ids
stringlengths 6
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stringlengths 16
1.02k
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stringlengths 117
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A0A3D4H9J5 | MPHLQEHQGESPIPEVAALFDEIRAANSPTPLIGKTVEELQDLLQTEAAVEQPNLIAKVEYGKLCMANSGPDTNGSQFFIVTNADGASWLDGKHTVFGKVIEGMDVALAIQEVETASDDKPVEDVKIIGVTIERI | 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: 135
Sequence Mass (Da): 14553
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A0A2D4LSP9 | MDATLFLEIREKMKSGLLIIRELNPESWPVDITLMPSLIELKSDKACRAFSLPPEVRIVPSTCRGLQYQPGEGLHMRLLVQADFGTKLAPAVGNGLTSKKSCTFFCQRCGESVINNRTFLRVLSLPFENWSDLVDEWCCHPNPFNDSLLHPQIDDCFLGHNYLLINSRTELSGTESGKLHSEDEWTTSSESVLVNIYKKI | Function: E3 ubiquitin-protein ligase which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and transfers it to substrates, generally promoting their degradation by the proteasome.
EC: 2.3.2.26
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: 200
Sequence Mass (Da): 22603
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A0A7V5BYU9 | MGRRIAEDAVGRLQAYGRWLVEEAIPAGGLGPREAARLWDRHLLDALSFAGAFRREPDGILDLGSGVGLPGIPLAILHSDVEVVLLDRSQRRVDLARRAVRLLGLGNVEVVAGELERTGLAASTVVARGVAAPARLLPRLLPRIAPGGLAVVGLSRARARPASPPPPPGTRLELVSVPPDVLDSGAWLLRMEVPRR | Function: Specifically methylates the N7 position of a guanine in 16S rRNA.
EC: 2.1.1.-
Subcellular Location: Cytoplasm
Sequence Length: 196
Sequence Mass (Da): 20837
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A0A220SZP1 | HPEVYILILPGFGLISHIVTMESGKQEAFGALGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGSAMTFSPSILWALGFIFLFTMGGLTGIVLANSSIDMVLHDTYYVVAHFHYV | Pathway: Energy metabolism; oxidative phosphorylation.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 141
Sequence Mass (Da): 15475
Location Topology: Multi-pass membrane protein
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A0A951MP75 | MTTNDMTGLVLAGGASRRMGADKALIDLDGRPLVEHVAERLATVCTDVLVAPGARRLPDLPWTQVDDRLPGAGPLAGILGGMAVTTTPLLAVVGVDMPACSPSVLVALAQRWSGEAAGVPVTGGRLQPLHAVYAVAALPRLAALFDDGERSPTSALQELEATLHEVTGPAPWAASLNTADDLARFRGQ | Function: Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor.
Catalytic Activity: GTP + H(+) + Mo-molybdopterin = diphosphate + Mo-molybdopterin guanine dinucleotide
EC: 2.7.7.77
Subcellular Location: Cytoplasm
Sequence Length: 188
Domain: The N-terminal domain determines nucleotide recognition and specific binding, while the C-terminal domain determines the specific binding to the target protein.
Sequence Mass (Da): 19386
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A0A0R0M345 | MCGIYGYSHKNITKSSKDIANILTTALQRMEYRGYDSAGVCMVCDENCLIVREKGRVEEVKNEVERVLTQSDDNSQFLKNNELSTSVAIAHTRWATHGPPCAKNSHPITSDKSNQFIVVHNGIITNHHQIRCFLKTQDISFETDTDTECASKLAYYIYKQNPTLAFSQIVRLVAICCDGAFAFVFVSTIFKNEMVAVRRHSPLILGIKMESDIGKNITISESNGLESVSGDVQDRLDSLVKQLKPEQSEPSIKSAEFFLASDTAAIVEHTRDVIFLKDNDLVLIKGDQLTYETVLSHDDIPSDPIREITHLDTKIESIMKGNFEHFMLKEIYEQSETVSNTMRGRLLEIGRIDEDVATIPTNISLPNDSIISEPVNNTMIEQGQPLEGLAGGFESSISNISANTSFNSALKKRIGMVTNNNMKKYQICLPELTPLLPILSHARRMLFISCGTSYHSSHAVQSLFEELTQLPVYLEIASDFIDRQPPVSSNDICFFISQSGETADSLQALNYCKNSGAYTVGLTNTQGSSISRLTDINLNIGCGPEIGVASTKAFTSQYLLLVMIALYISEHTSQSKTQSEKKRGRGRPKQIKSEISEDEKSRILAVENRRQQIMRELANIPEKISACLSLSDKIAEYAQSLVDSQNILLLGRGYQYSLCLEAALKIKELTYIHAEGIVMGELKHGPLALIDKDQKIIILAIQDKILEKTLNSISEVVTRNGLPFILCSNSLTTQLREHFPDCQLLPVPDTVDCLSGLLTVIPMQLLAYHLALAKGNDVDKPRNLAKSVTVE | Pathway: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; alpha-D-glucosamine 6-phosphate from D-fructose 6-phosphate: step 1/1.
Function: Involved in amino sugar synthesis (formation of chitin, supplies the amino sugars of asparagine-linked oligosaccharides of glycoproteins).
EC: 2.6.1.16
Catalytic Activity: D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate
Sequence Length: 791
Sequence Mass (Da): 87870
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A0A835A4R8 | MHPDPRETRSRFASSSAWPLHVTLSCMGSVDDKYITAHQPHSTKQRIKDRTSSSCPSRPINTRAHSPPIPASSHCQDTIRPRQGKAKQRSMAATPARWLLVAVAAVAVMAGSCVMAAAPRKPVDVPFQKNYVPTWASDHIHYVDGGREVQLFLDRTTGTGFQTRGSYLFGHFSMHIKLVAGDSAGTVTAFYVRLISLASSNSEHDEIDFEFLGNRTGQPYILQTNVFTGGKGDREQRIYLWFDPTKEYHSYSVLWNLYMIAFFVDDVPIRVFKNSTGDLGVRYPFSQPMKLYSSLWNADDWATRGGREKTDWANAPFVASYRGFHVDGCEASAEARYCATQGARWWDQPEFRDLDGAQYRKLKEVRDRYTIYNYCTDRDRYATMPPECARDRDV | PTM: Contains at least one intrachain disulfide bond essential for its enzymatic activity.
Function: Catalyzes xyloglucan endohydrolysis (XEH) and/or endotransglycosylation (XET). Cleaves and religates xyloglucan polymers, an essential constituent of the primary cell wall, and thereby participates in cell wall construction of growing tissues.
EC: 2.4.1.207
Subcellular Location: Secreted
Sequence Length: 394
Sequence Mass (Da): 44730
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A0A194AJK8 | MGERYYTTLRKQILTGMILVPVIPFLLIIGVGYYHFSTSIKENTIASMERIVRDHRDMVASFLRERRADLAFVLAEHGFQELQNPEILSTVFTHLQKESPTFVDLGIFDPQGVLVAYVGPYKLSGKVYKETTWFREVMNKGFFQSDVFLGFRNIPHFVIALSGNHEQQPWVIRATIDTYRFSEIVESIRIGRTGEAYIVNKSGIFQTQRRSGGRFLEHAGEQLHYPDRPNGIRTYVQKDHRDMTFLYATTWIIPHKWLLVVRQDKNDAFAALNKAAWMSLVIAVVSGMGMIFLAIVLSKRIEKRLRITDKEKASLQDQLIRATRLAELGEMAAGFAHEINNPLQVMESDHAYIALILEDMKQKGDFREGEDSQELEQALGQIKKQIRRCARITQSILRFGRQGKPEYKKIDLTTFMPEVVSMIAKKASVNGIELTSTLPEQPLTIHADPGHMQQVLLNLFNNAIYAIVERHGSEGGRLGITGTRTDEGLVEIRVQDNGGGISPENQKKIFSPFFTTKPVGKGTGLGLSVCFGLVENMGGTMEVSSQQGTGTTFTLRFPSR | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 560
Sequence Mass (Da): 63223
Location Topology: Multi-pass membrane protein
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A0A2M8HQ37 | MLNAELRQKLWSLVSKTHSNSSLIIRPDKKPSPIPLHHYFPGNIEQHFLELGSGWCEVILQLAEENVNTGFIAMERKWNRLRRGFELAEQKNLQNIFFSAINFQWFLTDIFPENSFDTIFLNFPDPWPKKKHHKNRSIDQNFLKSIYNILKPGGKFLFATDHFGYARWTIRHLRKFNRFEYTSQEYCFERPALPISSFEQEKMDEGKRIFYLERSKPWL | Pathway: tRNA modification; N(7)-methylguanine-tRNA biosynthesis.
Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
EC: 2.1.1.33
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
Sequence Length: 219
Sequence Mass (Da): 26275
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A0A2P5NB04 | MRERSFLFVKEPVWHANRAGLPQQLPSAARSWIYEAGSLTQRLRSFYGDSVKVKVLHQHYSKPFFSENRLLGLAPQTRQLVREVMLIAGNVPLILARTVIPDSTMMVAANTLSSLGDRPLGEVIFAYPDLARQQLDLCSVKPLSWTAKAGQLANIENKVLGRRTCYLIARQQPLLVSEFFLPGALALD | Pathway: Cofactor biosynthesis; ubiquinone biosynthesis.
Function: Removes the pyruvyl group from chorismate, with concomitant aromatization of the ring, to provide 4-hydroxybenzoate (4HB) for the ubiquinone pathway.
Catalytic Activity: chorismate = 4-hydroxybenzoate + pyruvate
EC: 4.1.3.40
Subcellular Location: Cytoplasm
Sequence Length: 188
Sequence Mass (Da): 21061
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U4LMA3 | MKSLTAFYTLLVAAATVTNAHNIVTHFHVNGKAEQSCVNLPPNTNPITDIQSQQMACNAIGTAAKSKCAVKAGDSVAFEWRTDFNIPPAEYPLNPNGEPIGVTDVSHEGPCALYAKKVSNSLDDASAAAGDGWFKIAEDGLDQNGVFCSTRLRKANAPYQATIPTSLAPGDYLLRAEMLTLNNAGSYSIGGEEQPQFYVGCVAVTISGGDSSAKAQEVSIPGYVTKQTPGLIWDIWNGKDANAGSFKAGSYPRVGPAPLSEGESSSPAPSAASPSKGSPSGKPSSKPSKPSSPTPAPETPAPSEGSGDEDSGSEDEQGNSPAESPAPSEKPRQKQPDNVVVVTKTVYVNAPVETHYVTVSQDARSWGKVRARRETWRA | 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: Secreted
Sequence Length: 378
Domain: Has a modular structure: an endo-beta-1,4-glucanase catalytic module at the N-terminus, a linker rich in serines and threonines, and a C-terminal carbohydrate-binding module (CBM). The genes for catalytic modules and CBMs seem to have evolved separately and have been linked by gene fusion.
Sequence Mass (Da): 39580
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A0A1T4ZLL4 | MGHGSWVDSIASPASPASPAPPASPALTRGLAATVDCNSRYVYLDPYEGAKAAVAEAARNLSCVGAQPIAVTDNLNFGSPEKPIGYWQLAESCRGISDGCKAFNTPVTGGNVSLYNETLDADGNPESIYPTPVVGMVGLITDLTKVCGQGWQGSGDLIYLLGDDKTLPTLGASEYLAVLHGTIAGKPPRVDFELEQKVQPTCREGIRQGWIKSAHDCAEGGLAVALAESCLSGKKGARVKLNLSSTAAAVRWDEVLFAEGGGRILVSVPPEYQSVWEEFLHQQLGEENHIWQNLGVVGSESEGLRILTSDDQGLIEVNLSEMGDHYFNGIERRLDG | 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 conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the ammonia molecule from PurQ to PurL.
Catalytic Activity: ATP + H2O + L-glutamine + N(2)-formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide = 2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ADP + H(+) + L-glutamate + phosphate
EC: 6.3.5.3
Subcellular Location: Cytoplasm
Sequence Length: 336
Sequence Mass (Da): 35642
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A0A938VQC3 | MGVAVALFYVAAALAVAGALVVVLARNVVVAALGLVGALVMVGGVFLILHADFLAFAQILIYATAVSILLMFGLMLTRQSGGRARAADLLQQPLAVVAGLAVTGLGLWVAFGTPWFRPGVNPPELRPVSAADLARGLFVQWAVPFEVASVVLLVALIGAVVIARREPPVK | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Catalytic Activity: a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+)
EC: 7.1.1.-
Subcellular Location: Cell membrane
Sequence Length: 170
Sequence Mass (Da): 17547
Location Topology: Multi-pass membrane protein
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A0A2P5DJG9 | MLSISYSVASLSLNHCDNTCPHLDCVVESAVKTAMSNDKTVPATLLRMHFHDCFIRGCDGSVSLESKGKNKAEKDGPLVTTIDASLRSICAAHNEVRNAGTSLDSTTTTFDNAYYKLLLQGKIIFSSDQALLTTPKTKALVSKYATSKQEFEKAFVESMIKMSNINGGQGIRHNCKVVN | Cofactor: Binds 2 calcium ions per subunit.
