ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
|---|---|---|
A0A845MHK2 | MLNRITKISEQILLVIACISVAIMVVVISADTLLRYVFNSPLSWAYNLTTYYLIVICFYFAISATFRDGVHISIDLFRFGMSKNVRLIADITWVLLSIIAFGLIAYANWKSIFETFVQNQHYEGIISWPVWLSYVPIFVGTCVLIIRLTLHVIALITKGNDPEVIFDGEQST | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 172
Sequence Mass (Da): 19563
Location Topology: Multi-pass membrane protein
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A0A3D4YFQ2 | MKKGFPNHPYIPNSVPEVEKEMLDFLGMESLDELHKNVPDALMFKGEMNIPEAFGSEYEMRRYVEELLDRDGDGKKYLNFLGAGCWQHYVPAICDEINSRGEFLTAYGGEPYNELGRFQTQFEYQSLVAELVGMDVVNVPAIDWAQAAATTCAMAQRKTGRKQIVLPEILDPQKRAIIENFCRATTEFITVACTEDGQIDLEDLKKKVGTETAGVYFENPNYLGVIETRGAEISRIAHEAGA | Function: The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein.
EC: 1.4.4.2
Catalytic Activity... |
I4YB15 | MSGQSLYRHLRNWYRVGLRDGWAQLNEWVDVKAGRLAGTDKFGNRYYENLEEEMPEVPWRQRWVRYAQEAPLENASQVPSEWHAWLHHTRLNAPHEDEVVKKITAQTQHWRPAETHVENLTGTRGAFTTYNTTAPKLYPWQPKVAQRQ | Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
... |
A0A970S4K3 | MAKRILVIGSANIDFVLTTSSIPAAGETLVTDGTYNFIPGGKGANAAITAARLGGEVIFCTRIGDDAYGDRLARIYAENGIDRRFVKVDPMEQTGLAVVMVEPNGTNRIIVYPGSNKNIGESDIEASFLTYPDIVLTNLEISALSVEYLSRLAFRNNLPLVLDCGGVTSDFSIKNIKKVEILSPNENEAEYLTGIRPDSLDNCLKACIKLCNMTDIKYVVLKLSTRGSYIYDGKYCDICGPYEVTAVDTTAAGDAFTAALALEYIRNGNDIHSACRYANAAGALTVTKRGALNSLPSEEEVKKFMAENKQI | Cofactor: Requires a divalent cation, most likely magnesium in vivo, as an electrophilic catalyst to aid phosphoryl group transfer. It is the chelate of the metal and the nucleotide that is the actual substrate.
Pathway: Carbohydrate metabolism; D-ribose degradation; D-ribose 5-phosphate from beta-D-ribopyranose: step ... |
A0A4P7J1N4 | MPFGLLKRRRFKHRLIRAILISLLCVLLGLISTLWQAASNLQRTTNIRMTNARQLVERTLDSARKASLDVKEYHGKPCLEPVELQLRMQVAYSQHLRSINLVRGHKIYCSSLYGNNEENINFDSYTNGMLYLMSDTRVRKGQPLIIYRMVVGHDSIVVRLYGDHILSELYVMSINLPLALVVGRQQWQTSAAPLFTSDMPGYMEQISSRYPFRIATVISSGDYAYYFWIFSRFTLLSWFLLAAIVGFGVFRWSGRLITVEYELLQALNLQEFIPYFQPVVSGEHSQWVGCEVLIRWSHPNLGIIPPDSFIPLAESCNLII... | Catalytic Activity: 3',3'-c-di-GMP + H2O = 5'-phosphoguanylyl(3'->5')guanosine + H(+)
EC: 3.1.4.52
Subcellular Location: Membrane
Sequence Length: 508
Sequence Mass (Da): 58239
Location Topology: Multi-pass membrane protein
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A0A3D2KNP7 | MSGGVNRLLRATAPRRGAGPKRLAPGAASLVCYPCVRTPVRGRSGGTVGLSRSGRRAPRARSGRAGRREDGTWVEVRSYLLYLAVAFALAVALSWSYSTAARLGYHINELKSEIAALERERENLSYQLSSLTSMARIEAEATGRLGMVHPDKVRVGSPVGSLTGRGSDREHDVARVIALAPPGDRPFHAEGIAAVPPEEGRSLMGSLWERFYRWLTGASLAEAKDWD | Function: Essential cell division protein.
Subcellular Location: Cell membrane
Sequence Length: 227
Sequence Mass (Da): 24538
Location Topology: Single-pass type II membrane protein
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A0A2N6AT81 | MKKIPNALTIFRIALAPVFIYVYFSKFENHHLIALSVFLLASLTDVLDGYLARKYNVISKLGIALDPLADKIMLLSVLASFYSDNLIPAIIFFLMLFIESTLIASGALVYFKKDLSVMPSNRLGKGATFAFTFAIVLVFLMPGSALSLAAVILAAMMKTAAFIG | Pathway: Phospholipid metabolism; phosphatidylglycerol biosynthesis; phosphatidylglycerol from CDP-diacylglycerol: step 1/2.
Function: This protein catalyzes the committed step to the synthesis of the acidic phospholipids.
Catalytic Activity: a CDP-1,2-diacyl-sn-glycerol + sn-glycerol 3-phosphate = 1,2-diacyl-sn-glycer... |
A0A8H6EXQ5 | MSKDVVNTGETADDKKPEKSELKWLGETLQYKTGLGMNNDEKKKFEKEKKAHDDEKQCDKCLEYRNWALRYSPNVRFMLDQIGNLGGEVPSDKMKCEICTDPKYGGFHPELGIQLCANYIPDKWVLNDTLSHELVHWYDNMRFQVDWLNLRHHACSEIRAASLSGGVCNNDGILETCRIYEGCKGSPEMCEKKSHSECFGPSRM | Function: Has a dual role in the assembly of mitochondrial ATPase.
EC: 3.4.24.-
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 204
Sequence Mass (Da): 23420
Location Topology: Peripheral membrane protein
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A0A455UD71 | MEKRQELYAGKAKSVYTTDDPDLLVLNFRDDTSAFDGKRKSR | Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate: step 1/2.
EC: 6.3.2.6
Catalytic Activity: 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + ATP + L-aspartate = (2S)-2-[5-amino-1-(... |
C1AAZ7 | MSQPRGPAGAARAFRCQPGISDGRNGCVTFLVVSFWCRRGPCCIVGDLMVPPDPTPHRRRVASPPPTDPQTRAEALSVAAKALRAAEHVCVLTGAGISAESGIPTFREAQTGLWAKFSPQELATPQAFASHPSRVWQWYAMRRAMVRAAQPNPGHAALLSLALRVAHCTIVTQNVDDLHERSGVREPIRLHGSLMHIRCSQGCAGSVPAPEEATAEVPKCPQCGGLMRPDVVWFGEGLPMGPFGAAREAAVACDVFLSVGTSNIVEPAASLPWISATHGATVIVVNPTMEGQRKGPSILPIEGPAGVMLPRLIAEAFAGR... | Cofactor: Binds 1 zinc ion per subunit.
Function: NAD-dependent lysine deacetylase and desuccinylase that specifically removes acetyl and succinyl groups on target proteins. Modulates the activities of several proteins which are inactive in their acylated form.
EC: 2.3.1.286
Catalytic Activity: H2O + N(6)-acetyl-L-lysy... |
A0A7C6FR26 | MKKILALLLTVLMLLPGLSILSEGTNTEPNSRPALGSDPIYDGIVIEPNRLLEQASTVTPVEEKAANTTLCVSYSVIPLNTAKTNPLAKPQIIAGVNSGTTDDELRMWKQMGINAVELSVKEEELNYEALYPIVERLRNFEHGGFEILLASYYRYQKNTIIHLQLEGWEEEIEKFKDYLRLMDSVNIRTVAIAWQPNGISRTGDVPVMIHGANASATDMEKLDPMELKNDRYYTREEMWKTFGDFLERVLPVCEETNVRMALHPNDPPVPYLGGVGSLIISSDDYRRAFELANDSPYLGMKLCTGCMLEGGLLFTDDLLG... | Pathway: Carbohydrate metabolism; pentose and glucuronate interconversion.
Function: Catalyzes the dehydration of D-mannonate.
EC: 4.2.1.8
Catalytic Activity: D-mannonate = 2-dehydro-3-deoxy-D-gluconate + H2O
Sequence Length: 425
Sequence Mass (Da): 47703
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A0A257A887 | MYDVSTSVDYNTWINRKRAFLRRLERDLVTGYFDMELYTLIKLLNSFDDMFTLSSCSGRLMLFSSKRPWDRKSIKIYLKKHNKACVSEVIKTLEESKDKNLWFVLQPPILHVSCLTVDRAQELLKLARNVGFKHSGIISFARTGIVVELRGNEHLEVPLKLKGKLICRKTRLKTLVKWANRMLIESKKKIFKLESEIKRNWLERKR | Function: S-adenosyl-L-methionine-dependent methyltransferase that acts as a component of the wyosine derivatives biosynthesis pathway. Probably methylates N-4 position of wybutosine-86 to produce wybutosine-72.
