ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
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A0A2N2WQJ2 | MNTLQITGNRWFRFSIWAFIYLLWVIWFGNWWFILGLAVIFDIFITRKVKWAFWKKNYKEGEKRNAWLDWLDAIIFALVVSTFIKSFFFEAYMIPTSSMERSLMTGDYLFVSKLAYGPKVSQTPLSFPLVHNILPVTGGESYLKWIQNPYRRLAGLSKVKRDDIVVFNFPHGDTVLKAIPTEDYYTHVRIHGREQTQMMYGPVVVRPDDKKDNYVKRCVAIAGDTLEIINGKVYVNGAPQQALGGVQNTYRIFTNGTPFNAKIIEGLGLSQEEIYFDSSMPGYSAFPLNEDEVKSIASMSNVLEIRQNIDIYPPDFPDFP... | 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: 451
Sequence Mass (Da): 52388
Location Topology: Single-pass type II membrane protein
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U5DF57 | MAKKDKSKERPVKAQKQQASKPSGSSVKNSTAKNGKEVKPKAESAGGFDLVKFSKETQEELAKVVWPSRKQLVSESAAVILMVTLVATLIYFFDNLFAWISGKVF | Function: Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation.
Subcellular Location: Cell inner membrane
Sequence Length: 105
Sequence Mass (Da): 11549
Location Topology: Single-pass membrane protein
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A0A090P8U4 | METQVSLNQLAAKPKSKLMATLDRISQLDGIIAAVFLAVIVVLMSYGVVTRYVFNSPSSWVEEVCLALFVWMTFMGSSALCAPMKWYV | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 88
Sequence Mass (Da): 9768
Location Topology: Multi-pass membrane protein
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A0A960QR53 | MSESTRYKAFPIGLVTSCSTLLIIGCGDETLQRVRDARKFDWYKIYLISPTLTDEVRAEVAQDERMIHLAREATEEDVSKAQVVVEDTEDLQKADEIAAWCRKYGKPLNAVDKNQYCDLYYMSLIYRGPLVISISSGGDAPALSVALRKHLEANLSEGWAYAADRMAALRKSLPGGQARKMLLKNMVRDKQLLEAIVQNDRDTIDQRFDEAIQRI | 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: 215
Sequence Mass (Da): 24335
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A0A8T0W0N4 | MEASAGLVAGSHNRNELVVIRREPGGGGPGAAARLAAEAPCQICGDDVGVGFDGEPFVACNECAFPVCRACYEYERREGSQACPQCRTRYRRLKGCPRVAGDEDEDGVDDLEGEFGLRHGGEEGGDGGGDPRDIAASMLRAHMSYGRGDAHHPAAGFGAAPGVPLLTNGQMVDDIPPEQHALVPSYMGGGGGGGKRIHPLPFADPSLPVQPRSMDPSKDLAAYGYGSVAWSDRMERWKKNQESLQHARSDGGGDWDGDDADLPLMDEARQPLSRKVPIPSSRINPYRMIIVIRLVVLGFFFHYRVMHPVNDAFALWLISV... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Pathway: Glycan metabolism; plant cellulose biosynthesis.
Catalytic Activity: [(1->4)-beta-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->4)-beta-D-glucosyl](n+1) + H(+) + UDP
EC: 2.4.1.12
Subcellular Location: Cell membrane
Sequence Length: 657
Sequence Mass (Da): 73326
Location... |
A0A8J3PCT0 | MTTTVRLGTRGSTMALAQARHVARELESAHAGLAVRIVPVSTHGDRWTGSLVTAGGKGAFTSEIDALLQAGDIDLAVHCLKDIPGDVALPEGICIAAYLPRDDPRDALISRDGLRLDQLARDAVVGTSALRRQAQLQRARPDLRVKPIRGNVDSRIARLDSGDVDAIVVAACGLHRIGQAHRITQVLPAELMGPAVGAGTIVVTTRTSGPAYALVMAVDDPDSRDTSLAERALLHRFGASCNSAVSGHASIDRDTVTLHAAVYAPEGDRTLATVVAGDRTAAPALGRQAADELLALGARKLLDPYLR | Cofactor: Binds 1 dipyrromethane group covalently.
Function: Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
EC: 2.5.1.61
Catalytic Activity: H2O + 4 porphobilinogen = hydroxymethylbilane + 4 NH4(+)
Sequence Length: 307
Sequence Mass (Da): 32221
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A0A960NLV6 | MNLAVVGANGMLGQDLNRAAQVRGITMAGFDLPEIDLCRPDSLAVLPAVDAVINCAAYTRVDDAETDREPAWRINAEGAGNLARWCAAHAVPLIHISTDYVYNGRKGSPYVETDDTDPLSYYGQSKLGGEVEVQRAGGKTCIVRTQSLYGLGGRNFVKAILNQILKGRTELTVVSDQVSCPTYTLHLAEGLLNLIQAQATGVVHLAAAGGCSWHEFACAIVEEVGAAVDVKPMHASSLNYPAPRPAYSVLDTSRYQSLTHATMPTWRQGLQAYLEEEPMVVELKQSNG | Pathway: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
Function: Catalyzes the reduction of dTDP-6-deoxy-L-lyxo-4-hexulose to yield dTDP-L-rhamnose.
EC: 1.1.1.133
Catalytic Activity: dTDP-beta-L-rhamnose + NADP(+) = dTDP-4-dehydro-beta-L-rhamnose + H(+) + NADPH
Sequence Length: 288
Sequence Mass (Da): 30988
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A0A8J7N7Q9 | MDDPKVILHVDMDSFYPSVEERENPELRGKPIAVCMFSGRTETSGAVASANYAARKLGIKSGMPIAFAKKKGGGNVVFLKVNKPLYETVSKNIMGILGANADVLEQSSIDEAFLDVTMRAQADFKKAEKLAHRIKAEVKEKERLTCSIGVGPNKLVAKMASGFKKPDGLTVVKPDDARGFLRKFTLGDIWGVGPKTLESLNREGIENLDDLENFSLEELMRIFSDKKGRWLYNAARGFDESPVEPATEREQLGRIATLKEDSKDPEYIGETTDRLAAEVFERFKERPEKFRTVSIFMVTTELTGKTRSKTIPLASRDPEV... | Cofactor: Binds 2 magnesium ions per subunit.
Function: Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5'... |
A0A2T3KML5 | MNLEKKREYVKTSLFIAAILLIKFVVIDMYKIPSGSMIPTLNIHDRVLVNQLAYSLRIPGTEYHIAKISEPKRGDVVVFYEHNSGDIYIKRVMAIGGDKVSQIGEQIYINDKPLKTKKVSYPNLTSQFDYFNEQNGGKSYIIQYNKNVSNWFNYINIYRHGDFGTKKEQRKIRYSNWVVPYGKLFMMGDNRDNSKDSRFLKGSFISIDQVIGKAIAVPFNLSPLNLQSRNGIEFIPRLTKANTGLYTV | 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: 248
Sequence Mass (Da): 28555
Location Topology: Multi-pass membrane protein
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A0A9D4P469 | MIKYTWIIIVAIFLFDYAQASFGDRLKLFQYFFINCYRNNCSKPNSLAQFESRQPVYLKLFGWDCQSECQLEAQWQTIDRLQNHETPQSIPQFYGKWTFYRLFGIQEPASFIFSIGNLATNFYCWQDYRIFGKYSNDPFYNLWQIQAFISMNAWFWSMAFHARETPLTEKLDYFSAYLIVIYLLFTITVKMFVEVFKFNSKMIQISLAMPSSASTFII | Function: Involved in the lipid remodeling steps of GPI-anchor maturation.
Subcellular Location: Golgi apparatus membrane
Sequence Length: 218
Sequence Mass (Da): 26068
Location Topology: Multi-pass membrane protein
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A0A6J1ITT8 | MLLIFFAETASQPFPSLHLSPPTAFTRRNGGSRFLHFLSLAESLLGNMNFDDVLVPEDHVSRSYNDTYYIDSQTVLRCHTSAHQAELLRRGYTQFLVTGDVYRRDSIDSTHYPVFHQMEGVRVFSLNDWEASGTDGTSLAADDLKKCLEGLARHLFGAVEMRWVDTYFPFTNPSFELEIFFQEKWLEVLGCGVMEQEILKRSDKENNVAWAFGLGLERLAMVLFDIPDIRLFWSADERFTSQFSKGKLGVKFKSFSKFPPCYKDISFWINDSFTENNLCEVVRGIAGDLVEEVKLIDSFTNKKKGMTSHCYRIAYRSMER... | Catalytic Activity: ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + H(+) + L-phenylalanyl-tRNA(Phe)
EC: 6.1.1.20
Subcellular Location: Mitochondrion matrix
Sequence Length: 347
Sequence Mass (Da): 40070
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A0A833QMY6 | MGLSTITGLAIVIMGVSGSGKSTVAESLANAIGCKFVEADDFHPPSNKEKMKSGFPLSDSDRIPWLESLRDAIKENIEHGHNVTLSCSALQKRYREILRSADCDYKPGNYSLCKVKFVCLEAPVEILMERMERRSEEGSHFMPSRLLQSQLDLLQLEKDEAIIRVDATMGLESISEFIIDLLNRNWNL | Pathway: Carbohydrate acid metabolism; D-gluconate degradation.
EC: 2.7.1.12
Catalytic Activity: ATP + D-gluconate = 6-phospho-D-gluconate + ADP + H(+)
Sequence Length: 188
Sequence Mass (Da): 21062
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A0A0G0REP3 | MATPKDIEDIKKSASVLIIFGATGDLSTKKIFPSLFELFKNNLLPEKFKIVAAARSKFKTSDFTSRLKENLNPSDKKAWQGFEKLIDYVSSDIEKNQDLDKIKGAISKFEQSANVCPQQIFYMAVSPFIFKRAVENLGKNKLNLGCQMHSKRARVVVEKPFGFNLKSALDLDTALFKYFEDGQIFRIDHFLGKETVQNILAFRFGNEIFEPVWNNQYIDNVQITMAEYVGVEKRGEYYDKTGALRDVIQNHLLQLMSLVTMEMPEKFDHTNIRRKKLEIIKSVKKLTPEEVISSTVRGQYEGYLNEEKINPKSQTETFAM... | Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 1/3.