EC: 1.11.1.7
Catalytic Activity: 2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O
Sequence Length: 179
Sequence Mass (Da): 19454
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A0A2D4M439 | VLLLITSYVVNFTRVGTLALCLHDVVDVVLEAAKMANYCKFQKLCDFLFLSFAIIFIITRLGIYPLWILNTIFFELPEIVGGFPGLSIFIIFLLILQILHCFWSYLIIKAAYKAVLKGKVRSMGMFFS | Pathway: Lipid metabolism; sphingolipid metabolism.
Catalytic Activity: octadecanoyl-CoA + sphinganine = CoA + H(+) + N-(octadecanoyl)-sphinganine
Subcellular Location: Membrane
Sequence Length: 128
Sequence Mass (Da): 14609
Location Topology: Multi-pass membrane protein
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U4KV68 | MAAPMAFNMARAAMGGSTEMAEKNISRYFSTLKPFFAVTNIYVIRKLYLLVNPWRHSPWSRQSTTRASANRGETETVYLQPREDINAPDMYIPLMSFVTYILLSALLYGLSGTFHPEMLGYTASSALGAVMFELVCLKLGCYLLSIGNSTLLDLVAYSGYKFVGVIFIILATAMTGSGWISWTVFGYFYLAQAFFLLRSLKYVLLPEDGQVEAANGYPMAPRQMRKRRTWFLFGYSYVVQFIFMMTLTSGVGKVKGA | Function: Has a role in transport between endoplasmic reticulum and Golgi.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 257
Sequence Mass (Da): 28844
Location Topology: Multi-pass membrane protein
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A0A6I6HX23 | MSKKFLAAALLPTAAFAQTTIPINPTLVITANRVEQPVSSVLAPVVVIDRAEIESRQVQSLPDLLKTLPGVQMATLGGRGHISSLFVRGTNSNHSLVLMNGRPIAAMVAGTPDLSQIPLGNIERIEYIRGPRAAVYGSDAIGGVINLITKTSAKNGSETHLKGGAGSNGYGQGELRTVQSLGQKTDMNMLIGYERTDGFDVVANTKQPDRDGFNSKNGQFGLNHTFNDAWSADFNAQRYQNLTEFDGRYDQQQVDTFQYDGGLKFQSKALTSRLEASYGENSSKSWEESKGKSSADPTHTGMTNISWINSWSGIEDLNLTGGVDWQREQMKSDSRSGGQPFTVPDRDNTGAFVVGSYVWRPFLFELSGRTDDNQQYGRHNTWSAASGLDIDEHHNVRLSYGTAFKAPSFMDLYYGVPAELKPEESKNLELGLSGRYSVWDWSVNLYRNRIDNLIYCLTSMSYTCNPKNTTADIKGVETELGIDTGPVHHRLSYDYTRAKDTGNQDLQLLRRAEHKGSWIADTRFDAATLTAELLYVGKRYDNNWATNQRVELGAYTLLNLAASYEVTQQFILGGRIDNLFDRDYAPAYGYASPGTEFKVTADYRF | Function: Involved in the active translocation of vitamin B12 (cyanocobalamin) across the outer membrane to the periplasmic space. It derives its energy for transport by interacting with the trans-periplasmic membrane protein TonB.
Subcellular Location: Cell outer membrane
Sequence Length: 605
Sequence Mass (Da): 66946
Location Topology: Multi-pass membrane protein
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A0A966MZS1 | TTLEISLAIAAVILATINMVGGFVVTDRMLQMFKGKGKPKKEKGDDK | Function: The transhydrogenation between NADH and NADP is coupled to respiration and ATP hydrolysis and functions as a proton pump across the membrane.
EC: 7.1.1.1
Catalytic Activity: H(+)(in) + NAD(+) + NADPH = H(+)(out) + NADH + NADP(+)
Sequence Length: 47
Sequence Mass (Da): 5065
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H9LB67 | IFSLHLAGISSILGAINFITTIINMRINGLSFDQMPLFVWSVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPTGGGDPILYQHLFWFFGH | 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-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
EC: 7.1.1.9
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 94
Sequence Mass (Da): 10323
Location Topology: Multi-pass membrane protein
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T0KJZ9 | MAQTGGPAEPTPENPKGGRSIWGGAFDDEIRPALKHSSRGIVSMANKGPGTNGSQFFILFDKAPHLDGLNTVFGRLIGDDSTVTLAKIEAVEVDRKNRPKEPVKIETVTIHANPLAG | 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: 117
Sequence Mass (Da): 12430
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A0A0G0M6D4 | MENIEKNLTEITPHQFDLKTDKMSVPARFFMSKDLLPEEKTFIQAEDIASNKDVLFRHTVAMPDVCSKPGRKNASGTTIISDKYILPQVNDSDPNCGMRLVKTNLTEDNISAEQIDELFKKLVDIVPTKKFVGTVVPFKIVVDICRRGTIAAIEHLGIKTKNELENTQHGGNFFGKEMTKQDIFDAIPKLYMHFAKFRLGILGAAGNHFLDMLKVSDIIDPEIAQKFGLKKGQYLLMVHTGSGILGQYTMYTHTAKKAEHLSQALMVMLGKLTFRSSKKDVYKKMQEKIAKHMTKDDSLLTYDGNGEDGKMYMNARAAASNFGTANRAVIIHNIATTMQEVLGREVEMDLIYDLPHISITKENHFEKDVWVHRSNTSRAFGPAKMAEHPIYKETGEPVFIPSSMSTDAYICVGTDRNEESFYSAPHGTGKGKNNAEKTIENKDELFAKMEEKGVKLYNAKSSIVINQDSARYKNIDQVIEGVEANGIAHVVAKMEPVAVIMY | Cofactor: Binds 2 manganese ions per subunit.
EC: 6.5.1.-
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: 502
Sequence Mass (Da): 56274
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A0A7V1E746 | MAFFQGILLGTIQGLTEFLPVSSSGHLVIAGKLLGLNQDSLTTNALLHLGTLIAVIIYFRHELSRILSSVWQWVRWNKKDSHSALAGYLLAATVPAAAGGALFEKFFSDAFDSTFIVGIMLLTTGAVLWTVESKELGVRNLDSMKLSDSVWVGLAQLAAIMPGLSRSGVTIAAGIWCGLEREEAARFSFLLSIPIIIGASVVSISRGQPLVDVTSIIAGMIAAGLSGFLAIAVLMKVVQEKRLRLFAVYCFIVGSIAIILTLKQ | 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: 264
Sequence Mass (Da): 28222
Location Topology: Multi-pass membrane protein
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U4LV35 | MNRSPLFSNFRKPHEHLLSISSLGGPTASTMPMSTTTTPRTHTRKRSSGGSSSGSQGDIGIPAEIESDDGDMGSFSRSRSRGPDRSKSRSVSPSWAQGSSAEVPLLSIGSEASSRGQSPHPDSCDDQGERWRPDTGTKWWQDGKLGKWLWTTPRGRTVYISILLLLYGIASFLLLVMNRLLLWSRFAYPLTTTLIELLFTQFFLYASASITRSFSRQLHGLGLGFIVAPNPSLKGKRHASNIRGLRDFANAIRPNTTGGVFEFKWAEAKLVLPLAIIYSGKIMLSNIAFAYTQLQIYQISRVITLIWALGLTHIYHRTQSLTVTTLSSCITMTLSLLMATLRPGSRFAIEGFIAGIFSTFFVSLYPFILSRVYRLLTHRLSSHEPTSPSMIGTMISIFAPTTSLPHPRSDGSSTRAFWKLMHYLNLLTIIILIPMCFITGEFRNISRNCYILDVAWFWLMMLGAGATAFSTFVMGFAVVVATTPLTMVVAAYPRAAVQLVMIMGVKMPVWSWVGVLMTGGGAGWYGVGRRVEWKAVGDVRGRRGSRDDRGEA | Function: Involved in the import of GDP-mannose from the cytoplasm into the Golgi lumen.
Subcellular Location: Golgi apparatus membrane
Sequence Length: 552
Sequence Mass (Da): 60998
Location Topology: Multi-pass membrane protein
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A0A8J7KSQ8 | MYVVLSCAASIDGYLDDSSDTRLLLSNAADFDRVDEVRAGCDAIMVGGNTYRRDQPRLRIRSADRIAARRASGLPEHPLRVVVSRSVAAVDDWLAYPSIDLALKDLEARGVRRLMVEGGADVLAQFLNRGLADELHLAVAPRFVGDPRGTRLNGIAEATLAEVTQLDQIVVLRYLLRDHAFMRQAIELSKLCPPSDTAFAVGAVIVREGKILSTGYSRETDPTVHAEQAALNKIGDAKGATVYSSLEPCSIRKSGARPCADRLIEAGIARVVYAWREPPLFVHGDGAAVLKDVGIEVVELTELAAEARATNVMMGP | Pathway: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 2/4.
Function: Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5'-phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)-pyrimidinedione 5'-phosphate.
EC: 3.5.4.26
Sequence Length: 316
Sequence Mass (Da): 34159
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A0A7V1E7Z2 | MELTDEFERNSLSTVCEETACPNIWECFFRREAAFLIMGTICTRACGHCRIKSGKPTVPQEGESRRIAESVASLGLESIVIASVARDDLHGGGAKYFVDTIKEIRARVPKCQIEVLIPDFGGDLNAVTEVVDARPDIIGHNIEVVSRLFPALRPQADYERSLAVLKKLVGDDMAVKSNIMVGLGETRSEIRAAGRDLVGLGLKTIMIGQYLQPSREHHAVRRYYRPAEFMGLAKYFQRLGFRRVVSGPIVRSSLRGVFHDLTPPKTLSGHTT | Cofactor: Binds 2 [4Fe-4S] clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Pathway: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 2/2.
Function: Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
EC: 2.8.1.8
Subcellular Location: Cytoplasm
Catalytic Activity: [[Fe-S] cluster scaffold protein carrying a second [4Fe-4S](2+) cluster] + 4 H(+) + N(6)-octanoyl-L-lysyl-[protein] + 2 oxidized [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + 2 5'-deoxyadenosine + [[Fe-S] cluster scaffold protein] + 4 Fe(3+) + 2 hydrogen sulfide + 2 L-methionine + 2 reduced [2Fe-2S]-[ferredoxin]
Sequence Length: 272
Sequence Mass (Da): 30156
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A0A1M6IZR5 | MKIIRSKQPKYPTLLKFAFSGENGEIPDFKAKEGEVVVRYEQGYTSVYCGLGERKDMAPYKARSAAAEGVRQVRKLERIGLSVILPQETPDKSAVDVACVEGLFLGAYEYTEYKSEKPKELRTCQLVGVKAPNKKINDAIAACQAACYSRDLINDNADNIFPERLADEARQICRQDGFSLTVLTEQMMEKKGLGLIHAVGRASTRPPRLVVMQYKGAPDKQEKIAIVGKGITFDSGGQNLKPTGSIETMRDDMSGAAAVLGVMKALAEIKPAVNVIGVLAAAHNAIGGAAFFPGDVYKSYLGKTVEIGNTDAEGRLVLADAIAYCEKNYRPTEIIDIATLTGGVIIALGTTVAGLFSHDDAMAERLFQAGEETRERLWRFPLYKEYYEAMKSERADLCNTAKHKKGWASSPTGAAFIGEFVSDAAWAHLDIAGTAYNEGGAKGEVPKFGTGFGVRLLLNYLGVI | Cofactor: Binds 2 manganese ions per subunit.
Function: Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides.
EC: 3.4.11.1
Catalytic Activity: Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low.
Subcellular Location: Cytoplasm
Sequence Length: 464
Sequence Mass (Da): 50335
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A0A835B2G8 | MFLIVLVIYSAWVCPFELAFLRDLPSKLLLVENIVNSFFAIDIVLTFFVAYIDSKTHLLVDDRKRIAVRLEKDIRFNYFWTRCSKLISRDSIQAASEFAARNQLPEKIKQQMLSHFCLQFKTEGLNQQAMLNGLPKGIRSSIAYNLFFPIIRRAYLFHGVSNNFIAQLTLITTVNGNEKVYGKIEEGEVFGEVGALCGIPQPFTCRTATLSQLLRISKIRLIEIIQEHREDSNILMNNLFQKLKLQENLPGFMHKYETFHVPREAWLLPQPYLQYKEHRCEDTGTKVPTFGADDGSTKLVAESNQLRKPQQENSHDQSNFNCGATDGMAGKEEDHDEVHINCEARKGSEELCIQIKSETVKLASYHNTSEGITRRRNQDSNYIKASNKRVTVHAYAYNATVSLVQNGKLISLPGSLEELFEIGSQKFPGFHPTKVFSRDYAEIDDISVIRDGDHLFLLQM | Function: Potassium channel.
