ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
|---|---|---|
A0A4R4YIT9 | MSELLNNLDRNVYERLMWQRILVLGDEVKDANANALCAQLLLLNAEDPRADISLYINSPGGSVSAGLAIFDTMNFISNDVATYGMGLCASMGQVLLACGTPGKRFALPHARIMMHQPSGGMGGTASDIKVQAEQAILARQDLAQLIAERTGQPLERIVADFDRDRWFTAEAAREYGIVDEVLTRPVAVPV | Function: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.
Catalytic Activity: Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. alpha-casein is the usual test subst... |
A0A1X7IAR0 | MIWGLASEAKINLTLRIVGTREDGYHRLVSVFKKLPPIERLSLEILPEGMEGMEDRVAMSEVKISDVNLVQKVIDFLRERGVSIPPLSVSISKVVPPGTGLGAGTGNGAAVLKWATAFFDLPSVWDISPLGADLPFMASDDRIAMVSGIGETFAPMEDISLRSVLIVPKWRCNTAESYRLLDDLYAPDSWPLSEEDGELEALDVLGRLRAGLKVGLLPNDFIAPLTDMHREYEALFDACDRSGAVAWGISGSGSSVFALYDFNLPSSELFRSFDGIGCVEKIIFLE | Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 3/6.
Function: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
EC: 2.7.1.148
Catalytic Activity: 4-CDP-2-C... |
A0A1V4RFC0 | MSDIAVFNGPNLASLGIREPAIYGNTSSVELESKLKQWCVQAGFGVVFGQYDSEGQLVAAVNKASLNCEALIINPGGLSHTSVAVLDAMRAFKGPVVEIHISQIHTREPYRHRMLTAGGAGVVVSGAGIYGYFSAIDIVRELLRR | 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: 145
Sequenc... |
A0A847X643 | GLPLAFGGPYLGIFACTKDFLRKMPGRIVGQTEDLDGKRSWVLTLSAREQHIRRDKATSNICSNQGVNTLATAVYMATMGKQGMKEVALQSTAKAHYMYDELLKLDGVEAFTDRPFFDEFTIKTSVDAQTINDRLYENGIMGGINIEKFNNELGHGMIIAVTEKRKKSEIDKFVEVVKEAF | 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... |
A0A2N7D1C9 | MRLKPILLSFIALFVLLSVIGGQWYWQHNFTSLQAQHESWLNRFVENIDSKLDKYRHIPQLLSQDRELVDALLSPDNSAQLEVTNRYLSQANRIVQASDTYLIDKFGNTIASSNWHLPHSFVGKNFAFRPYFQQAIQGRQSSYFALGSTSGRRGYYYSYPVTYAAEHIGVVVVKMDLSTIERNWQSDTSIYVATDNHHVVFMSSDADWLFHSLSSIDDDVLEDIKQSRQYLTTSIQDLGFKGKLSGDSSVITKPSRNVFTQDFLMTQRDSGVPNLTLRVLTPLSTLYIDIVGFIFILFLLFVTAYLIVVLIAMRQSKHRQ... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 624
Sequence Mass (Da): 70398
Location Topology: Multi-pass membrane protein
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A0A6G1CPP8 | MALDIGKQQRRHGKEERRRGLGSSASAAAAAEPRSVQLLLLGVALVAGSFYAGTVFRSPSSPALILPPSGSRSPDSSRTQGAPKFTNRVSLSYQTKPISVPDYGIAVCPLEYNEYIPCHDASYISQLKNLDRSRHEELESICPPQEKRLFCLVPPPNDYKIPIRWPTSRDYVWRSNVNHSRLAEVKGGQNWVHEKGKLWWFPGGGTHFKHGASEYIERWNIAERGRTSFAA | EC: 2.1.1.-
Subcellular Location: Membrane
Sequence Length: 231
Sequence Mass (Da): 25801
Location Topology: Single-pass type II membrane protein
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A0A2U1PEL7 | MVKVTSNKGCVAAMKQAGARVIVIEIDPICALQATMEGLQVLTLEDIVSESDIFVTNTGKQRHHHGIRHGQDEEQRYPLQHWSLQQ | Pathway: Amino-acid biosynthesis; L-homocysteine biosynthesis; L-homocysteine from S-adenosyl-L-homocysteine: step 1/1.
Function: Adenosylhomocysteine is a competitive inhibitor of S-adenosyl-L-methionine-dependent methyl transferase reactions; therefore adenosylhomocysteinase may play a key role in the control of meth... |
A0A1F7JWD1 | MQIHFQNTCGLDSRELAKVALSLTDYLAHLQSITKHYEYDGKETAMNLPFDKGIADETCEIAKKFSSNNLKFIFVVGIGGSNLGTSAVYEALTGKYDLTTNTYPKMIFLDTVTLLPHMHVESIVEEDAEDASDIVVNVISKSGKTTETIANFDVLYKMLTKKFPHVHERVIVTTLKDSPLWKAAEKNGFMCLDHRDVTGRFSVMSAVGQLPLRLAGFDVDSLLKGATDATQPGLSTDIHSNPALACAVSMYLNAMHGKNLHNVFFFNPELELLGKWYRQLIAESLGKNTEAGITPLVSIGSTDLHSMVQLYFAGPRQTFT... | Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 2/4.
