ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
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A0A8B6XN40 | MAVKLGVIIPINKRKKIKLPERMLNICKEKNIEVSVLDVNDDNFFETGPFDVLLHKIEDFYNECSPEEALQRTTKVREYAARYPDMIVLDDFDVSMKMTDRNFMTNVIQQACMTIDGITVFVPKIIEIPENSTLEECKQLVSSNFMKFPVLAKPLSASLDQGSHNMVLIFSMDHLNNLPKPCLLQEFCNHSGIIYKIFVIGDHISFCERPSIKDIHQSDQKNDTLYFDTRDVSKTGKAFIPDLHESNPNDRVWLSSDENPNMLNFNVVNAVVKRVKEVCNIHLFGLDILVEKETGNYALIDCNQFPGYTGINEEYLPKYL... | Cofactor: Binds 2 magnesium ions per subunit.
Function: Kinase that can phosphorylate various inositol polyphosphate such as Ins(3,4,5,6)P4 or Ins(1,3,4)P3.
EC: 2.7.1.134
Catalytic Activity: 1D-myo-inositol 3,4,5,6-tetrakisphosphate + ATP = 1D-myo-inositol 1,3,4,5,6-pentakisphosphate + ADP + H(+)
Sequence Length: 330
S... |
A0A258CPD3 | HENTKVEVAWTVIPVLILVVIAIPSFRLLKLQLEVPPSDITVKVTGKQWYWSYEYPQDGGAFTFDSLMLDEKQRAEAIAGNKIAAAEAPRLLAVDNEAVVPVGKIVRVQVTAADVIHKFTVPSFGVKIDAIPGRLNETWFKADREGIYYGQCSFICGQNHAYMPIAFRVVSQERYAAWLAESKQKFANAADAGGKVAAAGH | Cofactor: Binds a copper A center.
Function: Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).
EC: 7.1.1.9
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(... |
A0A173WSK3 | MNRTYIQEVQKEIGNTIKVQGFIENLRNSKYMAFIVLKDITGKLQITVEKEDHPELVDTIDRLTPDSVITVTGKVMENDYVKMGGIEMIPESIEIESIADALPIVRKEIAATKKKKAVERSSIDQRIDYRWVDLRTDENQLMFKAQSCMVNAMRKFLLDENFIEIHTPKLIAAASESGSEVFKVDYFDRNAYLAQSPQFYKQMAMAAGFERIFETGPVFRAEKSYTNKHATEFSGFDLEFSYITSFYDVMKMEEELLKAGLAAVKEAYGEQIKEAFGQEVIVPETPFPVVKLADLYKGLEEEFGYTVDDSEKGDLTTEAE... | Function: Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Catalytic Activity: ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-aspartyl-tRNA(Asp)
EC: 6.1.1.12
Subcellular Locati... |
A0A7C7I0J9 | MFSSKKPLFVADQPAKKPRKWLKITLMVFVVVAIIGAVVGYSQYSSYKTDLEPVDHNNPQTEIFIVEKGDTFSAVATKLEDQGLIRSADAMRWYLRFEAENDLKLQVGAFELNSGQSVEEILSSLVEGKVLQKKLTIVPASTIFDVEAAIVAAGYSEAEAQQALALDYSDHPAFADAPEDATLEGYLYPDTYLAGHLQPPQALLGLALDETAKVLQDPAIRAGIESQGLTLHEAIILASIIEQEVSSASGDRPQVAQVFLRRLEIGMPLGADPTFRYASQLAGVADSVSIDSPYNTRIYAGLPPGPIGAISRSSLQAIAD... | Function: Functions as a peptidoglycan terminase that cleaves nascent peptidoglycan strands endolytically to terminate their elongation.
EC: 4.2.2.-
Subcellular Location: Cell membrane
Sequence Length: 360
Sequence Mass (Da): 39155
Location Topology: Single-pass membrane protein
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A0A3D3HCA1 | MAETQLEDPYINKSGHLAVGDGHKIYYEDWGNPKAVAIMHLHGGPGAGFSESHKLIYDPKIHHVIFHDQRGCGRSTPFAAIKNNTTQHLIADIEKLRQHLKIDKMYVAGGSWGSTLTMLYALTYPQRAEKMMMWGIFLLRRSEIDYLYQGVARHTLPEAWERFISLVPVKDRNSSQDVTNFYGGKIQSKDRKTALKYAAEWNLWESSVVSITYDRRQVEREVLGGDEKQQNFNLAIARLESYYFQNNCFMPENHILKNINKIRHIPAYVVQGRFDICTPPISALDLAKAYGKNLNLQIVAAGHLRSEQEVRSVLRTFAST... | Catalytic Activity: Release of N-terminal proline from a peptide.
EC: 3.4.11.5
Subcellular Location: Cytoplasm
Sequence Length: 323
Sequence Mass (Da): 36895
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A0A967B4N7 | MGREGAIRVSIDDLESVYAGGAPGGREAPGMVPPQDRGAEQSVLGGMLLSKDAIADAAEELNGRDFYFPAHESIYEAIIELYGRGEPADAITVADELNKRGELQRIGGQAYLHELIQSVPTAANAGYYAEIVAERAVLRRLVQAGTKIVQLGYAPEGGDVVDLVNQAQAEIFGVSTGKDAEDYVRLGDVIEATADEIEAASSHSGELTGVPTGFADLDTLTNGLHPGQMIVLAARPAVGKSTLGLDIARSASIKNNMTSVIFSLEMSKSEITMRLLSAEAEIQLQHMRKGQMRDEDWTKMASTMGRIADAPLFIDDSPNM... | Function: Participates in initiation and elongation during chromosome replication; it exhibits DNA-dependent ATPase activity.
EC: 3.6.4.12
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 468
Sequence Mass (Da): 51085
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A0A098S2G7 | MNEKIKALSAPVGTTLDRWIDLNQDQFPYATGELSRLLRDIGLAAKILGREINRAGLGDITGMAGSENVQGEDQKMLDIVGHIRFVRALKMGGQVCCIVSEEKEELVLTGKNDAKYVIAMDPLDGSSNIEVNVPIGTVFGIYRRKTEIGTPPEVAKDALQKGVEQIAGGYVLFGSSTMLVYTTGYGVNGFTYDPSLGEFYLSHPKMRFPAEGNIYSINESHYFKYGEAVQHYLNHCKREGYTARYIGSLVADFHRSLIKGGIYLYPATPGVYPDGKLRLLYECNPLAFIAEQAGGLAYGNGQRIMEIAPVNMHQRVPLII... | Cofactor: Binds 2 magnesium ions per subunit.
Catalytic Activity: beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-phosphate + phosphate
EC: 3.1.3.11
Subcellular Location: Cytoplasm
Sequence Length: 334
Sequence Mass (Da): 36903
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A0A496NGL5 | MQIIHLDPKNPPPLPKIALTIGNFDGVHLGHKTMLYALKNMASQQHLHTAVMIFEPQPREFFTPNNPPARLSNLAEKSAIIKKLDIDYLLVVDFNDEFRSLSALDFTQLLKKLNANHLMLGDDFRFGHDRLGDKNFLQNQGFIVDNLTTICHQNARISSTQIRHALSLGDLTTAKMLLGQDYSIKGTVVHGDKIGRTLGFPTANISLSRLKPALKGVFGANVLFFNQNDELIKPCDLTHSHHKGILGIHPNSLLGAVNIGTRPSVHGADYRLEVHFPDFDGNLYGLTAQVIFLHYLHDEKKYADLSTLQSAIGNDIKAIL... | 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: 327
Sequence Mass (Da): 36476
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A0A0M2UB56 | MKGLLFERSIKLLRIKVALISLGCAKNTVDSENMLGILKREHFQVTGEATEADVIIVNTCGFISAAKEESIDTILEMARLKTQGRCKKLVVAGCLVQKYREDLLREIPEIDAVLGTGDIGSVAETVRQSMQGSRVVNVRPPGQEDFTGIIPRFRTTSVPTAYLKIAEGCDHRCSYCTIPEMRGPYRSRPAEALLGEAASLIADGAKELVVVAQDTTLYGLDRYQKKKLPFLLEELAQLEGLQWIRLLYMYPEHINQEMIQVVAEEPRICKYLDIPLQHASNVILRRMNRRQNKEEILKLVTGLRESIPDITLRTTFIVGF... | Cofactor: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein uS12.
EC: 2.8.4.4
Catalytic Activity: [sulfur carrier]-SH + AH2 + L-aspartate(89)-[ribosomal protein uS1... |
A0A843CDJ3 | MATFKTRISQISKKNGKVILANDYDLSVGNLEAKTIQNIKELHPYLCGIKLNFHLLLPLSSKEISRINKIAHRYGLQTIADIKLNDIGNTNRVATEHLWNVGFDAVIVNPIMGLDSLKKLVKSCHKENKGVI | 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: 132
Sequence Mass (Da): 14776
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A0A2A5V247 | MINISILNYGCGNILSLRRALIELDFNVNFCNDPKDLTNSEFLILPGVGGFENAMKLLEEKNLTQSIQEYCLIKKKPILGICLGMQLLLTESYEMGHHKGLNIIGGKNILIKSNDKKNKLRVPHIDWEEIVFEKNFIKKELNFEKFNKKSFYFVHSYIASLEKTDHLVASCQLNELKIPSIIKSDNIIGCQFHPEKSGVYGLMLLKEIIQKI | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 5/9.
Function: IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisH subunit catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the synthe... |
A0A1F6SER7 | MPQFFISSENIVNNNILITSKNDINHIVNVLRLKKGDKLILTDPGSLIYETEISEIKPNSIETIILDKYEPTRKLNIDITLAQSILKSQKQDIVIQKATELGVNTIIPFISQNTVVKLESEKDKNQKIQRWQKIAYESSKQCQRVTIPEISQIISINELIELNNFDVKLVCAEKDAQFSIKKLLLQNKENIIKNSRILVIIGPEGGWDDKELQLFRSKNITLVSLGNLILRAETASITAISDIIYEYEL | Function: Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit.