Subcellular Location: Membrane
Sequence Length: 460
Domain: The KHA domain (rich in hydrophobic and acidic residues) present in the C-terminal part is likely to be important for tetramerization.
Sequence Mass (Da): 52598
Location Topology: Multi-pass membrane protein
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A0A8T2CM37 | MRAITASFFIFCFLVPSVLAQLRHGFYDATCPLAEIIVTKVVVKHWARNQTVVTAALLRMQFHDCFVNGCDASLLIDSTSERPSEKSARQNANLRGFDLIDESKNVLESACPNTVSCADIVTIATRDSIALAGGPRFTVRIGRRDGLRSNPSDVDLPGPTISVDESIKAFKAKGMTVEDMVALIGGGHTVGVAHCSLFQDRLKDPTMDPRLKAKLNKTCSGPNDPSVFLDQTSPFRVDNVILRIDQNLGLDGLTKGFVSTFASSDRFFREKFAEAMQKMGEIGVLTGDSGEIRTNCRSTEKDSRGTLYGVGSLKGILRNGKRKQPGDSSSFVAMQEQLKEAQRKIEEQAAENAIRDAAVAAREKEHSRTVAEQKDKLEHLSLVEKYLRQTDPAFLDFIQSHSAPATTEPVSNGLTPTP | Cofactor: Binds 2 calcium ions per subunit.
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue.
EC: 1.11.1.7
Subcellular Location: Secreted
Sequence Length: 418
Sequence Mass (Da): 45709
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A0A354RD96 | MNKKNDFHSVISVLGISMGDEGKGRVVHEILDHIESGTGSSAAGVIKVNGGANAGHTAAGLKLNLLPSGVGNPRVNNLLIGSGVVADPRKFLWEAKPLEARGISVLKRLKIDEKCQMSDLCHRLLDLAWETYRVQQLGQENRGSTGRGISPAYCDETGQWQIFYQSFLLDRKEFSSALKERMQRAMDTIRFVCKVSEADWFSFFDVLTDAETRANRSSIEDGIFSPSEFDFKVFLKSNPFEINFELLEEIYWNTGQDLVSCIDDVRELLLSFKETKKSVVAEFGQAYWLDKRHGFTPNVTASHTSGAEFFNSGGIPISKISQVGCCKAYDTKVGTHHFITQLDQTKNPWGAKLSKLEFGTSTGRQRMVGWFDAVEKGNALRYCGFDHLVINKLDALTANQPNLEELKICKAYQLPDGTVTKIVPRAEIDRKKIIPVYETFQLWTEDLQSLNSFEDFPVAAQRYVSRMVGTLLEVAYPEGFADKKLPRILFVGVGPEPGQIITDVPETGELIRSFASNSPSGIQ | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2.
Function: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.
EC: 6.3.4.4
Subcellular Location: Cytoplasm
Catalytic Activity: GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate
Sequence Length: 523
Sequence Mass (Da): 58259
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A0A0J5QBW7 | MSEFNEAELPDVDLPAGWFAVDRGLVLITKITLAGIGLGFVGLVSSEVVSRFFFDRSMAEVNAIARILLVWFFMLGSGLALRQGAHVGIDLLRRSLRRRGPDIVQVLAELLFFVFLLEMLWASYLAVTSAARQFEGTLGISMVWVMAAFPAGFGLLTYHWGVMVVDRLRRRQRAAA | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 176
Sequence Mass (Da): 19565
Location Topology: Multi-pass membrane protein
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A0A0J5QEK8 | MTQAVPQTKPLDGALCIVENFMAVIAGAVLAVVMLLVSADAVLRHIFLAPIPWQFTLTESYLMVAGIAMGLPWGYRTGGRIRINLLLSFVPAGRRRLMLRVGNLLVAPYIAVLCWKSAEKTWDAFANSEYMMGIIDWPVGWSWIWVPLALAVLTIRLVFDAFGDVDHADSAEH | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 173
Sequence Mass (Da): 19127
Location Topology: Multi-pass membrane protein
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A0A2E8A8X2 | MTNPFNQKLFLVGMMGSGKTEVGLQFSRKYNLSFFDTDQEIEKMAGCSITEIFANQGESEFRKMEQAVIDSILTKESCIISCGGGLCIPEGMMERLKILGIVACLWAEPRTILARINKDNSRPLIDQGDPLSSIEEILQKRRNRYLAADKILNTENKSIQEIIQEISKFFPLNTV | 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
Subcellular Location: Cytoplasm
Catalytic Activity: ATP + shikimate = 3-phosphoshikimate + ADP + H(+)
Sequence Length: 175
Sequence Mass (Da): 19745
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A0A7V2JRH7 | MGVKLIRVLIVDDSAVARQAITNILESDSELKVIGYAKNGVEGVEQTLKLKPDIITMDIYMPKLDGYQATKEIMRLQPTPIIAVSASVDSIEMKTSFRAINAGALGLVEKPLSVSDKRFKQIKDNLITKVKIMSAIKLVRRWQRNETVKKLYLPRGRDKRNTKIIAVGSSTGGPSAVNLILKQLPKDFKIPIVIVQHITAGFSQAFADWLSGECQRMVRLAEDGRRILPGDILIAPDNTHFGISVSHQVSLADKVNYNHHRPSVNYLFDNVAKAYGSKAIALILTGMGNDGCVGIKAIKMAGGRTIAQDEASSVVFGMPKAAIKAGVIDEVVPIDEMVKTILRLI | PTM: Phosphorylated by CheA. Phosphorylation of the N-terminal regulatory domain activates the methylesterase activity.
Function: Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irreversible deamidation of specific glutamine residues to glutamic acid.
EC: 3.1.1.61
Catalytic Activity: H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)
Subcellular Location: Cytoplasm
Sequence Length: 345
Domain: Contains a C-terminal catalytic domain, and an N-terminal region which modulates catalytic activity.
Sequence Mass (Da): 37710
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R7GCZ7 | MKISVSTHQGKLYDDEITYAVIKNADGEFAIMKNHIPLVCVIPDGYIKLVVPGQELYLAIINGMLEFKENIITVIAQGAHIGYSKESALEHLESIRSERLESNRKANIDFTQKEKELLDNIRTTKAGSL | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane.
Subcellular Location: Cell membrane
Sequence Length: 129
Sequence Mass (Da): 14460
Location Topology: Peripheral membrane protein
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A0A3D4HHG6 | MRFQKRLRSFLYFYAFTLGIAYSLSANDQPSTQDNYPPNYPEAFLLGVVEGVTEYLPISSTGHLILVNHYLKLDEPTPILDGKGEPIQIKKNGTERTLTLQDAINAYSIVIQGGAIIAVVLLYWRRIVTILQGILGRNPEGLLLARNLIFAFLPAAILGLLLDDIIE | Catalytic Activity: di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate
EC: 3.6.1.27
Subcellular Location: Membrane
Sequence Length: 167
Sequence Mass (Da): 18618
Location Topology: Multi-pass membrane protein
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B8D483 | MDPIVLAGFVGAFMLAWIDGANNAANSIGTIIGVRALPVRRALLIASIFELIGGLAYGRFISSTLSSKIVSVAEISSRIITAGFVIALFVSFIIVFLATRKHMPFSISIVTVGAISGIGLAMGVEYVNTGLLLELFVLWLLIPFIGLLVGYIYYRLYSYLRSRRNIYVKIFLPLLLLYTSFTVSAVYMAIPEQLLENIYILAAVSSIIVVLTASIMIYLYMNIWGSRHEVIDVDTVVNRFNNRMLIASSAILAFTHGGHDVANAAAPLMLILGSRELNHDIESLLILTYSSLGLSTGILTWGVSVAKTIGEEITVLNPESVLIANIAGAQTTLIVTRLGLPSSMVGIIIGSIMGVGLGRGISSVNTRLFSRMLSYWYIGFLVATVVTYIATRILLYVSI | Function: Potential transporter for phosphate.
Subcellular Location: Membrane
Sequence Length: 399
Sequence Mass (Da): 43246
Location Topology: Multi-pass membrane protein
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A0A1V4MJR5 | MSIWESIGLGVLQGLTEFLPVSSSGHLVIAQSFIGEFEQPGVLFDVMVHFGTMLAVLVFFRRELFAVLRACLPGDRPAGAEGLSSAAGRKLAGIIVVATVMTGFLGLMFQDRIYALFESVQTVSAALVVTGVLLFLSDRVREGRRGLENMRIIDGIIIGLVQACALVPGISRSGSTITAGIFLGLKGEAAARFSFLIAVPAILGATILEMRQVSMVSFETMMIYCIGAAAAAVVGFVTIALLMFVVSRRNLRYFAYYCWILACVLCLVNNL | 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: 271
Sequence Mass (Da): 29088
Location Topology: Multi-pass membrane protein
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A0A101GMW2 | MDLRSIPIEEALGHPLAHDLTKIDAEKGIKGARFRRGHILQPEDLPVLREMGRRSLSIIHLGLDEVHEDEAALSLAKALAGEGFEISGPEEGRCGLVSTGRGIVRFDIEAVRSINKDREWSLACTQCNSVVGPGSVVAAFRILPLCLKKDSLDRAVEAASPFILIPFLHRRVGLVSTGQEILEGLVKDSFREKLERKLRELGGSFSGQRVCGDRSPDIADAINELLECGSDIVICTGGMSIDADDRTPQAIATASDEVLFRGVPMIPGSNLMLARKGLSWIIGAPACVAHDERTALDRLLIALFAGSGGELNVSLWGEGGLCRRCKVCIFPECEFARIPS | Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
Function: Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP.
EC: 2.10.1.1
Catalytic Activity: adenylyl-molybdopterin + H(+) + molybdate = AMP + H2O + Mo-molybdopterin
Sequence Length: 340
Sequence Mass (Da): 36740
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A0A3D4HH35 | MAIRIKVCGIATFQSASHALKVGADFLGINRYQGSPRCVSQSAARELMQNIPQGKRVVVDVAPSLDTLKEHLEEGFDYFQLHFDYIDAQSLLPKCRRLIGKERLWLAPRLNKGDAFPSALLEYADTLLLDACDAEGYGGSGLLADWPLFRDLQDAHPEKVWILAGGLGPGNVKRAIAESGARFIDVNSRVETSPGVKDLSLLKTVFESVRSIDD | 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: 214
Sequence Mass (Da): 23500
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A0A0G0JVC6 | MRISMSIDPYKAQEGNNLQIFNDIKIWLKKHGDDIVKREDKPEYEITFGGDSNLMRTASACSKLGIPVLSINAGNVGFLTYGHITDWEKPISEFLQGNFRIEERLGLMLKYGGKEFGPLVNDVYFEGSEGVPYYTIWKNDILVHDSLKANGVIVSTPTGSTGYNQGAGGPICEPDVQSIFIITTICPTVCNTRPLIVSDNSIIKIEVAPCRPPGSALLFGDGQKLDVVRDGGMIIVKKHPVKLKIVVLENSNFFLALQTKKGFRG | 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 Location: Cytoplasm
Sequence Length: 265
Sequence Mass (Da): 29197
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A0A848SYS1 | MAHGKIGQSPEADLVDRYIERAQWPVKITELAEGGGKIPPLPPRTKVVALDETGQQFSSVSLARQLQTWRDGGATEIRFLIGGADGLSDEERAGADMLLAFGKVTWPHKMARAMLAEQLWRASSILANHPYHREG | Function: Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA.