EC: 5.3.1.9
Catalytic Activity: alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate
Sequence Length: 426
Sequence Mass (Da): 47394
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X6F1L7 | MPWMAPKPSRMRLTPELVARVLSADDSLPQPFTAPSDADHDDTVRAILAAAPSADEVWLFAYGSLMWNPACDFVEQRVGFVPGWHRSFCLGWDRWFRGSDSKPGLMLSLDRGGQCKGAPPDAIEANLGRLFRREMRAKPSAHSPRWVNVRSENGPLQAITFVINRNSGRCVRGLSLEQIADALAVACGPWGSMAXCPRAVAGTDRRRARGRVRSVGFHGRLSPQHCKPP | Function: Catalyzes the cleavage of glutathione into 5-oxo-L-proline and a Cys-Gly dipeptide. Acts specifically on glutathione, but not on other gamma-glutamyl peptides.
EC: 4.3.2.7
Catalytic Activity: glutathione = 5-oxo-L-proline + L-cysteinylglycine
Sequence Length: 229
Sequence Mass (Da): 25237
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A0A2U1MIK0 | MERVMFSNSSKGSSIIKEPFGKLENIARSITDVKRIGREFKDTDKAVKTGNTDDILQKLGSKDLLKLGQRLFQGNRISLSSSAAITPQSSAKFLIPAKTKGTDANGKSSSSSHGDVLGLGGYASDDDEDKEVQNLSISSCASSRSTDLDDANGKSSSSSPGDILGLGCYASDDDEDKEVDDGKVPDTKSIKDESDSHGVVPNGGTDDYNDNFEKSKLDNYDALKSKQSVRDTNVGKHELPVKGGLKYLRVGGIKLWIVIIRDGLRQASLKIRTARHDGIKVEEVLDPDFGESAIGRVAPETVDVQTGIKLILNLCFSNGL... | Function: Invertase that cleaves sucrose into glucose and fructose.
EC: 3.2.1.26
Catalytic Activity: Hydrolysis of terminal non-reducing beta-D-fructofuranoside residues in beta-D-fructofuranosides.
Sequence Length: 373
Sequence Mass (Da): 40223
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A0A2Z5RD82 | MTNLMLISESLTSGFSPLGLDILSFGAILSGILVITARNPVISVLFLIALFVNIAGYLILLGISFIGLAYITVYVGAIAILFLFVIFLLDIKLAELHQDNNKNRSEAPLGAIIGVAFLYPLYSIIPSNITEMKSFSYYVFNWLNSLITGTTPSLKFLSITSSEPSFTGLDNSNLESVAKLEVESVFTNLWDGNFAAFSQISSIGNVMYTGYLLWFFVASLILLLAMVAAISLTFKPAAVSNSH | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity and assembly of complex I.
Catalytic Activity: a ubiquinone + 5 ... |
A0A2U1KAV9 | MKPFLEKLFPDVYTRMMIDTKISNYCKFNSQLLTAFTSSLYVAGLISTIFASPVTRAFGRRPSILIIGGVTFLAGAALGGAAYNIYMLIIGRLLLGVGVGFANQQMCPVKKVAGVALLPKWVLYPPGSGPRRIGYMLLI | Catalytic Activity: NH4(+)(in) = NH4(+)(out)
Subcellular Location: Membrane
Sequence Length: 139
Sequence Mass (Da): 15081
Location Topology: Multi-pass membrane protein
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A0A2U1MD61 | MTWAARQSAMPMGILDLSLTLSRYRNGSDHNPLVSLAFKELNHDGVGSIKASIVKTQKRTMETGSTNPTDQVLLANHILEASLMGFCLFLGLMIDRLHYYVKELWLLRKSLKAIRSQIGDSDVIQPVNKNKKA | Function: May play a role in anterograde transport of membrane proteins from the endoplasmic reticulum to the Golgi.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 133
Sequence Mass (Da): 14883
Location Topology: Multi-pass membrane protein
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A0A8S1ZUR2 | MVDQVQHPTIAQKAAGQFMRSSVSKDVQVGYQRPSMYQRHATYGNYSNAAFQFPPTSSRMLATTASPVFVQTPGEKGFTNFALDFLMGGVSAAVSKTAAAPIERVKLLIQNQDEMIKAGRLSEPYKGIGDCFGRTIKDEGFGSLWRGNTANVIRYFPTQALNFAFKDYFKRLFNFKKDRDGYWKWFAGNLASGGAAGASSLLFVYSLDYARTRLANDAKAAKKGGGGRQFDGLVDVYRKTLKTDGIAGLYRGFNISCVGIIVYRGLYFGLYDSVKPVLLTGDLQDSFFASFALGWVITNGAGLASYPIDTVRRRMMMTSG... | Pathway: Protein modification; protein ubiquitination.
Catalytic Activity: ADP(in) + ATP(out) = ADP(out) + ATP(in)
Subcellular Location: Membrane
Sequence Length: 1003
Sequence Mass (Da): 111510
Location Topology: Multi-pass membrane protein
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A0A2U1LU36 | MFLRRFARPSSLKMMSAAAAIVGQKVGPEVVPNSREVLIGLYTKTLNIITRVPEDEGYRKSMESLTRQRLAVCESEKDVENIEKQIGKVDELIEEAKFEYKVLDKLLEWDPWGVNDDYISEEMQNGIEIPKPAPVHSRPLPEDFFATLKAAANVKSVKDEDKDEDTDEDESTIPASS | 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.