EC: 2.1.1.282
Catalytic Activity: 4-demethyl-7-[(3S)-3-amino-3-carboxypropyl]wyosine(37) in tRNA(Phe) + S-ad... |
A0A2U2C3Z3 | MSTQPSGPRMRLSFSGTLRGVAAFAVVALLMVQIVIVALRYVFSLGAPWATDLLTYLFFLIVSLPLVGVILNNESVRVDVFSGRFPPRLRRAIDRVALLGLLFPASAWAAWNAVPMVRTSWRVLESSPTLGGLPGFFVLKTVTALVFAALALVALIVGLRPGLYGKDDQT | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 170
Sequence Mass (Da): 18387
Location Topology: Multi-pass membrane protein
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A0A3M8ADM8 | MTLGMQLLLLQVAIVLTTVVGTGVTAMLLQEHQLREAYQDRMIAVAQSVAGLPAITDAFDDPDPAATIQPVAEVIRRASDVTYVVVANEEGIRYSHPNPDRIGEKVSTDPAIPLSGEIYVGTQTGTLGESWRVKVPIFDDDGNVMGQVSVGILESELRADFLGGLSGLLVALVVAAVIGVLGSAWIGRLIRRRIYGLEPDEIRAMLETREAMLHGIREGLVAVDDNGRIVLMNDAAARLLDVPDPAAVLGARVEDVLDRELARFIASGEDRETPVLSGERVLLVHGDRVRVDGREVGSIAILRDRTELETMLRELEGAQG... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 556
Sequence Mass (Da): 58470
Location Topology: Multi-pass membrane protein
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A0A358PWU3 | MLMLIRQITTDILIIGGGLAGLSAAVEAAGTGHKVTLVSKGKAGRSGNTVITQNNMSVVWDGLRTDDSVERYIEDTMAGGANLNDRALVQILASEAAEAISWLMEQGVEFQKDKDDLLIKGSPGHSRFRTVRAVGVSKSNRTLGLGLSVPLADRAKGLGVELMENVIIVSLLVDIGRVCGAIGLDKKEAIVYILHADSVVLAGGGAGGLFELTTNTSDVCGDSFALGYLAGATTRDMEFIQFHPTVTVATPRLVISTAPFADGAVLRNGLGEAYMGRYSHQADMANRDVMARANFEEILRGRGTDRGGVYVDFSNVAQEV... | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate from L-aspartate (oxidase route): step 1/1.
EC: 1.4.3.16
Catalytic Activity: L-aspartate + O2 = H2O2 + iminosuccinate
Sequence Length: 520
Sequence Mass (Da): 55576
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A0A0K0EDW9 | MRKVIIVAGAATAAAAGTTVVAAGLDPKIRHQVEEAVPKSKDVFNYVLGSSESSIKHVKDNTTSSLVVAPKKVYQPPPMDIPTIKEETEKIPPKKSFEVSPIEVKQNVTDNSEISLAERKVKANHEIENKLIETLTNAQEKIQFANSAKIFTCEGINNYTKTFKQAVDSGADADWSTVTQAKKHVEKLQAEDKAAEVEALKLVSKLEKIIDEGKNNPLTAANPLVYNAAQTVYKLKAEIDRTNLLIKQSSSEIDLLRDYKNLVEESRKSFLEEVKAVAPSMDTNATGSALTEKELNNLLVHAHLKVSKLSKRLIEQELRE... | Function: Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane.
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 64... |
A0A0K0E7Z9 | MNPYSSKVSEYLELIQCVPLDTAEFVFAYGSGAISQGNENMKDKMVDFIIITNDPLKFHADNINKNPSHYSFLRKIGPKRITEIQTKFGARVYYNSRVESNNRMIKYGVISTDNVLQDLLDWNWLYVAGRMQKPILNVLKPTKKIEEAMEINHTSALQLALLMVEDTFTFENLFKHIVNISYNGDFRQVIGEDKNKVNKIVHGSYDKFMDIYKPLLEKDPRVTVLSDKCEQDNTTQAVYHRINLLPLGVINCLQEKWKRKNEPRKDVEEISFTLANRTDFDVIIRDMTSSIVAKSSRNQTIKNALSAGFGKSILYTSSKL... | Pathway: Lipid metabolism.
Function: Catalyzes the conversion of phosphatidic acid (PA) to CDP-diacylglycerol (CDP-DAG), an essential intermediate in the synthesis of phosphatidylglycerol, cardiolipin and phosphatidylinositol.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphate + CTP + H(+) = a CDP-1,2-diacyl-sn-gl... |
A0A832YZU7 | MAIQLERTIRARGGKTVTIYMKISNCRILDIAITGDFFSYPEDAIERLERALALCASIACIELAIDTISRSAHLLGVEWEELKQYLVDMFRLGCQ | Pathway: Protein modification; protein lipoylation via exogenous pathway; protein N(6)-(lipoyl)lysine from lipoate: step 1/2.
EC: 6.3.1.20
Catalytic Activity: (R)-lipoate + ATP + L-lysyl-[lipoyl-carrier protein] = (R)-N(6)-lipoyl-L-lysyl-[lipoyl-carrier protein] + AMP + diphosphate + H(+)
Sequence Length: 95
Sequence M... |
A0A8B6FB89 | MKPLNITSQAKSKRSDKSWYILSAGLIISVTVIFILDLQFFASTNFIRNTLNGKMLEVLSAADNFTNRFIDTMKHKLIIIDSDIPDSASEQHVTDRFSNHGNCTWPPLNLQGRTPLNRTDIPIEKLDKKYTFMADGHYKPKNCTAYQKIAIVVPYRDRQLQLRIFLNNVIPRIHRQQLEFGIYIVEQTAGSLFNRGMLSNIGFVQAMKDMAYDCVVIHDLDILPEDDRNFYICGDNPIHMATKVEKFKYRVPYHSFAGGISTFSRKQYEDINGFPNQFFGWGGEDDELFARIKRSNYKMTRPFDAHGHCGSVQHSGQRTG... | Pathway: Protein modification; protein glycosylation.
Function: Catalyses the transfer of galactose onto proteins or lipids.
EC: 2.4.1.-
Subcellular Location: Membrane
Sequence Length: 380
Sequence Mass (Da): 44111
Location Topology: Single-pass type II membrane protein
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A0A8B6FVH7 | MTKKILLIGVMTTKKYLDTRAVAAFNTWTNYCSGTCKVIFFSSEGSTTEKQIPLVSLDSIDDSYPPQRKSLLMLKYMHDNYINNFEWFMGADDDIFVIGNKIEKFLRCKQLCSPFHWSSWSRKKEEKGKLNRHEIHCMGGPRILFSHTTLRHVGPHISICIDNLLTTHEDVEVGRCVRRYTGLSCTWAFEVEDNINQVLQLMNKDAHQKGKMIDFKDLWYGYRRVSPLHGVDYKLDLLITYCKDKGDKMTAPVRRQVYLHQTFREVEFIEDPSTASSNIEYKASDSLFIFISLGKG | EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 296
Sequence Mass (Da): 34324
Location Topology: Single-pass type II membrane protein
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A0A2V2DVP9 | MKSIKINVTRLEITLYCVLAVFSFATMAVQLWLGLAELVFTAIYIAFNLITLEKRNRHLYTYLQNITSYLDEATRENLTNFPMPITLLNDKGEIIWYNELFHQVLHDGHIQEIFGQKVHAINKNISFENVKKHQSGKYDITFADKKYTVYILSQGEEGKDHFYAVYWMDNHTLHEQINKLRGDTLCVAYILLDSYDEIPENVTALQKTNFVTRVDVRVRQLAKMVNGLVQKPETDKYMLIFERRYLEALKESKFKILSEVKDIRIENILHATLSIGVGIGDGDILKTDEAARSALDLALSRGGDQAAITNTEKERFEFYG... | Cofactor: For phosphodiesterase activity, probably binds 2 Mn(2+) per subunit.
Function: Has phosphodiesterase (PDE) activity against cyclic-di-AMP (c-di-AMP).
EC: 3.1.4.-
Catalytic Activity: 3',3'-c-di-AMP + H2O = 5'-O-phosphonoadenylyl-(3'->5')-adenosine + H(+)
Subcellular Location: Cell membrane
Sequence Length: 665... |
A0A7C6S5A0 | SIDYIDLDKKSIDSLGKSIQVLGNDLTPLEYNGQYGNAVKISELPDYVPKAFVAIEDKRFYKHKGMDYIRIMGALLKDLKTMSFKEGASTISQQLIKNTHLSNERTIKRKLKEIHITRQLEKNYTKEQILEKYLNIIYFGNGLHGIESSSKAYFSVPAKELNIAQAATLAAIINSPAKYNPYNNWDNLVNRQKKVLKAMLKNGFITNAQYQEAINTTVRFNHDKQKKCQDIYTQHAVRQACQYINGSEKDLADCVIYTYYDRDVQDIISKTFDNFLPYTQNKHGVLPDYAGIIIDNGANSVIGLIESNDNNIITKRQPAS... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-term... |
A0A355JFZ5 | MNIMAVICEYNPFHNGHAYQLKTHRTLLRADGVVCLMSGSFVQRGAPAVFDKWTRAKAAVMCGADLVLELPVVYSAQSAMRFAAGAVSLLNELGCVNYLSFGSECGNIQLLQNSEPVVFSDEFARLVCAEMKKGTSYPAARLSAAKNYFPALSCDLLSSPNNILALEYVHALARLKSAIQPITLKRNDSFASASQIREMMDQGRDISEFVPNKAAFHTTPYDKSVFDQLVSYQFRRETPESLKTITDVSEGLEHRFIKVAKTSFGAEELATQVKTKRYTRTRIDRIIVNTLLGITGADTELPPQYARVLAFNKCGTQILK... | Function: Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at the wobble position of elongator tRNA(Met), using acetate and ATP as substrates. First activates an acetate ion to form acetyladenylate (Ac-AMP) and then transfers the acetyl group to tRNA to form ac(4)C34.