Catalytic Activity: pseudouridine(1915) in 23S rRNA + S-adenosyl-L-methionine = H(+) + N(3)-methylpseudouridine(1915) in 23S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.177
Subcellular Location: Cytoplasm
Sequence Length: 135
Sequence Mass (Da): 14830
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A0A835BIM4 | MGPVRLALLAAVALAAAAAVGEAVYIPYNTSAGVVPGKLNVHVVPHTHDDVGWLKTVDQYYVGSNNSIQGACVQNVLDSLIPALLKDENRKFIYVEQVNLASRVVITFEMRQSRLSKYLIICQVGFDAFYFFRIDYQDRDTRKGTKELEVVWRGSKSFGSSADIFAGIFPKNYEPPPGDFYFEVDDDSPVVQDDPLLFDYNVEERVNDFVAAALAQVQLDLIMVMFGFLCISLQIYTPQGSDGRINALYSTPSIYTDAKYAANEQWPLKTNDFFPYADNPNGYWTGYFTSRPALKRYVRMMSGYYLAARQLEFFKGKGKPGPTTDYLGDALALAQHHDAVTGTEKQHVANDYAKRLSIGYTRAQELVSTSLSCLTELGSKPRCSTPTTKFSQCLLLNVTYCPPSEMDFSKGRSLVVLVYNSLGWKREDVLRVPVFSDSIVVHDSEGREIESQLLPIASASLNLRDKHVKAYLGTTPGAKPKFWLAFPVSVPPLGFNTYFVSSSKKSGNFTSLSLVHTDLRSATQKYLSNSYTNPASVSLKSTVYSTQGSKDNLQVGQGNLKLQYNSAGTLSLYSDSKALVMILQIRDYRSEWKIEVHQPIAGNYYPVSFLCDSVHLQVNLGIYVEDGSKELSVLVDRSVGGSSIKDGQIELMLHRRLLHDDGRGVAEALNETVCLDNQCEGLTIEGKYYLKIDPQGEGARWRRTFGQEIYSPLLLAFSEQDGGNWVNSHVPKFSAMDPTYSLPDNVALLTLQELEDESVLLRFAHLYEAGEHKDLSALASVDLKQVFPDMKIGKIIETSLSANQERAAMEKKRLKWKVQGPTTDEKVVRGRPVDPSKLVVELGPMEIRTFIVSFDHSISGNQLL | Cofactor: Binds 1 zinc ion per subunit.
EC: 3.2.1.-
Catalytic Activity: Hydrolysis of terminal, non-reducing alpha-D-mannose residues in alpha-D-mannosides.
Sequence Length: 864
Sequence Mass (Da): 96208
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U4LDP9 | MRSFLARGAVLLTSLFVAIAQATPETAPQLNLPEKFAPPPVFKNTNLLRNIDLTKPYQREVIAVVVENISKDPQTDYYIPFDKEVAERISYIEARDKAGVLGFLDVAKAQSPGPTQWYRVFISEPVKAGEQITLHIAIGLTGVVEPVPAEINQVDRQYLKWTGTQYSRSAYVTGKQKTKIKLINNEVPDYTQLEPKSDGSSDPAKLGSTITYGPYEEVTSAQLGGDVISLRYEYTLPVITADTFSREIEVSHWGGNLAIEEKYALTNTGAKLKDNFNRVKWTATNYLNPPTAAIKSLTYGLTNFPLNPYYTDEIGNVSTSRFRQEQKPGEAHLELKPRYPLFGGWNYSYTLGWNHDLRNFVRQRGSSGNYVLRVPFMEGPKEPMVYKDVSVTVILPEGATDVAWYSPLPILSEERFFHKTFMDTLGRTAIKLRMSNVVDELQGRELRVSYNLSPVEFYRKPYVIFSALSALFLVSWVVAGIDVRIGPKKEGEEGK | Pathway: Protein modification; protein glycosylation.
Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 495
Sequence Mass (Da): 55692
Location Topology: Single-pass type I membrane protein
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A0A7C5GLC6 | GVNKSKMHRFFVHLYQNEKEIVVWGKTAELFIDTTTGDRILEIQNGERYEFNPNNNQMSFIRFDEHAIRIPLLSSTYQEKLSSTNTLSLLNSDELTHQAELHWRLAIIISAPLMALLALPLSHTTPRQGRYGKVAIGVLIYALYANALITGKSLLEDESIPSELGLWWVHLILMFFALWLIRRSFGKAT | Function: Part of the ABC transporter complex LptBFG involved in the translocation of lipopolysaccharide (LPS) from the inner membrane to the outer membrane.
Subcellular Location: Membrane
Sequence Length: 189
Sequence Mass (Da): 21671
Location Topology: Multi-pass membrane protein
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E7RVY8 | MSTLTWSIIALVVVVLVIVIAHNLWQGRRRRQQASALGLRKGYFDDDPQTLTGGAGPDDESSPRRGRGRREPVMRGAARQVPPDLAARPARFEGEDSRSLRKGGPSSDPADRHPSLALDDEDYIETPFENPAAVRPWSSAEDGARVEAARRAEAQALASRRIPDSLRRESARDGHSPVHAGQTDAGHDRHGARDEGRDAPFEAAGTRVGRGRTAGAHRADADDSRMEASMARPAVDHDGGGAEHPAEEDSSAAQRMTRGVASQGTPEDDDRRGSHRDASPTSVAADDGEADGQRRVDDVSPAQADDIEAEGAEAVPAEVAEPDPLPDAQVEHVVILEPPAPVNTDRLVALTSSLRHVGSKPVRIEVERLGSHWGPLTAGEKAVRIRCSLLLANRQGPLNAVELSDFNAAIESLASKLQAPVNIPDMAPILRNARDLDTLAARLDTQIEVRVELPEAAEPNRVAGVVRHLGLSERGNGRYEAFADSGDSLFTLAFNQTRDQIDFMLDVPRTAEKYEAWEGMVACAQSMAQALGGRLVDSSGRGLSVGMIGTVSRQLARRYAELAQVGLAAGNAAALRVFH | Function: Essential cell division protein that stabilizes the FtsZ protofilaments by cross-linking them and that serves as a cytoplasmic membrane anchor for the Z ring. Also required for the recruitment to the septal ring of downstream cell division proteins.
Subcellular Location: Cell inner membrane
Sequence Length: 579
Sequence Mass (Da): 62017
Location Topology: Single-pass type I membrane protein
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A0A938FDN8 | MSRKPGLLVLVGVPGAGKTTIGKELSSQTGVDFFDSDEEIVERTGSSVSHLFIEKGEPFFRQIERDVVAEGLKRSDGVYALGGGAVLDPATRELLKGVNVCWLKVSAPVAAKRVGLDQPRPVLLGNVRSQMVKLLNEREPFYKEVATFSVDTDEKAPSEVVLDVMAKNQ | 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
Subcellular Location: Cytoplasm
Catalytic Activity: ATP + shikimate = 3-phosphoshikimate + ADP + H(+)
Sequence Length: 169
Sequence Mass (Da): 18328
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A0A948CBD0 | MSGGLRSVDEHLAAILTAMTPLPALQLPLLDALDLAAAEDVVAPIQLPRFDNSAMDGYAVR | Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
Function: Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP.
EC: 2.10.1.1
Catalytic Activity: adenylyl-molybdopterin + H(+) + molybdate = AMP + H2O + Mo-molybdopterin
Sequence Length: 61
Sequence Mass (Da): 6416
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A0A7V1CJ51 | MAIKDTLNLPKTDFPMKANLANREPQMLEFWENIGLYKKAQEASKGKTKFVLHDGPPYANGDIHVGHTLNKVIKDIIVKYKAMQGFDAPYVPGWDTHGQPIEHNVLKELGDKRKSITDVELRKKCHDYAMKFVERQRDEFKRLGIRGDWEKPYLTLDPVYESANIRVFGELFKKGLIYKGKKPIHWCSYCATALAEAEIEYSDEKSPSIYLKFRVRDDKGVLADFKDVDFMVWTTTPWTLPANVALALDPKGDYVLVESKGEHLLILKDLAESVFAELERPYKEVKSFTGKDLQGMTVSHPLYEQESVVVLADFISREQGTGVVHIAPGHGQEDYLVGLEYDLEMPMPVNDKGVFTEEAQRFEGQDIYEGNKSIVKDLDDRGILLKLSFIEHSYPHCWRCRKPVIFRATEQWFVSMEKADLRKDALKEIKSVDWIPQWSQGRIEDMVTERPDWCISRQRVWGVPLPVFICKDCDEVLVNTDIIEA | 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 the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile).
EC: 6.1.1.5
Catalytic Activity: ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile)
Sequence Length: 485
Sequence Mass (Da): 55839
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A0A6P9A444 | MGSFAYHVSSHELLIPPEMTITTSGSSICHRLAKFLNINPKFFILILFGLVLFYIPAYHQLAQPQIRDEELDGWPRNGTRDVRLFIQPENVTTILSTTVCDGRQPFLVVVVCSAVQNFEARKVIRETWASSGSTVGKESNRSNEVLEDPPKDVFVVFLLGDPDNATLQSIVEEESRRYGDIVQEGFIDSYNNLTVKSVMLLKWVTQRCSNALYVMKTDDDTMVSLASLQSFLMLHQASIAKPNSRKVPLLTGNLICGAKPILDSTDKWYMPRYIFSGRTYPNYLSGSGYVMSQEAVQALYDAAQRVSLIPLEDVYITGQCAVFAGIRPAGHPGFSLGKRPMSTCSLGNPQVITTHRLNPRELKEAWDLSRMSTAHCNKTVPASTPAAASQTYLRGSMFGRKQRHIFNSRRGHGCF | EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 415
Sequence Mass (Da): 46329
Location Topology: Single-pass type II membrane protein
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A0A2E8A5J5 | MKQIVIFTDGACRGNPGIGAYAARLEYQGHQKVVAQAYELTTNNRMELMAMIKGLEMLKELCAVTAYTDSKYVQNAITEGWLKRWSSHGWRPKWKSPKLVKNVDLWKILHPLLEKHDVTVEWVKGHAGNGGNEAVDQAANEAIDSGNFLQDKGFLNKETHLNNPNQMDLGL | Cofactor: Binds 1 Mg(2+) ion per subunit. May bind a second metal ion at a regulatory site, or 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.
Subcellular Location: Cytoplasm
Sequence Length: 171
Sequence Mass (Da): 19220
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A0A101IW47 | MAKIERSQKLFLKALKEKFQGQDVESETAEFYKFNGVRQSPRKMEFMKASRAVEMDRGVSMYDPERCHLGGIPMGQRQLMTYEVSGTGVFVEGDDLHFVNNAAMQQMWDDIRRTVIVGMDLAHQTLQKRLGKEVTPETINEYLHILNHAMPGGAVVQEHMVETHPGLVDDCYVKVFTGDQELADDIEPQFLLDIEKLFTAKQAEELKAEVGKSMYQAIHIPTAVSRTCDGGTTSRWSAMQIGMSFIAAYRMCAGEAAVADLSYAAKHAGVIQMGSHLPARRARGPNEPGGIKFGLFADIVSTRPRPTPTTSSTSSPTTVWTTPGTSTRSTGRTRARATRSSRPRRSSTISQPRSPSTLWSSTSSSRP | Pathway: One-carbon metabolism; methyl-coenzyme M reduction; methane from methyl-coenzyme M: step 1/1.
EC: 2.8.4.1
Catalytic Activity: coenzyme B + methyl-coenzyme M = coenzyme M-coenzyme B heterodisulfide + methane
Sequence Length: 367
Sequence Mass (Da): 40596
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A0A174UWS4 | MNKEEALNFLKEQLKTMNYLGSTLSIVSWDMEVMAPSQAIDYRSEVMGYLSTQYHQLATDSRIGEALEALSSEISLTQHETKLVENFKDSYEKNKKIPESLQRELTIATSKGSQYWKKAKEQQNYEIFKPYLKQVIDLAIKQAECVGYEGHIYNAFLDDFEKGMTVEELDRIFPPLRDGLVALLDKIMKAKQDEPHHPEGEFDKDRQEQLSLMLLDAMGYDYKESGRVDETEHPFTTSLGPKDVRITTHYYEESIESAIFSSVHEGGHAIYDQNMPHQLAEYGIDEAPSMGIHESQSRFYENIIGRSLSFWRAFYPKLQKIFPEYQEISLEDFYRIVNKVTPSLVRTEADEVTYSLHVIIRYEIEKLMVSGAVSVDELPALWNQKYEEYLGITPPNDSEGLMQDVHWSEALIGYFPSYALGNLYGAQFYHQMKKDIPNVTEQIEAGDLTEIFNWLKTNVHEQGNLYTPAELVERVTGEPLNPQYFLDYLNEKYSRIYHF | Cofactor: Binds 1 zinc ion per subunit.
Function: Broad specificity carboxypetidase that releases amino acids sequentially from the C-terminus, including neutral, aromatic, polar and basic residues.
EC: 3.4.17.19
Catalytic Activity: Release of a C-terminal amino acid with broad specificity, except for -Pro.