Catalytic Activity: S-adenosyl-L-methionine + uridine(1498) in 16S rRNA = H(+) + N(3)-methyluridine(1498) in 16S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.193
S... |
A0A935NH22 | MKKIKSLGQHFLRSNAIAQRVANNVEVPYQNCTTVVEVGPGEGMLTQFLLQIPDIDLWVCELDDRLPQVLRAKFPETVLPSEKILLGDVLQMRLPQRFPDGFSLVGNFPYNISSQLLIMAYTHRQQIGQLVGMFQREVAQRVCAQPGSKVYGQLSVLLQAFFEVSYLFTVERGNFDPPPQVQSAVIRLTRRATDALNGTPEPIFRALVKQAFATRRKQLANCLKAYQFNFDDSVLPPTILQKRAEQLSLADFSELARIAVVKETKK | Function: Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits.
Catalytic Activity: adenosine(1518)/adenosine(1519) in 16S rRNA + 4 S-adenosyl-L-methionine = 4 H(+) +... |
A0A7C6VWE5 | MNYVPLYIKTHNSLLESMIKVSDLIDYAKENNIKTLTITDNNMYGVMDFYIACRKNNIKPIIGLEIKIDNYIVILYAMNYNGYKNIIKISTIKSEKELNESILAQHANDIICIVPYDSINKYNDLNKIYKEIFISYKNNEERLKLNYKNLVYMNSILYFNKEDAQYINYLTLIKNGKTEDEIYFENSNNNMLRDFNYIKEKYPYDLDNNYKIENMCNIVIPFNNNLLPVYNCPDGLDSYSYLKILCQNGMRKIFGSRVGRIYVERVKYELEIINKMGFCNYFLIVHDYIKYAKDNKILVGPGRGSAAGSLVAFLLGITTV... | Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
EC: 2.7.7.7
Subcellular Location: Cytoplasm
Sequence Length: 974
Sequence Mass (Da): 113062
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A0A3D9KEL0 | MMQQADNVERYRRKAVQPEEAQQTILNHIRALDAENVTLYEAWGRSLAEPLIAPHPFPPFRRSGMDGYAVRTADLAEAAPGRPAELVVLEHLPGGTEPKRSLGPGQASRIMTGGMVPEGADAVVMLEMTETDERDGLSFVRIGKAVPPGANISEIGSEIREGERLLPAGRQVEAGESAVLAACGCARVAVARRPRVAILSTGSELLEVDEPLAPAKIRNSNAPMLAALIREFGAEPTLLGKVPDDPEAAGKLVRQALADCDLLLTSGGVSVGDYDVMVDILAQPDVKLLFNKIAMRPGSPTSAALLGDKLILALSGNPGA... | 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: 422
Sequence Mass (Da):... |
A0A2N1W1F2 | MKISEILKNKEFVFSMEIFPPKPDSDISVIYNTLDGLKDLKPDFISITFGAGGGTRSRTVEIAERIENHYKIPCMAHLTCIGATKDSITGILNELQSKNIQNIMALRGDLPEGVKDPLKDFKYASDLVKFIKNKWDFCVGVAGYPEKHPEAKDIKVDIENLKNKVEAGASFITTQLFLNDDHYFNFVKLAREAGIKVPVLPGIMTATKISSLERMTKMCGVEIPERFKIATSTCAIDNPVCDETVKYTVGQINHLIKNGVPGIHLYTMNRVEQNRHIYNESDISKLRNGNV | Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
EC: 1.5.1.54
Catalytic Activity: (6S)-5-methyl-5,6,7,8-tetrahydrofolate + NAD(+) = (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + H(+) + NADH
Sequence Length: 291
Sequence Mass (Da): 32612
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A0A090RRB2 | MAGISIWQLAIIAIIVALLFGTKRLRTLGGDVGTAINGFKTAMKDDNKPDSNLSVQSGDEAK | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system.
Subcellular Location: Cell membrane
Sequence Length: 62
Sequenc... |
A0A3D9KG70 | MKIRSSIRYKLSVFLLISIIVPIAASIFLSFFYTKRSLKEDAIRENSNIVHQGATSLISQLNQMNNLSLSVYTNVHESSSLYNILSRGRSDFMVERNLYSGLHAIEQSAKEVQQVYLYSDLADQSYLLINGFLKRDVGQTGLEGHYVQPLNKDDPYFEPPHVSHNYGMEEFPYSPVNTVLTIHRPVYRAPLKERIGVLSIDFKLDRLRNLSDMLYDKGNEHLYLLDDTGTTVYSSETEWIGQKPPHSWLQHARYNLFQSGYFDWKDDGFHGIVIYEKFELIGRVWTIAKQIPNDYLYSNASRVLRINMILLVSFLVVAIA... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 602
Sequence Mass (Da): 68666
Location Topology: Multi-pass membrane protein
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A0A2N6DEM0 | MSGFIQKVLKSGLGIFTSRIFGLIRDIVVAGYFGASGLTDAFFVAFAIPNLFRAFFAEGALSSAFVPFLSDNMKHKSSKVADNYITSLIIAVSLMIAVILVITSLFPEYIIKLFMPGYANNQEIITTASNMMVVLMPYLLLVTICALLSGYLNLKGSYYIPHSSTAILNIAMITGAWIGYTKGVDIMYLCYGVFFGGIAQLLYVAIAAYIKGYRATLSGGFSKDVRKTFYLVIPSLAGVGINQVNFMVGRILASFLAVGSISYLYYANRLFQFPLGMFAVAVGTVTLTEISKANTEGDLHKRNGLIDKAVNSIFLIMLPA... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Involved in peptidoglycan biosynthesis. Transports lipid-linked peptidoglycan precursors from the inner to the outer leaflet of the cytoplasmic membrane.
Subcellular Location: Cell membrane
Sequence Length: 493
Sequence Mass (Da): 53822
Location Topol... |
A0A090S4Q3 | MITVILIVFLVNLFLGVPLFISLLVSSIAGFFFVDIDLAFRIIPQQFFSGIDSFSLMAVPLFILAGNLLNESGLTPKLMNLSKALVGHLKGGVGYVNVISSVFFAGVNGSAVADTSALGTLLVPAMKKEGYSTGFAASLTAGSSLIGPIIPPSIFMIIYASLTNTSVGDLFLAGIMPGLALEQSSLSSIGDMQENTI | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 197
Sequence Mass (Da): 20543
Location Topology: Multi-pass membrane protein
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A0A975AEA7 | MTSFGESHGNAVGCIIDGCPAGFRLSVMQIQAFLDRRRPGKNKYVTSRQEPDKVHILSGLFLGRTTGTPICVVVYNYNTVSSDYNNLTYAFRPGHADLSYFYKYGLRDHRGGGRSSARATIALVIAGAIARAILACFYNVRIYSYVTSIATDELDFLNQAHQSQSQFCFPNVFSNFFIKNCILAGTQNCDSVGATIKLFITNLFPGLGDPLYSKLDAELVSALMSVNAVKCVFLGNGNIANAIGGVLNNDAITSTGFLSNNAGGVLGGVSTGQDIVLTAVVKPTPSVFVPQRTISSAFKDIVLSIAGRHDPCVGLRAPVI... | Cofactor: Reduced FMN (FMNH(2)).
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7.
Function: Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to... |
A0A2J5I8I1 | MGSESRYQVALVGLGARGYQTWFECLRQSSSIAVSAVCDSKPATLEAFAARHPSVPAYLSLEALLQAQRPDFAIVSVPNRLHPGCIAQLAAAGVPVLKEKPVAESVADFQQLCRYNVPIGVVFQRRWQARYTHLKSFLPQLGRILSVRATLAGKYDPPLDGWRVMDNVGTFEDLGVHMLDILVWLLGRPSSVLGHQAEDGPPHARDRESHVSLRWDASGIVGHLHVSEVATRKEEGIVLRGTAGSLHLDGHDIIHRDTRGRQTFHLAVESYKEDAIQAMCQDFGDYVVRGSGPFSTSIARMGDTLAAVEAVNASFASHQL... | Function: Catalyzes the initial reaction in the xylose utilization pathway by reducing D-xylose into xylitol. Xylose is a major component of hemicelluloses such as xylan. Most fungi utilize D-xylose via three enzymatic reactions, xylose reductase (XR), xylitol dehydrogenase (XDH), and xylulokinase, to form xylulose 5-p... |
A0A6I9RW37 | MAVIATTSLFSSSLNPGLHLFPPPPSYPPPIAAVPSSACHCSHCFLDVTVLAWLEASEVSFNLSPSFDFYPSTSSAAVVVLNQLTCEGMKHVLKIMALLVAISAFWIGLLETSVVRRSYTWVLPIYLIVSLGCYGLLMVGIGLMLFPTCPQEAVLLQKDIAEAREFLKNKGIDVGSC | Pathway: Protein modification; protein glycosylation.
Function: Stabilizer subunit of the dolichol-phosphate mannose (DPM) synthase complex; tethers catalytic subunit to the ER.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 177
Sequence Mass (Da): 19094
Location Topology: Multi-pass membrane pro... |
A0A0S8FEY5 | MKKKPASRGNRSQDSSERRPRRYRFEIPSRNDVIGILRSSDRPISPKRLMSRLGLPSRKQQEAMNARLKAMIRDGQILINRNGDYCLVQRMPLVVGRVIGHRDGYGFLVPDDGSEDIFMSPRQMREVMHGDRLAVRIKGRDHRGRPEGSVVEVLERNTTEVVGRYVRESGIGFVVPDNTRITHSVAIPPRKSGGAKPGEIVVAHLTEQPGSETQPVGEIVEVLGAADAPNIETEVAIRAHGIPFEWNEEALAEAEGLGGRVRPKDKRDREDLRELPLVTIDGADAKDFDDAVYAERAGSGWRLIVAIADVSHYVQVETAL... | Function: 3'-5' exoribonuclease that releases 5'-nucleoside monophosphates and is involved in maturation of structured RNAs.
Catalytic Activity: Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.