Function: Catalyzes the oxidation of glucose 6-phosphate to 6-phosphogluconolactone.
EC: 1.1.1.49
Catalytic Activity: D-glucose 6-phosphate + NADP(+) = 6-phospho-D-glucono-1,5-lac... |
V6DID5 | MNKKNLLIGAHMSIAKGIEQSLYLGKEIGCTTIQIFLRSNRRWEFNDFTNQEIYKFNQAKIDTKIDTIVAHSRYLINLGSSSEEVQNKSLSSLDKELINCDKLGIKYLVLHPGAGNENIEKCINKVAQNINKILNNNHSRVTIALENTAGQGSYIGSTFEQLYMLLSLIEDKNRIGICFDTCHAWASGYNFTDKESYSQMWHEFDSIIGLDKLKVIHLNNSKTDISSHIDRHEEIDKGKIALEAFKLIINDKRLESIPKILEIPYNNYQELKRNLDLIKELVD | 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... |
A0A8J7M9F7 | MTDTNVEALAWRHADTEAARAGNAAVAETISGWIARDERDRVAAALESWSGADILALLVHLRLKKARRLFRWLGDDVSLAVLAELDPRTHGILLERETQRRLKKLVCRMKRDEAVRMLASLPRKMAGEIIDGLDDPEGWRRDLSYREDSAGEAMRRGFLAMPQDRTIGDAIEHLRQRSDEIDRLDALYVVDEEYRLLGYLRVRDLLLTPPETRLGDALRLDLVSVDAETDQEEVLRLAERRNLRVIAVKDPEGRLVGTVTPRELAAIARDEAEEDMLMMAGVDPHSTAHDTPLQIMRRRLPWLLAGLVGAAGAGAAMAGF... | Function: Acts as a magnesium transporter.
Subcellular Location: Cell membrane
Sequence Length: 469
Sequence Mass (Da): 50748
Location Topology: Multi-pass membrane protein
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A0A928L2R0 | MELSDLRAQIDEIDSEILGLFSRRMKVCEEVADYKRRNNLPVFQKGREKELLAGIKARAPEEYADGAQVIFSNIMDVSKCIQQSRNLDASTAFSPEMLDMEYSGTIACQGVDGAYSGAAGKRLFPSATVEFFPKFDDVFSAVAEGRVKYGIIPIQNSTAGSVSEAYSLMGKYNFSITAMIRLEINHCLAAKKGTDRKEIKKVYSHIQALSQCSEYLKSHGFEQVSYDNTAMAAEFVAGSDEAIAAICSCECAEKYGLEIIDEKIADVYPNCTRFICISRDFCSTSDADTVSVIVGIPDEKNSLYRLLTKFSVSGINLSHI... | Pathway: Amino-acid biosynthesis; L-phenylalanine biosynthesis; phenylpyruvate from prephenate: step 1/1.
Function: Catalyzes the Claisen rearrangement of chorismate to prephenate and the decarboxylation/dehydration of prephenate to phenylpyruvate.
Catalytic Activity: H(+) + prephenate = 3-phenylpyruvate + CO2 + H2O
EC... |
A0A3S3UQS9 | MRLGSSPPVRARHHRESRPPQQSEIRHHRRNIQVSNYQANTGIAQGVGTGEIPAVRANIRSVRRTPNQSRRSAIRTAFVFDLDGTLIDSAPDIADAANRLLVEYGGTPQPIGKVMKMVGGGAPKLLERAFAAAGLAMPPAEEVLARFLEYYHTGPAMMTKPYPGVPHLLGALHRAGNPIALCTNKPGRATDAILTRLGWDGLFDAVVSGDDLSVKKPDPLPVLAALFLAGGTPNRAVYVGDSHVDVQAARNAGLPVMVLTHGYAHGPVSALRADALATTIRPLLRLAGS | Pathway: Organic acid metabolism; glycolate biosynthesis; glycolate from 2-phosphoglycolate: step 1/1.
Function: Specifically catalyzes the dephosphorylation of 2-phosphoglycolate. Is involved in the dissimilation of the intracellular 2-phosphoglycolate formed during the DNA repair of 3'-phosphoglycolate ends, a major ... |
A0A8J7X0L1 | TVPGIKDLPVACKLALKDCDICVACGMPGGAEKDRVCAHEASQGLINAQLMCDKHIIEVFVHEDEAQDEKNLKKIVVDRCRKHARNAVYLLKNPEWLGKNAGKGLRQGFENAGSI | Pathway: Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 2/2.
EC: 2.5.1.9
Catalytic Activity: 2 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) = 5-amino-6-(D-ribitylamino)uracil + riboflavin
Sequence Length: 115
Sequence Mass (Da): 1... |
A0A1I2S671 | MIKIENVSKTYSTGVAALRNINLTIQDGEFCFIVGRSGSGKSTLVRLLTKELDPDEGSITVNDTDLGKLRRRHIPGYRRRLGVVFQDFRLLEDRTVYENIGFAQLIIGKTDDEIRENVTRIMHLTGIDAKRNSYPHQLSGGEQQRTAIARALVNRPEILIADEPTGNLDHENASEVMKLLERINEQGTTVIVITHDREMVARMRKRTVRISFGQIVSDEISGDSDYYFDDPLPDDHAQPEPSHESDSESPESPVEEPVEDDTQESSGKATSQAATAPSEGPAQDNTSLEWSMDDWIEEAPVRKPSKGLRGNHRRPHKSRK... | Function: Part of the ABC transporter FtsEX involved in cellular division.
Subcellular Location: Cell membrane
Sequence Length: 323
Sequence Mass (Da): 36241
Location Topology: Peripheral membrane protein
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A0A1I8JCE9 | YNHGKIQANRRHVRLRPALVETALAPRALLEQEELSVARRKLLVDRQKLADRRKLLVDRQRLQADRRELLVARRKLLVDRQRLQADRRELLVARRKLLVDRQRLQADRRELLVARRKLLVDRQRLQADRRELLVARRKLLVDRQRLQADRRELLVARRKLLADRQRLQADRRELLVARRKLLVDRQRLQADRRELLVARRKLLADRQRLQADRRELLVARRKLLVDRQRLQADRRELLVARRKLLADRLNPDQKTGFYNKMKVVGLVSGGKDSCYNMIECVRSGHQIVALAHLYPPSGAEMDSFMYQTVGSEAVALYAKA... | Pathway: Protein modification; peptidyl-diphthamide biosynthesis.
EC: 6.3.1.14
Catalytic Activity: ATP + diphthine-[translation elongation factor 2] + NH4(+) = AMP + diphosphate + diphthamide-[translation elongation factor 2] + H(+)
Sequence Length: 920
Sequence Mass (Da): 102346
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A0A192IKW2 | MTRQLGHWLRYLTSGLAIVADALVALMMLHIAFEVMMRYVFGISVPGTLTLVSKYYLPAVVFLPLAMAERRGNHISVEVLTQVMPRRVQKALEVFAWLLATAVFATLAYQTLLDALKKTRIGAFELDFGYQFMTWPSYYVLPVGFAAIALVLLYKIAITLFRKPDHLGLETGDGPAESAGAKRS | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 184
Sequence Mass (Da): 20486
Location Topology: Multi-pass membrane protein
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A0A937TBX3 | MSQPLSSADALISAVENQRMFDAIVPRYDRLNALMSLGLHRRWRRQAVNRLDPVAHALYLDLGTGTGDLCVEILRQEPAARVLGIDPSTAMLEQARTKFTQLGVQDRAQVVSGDACNLDIEDAHVSGIVSGFCIRNLTDRNRAFHEMYRVTVPGGRIVLLELTRPSQPLLRAGHRLYSRLVVPLLGRALSRGDAYRYLTHSIEAFAEPAAIVTELRQAGFEDAAYRPLTGGVVALFSARRPAGMTDGIEA | Pathway: Quinol/quinone metabolism; menaquinone biosynthesis; menaquinol from 1,4-dihydroxy-2-naphthoate: step 2/2.
Function: Methyltransferase required for the conversion of demethylmenaquinol (DMKH2) to menaquinol (MKH2).
EC: 2.1.1.163
Catalytic Activity: a 2-demethylmenaquinol + S-adenosyl-L-methionine = a menaquino... |
V6DFC6 | MFSLIFMFVAAALIVVALLLLMYGYKKSFIAQRLIEEAQAKLESVKRDIETEKKEALIKLKDELYKKRTEFDLEIKKERAELERFQAKLNSKYEAIENKDQRLEDLRKELQQKERTVSRTADIQRANEQKLKSLYEELILKLESISGMSKDEARQALFDSLENEVRLSNEKYVQKVEEEARHFAKEKAVNIIVTAMQRYTADQVSPASSGVIHLPSDEMKGRIIGKEGRNIKSLELATGMEFVIGETPEIITISGFNPIRREVARRSLEKLISDGRINPTKIEETVHQTEKEIEEIIQEYGKNAVLQFNLQGIKPEIISL... | Function: Endoribonuclease that initiates mRNA decay.
EC: 3.1.-.-
Subcellular Location: Cell membrane
Sequence Length: 519
Sequence Mass (Da): 58879
Location Topology: Single-pass membrane protein
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A0A2H5W2F3 | MIRVRVPSFAKINWMLEVLGTRPDGYHEVRTVLQTIDLTDVLDVERTEGEIEVFCAHPEVPEGEANLVFRAAHLLRRAKGVKAGARIRIEKRIPVAAGLGGGSSNAAIALLALARLWGVALEVGEQLELGCALGSDVPFFLLGGTALGIGRGDEVYPLPEVRADLLVLANPGFLIPTAWAYRQLTKRGIVGNISVCSRVWHRAVREGEPPSLSEIVGRNVFEEIVRERYPELARGLDRMRESGAVAVGLSGSGPTIFGVFESEDPAIRAEVAFATLGWWRARTRTVSRRQYWERLSAALSNEASRP | Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 3/6.
