da): 28306
Location Topology: Multi-pass membrane protein
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A0A7W1N785 | MPSTVIVGAQWGDEGKGKIVDLLAQQSDVVCRYQGGPNAGHTIVVGEETFKIRQTPSGVISGKASVIGAGCVVDPQVLLEELTDLEARGVDPSVVVVSGNAHLIMPWHVAIDQASERRLGNLQIGTTRRGIGPAYADKASRIGIRVQDVLDPKILRQKIEVALAEKNVWLERVYEVEPFDLEEMWSRYAAYAEQLAPYVGDVSLLVDTALREGKNVL | 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.
EC: 6.3.4.4
Catalytic Activity: GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate
Sequence Length: 217
Se... |
A0A0F2IVN2 | MIKDEKREGYYFAQYGGRYVPETLIPALEELEDAYNNIKRNEKFQKQLEELQRTYVGRPTPLYFAKNLSEYVGSCKIYLKREDLAHTGAHKINNAIGQALLAKAMNKTRLIAETGAGQHGVATATGAALAGLKCDVYMGSEDMKRQALNVFRMKLLGARVIEVSIGSKTLKDAINEALRDWTTNVKTTHYVLGTAFGVCACYVDASVCVLRVAELIGDFFNVF | Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5.
EC: 4.2.1.20
Catalytic Activity: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan
Sequence Length: 223
Sequence Mass (Da): 24818
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A0A6I3GHM7 | GPSYTVDTLQALRTLEPNSELFLILGGDAAGGLDTWERPDEVADYCRIVVVDRPGVLSHVAPGFSAQRVSVPRLEVSSTDLRQRAATAAPLQHLIPEPVISLISQLGLYGDEQ | 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... |
S7QBG9 | MESRKRTHAEDADPVVTKKRAVSNGYGSPTRVNGVATEVDEPKENDELESFRKEAIFRRMKHYSREHERSQHRIEELERRRNACEAGLSAIQACWTQLIDTIRLLVKPEALSSASVDTTGLFDMSTHVDSESSPELEKALQEQMNATRELVASFVQMGSQTRAALSADDMYITCQKARTECTALRSEVQVMRARLEDAESEKENYHSRLVAAENRLERLSSRTIPQSDSRSSAPPEKHTPKEEPVANAPSPTKVKVEDVQMKDESDGQPPTAQHGEASSPTEDTMPNGTGRPSAEEMDDWREIAAMREKEIRRLEEEITA... | Pathway: Protein modification; protein ubiquitination.
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.
EC: 2.3.2.27
Subcellular Location: Nucleus
Sequence Length: 8... |
A0A538LEI1 | RSPTENLRAVAAAKRTSVGDITAVILDRDRHKDLIAEVRQAGARIRLITDGDVAGAISTAWQESGVDILFGIGGTPEGVIAASALKCMGGELQGRLWPRNDDERRAALAAGYDLDAVLSTEELVRGDNCFFAATGVTDGELLRGIRYTNTGALTQSLVMRSKSGTVRRVDASHRLQKLREFSQISFD | Pathway: Carbohydrate biosynthesis; gluconeogenesis.
EC: 3.1.3.11
Catalytic Activity: beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-phosphate + phosphate
Sequence Length: 187
Sequence Mass (Da): 20143
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A0A538BG31 | MELDVHRDLAALSFLLGTWRGSGRGEYPTIDPFPYDEEVVVEHVGEPFLLYRQSSWSPDDREPLHLERGFLRPGSSPGEVELCLAHPIGLTEIAHGVVDGPTLELSTDRDGVVGRTRTGLDVTALSRTYRADGDRLTYELFMATETTPNTLHLRAELRRLP | Cofactor: Binds 1 heme b group per subunit, that coordinates a highly solvent-exposed Fe(III) atom.
Pathway: Nitrogen metabolism.
Function: Heme-binding protein able to scavenge peroxynitrite and to protect free L-tyrosine against peroxynitrite-mediated nitration, by acting as a peroxynitrite isomerase that converts pe... |
A0A2H0MKD0 | NVQIVKEVLVDCDDDTVLLKVEQVGGAACHKGYQSCFFRKLNGGLQVVDEKIFDPEKVYKNPKK | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9.
EC: 3.5.4.19
Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-5'-AMP + H2O = 1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide
Sequence Len... |
A0A845UNK5 | MSAEDTNIPDTDGTGEELGAAAKKGASKIVKIVALLLIGSFSLAGGLFLSVGKDGVMSALSGSSEEEQTEHAATDEHRADESHEAAGEGQKYSYLNFDEMIVNITGYTAAGRKTSRFMKIKFTMVYEDHGAEAAAELESRKLYMRDAFQDYLRQLDERDLQGSFGLVRLRSELLKRAKAVAGNDAPHEILIGDLIIQ | Function: Controls the rotational direction of flagella during chemotaxis.
Subcellular Location: Cell inner membrane
Sequence Length: 197
Sequence Mass (Da): 21391
Location Topology: Single-pass membrane protein
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A0A7N0TMK3 | MQAILSQPRSFYSFTYSNWSSRRKKIMSPKVNLLLLASILLSSLLFTSTARPLRHLSADPTLTATDEAAQLNLEMMDHGLDETEQPGCGGSAEEEECLARRTLVAHLDYIYTQKHNNP | PTM: PSK-alpha is produced by endopeptidase digestion. PSK-beta is produced from PSK-alpha by exopeptidase digestion.
Function: Promotes plant cell differentiation, organogenesis and somatic embryogenesis as well as cell proliferation.
Subcellular Location: Secreted
Sequence Length: 118
Sequence Mass (Da): 13255
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A0A2H0U9J4 | MTDTRSRNVLFVGRPGSGKGTQSRLLAESLGCKRFSSGEHLKALIDAGGPLSERIRRDYDRGQLSPDWLASYFFKEAVIHLAPEESFVCEGFPRSLPQAHIADEILTWLDRSYVLLNLVVGEEEALRRQLHRAATEHRPDSDDEEKIRARFEVYQNRIEPLIAFFKEKGTLLEINGEQTPAAIAEDIRAALKIA | Pathway: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from ADP: step 1/1.
Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Catalytic Activity: AMP + ATP = 2 ADP
EC... |
S7Q239 | MGMKKRGFGKDKYNGFGGKVEGGETSAEAALRELQEEAGITAPLQHSGAMLFVSEGVEAAFHIDYYAASTYEGAITETEEMRPEWFAVPNQYASGDANHSATLPAIPFDRMWEADKIWFPLFLSRKKFNGRVDFRLDESGQHRLQRWWFGTLAES | Catalytic Activity: 2-oxo-ATP + H2O = 2-oxo-AMP + diphosphate + H(+)
EC: 3.6.1.56
Subcellular Location: Nucleus
Sequence Length: 155
Sequence Mass (Da): 17447
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A0A7V9NRS4 | MAHYLPHTDAEIASMLEFTGLSSLDDLFECVPAALRLAGGLDIPDGLSEFDTAAEMERLANANTGADLICFAGGGSYDHDVPSAVRRLAGRTEFVTAYTPYQPEVAQGVLQALFEYQTMIARLSGLEIANASLYDGATATVEAVNLAVAATGRQGVWLSDGLLREWADVVRT | Function: The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein.