Catalytic Activity: acetate + ATP + cytidine... |
A0A3D5B398 | MRYGKAVIVGLVQGLTEFLPVSSSGHLALLARLGIAPSSVFFNLTLHLATLCALLLVMRKEVLFALRHPIRGKGFYVVIASLPTVGVALLVKKLCPALLLGSMLGFGFVLTSVVLFLAETVGKGSKERELSGKISLLTGLAQGIAVLPGVSRSGTTIATLSCCGVERVQGAKFSFLLSIPVIVGGFLSEGMESGFSAAGASFPEIALSAAAAFISGVIAVRFMLNIVKKGLKPFIPYTFALGILCYFLP | 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: 249
Sequence... |
V9P7Z6 | NNLSFWLLTVSLLLFMGSAYVEAGAGTGWTIYPPLSNSKHHLGITVDYLILSLHVGGASSIMSGINFVTTALCMRPGVMTLLXTTMFVWCIAXTGFLLICXIPLLAAGLTMLLTDRNFNTAFF | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
A0A524QEA5 | MKEFINDDFLLQSETARSLYHHHSSRMPIIDYHCHLNPEHIESDRRFDNLGQLWLEGDHYKWRAMRTNGIDEKYCTGKETTDREKFEKWAETVPYTMRNPLYAWTHLELKRVFGIDKILNSSTAAEIYEECTAMLQQPGYSARGLMKKFNVEVVCTTDDPADDLAHHLALRNEGFEIKILPTWRPDKSMAVEDPEKFRNYITNLSAASGVTISSFVTLLEALRKRHQFFADAGCRLSDHGIEQFYADDYTEKEINDIFKRVSSGRNLTPEEISKFKSAMLYELAIMDWEKGWTQQYHYGAIRNNNSRLFRKLGPDTGFDS... | Pathway: Carbohydrate metabolism; pentose and glucuronate interconversion.
EC: 5.3.1.12
Catalytic Activity: D-glucuronate = D-fructuronate
Sequence Length: 358
Sequence Mass (Da): 41618
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A0A061FCA3 | MEGAKDRLQPPTYGDLITILSIDGGGIRGIIPGTILAVLESELQKLDGEDARLADYFDVIAGTSTGGLVTGMLTCPNEKNRPLFAAKDIKDFYLNYCPKIFPQPGCPLFAQTSKVIKALSGPKYDGKFLHSLVKEKLGDTRLHQTLTNVVIPTFDIHHLQPTIFSSYQVTLVAMGEVSKEIIKGNADFFPIKPMDYGRFLVISLGTGSRKAEEKFSAQEAAKWGLLGWLTSGGSTPLVDVFTQASGDMVDLHLSVVFEALHSDKYLRIQDDTLSGVVSSV | Function: Lipolytic acyl hydrolase (LAH).
EC: 3.1.1.-
Sequence Length: 280
Domain: The nitrogen atoms of the two glycine residues in the GGXR motif define the oxyanion hole, and stabilize the oxyanion that forms during the nucleophilic attack by the catalytic serine during substrate cleavage.
Sequence Mass (Da): 30455
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A0A061DTL0 | MMMRSIIIIIIIIIISCLHCRSHIATMGTATALCHQRFTQAPPVSMNFLNVLSVPILCTLLFIRVHNRCPTCRQELGDIRCLALEKVAESLELPCKYTSHGCPEIFPYYSKLKHEAQCNFRPYNCPYAGSECSVVGDIPFLVTHLRDDHKVDMHSGCTFNHRYVKSNPREVENATWMLTVFHCFGQYFCLHFEAFQLGMAPVYMAFLRFMGDEMEARNYSYSLEVGGNGRKLIWEGTPRTIRDSHRKVRDSHDGLIIQRNMALFFSGGDRKELKLRVTGRIWKEQQNPEGGACIPNLCS | Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.27
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Length: 299
Sequence Mass (Da): 34247
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A0A3B9KVG7 | MDVLMNYFEKGTFGWLSIVDAVFVLIFLIAVMVFFFRKKNYRVGLFFVLFTLLFIGLDVVIAVFKIRSIFFAREIMRFLAVMFIAASAVVYQSDLKLLFAKFGGQAEENVYAKLHNGRDEDDLRYASGEIVKACQNLSKNNIGALIVVCPTIISSNMLDTGIRLNGALSAPLLESIFNPHSPLHDGAVIIKNNVVLAAGCFLPLSQNPSISKDLGTRHRAAIGITEETDVLTIVVSEETGIISLVQNGDIKRYITGEKLMDALDAAFGITDLSRRNSRQFGRNTKR | Function: Catalyzes the condensation of 2 ATP molecules into cyclic di-AMP (c-di-AMP), a second messenger used to regulate differing processes in different bacteria.
EC: 2.7.7.85
Catalytic Activity: 2 ATP = 3',3'-c-di-AMP + 2 diphosphate
Sequence Length: 286
Sequence Mass (Da): 31726
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A0A8B6CER1 | MQKMADIVFALFLPMWIITRLMVYPYVILYSIYIDLPAYANENRPYIQMHDRSTIGQVLKSLLVVLQILHVMWTIIILKSAATKFTKGKLQDTRSDTEEEDGNEANTETIDNKSNYKISNGNSVIGKDGNVMEPNGNRYSNGRT | Pathway: Lipid metabolism; sphingolipid metabolism.
Subcellular Location: Membrane
Sequence Length: 144
Sequence Mass (Da): 16437
Location Topology: Multi-pass membrane protein
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A0A367KNS6 | EQAVKTQLEEHRIILSAREKEIEALKRDRQTLLQDEDRLLSLFKLSEEQLLETEYIKTLQLSIDHYRSRCHDLEQRRVDLERDLDKMSAARKQLIDQVKTEKISQNMTMESEIRRMEGDLNRIRGQRDSFQSLVDEQKMKENREKESQEKIMSFATQGKTRISSLESRIDRLKNEQEMAGPFEKEATMYSNLKEQLIQMDILLSSIELIENRDVESILCFDTESLQKSLEKCNSHPLVKEYDQVLEESRKATLMADFFEKNEGHLLEEIDRVASIYGKLEEQQGKKVFDFSQKRDQILKLQAEVEKENELRKLNRNIEED... | Pathway: Protein modification; protein ubiquitination.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
EC: 2.3.2.27
Subcellular Location: Nucleus
Sequence Length: 4... |
A0A238GJB8 | VWGHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLGGMKSNKFSPLGLWFTGFLFLFTMGGLTGIILGNSSVDVCLHDTYFVVAHFHYVLSMGIIFAIVGGVIYWFPLILGLTLNNYSLVSQFYIMFIGVNLTFFPQHFLGLSGMPRRYSDYADCYLVWNK | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
A0A358ASA5 | MNAIIGMTTLAHKTDDLPKIKDYLEKVEASSRQLLAIINDVLDMSKIDADKFEIVKKAFDFEKMLQNVFNVVQVRLDEKGQQLCFKTNRPFKRLIVSDELRLSQVLINFLNNAIKFTPENGKITLKVDQDECGEGKVRIHAKVVDTGIGIEEEAQKKLFRSFEQADGGITRQYGGTGLGLAICKKIIDLMGGEIGVKSRLGEGATFLFTIEAELGGAIRDAAKPANAKTLSVLVVDDQTDVLEYFQKILAGFSVRCDAARSGEEAIGLAQKRLQGGGGYDMVFIDWHMPGMRGGEVAREIKRIAGEDAVVVIMSVSDWHD... | Function: May play the central regulatory role in sporulation. It may be an element of the effector pathway responsible for the activation of sporulation genes in response to nutritional stress. Spo0A may act in concert with spo0H (a sigma factor) to control the expression of some genes that are critical to the sporula... |
A0A7D9GZ90 | MAKLKGYTLDVGYPVYGAKFVNNKTLIVAGGGGEGKNGVPNKLTAIIVQPDHKKKPLKRYRELVLNEEEDCPMSLDVNNSVILMGVNENSEMIKRGVNKHLRKFKFINEHLKFVESCQIHPEANPQQYQKITSLSSDGSLGVIAMSDNPSSIYIVDTSEDLEERFKIVTNGDVKDISISPDGKLMCYITSSHLEAISTITGRSVFKTDIDFHMTKVGFYDNNIVVIAGSQKSGIIVAHYSIAKSQVVKKSVVYRNLKGVTSMDVNPESGLVALSGSDCSLMLVRFKDLKLLKKVNKVHNFAITKVTSSQDGHYIASVSAA... | Function: Guanine nucleotide-exchange factor (GEF) required for the formation or budding of transport vesicles from the ER.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 930
Sequence Mass (Da): 99749
Location Topology: Single-pass type II membrane protein
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A0A7J3I9U1 | MGITLKCRVIKLSESRIPNIYLINMSCGETSIQMDIHRSINVVKEGDLAEVVVDREVPTYVEGKDLVAHGYVISKRGADGNTRIYVSIWGYLVVIDTSNSAVADFFNYMDKVYIKISV | Function: DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
EC: 2.7.7.6
Subcellular Location: Cytoplasm
Sequence Length: 118
Sequence Mass (Da):... |
A0A3C1B0X4 | MTDKSRKDQNKFEEMLAYERLAWQQGYMLLAGVDEAGRGPLAGPVVAAACILDPAKPIYGLNDSKKLTPSSRNRLFSLILENAAAWQIGLADHAVIDSINILQATCQAMRQAIMELPVKPGLLLIDAVKLTGVDQPVWPIIRGDGLSVSIAAASILAKVTRDRLMDEYDVLYPEYGFAQHKGYGTPMHYEALAKYGPCPIHRLTFLKSVLNSTSDTNERNQDSRQLSFLPGDQ | Cofactor: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
EC: 3.1.26.4
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Subce... |
I4Y8B5 | MRAWYMDDIEGSFTAPHDSGVSVNADYLAKLGIQYTLNPDIEKVAIEQGYKNRDEVGISREALGDEEYKNKLNIFKVEHLHTDIEARLILDGSGYFDVRDRLNNNEKWIRIAVEKGDLIILPPGIFHRFTTDDNGYTRAMRLFTDEPKWQPYNRSNEVEKDPSHLDYLKSIGITA | Cofactor: Binds either 1 Fe or Ni cation per monomer. Iron-binding promotes an acireductone dioxygenase reaction producing 2-keto-4-methylthiobutyrate, while nickel-binding promotes an acireductone dioxygenase reaction producing 3-(methylsulfanyl)propanoate.