Function: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
EC: 2.7.1.148
Catalytic Activity: 4-CDP-2-C... |
A0A0G0TVC2 | MSPENETILKQTALVQAHKRVGAILVGFAGWEMPVRYEEGTLAEHRRVRAQVGLFDVSHMGRFEIQGSDAVRFMDWVVTNDVQSLEAGQAQYTAMCHEDGGIIDDLLVYRLEDRILAVVNASNKDKDLKWMQEHAKGLDVQIDDLTEQTALIAVQGPKAQQLLSRLTPTDLDKIAYYRFAQAEVAKSWSYLSRTGYTGEDGFEIWLPAGEAVRTWQTLLAVGQDLGVRPCGLGARDTLRLEMGYCLYGHEIDDTTNPLEAGLGWVVKLDKEDFIGRQALVSKKESGLERRLVGIKLERDHTPVPRQNYPIVQNGEQIGSL... | Function: The glycine cleavage system catalyzes the degradation of glycine.
EC: 2.1.2.10
Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolate + (R)-N(6)-(S(8)-aminomethyldihydrolipoyl)-L-lysyl-[protein] = (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + NH4(+)
Sequence Length: 376
... |
A0A059CEV8 | MAEAAPVNAELLEWPKKDKRRLLHVVYRVGDLDRTIKFYTECFGMKLLRKRDVPEEKYSNAFLGYGPEESHFAVELTYNYGVSSYDIGTGFGHFAIATQDVYKMVEEIKAKGGTVTREPGPVKGGTTVIAFVKDPDGYIFELIQRGATPEPLCQVMLRVGDLERAIKFYEKVCFLVLHIDEILLLMCFPMILFPVKMQLAATLSV | Pathway: Secondary metabolite metabolism; methylglyoxal degradation; (R)-lactate from methylglyoxal: step 1/2.
Function: Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione.
EC: 4.4.1.5
Catalytic Activity: (R)-S-lactoylglutathione = glutathione + methylglyoxal
S... |
R7CSR2 | MIIKITPQTLDGTIHVPASKSMTHRELIASALAKGSSTLRNVTMSKDIEATIRILCQFGAVIDVEKGEKETLIHVTGGLKKQEGTIIADAGESGSTLRFLIPIGIYSGNRVQWTGHGRLSERPLTPYYDLFDEKGIAYQAESGGLPLTVEGKWEGGLFELPGNVSSQFFTGILFILPLLAGGSALESTTEVESEGYINMTIDTMRKRNIALTLRRAGHYEVFGPQEYEAADTAVEGDYSQAAFWLAAGLSGGTVKLTGLTRNSRQGDRAILDILIRMNAFLAFEHDDIIAVESQTEGTVIDARDCPDLVPVLAAMASVSK... | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7.
Function: Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-ph... |
A0A292PGA2 | MLQKSPCHFRPCSSRSLHAGLCSRRARDPIKLSQLRNRCMKIDHVVLEYRSQVPINAVGHVVIEIHDMRLTEGDTKQAEFTIPIKCNCNLHYYSSSFFSIKDKNPWRVEYRVENTNVVNGVHFCKMLGKLKLSSAKHSTDVEFRPPKIEIQTKEFTVNDIDFWSVGSKPQTRRLVDGSRLMGHSSRSLRVPYLAIGPNESWASRSEIGHSSVTSRPYKNLRGLDDSAIDPGPSASQAGSITREEIADIITKTVEQCIKSNVNAPVSKDI | Function: Movement protein involved in the cell-to-cell and systemic transport of viral genomic DNA. Begomoviruses use 2 proteins to transport their DNA from cell to cell. The nuclear shuttle protein (NSP) shuttles it between nucleus and cytoplasm and the movement protein (MP) probably transports the DNA-NSP complex to... |
A0A0G1XBJ0 | MEYEPVIGLEIHAELKTQTKMFCDCKNDPDEKHPNINVCPVCLAHPGTLPVPNKDAIEKVILVGMALHAEIPERSHFDRKNYFYPDLPRGYQISQYEDPLVKGGYLEFAISSGSIRHIRITRVHLEEDTGRLSHDSKSQSSAVDFNRAGVPLMELVTEPDIRSAEEARCFGEELQLVLRYTGASDADMEKGQMRVEANVSVRPKGMKEFGTKVEVKNINSFKFAEKAIEYEIKRQTGVLEKGEKVIQETRGWDETKGVTFSQRAKEGATDYRYFPEPDIPPLVLDQAWLQSIRAKLTELPGAKRKRFAGEYKLDEKTIEL... | 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 ... |
A0A4R5IXY6 | MTALTAPTPAPTLAQTAAQTTAPTPAGRIWRFGDNVDTDAMAPAVLMKSPLPVLARHCLASLRPEFPGSVRPGDVLVAGANFGIGSSREQAPQALRELGVGAVVAQSFGGLFYRNAINLGLPVLVCAEAARLADGARVALDLETALLRLDDGSTVACEPIPGFLREILGAGGLVPHLKRRLAARA | Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 2/4.
Function: Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
EC: 4.2.1.33
Catalytic Activity: (2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate
... |
A0A915XM55 | MSTATEPTATTIQAVEAAHVLQTYKRQPVVFVRGEGVWLVADDGKRYLDLLSGIGVNVLGHAHPAMVEAVRDQVGTLVHTSNLFFHPFQGPLAEKLTKASGLERAFFCNSGAEAVEGCLKFARRFWYTAGKPRKQFIAFERGFSGRTMGALSTTWDAHYRDPFGPLVPEVRFVSNEDPDDLLSAVSDDTAAIIAEPIQGEGGVRPLPPQIVAAINKACGATGALYIADEVQSGLGRTGHMFHFEAIGLCPDLISVGKALGGGFPIGAVLVSSRVAASISAGDHGTTYGGNPLGCRTALAVLETLEGGLLDHVRRVGPVFA... | 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
... |
A0A9E0K6D8 | MNVLRVIANPKPVEQSASLKIEAAFMAALQQKHPDAQVTTINVFQDDVPQLDALLLPAFFGAPPANAEIERRRDRQRELLAMFLAADLVVIASPVWNFNGPPQLKAFIDAIMVAGKTFKYTANGPIGLVPEKKVVVCYASGMLYDHGQPPQQTLTPMLTTQLGFMGITNVTLIGAQGQGAGREKAAATLAAAIEKAQAAAAQF | Cofactor: Binds 1 FMN per subunit.
Function: Also exhibits azoreductase activity. Catalyzes the reductive cleavage of the azo bond in aromatic azo compounds to the corresponding amines.
EC: 1.6.5.-
Catalytic Activity: 2 a quinone + H(+) + NADH = 2 a 1,4-benzosemiquinone + NAD(+)
Sequence Length: 203
Sequence Mass (Da):... |
A0A6V8P5D2 | MGKNLARTLSNLQKIVIKIGSSCITSPSGRLDRPQMARLAREISELKKRGHEIIIVSSGAIAAGVESLDLKKRPGEIPRLQAAAAVGQGLLMHMYSTLFSQQGIRVGQILLTQEDTTRRQQYINARNTISTLLKFGVIPIINENDSVAVEEIKFGDNDTLAALVSSLANADLLIILSDIEGLCSTDPYLCDHPEIISEVEEISPEIEEIAGGAGSGRSRGGMVTKIQAARIATFSSIGVIIADGRKEGILQEILAGKEVGTYFKPRKEKVASLKRWIAFGRQCKGKIIIDAGAVKAIREDGRSLLPVGILQVEGEFESGD... | Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 1/2.
Function: Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate.
Catalytic Activity: ATP + L-glutamate = ADP + L-glutamyl 5-phosphate
EC: 2.7.2.11
Subcellular Location: Cyt... |
D4YME3 | MVDKLGFMSTPDRKQGQPETTSATHKDSTPAAAKRTRMQHVPNALTVLRIVMVPVFAVLLLMHGGQDPTLRWWALAIFLLAMLTDKLDGDIARKYDIVSDFGKLADPIADKALMAAAFIGLAIVGALPWWVPVVILVREIGITVMRMFMLKYEVMPASRGGKIKTVLQTATVALYIAALPLAVVTSAGFMFAYAIFAGFALTLTILVTVITGVDYVVQAQKIKKEAGQGKVAGANPTTASGEAPNDR | Pathway: Lipid metabolism; phospholipid metabolism.
Subcellular Location: Membrane
Sequence Length: 247
Sequence Mass (Da): 26557
Location Topology: Multi-pass membrane protein
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A0A192II12 | MKAPHFWAPGGAALPRLALRPLTLPWRAAAWLRRATANPHDPGVPVICVGNLVMGGAGKTPTVRMLADWFRAHGLRPGVLSRGYGGGLSRRGATLVDASRHSAAEVGDEALLHAAHGPTVVAADRRRGAELLARHADVIVMDDGHQNPALVKALSIIVVDTAYGFGNGAVFPAGPLRESVATGLGRANAVIAIGGGSIGERLQRGPLPVLRGDLIPDRAAEVLAGRKVYAFCGIARPGKFRDTLRGIGAEIAGHRDFPDHHPFRKTEIEAVLKAAAAEKATPVTTAKDAVRLPPDQRAKVTVVEVALRLDQPESLEALLS... | Pathway: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 6/6.
Function: Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form te... |
A0A059A9Y4 | MASHGEDHGRHANPAAAAKANSTTTKFAKNGHVTKFGPSDGPESATSPPPPEILRQSTALPRKSPPIRRPLSSSSSSALLLPARSNGDRNLEARDRDLEGAHAVAGGGGGGVFGGGAPPPRPVPRERGRGAAVEPKAKPTTSLKTFSIYRWTPDSPSKPKLKDYQIDLKECGPMVLDALIKIKNEIDPSLTFRRSCREGICGSCAMNIDGCNGLACLTKIPDGADASTITPLPHMFVIKDLVVDMTNFYNQYKSIEPWLKRKNPPSEPGKEILQSKKDRAKLDGMYECILCACCSTSCPSYWWNPESYLGPAALLHANRW... | Cofactor: Binds 1 [2Fe-2S] cluster.