EC: 3.1.13.1
Subcellular Location: Cytoplasm
Sequence Length: 748
Sequence Mass (Da): 845... |
A0A9D3MDZ0 | MGRWSVPGLRRARARVRGPWLCALGWCLGWCSCTGRVPLSSTVPFCCPATCRRTPSCSAPHLPLVPHPHPPAGRQVACGPPREPGRCCGYLGRGGVRGRGGAAVCTVFLLGRAEQGVDQAAVLEESRRHGDILQWDFRESFFNVTLKELLFWRWFCPERLGAARYVLRTDDDVFVDVGGVLALLRLHRGPAHPLYLGHAFVGTYPVRLWWNKYYVPQSLYHGGPYPPYLGGGGYLVSRETVRLLLGASASVPLFPIDDVYVGMCARVANVTAQPHPAFLPFEFAPSLPPCTYAGVLVLHRLEPQHLRQYWSFYKSQGHTC... | EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 330
Sequence Mass (Da): 36524
Location Topology: Single-pass type II membrane protein
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A0A1Z8KSQ7 | MAKWLNRLLIALPVALIQLYRLLISPFLGQNCRFEPSCSVYAIDALKVHGVFRGGWFGLRRICRCHPWGGHGYDPVPPANSDKDKNRKDAAAPCGCER | Function: Could be involved in insertion of integral membrane proteins into the membrane.
Subcellular Location: Cell membrane
Sequence Length: 98
Sequence Mass (Da): 10994
Location Topology: Peripheral membrane protein
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A0A0M2U637 | MRVAYQWLKEYVDVNLAPRQLAEALTLAGIAVDRVEDLGINNVVVGEILDVAGHPNSDHLQVCLVRVEEGKEPLSIVTGAPNVRVGQRVAVAVEGAELPGGQTITTTNFRGVVSQGMLCSAQELGLDLTDLPDEQLHGILDLPQGSPVGAKVDQIFGIADQVLELDLTPNRADCLAMVNVAREVAAVTGGHLHLPEISLKPEARNAADMTSVDIEATDLCGRYVAKIIENVKIGPSPQWMQKRLLAAGVRPINNIVDITNYVMLEMGQPLHAFDYHTLEGRRIIVRRGRPGESIVSLDKVTRQLDPEMLVIADAVRPVAI... | Cofactor: Binds 2 magnesium ions per tetramer.
Catalytic Activity: ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + H(+) + L-phenylalanyl-tRNA(Phe)
EC: 6.1.1.20
Subcellular Location: Cytoplasm
Sequence Length: 808
Sequence Mass (Da): 88745
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A0A257CGY4 | MQRLEFISDLHLSPELPRTCAAFFAWLEQSDADALFILGDLFEVWVGDDMLSQAFEQECAARMAQAARQRPLHVMHGNRDFLLGDAFMAATGCVSLNDPTLLVSDFGQVLLTHGDALCTDDTAYQAFRAQVRTPAWQTAWLARPLPERLMIAAQMRAASQEHQQGQAPADWADVNPVLAQAWLEEAQCTTLLHGHTHRPCHEHRPEGWERLVLSDWDLDQAHSAAPRGDVLSWSANGWRRRPCTAPG | Cofactor: Binds 2 Mn(2+) ions per subunit in a binuclear metal center.
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 4/6.
Function: Hydrolyzes the pyrophosphate bond of UDP-2,3-diacylglucosamine ... |
A0A0P6XQ33 | MSVSQHSRNLLVMKFGGTSVGDVLAVQQVVDIVREARSSWSSVVVVASALAGVTEALLSQAFKVAQGDESEIEANINNLRARHQALLEAFVAEEERRREALQSIEYLLQRLASLWQAIAVLGEATPRALDAVAGMGERMSVRVLAAILNAVEIPAQAVDATELIVTDAQFQSAHPDMEATRVKVETFLRPLLALGMVPVVTGFIGATPEGIPTTLGRGGSDYSAAILAAALHANEVWIWTDVDGVMTADPRLIPEAQTVPRLTYREVAELAYFGAKVLHPKTIRPIIEAGIRLRVLNTFNPSHPGSEIVGDAPMILDGVI... | 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: 475
Sequence Mass (Da): 50551
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A0A098S8G7 | MITYIKGNITHKSPTYVVVEAGGIGYHINISLHTYALIEKLEAVKILTHQHIKEDSHTLYGFAESIERNLFRHLISVSGVGPSTAQLMLSSMTPDEMRASIIGEDVAGLKRIKGIGAKTAQRIILDLKDKLLKDGGDENLPANVPQADNTIREEALSALVALQFNRIHAQKALNKVLKAQPGIGQVETLIKLTLKELS | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an ... |
A0A955JH54 | MNKKKTAAKKRLRPQNNDPLRLPFLEHLLELRRRVFIVSASVVGWSFVAYAFEQQIVHWLLKPANGQQFIYTTVGGGIDFLFRVCLYVGIVLSIPIIIYQMLRYLQPVIGQHPTRFIVLGSITSGVLALLGILFGYFIGLPAALNFLLNQFNTSDISALITIQSYLSFVILYLLGSSLMFQVPLIIYFINRIKPLRVRTLLKQERWVILFSFIAGAIINPSPRAQDMALLAVPMIISYQIGVVIVWYVNRYRVHSPEIQQLFERDTLLQQERKQRLQTIEYVLDQAELSASMATPPVNSVSSAETSKTVTASPTPAKSTK... | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes.
Subcellular Location: Cell membrane
Sequence Length: 336
Sequence Mass (Da): 38010
Location Topology: Multi-pass membrane protein... |
A0A955GD27 | MANDTLYFYDLETSGINPRSARIMQFAGQRTTLDLEPIGPPDNTLIKMSDDILPEPQAILVTGIAPQQTIADGISEREFCRYFIESIATPYTTILGFNSIRFDNEFIRFLLYRNFYDAYEWSYANGRSVWDMLDVVRMTRALRPDGIEWPFASDGRPSNSLELLTSVNHLQHENAHDALSDVYATIAVAKLIKQTQPKLFSYLYAMRTKQAVQAVVNSGEPFVYTTGRYNGAYEKTSVAVLLADHPVYPGNRALVYDLRFDPTEFLKMSIPDMLERMQYTKDETAPVRLPVKELVYNKCPAVAPLTVLTPSAQKNIFIDM... | Cofactor: Binds 2 Mg(2+) ions per monomer.
EC: 3.1.11.1
Catalytic Activity: Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Length: 483
Sequence Mass (Da): 55096
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A0A8D3EC35 | MAVCNSTLWSVTVFLLWTWTWEAGSGTQYQAEEVEIFNSDKRARLMWTSDPRREWTEIQLRLGAQNPVPVLQACGRRMTRTILSHWMEREEAHNLLMDLTFAQEEEPPGQLGPLGVHLFDTDTPIGMFQNRWTVLEIQTSKLIPGTVPPSQISSYLNRSLALSLGSVSRRGFQLAFSYSGTCVFLTSLRLYYRRCPDAVAHLALFGRTGAGSGPLTGACVKGAVEVSLPVRECDSDGVWGPLQGGCTCEPGHQAMDDICQACMMGYYKPANDSAGCRLCPANSRTRREGSERCDCLQGYSRLPTDSVDLSCTKPPSAPVN... | Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
EC: 2.7.10.1
Subcellular Location: Membrane
Sequence Length: 659
Sequence Mass (Da): 72864
Location Topology: Single-pass type I membrane protein
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A0A0A5FY80 | MNIGVIGGGAIGLLTSYYFHKQGHALTLYVRREEQMEAIQEKSLHVHPIDKKVEINTSLTDDLENQDVLIICTKQQAVDNVIQNLQDKHITCPLLFLQNGMGHIYKVQNLSNPVSVGVMEHGALRVDEHTVKHTGKGKLRIAAVNMNEQELKTMRSNMTCDEFPIDIEDDWYNMLAKKLVINVVINPITALFQVKNGQVIENPFLERIAKRLCEEACHVLKLESQNQWENVYQIARFTEENTSSMAKDIQGKRETEVEAILGFLLHEASFDIPTIQYMYESIKAIEYSFKKEGEV | Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 2/2.
Function: Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid.
EC: 1.1.1.169
Catalytic Activity: (R)-pantoate + NADP(+) = 2-dehydropantoate + H(+) + NADPH
Sequence Length: 295
Sequen... |
A0A3C2ECP1 | MKNLFFNVFKVFCTTMIFFSTVLFTQNLSAQRDRNDIDPKYKWDLTHLYPSDEAWKISLENQMPKVDELVSYRGKLSTNAKTLFTFLEKQSNLYKEMSRLYSYASMKADEDTGNAFYQGMNQEISQKFSIAGSKMSFVSPELAAIPKETIDKFMKQQPKLKTYAQFFDNLYRQQKYILSDKEERIIAEAGKLKQAPYNIYNIFSNAEMPFPTITLSTGEKLYLDQAAYTKHRSNENAADRALVFREFWKSFENYKSTFAQQLYANINADVFTKNARGYNSCLESSISANNIPVEVYHSLIANINKNLPTFHRYLNIKKRL... | Cofactor: Binds 1 zinc ion.
Function: Has oligopeptidase activity and degrades a variety of small bioactive peptides.
EC: 3.4.24.-
Sequence Length: 630
Sequence Mass (Da): 72345
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A0A2H6F982 | MTILEKTIQTIKKYSMLSTGDRILVALSGGPDSVCLLHILNKVKSDYNLLLYAIYVDHGLRPKETPGEVDFCRALCKSMGVQFEVKEINVNSSPLVKKSGKQGAARALRYKAIAETASELNADKIAVAHHKNDQAETILINLLRGSGMKGLTGISPVRKNIIRPLIDVGKEEIIDYLSNIREGYMVDSSNLGNAYLRNKIRAFIIPELKNLNPGIVETLNRTAGILTQENDYLEMAVTRTMIRLFSRKTESRIEMFLIPMETIPAVLLRRILRRTIAEITELKSLSLRNIEDIIELIKRGKSGDRIYLPNNLRAIRNYSL... | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34)... |
A0A346E0H5 | MKVFLYKKYKPTNILNFVGQKIAKSFFFFFLKKKKFPSSYILYGSKGTGKTTFSKIFSKSIMCKKRKKICNCKSCINFKSNIDFNEIDAASNRKVEDISNIFENINYKPVFGNYKVYVLDEVHMLSKHAFNFMLNILENLPSYIKIILVTSEIEKIPETVSSRCFKIHFKKFKEKKIYNFLKCIIKKENIYIKKKILKEISFCSNGSIRDALVQLDYFFVLKKFLNSKEIRKYFGLFNIKYSCKIINYIIYNKKKKLFSIMKKINNEINFKNIYVRILEKLNSIILYIYTNKNNIKFSKNYKQFKNIKIDIFMLFRKLIV... | Function: DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity.