EC: 1.4.4.2
Catalytic Activity... |
A0A2G8JMP2 | MAIGTERKCLNVLLVVMTVIAILLTCGIRTLRVEQYPKRKGTANFTVFELRPWDAYSKTLQQVQNESSWNLSYTQNRVVPDQRVINDTLIAAVFSCNPYWASLKGWFPRTFECPHTDKRITFIASIADASAIKDADVVIFAAGVNSSTWERAMAVRKAHQVWVLALMRDSERRERGSARPLGFNGYKFNMSFTYYSKSEVVAPFGEYIPFKEGIIMKKVNITSKSQSKKMVAWISSHCNPNAWNRTTFVHDLARLIPIDMYGACGTKEHLPRGSSATALLQTYKF | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 285
Sequence Mass (Da): 32340
Location Topology: Single-pass type II membrane protein
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A0A2G8JSK1 | MDNATFLSLFRHLREEQYDDAIRMRWFQKYSWVSALICCVYVYLVYRGRRWMESKPKLSLRIPLTLWSLSLALFSARGAYVMSTYVFTSLYRNGLQGTLCSDNFYDGISGYWKNEMKKQ | Catalytic Activity: a very-long-chain acyl-CoA + H(+) + malonyl-CoA = a very-long-chain 3-oxoacyl-CoA + CO2 + CoA
EC: 2.3.1.199
Subcellular Location: Membrane
Sequence Length: 119
Sequence Mass (Da): 14216
Location Topology: Multi-pass membrane protein
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A0A2G8JU74 | MSRKRKTHKEPTPFQVLEFETTVDNKESLGEGTEKVSNLREKAISKPKAKGKQLNYLGKLDVGSSTGGGRTKHDSEDKVEANEDLARVGRKRKKRKRKPRNNKYEGMSKKLTDEIEIQNVQTVCQESRHRDTQESQSESILAKVGSYQSKGSNIGTELAKDHEEHTSTKMRTNKKRKKVGKDKVNAKKQRKADGDEDDDNQIETREGVNGKKSEMKFRNPVVSEQTDIIYVSKKRQKRRDQIWKNSREAWGHQLKSARFRFINETLYKSSGHESFKQFKGDKSLFQVYHDGFNQQIQQWPENPVDVIIKYLNNRPQNCIV... | Function: Probable methyltransferase required to silence rDNA.
EC: 2.1.1.-
Subcellular Location: Nucleus
Sequence Length: 431
Sequence Mass (Da): 49437
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A0A1C8XXU1 | MIFFMVMPIMIGGFGNWLVPLMLSAPDMAFPRLNNMSFWLLPPSLTLLLTSSLVESGTGTGWTVYPPXSSTLSHSGASVDLSIFSLHLAGISSILGAVNFISTIINMRAPGMSFDKMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSF | 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... |
A0A8J6YMT3 | MRSHSNLPVCVGFGLSKREQVEELSPYCDGVIVGSALIRHLHEGKGIKEFCEAFLPSGRVSSR | Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5.
EC: 4.2.1.20
Catalytic Activity: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan
Sequence Length: 63
Sequence Mass (Da): 6915
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A0A944PZC2 | MDGYGGDQIRAAERPHLEAGEPLMQRAAEGLAAVVSGLLDDPAVRPGEGPGSVLLLVGSGDNGGDALFAGARLAADGRHVTVLRVGSRVHGAGLAAALAAGATLLDDPDDDRSADDLAGAADILRAAEAHGSTRLAAIAAEAALEADLVLDGILGIGVHGAAPLRSPAREVVGAVRELARDQRAPFVVAVDVPSGIDVDTGGIADDHVLQADVTVTFGGVKAGLLRGPGATLAGRIELVDVGIGAELAAMEPLVRS | Cofactor: Binds 1 potassium ion per subunit.
Function: Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX... |
A0A7V9EHS0 | MTIRVGHLYPEYLNIYADRGNIAVLARRATLRGYELVVESIGIGEQVRPGAHDLLYVGGGQDREQMLIAPDLAEKGAAIREAVAEGATLLAVCGGYQLLGRGYRGRDGSLMAGAGLFGHETVAGTKRMIGDVLLECELEPGIRRPLAGFENHAGRTVLDSGAEALGRVVHGFGNDGESGFEGCRLGRAIGTYLHGPLLPRNPWLADWLLAQALAHSQSGEPPSLDPLPDDLEAEAFRVAAGRARQRGGRR | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: The lipid II isoglutaminyl synthase complex catalyzes the formation of alpha-D-isoglutamine in the cell wall lipid II stem peptide. The GatD subunit catalyzes the hydrolysis of glutamine to glutamate and ammonia. The resulting ammonia molecule is chan... |
A0A7N1A132 | MEAVETNSSKEDMLSPLSDSDSHPHPLQLQPHLHPPLIHTRPANPNPHLLSTPVNDNNNSSSSSFTGFTLLSQSANGAVLDSDSGQKKKRGRPRKYDADGNLRASYASPLGVSPPPPPHSTPMLPPPGFGISPPASFGGPDSLGSQKARSPSPYGFGEIFARTAVGDFTPHVVTVSRGEDVAGKILLLGQQGHKGICVLSAIGVVSNVTIRQPTSAGGILTYEGRFEILSLTGSYTVASNTGSGGGKGWVGALSVSLAGPDGRVVGGGVAGSMTAASPTQLVVGSFTPGGYKPQKRKYVRKVSPAPMNILDPVMAAKPIS... | Function: Transcription factor that specifically binds AT-rich DNA sequences related to the nuclear matrix attachment regions (MARs).
Subcellular Location: Nucleus
Sequence Length: 380
Domain: The PPC domain mediates interactions between AHL proteins.
Sequence Mass (Da): 39672
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D3UG24 | MRNNIILTGFMGSGKSTIGKMLAETLDKKFIDSDSFIESQKGCSIKEIFARQGEGVFRELERNFITLHAGLWGHVIATGGGMPIFFDVRKMGFVIFLDAGFEVIASRLHGNITRPLFKNKQKTKTLYDMRKKIYLERCDMVINAEEPRKEVVAKIIKNLPPDP | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.