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis v... |
A0A0K0ENU4 | MILIIYFLSFFIIPLSQSYKILICNPKIGYSHVNFFGQMADILHEAGHDVTVLSVEMDLSVKHPGAYKAKIINYPSNPIASEIFSKQSHINTIWESEDNTISQLNAINSWPDAMYEQGKMIFNDKNFTLKMIDEKFDFAITEALGHYFVGLFKVWGIKKYALGSAVSLLNSLYDEFGLQFPASFIPTVMNYFGNDITFNDRFLNLISHWMTLLYTVWKWNKSTLHKEFNEKYGKNFFDIRKSISDTSFFFINSNPFLDYPGPKVPKMIEIAGIGIPKPKPLNNYWDRILSKNKYNILISFGTISKCQNMPDKKKNAIINT... | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
EC: 2.4.1.17
Subcellular Location: Membrane
Sequence Length: 524
Sequence Mass (Da): 60372
Location Topology: Single-pass membrane protein
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A0A7U3QAJ2 | ALIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWMLPPSLTLLLASSVVENGAGTGWTVYPPLSSAIAHAGASVDLAIFSLHLAGISSILGAVNFITTVINMRSKGITLDRMPLFVWSVVITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
A0A316RLM1 | MKIRIKPALILSALIILLSVCAGFLPVFAPATGPQTAVPSSDGFSDGEKVYFSGAAVSTSAAADILMEQSGIILSGKNISARMGMASTTKIMTALIAIERLDPDSVVSVPKKAVGIEGSSLYLTEGEKTTVSDLLYGLMLESGNDAAVALAIAVSGSEEEFVALMNRRAEELGLEDTHFVNPHGLSDDDHYTTAYDLAKLTCAALENETFERMVSTGTAVISDGRRTLYNHNRLLGSYEGCIGVKTGYTIATGRTLVTAARRDGMTLVAVTLNDRSDWADHAALLDYGFDNFFVQPLSPPSDMSVPVVGGKAESVAVRSA... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors.
EC: 3.4.16.4
Catalytic Activity: Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanin... |
A0A7C6Y3R1 | MEKENLRKRIDEIDEQFIQLLEERLDIARAIGEEKKGQGLPILDMAREREILNRMAERAGDKNETYAKLVFSAILAASKNAQTHVYYKNEEKWEEKIAAAKKDAFPSRADVACQGTEGAYSQQACDKLFPMARILYSSTFEGVFKAVETGLCKYGILPIENSLAGSVSTVYDLMKKHKFYVVRSVRLKIDHALLLPKGAKFSDIREVVSHEQAISQCSEFLQQHGEWKVTRFENTAAAARFVAQSGRKDIAAIASRRCAALYDLHIERENVQNQSDNFTRFLCIAKDMEIYPGANKISLMLTLPNLPGALFQLMAKISAM... | Pathway: Amino-acid biosynthesis; L-phenylalanine biosynthesis; phenylpyruvate from prephenate: step 1/1.
Function: Catalyzes the Claisen rearrangement of chorismate to prephenate and the decarboxylation/dehydration of prephenate to phenylpyruvate.
Catalytic Activity: H(+) + prephenate = 3-phenylpyruvate + CO2 + H2O
EC... |
A0A3D2G5K2 | MWALTLIYTVFTLLNLGTLSFPTSVWTAQSGAAVRIDLGAEYDVAEIWTNGNIAEGSAVFTGDDGSTAEYTQKYATMFTWRTQTAAMHTRYITLQCTAGKVSLNEIAFFDAAGNRLPAVIAAGTTEGAALLDEPDTVPDEPSYLNGMYFDEIYHARTAYEFLHTMSVYEWTHPPLGKILIMLGVVLFGMKPFGWRVVPALFGAAMLPVFFTLAKRLFRRRDLAFLAAALLALDTMHFTQTRIATVDVFILFFILLMVLFMTDYIQMDYMKEPLKKLFLPLGACGVSFGLGVASKWTGLYAGAGLAVMFFAHMIRTGIACR... | Pathway: Protein modification; protein glycosylation.
Function: Transfers mannose from Dol-P-mannose to Ser or Thr residues on proteins.
Catalytic Activity: a dolichyl beta-D-mannosyl phosphate + L-seryl-[protein] = 3-O-(alpha-D-mannosyl)-L-seryl-[protein] + a dolichyl phosphate + H(+)
EC: 2.4.1.109
Subcellular Locatio... |
A0A1G4MAZ9 | MTKTVVVTCGATVPFPKLIEVLLEIRTLEKVRSLGYDRIILQYGRGFNLKFKQLLAAVNGIKCKPAGTNGSLSAKELGNDHFDVGDYRGVEILGLDFTPNILQLISAHADVVISHAGTGSILDALRASKPLIAVVNTSLMDNHQRQIADKFESRGYLWSADPRAEDVIASLEKAQYGARSTLPNGFNSAFEQLLAETAYS | Function: Involved in protein N-glycosylation. Essential for the second step of the dolichol-linked oligosaccharide pathway.
Catalytic Activity: N-acetyl-alpha-D-glucosaminyl-diphosphodolichol + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N,N'-diacetylchitobiosyl diphosphodolichol + UDP
EC: 2.4.1.141
Subcellular Location... |
A0A101XED5 | MDAAGLLLSVTSVSSVYFASSEAWLTMLMFAWLPVAAYGLYLVTRFVSRRGVDAVGLLTMAIVVALFAISIMVIAQAGIPIAAAPQQIVSTTQPAIPSSDWLDALYWIQYNTPKASVLASWWDYGYWLAIMGNRTSLADNSTVNGTQIALIASAFTTTNVTKALELLHSVGANYVVVFMPYMAFPITVPSPMSALSIGGSSQSYVALCGLYPEYPTGGDFVKSYWMSTISGNSREYTNTHILSAAEIVYSTPSGGVNTLNLYVPLTNTTLYRLLFDLEAPAYSLDVDQCLVQLRSMTTATPFTLPLWLFNTWPTYSQSSS... | Pathway: Protein modification; protein glycosylation.
Catalytic Activity: an archaeal dolichyl phosphooligosaccharide + [protein]-L-asparagine = an archaeal dolichyl phosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine.
EC: 2.4.99.21
Subcellular Locat... |
A0A1W0ABD4 | MLQRVRKFSATAESRLFLRDLKAVPRDMRRKLRLEAENSAGINPAAKNNKTPASRLILRTIFGATGLGVAAWHFYLSEEAKSNISQNINDSFVGSIADYIAAQVQEMASPFTKPSRDKLLPDWPMINRGVPEGYPQIPVLVLGVEDRKFGWRHAKRPHVDEFLETLARYYEIVLFSSEPRMMVEEVLAKLDSKQCAFHYLTREETHFLNGTHVKDLGPMNRDLRKIIVIDHKPENFQLHLSNGVTIPPYLDGADRSDRVLKDLIPFLEAIGKENVQDVTKILSEFKDQDGIIRDVGPKWNTKLMALEERKRQNEAKGFGG... | Function: Essential component of the TIM23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane.
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 589
Sequence Mass (Da): 67645
Location Topology: Single-pass membrane protein
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A0A924AAN9 | MNNMMQRAITGFFFIGIIISCVLYNVWSFGILLALINLLCIWEYLGITVKENKKLHQISGIITGSLFYVCFVLNIIKYASFEILFIPVILIFCVLIFKLFTKETNPFEGFGQILVSMVYITVPMVLLFKLSFTAYNYFSLIPLLIFISIWSNDTFAYLTGKAFGRNKLFERISPGKTWEGFFGGIICNILIFNLFSYFFLSPKSGYEITPWLIILPIIISVTGTLGDLIESMLKRSYGIKDSGNMLPGHGGFLDRFDALLFLIPFVYVYMQIS | 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: 273
Sequence Mass (... |
A0A511W634 | MTTIALIGFMGSGKTTIGQRLARSMEIPFVDTDDEIVNRVGMSVPEIFDHFGEQYFRSVESEILKSLSKKKCVVATGGGIIKLDTNRQMLRSDDFLTVWLDLTFDTVMKRIANDESRPLWNQDVEKRMSLFNSRQALYDDSSHFSVNVDGQPVEELIEEIKRYIYSYTMFGTKRQSDENR | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.