EC: 2.7.7.7
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Length: 355
Seq... |
A0A951P919 | MASARFLQLYLMRFLTRFLSLSSVKRIIWQYCLSMSLTALLYFLVSKLVFAELKLGIEPSPVWPPAGIGLFVLLSQGRQAWLGVTLGILLMGSWLGVGWSLALGSALGGTLEALVGVSLLRRVGFQNDLERLPDVLNLIGLAGLAAPLLNATISTGVGLATGLIDRGQIGQTWWTFWLGDSMGILVFTPLLLVCSKQLRRRQQGQLDQWSEPQLVEKLICFSLLLSVSILVFWLHPSQILVNYPIEYLPFPFVIWAALRFGQTAGILASFMLSIVAITGTVAGCGPFATMTSQMPQQSRQVILLQQAFLAVVTMTTLILA... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 888
Sequence Mass (Da): 99258
Location Topology: Multi-pass membrane protein
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A0A1Z8KYJ9 | MTILLASYRGLTRLSAPILRALLDRRLTRGKEEADRITEKQGIAGVARPNGPVVWCHGASVGEALSILPLIDRLLAHDSSLTVLVTTTTVTSARLMAARLPERAIHQYAPLDHPLWVERFLDHWQPSMALWLESELWPNMLKTLKDRQIPAVLINARISDKSFATWQRFNGSVAAMLASFQLCLAQSSEDAKRLTTLGADTVDCLGNIKFSAPPLPIDADAASALKAAIGDRPIWLAASTHPGEEEQIVEAHQHVAEHYPDLLTVIAPRHPNRRKEIATLLDETGLTWCERSPGTLPGEDDAIYLADTLGEMGLLFKAVN... | 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... |
A0A5N5JHP3 | MDASSSAFKLKRKPVGSSGHGSSGSSQPNPELVPPPSYADVERLSAQTSGLTINNNTPSSDGKDENWGDIRPPLPPRGRTPTWSPAARAPSPQPGTSQPKAWQTALTTTRDLALRLAPQNTTSTKHYTILLHSSQLIVYRGPKTNITLTIFSSPSHPLPPPESRTLHLQPRGYSGDTGSRLKAFIGFTESWVDVTPALRVSSPTDVEPSVASRWENDIARATKRLAKNAGKHGSHVARETHVVRIPAAAQDGYFRVVLCNTETSGDKKKHKVLCAGPMVRIASLSNDAARFRGAKLRTLPLEAGIQAATVFANNTVGTFV... | Pathway: Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin (ATP route): step 1/1.
Function: Catalyzes the phosphorylation of riboflavin (vitamin B2) to form flavin mononucleotide (FMN) coenzyme.
EC: 2.7.1.26
Catalytic Activity: ATP + riboflavin = ADP + FMN + H(+)
Sequence Length: 603
Sequence Mass (Da): 6552... |
A0A2H0W0P7 | MKNKQIIGIIGGVASGKSFAGHFFQWQGSAFIDCDEIVATLYEKGGMGSKKIETFFGEEFMKEGAVDKARLGIFVSKDEKKLRILEKIIHPLVLSETQKAIDKAQTKVVFVEIGAPVDKFLRLCDKIILIAAPRDQRIKRIRTQYLQKIDSFKNLSKIRYDIKVINNFDKKTFGQKLTKVYNRITD | Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
EC: 2.7.1.24
Subcellular Location: Cytoplasm
Sequence Le... |
A0A1G6U0E9 | MAGLKTRKRQRLVVMIVAVAVLALAAFLIVFAGRQTGSFNLFLQPSEVFQQKVAVGQRFRLGGLVETGSVARKDDGLTYEFRVTDCAADLPVSYTGIMPSLFREGQGVVSEGALNADGVFVADTVLAKHDENYAAPGTLPKNEEACGHPEALTAGQDGR | Function: Heme chaperone required for the biogenesis of c-type cytochromes. Transiently binds heme delivered by CcmC and transfers the heme to apo-cytochromes in a process facilitated by CcmF and CcmH.
Subcellular Location: Cell membrane
Sequence Length: 159
Sequence Mass (Da): 16942
Location Topology: Single-pass type... |
A0A2E0VWH7 | MQALLIVGAGSFVGGMLRYGISKWVQIKLLTTYPFGTFTVNIVGCLIIGLVMGMSERYNISSEWRLLLVTGFCGGFTTFSAFSIETMALLRDAQYLPAFLYIAGSVIIGVLVAFAGYSVHRFI | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Subcellular Location: Cell membrane
Sequence Length: 123
Sequence Mass (Da): 13421
Location Topology: Multi-pass membrane protein
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A0A4V2ALK0 | MKLHIAKDATDLSMQAAVWIASIIKQTLEKQDRFTIALSGGSTPQKLHNLLSGYPYKEEIDWSRLHIFWGDERAVPFEDERNNAKMAFDTLLDNVGVPMAQIHLMRTDISPEESAAEYETILQKYFDKSGPSFDLVLLGMGDDGHTLSLFPGQPVVHEASAWVHSFFLAAQNMYRITLTAPIVNRSAHVAFLTAG | Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 2/3.
Function: Hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate.
EC: 3.1.1.31
Catalytic Activity: 6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate + H(+)
Sequen... |
A0A4Q3CTX4 | MEIKISKTSNSRAHELKRDEIVFGQEYADHMLVCDYKDGQWGTPEIVPFGNISICPSLSALHYGQSIFEGVKAYRQPNGGSAIFRPEKNWERFNKSAKRLGMPEISSEIFLDGLRALINVDDAWIPNEADTSLYIRPFMFATDEFLGVRSSLTYKFMIITSPAGPYYNKPVSIYVQSSFVRAVAGGIGFTKAAGNYGASMYPTAEVRKMGYDQILWTDAFEHKYVQEIGTMNVFFIVDGKAITPDLNAGTILAGVTRDSVIALLEENGIPVETANNEITCEISGNARLLGIEAGNNQDMGDYTDNIQHAFHGKMIVYIQC... | Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 4/4.
EC: 2.6.1.42
Catalytic Activity: 2-oxoglutarate + L-isoleucine = (S)-3-methyl-2-oxopentanoate + L-glutamate
Sequence Length: 346
Sequence Mass (Da): 38362
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A0A0M2UAU2 | MPILGGHGGNVRKASEKYGIPENEILDFSANINPLGPPEGVYRCLRSNLHQITRYPDPENAELRRALSAHLGVEEDRVLAGNGATEIIFLTIYALKPRRVMVTAPAFSEYARAAWSGGAQVVSYPLREEEGFNLKPFEIIKDLTGVDILFLCNPHNPVSNLIPPEALMTVIEHCRYTGTLVVVDESFLDFVEERRDYTVVPYAARHDHVLVLYSLTKLYALPGLRLGCAVAHRELVARLEACRDPWSVNRLAQLAGVAALQDPAFSDRTRRWLRKEKEFLFRKLQEVPGIRPLHPEVNFILVDLSESGKGASEVTEKMAR... | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
Function: Decarboxylates L-threonine-O-3-phosphate to yield (R)-1-amino-2-propanol O-2-phosphate, the precursor for the linkage between the nucleotide loop and the corrin ring in cobalamin.
EC: 4.1.1.81
Catalytic Activity: H(+) + O-phospho-L-threonine = (R... |
A0A931Q237 | MAKNYFKFKQFTVQQEKAALKVSTDSCLFGAWIASQLQTINNKPQTILDIGTGTGLLMLMLAQISSALIDGIEIDKPSFEQAQENIAASPWKERLNLFNGDVKNFSFDKKYDFIISNPPFYEGNLKSVHQHINVAKHDAGLTLEELINTTDQNLTAEGSFAVLLPYHRTEEFISVVEKKNYYLAELVRVKQSFKHKYFRSILLFSRKQCDKKESLIIIREADDAYSPKFISLLKDYYLFL | Function: Specifically methylates the adenine in position 37 of tRNA(1)(Val) (anticodon cmo5UAC).
Catalytic Activity: adenosine(37) in tRNA1(Val) + S-adenosyl-L-methionine = H(+) + N(6)-methyladenosine(37) in tRNA1(Val) + S-adenosyl-L-homocysteine
EC: 2.1.1.223
Subcellular Location: Cytoplasm
Sequence Length: 240
Seque... |
A0A955FF92 | MKHPVVHIGVGNVGKETASQITQFGENLTYSALFDRTGGAFAETGLSSDAVSRFPEGASADITPDSVIDELTGPCIFVDTTAADTTLASMKKVLSKGGAVVMSNKKPITGTQADWDELHRLGDDRLFYETTVGAGLPVIQTLKSLLATGDKIIEIQGCFSGTLGFLFSELEAGTSFSTAVTSAKEQGFTEPDPRDDLSGMDVARKVLILSRVMGKELEITDVSVEPLYNDALAKLSKEEFMEQVTTLDQEYAARAEQAAS | Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 3/3.
EC: 1.1.1.3
Catalytic Activity: L-homoserine + NAD(+) = H(+) + L-aspartate 4-semialdehyde + NADH
Sequence Length: 260
Sequence Mass (Da): 27727
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S9QNP7 | MSPGLARLGAWLQASRLPSQSYIALPLLLGQFIAVHATGGALRVGTLVAVQLFGVLDQLFIVYANDWADQETDRRNRTATVFSGGSRVLVEGRLSPRALGRAAIACAVALVGVSVGLAVVHRAPLLGVLAVAAVALLWAYSYPPLRLSYRGGGELLQMLGVAGVLPLYGYLAQGGALADFPWALMVMLWPTHLACSIATALPDEPSDRHSGKHTLPVRVGGERAAWVIVALNGLTWALAPRGLASVGLEVGAALWVPVAATLAVVGVRPAPPGSWRIQVRVAAAITATLAMVAWPLLGLAWP | Pathway: Quinol/quinone metabolism; menaquinone biosynthesis.