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; fumarate from succinate (eukaryal route): step 1/1.
Function: Iron-sulfur protein (IP) subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible ... |
A0A2B8J8E9 | MATILGIPFSEKNMAQTLTALNHHLDQKSFPFHVVTANPEVVMQAKRNRRFRMVVKQADMVTPDGIGIVIGSRILKENVPERVTGYDLIMNLLSLREEQQKKTRVFLLGAKEDVIPLAAEQLSSQYPHIDVVGYHHGYFEEESTEEDKIVKTIKESNSDLVLVGFGCPRQEMFISQYKEAIGAKLYIGCGGSLDVVAGEVKRAPEFIQKVYLEWAWRLVKQPSRWKRQLDIPRFLVEVVREKRKKQG | Pathway: Cell wall biogenesis; teichoic acid biosynthesis.
Function: Catalyzes the conversion of GlcNAc-PP-undecaprenol into ManNAc-GlcNAc-PP-undecaprenol, the first committed lipid intermediate in the de novo synthesis of teichoic acid.
EC: 2.4.1.187
Catalytic Activity: N-acetyl-alpha-D-glucosaminyl-di-trans,octa-cis-... |
A0A517YW13 | MGIKVCKYGGTSLADAKQILKVKSIIDADIDRKFVVPSAPGKRHSEDQKVTDLLYLCHEHAKQGLPFKEVFGLIRNRFEEIIKDLGLDLDFTAALDQVQVGIAKYADRGPDYAASRGEFLNGQIIAALLGYTFIDAAEVIFFNEKGRLDAAKTYHSVAARTEGVDRAVIPGFYGTDQDGFVKTFSRGGSDVTGAIIARGVNADVYENWTDVSGILAADPRIVEHPKTIESLTYRELRELSYMGASVLHDEAVFPVREAGIPVNIRNTNRPSDDGTLIVSTEKAPNTIGSVTGIAGRKDFTIIAIEKAMMNAEIGFGRKML... | Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 1/4.
EC: 2.7.2.4
Catalytic Activity: ATP + L-aspartate = 4-phospho-L-aspartate + ADP
Sequence Length: 441
Sequence Mass (Da): 47842
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A0A2I0M0H7 | MEVRKQTKQVENSQTTCHLFLKYQVCFILARKFTDKHEWVSVENGIGTVGISNFAQEALGDVVYCSLPEIGTKLSKHDEFGALESVKAASELYSPLSGEVTDVNAALADNPGLVNKSCYQDGWLIKMTVENPADLDELMNEDAYEKYIKSIED | Cofactor: Binds 1 lipoyl cofactor covalently.
Function: The H protein shuttles the methylamine group of glycine from the P protein to the T protein.
Subcellular Location: Mitochondrion
Sequence Length: 153
Sequence Mass (Da): 17058
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A0A2G9MS03 | MYMKLKLYIFRHGQTFYNKSHVFTGWKDSKLTSQGYKDARKVALKLKNKRIDVAYHTHLSRSKATLKEVLKYHPECKQVIEDDRHIERSYGIYQGKHHSSIIDEEGIDSYKTLLQWHKIDHLSGKERKEFVQKLGEAELQVIRRSYSVAPPKGESVKMVGIRVLPFIKDVLKKMRKEKVNVAISSHGNAMRPLRKYFEKLSIKQMMELENPWDNYFEYTIEVKDEKKKPERTKK | Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.
Function: Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
EC: 5.4.2.11
Catalytic Activity: (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate
Sequence Length: 234
Sequence Mass (Da): 27787
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A0A1I8FAU2 | LRFPSAIGKCHASEQVHRPAVPTRQLVVWSLFYGRCITAGIRSNILPNDTVNRWKEELNNIYWLPQSDSNISPCSYRTCNSVWSLLIYIFVLSGLLSGSLVAGGSNLSCAWPGHAMLVSCACLCSSATALLWWVFADQKEPAGWPRRLCKLIRSPVAGSEPFQIPKFAGLIYYFDIAAYPMLPQQLLTAANFPCLDLELKRGTHSWCCQSAEHSAAACSCCSALCVLVCSKEPRYVALYSFKRAVRWSVPQPDALPANCHLPVARQPVRSLAVDSGLHSTSRSASQRARMIPSITMNNSLIRSLLEPCLAIWTAAVIGCP... | Function: Choline transporter.
Subcellular Location: Cell membrane
Sequence Length: 600
Sequence Mass (Da): 65547
Location Topology: Multi-pass membrane protein
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A0A2I0M2U8 | MGVSTVTAARILKGQLQNRKGEESLLEMDKFPYVALAKTYNTNAQVPDSAGTATAYLCGVKANEGTVGVSAGVTRDRCNTTKGQEVTSILRWAKDSGKAVGIVTTTRVTHATPSAAYAHSANRDWYSDGEMPPDALEGGCKDIARQLVENIPDIEVGGGQGHQEQGDGEVTTRLSAGRQVRVAPAGGARSAVLTSSWVSSSRVTWCTSWTGITRRTRPSPRWWLWPSGCSRKIPAGFSSWLKGAASTTGTTRGRRSRRCTRRWSWTGPSGWPPVSPPRRTRSASSPPTTHTSSPSVATPPVGTPSLVWPPCRATLTASPS... | Cofactor: Binds 1 Mg(2+) ion.
Catalytic Activity: a phosphate monoester + H2O = an alcohol + phosphate
EC: 3.1.3.1
Subcellular Location: Cell membrane
Sequence Length: 413
Sequence Mass (Da): 44496
Location Topology: Lipid-anchor
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A0A0N5ASI5 | MACSGGNPENVGICAMEMYFPSQYVDQTELEQFDNVSAGRYTVGLGLKEMAFCSVDEDVTSVCLTVVSALLKNYEIDKKSIGYIAVGSETLTDKSKGVFTALRSLFGENDEIFGSECIGACYAGTSALFNAVDWIYFYNLLGKYAIVVMADIAIYASGPARCTGGAGGFAALVGPDAAIAFDLGLRSAVLRDVWDFYKPVCGVSSEYAVVDGKLSLETYLSMLDVAYLRYRKRTSEQTSIASFDAVMLHCPFSKLVRKAFGRLVFADYLKGFKKDVINPESMDSMKNLNLENTYTDRQFVAVTVACSENLWQKKTNPNLH... | Pathway: Metabolic intermediate biosynthesis; (R)-mevalonate biosynthesis; (R)-mevalonate from acetyl-CoA: step 2/3.
Function: Catalyzes the condensation of acetyl-CoA with acetoacetyl-CoA to form HMG-CoA.
EC: 2.3.3.10
Catalytic Activity: acetoacetyl-CoA + acetyl-CoA + H2O = (3S)-hydroxy-3-methylglutaryl-CoA + CoA + H(... |
A0A955HWR4 | MSVFQAILLGAVQGITEFLPISSTGHLLIAQRLLGFSQSLMSFDIALHFASLLAIVYYFRSTLLSLRLKDIRLLVIGTVPVVIVGLLVKDLVEQLSLITWYIAIELIITGSINIMIDRLLVKQQENPASISPLSSRSAWWTGVGQVFGISPAISRSGSTVLAALSQGIERTEAFRFAFLLAIPSLLGATMLELFDGVRDPTALSNISLPVLGAGMITSFLVGLGSLRVFEYVMQSAKLRYFGYYCIVLGVLLFVGSVGGSGLVAKL | Function: Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
Catalytic Activity: di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate
EC: 3.6.1.27
Subcellular Location: Cell membrane
Sequence Length: 266
Sequence... |
A0A840IL10 | MSARAAGGAGGGAKDGAHRERGAGGGAAAGGAGGGADDAAHRERGAAGGAAERGRFVVIEGLDGAGTTTQAERLAAALRERRGLAVELTKEPTNGPVGAVLRQAIEGRVTLDPVSLALAFAADRADHLFNPVNGVVAALEAGRWVVSDRYVLSSLAYNRGGATSREWLAELNRHAIAPDLTIFVAVDPDVCVSRIGARSSAEELFHSREQLVAVDRNYRELIDAGHVRGPLATVDGSGAIAEVEAAIWTAVERLQG | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
EC: 2.7.4.9
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Length: 256
Sequence Mass (Da): 26256
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A0A953W8T6 | EIKKASPSKGLIRADFDPPALARAYRDGGAACLSVLTDSPSFQGAPQFLRDARVAAALPILRKDFMIDPYQVAEARAWGADCILLIMACLSDDHARELMRAAERWDLDVLVEVHDEAEMARAAALGATLIGVNNRNLKTFETSLETTERLALLAPETALLVSESGISTHEDLVRLAGFGARAFLVGERLMRQNDVAAATRNLLAPVQNA | 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: 209
Sequence Mass (Da): 22611
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A0A1I8JE38 | CAISYNKMKVVGLVSGGKDSCYNMIECVRSGHQIVALAHLYPPSGAEMDSFMYQTVGSEAVALYAKATGLPLYTRPIVGESRDTGSADHYASSSNSGDSEDEVEDLYKLLAEVKAGIPGLQAVSVGAILSNYQRVRVESVCERLDLQVLAFLWRRDQTELLDEMLFSGLDAILIKVAAYGLSPKRHLGRRLVDIRDELVRLAAPAAGGLSPCGEGGEYETLALDCPLFKHGRIVLDNGHLTAAGTDSRVVVHSDDAFAPVCYLKLTGCCRLGEPK | Pathway: Protein modification; peptidyl-diphthamide biosynthesis.