... |
A0A101G9R0 | MRRRRCELSLQPASAAVLVGGKSKRMGKNKALINIGRDSLVEITINKLRPFFQEIILITNKVESYAHLKFSMASDIYKNCGPLGGIHAALKAASYEFVFVVACDMPFIEPKFVEHILKSGDQDSDIVIPRVNDYYEPLHALYSKKCLPAIEACLNRGELKAASILPYVRVKFIEQGEISRFADPLEVFFNVNTPVDLSKAKKILGV | Function: Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor.
Catalytic Activity: GTP + H(+) + Mo-molybdopterin = diphosphate + Mo-molybdopterin guanine dinucleotide
EC: 2.7.7.77
Subcellular Location: Cytopl... |
A0A2U1KJZ0 | MLSESFVPVANNLCSNPLAHAANVIKALSGPKYEGGYLHNIIQEKLQENRLHDTLTNVVIPTFDIKYLQPTIFSSYQLQTTPSLDAKLSDICIGTSAAPTYLPSHSFQTEDSEGKLLKEFNLIDGGVAANNPTLVAISEVTKEITRGSPNFFPIKPTEYGRFLVLSLGTGSPKFHEKYDATKSSNWGILGWLAGGGSTPLVDVFTQSSDDMVNYYISVVFQALHSEENYLRIQDDTLSGDLSTMDLATSENLENLVKVGENLLKKPVTRVNLGTGISEPYHHTTNEMALKKFAAILHKEKYVRELRSPNTNRGRVNQGKS... | Function: Lipolytic acyl hydrolase (LAH).
EC: 3.1.1.-
Subcellular Location: Vacuole
Sequence Length: 351
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 cleava... |
A0A6L5GP69 | MNPNNPLTFYDLHSHFLPGMDDGCKTPEESLALLTEHYRQGCRGVVSTSHYYAQESIDHFLKRREQAAARLLKAMNGRMQALRRKGQKVTADALQLPALTFGAEVAYRDTLVNDSDLEKLCFGKSRYLLLEMPFEPWSERTLRGVEEIENLWGIKVIVAHIERYRGYADDDYIEALMDMDVTVQLNAGNFGRRKTARNAIKLIKNGRIDVFATDSHNVENRPPNMIWAIEALQKKGMDDTLDAIFANNARIFAAAKGR | Pathway: Capsule biogenesis; capsule polysaccharide biosynthesis.
Function: Dephosphorylates CpsD. Involved in the regulation of capsular polysaccharide biosynthesis.
EC: 3.1.3.48
Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Sequence Length: 258
Sequence Mass (Da): 29350
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A0A2U1KLQ3 | MEEEKEQGKSFKELGLVEELIEACDSLGWKNPTKIQLEAIPQALEGKDLIGVAQTGSGKTGAFALPILQAMLEAPRLPAFFACILSLTRELAIQISEQFEALGSSIGVKSAVLVGGVDQVQQSIALGKRPNIIVATPGRLLDHLSNTKGFSLGRIKYLALGADNQWQKSVAAATENNRYHKIQNKEYMGYEIGGLN | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 196
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Sequence Mass (Da): 21181
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A0A1G6MBF6 | MELSMPQWGQLFTLLMISVALGMDAFSLGIGVGMKGLGIPNILKISGTIGLFHFLMPLVGISMGQYLGQLVENIAVITGGGLLCALGVNMIWQAFRSGAGDDSFNIATTSGVMLFSLSVSLDSLSAGFSLGLFEADRILTVLLFGCVGGLMACFGMWLGRHVGGWVGDYGEVVGGMILITLGLRFLL | Function: Probably functions as a manganese efflux pump.
Subcellular Location: Cell membrane
Sequence Length: 187
Sequence Mass (Da): 19603
Location Topology: Multi-pass membrane protein
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A0A6N2JQK5 | MDILSLGWFGVLGMFTLSIAFVVWGRNGL | Function: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
Subcellular Location: Cellular thylakoid membrane
Sequence Length: 29
Sequence Mass (Da): 3201
Location Topology: Single-pas... |
A0A1G6JTW9 | MISPGIGLILLAGGQSRRMGQDKALLSFAGEPMVKRLLRRLDFDGNSIVLISANQPEPYQKWGIPVVADDLPGAGPLAGIQAGLRRSPCTFNLVVACDLPFASAAVARRLSQVAEDGDYDAVVPVCDGRAHPLFSIYHRRLQGELDAFLQEGKRRVGDFLDRVQTRYVTESFPSQAFFNMNRPEDYRRAEAWEEE | Function: Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor.
Catalytic Activity: GTP + H(+) + Mo-molybdopterin = diphosphate + Mo-molybdopterin guanine dinucleotide
EC: 2.7.7.77
Subcellular Location: Cytopl... |
A0A2U1PSV2 | MSVILLCLKSLFKVVRTSIAQVLTVILQTQKAKLREAYKKEYLPLDLRPEKTRAIRRRLTKHQAHNLQFTGQKIWLAAIDELIGKGMRYAKHALLSGSGGLASILHCDEFGHLFSRNTKVKCFADAGMFMDA | Function: Hydrolyzes acetyl esters in homogalacturonan regions of pectin. In type I primary cell wall, galacturonic acid residues of pectin can be acetylated at the O-2 and O-3 positions. Decreasing the degree of acetylation of pectin gels in vitro alters their physical properties.