Subcellular Location: Membrane
Sequence Length: 302
Sequence Mass (Da): 31539
Location Topology: Multi-pass membrane protein
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A0A924HUV2 | MNDLEFNRLAIRYVFGFASALCLSVLGYFIIVDDWFNSSASAMAVLLVLAAIQLIVQLVCFLHLDGRGRSRGRAMTLGFTLLMMFVVVIGSLWIMENLDYRMGMNGQEMEEYMQKQNKKGF | Function: Cytochrome bo(3) ubiquinol terminal oxidase is the component of the aerobic respiratory chain of E.coli that predominates when cells are grown at high aeration. Has proton pump activity across the membrane in addition to electron transfer, pumping 2 protons/electron.
Subcellular Location: Membrane
Sequence Le... |
A0A2S6QGB7 | MTSQPKTVWTRKQVIEATGGHCVFDSVKDWSAEGISIDSRTCDHGDIFLALSGPNFDGHDYVSQALDKGAVAAIVSKVPEGIKKSEKLILVKDCENALNQLADFARNRTKAEIVAVTGSVGKTITKDGLSIALGASGLTHSTDGNLNNHYGAPLTLSRLPEDSAYAAIELGMNHTGELYSLSKLIRPSVAIITTIEAVHLEFFDSVASIAEAKAEVFAGLTGEKTAILNRDNIYFAYLSMLAEEYGVGRIIGFGADPEADVRLLNIRSNDLGTYVTADIRGKTISYNLNTPGRHNIINSLSILAAVSALNADVDKAAKAL... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Involved in cell wall formation. Catalyzes the final step in the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the precursor of murein.
Catalytic Activity: ATP + D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-d... |
A0A4Q3BUL6 | LGGGITGLSAAFYLEKAGAKNISIIECSALGGKMLTLKDNDFLVEAGPDSFITLKPHAVNLVEELGLSDELIQPKTSKFHILNHGKMLSSPKGLNMMVPTDMESFMQSELFTADGKERVLQEKNIPTRESDEDESFASFISRRFGLEMLRKYAEPLFGGIYATPSEELSMQATFPQFLQMEKKFGSLTAAVENQPKQTESNIQNRSPFVGLKNGIHSLADALMKSLKETQFVNKTIETLYIDRSKNAFTIGFSDGTTLEADQVIMALPVVAAQKLMANISADAAELLSQFTVSSSKIVTLAYKKFDIDSDVNATGFVAVR... | Pathway: Porphyrin-containing compound metabolism; protoheme biosynthesis.
Function: Involved in coproporphyrin-dependent heme b biosynthesis. Catalyzes the oxidation of coproporphyrinogen III to coproporphyrin III.
Catalytic Activity: coproporphyrinogen III + 3 O2 = coproporphyrin III + 3 H2O2
EC: 1.3.3.15
Subcellular... |
A0A6I9RRM7 | MAYYTLPSNLAPSPPLSIAHSPPPTSSSLSLPPTSPPQAQPGTDSEPSNPSQSSSPPPASNAPSNPSQSSSPPPASNAPSNPSQSSSPPPASNAPPPSSPQPPPPPLPTSPPPASQPPSASPPPPSATPPPPISYPAPPPISPPPYASSYPYLSPPPPYTPPPTPTLSPPPPPSAIPPAISPPPHSSPLSPPPAPPVSPPPPIAIPSPSPANSKSSPPPPPPLDQPPKNPSPPPSSAEPPIYSSLPPPLAKPPKCSLPPPVLPSPPPSEPPTPPISPAAPPPKSQPTPPPSPPASPPPSNPSRSTTPSAPDIPSPSTPTS... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
EC: 2.7.11.1
Subcellular Location: Cell membrane
Sequence Length: 782
Sequence Mass (Da): 82188
Location Topology: Single-pass membrane protein
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A0A8C3V7S4 | EQQMSSGRMFCGHVNKAGNLADIFKGVYVGRREGEAILSRVSPFLCRSCLFMVLHVALQAAVFGEYTWEVFVYCWELQFHLLLLLLPYLLLAGNLGCFLLCSRANPGTVTKSNAAALVQVYAYDGVLFQRGLVCPTCTVEKPARSKHCSVCRTCVHRFDHHCVWVNNCIGASNAGVFLLYLLSLTATAGALAAVTAAFLIHVLLLSDIMHSTYLDAQGQEHPVEIPFVIQHLFLTFPRIVFMLGFVILLTLVLGGYCSFSLYLALTNQTTNEWCKSRRSGGSPHLPSQPQDRPLVYKNIYSKGIWRNLKEIFNPPAVLER... | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 324
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 36152
Location Topology: Multi-pass membrane protein
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A0A7C7HUG7 | MIEFAQKQVAVAGFGVEGQATAKFLQTRGAIVTVLDENTQLDQAGPYTFKVGKQAFSDLESYDFVFRTAGLHPRKLSVDQSKILTAYSLLLQDYRQQVIGVTGTKGKGTTSTLIGHILKAAGKDVYVAGNIGHSPLDFYDQLTADSLIVMELSSFQLIDAQQSPHAAVMLMIEPDHMDWHSNMDEYIDSKLNLVRFQSDLDIAVYNPENPNTKDISQEFEWALPYLRGTQGHVRNGYICFAENKITPVSEVGLIGPHNLENICAATTVCWYILKEQGLDEKQIITALNAAIRSFSGLPHRNEDLGEVNGVRYINDTFSAN... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).
Catalytic Activity: ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-... |
A0A098S599 | MPTRLSVNINKVALIRNARLGNLPNLVQVAKDCERFGAEGITVHPRPDERHIRYSDIPQLKAVNTTEFNIEGNPTEKFMELVQQHQPTQATLVPDSPDVLTSDQGWDTIKHKAFLKDITQQLHASGVRVSVFVDPVAKYVEGAKEAGADRIEFYTGDYAKQFEANREKAVAPHVQAAKVAREAGLGINAGHDLNLDNLRFYQENIEGLLEVSIGHALISDALYFGLSNTIQLYLRQLG | Pathway: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 5/5.
Function: Catalyzes the complicated ring closure reaction between the two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and 3-amino-2-oxopropyl phosphate (1-amino-acetone-3-phos... |
A0A101IUI4 | MIQEICVAMAEDAPLPQGGLGLAFDDLISGSATPAQAGAFLYALRNRTLTGEDLATCASVLLSHARTITIPGSDRAVDTCGTGGDHSMTFNISTAAAFVAAGAGVPVIKHGNRAQTSRSGSADLLTALGVCIDASEERVIRSFQEANIAFLSAPTYHPALKTLAGVRSELGFRTILNISGPLCNPAGPINRIIGVADPALLGPMAEALQRLGVKKALVVSGDQLDELSLTGENRICELSSGQIDYYTLTAADLGLAEAPRELLVAESPEESAAIISRVLQGGDDGPARDIVLLNAAGAILAGGGSAGFSSALKMAEDAID... | Cofactor: Binds 2 magnesium ions per monomer.
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 2/5.
Function: Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).
... |
A0A7C7LX86 | MASKEDIVTLPTKNLRQQSDEVSFPLNKKIEKLIADMKSATLDWEASRPHEFGVALAATQIGVLQRVVVVRQSFRDKSNTNFDIFINPEITRYEGEVVEEHEGCLSVSDVYGMVPRYSKVKVKAKNEFGRPVKFVVKGFLARVFQHEVDHTNGITFVDKIGAEGRFFKLLPEGQMDEVTGDEKTKLLKYMDVTKNAT | Cofactor: Binds 1 Fe(2+) ion.
Function: Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.
EC: 3.5.1.88
Catalytic ... |
A0A7C7M9G6 | MFIHCYHYGMEILWPKPGKYIVAVSGGVDSVVLLHRLAVRSSQFAVLPTDRLVRNNLESTNDQPNNEKSMKGEKRKIKNRYELIVAHVDHGWRTDSSDDERFVRELAQKYKLNYVSTKLTLPKKSEAAARAGRWEFLHDLRVKHDATAIITAHHADDIAETILINLQRGTGRSGLTSLKETLHIKRPLLNVTKNQIYEYCVAHNIEFVEDSTNKDNTYTRNAIRAKLGRAQNTSKKLQKIYSRMLTINAEIDELLGGIEKAVSDKQGARINVDRQAFSSLDQKIQHELLRFLVLRLNSDAELNTEQITRGADSINASLPS... | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34)... |
A0A086ZGK9 | MVRMGKKAIVASHRSSKRMIFWTFVGLFAGGACGSAVRLGYFALQGRVVDWPWITMMVNLVGCFLLGCLTVVMASFGADSGAWRRVRLVVGTGAIGGFTTYSTFVLEGTTRVMSGAVAQGLAYLVACVGLGLVCAWAGLVVGGVLARALHAFLNRRPKTIRHRALAHDVRLADAGVASDAFDVGAARDEVGEDVASYTADWRVPLEAGMIGLIVLAIPAFGFGVGRWRDPCALVRLIAASLLGGLGVLIRYAVDGWVSRDCSGSIPVGTFVVNVTACLAIGLVFGWAARHAGFDVIRYLLASGLLGGYSTFSTAGVEGAR... | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Subcellular Location: Cell membrane
Sequence Length: 352
Sequence Mass (Da): 36749
Location Topology: Multi-pass membrane protein
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A2SXN1 | QDPATPVMEGIINFHHDIMFFLIMITVFVCWMLFRVVILFDEEKNKTPATIVHGATIEIVWTSIPAVILLIIAVPSFALLYSMDEIIDPIITLKVIGSQWYWSYEYSDNLEFSDEPLVFDSYMVQENDLEIGQFRLLEVDNRVVIPTNSHIRVLITASDVLHSWAIPSLGIKLDACPGRLNQTSMFIKRKGVFYGQCSEICGINHG | 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... |
A0A955K6A4 | MQVNMFNYRNKYHHSPKKLSRLMIVGLIIFGVLCLSGAGSIWWYKAELKPPSASSQTIKFEVIPGQTPAQIADNLEAKGLIKNSLAFRLYLKINHLEGVLQAGDYLLSNDLTVQQIVDELSNGQIESRSFTILPSKRLDQLKESFSEAGFSDSEIAQAFDPANYLNHPISKYKPANASLEGYIYPETFYITDNTSAKEIVEKSLNEFYKHLTPDLVEKIEDQDLSVNEAIILASIVEQEVSNVSDKPTVAQVFLKRLRLGMQLGSDVTFFYAAAVYGGEPTPSLDNPYNTRLYSGLPPGPISNFDLSSLEAVAEPSNTDY... | Function: Functions as a peptidoglycan terminase that cleaves nascent peptidoglycan strands endolytically to terminate their elongation.