EC: 6.3.1.14
Catalytic Activity: ATP + diphthine-[translation elongation factor 2] + NH4(+) = AMP + diphosphate + diphthamide-[translation elongation factor 2] + H(+)
Sequence Length: 275
Sequence Mass (Da): 29612
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A0A3C0QR92 | MNQNNINANWDLTPIYPDVSAWEQAFQKAEQMVKDFPPLLETMIDSAENLYHACETFTLLYADVEQIYTYAHLRYSENTKDNESRQLMGKAQNLFASLSSASAPFSTTILKLSETQFNDYLKEFPALETEYGIYLRNIFRYKSHILTEAEEKLIASFSKQMGTAEDTYETLTTSDMKFENITDEDGNSVELTNTNYSLHMRSQKREVRQSAFKTLYKGFNQFRNTFASLYAGQIEVEKVSAKVKHYDSALQASLFPDYVTPEIYQNIIDNISGHLDVLFRYYSLKKEVLGVDELHIYDIYQPLIKEYDKKFTYDEAVETV... | Cofactor: Binds 1 zinc ion.
Function: Has oligopeptidase activity and degrades a variety of small bioactive peptides.
EC: 3.4.24.-
Sequence Length: 595
Sequence Mass (Da): 68746
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D4YP78 | MEDTAEEQHEPKKSKKAKKDSRTATQKFLASLREIAIIVVIALIVSTALKAWVVRSFYIPSASMEDTLQIDDRIMVNQLPFAHPKRGSIVVFNDPGGWLPPGTAEEYKPNPFLEFVGLAPSNAGQQLIKRVIGVGGDHVECCDDQGRIMVNGVAIDETYIKPGAPPSEVEFSVDVPQGHYWVMGDNRSNSADSRFNGDSEGGPFVPEDEVVGTVFVISWPTNRFSWVTAPDTFDKVPDPS | 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: 240
Sequence Mass (Da): 26361
Location Topology: Single-pass type II membrane protein
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A0A2P7AQ27 | MERSTIVRVHDGLHARPATRFVKLAKSFESDIELIKADKSVSAKSSVKLMLLGVKENEEITVRATGADAIEAIEALIGYLENPRSGTEEEGASSVETKSAEPTSKPQTALYSNETKAAGNMRGVAASEGVAIGPAFGFFPAEIKHENRLLGAGEISSEIARLKQAFAMVQQRMDKSLATNNLAESDRGIIAALKDIACDDELTGSARELVHGGIDAVSAVIGATSRIAADFASMDDPYLVARADDVNAVGRQICLALLGQDDANLDAVPAGAILIAEDIGAWDLARAPLRRIAGVICGHGGATSHVAIIARAHGIPAVLG... | 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... |
A0A2A8TDV0 | MEVRETKVVIEDNLTIKDLVAVARHNASLELSEKRKKCIIQARKLVERFVEENQVIYGITTGVGENSKVRISTTESKEMQKKLIMSHACGVGEPLKPEQVRAIMVMMIQNFSQGYSGIRLETVEALIKLLNKGVTPIVPKEGSLGYLNHQAHISLVLLGMGEAKYKGIVMSGKEVLQSIGISELELHEKEGLSLINGTVDMTGIGALAIYDAMNLLKSADIISMMSFEALRGTYYAFDPRISQVKLHPGQQKTTSNIHKIINGSKIAETFKEYRTQDALSIRSIPQVHGACKDAMNYAKEVVEREMNSATDNPLIFHEGE... | Pathway: Amino-acid degradation; L-histidine degradation into L-glutamate; N-formimidoyl-L-glutamate from L-histidine: step 1/3.
EC: 4.3.1.3
Catalytic Activity: L-histidine = NH4(+) + trans-urocanate
Sequence Length: 511
Sequence Mass (Da): 55994
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A0A2A4VP38 | MYWYDITTQEGGMKYFNRAMKTVSAVAVTVMVLTGTAVYGAAAAGSNTTAMVGKKSSDYLPIKRIQPQYPKRAIDEGVSGYVILELTVAADGSVVPGSIKIIKAEPKLYFEKASMAAAKLFNYVPKIVDGNPVVVPGVRYKFSFSLKPKT | 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... |
A0A9E0K9T7 | AVHGHETAPERCRECYALRLGRTAQQARAAGCAVFTSTLVTSRHQDHELIRAAGEAAGAAASVEFLYLDARAAEADPRLVHMLYHQQYCGCVFSEYDRYKGTTAHLWPPPPAPTQTNPA | Pathway: tRNA modification; tRNA-queuosine biosynthesis.
Function: Catalyzes the conversion of epoxyqueuosine (oQ) to queuosine (Q), which is a hypermodified base found in the wobble positions of tRNA(Asp), tRNA(Asn), tRNA(His) and tRNA(Tyr).
EC: 1.17.99.6
Catalytic Activity: AH2 + epoxyqueuosine(34) in tRNA = A + H2O ... |
A0A3C0IHW3 | MYPVFLQLKQVPCLVVGAGAVAQRRIFSLLEQEANVTVLAPEPIPLPLQHQSLRYIQAVYATSFLKDRKLVFVATNDIQLNQTIVREAQERGILVSSVTDGITTDFSVPAHTTTGNLTAAISTNGGSPSLAAAICKEVTPILSTYEPLCSLQVQIREEWKEWIFDARKRKQLLSSLSTPEALACYREQGTAAY | 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: 193
Sequence Mass (Da): 21235
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A0A3C1H0V8 | QAGMNVARFNFSHANYEKDRKRFEQVVRLREELGLPVATMLDTKGPEVRLRTFPDGPATVADGAVYTLTTRDVPCDAQTGSVNYPRLTKDVKPGDTVMINDGLVEMRIEHVTATDIECRVIHGGVLTDHKSCNFPDVHLSMPYLSDADMEDLEFGAKLGFDFIAASFARTGADIRYLRKFTQSLGWYGVRIIAKIENREGVNNIDEILEAADGIMVARGDMGVEIPFEQIPDIQKKLIRKGYEAGKQVITATQMLESMMTNPRPTRAEITDVANAIYDGTSAVMTSGETAAGQHPVETVRTMARIALTTEASIDYKSEFM... | Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5.
EC: 2.7.1.40
Catalytic Activity: ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate
Sequence Length: 447
Sequence Mass (Da): 48804
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A0A3S2Y0R9 | MAADQNAGGGGGGGAGSDEPETLGGAWAAKLSQHPGAVQDIGVDLTAVLGTAEMKVSNLLKIGRGAVIELDRRVGDTVDIRVSGQAIARGEVVVVEDHLAVSITDLVKKT | Function: FliN is one of three proteins (FliG, FliN, FliM) that form the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation.
... |
I6LZD3 | MRLKGRCMKIDHIIIEYRNQVPFNATGSVIVEIRDNRVSLEDAAQAAFTFPIACNVDLHYFSSTYFSISEPSPWKIMYRVEDSNVIEGVKFASIKAKLRLSSAKHSTDIRFKPPTINILSKGYTKDCIDFWSVEKGEIRRRLLNPTPTAHTPRPITHRPITILPGETWATKSQIGLPSSSGPARLEHFRSQSMRMDPSTTPTDLDNDSTDYPYQKLHRLHTPELDPGDSVSQAPSDSISRKDLETLLESTINKCLIKIKSDAPRQL | Function: Movement protein involved in the cell-to-cell and systemic transport of viral genomic DNA. Begomoviruses use 2 proteins to transport their DNA from cell to cell. The nuclear shuttle protein (NSP) shuttles it between nucleus and cytoplasm and the movement protein (MP) probably transports the DNA-NSP complex to... |
A0A951SXZ9 | MAGLKIIKKRISSVVNIRKITKTMELVSAAKSRKMMVKVHDSLPYGNKVIELLNTISGITGDVELPLLRTEETPKKIILLVITANRGLCGGYNAQLLKLARLRIKELQSQQIPFDLHVIGKKGISYFKFIKVPVAKSWTHFDDGFVYLDAKTLATEYIQDFVNESYDQLELISTRYISAVVQRAENFTIFPMTQAGAADDATTKTANFIFEPSPDEILKTLLPHVAEYLFYKTVLEAITSEQIARRIAMKAASDAANDMNKSLTRIYNRKRQAAITQELAEIIAGADAIK | 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: 290
Sequence Mass (Da): 32471
Location Topology: Per... |
A0A5B8XDZ2 | MDFEDIAKHIKGLVRISSVISARMRLVPNGAGKFKANCPFHKEKTASFHVDDERGIYKCFGCGKGGDVINFIKDYDNISDFRTALESIAQISGIELPKSSFATKEYSMQKRVFEINEFILQFFKNSLKNSRICMDYIQKERKISDNYIDLFSLGYAPDSYSLLIDEMVKNGFSADEIISSGAVKQSNGQMYTIFRNRFIIPIFDASNRCVGFGGRSLTKDAMPKYINSFESVIFKKGMSLYNLANAKQISVNLKENFVILAEGYMDVIALCMGGFPAIAPLGTAVTDAQISLLRRYFSSVYVWLDADTAGQNAAFKTAKI... | Cofactor: Binds 1 zinc ion per monomer.
Function: RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.
EC: 2.7.7.101
Catalytic Activity: ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.
Sequence Length: 560
Domain: Contains an N-termi... |
A0A0A7LCG9 | MKGSRALLKMLEDKGVETMFGYPGGVVIPIYDEILDSSIRHVLVRHEQCAAHMADGFARASGFPGVCMATSGPGATNLVTGVATAYADSSPMIALTGQVGTASLGLDAFQEVDAYSLMMPITKHNFRVLELNRLPHAVLEAWDICQTGRPGPVHIDFPADQINANIDEALLNETFGIKVPKEDYSGIDQAVQWIKEAQRPVMMVGGGVISANASAELIKLAEMTNIPVITPLMGIGAIPTSHPLCLGSLGMHGRMCSLHAFRDADLIIAIGTKFSDRTYSAQTAPAKSCRIIQIDIDPTVFNKHGRERINIAGDAKKAMR... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 1/4.