EC: 3.1.1.-
Subcellular Location: Sec... |
A0A2U1QHV5 | MALANDYKLLEDNSYYVSLTRAQTSHPLDPLSAAEIKVAIATVRAAGATPEVRDGIRFVEVVLSEPEKNGVALADAYFPHLSSLLCCPEAKVEL | PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue.
Cofactor: Contains 1 topaquinone per subunit.
EC: 1.4.3.-
Sequence Length: 94
Sequence Mass (Da): 10146
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A0A844SZG5 | MRPVGVRPAVEGHDWRHFAEIDAEVRPLLKLVDHRHLNDVEGLENPTAAVIVDWFFDRILGC | Pathway: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
Function: Catalyzes the conversion of 7,8-dihydroneopterin triphosphate (H2NTP) to 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) and acetaldehyde.
EC: 4.1.2.50
Catalytic Activity: 7,8-dihydroneopterin 3'-triphosphate + H2O = 6-carboxy-5,6,7,8-tetrahydropterin... |
A0A1K1YPQ8 | MRLVVDENLPYVREFFGRHAELQLMPGTAITARDLEGADGLLVRSVTRVDAALLQNNTSLRFVGTATIGTDHVDQSCLAERGIHFASAPGCNADSVVDYVISSLLWLVAEQGLQLRDQCIGIVGVGQVGGRLARRLQAYGCQLLLNDPPRAVAGDTGLVDLDALLEAADIICLHTPLTRAGESSQPTFHLFDEGVLSRLAGKVLLNAGRGAVVDQQALLRLLQQGQAPALLLDVFEGEPLLDASLIDQCLLATPHIAGYSLEGKSRGTEMLYQAWCAFTGQTVCQSLPQLLPAVAIDQLHLDVACSPEEACRRVAHLCYQ... | Pathway: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 2/5.
Function: Catalyzes the oxidation of erythronate-4-phosphate to 3-hydroxy-2-oxo-4-phosphonooxybutanoate.
Catalytic Activity: 4-phospho-D-erythronate + NAD(+) = (R)-3-hydroxy-2-oxo-4-phos... |
A0A7S4K5P7 | LWKTRRLVKVQAEMEVKERQEAETATSVLPRKGKKKGILKKAKPMTQEAAEKRKLLEEYRKKIESQLLAKVERERKVLVMCRRLFENDSVSLEELEETGEWISIQDYEDATKERALKGLCGYPLCHRSLQDASKPVGKSQILFERRTVSSVKGRKYFCSEGCGMASSIFKGSLQAYRPMKDVSEEMMSGTGDDKHKIVEKQPSPPSFEFKPENFSSIEGHRARAAQESKHSPTSTSSSHPPPHPHPHPPHRSSTQAPVVEERTSGGNAIQSTDEKRIRFGVQHTEVEHVIKERRAAKDQEQEQEQEQEQEQEQ | Function: Putative RNA polymerase II subunit B1 C-terminal domain (CTD) phosphatase involved in RNA polymerase II transcription regulation.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
EC: 3.1.3.16
Subcellular Location: Nucleus
Sequence Length: 313
Sequence Mass (Da): 35773
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A0A142Y7J1 | MASVFIEEQNRTISDPAEISAFLKPFGIWYEHWQVAGRLKSDASDTDILTEYQPEIDAVKAKGGYVTADVINVHPQTPNLDAMLQKFNKEHTHSEDEVRFTVSGKGVFHLHPEGGPVFGVTVESGDMINVPRGMKHWFNLCDDHHIRCIRFFEDATGWAPHYVDNPIHEQFSPMCFGGSYLSSENADESKGGIPSKFEMRSAPSN | Cofactor: Binds 1 Fe(2+) cation per monomer.
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 5/6.
Function: Catalyzes 2 different reactions between oxygene and the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (D... |
A0A2U1PCW7 | MKVAAATAFGAEFKIAFRIRGRCLNLASRGRLTYPADLYAEAIRSGQTNADTVQSWAFRLVLRKPEAEWQFTTATTVMDSGTQLKGLILGIKEYSSPPVAVADVWIRARYNFLLFAYVTCKTMVAWILGKSFFMEFYRPIREKHLHQCIQGFPEGALRRIILTASGGTGRLKDLKMLQVADALKHPNWSMGRKITVDSATLFNKVIF | Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 1/6.
EC: 1.1.1.267
Catalytic Activity: 2-C-methyl-D-erythritol 4-phosphate + NADP(+) = 1-deoxy-D-xylulose 5-phosphate + H(+) + NADPH
Sequence Length: 207
Sequence Mas... |
A0A142XZW3 | MPNSRFEAVLAIARNGVIGDKQGLPWRLRSDLMRFRKITMGHALLMGRKTYESIGRPLPGRQTWILSRQGGLQVPGCHVVRDWNDAIASLPPQGRLFLVGGAEIYRLLLPECGVVHLTRVLADVPGDTRMSHLGLEQYTCAERMYVPADSQNDWPTEYERWVYSA | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1.
Function: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.