Function: Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
EC: 2.7.1.71
S... |
A0A7W0L2R5 | MPDKEDKRARHRATQQAAAARRRKEELARRRRGRIIGLAILVGLAVLTVFVVGAQTGEDEDAPTDSTGEQSENEEPTASEGESGDCDFSVEPPENDARQYEQPASQEQVLSVVADYFAVIETNCGVIEVDLLEEEAPATVANFIFLAEDGYYDGLTWHRVIEEFVIQSGDPEGTGKGGPGYEFEDELPEDSSVYTFGAMAMANSGPDTNGSQFFIVSHAAKNALEGEETPAPAGLQQLYSHFGQATEESYETIAAIASVETSSEPETQDRPVEPVYILSVTIEER | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
EC: 5.2.1.8
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Length: 285
Sequence Mass (Da): 31003
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A0A7V1XNP8 | MTVRAAPRSGAARRRPRGRSRRVWTKEDEVADGAKAKKGGKLKLVVPVILLLGAGLAAKSLLLGSPAQKAEAKPKKEEGAIVTMDPVTVNLADAGFHYARVGFGIVLTTTANSKEVEERLPLFKDEAIRAVGAFQSRELKTVEGQDELRHRLTEVAFELYGEEEVMKVILTEIVVQ | Function: Controls the rotational direction of flagella during chemotaxis.
Subcellular Location: Cell membrane
Sequence Length: 176
Sequence Mass (Da): 19187
Location Topology: Single-pass membrane protein
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A0A7W1JH14 | MSDAAVPAPQAPQFKSSSARSLPARLMAAFSGTNGLIAKLVLLGLFNAMVVWAATILATHHKWIALLIVAVAAGAIDAIYLVPRKATLPLKFLIPGTIFLVAFTVIPIVYTVDLAFTNYSTGHILSKPEAIEQIKLRSLSQPPNGRTYTLSPALDGGGKLTLLLVDNKTHTAYVGTRNGLGKLPTSRVTITGGAITAATGYKLIKGAKLFSLDTELDQFRVPLPGGSAIHPEGADYAVQLIPDKKYDPKAGAFTSTGSGVVYRDNGAGSFATDTGQKLEPGWKTYNGFKQFSKIVTNPLYRRPFLRVLAWTVVFAAMTVL... | Function: Part of the ABC transporter complex MalEFGK involved in maltose/maltodextrin import. Probably responsible for the translocation of the substrate across the membrane.
Subcellular Location: Cell membrane
Sequence Length: 452
Sequence Mass (Da): 49117
Location Topology: Multi-pass membrane protein
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A0A7M3ZRH4 | AGASGKGGLEINMNQIKALTEGGAQAAVDMGIGFDEDLPSLESNGLLEVDDVSLSSRALERGLRALGTLGSGNHFLELQSVEKLVDEETSKQWGLYEGQLLAMIHSGSRG | Cofactor: Binds 2 manganese ions per subunit.
EC: 6.5.1.8
Catalytic Activity: a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + a 5'-end dephospho-ribonucleoside-RNA + GTP + H2O = a ribonucleotidyl-ribonucleotide-RNA + diphosphate + GMP + H(+)
Sequence Length: 110
Sequence Mass (Da): 11515
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M1WF92 | MEESAAKIAHEKSMHELLMKHPHPNIVQCILCVPEGFFMERMEATLRTRIEQYSAGHVPSNRTKARWITQIASALSWIEGLGFVHGDLRPANILLTANENIRLADFDTSVKIGEELEAASDPFVKLNKGFKTPQAGPITEQFALGSCIYTIRFGSDHSYLNIRLADFDTSVKIGEELEAASDPFVKLNKGFKTPQAGPITEQFALGSCIYTIRFGHIPLDGVDPPDRVQKLMNNELPSTENDAEFGGALP | Function: Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N... |
M1W0Q8 | MVRHKKDLAARGKRGGRGGGGGSRQPRQHDGGDDDSDSAQTGKPAFKAACWDLGHCDPKRCSGKKLMRLGLMRDLHMGQRHNGVIITPNGRQVVSPADRELMDQYGAAVVECSWARTQEVQWSKVGGKCERLLPYLVAANTVNYGKPWRLNCVEALAAAFYICGHADWAEQILEPFSYGESFLEINSRILKRYAACEDAAGVKKTEAEWMEKLEREYNESREQASQEDMWTSGNTNYRPESSSDDDDDDDDDDEQDSDARSDRQGSVDGIYLGKKPPRDPKPGEIPTHMADSSTKQDKDPFDITDDSDDDDEAAMEEIRR... | Function: Aminocarboxypropyltransferase that catalyzes the aminocarboxypropyl transfer on pseudouridine at position 1191 (Psi1191) in 18S rRNA. It constitutes the last step in biosynthesis of the hypermodified N1-methyl-N3-(3-amino-3-carboxypropyl) pseudouridine (m1acp3-Psi) conserved in eukaryotic 18S rRNA.
Catalytic ... |
A0A2G8LIH7 | MMNSNWVLSDFDRDGRERRLKEYKKVVFVRNPMVRVLSAYLSKLKNFRDLQRHWEYAFGVDILRKYRPNSTHVVQEALSIPFSQRPFLNVTFAEFIQFITDRETNITLTDLTDHWLPQHIVSHVCEIGYDFIGKYENLAVEAPFVLEWLGLTSITTFPDIHESNAVFQMANEYLNVPVGHLQALLEYYSQDMEFFGYDAIDDFYENFNETLRLQMMSTIPR | EC: 2.8.2.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 221
Sequence Mass (Da): 26214
Location Topology: Single-pass type II membrane protein
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A0A7C2E8D6 | VEEGQADKAVVPIENSIEGSVNATLDSLAFEADLFIQGEMVRQVRHHLLAREPMPLSEVKRVISHPQAAAQCRRHMVELLPGVEVEAANSTSEAAMRVAESREAVAALGSGLAAELYGLTVLREGMEDHPENRTRFVLLGKEKAPPTGHDKTSLVCFIYQDRPGMLLQILQEFAYRYINLTKIESRPTKEVLGEYCFFIDCEGHEQDEVMASALKCLQCKLPQVKMLGSYPRWREEGEGA | Pathway: Amino-acid biosynthesis; L-phenylalanine biosynthesis; phenylpyruvate from prephenate: step 1/1.