EC: 2.2.1.6
Catalytic Activity: H(+) + 2 pyruvate = (2S)-2-acetolactate + CO2
Sequence Length: 559
Sequence Mass (Da): 61111
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A0A951Y1X6 | MRTARSARRATSFRRARQRVSPQEGRRGDFVSEPVSPPLRAGIIALIGRANVGKSSLLNAILGEKVSIVSPIAQTTRNVVRGIHTEARGQLVFHDTPGIHKAVGDLGRVMNRMARSAAVGADVAMLVLDASQPPREEDCGWMKRLHREATPLVIAVNKMDVAGASAEPFRAAWEAERPADAVERPAPIWCEVSAATGQGLEALTAILFEQVPEGPLLFPDDILSDFPRKLAIADVIREKLFGVLREELPHAIAVWVEQLDEEADPWQVTATIFVQKHSQKGIVIGEKGRLLRKVRREAEAELATWFDKPIKVELWVKVEA... | Function: An essential GTPase that binds both GDP and GTP, with rapid nucleotide exchange. Plays a role in 16S rRNA processing and 30S ribosomal subunit biogenesis and possibly also in cell cycle regulation and energy metabolism.
Subcellular Location: Cytoplasm
Sequence Length: 336
Sequence Mass (Da): 37327
Location To... |
Q5NE61 | MIKKIIYSLSILSCSLGFSADSDTKYEKAIFAGGGFWCLESDFEYMQKHQDLSHNGIIKVISGYDGGLQKDPTYKTVSAGITNYKESVEVIYDPTKISYQELVEYFYRRIDPTDFKGQFCDKGKQYQSAIYYNNDKQKQVAEEVTKKLKEEFKKHNQSVYTQILPSTHFYKAESYHQDYHHKNPKRYCYYRTGCGRDLTINKVWQNIDWKYSNVVPFDIPSSYAECLIR | Function: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.
EC: 1.8.4.11
Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionine = [thioredoxin]-dithiol + L-methionin... |
A0A833D245 | MSPTDVIDISREAIVVILKIGAPVMLVALVVGLVISFFQALTQIQEMTISFIPKMIATFGIIFFLMPYMSQVMTRYTHDVFNLIAHQSG | Function: Role in flagellar biosynthesis.
Subcellular Location: Cell membrane
Sequence Length: 89
Sequence Mass (Da): 9921
Location Topology: Multi-pass membrane protein
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A0A5B8XFN6 | MLNDENEIPENEIMQGDYGADSIKVLKGLDAVRKRPGMYIGDTDDGTGLHHMVYEVLDNAIDESLAGHCTKINVCINENGSVTVRDNGRGIPTQMHEEGVSTAEVVMTQLHAGGKFDKNSYKVSGGLHGVGVSVVNALSSHLKLRIWRDGKEHVMEFSHGVADYPLKIVGDSDQKGTEVTFMPSTETFSDIEFKFETLEERIRELAFLNHGVFIILEDKRLGREKLIEFKYDGGVAEFVKHLARAKTALHQIVSIRGAENDIVVEVSMQWTDAYTETCRCFTNNIPQRDGGTHLAGFRGGLTRAINQYIPQHLSKKDEVE... | Cofactor: Binds two Mg(2+) per subunit. The magnesium ions form salt bridges with both the protein and the DNA. Can also accept other divalent metal cations, such as Mn(2+) or Ca(2+).
Function: A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modu... |
A0A960QN76 | MNVQVESSGPCRRHLRIEIPADRVKAELNQVMDAYLQHAKIPGFRPGKAPRKMVEKRYEKQIHKEIKERLVPEAYQGAVKENQLRTVAVIDVDDPALTTEAPFVFNVVVDVQPEFDMPSYQSLTIKAQPVEVGDAQVEEVLTSIRSRNAKFEDAPEGAVVASGDLVSIDTDATAGGQPLADTVPELKDLVAGKDFWLFADDEQFLLKELSQGLVGLTQGAQTEMEVPFPETFPNEKVKGITGTFKVTVKGIRKKVLPEIDDAFIKELQAESLDDLNRRIREDLTRMKEDQEKQRQKNDAVRQLLDAVKMDLPESVVQEET... | Function: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
EC: 5.2.1.8
Subcellular Location: Cytoplasm
... |
A0A517YQP0 | MRVKLPQLMLGAAITAALSGQAMAQDGSAALPMPYYLAPAGAVLALIMAFFFYKGFMAQDEGDENMVRIAQAVRDGAYAYLKRQAKVVYAVVAVLVVILVVMGLAGLQSELTWAGVAIASLFSGLCGYLGMKTATNASARTACAAKNSLNDGLKVAFRAGAVMGMCVTGFALLDISIWFVVLTKIFGMATETLTEITTITLSFAMGASLQALFARVGGGIYTKAADVGADLVGKVEAGIPEDDARNPATIADNVGDNVGDVAGMGADLYESYYGSILAAMALAAAAAYSLGLESTDAIKLVIAPAALAGLGIITSIFSIF... | Function: Sodium pump that utilizes the energy of pyrophosphate hydrolysis as the driving force for Na(+) movement across the membrane.
Catalytic Activity: diphosphate + H2O + Na(+)(in) = H(+) + Na(+)(out) + 2 phosphate
EC: 7.2.3.1
Subcellular Location: Cell membrane
Sequence Length: 855
Sequence Mass (Da): 88935
Locat... |
Q5NGC9 | MKIITNLNKTKDFLPKAIAIGSFDGVHLGHQAIIKKLLTIAKENNLVPYILFFEPLPKEFFLKDKAPFRIYDFRNKVINIHKLGIKHIICQKFNTKFANITANEFIEEFLVKKLNTKHIIVGDDFKFGKNRGGDYALLNQYSQTHDFNVDKVSTLNLDNHRISSSDIRQALTNHDLIEANKLLGESLKINSRVIHGQKNGRKIGFNTANQKLPKNSALKGVYLTRVFIDDVIFYGVANAGTRPTIDGKNNLLETHIFNFNQEIYGKHITTEIVSFIRIEMKFNSFEELKLQISKDIQTAKKLISTL | Pathway: Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step 1/1.
Function: Catalyzes the phosphorylation of riboflavin to FMN followed by the adenylation of FMN to FAD.
Catalytic Activity: ATP + FMN + H(+) = diphosphate + FAD
Sequence Length: 306
Sequence Mass (Da): 35018
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A0A4Q9KE96 | MSTYRQRLKEVVAARGNLCVGIDPHANLLSSWGMPLTASGLETYCRTIVDALGETVAVFKPQAAFFEVYGSAGMAVLERVLADIRAAGALSIVDAKRGDIGSTMEAYAEAYLGKDSPLAGDAVTLSPYLGFGSLMPAFERAVAFDKGVYVLARTSNPEGGQVQLALGRGGSVAQEVVDAAKELNTRARTRAIGLVVGGTHGSLGIDVSDFNGSILVPGIGAQGGRMEDLPGLFGAAFDNVLPMVGRGILQAGPDAEALRRRVSTFLAE | 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: 268
Sequence Mass (Da): 27878
|
E1UIW4 | IAALAMVHLLFLHETGFNNPTGIPSNADKIPFHPYYTIKDILGILLLILSLMLLVLFAPDLLGD | Function: Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membra... |
V6DI02 | MVTIKRKSDFEPLYYEKKAWAENKLICGLDEVGRSCLAGPVVAAAAILNPYVEHQYLKDSKELTPEQRFKVYQWLLKNSIFSVGIIHHRLIDQVNIHNATLYAMKRALFQLLASCPNSPDLILVDHMPLILDTVDIPVLHFSYGERLSSSIAAASIIAKVTRDSLMCRVDGFLPGYKLSNNKGYGTKAHKAAIDSDGLVVYHRNSFVSKFYLNSHN | 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... |
A0A267GEZ7 | MEATNELNESTNEVYETGLSRSRQKLEKSKLNVGDTDSVSKSEEERCHFAKLIENHKVDNITIEFFYKPHTLSLLFCIICGLIYLALGRTDTTLKEDVWHGSIAVCTVFLIISILVMPNGPFIRPHPAIWRVVFGISVLYFLVMVFVCFLSYEDARRALVWMYPDLANMTYDDILDKEYAANCSEITLSRLYSHLDVFAVAHLFGWVMKAVLLRHYGLTWLLSINWEITEMAFSHILPNFQECWWDIVILDVFVCNGVGIFIGMQLCRWLEMRSYHWESIRSLSSTSAKIKRAFFQFTPGSWTPTRWLDPESSFMRVIGV... | Pathway: Lipid metabolism.
Function: Catalyzes a base-exchange reaction in which the polar head group of phosphatidylethanolamine (PE) is replaced by L-serine.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + L-serine = a 1,2-diacyl-sn-glycero-3-phospho-L-serine + ethanolamine
EC: 2.7.8.29
Subcellula... |
A0A481P7V7 | MKLGVFYVVSVFFGLVVGYRLFVLRLGYGSIWPHRFGRPGSLKALKLYEFHSYLVSLMLVVVVGVFLLVFFLWGLSGLSRRWGFLEHDRIETFWTVWPLFLLLLVVLPSLTLLYVLEESVSRVWSTVHVVGRMWYWEYGYLKGSGGYEFFESRLLKEGDVYRPRWEVDNACMMAVGKYFRFLVTSGDVIHSFSLPRLGVKVDCVPGRVNQVYMSPLFVGVYRGQCSELCGAGHSQMPIECRVLPVSSYLLWNK | Cofactor: Binds a copper A center.