Sequence Length: 499
Sequence Mass (Da): 57862
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A0A965DTZ6 | IAPFFLDLNTTEAVIVGLVLALTGTAGDLFESFVKRNLKIKDFSSLLPGHGGMADRIDSLAFNSLSSFLLFGFFLGF | Pathway: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 3/3.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphate + CTP + H(+) = a CDP-1,2-diacyl-sn-glycerol + diphosphate
EC: 2.7.7.41
Subcellular Location: Membrane
Sequence Length: 77
Sequence Mass (Da): 8303
Location Topology: Multi-pass membrane protein
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A0A938J203 | MDRCRVHRGAEPGRGSIPDQHSYPGGVDGDRDPAAGRCDGAPRGALVPQGPVAGSHRPTRRRCRRGGGLTPVLLSGRVHVALVGLSGSGKTVVAPVLADLLGLVAVDTDAAVARVAQRSVGEIFAEQGEATFRELESGALRALLSGPPAVIATGGGIVLAETNRSLLRDHCEVVWLRSSITTLADRIAASGEPRPLLQHGGRTALAQQLLEREDLYAEVADHVVDTDSLEPDQVARLVVSEVTRG | 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
Subcellular Location: Cytoplasm
Catalytic Activity: ATP + shikimate = 3-phosphoshikimate + ADP + H(+)
Sequence Length: 245
Sequence Mass (Da): 25622
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A0A364NBT8 | MMMKGREASNAPWVAPPPSLTTNFPQFLNMLEPDVFGVSQDLVPAAPIKPAGISKVDFDGLLSPPLKLHEDLKNGCGGQLWPAGMVLSKYLLRKHRDDFAGKEIVELGAGGGLVGLAVAIGCNVDTTLHITDQIPMFDLMKRNIALNNLESRVSASIYDWGEPTPSQLPAHPDIILAAECVYFEPAFPLLQQTLRDLIGENTVCYFCFKRRRRADLTFMKTARKMFDVQEVDDDPDKEVYSREKLFLTRHIDLEEPLHQKDEHLADLGHSWELYTFGGSIRTVDQPSRFMTYYMPHSCYADPKSLKSFVFVPHWWISAWFHKGTWANFEHLYHKGQLRLPTEADSGYALRQSEADETLGYSLFIKAVNSFVEKFTELMLSPECIDKRSPEASRQWVRRVYCIYRSQHDDLAMRVTSRDAILDISANPGN | Function: S-adenosyl-L-methionine-dependent protein-lysine N-methyltransferase that methylates elongation factor 1-alpha.
EC: 2.1.1.-
Subcellular Location: Cytoplasm
Sequence Length: 429
Sequence Mass (Da): 48735
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A0A2D8I3L2 | MANEKGAKTIFVLVILLYRILYPLFFIVLSPYYFKRMVKRGGYGKNFFYRFGLWPSLPKKKNKKRIWIQAVSVGELSSIHPLLESLINQSDIEIVLSGTTSTGLRIAQKKYSEQILKLGSFPLDWFPFSSLAWSKIQPDLAICVDSELWPEHMNQAKKRRVPFYIVNGRLSDRSFKRLLSIGSLRKILIPENLNVLASSKKQRDRWIKVGANPENCASFGNIKIDMAPINVPEDSEKAFLKKELGFAESSLVVAGVSTWPGEEKLLLESLTQLEKELPDARLLLIPRHAERRRDVANQIKSSSFSFSQRTKTRNKPIKCEVYLADTTGELIKLIRCADIAFLGKTLPPRHEGQNPVEPVSTGLPIVLGPSCTNFEEISSELIGCGSAIQGQTESEIKKIIYDLSTNEGLRKKMSEAGKMWRLEKGSPTQKTLEKLNKVLLDLQSN | Pathway: Bacterial outer membrane biogenesis; LPS core biosynthesis.
Function: Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of 3-deoxy-D-manno-octulosonate (Kdo) residue(s) from CMP-Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A.
Catalytic Activity: CMP-3-deoxy-beta-D-manno-octulosonate + lipid IVA (E. coli) = alpha-Kdo-(2->6)-lipid IVA (E. coli) + CMP + H(+)
EC: 2.4.99.12
Subcellular Location: Cell membrane
Sequence Length: 445
Sequence Mass (Da): 50285
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A0A2M6ZTG5 | MSHISILQAIVLGVVQGATEFLPVSSSAHLVIFQNLLKVNVAAGQIVAFDVCLHIGTLFAVLLALKKEISVILRGFFVPKENSIELDGGFSETNSRKAIWLVLIGTIPAVIIGFSLKDFFERLFASTLSAGAALIITGFILFATRFVKRSETSLKDMKSKHALAVGLAQAFAIIPGISRSGSTISIGLFVGLKKELSAKFSFLLSIIAIGGAGLLEWKNLRYISQGNFMAIILGTLSAFVVGYICVRWMLVIVRGKKLSWFAFYCWIVGLLTIYFYGGFGFIK | 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: 283
Sequence Mass (Da): 30755
Location Topology: Multi-pass membrane protein
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Q8FNJ5 | MIPNSTNTPETPDDARTGMLTTLVGILSDVGGVSAEDITTTARLREDLAISSLNLIEAVVRVEDAFGVRIEDADVQGFTTTGDIVDFLEANRSETVT | 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: Acyl carrier protein involved in meromycolate extension.
Subcellular Location: Cytoplasm
Sequence Length: 97
Sequence Mass (Da): 10313
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A0A6P8ZPB3 | MAKASVSDDCIDMVTPWNEYLSAKYKRSFAYHTVRNRLPVTVTQVIDHLSRSKEALVQTYGEGSREEIKQIIGYLSKLKNEMQTNKPLISLEANEVDASDWNNFLNTTEERLGRPLLWFADVWLHIECYLYRRIRESFALTKHLNQYDPFRHQKEEAFTGSLQAISVVGSYLLKLIESDAKIDTEQCVLQFLKLSLWGNRCDLSISGGKDISQVENPLDMISTLDELILVNDLQKVWSALNSTSSGPKIIDIIFDNSGYELFSDLCLAHLLVKLGLANKIRFHGKRVPWFISDVMEHDFHWLIQEMANQTRAPCLSKLSTMWKDFLSSGTWTYLTESFWTLPYSYDAMKQIDPELYNSFEGSKLLIFKGDLNYRKLVGDVFWPHTEKFSVALRGFEPAPLVTLRTIKADVVVGLQPGQAEKVAQKDTDWLVTGKYAVVSCLVK | Function: Metal-dependent phosphatase that shows phosphatase activity against several substrates, including fructose-1-phosphate and fructose-6-phosphate. Its preference for fructose-1-phosphate, a strong glycating agent that causes DNA damage rather than a canonical yeast metabolite, suggests a damage-control function in hexose phosphate metabolism. Has also been shown to have O-methyltransferase activity that methylates glutamate residues of target proteins to form gamma-glutamyl methyl ester residues. Possibly methylates PCNA, suggesting it is involved in the DNA damage response.
EC: 2.1.1.-
Catalytic Activity: L-glutamyl-[protein] + S-adenosyl-L-methionine = [protein]-L-glutamate 5-O-methyl ester + S-adenosyl-L-homocysteine
Sequence Length: 443
Domain: Subfamily III proteins have a conserved RTxK motif about 40-50 residues from the C-terminus; the threonine may be replaced by serine or cysteine.
Sequence Mass (Da): 50750
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A0A6P8YJ95 | LAVAADALADTQGSSSPRSHYWAKDQLRSQPGKPPPLPPWSSSESSSESSSNHSDPSVPYSASPLHSVHSLVQSLNGTVQGRQLIPLLLVEGGVEASAAASTALDGDYLLGYSHNPWGRSSAFRDVLDDLGSATTQVSAAKPGKPAQRRSRRSVLHLYNMLVCSTGCDPMAYKGYGCYCGFLGSGYTTDGIDRCCKMHDWCYDTASCPMFLEYFVPYLWKCYRGRPLCALNGSACSQRLCECDRRLAECLRHYPCPRRKAVCTSSPWRLLQNLFML | 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: 276
Sequence Mass (Da): 30219
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A0A942KM26 | MITEVISGHIVFAILSATSIAGAAVVVLTRDVMRLTLGLGAFFLSVAGWFLYFGHGFLATAQVFVYAGGVLVLILFAIMLLGRSEEGAPRLHSSHAIDSAVVSLGVGLLIVFSLLGVVPAVLLPDGSAHSRPVTDWLLGPFLPHLLASGLLLLVAVVTVIVVLGGERE | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Catalytic Activity: a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+)
EC: 7.1.1.-
Subcellular Location: Cell membrane
Sequence Length: 168
Sequence Mass (Da): 17480
Location Topology: Multi-pass membrane protein
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A0A6C2C379 | MNKHRVETFTDAIIAIITTIMILEFKVPDTFKLHAIIEELPALFAYGSSFFFILVAWYNHHYLFSLANRISKRIYWINNLWIFTMSLLPVATAWVGRYINKPAPELFYFFIFFIWSITFLLLAKAIANELSKVDLNAAQKIIAMPAVSFLNSKLLTVLTFCTLVITSFFPLFLIIMTVGELIYMAVRTPADGDQLDRQ | Catalytic Activity: K(+)(in) = K(+)(out)
Subcellular Location: Membrane
Sequence Length: 198
Sequence Mass (Da): 22847
Location Topology: Multi-pass membrane protein
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A0A2D4M3I8 | RGIYPPLVTPFTSQGRVDYAQLQDNLRLYAEIPFRGFVVHGSNGEAPYLTQEECLEVVMRVHQAVPKEKLLLVGSGCESTYCTIEKTKQIADKGADAVLVVTPCYFRGSMTSAALIHHYSQVADASPIPVILYSVPANTGLELPNEAVVNLAQHPNIAGIKDSDGNITRLGLLVHKTQNEDFQVLAG | Function: Catalyzes the final step in the metabolic pathway of hydroxyproline.
EC: 4.1.3.16
Catalytic Activity: (4R)-4-hydroxy-2-oxoglutarate = glyoxylate + pyruvate
Sequence Length: 187
Sequence Mass (Da): 20332
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A0A960BPP2 | YAQAQAGTMTSDAPTPEPAAVATAPDTLTHGSVVIAAITSCTNTSNPSVMLAAGLVAKKARARGLKAKSWVKTSLAPGSRVVTRYLEEAGLLEELAAVGFSLVGYGCTTCIGNSGPLIAAVGKQVAAEDLHVVSVLSGNRNFEGRVNAQVKSNYLASPPLVVAYALAGTVDLDLTQEPLGEDADGRPVHLADLWPTPQEVADAVRQAVKPAQFADE | Pathway: Organic acid metabolism; propanoate degradation.
EC: 4.2.1.99
Catalytic Activity: (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = 2-methyl-cis-aconitate + H2O
Sequence Length: 216
Sequence Mass (Da): 22234
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A0A2G4G5J6 | MDAQTHDIQNQFAEALNLHRAGQLAQAKDSYNKLLRLWPRHAESLQNLGILYAQEKDFAQAVDCFKRATEADPLNANYFSNLGTALNDLGKPDQSVEFFEKAISLNPNFPDACYNLGNVFQKLGQYAKSIEYYKKTIEFNPAWLEAYLNCGNSYDMLGDFNSALGYYDTIIKINPYFSAAHVNRGNVLLKLNQKELALQSYEIVKKLGLDSFQAHLASAEILQGRGDYRKAIEACFNAIRINPYDTQAYYVLGINYFNIRDLNAAVDNFKNAINLKPDYAQAYNGLGVCFVKAVHFAEAQINFKKALELDPNLIIARINSADAYYASGDIVSALAQFQKLPPDSQPVGLMQFFKQRLADWTNYQADYDNFINRLDQPRFLNSMEDPWHMQRITDSPELAKRVAENFVKTSGVVIQEHKTSAVRVKNKKIKIGYFSSDFREHAVTHLALQLFSLHSRDKFEVYAFAFGKNDGRPALRERIEKSFDHFININDKNDLDAAQMVRDLNIDIAFDLSGITNEARPAIFLNRAAPIQVNFLGYTGTLGTPYHDYIIADPVVIPVESRVHYTEKVVHLPCMMPFDTSHDLSKIKFTRAEVNMPPEGFIFCSFNQCFKITPETFDSWMRILKRVPGSCLWVSAPYEPQAITNMKKEAEHRGIDPARIIFAERMREVDNHLARISLSGLFLDTFPYNAHTSAIDTLWAGVPIVTRMGRSFASRLAGSLLKSIGLDDLITNSVQEYEDLAVDLAMHPEKLKKYRKLLQDNRSTHRLFNMNLYAKNFEKALIEIYNKQQAGLPPDHIVIE | Pathway: Protein modification; protein glycosylation.