EC: 1.5.1.3
Catalytic Activity: (6S)-5,6,7,8-tet... |
A0A124BTE2 | MPATVPTARNIRSVGIGDRPARVGAKHNGATGQHHAGSDAGCTFTAHDGTYMDTQELVSEISELNLTYLMLAQQMLAKDRDAALFRLGISEELADILLTMSPAQIVKLASTNMMLCRFRFDDHAILGLVTQPHRDKGLQQSQMSILLARQAVEQIS | Function: Functions in complex with FlhC as a master transcriptional regulator that regulates transcription of several flagellar and non-flagellar operons by binding to their promoter region. Activates expression of class 2 flagellar genes, including fliA, which is a flagellum-specific sigma factor that turns on the cl... |
A0A8S1ZWM9 | MGSFVKEETSSLMTDFLEKCGGYAVVDGGFATELQRHGADINDPLWSAKCLITSPHLVTKFYKVSIESARFLRCASSGRVMREPSMLVREAAAEQLEETQSDWLSLCWWPTHLKSTHNDASDLDNGTDDLPSFTEFSFDQLRAATCGFSTDSIVSEHGVKAPNVVYKGRLEDDRWIAVKRFNRSAWPDTRQFLEEAKAVGQLRNERLANLIGFCCEGDERLLVAEFMPFETLSKHLFHWDSQPMKWSMRLRVALYLAQALEYCSSKGRALYHDLNAYRILFDQDGNPRLSCFGLMKNSRDGKSYSTNLAFTPPEYLRTGR... | Function: Serine/threonine kinase that acts as positive regulator of brassinosteroid (BR) signaling downstream of the receptor kinase BRI1.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
EC: 2.7.11.1
Subcellular Location: Cell membrane
Sequence Length: 672
Sequence Mass (Da): 751... |
A0A1K1VCS7 | MGLQQVLILLGVVIFAGVLLDALRRKRAATRRRMAEDFDDPEEAERKACIARELPGLNRDRRALDPLFDDIDVFDDDPIPVLRKRLPEATAVVADKDHQTEQHQPEPERTAAISSRAMVEEDLPEDEELAWEKMRRQFEVDPEFLAESRRSMVEQQQELQRLQQRRVATVGGSVDEVAETPVEPPILVAAAANDEALLTPDDDDLVDLPSAVPTRAAVSTAPVSNKPGKIDPVAEADDEDPALTAEELETYLREEEDEEQQLRAAVLTNLEKSTWGSSEEFLTINVQAPDDQPFHGRHLKKFMEMIGMRLSLSGFYHYVD... | Function: Essential cell division protein that stabilizes the FtsZ protofilaments by cross-linking them and that serves as a cytoplasmic membrane anchor for the Z ring. Also required for the recruitment to the septal ring of downstream cell division proteins.
Subcellular Location: Cell inner membrane
Sequence Length: 4... |
A0A1Y2ZUZ4 | MKILQLLENAPYSETQRAWLGGFFSGMRSQLKQNAGAANATVAQTIHILYGSQTGNAESVANDAATAAKAHGLKPVVTSMDAIDSDALAAMDTLLIVTSTYGEGEMPDNAQMLWEAVSAESMPQLPNMKFSVLALGDTGYDLFCKAGIDWDNRLAELGATRIYDRVDCDVAFEAPAESWISSVIPQLDGRDAINRVSTMVVDTETAVPKSQYSRKNPFPAKLLVNRLLTAADSSKETRHYEISIAGSELSYEAGDALSIVPTNCPDLVAAIINAIGCTGDEIEPVNGESMSLSDALRTQFEIKLPSKELVQEIATRSGNQ... | Cofactor: Binds 1 FAD per subunit.
Pathway: Sulfur metabolism; hydrogen sulfide biosynthesis; hydrogen sulfide from sulfite (NADPH route): step 1/1.
Function: Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the bios... |
A0A2U1MWE5 | MPPRSKITPVVVLWALLLFGTIVFVLNKVSDSGIASEQKSVNNKVNHKEEGSKGDLDEVTHKVYFDVEVAGKPIGRIVMGLYGKTVPKTAENFRALCTGEKGIGKNGKPLHYKGSTFHRIIPSFMIQGGDFTRGDGRGGESIYGEKFADENFKLKHTDPGVLSMANAGPDTNGSQFFITTVITNWLDGRHVVFGKVVSGMDIVYKIEAEGRQDGTPKSSVIVVDSGELPL | 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: 230
Sequence Mass (Da): 24941
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A0A2U1MIT6 | MSRTTTLLLILALLLCSTQSQSTRLMVADTANTKLQNKVYIFGGDETAEIEQGCEGIGEDECLMRRTLAAHIDYIYTQKKNP | PTM: PSK-alpha is produced by endopeptidase digestion. PSK-beta is produced from PSK-alpha by exopeptidase digestion.
Function: Promotes plant cell differentiation, organogenesis and somatic embryogenesis as well as cell proliferation.