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-cytochrome c oxidoreducta... |
A0A267EY66 | MSMLMKFTGLLGLLLLVQLPGGKSAPTDWDYVSNDPSEWPSAFKKWCGGRAQSPIKLIYSEARYDTDLPPYSIVEDNTPGRKFKVYNDGHKVSIFFSSAMMNVTVPGHPNSCFRPHSIHWHWGADDSHGSEHWMEGRHYPLEGHVVMWNCQFYSKFEDAANSFSGLAVLGILYEPDSSVTTYSRPLANMISLVASDPRLQRCAGCANETFEPPKVDMDAFPLGDLVPADRSQYYLYGGSLTTPDCRQNVMWTVYRQAQRVPPSVLATLRSLKYPDGSAMISNFRPPVPLNPTSPFGARRIVVRSFNSGSTPGLPRGASWL... | Function: Reversible hydration of carbon dioxide.
EC: 4.2.1.1
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Length: 344
Sequence Mass (Da): 38079
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A0A2R4MIR3 | MPLLIKICGLKTPELVDVAIEAGADVIGFVHFARSPRHLDFSDIGKLIRHVDGRVKTAILTVNPDEDLLEHAVSLSPDYIQLHGQETVERVEHIQQMGVDVIKAFSIGAEEDLAPVPAFAGKADLIILDAKPPKDAAHPGGNGEVFDWSILKALDPGIKFMLSGGLTIENVQQAVNEVRPFGLDVSSGVEVRKGEKDADMIKEFMRRARDYHRSTTREIE | Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5.
EC: 5.3.1.24
Catalytic Activity: N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Sequence Length: 220
Sequence Mass (Da): 24150
|
W6LCL4 | MNSKFDPLFQERIVSLDSSSIPHGESTAIESGAWDAAQMAKLSNGTSSVPLPGATGSLDVPSAPADTQLKWDDICESAGSTTDTQKPSPADFQGSPYTTRLTTPPTNDIKKQSINPVLKALQEQIAKRTMLIDAATKEKMTKIIAASKEYIEEQKSKRERQIAEAKELHKKTQDDDEKNNEDLKKSDAVWTGVGKVVDLQKPNPYSKNTERMRSILSTLNQPDKVISK | Function: Clathrin is the major protein of the polyhedral coat of coated pits and vesicles.
Subcellular Location: Cytoplasmic vesicle membrane
Sequence Length: 228
Sequence Mass (Da): 25045
Location Topology: Peripheral membrane protein
|
A0A0N5AND2 | MLKERRRAFLDITIDGRVIGRIVLELFNDVAPKTCQNFLMLCTGMAGIGKVSGKPLHYKGSTFHRVIKNFMIQGGDFTKGDGTGGESIYGGMFDDEEFVMKHDEPFMLSMANKGPNTNGSQFFITTTSTPHLNNVHVVFGKVVSGFEVVKEIEHLKTDSKYRPIADVVILNCGELVKKTKKRKKSNSDASSTLFRSTTPEKRRNNKVEKHKESKESSSKRSRRDNDFRQYSRPRLTRSGHKIKGRGALRFRSDRDRSRTPPHWRREQVKYYLHCIIKSSLCCL | 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: 283
Sequence Mass (Da): 32352
|
A0A267GH04 | MDSCAFKACLSCVAGGALGAFFGLFTASIDPMSTVVPGAETPSTRQVLREMGSRMVSYGKNFAVLGIMFASTECALEVVRAKTICSMALAPAPSLAACWDFAPV | Function: Essential core component of the TIM22 complex, a complex that mediates the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. In the TIM22 complex, it constitutes the voltage-activated and signal-gated channel. Forms a twin-pore translocase that uses the membrane ... |
A0A833QYB6 | MVGFDLDPELRLSLHTGYTESTSSSEKHATDTRDEICNGKASDDKRTVTIFYDGQMCTSNVTEIQGRAIISMAKREMEKGRSKELKERTNMYPLQFLSQFHSNSSQMLNQGLSMKQSLQRFLQKRRTRIASASPYSS | Function: Repressor of jasmonate responses.
Subcellular Location: Nucleus
Sequence Length: 137
Domain: The jas domain is required for interaction with COI1.
Sequence Mass (Da): 15611
|
A0A8J4FHI9 | GAELEGGKRANMDMGAERCTVKHPDRWKVSLRLDVYLGLHFLRNLVVSEVESVPLAPGGRSNPHCNGFKMVETELLSTSGAQRTHNFFTARFWSIKNPYSINPISKRPVSYRLLPAASPAMMSHPSSLVARRALFATKQLWVTPHSDSQRFPAGEHVVQSNRCMGLAEWTRKDLSLRGTDPVLWYSFGVTHAPRVEDFPVMPVEVCGFSLKPDGFFAGNPAVDLPPCRDQASTEQLPQQHNHQQQQAVQAGAGGSCCLLLSKL | PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue.
Cofactor: Contains 1 topaquinone per subunit.
EC: 1.4.3.-
Sequence Length: 263
Sequence Mass (Da): 29074
|
A0A1I8FJ12 | MGHLFDHIQPFGAWFFGISVLYFLVMVFVCFLSYEDARRALVWMYPDLANMTYDDILDKEYAANCSEITLSRLYSHLDVFAVAHLFGWSLVF | Pathway: Lipid metabolism.
Function: Catalyzes a base-exchange reaction in which the polar head group of phosphatidylethanolamine (PE) is replaced by L-serine.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + L-serine = a 1,2-diacyl-sn-glycero-3-phospho-L-serine + ethanolamine
EC: 2.7.8.29
Subcellula... |
A0A0L1JB97 | MKLSLLVTAVIAPFVSAHYFFDTLVIDGQESTPNKYVRSNTRPEKYNPTKWKNTRDDMTPDMPDFRCNKGSFTFAGQTGTAEVKAGTKLAMKLGVGATMKHPGPGLVYMSKAPGAANKYQATVTGSRSTRSLSVIRTRISKPMPGALGERTVSSSLFLWICRMASILFGPSTSVCVHGAHDGQAEFYYECAQVKVTGGGHGTPGPTIKFPGGYKKDDPSFNFSIWGGMKDYPMPGPAVWGGASGSKPASKVANVNGAGASHQEEPGTCGSHREHARDFSY | Function: Has endoglucanase activity on substrates containing beta-1,4 glycosidic bonds. Involved in the degradation of complex natural cellulosic substrates.
Catalytic Activity: Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
EC: 3.2.1.4
Subcellular Location: Secre... |
W6KWV4 | MQAWEQVVIAYEPVWAIGTGKVATPKQAQEVHHLVRGWLAANVSPGVAAAVRILYGGSVTAANALELYRQPDVNGFLVGGASLKADFLKIIDSTKD | Pathway: Carbohydrate biosynthesis; gluconeogenesis.
EC: 5.3.1.1
Catalytic Activity: D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate
Sequence Length: 96
Sequence Mass (Da): 10217
|
A0A7R9K9B2 | MVVRQYNEELKYLEKINAHSWRIKIGFQPNMNVEGIFYVNQNLEKLMLEELRNSCRPGTVGGFLPGVKQIANVAALPGIVGRSVGLPDVHSGYGFAIGNMAAFDMANPKSVVSPGGVGFDINCGVRLLRTNLREQDVLPVKTIVKTIEKESKKVDILDILCGLKEDHKEFAANSIKTMWIPVSNVDTECAFSAYSNGSTRAFPPHHPLIPVDYQLTGQPVLIGGTMGTCSYVLTGTEQGMHETFGSTCHGAGRALSRAKSRRNLDYQDVAHKAPSSVEKSGTKQIRFEKYCTS | 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: 293
Sequence Mass (Da): 32121
|
A0A1I8FSY4 | MQRLGIVMGMKTCNYLSLKPYILTSMWNIPGLQRFVLQFTPYRWTDFDWTPTKSFRRWVIMLMVIAMFLLAEVNTFYLKYVLWVPPPHFLCLGRLVFFLFMGATAMREVFQYLDDPKANKFGRQSWVISAIIITETLISVKFDPATVTKPLPRHVIIIWSVGFSLLSAWTVWNFFLKRFFYSLAVAKETASPKTKLLSLV | Pathway: Lipid metabolism.
Function: Catalyzes a base-exchange reaction in which the polar head group of phosphatidylethanolamine (PE) is replaced by L-serine.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + L-serine = a 1,2-diacyl-sn-glycero-3-phospho-L-serine + ethanolamine
EC: 2.7.8.29
Subcellula... |
A0A1I8FRX9 | ELHTAAVCLYPYQLAAAKSALDQIGASNRIRLACVATGFPSGQYGLESRLAEIRWAVEQGANEVDIVINRTLALQGRWSDVYEEACGPSVCLKTILGVGELAAYETVYKASLVCMYAGADFIKTSTGKESVNATLPLSLVMLRAISEFHARTGPASGNPGLRRNALDYLHLVQFALGPDWLQPNLLRIGASSLLGEIEKSAFRLLIGRDATAGDLPMA | Pathway: Carbohydrate degradation; 2-deoxy-D-ribose 1-phosphate degradation; D-glyceraldehyde 3-phosphate and acetaldehyde from 2-deoxy-alpha-D-ribose 1-phosphate: step 2/2.
EC: 4.1.2.4
Catalytic Activity: 2-deoxy-D-ribose 5-phosphate = acetaldehyde + D-glyceraldehyde 3-phosphate
Sequence Length: 218
Sequence Mass (Da)... |
A0A267EXL1 | MYPNYSLYGGQPQSQQQPPPAYEVGAVACGGGSGLDSLLAQLKRMDKEELQKLLDSDDKVAEMTSSSGELQQLGQAKQTAMAANRQTAELNFALGPRIEESRRRLAALSDEADAQRAILLETRSRLESLNSAASPDTLLTLLEAACMEADEQAESVAEALATGSLDMAGFVRQYSEARQLYHLRRAKVDWLAKETH | Function: Component of the ESCRT-I complex, a regulator of vesicular trafficking process. Required for the sorting of endocytic ubiquitinated cargos into multivesicular bodies. May be involved in cell growth and differentiation.