EC: 4.2.2.-
Subcellular Location: Cell membrane
Sequence Length: 358
Sequence Mass (Da): 39986
Location Topology: Single-pass membrane protein
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A0A0G1PHE2 | MLKIFSTPALRKRILFALFVILLFRFLAHIPVPGVDVAAVKSFLSGNTLLGLFNLFSGGGFANFSIVTLGLSPYITASIIIQLFTMMIPQFEELSKEGETGREKLNQYTKYLTVPLSFVQAYGVYFLLGKQQGIIGTLDSMSLMVFIFTLTGGAMLLTWLGDLVTEYGIGQGISLLIFISIVSALPSSLATFFVSLNTYDLMNVLLFLAIAALVIVGVVLINEGTRNVPLEYGRRDTGSWRVSNYMPIKVNQAGVIPIIFAVSLILLPSFVAAPLAATSVPYMQKLGDFLLTNFSSQAPLFNVVYFLLVFGFTYFYTTVQ... | 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 compos... |
A0A8A1MMZ3 | MGVYVILCIGESLEEREAGKTLDVVTRQLNAVAERLSSRDWPKVVIAYEPIWAIGTGKVATTEQAQEVHASIRKWLGDKISTDTAENVRVIYGGSVTEKNCRDLAQQPDVDGFLVGGASLKPAFIDIINSRL | Pathway: Carbohydrate biosynthesis; gluconeogenesis.
EC: 5.3.1.1
Catalytic Activity: D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate
Sequence Length: 132
Sequence Mass (Da): 14429
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A0A1V1P9W3 | MSNIITRFPPSPTGYLHLGGARTALFNWLYARHTGGKFVLRIEDTDVERSTRQSADAIIESLNWMGIDWDEGPFYQSDRLDLYQEKVQILLNTGHAYYCTCSPDTLEAKRKAAMAAGKPVKYDGSCRDKNLSKSNDAVIRFRAPQTGSTVVNDRVKGNVAFQNHEMDDFIIQRQNGMPTYNFVVVVDDIDMQINTIIRGDDHLTNTPRQILLYQAFNQSLPEFAHVPMVLGSDKSRLSKRHGAMSVLEYRDKGYLPDAFINYLVRLGWSYGDQEFFSRNELIEKFSFENMGRSAGIFNPEKLLAINAEHMRCNSGALIYP... | Function: Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).
Catalytic Activity: ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu)
EC: 6.1.1.17
Subcellular Location: ... |
A0A8B7D791 | MDDYLDIDGSHLEGGGQILRNAVALSCLLRKNITVFNIRANRPGPGLKSQHLHGLRLIRDLCEGQLLGDDIGSTTIHFAPKKLKTGYYEADAKTAGSVCLLMQVSIPCAAFIGSRTEIKFKGGTNAEMAPPIDYYIEVFQPIASKFGLDFSCELVRRGFYPKGGGQVNVVVNNAQHFKSVNMVDFGKITEIYGKVYVAGALQDKVGIEMAESAAKYIEDHLNIKPLISRSRVHQAVGTGCGIIVVAKTSTGCIIAGTAAGKKGKPSSCVGVEAAEMLVKEVKLGACVDTYLQDQLILLMALSEGCSKIRTGPITLHTQTA... | Function: Catalyzes the conversion of 3'-phosphate to a 2',3'-cyclic phosphodiester at the end of RNA. The mechanism of action of the enzyme occurs in 3 steps: (A) adenylation of the enzyme by ATP; (B) transfer of adenylate to an RNA-N3'P to produce RNA-N3'PP5'A; (C) and attack of the adjacent 2'-hydroxyl on the 3'-pho... |
A0A2N1W428 | MMVRGIRFDFSKPCIMGILNITPDSFSDGGSFDSTEKAVMHAVYMAENGADIIDMGAESTRPGAAAVTEQEELSRLIPVISAFRELNKNTPVSADTYKAKTAAEAIKAGADMINDISGGTFDSAMMQTAGKLDVPYVIMHTKNTPDKMQKDTAYSDKGAVSDILEYFRERIAAAIKAGIKKDNIILDPGIGFGKTQQDNIEIIKNTVEFKKLGFPVLIGASRKSFIGNITGKPPDKRIFGSAAAAAVSVIFGADILRVHDVPEMRDCVKTAYEFIKTKKEG | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2.
Function: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7... |
A0A3R6ZU85 | MNEYVKVAGGLARFGSLVFCMQQLGDVVLCVGPSMLPTLNEHGDVVLLDKLTPRFSKLQNGDVIIAKSPTNFRQTVCKRIIASEGETVGLKHRYHPTKIELKQVPKGHVWLEGDNKHDSHDSRYYGPVPYAMIQGRVLCRNKRVLWYMCGPTVYDITHLGHGRTYTCFDYVRRILEDYFGYQVELVMNITDVDDKIIVRAAENGWTEAHPGQSLPASKDEAAKTVLAWASEQTAESNMQRTSDLSKYFEKTFMDDMAALNIKPPTVLTRVSEYMPEIVEFVQGIIANGYAYESNGSVYFDTVAFAKAKGKNYGKLVPENV... | Catalytic Activity: ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-cysteinyl-tRNA(Cys)
EC: 3.4.21.-
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 733
Sequence Mass (Da): 82280
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A0A936TU37 | MTKKINIAIDGYSACGKSSTARQVAKRLGYLYIDSGAMYRAVTLYFQEHLIDLDNAEGIERALPFIDIEFIKRGDSHHTFLNGTDVEEFIRQPEVAALVSEVAAMSNVRRMLVRQQQKMAVQKGVVMEGRDIGSVVIPDAELKFFMTADVDVRTQRRQDELLKKTGKLFPLEELKANLQHRDRIDSTRADSPLTKVPEAMEIDTTHLTLDDQIEWICRKAEEEINKG | Catalytic Activity: ATP + CMP = ADP + CDP
EC: 2.7.4.25
Subcellular Location: Cytoplasm
Sequence Length: 227
Sequence Mass (Da): 25799
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A0A936TUG2 | MFHIAHDLQNYLLETNGLDKNLVGFVPTMGALHEGHISLIEASKSKTNCTVCSIFVNPTQFNDKADFEKYPIRIDHDLEMLLAAGCDAVFMPSVEEIYPQGTTLQTDVDLGFIGTTLEAQHRPGHFQGVLQVVKRLLDIVQPDVLLMGQKDYQQCMVIARLIEHYRLPVLLKIVETMREKDGLAMSSRNMRLSPEERISAVKLSAVLFTIKKNCKTTPLEQLLREQHAWLSQDELINIEYLAAVNGKTLEPVTTFSEDIPTTILIAAKVGNIRLIDNLIVN | Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1.
Function: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
Catalytic Activity: (R)-pantoate + ATP + beta-alanine = (R)-... |
R9N6V6 | MHTGIEFPNIGIHLESVGDHISVMGFDIAYYGIIIGIGILAGIFIAAWEARRTGQKPDDYYDLAIYAVIFAIIGARIYYVIFSWDMYKDDLLSVFNIRQGGLAIYGGVIAAVLTVIVFAKIKRLSAPLLMDTAGLGLVAGQMIGRWGNFFNREAFGEYTDWILAMRLPVDAVRGSDITDLMREHMETVEGVSYIQVHPTFLYESLWCLFILILMLLYRRHKRFHGEVFLLYLAGYGFGRFFIERLRTDQLLLPGIGFPASQLLAGVLVVVSIGMIIYRRQKSI | Pathway: Protein modification; lipoprotein biosynthesis (diacylglyceryl transfer).
Function: Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins.
Catalytic Activity: 1,... |
A0EZT8 | FGGAISKKRKFVSDGIFKAELNEFLTRELAEDGYSGVEVRVTPTRTEIIILATRTQNVLGEKGRRIRELTAVVQKRFGFPEGSVELYAEKVATRGLCAIAQAESLRYKLLGGLAVRRACYGVLRFIMESGAKGCEVVVSGKLRGQRA | Catalytic Activity: 2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-monophospho-2'-deoxyribonucleoside-DNA + H(+)
EC: 4.2.99.18
Subcellular Location: Cytoplasm
Sequence Length: 147
Sequence Mas... |
A0A951PDW8 | MCGWSSRLEVKELLYDCDGDTILLKIEQIGEAACHTGARSCFFNRA | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9.
EC: 3.5.4.19
Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-5'-AMP + H2O = 1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide
Sequence Len... |
A0A8F4QC52 | ALTRSPTIRNVLPRHEQGGVFAAEGYARASGKPGVCIATSGPGATNLVSGLADALLDSVPIVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVLDIEDIPRIVSEAFFLASSGRPGPVLIDVPKDIQQQLAVPNWNVSMKLPGYLSRLPKDPSELQLEQIVRLISESKKPVLYVGGGCLNSSEELRKFVELTGIPVASTLMGLGSFPLNHDLSLSMLGMHGTVYANYAVDKSDLLLAFGVRFDDRVTGKLEAFASRAKIVHIDIDSAEIGKNKQPHVSICGDVKLALQGVNKILESKSFKSKLDFGKWRDELNDQK... | 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: 479
Sequence Mass (Da): 52235
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A0A1Z8L0J1 | MPTTIPPLADLLDPIRDYARRAGAVIMTHYQPGGMGDDVEAKGDGSPVTAADREAEAIITPLLNALTPEIPVIGEEAASAGDLPEIKQGPFWLVDPLDGTKGFIKGSGEFTVNIALIVDQRPVLGVIYAPAFDEEFGGYGIDTAFMKQGDGADQPISVTSPPPAKVRVTASKNHRNQSALDAFLAGREVADCDARSSSLKFCEVAAGRADIYPRFGPTCEWDTAAGHAILEAAGGLVTDVNGGPFEYGKADRKFLNDSFIAWGGTDPAEWFAKTGS | Function: Converts adenosine-3',5'-bisphosphate (PAP) to AMP.