Function: Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
EC: 2.7.1.71
S... |
A0A3D4EH31 | MKKNFRFYIALWISKAAMLLQRMLGMNASYFPGKLAIKLCPDFLGRIDKPKTIITVTGTNGKTTCCNMILDVLTENGYDVLNNKAGSNIDAGIASSLLGDASLLGHIKKQIAVFEVDERSSLKIYAYVHPDYAVCTNLFRDSIGRNAHAEFISSIIERALPDDTHMILNADDPISSQLKPNNKRTYFSIARLDTDRTECVNIINDMRSCPKCGGKVEYEYVRYHHIGKMRCTSCGFASPEADYTASPDFSTGTFTVAAPDGEETYPLMSDSVFNTYNQVTVVALLRTFGLSAEAIAASFEHMSIVKSRYTKREKNGVEVV... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: The lipid II isoglutaminyl synthase complex catalyzes the formation of alpha-D-isoglutamine in the cell wall lipid II stem peptide. The MurT subunit catalyzes the ATP-dependent amidation of D-glutamate residue of lipid II, converting it to an isogluta... |
A0A357CVT5 | MKNKLKTYLKNSGFTLTVLFMALYCCYIIRNIDDGSNFAFHIFLVAVVIVSRFTKGYIYGFAASLLSTIGFHVMVNYPNYVFRFPDEFLSASFAAFIIVSVVICEQNTRIDEYKTKNGELVSAIEKYKTKLNLLRGASHDLRTPLTGIMGAADTLIERGDDIDDKARMRLLSDTKNDAQWLLCLTGNILSAAKVEDGTPISKRPEAVEEVAAESVERLKKHYKEQNITVTVPDELLMVPMDFVLIEQVLINLLENACIHSGQADEINLKISSENGEAVFMLTDNGCGIDDEVIDKLFEEPVFSQRSENEKEKKRNMGIGL... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 361
Sequence Mass (Da): 40479
Location Topology: Multi-pass membrane protein
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A0A8B6DR78 | MYAIELPIAIKVVDVIELSEAIEGMYAFEVPQAIRDMYAIEYPKAIEGRYAIELHEVIKYMYAIECLRRLNEYLKWGYFRGGIPPPFWSCLENSEMCASTMQSPVAIKTKNVVKNNNIEPFDLSELTETSGIKMEMTNTGLAVKVDFLDYQPTIQEGGLPGPHKLSGFHFHWGRNSGRGSEHTINGYKFAMEAHFVFLPTKDGAKNFAAVLGVMIYAGSYNPNYEQIVSKLKDIKNKGDKVVLDNFPIMDLLPKTTSCWYRYCGSLTTPPCTETVIWTLFENSISMSEYQLKEFRKLMGEPEIFTEGDNYIVDNFNQYSR... | Function: Reversible hydration of carbon dioxide.
EC: 4.2.1.1
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Length: 327
Sequence Mass (Da): 37307
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A0A172NXZ6 | VKNLIGNDQIYNVIVTAHAFIMIFFMVMPILIGGFGNWLVPIMLGAPDMAFPRMNNMSFWMLPPSLSLLLISSMVETGTGXGWTVYPPLSSIIAHTGSSVDFSIFSLHIAGISSILGAINFISTMMNMKIKFLKFNQISLFIWSILITTILLLLSLPVLAGAITMLLTDRNLNTSF | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
A0A943WTY8 | MFRIICLIIGYFFGCIQTSYFVGKKNNIDISKTGSGNLGTTNTVRALGIKVGLFTFFCDALKAAAAFYVCYFVFGENAVTAGFYGATGAIIGHDFPFFHHFKGGKGIAAMLGMMLGAFPFPALIVYIIAIAVLMSGYVSLTSLVLSVLIPISLSIWHYPTEVVVLTSALALLAFIQHRQNIKRLINGTESRFDIIGKLKPKKKER | Pathway: Lipid metabolism; phospholipid metabolism.
Function: Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
Catalytic Activity: an acyl pho... |
A0A970CTQ5 | MKTVAIITEFNPFHKGHEYIIKKAKEVTGATCCIIITSGNYVQRGEPSFIDKYTKTEVALNHGADIVFELPVFFSTASARYFSMAAVGLLDKLQVVDYLAFGVESNSLEDLSTIVQELTNENDEYKEYLRESQKCGNSFPTSRRDAILKMYGEDTAALLDTPNNILAIEYMRALALRSSNIKPIGIKRIKAAYHEDFNEIKNITDSNYICSEDSPRLYSASNLRKLSDDSLVDILSLIDNVYAWNYKKTYPVGITSDFSAITGLKLYDAIANNTLSDIFDLTLDIANKFANNFSKYTNFSSFITLNKSKDVSYTSLSRAL... | Function: Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at the wobble position of elongator tRNA(Met), using acetate and ATP as substrates. First activates an acetate ion to form acetyladenylate (Ac-AMP) and then transfers the acetyl group to tRNA to form ac(4)C34.
Catalytic Activity: acetate + ATP + cytidine... |
A0A3D5MQW0 | MRDLLALWAGRAVLKLSRRLGHGGSSLPGRVALRIQPALLRRLAGKLRWGSVIITGTNGKTTTARLLSTILQDAGYRLVHNRSGANLKEGLTSAFLEDAAAAGRRADIALMEVDEATVPEAVRELRPLGIVVTNFFRDQLDRYGELDTTVSLVGRGTDAVGGRGFVVLNADDPLVAALGRGRGERAVFYGVEDDRCGKRTMTQTREQRHCLTCGRELDYSVFYYGHLGRYACPGGDFRRPAPDVRAGAVCLEGARGASFTLSVRGEGEVRVAMPVPGLYNVYNALAALAAALELGVPLSRAAASLERARASFGRMEVIPV... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: The lipid II isoglutaminyl synthase complex catalyzes the formation of alpha-D-isoglutamine in the cell wall lipid II stem peptide. The MurT subunit catalyzes the ATP-dependent amidation of D-glutamate residue of lipid II, converting it to an isogluta... |
A0A3L5TV43 | MSESEHTCDLCYEDFDRDNHEPRKLPCCHTYCSQCLEKMVSRNASITCPNDRSIHKLGILGVFGLPLDSSKLADIDKREVTSPVGSINFSSDFVDPSRPTTARSYRQAQNPVNNNPIPVSSHREQNNTPQSTGNNYYMQPYPNMPYNYYTQFQGFSQIPIYGQQITSSVWPSPYQCHFNNTSQFYQPMMTTATTFTHDGNCGQNIIVSSPGGH | Pathway: Protein modification; protein ubiquitination.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
EC: 2.3.2.27
Subcellular Location: Cytoplasm
Sequence Length:... |
A0A455UA73 | MIKPNMATMLGFVVTDAMIETPLLDRLLRQTVDRSFNCITVDSDTSTNDACMLAATGTGPKIVDDEQIAVFSNALQQVMTELAQAIIRDAEGATKFVTLQVGEAKSRQEALDVAFTVAHSPLVKTALYASDANWGRILAAVGRAPVSDFDVNRVVIDLGDVRLVEHGGRAAGYTEAAGSAVMAQSEITIRINLGRGEESATVWTSDLSP | Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; L-ornithine and N-acetyl-L-glutamate from L-glutamate and N(2)-acetyl-L-ornithine (cyclic): step 1/1.
Function: Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of N-acetylglutamate from glutamate and ace... |
A0A101F7S1 | MRTIKLDEKEWLRLIKLHFFEQVLWRGGADLVAGVDEAGRGPLAGPVVAAVVVLDQELLIPGLNDSKKVNPGKRDLLAQEIKMKAVDWAVGIVSPRDIEEFNIQEATYQAVRKALKQLSVVPDHLLVDGWAIPGLEVPQTPLVKGDCRSAAIAAASLLAKTTRDELMKFYARFYPEYGFEKHKGYPTKEHLKALQRHGPCPLHRRNFRGVLGSSGVER | Cofactor: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
EC: 3.1.26.4
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Subce... |
A0A1V9Y6U2 | MDFECNICLDRVKEPVVTLCGHLYCWPCLFQWISEHNECPVCKAGVTKENVVPVYGRGANSIDPRVSQALDGIPNRPRGQRPEPTIRRRAPQQEPDALMGQQGQEAAFSPMIGFFPSLFGLQFVRQYNATMNMPLGHTGPVPLTPAEIRQQVQFAFLSKMLLLIGTINKMTDDGNMHNKLHGLTASEQVAIVDEHNQVIGKADRSVMRVYNLPHRATYIVIRNSKGEFYVQRRTLIKDYCPGFLDPMAGGVVQFGESFQENAQREAAEEMGIVNTPLTYITTFFYKDGRSAVWGGMFECVYDGQLTLQPEEVSEVLLMSG... | Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.27
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Length: 346
Sequence Mass (Da): 38960
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A0A7Y2TER1 | MLYVSLFFVLVQVACSGKDNAPSQQEKTYPIVKIETRLGVMHFWLFDETPNHKAKFIELANAKHYNQFTFNRVIRNFVIQGGCPDSVQYFKDSPYLLEPEFVDSIKHVYGALGMGRDDNPEKLSNACQFYVVNREMGLPNLDNNYMIFGKIIDGEDVLEKIEIEPTNANDKPKVAIPLDVGIVELSQQQLLDSFKFSIPE | 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: 200
Sequence Mass (Da): 22844
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F8ACX8 | MPERDLILDIAEIFVSLQGESTYVGLPTFFVRLAGCNLQCQWCDTVYAQQPQKNFISLSEILDRWQRGGKLKVVQITGGEPLLQENVYPLMKAFLDKGATVLLETNGSMPLERVPREVVKIMDIKPPSSEMNAYMRFENLAYLDRKDQVKFVIADREDYKWAKNVMTKFYLPVYTQVLFSPVWQRLEPRELAEWIIKDKLPVRFQLQLHKILWGEKRGV | Cofactor: Binds 1 S-adenosyl-L-methionine per subunit.