EC: 4.2.1.51
Catalytic Activity: H(+) + prephenate = 3-phenylpyruvate + CO2 + H2O
Sequence Length: 240
Sequence Mass (Da): 26724
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A0A7K0NVG2 | MLADRCALSVTVVADEPQSASGRASRSDTSRLEALSDGVIAVAITLLVLDLKVPHVEDESLWNALVTQWPSYFAYITSFLVIGILWVNHHSIFRQIRATTRGLMLINLVLLMLIVAIPFATSLVADYVTKPGVNATVAMATYSAVALAIALAIASLWGYALRHPALLEPEVDVEAARKAFPRFSIGSLVYLVLLVVSFVSPILALTGTFLVALYYSFEHLPKARATEA | Catalytic Activity: K(+)(in) = K(+)(out)
Subcellular Location: Membrane
Sequence Length: 228
Sequence Mass (Da): 24713
Location Topology: Multi-pass membrane protein
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A0A7W1I7L2 | MPSTRRVLTENEARRIVAERCLPATTRHSSIGLELEFLSFTADRGRPSLDTLESLAATPLPSGGRVTCEPGGQVEASSPPQPTAAEAIAVTAHDVAALRKRAEAGGVELVAVGADRWRPPQRVVDSCRYRAMEAHFDAINDAGRQMMCNTAALQINIDGGHDRWRVAHLIGPAMVAAFANSPGDDRMRSTRVANWLAMELGRTRAVTGPLPDAWIDYAFAAPALVARNDDDGECIAIPEPAPFLEWLNRGGALGFPTAADLTYHLTMLFPPVRPRQWIEIRYLDALPSPWWEVATLVVAALLDDAVVTETTAAVAGTETL... | Pathway: Amino-acid biosynthesis; ergothioneine biosynthesis.
Function: Catalyzes the synthesis of gamma-glutamylcysteine (gamma-GC). This compound is used as substrate for the biosynthesis of the low-molecular thiol compound ergothioneine.
EC: 6.3.2.2
Catalytic Activity: ATP + L-cysteine + L-glutamate = ADP + gamma-L-... |
A0A6I2ZQM6 | MMTTIRAVLPDADEPKREKSTNTPAHGEERRVEAVQREVDAVTFWERGEEPEFGRIAFFTDAVFAIALTLLVLDLRLPRMSGNPDDPASILNALGDLTPKFVSFGIAFALLAKYWIANHGFFARIGRFDKRYLTICMCYLATVAFLPFPTSLIGEYESNPISGVLFALSLAAVSGLETVLLWHAQRAGLMRTPASEQVYRWQVSVALIPFTMFLVTIPLAFVSPTVMLLSWIVIAPLAGRWAHRRKPAALTSRQNPIPDGDSCE | Catalytic Activity: K(+)(in) = K(+)(out)
Subcellular Location: Membrane
Sequence Length: 264
Sequence Mass (Da): 29342
Location Topology: Multi-pass membrane protein
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A0A7X8YVW2 | MAERVRRRKTRSSDPFRFDKALLEEGLAAVCEASSLCGAHRRDDLRLAGVDEAGRGCLAGPLVAAAVVLDYAAAPFVALSGLTDSKQLSLDAREGMYGGILGSAARVCWVACSPRTIDRDGLHVCNLRALSEALETLGGEYALALVDGFDIRRPELRARSLVGADYKSAAVAAASVVAKVVRDRLMKTLAPRYPEYGFAEHVGYGTGRHRNALKQHGPCPLHRLSFQGVAEPQLGLWDE | 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... |
A0A6I2ZZX1 | MFGTFVRFKCCPQGAAIRSCPTSSQSGKKVKRILLVGGGTAGHVEPALAVGNWLLVKSSDIACEFVGTKSGIENELVPLAGLKLHHILKAPLPRSITPSTLLWPIKFAISISQALKIVKSADLVIGFGGYVSAPCYLAAKISGVPLIIHEANAIPGWANKLGARFADEILVAFKSSLKEGGKWASAKLVGMPIREEIFAISNMSKSDRSGIWDATYRELGLDRSKRTIFIFGGSLGAQTINNVVERTLPELLKLDINIIHGIGRGNTLPKAVPGYVPLSYISNMAAMYIASDLIISRGGAVTCAELDLSNAFALIIPLPI... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II).
Catalytic Activity: di-t... |
A0A2G8K0S4 | MNQAEAARRNMKDFLTMYNNFTESCFNSCARNFNYRSLTPEEQRCTDRCTDKLVNINHRLISVYVEINPMNRQLASAQETPTKVDQPQQPLQNELQPPESQPQPVGNLASQVQDVFGEGTKVTKENSGHVITGGADEGPQQKG | Function: Mitochondrial intermembrane chaperone that participates in the import and insertion of some multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer me... |
A0A168LHG6 | MAPNVELSQQKHSLGLYHAPTGLIDAKDRGTPDAHVSRDPNLTRLTGKHPLNAETPIPLLMDHGFITPNSLHIVRNHGPVPQNQWDTHSIAISGLVNKPVTITMDDLLQLPSHTLAVTICCAGNRRKEQNMIKPSIGFSWGPGGIGTAYYTGVFLRDVINHLAGGLKPEALHICMEGNDNTAKGGYGTSITVNRAMSPEFDVLIAYKMNGEPLPYDHGYPVRCIVPGCIGGRSVKWLSKIEASTDVSQNPFQNADNKVFPSTVLSADQATAENWWTNPDYSVYDLNVNGVIAAPYHGSRIALDDLSNKVVVVNGFAYGGS... | Function: Nitrate reductase is a key enzyme involved in the first step of nitrate assimilation in plants, fungi and bacteria.
EC: 1.7.1.3
Catalytic Activity: H2O + NADP(+) + nitrite = H(+) + NADPH + nitrate
Sequence Length: 868
Sequence Mass (Da): 96577
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A0A7V9KYJ4 | MSDGVRVALTRAAGGNDELAARLRQEEFDPVECPLIRIEPIGGSPICVEGYDWLVLTSRTAVDELLRRLDGSPPRIAVIGPGTADALRERGLEPALVAAESTQEGLVRELPRPAGRVLFAGAEGARPVLVDELGADFAPLYRTVEERVDTFPDADLVVLGSASAARAYAVLGRATPCVSIGPVTSKEARGRGLHVVAEAASPALEGLVEAVKLAASSIASSRS | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 3/4.
Function: Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III.
EC: 4.2.1.75
Catalytic Activity: hydroxymethylbilane = H2O... |
A0A537WUF0 | MPSSPPRRARIHGTPTGSPTSTTETCVDHEPSTDSEATYRLPRSVTPSRYDLTLEPSLETSTFEGNEAITVTVHEPVTEIVLNAKELEVLDGSLEAADGSAIDLEKVVLDVGSERVTLGLAETVSTGEWILRLRFRGTLNDRMVGFYRSRYDDEGASHVIAATHFEATDARMCFPCWDEPDLKATFGVTVIAAGGLTAISNAPEIERASLAEGRIRVRFADTMVMSTYLVCVIVGRLVVTEPANARGVPMRVASRPGKEHLTGFAADVGVFALDWFADYYDIAYPEAKLDQAAIPDFAQGAMENTGLVTYRETLLLMDDA... | Cofactor: Binds 1 zinc ion per subunit.