Subcellular Location: Secreted
Sequence Length: 82
Sequence Mass (Da): 9141
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A0A2U1MNZ5 | MTVSVKWQKELYKGVEIDTTQPPYVFKCQLYDLTGVPPERQTILLKGATLKDDSDWSKLGVKEGQKLMMMGTADEIVKAPEKGPVFMEDLPEEEQAAAVGHSAGLFNLGNTCYMNSTMQCLHSVPELKSALIEYPQSGKSNDLDQSSHLLTVATRDLFNELDKNVKPVAPMQFWMVLRKKYPQFGQLHNGSFMQQDAEECWTQILYTLSQSLRSPSSSVNIDAVKQIFGIDLVSRVHCAESGEESSETESVYSLKCHISHEVNHLHEGLKHGLKSELEKASPTLGRSAVYLKDSRINGLPKYLTIQFVRFFWKRESNQKA... | Function: Recognizes and hydrolyzes the peptide bond at the C-terminal Gly of ubiquitin. Involved in the processing of poly-ubiquitin precursors as well as that of ubiquitinated proteins.
EC: 3.4.19.12
Catalytic Activity: Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the ... |
U2V5L0 | MADESVTAPNTHQAAHAAPSDGMPPKTSPAAIGNPKADIDALDNLERHRYAHRYASTGISCYGPSLDPADATADRGEALSILEEEDQALLCSKETGELLERLSKMGHILTETQEAQARIIQRDRARLVGVPADVQGGFARLTNEADAVWRKAKADDDWASFEPYLDRLVAQATTIARLRRPDSAPYDVWLDDFEHGTDRGFYDAFFAEVKQAVVPLLSAIRQKGWQPPRTVVEGKFDERRQMELAYDLMRLEGLDGNKMLLATTEHPYSDALTTNYGFIACHVREDDVCSNVFTMLHEGGHALYETGVESAYNYTSLKGG... | Cofactor: Binds 1 zinc ion per subunit.
Function: Broad specificity carboxypetidase that releases amino acids sequentially from the C-terminus, including neutral, aromatic, polar and basic residues.
EC: 3.4.17.19
Catalytic Activity: Release of a C-terminal amino acid with broad specificity, except for -Pro.
Sequence Le... |
A0A2U1PLF9 | MAPIRHATIHIRDCSIEVPRGLECLFQLLVTVDILFANIINYFTSSHPYGWRISLGGVAILTLFLAIESLAIVETPASLIERGHPEKGLATLRKIRGAEDLDHLLFQCQFATEVWGKVKGLAEMSGQGTNWHQIINDMVNSGNGNNIMSVVRRLLLAASVYNIWKERNGRIFRDVTRSSEDVFKGIVETVKTRLMSLTVRESMAVRRMESLWGITCKRVVS | Catalytic Activity: NH4(+)(in) = NH4(+)(out)
Subcellular Location: Membrane
Sequence Length: 221
Sequence Mass (Da): 24852
Location Topology: Multi-pass membrane protein
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A0A6G1F549 | MPPDMHINLLERQTQMLWVYEGKAMVRRNISYIPALYTMFDRILLFSARIGISQIDILRVSINVAKGRISIYSHGDGLPVEAIPEDINPRELFFHGILSDNINIKKTGADRSNSGDVFTFFSKLIIEISDSGQKYKQVFYENLGKKKNTKITMCHTKVCWTRVTFFPNLDMLNMTHLEDDIVALMRRRVIDMLGILKKEIKVELDGHVLPDYCFPDYVDLYLQSASRERSQNVPRVYQKLNRSWEVCVSLSKGQFEQLSFVNGIATIGGAHIDIVTRCIEKRLISAVKKKSRNAVILLSNVKNHLWVFINAVMPSAEFDS... | Function: Control of topological states of DNA by transient breakage and subsequent rejoining of DNA strands. Topoisomerase II makes double-strand breaks.
EC: 5.6.2.2
Catalytic Activity: ATP-dependent breakage, passage and rejoining of double-stranded DNA.
Sequence Length: 975
Sequence Mass (Da): 111611
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A0A060LYD6 | MLALRNKHILLTREEKDAKQFADLITAYGGTPYFLPLIKIVFRPVGVESTKKAARADWLVFTSVNGVRSFFSTYQGEPLKAKMAAVGVQTAHEIERYGYHTSVVPKIQDGEALARLLQTVVGQEERVLVVRGQLAKPTIIYGLKNKGINVEALTTYDTIMPKEAIREAKALPNLVFDYVTLTSPSTATHLRAVMEACTISYRKVACIGPRTNERAIQLGLTPTVTADSYSTNGLVKAMLIEEAHKHERNI | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 3/4.
Function: Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III.