Pathway: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
Function: Catalyzes the complex heterocyclic radical-mediated conversion of 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) to 7-carboxy-7-deazaguanine (CDG), a step common to the biosynthetic pathways of a... |
A0A7C6S539 | MRQSKIKILIINGANLNMLGKREPHIYGTQTLDDINAQIQAAAPEDAELEFFQSNHEGEIIDKIHSADADALIINAGAHTHYSYAIYDALKCISIPKYETHMSDIFKREESFRHKSVLTPAVDEMFFGKGVISYIEAVFAAYNKVKKIKND | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.
Function: Catalyzes a trans-dehydration via an enolate intermediate.
EC: 4.2.1.10
Catalytic Activity: 3-dehydroquinate = 3-dehydroshikimate + H2O
Sequence Length: 151
Sequenc... |
A0A7C6S4K3 | MTFQRVAELLAEHKDLKVEEIKEDSTFESFGFDSLDVVELIMVFEQEFGVSLTISQDLKTVGDLVKLIDQTK | PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine of apo-ACP by AcpS. This modification is essential for activity because fatty acids are bound in thioester linkage to the sulfhydryl of the prosthetic group.
Pathway: Lipid metabolism; fatty acid biosynthesis.
Function: Carrier of the growing fatty... |
A0A358M949 | DIAADPSSIFDIQVKRLHMYKRQLLNILHIMDLYNRLCDDPSLEMIPRTFIFGAKAFPGYLLAKNTIKLICTVADRINRDSAVSRKLKVVFMPNYGVSLAQRMIPAGEVSEQISTASKEASGTGNMKFMMNGAVTVATLDGANVEIHREVGDENIVLFGLRSDEVIAYQKNGNYSAAEVIRSDPRLQRLLRQLQEGYFGLAPQHEFDPIVKHLTEENDPYFTLKDFDAYVRAQEKIDTLYADRNAWNKMSVINTAASGVFSSDNTIRKYADEIWNV | Function: Allosteric enzyme that catalyzes the rate-limiting step in glycogen catabolism, the phosphorolytic cleavage of glycogen to produce glucose-1-phosphate, and plays a central role in maintaining cellular and organismal glucose homeostasis.
EC: 2.4.1.1
Catalytic Activity: [(1->4)-alpha-D-glucosyl](n) + phosphate ... |
I4YIE2 | MPICVNCRQYLENVATIYSFTDSRIELCPACSNLSDVYIGSRNLSLLSDLVLLKPQVLRHLLYNRRAEPAQSERFRSLNPGYRHNNVNTTTHLVKLGGILVIADAFVSWVHFRADGMSFMKLLIAATLDALSYHIAVIFAVRILTVRSVSNLQISLAIFYSSFAKLFLLLLLIIADPVPQSSSTVSNVPDNFLTGMHLTDDNRKAVWNVYTSLDDDRIDRPWIVNTVVGGMSAGFGLRVLLNTPPITSTIIILSGWIARSVTLELLHMYF | Function: Mediator of sterol homeostasis involved in sterol uptake, trafficking and distribution into membranes.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 270
Sequence Mass (Da): 30202
Location Topology: Multi-pass membrane protein
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A0A4Q4VCV3 | MAQSTAIPPPPTSTVSRPWDRCLSNMIIKSSLGFGFGVIFSVLLFKRRAWPTFLGTGFGAGRAYEECNWSLKQASKDLKQRA | Function: Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane.
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 82... |
C1AB96 | MSFPFLRGPMPRTSLTRRVLFAAAHRYRRPDWSDQENADVFGACAHPNYHGHTYLCDVTVAGPVDEETGFVVDLGFLDRVLQREVRERFDHRNINLDVPEFAEGRLIPTGENLARFICERVQAALAHTTARVVRVHLAEDTTLSSTYEVDA | Pathway: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
EC: 4.1.2.50
Catalytic Activity: 7,8-dihydroneopterin 3'-triphosphate + H2O = 6-carboxy-5,6,7,8-tetrahydropterin + acetaldehyde + 2 H(+) + triphosphate
Sequence Length: 151
Sequence Mass (Da): 17154
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A0A151BE43 | MRGSALLNRGEIKKLVEEEGLIMGYIDLETQLQPAGFDLSLAEVHEYLDAGSVDFSNAERRLPRTRPLQPDGEGWYRLPRGCYLIVYNEAVRIPLDLVAIARSRSTILRCGASIGTAVWDPGYEGRSSSLLVVHNPRGIRLRRNARVTQLLFLRVRGVEEGYRGAYQRERLEG | Pathway: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 2/2.
Function: This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA... |
A0A061DVV0 | MSNLLLIALPSSAAYHGFPILSSPPLPCLCYVSAVRASLLLNAIFAGVFTGASYAGPYLVPNFITYISGTGRHDEPRYYGLLLAFLFFFAKTLESLCERQWRFGANRIGIRVRAALMATIYKKSLSVRNAGAKNGQIINYINADIEKVGELVARCHEFWLLPLQVVLALIIMKKHVGWLPSIAAITATILVMVMNTPVSKLQRRWHSGIMEAKDCRMKATSEAIKSMKVSKFHGWESTFLQKLFQLRERERGWLKSYLYAQALVVCLYWSSPSVILLTTFGICTLLRRPLTSGSVLSTLATLRILQEPIYNMPELASLIA... | Catalytic Activity: ATP + H2O + xenobioticSide 1 = ADP + phosphate + xenobioticSide 2.
EC: 7.6.2.2
Subcellular Location: Membrane
Sequence Length: 957
Sequence Mass (Da): 107001
Location Topology: Multi-pass membrane protein
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A0A840W913 | MTVLESAILGVIQGLFMFIPVSSSSHLALAQHWLIQNGSALPPPESPEMVFFNIVVHVGTVVSILIVYRRALTDLVARSVADLRGLVGAGPRTEGLYLKLMMMGLFAVAVTGVLGLTIRKPLENVFANPALIALMLCVTGALLLWTDLLSPRTKGLRDFTWMMALFIGLAQAMAFAPGLSRSGTTIAIALLLGLRRRWAAEFSFFIAIPTIIAGNVLLPILEPEILSAFDPLPLLTGFVVAAIVGTFSLLLVLKLLYKARLRYFSYYVWALAALILADAYGLVDIGLTGAVMGHP | 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: 295
Sequence... |
A0A8B6EUQ2 | MIVYIFLVFQLSAASDWTYEGLHGLGHWDKEYPDCGRQHQSPIDIPSNPTLDPSIFMNFNGFEKTKEFSLTLRNNGHTAVVKVDSPNHSVFVTGNHLRGFIFKTMQFHFHWGKDSTSGSEHLVKGQSFPLEMHIVNYNYLAYKSIQEAMKHSDGLAVIAILFETTAEDNEDLKPLIEGLEKVKSKNSESSIDSLSLSKLLPNNTRCFYRYDGSLTTPGCFESVTWTILSQPQTISERQLNKFRALCDDNGNHLIKFNNRPTQGLHGRKVLRRDLVQALRKKGPYLAVNIEQVILHQDNTPAHTIKTSLEIDLLGFECLKH... | Function: Reversible hydration of carbon dioxide.
EC: 4.2.1.1
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Length: 343
Sequence Mass (Da): 38795
|
A0A352A4J7 | MKIMKKVLLLAMTGLMVLQLAACSNKSGKEFEITMDEFNTVLEQYKAKYKAQVGEETWNDKLKDDKAFIENLEELVLEQVILEKVIMDEAITAKVEVTDEEVNKELDTVKSSYTKTEDYEEYLSKNNFTEETFKEDIKKQLILTKFLKSKADEIMKIEPNEKELKKLYDQYASAFKKVQASHILVDTEEKAKEIKAKLDKGEDFATLAKEFSSCPSKEKGGDLGYFASNEMIAEFSNAAFAMSVGEISNPVKSSFGYHVIKVTDIRDTYEKTDKEDIKYQYRALKYDEMINNFIKDANVKMPKELEKIRERGNKKNI | Function: Plays a major role in protein secretion by helping the post-translocational extracellular folding of several secreted proteins.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
EC: 5.2.1.8
Subcellular Location: Cell membrane
Sequence Length: 317
Sequence Mass (Da... |
A0A3N0ZCM2 | MILPNFEEEKKFWSKGILVAGVDEAGRGALAGPVFAAAVVFPVDFEPDFNVYDSKAISSKKREFLYEKIVSSCLAYSVEFVDVEYINSTNILRATFLAMNNALSKLSHLEPFALIDGNRFEGNFKHRTIVDGDAKSFSIASASILAKVERDRWMTNIAHQKYPNFGFDKHKGYGTKYHIEQILKNKPTPLHRNFFLRKILKEDYILFK | Cofactor: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
EC: 3.1.26.4
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Subce... |
A0A3D0IES2 | MIRRIALTGMMTALAEVLMLLEIALPLMPGFLKYDFSDIPALFAGFACGPVSGVIVELLKNLIHMPFTNTQYIGEVANFLSGSIFVLTTTIIYLRMKNKKGVILSLAFGTVALVIATSFVNYFFTIPLYEKVMGFPLAVIIDMCDAANTLAKIDSKLDVILMTFVPFNIFKGITISLVAFLCYMPLRGFFEEKKDQAEDPKPEDSEEE | Function: Probably a riboflavin-binding protein that interacts with the energy-coupling factor (ECF) ABC-transporter complex.