EC: 3.4.11.-
Catalytic Activity: Release of an N-terminal amino acid, Xaa-|-Yaa- from a peptide, amide or arylamide. Xaa is preferably Ala, but may be most amino acids including Pro (slow action). When a terminal hydrophobic residue is followed by a prolyl residue, the two may be... |
A0A7K1IT21 | MAGSRRERELAKQKLQRQLDKQAATATKSQGRNIAVIAGVVVIALIVIGAVIAKANSGSTTASRPTPTISSAPVAYKCTPVTKLQTVAKQYPNGPENITLAQGLTLGVKLKTNCGDITIDLESQSAPENTKALIFLANTGASQVLVPGDQNSGVRQVEGYFDNTACHRLTTAGIYVLQCGDPTGTGGGGPGFKTKDENLTALGTGSSVIYPRGIVAMANAGPNTNGSQFFIVYKDSPLPPNYTVIGEVTKGLNIVESIAKGGVQGGGTDGKPKLSLILKKVDSFQTQSVNNPKIIGGNAG | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
EC: 5.2.1.8
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Length: 300
Sequence Mass (Da): 30980
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A0A8J6YU13 | MFRDKESFKQAFQERLESFYGKSLTDTTQMERYSTLANMVREHVSADWIHTNRLYKKTGTKKVYYISMEFLMGRLLRSYLVHLGIYDLCAEGLEDLGISLKELEEEERDPGLGSGGLGRLAADFLDSMAALKLPGHAYGIRYRNGLFEQKIVDGYQVEVPDYWLQEGYDWEVRRFDRSVEVHFGGRV | Function: Allosteric enzyme that catalyzes the rate-limiting step in glycogen catabolism, the phosphorolytic cleavage of glycogen to produce glucose-1-phosphate, and plays a central role in maintaining cellular and organismal glucose homeostasis.
EC: 2.4.1.1
Catalytic Activity: [(1->4)-alpha-D-glucosyl](n) + phosphate ... |
A0A0F2IZZ3 | MFRNIPNKFFLTKAFLQLSLAFQFLTIIPLPFSNRRHREINDESIIGKCSAYFPLVGLFIGVLTASIYLFFISLLPYDIASALVIAVMVIITGGFHLDGVSDTFDALAARKPIAQKLEIMKQGSAGPIGVSAVVLTLLIKFALLKSLIVMGSDDLIYLSVLFPVIGRWCAVCALFYGKSARADGLGALFIRYTGAVELIISTVILLFAVIFLNLYTFGFTFYLILNPIAIILFFYIGVFFTVKFFHGKFNGLTGDNLGFIIEFNEILFLLAYQVYN | 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... |
A0A2G8LCL3 | MTMRLIILYIVMCVFAVTFSRSSKDIHQTSAVRRNLVGTDEDTERSNRDDGNRRRFTALWELDFMVGCTTGRGFIEAIYDYAWYGCYCGLGGKGVPVDETDRCCMLHDHCYDVAFHSRDCPLEPDVYFIPYKRHYHMTNCQTPDARITCDTPRSYPWWFPYPHCAAAICRCDAAVAMCLGGSRFNPENVLYPKYTCRKGTAPTIQVATDLVSAPNTLETTFATDTVTEFFEETTVLETTELTTNVNKAANDADDDVIDDVTDKARKVLRGYSRSRFLLKMKQYRSSQFLHYPKKYSINIGK | Cofactor: Binds 1 Ca(2+) ion per subunit.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+)
EC: 3.1.1.4
Subcellular Location: Secreted
Sequence Length: 301
Sequence Mass (Da): 34452
|
A0A7J9X064 | MADDLNERAPVETGNADEDVRGPDWTRLDWLCVTLITLAGGLVRFIGLGDAKGQMFDEVYYARDACLYAGQPSSVCGIASPENYVHPPLGKWLIAGGIRVFGHNEIGWRVAAAIAGTLTILLVYLLARKILRSTFGASLASGLLAMDLLAFVQSRVSMLDVFVPLFGVAMFLFLAYDRDRLAALAVERANWRPWRLAAGVAAGAAVATKWSGVFFLVAAIAITVIWEVAARRRSGEGRPLRRALAEEGPAIVAWLVLVPALVYVATYIGRVDGSVLALPWGDGSWFHNLFEEQRRALDYHWQLKARHPYESPPWSWILLK... | 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... |
A0A7J4G1K9 | MSVEEELEEELTFWDHLSELLIRLRRVVIFGFISMVTYLIMPASIEDLSKMVRGEVYNPLSLYLLERVRSDLLEEVADRVELIPATFAAPIELYFQAALVLGIVTTLPYLAYEIYMFLEPGLYPHEKKFLKRFIFGFSFSFLIGALYGYYVIMPITFRILLLFSGLLDLTNFFNVTSFYELVFLGVVSTGFVFTLPVFLVLAFKFQVLDPNQLANIRRYLYFGVFFITAVLTPDPTPISMILISLPFIILFEISIWIGRKVYAG | 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: 264
Sequence Mass (Da): 30516
Location Topology: Multi-pass membrane protein... |
F2NQ08 | MCRVAEGEHARPWPRTEAEQRTRELETLQRLAQATLRSLEPREVLQSALATLVHTGWFRCGEAFITGTAGLDTVAVGTCPYTDLKACALRPALLEWVREALEAKEVRQVQGWQIVPIDAEAAIAVSGGQVSRPFLNTVVECIRAAFERARLYTALKEKEAQRARLFKALLNAQEEERTRISRDLHDQVGQALTGIILGLEAALADPNPARLEGLKELAGMTLADVRRIALDLRPSVLDELGLEAALKRYTREVGERYGLEVELVARLPLRLPPEMETVLYRVAQEALTNVVRHARAQRVSVVLTAHRDAVQLVVEDDGVG... | Function: Member of the two-component regulatory system NreB/NreC involved in the control of dissimilatory nitrate/nitrite reduction in response to oxygen. NreB functions as a direct oxygen sensor histidine kinase which is autophosphorylated, in the absence of oxygen, probably at the conserved histidine residue, and tr... |
A0A538E4P7 | MSSDANPKVLVVDDVPRNVRLLEAVLSPNGYTVTSASSGSEALERVAADLPDLVLLDIQMPGMDGYEVCRRLRADPATRFLPVVMITSSDTEVRVNALEADADDFIRKPFDQEELLARVRSLVRIKHYHDTIEAQAAELAEWNQTLEARVDEQTEELRASRTRVVSAADAERRRIERDLHDGAQQHLIGLAVRMRLARDLADSEPEKAMEMLDALGDDVQEALEQLRDLAHGIYPPLLQDRGLPEALTAAAGSAPIRTRIQVDGITRYEPDVEATVYFCCLEALQNAAKHAGEGATATVNAWQEAEELRFDVADDGAGFD... | Function: Member of the two-component regulatory system NreB/NreC involved in the control of dissimilatory nitrate/nitrite reduction in response to oxygen. NreB functions as a direct oxygen sensor histidine kinase which is autophosphorylated, in the absence of oxygen, probably at the conserved histidine residue, and tr... |
G2QIJ9 | MVQFYTVVGALALTFSAVQAAPNLSARQNIPDPAGEKNVGNGRGLQFIGGQCLGAADCASGCCAILPKGGQTIGVCSGVGAQNQAGKQGCGFESGVGAGNQTQGGSQGGNQNNTGGNQRNGGNNQCNNQGDNQNNGQTGATIRPSTLKPDPAGAANVGNGQGQQFIGGECTSDADCASACCALVNTGEERFGICSGPAANTQNGKQVTTARDAPKNLLEFYDVIRAKGHCRHELASGFYSRDNGPNNFAYCGDYLDSAGVIYIQGRSGALANLDVDCDGSSGGPSDDGRCRRELSPDLQNATSFRDVLASYGRAGVAELN... | Function: Chitosanase catalyzing the endo-type cleavage of chitosan, the deacylated form of chitin. Chitosanase may be crucial in the degradation of the deacetylated portion of chitin in the fungal cell wall.