EC: 4.2.1.75
Catalytic Activity: hydroxymethylbilane = H2O... |
A0A0L0D5M5 | MTTPGEMFHVAAPERVLRARQKDGQHVSELRGRLEELVRGMVGGRASEAAAGTVSLVASLVYYGLTKGLCQPSVGEEYGYVLATRSSAPLEGIVPAAGPLSAPGRVRAANGSIKWAPSDVPLVRMWLALLLKIVAPLLVARADVRAAVARLIGAWVDRHWPLIQRLAAAVIALHEAWFFAVGSYASIADRLLGIVHADVAPSTSHLARTRNQGYVGMAVLHAIPPAIDLVSALRTLATPPAGESTDDSEHVRGAQLLAPEIDCPICFEDMSHNVSATLCGHVACWDCLIQFTASDACCPTCRAPTKPSDVVRLYNY | Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Membrane
Sequence Length: 316
Sequence Mass (Da): 33668
Location Topology: Multi-pass membrane protein
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A0A328RGT8 | MGAPGSGKGTQTEYLKKEYNIDAFAAGDIIRSEVDKLSEVGVLAKNYILKGELVPDQVVIDMFQSHILNGGFIEKGFISDGYPRTIKQAESFSALLKNGKYPIKVIYLDVSSEALKKRLMQRGRMDDTLESIERRFQIYNDLVNN | Catalytic Activity: AMP + ATP = 2 ADP
EC: 2.7.4.3
Subcellular Location: Cytoplasm
Sequence Length: 145
Sequence Mass (Da): 16283
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A0A1V8MAN3 | MKLLGFIYGVIAYTLFMSWMVYMIGFLGYFPVPKSVDSVPTSSVGISIFINCLIVAIFAVQHTIMARPAFKQWITKYIPKALERSTFVLVTDIIIWVMIWQWQPIDGVIWDVQNAMVANILIAISILGWAVVCLSSFMINHFELLGLEQVWHYFKGTEPKKMTFQLRGFYKHLRHPLMFGFMMFFWVTPYMTLSHLCLAAIFTTYILIGVKFEERDLIKNHGDEYLKYKEAVPGLIPFAKGKKNG | Function: Catalyzes the methylation of methanethiol (MeSH) to yield dimethylsulphide (DMS).
Catalytic Activity: methanethiol + S-adenosyl-L-methionine = dimethyl sulfide + H(+) + S-adenosyl-L-homocysteine
EC: 2.1.1.334
Subcellular Location: Membrane
Sequence Length: 245
Sequence Mass (Da): 28332
Location Topology: Mult... |
A0A328RM18 | MTKETNITTSDTTFPDVASDERSPHPYTIEKVGMRQLQIPILIEDENGNYFKQSSTMNVYVDLIDPFTKGIHMSRLYNTLVKHFDATPFSLVNVESILKELADSQGEISSNSFLKIAYDHVIHKPALLSQNKGWRYYPVSYDFSYKNGLLNTKISFEVTYSSTCPCSAALSRQLLGEKFKDQFSEKDSISPSEVKNWLENKNNMGGVPHAQRSVGSIMLRVNPKKTGSLTECIEQVESAIQTPVQAAVKREDEQEFARLNAENLMFCEDSVRLIKHLFESKEEVLDYKIEVEHYESLHPHNAVAIAVKGLPNGYR | Pathway: Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1.
Function: Converts GTP to 7,8-dihydroneopterin triphosphate.
EC: 3.5.4.16
Catalytic Activity: GTP + H2O = 7,8-dihydroneopterin 3'-triphosphate + formate + H(+)
Sequence Length: 315
Seque... |
A0A8J2ZMG7 | MLNVFGSINLDIICDTQRVPGPGETLAARSMRRMAGGKGANQAVAAARAGAGLRMFGMVGHDDGASLALANLRAAGADVSGVGTADSVPTGTAIVMVEDSGENRILIDEGANGCLTADMLTGLGARDWLVLQLEVPADVTRGVVARAAAAGAHVLLNLAPAASVDRATLEQVRLLVVNETEAQFLASSLGCAPDARALSGALGNTVLRTLGAEGAEAFGPMTAGQTVSVPSPRIRPRDTTAAGDTFIGYLAAALEGGVSLPDAMARAARAAALTCLSAGSQDSIPDAHAVDAADFELNA | 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 ... |
A0A8S1ZKQ7 | MISSIKPVSSSLTAIAGVRRSIPAKLQFSPLPIIGNFQKPKPLPQKPLLSSQNLSNFPLAAAAAAQRSDVFRVGAYEADRSRPIEIGIDVPDEQSGQKVKIGIYFATWWALNVVFNIYNKKVLNAFPYPWLTSTLSLACGSLMMLVSWLNGGELLRLLICDVCSHCYSFYKMPSLDQTSSGEANEEVGLVFIGEFDAPILRAEDSRRFIHVKISRGDVELEMASDGFPSWLTILDKKFISSTPELLKMNADIVVAKDGTGNYTTVSEAVDAAPENSKRRFTIYVKEGVYNETIEIGKMKTNLTLIGDGRDATILTGSLNA... | Pathway: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 1/5.
Function: Acts in the modification of cell walls via demethylesterification of cell wall pectin.