Subcellular Location: Cell membrane
Sequence Length: 208
Sequence Mass (Da): 23091
Location Topology: Multi-pass membrane protein
|
A0A832Z108 | MSIKLRCKVVDVTRSYIPNIYILDLDCDRAYIKMDMHRLVMIVDKGDSTEINICKSLPVYEEGKDFLARGYVITKRELADGKHKYKVLISLWGFLIVLETNDPSIYSELNYMDEIYFHMKRI | Function: DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
EC: 2.7.7.6
Subcellular Location: Cytoplasm
Sequence Length: 122
Sequence Mass (Da):... |
A0A7S2USS1 | KHVMVMQVIYTFFTMMLGGYRLYQIVELKVAIYQIWDVWAYTEMSFLHKILAALYYVFTLRSAFQLTDPDLYSQDVWIDKYFQGISSTNVPQKPGVMGSPRASPRPPSPRAGGGPTADRARAGSSKPGAGRMLDSRPVGSAVSVT | Function: Required for ciliogenesis.
Subcellular Location: Membrane
Sequence Length: 145
Sequence Mass (Da): 16130
Location Topology: Multi-pass membrane protein
|
A0A386MJ58 | FLFGAWSGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSTIAHGGASVDLAIFSLHLAGISSILGAVNFITTIINMRSVGISFDRMPLFVWSVMITAILLLLSLPVLAGAITMLLTD | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
A0A7S2XW02 | WAGDKLRMNPNFFADSSTWQRPKYLYLGCADSQVCPEDIMGQDVGDIFVHRNLGNMVVNGDMNLLAVLQYAVEHLQVVDIIVCGHYGCDGIKAASSVEKDMGAMEHWLRNARDVQRKHHSTLQAIQDPEERHKTLVELNVREQCFNLLCHPIVQNSQAQNGCPKVHGFVYDSSTGFLRDLEIPMEKDVAKYHDIYAVHSLREISDNYLSATMI | Function: Reversible hydration of carbon dioxide.
EC: 4.2.1.1
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Length: 213
Sequence Mass (Da): 24176
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A0A1V5VP85 | MIARAHNRREADGDATAHAELLVIRAASAVLGQWRLEDVTLYCTLEPCAMCAGAMILARLPRLVYAAPDPKAGASGSVLDLLNHPQLNHRVEVAGGVLAGEAAALIREFFAGLRAQGQK | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the deamination of adenosine to inosine at the wobble position 34 of tRNA(Arg2).
EC: 3.5.4.33
Catalytic Activity: adenosine(34) in tRNA + H(+) + H2O = inosine(34) in tRNA + NH4(+)
Sequence Length: 119
Sequence Mass (Da): 12612
|
A0A7S2XWF5 | TVDREEALEFMVFLPAPHHTPLAVARTQDPADTHRFEAFEIPGFGGVAILNLPPPSTAHDPEEVVLTSEDMRRPMGAFVAQLRRILGLAPRPRVSSEGEQIPPGASTKPAGTAAKTGRRVLGPPVFLPSPSDGITDWELDLL | Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 142
Sequence Mass (Da): 15291
Location Topology: Multi-pass membrane protein
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A0A239QFC2 | MKRIAVIGDYNLNEESHRLIIESIKDAAAEIQGELEAQWIMSDTLDVSVAYLKHFDGFWFSPGSPYKDVNNVLSAIQYARENKVPALGTCAGFQHMVIEFARNVLGLHHADSEENDPECTDTVIEKLSCTLVRKKEQLEIPDSSSILARTIDGQRFIGEYRCNYGFNEAYRNAFQSSKMISSVVETENGYLRGFELKEHPFFVGTLFIPQLDFRGNGPYRIINSFVKAVLGRSAFV | Pathway: Pyrimidine metabolism; CTP biosynthesis via de novo pathway; CTP from UDP: step 2/2.
EC: 6.3.4.2
Catalytic Activity: ATP + H2O + L-glutamine + UTP = ADP + CTP + 2 H(+) + L-glutamate + phosphate
Sequence Length: 236
Sequence Mass (Da): 26673
|
A0A8D8F0R0 | LESPAHTTHVLEKDGDFFNLTMTYRLDSDVPWSYGQLAEIDGAVVGPSERALWLKSGFRNYANQTLLGLVRNKTKMAAQYVSHCGAISRRDKLVKEIQKSVQVDVYGNCGPMRCPLGSPRCARMLTDDYRFYFSFENSLCRDYVTEKLFNAMDNYVIPVVFGGADYTKFVPPHSVINVQDFKTVKELVNRLKFLADNPE | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 199
Sequence Mass (Da): 22622
Location Topology: Single-pass type II membrane protein
|
A0A8J6IEF3 | MSDGTDRMSALDAFFFYTEEDGRNHMHVGGFALVDGTAPSADEVVKALAPKIARIPRYTQMVRPAPLHVNRPEWIPAPDFDMHDHVRAVTAPRPGHLGLRDAIEDLISFQLDRSKPLWELVVVDGLSADQFAVAWKIHHSMVDGVSGTELLTILFDATPDGAPLGDQMVPTPAPSVERSRVKAVAGSVTGLGRDVVRHARGINPGTVRRAARVGAAGLALTRRNLAPDLRSPLTGSGGTT | Pathway: Glycerolipid metabolism; triacylglycerol biosynthesis.
EC: 2.3.1.20
Catalytic Activity: a 1,2-diacyl-sn-glycerol + an acyl-CoA = a triacyl-sn-glycerol + CoA
Sequence Length: 240
Sequence Mass (Da): 25758
|
A0A1W1ZKW1 | MRLGTTEIILIVVLALVLFGGGKLAGVGKALGKSIKDFKHEVKEDDDKSEEDGEEEKPAQKTTKAKK | 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: 67
Sequenc... |
A0A353EYL9 | MTEALGAVRVSGAFLRRCKMLEAMRISLTDPDVFAVTVFLAGLIGVCVGSFLNVVIYRLPRGMSLAMPPSHCPSCNRRLRWFENIPILSYLFLRGRCRTCRARISPRYTVVEAANGALWVAAVFVWRSNILMAVVAALAVSLCLCVCFIDWEQGFIPDRFQVLLALLAIPATLLDGYDGWVSHVIGGAAGGAVLALVGFLVSKKLGREALGWGDVKFVAVSGAFLDWKRLLLMLLLASVGGCLWSLLRRKREKQKTVAFGPFLTLGFTVALFAGEKIIRAYLSLFAG | Function: Plays an essential role in type IV pili and type II pseudopili formation by proteolytically removing the leader sequence from substrate proteins and subsequently monomethylating the alpha-amino group of the newly exposed N-terminal phenylalanine.
Catalytic Activity: Typically cleaves a -Gly-|-Phe- bond to rel... |
A0A972J620 | EEAVQRLLKDFYIVRISWVFGVNGKNFIKTMLRLSEEREEISVVSDQIGSPTYTKDLAETLVALMESGRFGIYHATNEGICSWAEFAAETMRLAGKSTRIKEISTSEYKTAAKRPLNSRLSKSSLDKAGIPRLPHWKDALGRYLKELSKTA | Pathway: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
Function: Catalyzes the reduction of dTDP-6-deoxy-L-lyxo-4-hexulose to yield dTDP-L-rhamnose.
EC: 1.1.1.133
Catalytic Activity: dTDP-beta-L-rhamnose + NADP(+) = dTDP-4-dehydro-beta-L-rhamnose + H(+) + NADPH
Sequence Length: 151
Sequence Mass (Da): 17046
|
A0A0K6HBD7 | MAEFKRINVTTAHQMWQQGNTRFVDIRDERSFAAAHIPGSQRLTDANLQDFLNALDDDHPVVVVCYHGNSSQGAAQYLVNQGVEDTSSLDGGMTAWAQQFPEAVERG | Function: Catalyzes, although with low efficiency, the sulfur transfer reaction from thiosulfate to cyanide.
Catalytic Activity: hydrogen cyanide + thiosulfate = 2 H(+) + sulfite + thiocyanate
EC: 2.8.1.1
Subcellular Location: Cytoplasm
Sequence Length: 107
Sequence Mass (Da): 11851
|
A0A3D8QCA6 | MQTSTLFTCILTLGFSLANPLPQASSAATACKAYTLLFARGTGDPDLSTSAANMGSVVGPGLQTAVQNALGANAVNVQGVNYPADASGITAELSGSGPGSVAMTQLATTALASCPQTRIILGGYSQGGEVVHNTVTQLKTQESNIVAVVTFGDPFKGSKLTGVDSTKWRSFCGSGDSVCGTGTCAASSCASASTSGHLGYGSDVTTAATFIASVVGTSGNTSGAAGGGASSPTVTTVTGSSATLAAATSSAALPWFGW | Function: Catalyzes the hydrolysis of complex carboxylic polyesters found in the cell wall of plants. Degrades cutin, a macromolecule that forms the structure of the plant cuticle.