Subcellular Location: Late endosome membrane
Sequence Length: 196
Sequence Mass (Da): 21361... |
A0A1F5GG14 | MDFVKKNKFLLIYFLFFLIFNVLLYLFIQNFNQTIKFNNLNYKYNAHHYFQDERINGGPFNLLRALGQYDAQWYLKVANSGYPKDPENTNLSDKSEMGSLSYAFFPLYPLLLFLFNKVFANIETSAFILSNILLLVNFISLIYVVGKLFSKQIAYKAVFLLFTFPFAIFFRSYFTEGLQLFLLIWFSYFLVKKRWVKSAIFLSFLTITKGNVILLTILFFYTCFREVKPKSFFKKDMMALLAIVFAPFLLWIAFNYIYTGNPLYFYNIRSEWFKPSFPLLPLLWNFALLFYYPALPFHSFHLSMIDYLSVILILLLLFKS... | Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 396
Sequence Mass (Da): 47181
Location Topology: Multi-pass membrane protein
|
A0A0G1W5R7 | AYFLAWTTTPWTLPGNVALAVGKDIVYVEAKVGKDIFVLAKDKLSLISEPYEIVAEHKGSEMVGMAYEPLYPFLEGKSDKAFKVYIADFVNTEDGTGIVHTAVMYGQDDFELGTKVGLPKHHLVSPDGTFIKGTDWLEGRSVVDETLAVDILKDLQNKGLLFGKENHTHSYPFCWRCKTRLIYYARDSWYIKMSELRDKLVKENEKINWEPDYIKEGRFGEWLREVKDWAISRERYWGTPLPVWENADKSKRIIVDSLETLKKYAKKSGNEYFIMRHGQAESNARKVLDLSGDPDNHLTEEGKKEAGRVDGNKFDLVFSS... | Function: Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves ... |
A0A840I462 | MLIVCTCLSLGFLASLPFFGLRSDAARQLSGRLAGSARRIVLAAFVLACCATLLLALAMGIVVLLRSVFSISLVWLQELPLYLFGATFLLSGGAVLLADAHVRVDVLYSRWPPRRRALVDLCGLTLFVLPVCGLIVVAAGPYVAQSWADLERSPEPSGIHAVYLLKSLIPAFGVLVALAAFVRADGLARGLRR | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 193
Sequence Mass (Da): 20619
Location Topology: Multi-pass membrane protein
|
W2SEA9 | AARARLAAGPVARRGFTSTRVRPDQYNFTPYHYPEGPRSNLPFNTQTRFFAVRYWLFM | 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... |
A0A893DB41 | TLYFIFGTWSGMVGTSLSILIRAELGHAGSLIGDDQLYNVIVTAHAFVMIFFMVMPILIGGFGNWFFPLMLGASDMAFPRMNNMSFWLLPPSLTLLLSSSLVENGAGTG | 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... |
A0A850SNZ4 | MQAPEKTSVIVTRPAPDAAAFASLLAGRGMTAILSPVLRIDPIDISGEIGRGEALAFTSANAVRSYLQSGGAAGLRVYAVGEATAEAARAAGFGDVIAGASNADALSALIAAQAPERRERVLHVVGREETGDLVGRLRQAGVEARRVVGYAATPIETISREAAAALERGGAWVAHFSPRSARLFCAAASAAALDAAIAKTGAACLSAAVAEAAGPGWARKAVAVRPTAGALIDAIAAAR | 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... |
A0A1I8J037 | PLPRSDRSDRKLLAPHFFAELNTDLASYADAASSTMSDAGEGGRGGGRSRWRRLRMRLCRFCNSDAFVDWSVERLYRKYAFRLERAMLSRFLLTYVCLLLALTSIDYAFGHRFSYKAAVYVASASAFLFAAVFLHSRLMRPEHTSTGCALVLLLVSLIAATAFPVSWVSASTVQQQQIFTMADGLWQVAFAVFAVYCLLPGQLLATALYGSVLSLCYLACSAVLTRQQLVEPSRADSVARKHITESYWTSLIASSLVLLCANLGGACLQRFRDSLLRRSFLETKACIANQLQLEDETYKLERLVQSVVPSDLTDDMRADC... | Catalytic Activity: ATP = 3',5'-cyclic AMP + diphosphate
EC: 4.6.1.1
Subcellular Location: Membrane
Sequence Length: 472
Sequence Mass (Da): 52334
Location Topology: Multi-pass membrane protein
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A0A8J7FB87 | MLFDLKRKKDVVHVIGIMILLITPAILSYNSKTELQAIRESGSLKFVTRNTPSTYFLEKGDPAGFEYELAQAFASFIKVELEVVLAPTFSEIFTIIKNRDAHLAGANLTVTPQRLEQFAFAPPYLQTSSALIYRITQGRPAPKTLDDLKERTLVVPANSSHIEALLALKADNPDLTWTESPDSSTIDLLEQVHTRSIDFTVMDTVTYESHSSYFPGVNKSIPLTEPQPLAWMYSPHPDNSLKLALERFFQKPETEQLIERLKVKYLQRENRLNFFDTVTFRKQMEERFPLLEPYFHDAEAETGIDWQLLSAIAYQESHWN... | Function: Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates... |
A0A8J6BTY3 | MDDVLASRLLTAIHTIRYDSHMDDKTVEELVSCMEEAYVTVVRGPSSFIRKIGSSQSLPTVKRRRSKRKKFARNASSAHWIHVLLMLVIRIIAVFQLSYLDPDEFFQAGDPVVRPRDGLTWEWARGLRSILHPALIAPAGLALHPWGRILVARLIQLAVTLGSDLVFLRFRRLVGLGTIRFTILVTGNILALLYGCRTYANALEAALVLLSVSFFPLTSSVTSSHAFAAYSIAGVCCWIRPTSAVFFLALFLMSARPFFRHVALGLAAVPGVLLTCGGAEYLYYGRIVIPPLEFIKFNVLEGNAAFYGTNAPWYFLAVAA... | EC: 2.4.1.-
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 528
Sequence Mass (Da): 58449
Location Topology: Multi-pass membrane protein
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A0A655ZI97 | MRRLAQDGHEIVYVPCHRSHMDYLLLSYVLYHEGMVPPHIAAGINLNFFPAGXXXXXXXXXXXXXXRCATLFNDFP | Pathway: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 1/3.
EC: 2.3.1.15
Catalytic Activity: an acyl-CoA + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-phosphate + CoA
Sequence Length: 76
Sequence Mass (Da): 8675
|
A0A8J6E126 | MKFFDPKSEFVLSLDGFETVTDELLESQATAFLAKSALAMVEKIEAGEVVNTTAHPTESEDRAVDHYNHRMEASPVAGKSLADSIAQWNTIKTEIDAILDGKTTTPEGKRYTDVIFNGLGGSFLGPLMLVISQYGDEFNFESGLPVRIHFMSNTDPDTYHLLFNKLDVATTVMVSMSKSGSTAETKGATDAWTALVASTGLELGPHSMAVTTPGSMLDKFAQEHKFLGIYYMATETGGRTSIGTAIGMVPAAFARIDFADFLRGQGHMDAMTRRPEIKQNPAMLLAVAIHQMTLMQGSKNMIVLCYSDFLKEFAHYLQQL... | Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 2/4.
EC: 5.3.1.9
Catalytic Activity: alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate
Sequence Length: 536
Sequence Mass (Da): 58407
|
A0A401XI71 | MKTIKDLVDFLIHLEKKFTQSEIKMQELMLHPNYDVSAKNLAKYLVLRSHELRPIQNQLHHLGLSSLAASESHTHYQLLNVLKWLAPEYKGKACTLSDDVGREMISQRTRKLFGEKHADHNIPYLMVTIDERKAGDVKYFEKLLINGMNIARINFAHADELTVNQIVNTLQTAIINTGLPCKIHMDLAGPKLRTLIPNKKKKIELQLNDVIYLQATTTNENFPKKTILISETRVFETLQSGHRIYFDDGKFHGIVEEVKNQTAVIRIVKTPLNNAVLKQDKGINLPDTHLNTQSLTAEDIKNLKMIASYADLIGYSFVRK... | Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5.
EC: 2.7.1.40
Catalytic Activity: ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate
Sequence Length: 498
Sequence Mass (Da): 56817
|
A0A175W9K6 | MGIPHLRRHLERYAERSVIETCNAVLDGPALAYHVLSLCSRETRKASPFEQPSYDLLGRTAVAWLDRIERCGLSISAIYFDSYLPSTKRPERLQRLVKSTQQLIKYRSAWLAGVPKGDHHRASEARVDLFPNSWPGEKKAKPPPPPFLVPAVIDALKGSLNYGNLVKLVPGEADGFCARHIRLSAGLVLTSDSDLLIYDLGQDGGIVFFSDIDVDIERQKLTSPQYRPTNLCRRLSLKPDTGLAYLAFEISRDPYLTLEQAIERSKRAEAVSVSREEYTEFMEQYLFPEVAQDLETDLALTLDPRVSEITLRSLRASGTA... | Cofactor: Binds 2 Fe(2+) ions per subunit.
Pathway: Protein modification; eIF5A hypusination.
Function: Catalyzes the hydroxylation of the N(6)-(4-aminobutyl)-L-lysine intermediate to form hypusine, an essential post-translational modification only found in mature eIF-5A factor.
EC: 1.14.99.29
Subcellular Location: Cyt... |
A0A059B3I8 | MGSDVGEVVETSYPSSFKVHHALCAEFMKLVDKVSSMLPVIEAARPRCSAGIQALCLLHRAIEKAHLILQHCSESSKLYLALTGDAIVARCERSRNMLEQSLGQLQNMVPVVLAIEITKLLDDLRSATFILEPSEEDAGKAVHDLIRQGSSESGSTENSELKALQFAASKLFITSRKSILVERRSIKKLLDKVGESDTKKKILLYLSSILKKYGNSIASGQTQSVYLENEGTYLTANSPHNSVYTETAEVAEAPLPGHHEAQVDVSVDTIVPEEFKCPLSSRLMYEPVVIASGQTFERMWIQKWFDEGNTYCPKTKKKLA... | 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: 766
Sequence Mass (Da): 85618
|
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