Catalytic Activity: Endohydrolysis of beta-(1->4)-linkages between D-glucosamine residues in a partly acetylate... |
A0A0N1B756 | MPAVAPETGVVHVYQRVGELTRTLHNTLRDLGYYNEIEDSLSNLPDAKSRLTYIARLTGEAAEKVLNAVEVAQSEQDALAERAKAARAALLENPVKAVATGGVLDFVDSVIANTAKTNATLTDIMMAQDFHDLTGQVIRKVVSLAGNMETQLVKLLVEVTPPEQRQKIKQDEKLGGPVVNPEVRADVVKGQGDVDDLLASLGF | Function: Plays an important role in bacterial chemotaxis signal transduction pathway by accelerating the dephosphorylation of phosphorylated CheY (CheY-P).
EC: 3.1.3.-
Subcellular Location: Cytoplasm
Sequence Length: 203
Sequence Mass (Da): 21886
|
A0A538KCM0 | MVDVLVIPDGAAQPVRPGVPTALQAARTPVLDALAADGTVLRVATTPAGWPAGSETGIPALLGAAPAAPVGRGRVDAAAHGIDVPDGLIAWRADLRYANGRRASVRQARDVCAHMRGWAFSIGGHRLVLVAAARPQDRRTLGLRLTVWDDGASLSGPLPVPTTVVAARGAAAGCARLLGAGVVVPGGATGDVDSDLRSKAQAAIGAVAAGAERVVVHVGAPDEAAHRRDPEGVVAALERLDAELVAPLRDLVGAQGGRLVVCPDHGTDPATGAHDGAPVPAVLWGAGVAASGPDRLDERAAGECRVVEPVALLPLVAEAA | Pathway: Carbohydrate degradation.
Function: Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
Catalytic Activity: (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate
Sequence Length: 320
Sequence Mass (Da): 32079
|
A0A7V9D9T2 | GASVLASAELGPDSADKRPSVQVGDPLTEKLVIEASLELVAKSIISGLQDLGAGGICCPASEMAAKSGTGIRIDLDAIHLREPGMAPFEIMISESQERMLAVVAAERAPEALEVCRAWELEARVVGEVTNSGLVEVVVSGETAASIPAAALASQAPLLSRPAVRPEGLDVVRAGPCGDDPHEDLGGCLLALLASPGGASARWIWEQYDHMILLGTVLGPGGDAAVIRLPGSAAAVALSLDGPGRLCHLDPYEGARLAVAEAARNVACTGARPAAVTNCLNFGNPEKPEVMWSFQEALRGIADSCSALGLPVTGGNVSFYN... | Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 1/2.
Function: Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent ... |
A0A7K0VG31 | RTLKDAVNEAMRDWVATVSETYYCLGSVMGPHPYPWMVREFQRIIGEEAFTQCRELLHGDDPDFVVACVGGGSNAMGIFSGFIDTSTARLIGVEPAGGAAVGRGVPGVVHGMRSYLMQDEHGQVQEAHSISAGLDYPGVGPEHSYLASIGRAEYPTVTDDEVISAFQLMARSEGIIPALECAHAMAWIVREAPKMQGKVVLMNLSGRGDKDVGQMMEILG | Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5.
EC: 4.2.1.20
Catalytic Activity: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan
Sequence Length: 220
Sequence Mass (Da): 23703
|
A0A7V4MY58 | MGTTIGIIGTGNMGSALVRGWLRAGDPGLRLLVWDKMEDAARRLLTCEAVAMPPSLEWLVQQADPLLVVVKPKDAASVLQSVAPLLRSGQKLISCMAGVDLAQLRAWTGPAPVLFRIMPNLGVELGAGAVAVSDEPGGPAADLQAVIDLVSQLGLTFAVPEDMLDAVTALAGSGPALLAVAVEALEDGAVAAGLPRGLARRLVRRTARTTACSLPSFGDSPSRLCEAVTSDDPRERSVFTRFRERGIADSYRAAIVAAARRGRELRAQAATHESAPCTLEGDAGPTTEEG | 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... |
M1W764 | MNRRRAIVSRGTTCYETQHGHVAKFQWALDQPPLEFEQLKLAETMGVEGIVRVVAHRRFTSIAEMREGLQFPKAYRFRLPSEDERLSDMRGFSCSSHTPDGPSGSKKPASADQESNLENGCNDDPSNAEAKPGLDTPGEKLWENKIFSCLVISPAGREISDFGSIKELLECERDAIRAHRSLYVEGKILHRDISPHNIIITRPATADGFKGMLIDLDMACTRGSDQDGPSHAVGTLPYMATEVLLKIDHTYRHDVESFFYVLLRMCGREAWDPVKGLAVEGEKQRKESRFRTWHVGTLRDIGELKQGQMGAPRTLNNLMK... | Function: Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N... |
A0A538IDE9 | MSVSIHDLAAYKARGEKFVMLTAYDFPTAQILDEAGVPVLLVGDSLAQVILGYDTTIPVSVDEMLHHTRAVARGAHNALIIGDMPFGTFGLTPQSVHLFGGYKVQGRSEEQAENIVRWAKELEEAGAFSLVLECVPSDLAARITRALSIPTIGIGAGPDCDAQVLVINDLLGLTPGKAPKFVKRYANLREEISAAARRYADEVARGEYPGPEHSYS | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 1/2.
Function: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ket... |
A0A1Y1LIT3 | KEQLARTREELATALYQHDAAVRVIARLSKERDEARDSLSKVTVTDGAINGEEMVVDSVEGLPEALAEKVDEVHASLSKGRKKRPVPEGWATSDDISAFDTTASSALPVSETTSIDLEGGYAALGGLKGEAAIYSIEADKLERKLPVNEAVTNTLWSGPKLFFATSQGNVKVYEGGNEVASVSEHSGPVTGLSVHPGADILGSVGTDKSIVFYDLATMKRASRAFADASLTTCTFHPDGHLFAAGTVSGDIKLYMTKNLDQAAIFKLGAPVQALVFSENGFWLAATAKGQTTVTIFDLRKEGDAATAKVLETGGSVQSLA... | Pathway: Protein modification; protein ubiquitination.