Catalytic Activity: L-threonyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-(N-acetyl-beta-D-glucosaminyl)-L-threonyl-[protein] + H(+) + UDP
EC: 2.4.1.255
Subcellular Location: Nucleus
Sequence Length: 800
Sequence Mass (Da): 91084
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A0A931QCJ1 | MDERPEDQDQTTERVVAPAEGVRIIGAEEAADALERGDADPRLPEGAPRYGDRPSDPPRDQRPQARFPLSDPDGLDAVRAAGTAAPVLPPWTDPPTGEVPRVFADSRDESHSSSASSGDGDVEDDLDAWMGVTGAPRWRDHPNDWDEPDYLDLVAKEDDPLVASSEQPIGVRSDSVGGEIENARSSAQPDFFSAAFDPEPDLPTSTPHRAAAPRVARGVSTVPGRSGETGGRPSGGTGGRPSGGTGADRVVNGYATNDDRSGEADMRVRVITGLGMALVALVLFSMGPAMALAAVLVVLVAAAAEFYGMLRNGGYQPATLVGLVATASMVLAAYWKGTMALPLVVALTVVTTLVWYLMGVTGGAPTLNAGMTVLGVGYVGVLGSFAALILRFDNGVGILIGLILAVVANDVGALFTGRKFGRTPLAPHISPHKTREGLIGGSLGSIGASVLVLGMVGLHPWSISSALQLGLLVSVVAPLGDLCESMIKRDIGVKDAGHLLPGHGGVLDRFDALLFVLPAVYYLCLLIEVF | Pathway: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 3/3.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphate + CTP + H(+) = a CDP-1,2-diacyl-sn-glycerol + diphosphate
EC: 2.7.7.41
Subcellular Location: Membrane
Sequence Length: 530
Sequence Mass (Da): 55128
Location Topology: Multi-pass membrane protein
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A0A2H0NMG3 | MKYLVLFSALAGVLLLYLLASASGNTELYSQNYAALLGLTGSLALGLLLLVLYQIGQLYGKLKRRVYGAKLTLRLAAFFSLIAVLPGLLVYAVSVQFLQKSIESWFDVRVEKALEGGLNLARSTLENGLDELEKKGRFVALVLAEQDPRRHAATLNRFIAEGLTQKAAVFDRKGNLLAHAGDARPAIGPLKESIDTAWQVGKFRRIDALPNEQLTLQVLLPIRSSRWQTPRLLQFTQPVSAQMASDAEVVRAVYGDYQQLSLSRLGLKRLFGITLTLSLLIVLLSALSAAFYFSARLSAPLAALASGTRAVAQGNFSGNYPVYGRDELGGLTVLFNQMTAQLASAKQLNEEQQQQVADAKAHLESVLAHLSSGVLVVDAQAVIRSANASAGRILEIGEEALNGQSLPTLAQAHPLLRPFIESVQQGIATASGSVWQRQMERMSKNGEQVLLLRCNILGAGGQFSHVLVFDDISHLLQAERQAAWGEVARRLAHEIKNPLTPIQLSAERLQHKLSAKLEQQDAQLLQRATATIVSQVAAMKSMVSDFADYARVPAAQLAPLDLHALLREVTGLYEANSSPVTLRLQASRARIEGDATRLRQVVHNLLQNAHDALQQTADPQIVLATEDAPHNMLCLSVTDNGSGFTEHFLAKAFDPYATTKPKGTGLGLPIVKRIVEEHGGSISIQSTQSGGARIAILLPLLQQKTEMSA | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Cell membrane
Sequence Length: 709
Sequence Mass (Da): 76858
Location Topology: Multi-pass membrane protein
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A0A960GFB7 | MSEQMHIRSYQGRPGRMSPRLAEIWAQRGPELRLPASRWQLAPVDRVVLEVGSGMGASVIGLAAAEPSTTVVALDVHVKGLARTIRDADVLGLANVRIFEGDALIALEDYVPAGSIAAINVWFPDPWPKRAHHKRRLLRPAFVTAAAGALRDGGHLNVASDIPEYVRWVRDLMRSSGDFRPEGEDGVVPRPTSRSLTKYESTAHQEGRTVTDLSYRRAARADTAAPPG | Pathway: tRNA modification; N(7)-methylguanine-tRNA biosynthesis.
Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
EC: 2.1.1.33
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
Sequence Length: 228
Sequence Mass (Da): 24885
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A0A7W6NKH8 | MMTMKPARWAFLSLLLLAQAIPASAGPLPVPKSTADIAGPLMAVTHWRGFYRVRGVYFYNGYRGIVVARPGYRFYRGYWFPPAAFAAGVAVGRSTLPDVPGRLNAHMRWCFEHYRSYRASDNSYQPHIGPRQQCRSPFA | Function: Has immunoglobulin-binding and hemagglutination properties, and can bind to mannose. Essential for virulence. May be involved in LPS biosynthesis or polysaccharide transport.
Subcellular Location: Cell membrane
Sequence Length: 139
Sequence Mass (Da): 15699
Location Topology: Single-pass membrane protein
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A0A938DZQ3 | MTVTPGSAPELVELLEHAREIGLLGPGPIGKHLAHASAWASALGPFGGRLLDLGSGAGVPGLILALAWPDCEPVLLDASRRRVAWLRHSIRKLSLEDRAVAVAARAEMAGHDPRYRERFDLVVARGFGPPAATAECGAAFVTPGGRLSVSEPPGEAPGRWPEGRLEDLGFGPASRVVHGRASFVILPKRGAIAERWPRRNGRPHRRPLW | Function: Specifically methylates the N7 position of a guanine in 16S rRNA.
EC: 2.1.1.-
Subcellular Location: Cytoplasm
Sequence Length: 209
Sequence Mass (Da): 22356
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A0A835KKX6 | MTSSHPSFFPIRTGDRNVFGQVVLGGGVMRNRETPVLSLSLLWDDARFCQRLAASINALRCVLCRPDVPMPPPIYIQIGGARDMHASNREKSKQASARSSRMRVKVELVVITMTTLLLLACRGSHGYAASAADIEEELPPAWAVPHLRRLLARHKVDAVVDVSTRGGHHYGSIAEALAAAPPPPGRYTVHVRAGIYREPINITRSDATLIGDGMGPVSGDGFMARDLTLQNTAGVSAGPAVALMSMSDQSVYYRCELDGYQDTLNVDCKRQFFHSCRIMGTVDFIFGYAKAVFQECQILVRRSVDGKDNVITAQGRDGPDNQSGFVFQRCAVKALPGDHLDTTTTKTFLGRPWKKHSHVVFMRCALDSIVNPGGWLQWNATTPVPDTVYYAEYRNTGPGANTQGRVKWDQLHLLKEPAEVANFSVHNFIQGDDWLPRFGIIYDQE | Pathway: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 1/5.
EC: 3.1.1.11
Catalytic Activity: [(1->4)-alpha-D-galacturonosyl methyl ester](n) + n H2O = [(1->4)-alpha-D-galacturonosyl](n) + n H(+) + n methanol
Sequence Length: 445
Sequence Mass (Da): 49099
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A0A938JD76 | AVFAVLVSTLITGTFHLDGLADIFDGLVGGWNIEDRLKILKDSRHGTYGVVAIVIQIILQISLIASLNSKDGALALIAAHTIAKVIPVILMLIPAVSTHQGMGASTAREIRFPQVSLNIFIAAIFTIPFCGYYFFTILLALVIPLFIFSKWIINKIGGMLGDAFGAGEQIAETVILLFFVLNFSIYGVILWNF | 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-ribazole 5'-phosphate.
Catalytic Activity: adenosylcob(III)inamide-GDP + alpha-ribazole 5'-phosphate = adenosylcob(III)alamin 5'-phosphate + GMP + H(+)
EC: 2.7.8.26
Subcellular Location: Cell membrane
Sequence Length: 193
Sequence Mass (Da): 20956
Location Topology: Multi-pass membrane protein
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G3JA65 | MKAAQIKAEQLSSNTVEATQESRLTSDFGTKQSNTDDWLRVANDDKTGPSLLEDAFGREKIHRFDHERIPERVVHARGAGAFGTFRLFESAEDVTHAGVLTDTSRETPLFVRFSTVLGSRGSADTVRDVRGFAVKMYTDEGNWDLVGNNMPVFFIQDALKFPDLIHAGKPEPDGEIPSAQSAHNNFWDFMFLHSEATHMFMWAMSDRGIPRSYRMMQGFGVNTFTLVNASGKRHFVKFHWTPALGVHSLVWDEALKICGQDPDFHRKDLMEAIASGAFPKWRFGIQTIAEGDEDRFEFDVLDATKVWPQDLVPIRYIGEMELNRNVDEYFTETEQVAFCTSHVVPGIGFSDDPLLQGRNFSYQDTQLTRLGVNWQELPINKPVCPMMNFNRDGAMRHRISKGKFNYWPNRGGVQPPAAADSEGGYRDFPQNVAGVKVRGKSAKFKEHISQAQLFYNSLAEIERKHLQAALAFELDHCDDPVVYTRVTRRLAEIDPALGQTVAHMVGGAAPPAPERKNHGNKASGLSQLEYVPAKVTIESRKVAILIADGYDGAAFAAMLGALKAAKAVPVIIGPRRAAIFAAGEDHSSSAGVVPDHHLEGQRSTLFDALFVPGGANAITQLASTGRAVQYVREAFGHLKTVAATGEGVRLLHKAIQLDQVTLSAGAEAVSSYGVVSLERPGPDGLGEVLQAAKNATRFLDQFVYAVSQHRCWERELDGLVDLVAY | Function: Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide.
EC: 1.11.1.6
Catalytic Activity: 2 H2O2 = 2 H2O + O2
Sequence Length: 725
Sequence Mass (Da): 80046
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G3J3S1 | MRARYKWPGGTGIITIGDDATLGDVVKELTAKTLLTNFGIKFGPPNAMKALDMNRTDQTARDLGLHGEMLTLVPHNERRSSSRQSISAERSLRPESERSQKMGSHDVKVPWSARDGTLSFGGALPQQVLPSKLRQMMADYIQEHADVYSEAILGVPPQQYCQAITDPDRWGGGIEEEVSDQLQTQNIISFGEGKRDQCILVYSGIHYDRIAFSYSEYPYTDAMLPPEMDRTTWPVEDEEVLTKAAELVGKLHGAHYFTNMDGLVLKCDVDGCGWIGSGQAEGQRHAEETGHTQLSEIVDTQTDAILRKCNMRGYESADCPSLPTRGSVFRACSSIPADSGRTVGLLILVVICRRRLSNSVYQHSNKGNTREDIKAKSKAK | Function: Hydrolase that can remove conjugated ubiquitin from proteins and may therefore play an important regulatory role at the level of protein turnover by preventing degradation.
Catalytic Activity: Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
EC: 3.4.19.12
Subcellular Location: Cytoplasm
Sequence Length: 380
Sequence Mass (Da): 42039
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U4UEN1 | MGSESDIPSWYAGQSIFVTGATGFMGKVLVEKLLRCCPDVSTIYIVIRHKKGRNSSQRLEDFWNSPVFDKLRDSQNSETILNKLKCLSGDVVHPNLSLDEDVIQELEHNVTVVFHMAANVRFDQPLKSAVLLNTGGTLNVLDLACRFKKLKVFVHTSTSYCHCDETRLEEKLYPAPHNPRHILDLAKWMDGDLLKLLTPKLLGNSPNTYAYTKCLTEQLVSEYQSKLPIAICRPSIGFEAVVYGNFFLTFRPQLRWTLSKAMRQWAKFNCWIPRRIYAVCAHAWGMGGGSNASAHMLFGAKRAFNLD | 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: 307
Sequence Mass (Da): 34733
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A0A4Q7DKR1 | MLLEKDVAIIGAGPVGIFTVFQSGMLGLSTVVIEALGAIGGQCTALYPEKYIYDIPGYPSILASDLIDSLYQQSKPFNPTILLNSTMVGLRRRDDAFVIRTSKGEEIAAKAIILATGAGALHPKPLSLDNAALYEGKSLFYAVSKKEVFRDKTIAIFGGGDSAVDWTNSLADIAKKIYVIHRRDKFRALPDSVEKMYQLVKQGKVEMAIPYQLDQIYGQDGYISSVDLIDFDRNVKNLKIDAILAFFGLSMDMTFITSLGLDVSNKYINVNPISMETNLKGVYGVGDAVTYPGKLKLILTGFAETAVACHAAHAIIRPGATLRFGYSTTVLKDILK | Cofactor: Binds 1 FAD per subunit.