Catalytic Activity: adenosine 3',5'-bisphosphate + H2O = AMP + phosphate
EC: 3.1.3.7
Subcellular Location: Cell membrane
Sequence Length: 276
Sequence Mass (Da): 29098
Location Topology: Peripheral membrane protein
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W9GN01 | MTTYDDDLRLAHVLADAVDRLTMERFRAADLVVESKPDLTPVTDADRAAEELIRAQLKRSRPRDAVEGEEFERTGHGPRRWIIDPIDGTKNFVRGVPVWATLIALVDDGRPVVGLVSAPALQRRWWAATGSGAWTGRSITSARRILASGVTRLEDASLSYSSLSGWRDRGLRDAFLDLMDACWRTRAYGDFWSYMLVAEGAVDVAAEPELAVHDMAALVPIVEEAGGSFTGLDGRLGCWSGNAVATNGHLHLQVLRRLTPEDDPSGGGATVRVAEAADIDKVAHVAAATFGLACPPTITPERVSAFITEVLSPERFADYL... | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 8/9.
EC: 3.1.3.15
Catalytic Activity: H2O + L-histidinol phosphate = L-histidinol + phosphate
Sequence Length: 442
Sequence Mass (Da): 47780
|
A0A4Q3D0W3 | MLFKDTIVAISTAAGVGAIGLVRLSGPQSLSIVSALFSGKPLEQQASHTVHFGHIYDRDRKADGARMIDEVVVTLFLGNKSFTGEDTVEIAAHGSPYILDQVLNACIMAGARLAGPGEFTQRAFLNGKMDLAQAEAVGDLIAAENKASHEIALNQMRGGVSSELAALREQLINFTALMELELDFSDEDVEFADRTALKNLIQQLQSKIQNLIKSFEYGNAIKNGVPVAIIGKPNAGKSTLLNALLKEERAIVSDIAGTTRDVIEEAINLAGITFRFIDTAGIRNTQDTIEAIGVERAKEKVQQAKVVIHLYEQDTDLLEE... | Cofactor: Binds 1 potassium ion per subunit.
Function: Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
EC: 3.6.-.-
Subcellular Location: Cytoplasm
Sequence Length: 459
S... |
A0A3T0RQV9 | MKKLILGSTSVYRKELMLKLGIPFETIKPSCDEDALKKNLLSQHKTPLEVAESLAFAKAASLNKEFKSAVVIGGDQLVDFDGNIIGKSKSHDKAKEQLQSMSGRTHQLITSIAILHEEQKYTLNHISKMKMKKLTPSEIDNYLRIDLPYDCAGSYKIERSGICLFEKIETDDFSAIQGLPMMWISQKLKELGYELFTNQ | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes 7-methyl-GTP (m(7)GTP). May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: H2O + N(7)-methyl-GTP = diphosphate + H(+) + N(7)-methyl-GMP
EC: 3.6.1.-
Sub... |
A0A3S0FX69 | MGFDRNTVIGFVLLMALLAGYIYFAQRGQVAAAKEKQRIEDSIRKAQAKNIDSVKIKEEIKKADSAKQVQTAGTFTGAGTGEEKLTVVENDFLKVTFTNKGAQPKIVELKKYKTWDNKPLELVKGDFNKLSYQVNTAPGRSAQTSDLFFTGGEVVKEGNNQVVRFSLKDSAGTGIEHEYIIKPDDYMIDFNVKLNGADRLLTQNALNLVWQVQGNQQEKDAKYEKQQSQVVFMQGNDDYDYYTTLANNDKKLEKGVKWFSVKQQFFNSTLVYKTGFTSGDTKWTVFPDSTHILKQVITNLHGTVPAGATATVPMQLFYGP... | Function: Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins. Aids folding of multispa... |
A0A418AJ25 | MFLRDNVHHVEMNSRQGDYPGPRGNFQLAGHTEELVTSLGHALAVLDAGIAKQGRHGTAHTVLRVVDPGLNKSLLAFGHIMWKRSHETMTHHPMIERADLPYGDSQLTRLLEPSLGPHASLAMLCTISPSLPCLTETHNTLKFASRWEMPSLAPSDDDGDSSAWDDPDAVPPSDNGTAQEDNAAVHAATLDLLRRNLDPDDASMLLHGLLPTHRALFGAASSRGIRSYNEDTFRVITSLEAYAHALVMHQRQRDVNHPADVDSSQSMRTTLDTVIRDNTMDADTTSPLASWTLTPVESCVGPSRLPRGSKTGASSTSTSQ... | Function: Enzyme with a broad specificity.
Subcellular Location: Membrane
Sequence Length: 470
Sequence Mass (Da): 50669
Location Topology: Peripheral membrane protein
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A0A2N1W1A9 | MATLRDIRKRIKSAQNIQQITKAMKMVSAAKLRKAQDRTLASRPYAEKISQVIGELMSSDAGSRFPLLKEHPEVKKEAVILVTADKGLCGSFNGNLAKEVMMMMRENPDMSLFYIGKKGFDLLKRFGKENEKFKFNDRYIGWPDVEEVGKMVIDNFSSGKYGKVTLIYSKFQTNLTQNIIKKQLLPVVFEGSTEQHAKRDFIYEPSEKAVLENLFVRYVKTTIYSAVLESQASEHGVRMASMEKATNNANDMIRSLTLLANKTRQAAITNEILEIVGGANAIKG | 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: 284
Sequence Mass (Da): 31972
Location Topology: Per... |
A0A0S8FAP9 | MNAPRKRRLFFALWPSQEVRAGLAAASHAVRQNASGRAVPDDNLHITLAFLGSVDDETFECVQRAAEALVAESFDLVVDRAGWWRRTGILWLAPSRAPSALNRLVKALWDGLEPCGFWPDYRDFHPHLTIARRCRRAALPDIEPISWPVSELTLLESHTGQRGARYTVVDSWALRAFSGEAEGNAGCPTSRSVE | Function: Hydrolyzes RNA 2',3'-cyclic phosphodiester to an RNA 2'-phosphomonoester.
EC: 3.1.4.58
Catalytic Activity: a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + H2O = a 3'-end 2'-phospho-ribonucleotide-RNA + H(+)
Sequence Length: 194
Sequence Mass (Da): 21590
|
A0A917ZUH5 | MAQSPTGGRTPMHPRVQALTQRPGVDAAFASDLALATQIDRAHIVMLTEQGVLPPATAAALLTAVDRLRALDFAPLRERPAPRGWYLMYETYLVDTLGPDIGGSLHIGRSRNDLTATLHQLKLREPFLGLLWECLRLLGALARQARRHARVVMPAFTHYQPAVPITYGHYLNGVAVALAADIEALLGVADDLDRCPLGAGGVGGTTVPVDSGRTARLLGFGRACPNSVEAVATRDAALRLLSSAAVIGVLLSRVSADLLLWTTADLGLLTVPDSLTGGSSMMPQKRNVFVLEHVSGKAAAPLGAFATAAAAMQKTPFSNA... | Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3.
EC: 4.3.2.1
Catalytic Activity: 2-(N(omega)-L-arginino)succinate = fumarate + L-arginine
Sequence Length: 520
Sequence Mass (Da): 54182
|
A0A955EKZ8 | MQVTRKDISETKVKLTIELGLEELTHSKQHELQEKAKVAKITGFRKGKAPLNLIEKQLDQNQLQADVINHAINDYYGQALTAEKLRALDQPNVTIGKFVPYTELQFTAEVEIMPRIKLGDYKKIKKSPKIAKVEADEVKKVLANLSERMAAKKDSSKPAKLGDDVVIDFDGKDKKGQPVAGASGKDYSLNLGSNSFIPGFEDGLVGSKSGDKKELKLKFPKDYHAENLAGTDIVFEVQVKKVQSVELPKLDDEFAKKVGPFDSFKSLQADIKTQLEDQKKQEAENALKDEIVEELVKKSTLVLPDILINDQISMLEHDFN... | Function: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Subcellular Location: Cytoplasm
Sequence Length: 407
Sequence Mass (Da): 46039
|
A0A7C7LW79 | MTSFVYYGSDWCPDCVRVKRWLSENNLTDYTERDPDDGQEIVDEMLAKTNGHHEIPTLDINGKILVNPSNEELKEEFKTMSAEHSEDKIYDVVGIGAGPTSLAAAIYTTREDLETVLLEKGVVGGLAAVTESVENYPGFPDGVGGMELAQNLEKQALRFGTTIQLAEVTAIEDKGDYRVVKSTDGDYKAKTVLIGTGSDYKKAGVKGEKEFYGRGVHYCATCDGALYRDQVMAVIGGGNSAAQESLFLTKFAKQVHVFIRKDHWRASDVLIQKVQENDKITVHFNTEIEEIQGEGVRIHSITTKNNQTNETQEMNVGVVF... | Cofactor: Binds 1 FAD per subunit.
EC: 1.8.1.9
Catalytic Activity: [thioredoxin]-dithiol + NADP(+) = [thioredoxin]-disulfide + H(+) + NADPH
Sequence Length: 393
Sequence Mass (Da): 42929
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A0A346E0D6 | MKIKNKLNGCIVSIITPMKKNKNIDFYEFKKLLTKLLNKVDGFVICGTTGESTSINTKEKIKLAKISRNVVKNKPLIFGNSEIDTYKAIKLNLKLKKMGIDAILQNVPYYVCKNSKNILAHFKEINKHNIPIIIYNIPSRTGVDINLKTIIKVSKFKNIIAIKESSYNIIKILDIKYNTNLKCFSGDDVTSPISFFLGADGIISVTANIFPEIISKSFKEKKINKEIYNFNKILFIESNPCPKKYIIKKKKIIKNYTTRLPLVNINKKNKKKILKAYNNVKKKNI | Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4.
Function: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
Catalytic Activity: L-aspartate 4-semialdehyde + pyru... |
A0A4V1ST87 | MVLAYELRDLPFKVNAVDPGYTATDFNHHSGQASGNGDTINTWTSATTFVFGNDFSAENMGFRNDAGFTSGQAVALRIEGDRAVFRNCSITGFQDVLFLSGAGKRSYFRDCYIEGTTDFIFGAGTAVFRDCTIHSKKNSHITAASTDSTTPYGFVFFDCRLTADTNVHKVSLGRPWRPYSAVTYIRCRMDSHIIPEGWNNWKNPANERTARYAEYGSSGPGASPATRVPWARQLAAREVRTMTVRRIQRGWRPAQDGK | 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: 258
Sequence Mass (Da): 28672
|
A0A3T0RPD8 | MSKSCVVLGLGSNIDPIKHLRLALAEIKRLSQVSVINIASIYESDALLPENAPANWNKKYLNSAVELEVTNFEPLKLLKEIKAIEQKLGRAGSDRWAPRNIDIDILWAQDFTLNSEALNIPHAQILNRPFALLPLLELRPDFPFNEPDWMWQNPKPFHTEISKQHVWPKFAGILNVTEDSFSGDGVTSLGRPPSITLRLGQLLDAGADIIDIGAESTRPGALIIDPDEEYSRLATTIDVINKYKADYNRQFEISIDSRKPEVMQKIINNYHIDYLNDVEGFRQPQMRELLKLTTAKAICMHSFSVPPLKNETISESEDVW... | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 4/4.