Function: Ubiquitin-protein ligase which is mainly involved pre-mRNA splicing and DNA repair. Required for pre-mRNA splicing as component of the spliceosome.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysin... |
B3IT86 | SVSALVHSSTLVTAGVYLLIRFNLLLIDMFFLKLLLLFSGLTMFMAGISANYEFDLKKIIALSTLSQLGFMMSILSMGMADLAFYHLLTHAMFKALLFMCAGVIIHMMNDNQDIRMMGGLSLYIPLTSLCLNISNLALCGIPFLAGFYSKDLILEMVSMSNLNMLIFYLYFFSTGLTMYYTLRLLMYLMINDYNLLSIYNLYDEDYIMLKSMFILLFMSVITGSFLSWMILFIPYMIYLPLNLKLMIIYVSLIGMLLGYMISNMNINSLNKFLLTYKLSLFFCLMWFLPNLSVYGLNYYFLNFSYKMMKNIGY | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed... |
A0A1C8XZZ7 | NALIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLSAPDMAFPRLNNMSFXLLPPSLTLLLTSSLVESGTGTGWTVYPPLSSTLSHSGASVDLSIFSLHLAGISSILGAVNFISTIINMRAPGMSFDKMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTS | 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... |
G2Q3L5 | MSIPATNPTYYEILNLSPSALTSLDEPAAASLIKRAYRRALLRHHPDKKSSTSSSPSSLPSSSPASAPGYTIDQISTAYATLSRPALRQAYDRSLLVLQSQRHRPSSLAPSSATESPGGGGGGGGAADFQTGIETVDLDDLDYEEKGRGRDSETTWYRSCRCGNPRGYQFGEADLEDAADLGELMVGCADCSLWLRVCFAVLDDDDDGQDEKGGEKREQHAGKGSGDGMKPVLLNSGEVAA | Pathway: Protein modification; peptidyl-diphthamide biosynthesis.
Function: Required for the first step of diphthamide biosynthesis, the transfer of 3-amino-3-carboxypropyl from S-adenosyl-L-methionine to a histidine residue. Diphthamide is a post-translational modification of histidine which occurs in elongation facto... |
A0A2J6X2L2 | MEKGRKLYIRSLVNIAAEPIAYFWPMRTFITRNPLREFEYKPFKEALKDGELLFGGRGYLKREDYRYLYFEGHMKEESLKEGIREFLSSVESASGLPYEELLFTLFVEDVKEPSLNALYKGKISNDTMSVLLEHFKEDPAKVCKDILTSAGLKHTLQDIIDILTGKDLSQTIDELTIKTAFDFLDEGQSTIDMPGRSAGFYKAWRELARKNLRFFLWTGKNLKDMVENFEEPEDAIDYVLKSFGIPEDLWEKYISLELARLKGIAGFIKWRSHNKFYYWQKVHPVDMVDYTAIRLLIAKAVIDANKKDLPFEANYKALEE... | Function: Part of an energy-coupled inorganic carbon pump.
Subcellular Location: Cell membrane
Sequence Length: 999
Sequence Mass (Da): 115283
Location Topology: Peripheral membrane protein
|
A0A537WWZ9 | MPSRSRERQLAKLAARRRAEQTQSNRRRRITAGIVGAVVGLAAIGVGAAVLLDRNDNPTVSASPSGTSSPSAPAPVGLPTKTGTVTAQASPAKQVACGGKRPAAADTPKPQFDHAPAAKDVLNKNTIYTAVMRTSCGTIRIQLNTTDAPQTSASFVFLADKGFFDGLFFHRVVDSIDVIQTGDPLGTGSGGPGYAIPDELTGKEHYTAGTAAMANGGANTGGSQFFIITGPQGTNLDGNPSFTIFGKVVGGLDVAKTINALMPAQKNYDGAPTKAVYIETMTIETAKAPASPSASPSA | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
EC: 5.2.1.8
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Length: 298
Sequence Mass (Da): 30527
|
A0A2K5AUF4 | LLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLTYSPAMLWALGFVFLFTIGGLTGIVLSNSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGIIHWYPLFTGLTLNNNLLKTQFLTMFIGVNVTFFPQHFLGLAGMPRRYSDYPDAYT | 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... |
A0A8I1V3H1 | MASNQQRREAAKRKLQRQNQRRVQQAKAAHQRLMIVGVIAAVLVIAGGVWLISSLFSPGNDTAAKSGGATKAANAYGTGTDAPTATGQSGSASDTAAPTSTAPATECSYPKGGTAAKPVKPPTDLNPPKTGTVDATLTLNTGDVTIALDRANAPCAVGSFLSLAQQHYFDNTTCHRLTTAASLKVLQCGDPTGTGTGGPGYSFADELTGKEKYTTGVVAMANSGADTNGSQFFIVYGDSQLSPNYTVLGKVSSGLNVVQAIAAKGVKGGGQDGAPADPVTIEKVAVGS | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
EC: 5.2.1.8
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Length: 288
Sequence Mass (Da): 29145
|
A0A6J1A564 | MEEKLCMKNSMGRESLSSKSPGRFLPAFVPENEKKLVAERKKTFANNAVAKKSKELGLQRAKEFGWTNAYVFTKAMGEMIIDPMRENTPVVIIRPPVVEGTCKEPFPGWIEGHKCGKGKLTGFPGNADNVIDIVPVDMVVNATLAAMVRHGVTRKVDINIYHVSSSMSNPLTSQDLFRLFCQHVMSPCIGANGKHINIQKLKIFASMEEFDAHLLREATTNSSDRNRRRKIETRKFMELPKHLVLLIVALRGMVVGFFCCRVHSPGRVFENPFLMLAAIGSALVVAAIGSALVVAANGSVLGFGRLLSNP | Function: Catalyzes the reduction of fatty acyl-CoA to fatty alcohols.
EC: 1.2.1.84
Catalytic Activity: a long-chain fatty acyl-CoA + 2 H(+) + 2 NADPH = a long-chain primary fatty alcohol + CoA + 2 NADP(+)
Sequence Length: 310
Sequence Mass (Da): 34166
|
A0A538DAN3 | MDRAAVLELVRDRLADILEIEPGVINEGDSFRDDLQADSLALIELVEAIEEELSERTVGFRIDDEDLEDLKTVRDAVDYVVSRLG | PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine of apo-ACP by AcpS. This modification is essential for activity because fatty acids are bound in thioester linkage to the sulfhydryl of the prosthetic group.