EC: 1.18.1.2
Catalytic Activity: H(+) + NADP(+) + 2 reduced [2Fe-2S]-[ferredoxin] = NADPH + 2 oxidized [2Fe-2S]-[ferredoxin]
Sequence Length: 336
Sequence Mass (Da): 36537
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A0A1V4MLR0 | MNAHFKRWLTAFIAVPLLILIIGYGSELIFALFIAAVITAGIIEYNTMVFEKDRRTERCLTVVIALLIAASAFTGDRSFMMATVTLSIPAVLAMRLLRTDSGGSSLKNTANIFFGVLFIGVTMSHFILIRMDGCGITWIFFLIVMAFSSDVAAYYVGRFMGRRKLLPSVSAGKTVEGAAAGIIGCMMACVIFEALFLPGMGAGHAAAMGFLGSIFGQLGDLSESAVKRTFNVKDSGFLIPGHGGILDRLDSFIFMAPFVYYYKQFFLII | Pathway: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 3/3.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphate + CTP + H(+) = a CDP-1,2-diacyl-sn-glycerol + diphosphate
EC: 2.7.7.41
Subcellular Location: Membrane
Sequence Length: 269
Sequence Mass (Da): 29252
Location Topology: Multi-pass membrane protein
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H5ZWM8 | VLHDRYYVVGHFHYVLRIGAVFAIFRGFHHWFPMMRGIGLHPVWSKGHFWSIFISVNVTFFPHHLLGLAGIPRRY | 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-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
EC: 7.1.1.9
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 75
Sequence Mass (Da): 8917
Location Topology: Multi-pass membrane protein
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A0A2A4PGN2 | MDTPTINNHFSSGISLVTRASQILAIIITFGLGGMISSILISENINDKAKIINQVSAFGITASALLNTQVNDSSTSTIQNIQEAQQQLDGIYSITRSEIKSDAKYASLLQKVKKDWAEIKSNNFSPMRVQQFTKSLQGLINHLQLIIKKEIQLLRIIQYTGFFSIILISYIAVYSLQNRVIHPLKRLLQVAIEAGNGKFNLRADETAKGELGLLAKTLNDMSQQLSIRYQDLERSVTHKTIQLEQKNRSLNILYRSSHNLSKNIHVHDINSLITELEATIGTGNIFLKLTDSNLIQNEPRHIQPPLNIRHQYPINKEKHHFGDLIWETEQQINPQPWQDELLKAMANLFASFVDLQNKRHANSRLEIMEERAVIARELHDSLAQSLSYLKLQTSLLNKQVEKNTPRAEQLATLQEISRGTNLAYGQLREILTTFRLKLKGISLENSLKETIDEYINKCHHPISLEHHLQHNALTPHQEIHLLQIIREALSNIHKHAQASHASITIHQYNDTVVVDINDNGKGMLTNLPDEGHFGIKIMHERAKSLHGELKVSSNQPSGTHISLSFQSVSNK | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Cell inner membrane
Sequence Length: 571
Sequence Mass (Da): 64608
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A0A5P8N5U9 | MAHIGKIKNIIMAAIVVLTFASVAYSPMSGVLGASIVMMVAVLPQETQVDRVLEDESPVHEAEGIYRVYEHIGPWSFLKGVATITGGSIVSSLHVTGNRAVWVEDRLYQPSVIQPTDDFIAWGRPPVIKPLKEDDEVVALALHPISNTILPLRSRTARIQGNTIYQLARTSPGVSGSPLFVVDTTEEGTTTFALAGTIGRSIRSGPNKQFEIQSHLPLPTVPYDTILKAGMVLQLFSHPGAGKTRAMPEYVRQLMTWSNKVYVAGPTRVVAREMLESLQATKWVCAMIKGLPRPHALARVVVTTHQTLLRYALTSGLLASRDISYVLDETHVDSAHTKVLRALVHQSVSKEKSKAACIEMTATGRDEATGEQKVSMGSNYPITDRTYSTNVSTAVRDYAARNGPKRIAVFVPGLTGRNGALQVAKNIRLTTHYTTVVLSRKTYDTNINSVFKTYPNGLCIVTTSISECGANYDLDAVFDTCQQYHYLVTPTGTKGVITASTQAQTCQRRGRVGRRREGEYYRPVGYDITQAPVLDHPDSVTLLEANMCLIALGLPEIEAGQAVKKALEKIQPSKEQVYKWLTDQERETLTEIMAMYSTEGNRRSREQERTVRNQMRGSFNDARWETKDPVDEQLPVTPGDYIRDDEGEATISGAVMCRPPPLTELG | Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 666
Sequence Mass (Da): 73348
Location Topology: Multi-pass membrane protein
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A0A0R0LU23 | DKKSSIQSIDDTLKGKITDINVKDTIRYRPLPLRTVDMQKALSRFMSSDSLMKIAEDLYTRGIISYPRTETDCFDKTFNWRQTLQNVTRSVNDHTTGNNDLFTENTTTMNGISMNTITVNGISMVWNGPRKGKNNDFAHSPIYPLKPFHSDKRDEQLVYNYIKDRFIACCSEDAIIEECRVKMAVFKGQFTEYFTCNGKRVKREGYLAIYKHDRVNEQRIGNFIQNEVFVIKYSSNYQDSEQTALNSEHTAFNSQNREVRNHYSNNESEHRGTRNHYSNNVSENTAFNSQNRGTRNVLFMKKSQTQPPSHLKEPDLISLMDKYGIGTDATIHEHIKKILIRNYAFKKNGYFLPSYLGRNLILFYKRLNLNLDKPVFRADLEKKLKRIENGEILRSNVISEEIEMYKRFYRVIEGNIGTFSENLSGDTGDFGGNGFGGDGFGGNGFGGNGFGGNSTGGSNTGSFGGHPFKKRKKTEQAIVQPPGHGNQRGNHSNESEENRPYNRNRDKTRNHQSRDKTRNHQSREKTRNQNETSTLKISYEDCDTNVQCNCREPALIKIVQKGKNKDKEYFGCKNNNCQFFKWKGIQNLVDQHGPSEIKCQCGDITRKMVSNT | Function: Introduces a single-strand break via transesterification at a target site in duplex DNA. Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand.
EC: 5.6.2.1
Catalytic Activity: ATP-independent breakage of single-stranded DNA, followed by passage and rejoining.
Sequence Length: 612
Sequence Mass (Da): 70238
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A0A3G1XAG9 | FIFGAWAGMVGXSLSIMIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMMGGFGNWLVPLMLGAPDMAFPRMNNMSFWMLPPSLTLLLASSMVENGAGTGWTVYPPLSSSIAHSGASVDLAIFSLHLAGISSILGAVNFITTIINMRSFGITFDRMPLFVWSVGITA | 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-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
EC: 7.1.1.9
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 173
Sequence Mass (Da): 18590
Location Topology: Multi-pass membrane protein
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A0A4R8DQX0 | MTKARLESFSDGVFAISVTLLVLNIHIPGTEAKTNADLVKAIRNSWPNELTYIFSFLVVGVFWVAHQRIFAYLRYVNHFILWANIFYLMSIAIMPFPAAVLAMHPLFPSAIVLYCGVLFLCASEHYIFLLYIHRHAWLREPSYNPGENRWTLAVAGVGPLCYLLAAICSGFCPLASFCFIVVALFFYIVVVYFLTKRRPTEK | Catalytic Activity: K(+)(in) = K(+)(out)
Subcellular Location: Membrane
Sequence Length: 202
Sequence Mass (Da): 23025
Location Topology: Multi-pass membrane protein
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A0A966YKN5 | MRDTVELRDTAIAVFALGTVPRKTEKLGEGRRDVVVTFGGATITPGDTVYADPDGVVVLTR | Function: Catalyzes the aldol cleavage of 4-hydroxy-4-methyl-2-oxoglutarate (HMG) into 2 molecules of pyruvate. Also contains a secondary oxaloacetate (OAA) decarboxylase activity due to the common pyruvate enolate transition state formed following C-C bond cleavage in the retro-aldol and decarboxylation reactions.
EC: 4.1.1.112
Catalytic Activity: H(+) + oxaloacetate = CO2 + pyruvate
Sequence Length: 61
Sequence Mass (Da): 6504
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A0A397I024 | MLIYPLFITDNPDEETPIPSLPNQHRRGLNRLVTFLKPLVQKGLRSVILFGVPLHPTAKDALGTAADDPSGPVIQAIRLLRSRFPNLYIVTDVCLCEYTSHGHCGILREDGTLDNAQSVDRISDVALAYATAGAHCVAPSDMNDGRVRAIKLKLIEAGLAHRVLLMSYSAKFSGCLYGPFRDAAGSCPSFGDRRCYQLPPGGRGLARRAIQRDVGEGADIIMVKPASSYLDIIRDAKELAKDMPIAAYQVSGEYAMIHAAAKAGVFDLKSMAFESTEGILRAGAGIIVSYFVPEFLDWL | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 1/4.
Function: Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen.
EC: 4.2.1.24
Catalytic Activity: 2 5-aminolevulinate = H(+) + 2 H2O + porphobilinogen
Sequence Length: 299
Sequence Mass (Da): 32463
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A0A965E4Z0 | MKVLIWTFVYPFLVVIITFFLGLFLALTINHPKIKPKKLYRILLIVPYAMPGVLSILTWKGMLNESYGIVNKLLPGTVPWLSDPWWAKVAVVLVQVWAGTPYMFLIATGAIQALSPEVVEASEVDGASPRQVFWNIKLPLVVIALTPLLIASYAYNFSNFGSIYLLTGGGPVMYDSGGVAGYTDILISYTYNLAFTAGKGRDYGLASAVSFINFLIVAVISIQAFRRSKQMENIN | 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: 235
Sequence Mass (Da): 25952
Location Topology: Multi-pass membrane protein
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G3JCK1 | MSTKSSFESYPMPRFLLPQGVGDTEEVENYEPGGFHPVHLGDTFDDGRYRIVHKLGAGGFSTVWLARDEKDKKWVALKIVAARHSVPTAEKSSLTHAMLPVDGKQRVVVHRRQFTFDGPNGHHLCLVLPVLGPSMSELSYHWNCRLTPWMARKTAYQAVRAVADLHSQGLCHGDVTTGNLLLGMVDIDHYEEDDIYALFGKPVTGVLETENGEMPGPEAPRYIVRNIDFLSAPSDILELDIKLMDFDQCFPISSPPSKMLGTPVDFLAPEVAMGLEAGPASDVWALGCCIFRLRAGDGPFSSPFEVTCPCDLVGFVLDTLGGDVPHTCKDTLWDSRGMPTKDASKGKPLREPHADDRRPLRDLVYKIWDEPNGRAIHTGSPEEQKVYLEDRHQPFHSSWSKMAWNPRAIRVDDVGYLSGYNDRWDTLLALLPKIPDREAALLYDLLLTIFVYDPARRPTAKELLEHPYFHLDGPEE | 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 N6 group of A37. BUD32 has ATPase activity in the context of the EKC/KEOPS complex and likely plays a supporting role to the catalytic subunit KAE1. The EKC/KEOPS complex also promotes both telomere uncapping and telomere elongation. The complex is required for efficient recruitment of transcriptional coactivators.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
EC: 2.7.11.1
Subcellular Location: Chromosome
Sequence Length: 476
Sequence Mass (Da): 53299
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A0A0H3KSU4 | MVIMIKLFSKYFSVGILNTLIHWGIFSILYATGSSQTLANFGAFCVAVTFSFFVNAKWTFNAEASTIRYMIYVLFMGSVASLVGWISDKSMLQPLYTLIIFSFISLICGFLYSKYIVFRDAR | Function: Involved in O antigen modification. Involved in the translocation of bactoprenol-linked glucose across the cytoplasmic membrane.
Subcellular Location: Membrane
Sequence Length: 122
Sequence Mass (Da): 13858
Location Topology: Multi-pass membrane protein
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U4KVZ2 | MPRTRPNIVITGTPGVGKSSHSLLLSESTGLNLVDVNQIVKDNKFTEEYDEALQTWVVDEDRLLDEIEPQLEQGGNVIDWHVCDLFPERLIDLVVVLRCENEAKLQENLDAEIMQVVLDDAREGYDENIVVELRSDSSDDIDTNIERITQWYENWQKDHPEGV | Function: Broad-specificity nucleoside monophosphate (NMP) kinase that catalyzes the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates. Has also ATPase activity. May be involved in rRNA maturation and transcription regulation.
Catalytic Activity: AMP + ATP = 2 ADP
EC: 2.7.4.3
Subcellular Location: Cytoplasm
Sequence Length: 163
Sequence Mass (Da): 18691
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A0A5B9EM08 | MTGEVVVSSENWGHLPDGQPVELFTLRDGSLTVQTSNYGARIVAIRAPDRSGRTGNIVLGFPNLEPYLEPRNSVMGATVGRFANRIAHGRFSLDGMEYTIPINNNGNALHGGTVGFNKKVWSPRIVKDGVEMSLVSPDGDMGFPGSLSVQVTFTLVRYRHNPALVIQYRATTDRTTVVNLTNHAYFNLSMSGQEPVFEDIAWIDAAHYTPTDATSIPTGQIESVHDTAFDFTTPHPIADKIPELGYDQNFALNSHRRSSPNAEVRDQKSGRTLQVITDQPGLQFYVPRFPTPPAGAQRAGIAAFCLETQHFPDSPNRTNFPTTTLRPGQIFRSQTVYIPTVDTKH | Pathway: Carbohydrate metabolism; hexose metabolism.