EC: 2.7.6.3
Catalytic Activity: 6-hydroxymethyl-7,8-dihydropterin + ATP = (7,8-dihydropterin-6-yl)methyl diphosphate + AMP + H(+)
Sequence L... |
A0A1W0XBM4 | MPLVVSCLLVGFTITTVNMLIFPGVSAGIDCGIAGQCPNILSDSTKKYCCRTEGVAIGYCCDANDYAKFPFDGPTKDFNPQSNSVGGGESPSAVTNKSNESKIPLEIVQSQYRQGPRQVLTDTIIEAKLRKNLTFEQIAQGTGLSLVYVTSALLGQHPLPAKAAKIVGQQLGLSKQDCKLLQTIPQRRAGGGPSDPTIARFSEMIHLYERTLKVLVHEQFGDGVVSAVNFKINLTKVPDPEGGHRAIITLDGKFQPFKPFK | Function: Catalyzes the reaction of cyanate with bicarbonate to produce ammonia and carbon dioxide.
EC: 4.2.1.104
Catalytic Activity: cyanate + 3 H(+) + hydrogencarbonate = 2 CO2 + NH4(+)
Sequence Length: 261
Sequence Mass (Da): 28140
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A0A496NEB9 | MTNLRTNFYPPNSPQNFATPIHALIVAAGKGSRFGTEVPKQYLKTQDKTILQHSVARLNHLQITDLTIVIAPDDKVASNLSFEFAHPIYFACGGCERFLSVQNGVKAIIERGASDDDWVLIHDAARPCLALPDLAALIAKIQKTPNLTGAILASPVTDTIKFVENHTISHTIDRSQLWAAQTPQIFRLKALEKMLQTVIAKNLIITDEASGFEMMGEKIAIVPSKHINIKLTYPQDLMLIQALLTQD | Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 2/6.
Function: Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
EC: 2.7.7.60
Catalytic Ac... |
A0A420Z312 | MTAGIGAGIGQGYAAGKAAEAVARNPEAESKIRSMMIVGAAIAESAALYAFVIAIMLIFVA | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
A0A7C7HVP5 | MDAVSDIKAKLALEDVVADYLELKRSGSNLKALSPFSQEKTPSFMVSPAKQIWHDFSSNKGGDMFTFIQEVEGVEFKEALELLARKAGLNLDDYQTKRGPGREVKKQYERALNLSARFYQEQLIHNKAALDYVTKKRGFNKQSIIDFNIGYAPNKTDALSKYLLSKDIDTETIVKSGLAVERRGRLVDMFRGRVLVALADRSGSPIGFTGRQLIDGDGPKYINTAQTILYDKSRHVFGLHLAKDAIRKQDLSVLAEGNLDVVSAHQAGFKNVVATAGTALTIQQLKSLKHLSKNIALAFDGDEAGVRATIRAIPLAQGEG... | 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: 572
Sequence Mass (Da): 64163
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A0A955GEW1 | MKKTFIIAVSGGVDSVVLLHKLVSVKHPNINYIVAHFDHGIRPDSNADAEFVEQIAKNSQLAFELGEGNLGKNSSEDEARRARYNFLFTVMQKYKADGIITAHHRDDVIETMVVNILRGTSPRGLMGFSRAEIIRPFIDKTKADLIKYAHEHKLTWHEDSTNSDPKYLRNYIRQNIIPKLSAKQSTELLKIREKLVDIYREVDALDKKILVQCMKKSELVRSRFVVLPVKVQMEILSTWFRLNNVAFDSKLLEKAANAIKVFKPGKVFELTSNKKLIIGRLRINLQID | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34)... |
A0A346E0D4 | MKKIGRILNIRIFKKIIFLKLVNIKKDIQVVIKKNIKKIKKKIKIGYIVKVYGKHGKTKSGEKSIFCQKIKILSKCIIFPNKYFKNINKEFSYRKRYIDLVINKKSRYVFNKRFNIIKNIRKFFYKEKFVEVETPILNKVYSGADAEPFVTNHNFLKKKNYLRISPELNLKKLIVGGYEKIFEIGKNFRNEGCSNIHNPEFSMVEYYYVDKNYLDIMKLTKKLIKSLAKKTLGKKKIIFDKKILNLNKFKILKIKEALIKYKKINNISKNFLIKEILKKTKILSYKKKNLMYQYFDEFVSKKIIKPTFIIGHPKIFSPLA... | Cofactor: Binds 3 Mg(2+) ions per subunit.
EC: 6.1.1.6
Catalytic Activity: ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-tRNA(Lys)
Sequence Length: 408
Sequence Mass (Da): 48280
|
A0A955G1C9 | MVSARTYYRLTKPGIVYGNVFHAAVGVLLAHASGLTLLWSGGGLILGITAVIASACVANNIMDRRIDSKMARTKKRAMVIGQIETPSAVLFALVLLTVGVTVLVRTTNFLTVILCLVAYIWYVWIYGWAKRTTWWSTVIGTVPGAIPIMAGYTAVTNYLDLSAWLLFAMLVLWQLPHFYAIALYREKEYRAAKLPIISVSLGRHQTWRQMAVYGTLYVLSLVGLVIAQTFALIPGLIILAAGAYWLVIIFRGRTHVSDTWARHVFRLSLLLTIVLFVASSITVVIS | Pathway: Porphyrin-containing compound metabolism; heme O biosynthesis; heme O from protoheme: step 1/1.
Function: Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.
Catalytic Activity: (2E,6E)-farnesyl diphosphate + ... |
A0A7T5RVC6 | MTRRIGIYPGTFDPVHDGHIAFCLEARKVCGLDTVYLLPEANPRGKRDVTDQQERIRLLGEVVEKHSPLQLVTVSSPQFTVAETLPELEREFAGDELTFLIGSDVARSLYLWTDLKSLLSKSSLIVGLRGLDTQQEVHRMIREAERAHGIFANYEIIVTKHPFVSSSQIRALKASSTF | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
EC: 2.7.7.18
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide... |
A0A846ZSL9 | MQYKNKILFLIGLLGIVTIILIIVLTTLYGPMTTNSNEVEVVIPPGTSIKEIGAILEEANVIRSKNLFYIYVKLYNVGYLGSSNYILNTNMSVKEIINTLKIENNNPNQIVITFKEGIDIDEFINLVVSKTNNNNNTVKTKLKDKSFLNSLIDKYWFITKDILNEDLYHPLEGYLYPNTYFFHNKDVEVETIIIKMLDAFERDLKPLKKEMLKSDYSAFEIITLASIIELEGAKTEDRLNIANVFYNRLNKRMNLGSDVTSYYGVSVKIQERDLTVEEFNDDNPYNTRLANMQGKLPVGPICNPSKDSIIATIRPKKNNY... | Function: Functions as a peptidoglycan terminase that cleaves nascent peptidoglycan strands endolytically to terminate their elongation.
EC: 4.2.2.-
Subcellular Location: Cell membrane
Sequence Length: 356
Sequence Mass (Da): 41172
Location Topology: Single-pass membrane protein
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A0A2R5F743 | MLQIEIDGKAVEVEHGSTIIEAADKLGIPIPRFCYHKKLSVAANCRMCLVQVEKFAKPLPACATPVSDGMKIFTRSEAAVDAQKSVMEFLLINHPLDCPICDQGGECELQDIAVGYGASKTRYTEEKRVVLNKNIGPLVATDMTRCIQCTRCVRFLKEVGGMMELGLINRGEHAEITAYVDKSVDSELSGNIIDLCPVGALTSKPFRYTARPWELARRPTISAHDALGSQLEMHVKNNRVLRTIPREKESINECWISDRDRFAYEGLNSDERLTVPMIRRGDQWVETDWQSALEFASSRIKDAVAREGGNALGVLVSPNS... | Cofactor: Binds 1 [2Fe-2S] cluster per subunit.
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 ... |
A0A6I9QET8 | MERKNSFRGIQGAISKINPELLRSVITSGTAARGGPEARSPPGAATAFRHATTPLPVLTSACRSGSKGTAPLTIFYNGTVAVFDLPQDKAESILKLAEKGNVGGVLEAADPTASGHEEDLLTKLNGELLPIARKKSLERFFAKRKERYAWLCSPLLPTSFLVLLIRFGSSPLLTNKYLRPSIVLFICRPCFSMRHVGDDSLLSRRRSQTLTMSQPYKMAEREANVALVKETGTITAA | Function: Repressor of jasmonate responses.
Subcellular Location: Nucleus
Sequence Length: 237
Domain: The jas domain is required for interaction with COI1.
Sequence Mass (Da): 25744
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A0A7X8BU13 | MNLEKFERIYFAGIGGIGMSAMALFFLDNGKKIAGYDKTPSDITQNLEKLNVPVSYEDEISTIPEAFRQNPENTLVVYTPAIPSDSIILNYFKDHDFKVAKRAEVLGWITKDRFTIAVAGTHGKTTTSWMIAHCLRTAGIDCAALLGGISVNYKSNYLKPEREDCRIMIVEADEYDRSFLQLNPDIAVVTSAEPDHLDIYGNENELLNNFIQFTHKIKQNGTLVKSNMVNLPKPEGISAMITYGNDNKCDISIEKSRISDACFTFDCRIKERVLTNICMGVPGYHNIFNFMAAMGVLSSLTEIEEKTIKKAAESFCGVKR... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation.
Catalytic Activity: ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine
EC: 6.3.2.8
Subcellular Location: Cytoplasm
Sequence Length: 462
Sequence Mass (Da): 51808
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