Pathway: Lipid metabolism; fatty acid biosynthesis.
Function: Carrier of the growing fatty... |
A0A7N0UHU4 | MWDRHCSTHGEYLGLTGARLDGPEMLACGLATHYVPSQKLSLLEEELVKSDSSDAAITSEIINKYSDQPRVKQKSAYLRLETIDKCFSRRTVEEIVSAVELEAAIKADDFINTTLQSFKKASPTSLKITLRSIRRGRLEGIGKCLTREYRMVCHVMLGHVSKDFLEVTISSHGTLRLHRPQQIKSHDLSDFKCRVAELYLSTRIETQSGRLLN | Pathway: Amino-acid degradation; L-valine degradation.
Function: Hydrolyzes 3-hydroxyisobutyryl-CoA (HIBYL-CoA), a saline catabolite. Has high activity toward isobutyryl-CoA. Could be an isobutyryl-CoA dehydrogenase that functions in valine catabolism.
EC: 3.1.2.4
Catalytic Activity: 3-hydroxy-2-methylpropanoyl-CoA + H... |
A0A7N0VJJ0 | MERLQNEIIDCELFTCLKHLRGESYQNFMMNKLVPVVGNVCEANLGMDADVAAEMANEVEVIVNSAASTRFDERYDVALNTNTMGPCRLLSFAKLCKKLQVFMHVSTAYVNGEREGVVLEKPFRIGESIAAERARSDAERSSIPVLDIEAEIKLASRVCDNNDSCCQKMRDLGEERAKVYGWQNTYVFTKAMGETMLDVMRGDIPVVIVRPSVIESISNEPLPGWIQGNRMLDPLILSYGKGQLPGFLLDPQAVIDVVTNLTHTLLSPFSVPA | Function: Catalyzes the reduction of fatty acyl-CoA to fatty alcohols.
EC: 1.2.1.84
Catalytic Activity: a long-chain fatty acyl-CoA + 2 H(+) + 2 NADPH = a long-chain primary fatty alcohol + CoA + 2 NADP(+)
Sequence Length: 273
Sequence Mass (Da): 30337
|
A0A538FMA7 | MAVVVLFIHHDRPDASRLAAEAAGWLHGQGHSVRVPDDDPVGRDSADETLPPEEAARGADLAVSLGGDGTVLRTAELVAPWGVPVLGVNMGRLGYLTEVEAAGLEKALDRFWAGDYQLEARMTLAVTRDDDAERPMVALNDAVLVKSHSGHTVHIGVTISGRPFLDYAADGLIVATPTGSTAYNLSARGPIVSPRLRALLVTPVSAHMLFDRALVLEPTETVRVEVLDGTAAELIVDGCLQANLEPGRTVTCAAGECDARFVTFGERDFHHILKSKFGLADR | Function: Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
Catalytic Activity: ATP + NAD(+) = ADP + H(+) + NADP(+)
EC: 2.7.1.23
Subcellular Loc... |
A0A7K3L4F5 | MFGIGGFELFLILLFGFLIFGPDKLPAMAKTLGKAIAKFRNAQEEMTGVLKGEVFDKDADEPFKNPLDALDNAAAKASKVTDQAKKAATQAHEKAESFSARKARYDRERAAKKAAEAAGASGVAPAASTATMSFSERKARYDRERAARQAEQAKPVAEAADEPAPAAGPAADASADQKGGE | 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. TatA could form the protein-conducting channel of the Tat system.
Subcellular Location: Cell membrane
Sequence Length: 181
Sequen... |
A0A538AQY9 | MIDARKAKVGERQPAQTGDGFVGGDDAGLQVVEQPAQGRFVHRGGHYPRTVTRVAFLGPAGTFTEEALLSQPDLAEAELVALPSFPDVLRATAEGTVDYGFVALENSIEGTVRLVMDLLVFEHELLIQREVVLPIRQNLLAPPGLALGDVRRVVSFPDALAQCREFFERELPGVEIVAANSTAEAVRMVAEERPAATAALGTSLAAKLXX | Pathway: Amino-acid biosynthesis; L-phenylalanine biosynthesis; phenylpyruvate from prephenate: step 1/1.
EC: 4.2.1.51
Catalytic Activity: H(+) + prephenate = 3-phenylpyruvate + CO2 + H2O
Sequence Length: 210
Sequence Mass (Da): 22477
|
M1WEV9 | MAMHATLVRWSLRALADMKDCSRATVKSFTSRSDAEAFAAGEKIPASSGDPERFYAVAVGNPTGIYTDWSEAAAAIKGVKGPKYKKFGSRKDAAAYIRQYGSPEAVEALGEAIPASEAVLALKSVTSGAAPPARKTATARTAAAAAAAAARADSGVACPAEGVLQIYTDGSSLANGRAGARAGVGVYFGDADARNVSERLVGEPQTNQRAELMAMLRALEIAPLKQTVQIISDSQYSIKCLTEWAIGWKRKGWKTATGENVKNQDIIRAILDKMDERTRANSTTYFHWVKGHASDRGNMAADRLAVRGANLP | Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
EC: 3.1.26.4
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Length: 312
Sequence Mass (Da): 33068
|
A0A1E3GN28 | MSDETENTSQQIRNVFFVSDRTGLTAESYGKCLLAQFPDIEFETITLAFVDSKEKAEDAREQINSLCAESDLPPLVFSTLVNNEAQQIIEDSDGLVISLFYNFIGSMEGFLGIQASQKVGVSRILISDTTYQKRLDAIDYALTHDDGIRPDQYEEADVILVGVSRCGKTPTSLYLAMNFSLKVANYPLTVEDLEAEELPEYLKIHKHKLAGLTIKPVPLSRIRRQRRPDSNYSSLEICQAELDKAMIMFDKIDIPVFDTTNTSIEEISSRVVRTLGLARERIRESTITFNKTKNLR | Function: Bifunctional serine/threonine kinase and phosphorylase involved in the regulation of the phosphoenolpyruvate synthase (PEPS) by catalyzing its phosphorylation/dephosphorylation.
EC: 2.7.11.33
Catalytic Activity: [pyruvate, water dikinase] + ADP = [pyruvate, water dikinase]-phosphate + AMP + H(+)
Sequence Leng... |
A0A6L6ETY1 | MDTDGQPRQPPPQVPAHEGVGLLAGLRVVVTRPRHQRSALIDRLTALGAEAVSVPTIDIVDPRDGGQALAAAVGELQTYAWVAFTSANAVSRFCGLLRDPRDLVGVRIAAIGTATVAELSRHELVADLVPERFIAESLLEVFPLPDPHVGGDRGSPSGRVLIPSAEVTREVLPKGLRELGWSVDVVTAYRTVPAVIS | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 3/4.
Function: Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III.
EC: 4.2.1.75
Catalytic Activity: hydroxymethylbilane = H2O... |
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