Catalytic Activity: cutin + H2O = cutin monomers.
EC: 3.1.1.74
Subcellular Location: Secreted
Sequence Length: 258
Sequence Mass (Da): 2515... |
A0A3B9I1Y2 | MYDFHVHSIYSADCKFSIERMATEAIKRKIKLIYIADHFELSEITGHDMTFDLNEYKKEIQRVNKKLPEIEVLSALELGCDKSQFARFNELINEDPLDMIIMSTHKVGDVYLSNEKFYSEKHTLSIYEEYYSEILENIKSFDNFDVLGHLDLIDKFKDRY | 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: 160
Sequence Mass (Da): 19011
|
A0A061FGI7 | MAATSSHMACTKFSMLGWGRGKRDLRKTRFVSVSAQQQAQVGEEAQEAQVQEEQEKVKQQSTQPRPVEPQLNVKSKNMSKEYGGQWLSSVTRHVRIYAAYIDPQTSEFDQTQMDKLSLILDPTDEFVWTPETCNKVYSYFQELVDHYEICLMFLL | Function: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to prot... |
A0A7S3XE14 | ETAVDQAPETLVREEEIGTGDGMRERFEEMIRKAQNDICAAVEEVDGGKFHEDSWTRPGGGGGISRVLQGGNVWEKAGVNVSVVYGSMPPDAYRAATGGSGNKVTE | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; protoporphyrinogen-IX from coproporphyrinogen-III (O2 route): step 1/1.
EC: 1.3.3.3
Catalytic Activity: coproporphyrinogen III + 2 H(+) + O2 = 2 CO2 + 2 H2O + protoporphyrinogen IX
Sequence Length: 106
Sequence Mass (Da): 11270
|
A0A350J5K9 | MSWFSAFWSSFIEHLLEEIKIGDIGEEINHGILQWKHYFDIGGVKFLLTDAIIVSWIAIIITMIIFLLLIRKPSVIPNGRQNVVEALVGLVLSTCEGFGMNKKEAEHVAPMIMTIAMIIAGCNVISAFKISPPAKNIAFPVGMAAFTIVYVLYVSIRFVGLKGFWAYMTEPIPWLVPFKVLDLIIKPVSLALRLFGNVFGAYVFMEFLYIVIPVLLPGLLGLWFDIADGLLQAVVFSYLTMSYIGEIVEVGHERLEHPENFVKKKKEKKVKVQAENA | Function: Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.
Subcellular Location: Cell membrane
Sequence Length: 277
Sequence Mass (Da): 31123
Location Topology: Multi-pass membrane protein
|
C1A8P9 | MLSRTPPRAYIDTDHGTITLELFGREAPLVVEAFIRLAQNGTYRNTTFHRVVPNFVVQDGDASGDGSGESGFTLRESWTRQRHERGCLGLATSGPDTGGSQYYMCHSTQPHLDGGYTVFGRVIDGFAAMDRVVQGDRMLRIRVP | 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: 144
Sequence Mass (Da): 15921
|
A0A0T5ZZA4 | MTGELLRTVDIVISWLAVLLGVGFSVIPRAPLRCRQIAVLLSIGLALRYILWRAVFTLNQATVLEAVLSYTLLLAEVYGLSYLLVFYMQSWSRPDRAESPPVPERTPSVDVFITVCSEPIEILFRTAFCCTRLDYPSKRVYILDDDGRQEVRELAARLGCTYLHRPNRLGAKAGNLNYGLAHSSGDLVACFDVDHVPVNSFLRETVGYFRDPKVALVQTPHTFINPDPFQRNLLLSRHIVNEQDLFFHIAMPGRDRWNAAFFCGSAAVLRRSALVEVGGFRTETVTEDLHTSVHLHSRGYRSVYVDRPLSRGLAPESFAG... | Catalytic Activity: [(1->4)-beta-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->4)-beta-D-glucosyl](n+1) + H(+) + UDP
EC: 2.4.1.12
Subcellular Location: Cell inner membrane
Sequence Length: 767
Sequence Mass (Da): 86386
Location Topology: Multi-pass membrane protein
|
A0A0K0E4G5 | MFLKKLIIYNFYKNIKKIFELLNLYTIYILFLLIILIILLFFYFLQLNIIIYFIKSSQIDLDNIFDGNFNIKANTDRVLEQLNFTPNKNFEGTILFYDHTTSSNNNSGSFYQSNCPYKNCFITNSIEYLNKSNYIIFAPNEMDDVTLTKLHNKRFNNQIWVLKLFENPENTENLNKYNNLINYTSSYRWDSDIVVPYGKFVTNDNENSINKNYKNTKNFIKKNELTILLDQKEKRIAMFVSNCFTKNFRLNYTYQIDKYYPVDIYGKCGDKTINRSDGYKLLKNKYKYYLAFENGNCQEYVTEKFFINALQNYVIPIVLG... | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 416
Sequence Mass (Da): 49994
Location Topology: Single-pass type II membrane protein
|
A0A3D5R9U9 | MKKCLLFIILFMTIISNRNIYATPTLDCTSDILIDADSGRILHGHKENMKIYPASLTKLLTALTVLDLGELDDTLIVDENTPYEVDGSHIALEPGEELSLEDMLHGLLIASGNDVAEVISKNYSSYEGQFIELMNKKAKDLGALNSNFVNPHGLHDDDHFTTAYDLSRIAKAAYDNEIIRDIISKTKYTIGVTNKKSEERHLISTNKLLVGMGYGNQIIINNLWVNMKYEGANGMKTGYTPEAGSCLIGSAERDGISLITVVIDGSTTEVYTDTHELLNYGFENFEKINLINSNEFIKNIEIESGDSKYLTILSSDSLNA... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors.
EC: 3.4.16.4
Catalytic Activity: Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanin... |
A0A455TZ32 | MPVAIVNGRLSPRAFKRYQRLWSLMASTLADISWLAAKSTADAERFKALGSRAEMTSTVGSLKFEIASQNSNLKEGERLHQEWGERPVWVAGSTRDGEEALLLKAHRQVLARYPNALLVLVPRHPQRFDEVAKLCNIEGWTLSRRSQQQSVTAQTQVYLGDTLGELAALYAAGSVAFVGGSLVSLGGTMCLNRLR | 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... |
A0A455U2R1 | MSHKTDQEPNGLKDDAHAASAIPESIADGVDDDVVESNRRLFTGWQFLLFAALAIVYSSFHLISLNVYPMETWSFRIVHIAGALVLGYGLFSGARFADDGHQASGAWIKWASYALLIPAAYTLAQVFVMYQTLSGGAMRIDPNIENWHYGYPLMATTAGAIVLSWFYRQARHRFNPADLVLMVCALASAGYLLVAYNTNIRMSTGTSFAPSGISWAAIAGSLLILELTRRVAGLALVVISAVFLTYVFAGPYLPGFLGYPGLSLQRFFSQVYTDAGILGPTTAVSSTYIILFIIFAAFLQASKVGDYFVNFAFAAAGRAR... | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 332
Sequence Mass (Da): 35871
Location Topology: Multi-pass membrane protein
|
A0A367KRP0 | MSSLLAILLVVNSTRGHHYLYSYPPDPRRFSTARKTNNNEKSTSFTVGSAFSVSKQAEVLIKDSRRSSSASKSNNSTKNDDISTHETNTSDKDIFAGRDRIFNIDVSFLADALAPKLPLCDRKFQLSMDDLTFVGHPVSLTSPQHPNETEDLNDSTELNASVPATPPSHTYSPLPTVPHTPASGYNTKRSSPNDAADDGLDLRGNDESDGQQKDTSDSSDDSSDDNLQHDDSDTSISETFPGSTSIHMTLFHVVFVLSPPDLELNAQVDTLYKNVILRYSSALRYEQLRCGYVQEEIEKVLGLKEEAFNKGIPYDETMRE... | Function: Mediates inactivation of the TORC1 complex in response to amino acid starvation. Required for meiotic nuclear division.
Subcellular Location: Vacuole membrane
Sequence Length: 682
Sequence Mass (Da): 77037
Location Topology: Peripheral membrane protein
|
D5J6P5 | MVGTSLSLLIRAELGNPGSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPPSLTLLISSSIVENGAGTGWTVYPPLSSNIAHGGSSVDLAIFSLHLAGISSILGAINFITTIINMRLNNLSFDQMPLFVWAVGITAFLLLLSLPVLAGACT | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
A0A367IZ34 | LGVFTRITFPLYAFPIGVAFLVQTFKKNQGRLQSLFCLLLGTVLCAGACILIDSVYYGKLVFTVHDMPFRDIFHVVSSVSDLTALSNIRAYGEIVITPLNNILYNLNVDNLAQHGLHARYTHLLINLPLLFGPLTFFGLFCMPKVFSKLKTMNNDLVYGLIGLSIMPHQEARFLCPLLVPFVLIYAWDQSTFPLLFWMAWILFNTVTTFVFSFVHQGGMVPALGFIQRHTTGIHDCHVLHSGDLSCFVDLNQATDLNGFDLTTHLVFYKTYMPPRHLLALPLENKAHHVHIIDFGSDHHGLVSELTQRPGIPLRRHSKDK... | EC: 2.4.1.-
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 400
Sequence Mass (Da): 45396
Location Topology: Multi-pass membrane protein
|
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