EC: 5.1.3.3
Catalytic Activity: alpha-D-glucose = beta-D-glucose
Sequence Length: 345
Sequence Mass (Da): 37981
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A0A942NQM8 | MSILNKIKIFIYHCVAFVYAMALAIKRKASSGNAIPEQIDEYFLPDTEGGFTNLADSILIYAATVGELRAASVFIQKMRQAWPNCNLIIVPGQRQYAQTFFETHPYARVMIEFPSAPAVTDQFFRQNRIKFCVFVEGPSLHGYFPIRQDLSLPVGCLKHQVPIVIINACLYKKQLHSRIDLLEHRLFSGLFRLSVKHWYVPTAEICADLRKHQISKQNISVVGDIKFDNVFSDGFQPSANQELEAYIHGIGSNNRMIVAGSVNAFEEQKALVLAWLHTRSSISDTVLILAPRYINDKNMMARLTQFLRDRGIEYALRSESISAAGNKQLIIIDTFGELAYFYKQANIAFAGRGHGVLEPMKYFKPVVVGPHECWTKENSTSYLLYQEMRENQALIECSSYAELGGLFLKMLEDTAFGEAYVQRYMRVIKGKMGASEKIIDHMSNFLNLQSGAN | Pathway: Bacterial outer membrane biogenesis; LPS core biosynthesis.
Function: Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of 3-deoxy-D-manno-octulosonate (Kdo) residue(s) from CMP-Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A.
Catalytic Activity: CMP-3-deoxy-beta-D-manno-octulosonate + lipid IVA (E. coli) = alpha-Kdo-(2->6)-lipid IVA (E. coli) + CMP + H(+)
EC: 2.4.99.12
Subcellular Location: Cell membrane
Sequence Length: 453
Sequence Mass (Da): 51316
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A0A364MY47 | MTAPTHLDPSELGTKSYWDAAYDTERKNFAANACDEGTIWFSDAGAEERMLSFLEDVSDEGHIQKGGEDDADEPGARFLDLGTGNGHLLFALREDDWCGQMVGVDYSAQSVTLASSIRDAKDDSYADIAFHEWDILSQPPGAWLGDGFDVVLDKGTFDAICLSQEQDAQGRRICEGYREKVEPLVKRGGRFLITSCNWTEEELKGWFGGGGLEFDGKVKYPSFTFGGKTGSSVVRKLAPLFLAVEVGSPQFQLSVFGITIQDNGVGIFAVLVLQIIADGPTKRGTKDVLGGEGPVDRTAEVDEGGQAHRRGGLVYCGEVTKCSTRYGTLLGSTLFQSFVSGIVAFRVLPRPQFSTLQKHTFPVYFALQTAAPVAMLLTYPRGGATALLPSFLLPSSPASPAPAFSFFAPASTSRSTNTLAMWLHATMAVTALVNWVYIGPKTTEVMGLRKHQETRDGKRSYDNGPHSKEMQALNKQFGILHGVSTVVNLIGLGAMVWYGAVLADGLSL | Function: S-adenosyl-L-methionine-dependent protein-lysine N-methyltransferase that mono- and dimethylates elongation factor 1-alpha at 'Lys-316'. May play a role in intracellular transport.
EC: 2.1.1.-
Subcellular Location: Cytoplasm
Sequence Length: 508
Sequence Mass (Da): 54901
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G7UU44 | MKDAIAAIARGEMVIVVDDADRENEG | Pathway: Cofactor biosynthesis; riboflavin biosynthesis; 2-hydroxy-3-oxobutyl phosphate from D-ribulose 5-phosphate: step 1/1.
Function: Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate.
EC: 4.1.99.12
Sequence Length: 26
Sequence Mass (Da): 2789
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A0A6P8Z4X4 | MFSRFKDFVNRHRRKFIVTGVVVGGTWLALRYAQRKLREYTENEAKEFIERNRRQQHFKSTERTCDQTILSLSPAIHEAIINCVNTEELVTELQTATTGKYGIWERLKVRAFTRIAALVYANSMLVLLLRIQLNLVGGFLVRDANGEGVLSTELQHLYLSLCHHLRDTGIIDLCSLIERHVQPIMENISLKKQMSLRDTEELFWSIQNSVESNMYENPIKSMAKFCIPSKENTDTGCLQEQEVQQLFNIISETSDLLESDEAASLMRSCISQSFAGVIDKLADQFAPINHSEPAPGPSSDKVADAWTSAVNGSAKSSFVHPSNVTMPLAKLIPIVNKMTELSPSKKDLWMYQLVRNDLVKVFGANVYEAFGQLE | Function: Involved in peroxisome biosynthesis and integrity. Assembles membrane vesicles before the matrix proteins are translocated. As a docking factor for PEX19, is necessary for the import of peroxisomal membrane proteins in the peroxisomes.
Subcellular Location: Peroxisome membrane
Sequence Length: 374
Sequence Mass (Da): 42365
Location Topology: Multi-pass membrane protein
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A0A6P8Z7W4 | MATIIKSMVKGYNFLFYDIGNPETRDWLLMSSPFPTLAIMGIYLWFVNDYGRKMMEYRKPFKLDRIIQVYNAIQIFLSSYTCYKLLKHGWYSRYSWQCAPVIFELEDPDDYAMASMMHLYFITKIVDLLDTVFFTLRKKYNQISFLHLYHHTGMVALGWGAVNWFTTGHGTMLMTVNSAVHTILYSYYLLTSISPQYGNTWWKKYITKIQLLQFLFLSIHFGKLVFNNPCNFAPFGLMIIIPQNMFMFILFSDFYYKAYMRPKPVKASNVMQRLWEWQHYHFVEKVDPRISSYPLFGPSLGLGPPWGLFGIVAAYIYFVKFLGPRLMENRKPVELRRIMIAYNAMQVLFSGYTFYESFVAGWGGRYSWFCQYLGPDDYTPMDIRAARCSWLYFFSKIVDLADTVFIVLRKNYKQLSFLHVYHHAVMVLGVWYGIAYSPGGHVTFVGFLNTFVHTIMYSYYLATLLFGTKSFNFLKKWITRMQLLQFLGVFVHSAQVLFQPSCRVDRSNMVFLMIQSVIMTALFSNYYYHAYVKKKHQA | 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: 538
Sequence Mass (Da): 63529
Location Topology: Multi-pass membrane protein
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B8D0S8 | MISALKNAFKVKEIRKKILFVLGMMVVYRIGAHIPVPGIDVVKLREILFQGTAQGVFDYLDLFAGGALRNFTIFAMSITPYITASIILQLLTGVIPRLEELQKQGVEGRKKLTQYTRYGTVVLAIIQAFGITMLIGRHNVIVNPNLFNLMLIVISLTAGTAFLMWLGEQITDKGIGNGISIIIFTSIISRFPSYIHRNWELYKTGDITALNILFFLVLAVVIIAGVIFIQQGERRIPVQYSKRVVGRKVYGGRSTHIPMRINQAGVIPVIFAQAVLQFPTVIAAVLPYGWAQDIATALEPGKPVHLVLYAAMIFFFTYFWTAFTFNPEEVADNMRKSGAFIPGIRPGKATENFLTRILVRVTLAGAIFLTVIAIMPYFISDITRVRISFGGTSLLIMTGVALQTMQQIESQLLMRHYEGFMK | Function: The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Subcellular Location: Cell inner membrane
Sequence Length: 422
Sequence Mass (Da): 47074
Location Topology: Multi-pass membrane protein
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A0A1Q9NUK7 | MVIKRLLLGPLYSIYENNLRRQVTKKDPPQHIGIILDGNRRAAKSLRIPMEIGYEIGSNKLEEVLEWLWDMKVKVVSVWIFSTDNFDRDIDQVSTILNMAEEKTRKIRDDKKIHDRGVQVRYSGDLTRLPKSLRQQIDKTEEATEKYSNHILNVCLAYGGRAEITFAMKKIASLLSNGKLTIEQIDEELITEHLYTNGLPDPDLIIRTSGSARLSGFLMWQSTYSELYFTDVLWPHFRRIDLLRAIRDFQGRKRNFGS | Cofactor: Binds 2 magnesium ions per subunit.
Function: Catalyzes the sequential condensation of isopentenyl diphosphate (IPP) with geranylgeranyl diphosphate (GGPP) to yield (2Z,6Z,10Z,14Z,18Z,22Z,26Z,30E,34E,38E)-undecaprenyl diphosphate (tritrans,heptacis-UPP). It is probably the precursor of glycosyl carrier lipids.
EC: 2.5.1.89
Catalytic Activity: geranylgeranyl diphosphate + 7 isopentenyl diphosphate = 7 diphosphate + tri-trans,hepta-cis-undecaprenyl diphosphate
Sequence Length: 258
Sequence Mass (Da): 30016
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A0A7H4P9V7 | MRTARSCCGQKLREQGSRTEVMSGQQAAAEVAALDEVEQVMAAIVGAAGLVPTLAAIRAGKTVLLANKESLVTCGRLFMEAVQQYGARLLPVDSEHNAIFQSMPEPIQHNLGYADLTQNGVASILLTGSGGPFRETAISELAAMTPDRACKHPNWSMGRKISVDSATMMNKGLEYIEARWLFNASAEQMEVLIHPQSVIHSMVRYQDGSVLAQLGEPDMRTPIAHTMGWPKRLNSGVKPLDFCQLSHLSFSAPDYGALSLPEAGHGGF | Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 1/6.
EC: 1.1.1.267
Catalytic Activity: 2-C-methyl-D-erythritol 4-phosphate + NADP(+) = 1-deoxy-D-xylulose 5-phosphate + H(+) + NADPH
Sequence Length: 268
Sequence Mass (Da): 28879
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A0A927X5R5 | MTTEKLEQSRVKAVFDVTADEFEKALDKAFEKLNANVTIKGFRTGKAPRSAYEKTYGEMSLFDEALNVILNQKAQEIYKDEKLARQICGPFEPNLEGEDRVTRGKDFKVSLSFDVYPEVKLPQYKGLEVKAKVLTATDEEVENAVKNILKKDASKANKEEQVIASGDYAIFDFAGTVDGVAFPGGTAENYELQIGSGQFIPGFEDQMIGMKAGEVKDVNVTFPENYGAADLAGKAAVFKVTVHEVKVESFPELTDEYVQNLKLEGVNTVSELKASKKAEIEAQKAVSEKDRQVDELINKILDNTVVDMPKSLIDDKVNAIRGQYINQAKMYNIPFETFLSLMNIDKNTFEAETLKQGARQALFSVVATKLIEVENLQPSKDALEAKAEADAKASGKTKEAMLKQNLDSYFNQLSYEALINMLLTNAVEVEGEAKPAQKKTTASTQAKKTTASTAAKKTTASTQAKKTTASTAAKKTTASTAAKKTATATKSE | 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
Sequence Length: 492
Domain: Consists of 3 domains; the N-terminus binds the ribosome, the middle domain has PPIase activity, while the C-terminus has intrinsic chaperone activity on its own.
Sequence Mass (Da): 53875
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A0A849XZK0 | MKTFPLEFERPLAEMERHIEEMRARAKANKLDLTGEIAVLERRLAAERRQIYSNLTAWQRVQISRHPRRPYFLDYAARLFTDFTELHGDRIHADDQALIGGFATFHDGKAPWRVMAIGQQKGHDTKENLLRNFGMAHPEGYRKALRLMRMADRFDLPILCFIDTPGAYPGVEAEERHVAEAIAVNLREMFSLRVPIVAAVIGEGGSGGALGIGVADRVLMLENAWYSVISPEGCAAILWKDRAHAPAAAEALCCSARDLLRAKLVDEIVPEPLGGAHHDVEGVARDLKMLLAKHLAALARQPISRLLESRYRRYRSIGVLQAPPTRRARARRGKTAASVSQR | Pathway: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1.
Function: Component of the acetyl coenzyme A carboxylase (ACC) complex. First, biotin carboxylase catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the carboxyltransferase to acetyl-CoA to form malonyl-CoA.
Catalytic Activity: acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein]
EC: 2.1.3.15
Subcellular Location: Cytoplasm
Sequence Length: 342
Sequence Mass (Da): 38319
|
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