Catalytic Activity: [(1->4)-alpha-D-galacturonosyl methyl ester](n) + n H2O = [(1->4)-alpha-D-galacturonosyl](n) + n H(+) ... |
I4DXI7 | MYKITVIVALLGAVRGLDKICLGHHAVANGTIVKTLTNEQEVVTNATETIENTSLNKLCMKGRNYKDLGNCHPIGMLIGTPTCDLHLTGSWDTLVERENAVAYCYPGATVNEEALRQRIMESGGISKMGTGFTYGSSINSAGTTKACMRNGGNSFYAELKWLVSKTKGQNFPQTTNTYRNTDTVEHLIIWGIHHPSSNQEKNDLYGTQSLSISVGSSTYQNNFVPVVGARPQVNGQSGRIDFHWTLVRPGDNITFSHNGGLIAPSRVSKLIGRGLGIQSEAPIDNNCESKCFW | Function: Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. This attachment induces virion internalization of about two third of the virus particles through clathrin-dependent endocytosis and about one third through a clathrin- and caveolin-i... |
A0A0L0DMC4 | MSWTLDPFTSARSCMVHPPNTSAAPVGGELLGPPALAVAPPPSSAASASAAAPAVRYEWLDDSGWKPYSPELAARLAAAEQAGTTASFKFGRSRYTIDVGAGTQTNDATGFVRQVRRVDGSAQTSPDAAAGAGYEWRDDSGWKPYSPKLAARLAAAKQAGTTVSFSFGRSRYTVDVAAGTQTNDATGFVRQVRRSKSAGGSSGYSAQPSSEPSSFDIFDLSNSARYEHDLVFEVRDEHGATQGSDAEALVAQTTAEGRGTSSTETRCCICLDDFDATAIHFVACGHPFHKACLVAAMAVTPKCPLCTKAYDTLIGPQPPG... | 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: 446
Sequence Mass (Da): 46871
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A0A6J3XIA2 | DFYFWIWAGMVGTSLSLLIRAELGTPGSLIGDDQIYNTIVTGHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLISSSIVENGAGTGWTVYPPLSSNIAHGGSSVDLAIFSLHLAGISSILGAINFITTIINMKINGMAFDQMPLFVWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHLENLK | 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... |
M1IPK2 | MQENSSNFIRHAPCENCDSQDNLAIYLTPDGSHGHTYCFGCHSYEKTNGELPEVATTKKITNMIEGITEALPSRKINSETCKKFNYETGTYKGEPVHIANYYDKDYNKVAQKLRFADKRFIWLGDPDKITLFGQQVWREGGEKSKIILTEGELDCLSVSAVQGNKYPVCSIPSGSASAKKFIKKELQFLSKFSSIILMFDTDEAGVKASVEVANLLPVRKVKIARLPAKDPSELLQKGQGSKIIDAMWEAKAYTPQGIIQGSDTKDLLLNDEEVETIPYLWNGLNEKLQGIRFGELNLLCGGSGTGKSQMCREIAYDCIL... | Cofactor: Binds 2 Mg(2+), one of which is catalytic.
Function: ATP-dependent DNA helicase and primase essential for viral DNA replication and recombination. The helicase moves 5' -> 3' on the lagging strand template, unwinding the DNA duplex ahead of the leading strand polymerase at the replication fork and generating ... |
A0A142Y6M7 | MNDYIAALLQGIVEGLTEFLPVSSTAHIILTQELLGIDRTLPFWKMFAVVIQLGAILSVIAFFRARLAAFLVSFRASLKSDWKASYRHPLALVLVSFVVTAIPCFLIDEIIGENLESLWVIAIALVIGGIAMVVIDRVYSDHAKTERLEEMSLRQAIAIGFFQILAAAFPGTSRSMATIAGGQIFGLSRSAALEFSFFLAIPVMFAASGFKLVKHLATEPMPSGGEWTSLAIGFVTSFVVAYGVIAWFIQWVRSRGFVPFAVYRVIAGTGLLLWLWLR | 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: 278
Sequence... |
A0A1V3SI70 | MNSNIDATKQPATWSPSDRWAQAAQRPWHRPLYLPLDAPHHMAFRLRGNPEGGAWLLLHGGPGGRCQPGMLSPLDLARHWAIAPDQRGCGNSRPQGRAVHNHTHALVADVEALRVHLGLERWSILAGSWGTVLALAYAQRHPERVERLVLRGAFALRRREVGGLLQGARRSGKTMRPAPRSWPTAPGTSLPALLSRLRQLLQTGTPAVASLRAARRWALLEMRDAERGLRRALVHVALQQPESAPALRGAWASLRRGARQRAAALERPAGRDDLALQRQYSVQSHYLLHRGFVRPGELDRAVRTLAQRGVPVAWVHGRCD... | Catalytic Activity: Release of N-terminal proline from a peptide.
EC: 3.4.11.5
Subcellular Location: Cytoplasm
Sequence Length: 370
Sequence Mass (Da): 40586
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W0ZCR3 | MTVIEPRLTLERRLLRERPIVIACDEVGRGALAGPVAVGATAVDAGRARKRIPQGLRDSKLVPEARRADVAARAADWVSASGVGWASAAEVDEVGIMRALGLAAIRALADLRAHGIELEEGIVILDGNYDYITAAGATGLTVQPVIKADRDCASAAAASVIAKVARDAVMTGLHDDLPEYQWARNKGYASAEHRLAIDEHGLSPHHRASWAIAPATLF | Cofactor: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
EC: 3.1.26.4
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Seque... |
R6XGK3 | MDKAKLIEELICYATKNLSLKELDSYYVRNVLMRKFKVDKTYDGEIDKKAIEELSLPDSLIEKIKELAKEEHLVDEGDEDLFACEIMGDLSLLPQNFVDEFHKIAEEKDKQAALDWAYDYEIKNNYIAKSAIDKNIVWSCQDGKRHVEISINLSKPEKTNKDIAKAKAAPATGYPKCALCIENLGFKGGNGKPPRENIRIVPLTLCGNPWFLQYSPYGYYYQHAIVINTKHSPMFISRQTFANLLSFLDVFPTYFVGSNADLPIVGGSILAHEHYQGGRHRLPVYDSADLFEIEHKNFQDLKITYLDWYNSVIKISGKNK... | Pathway: Carbohydrate metabolism; galactose metabolism.
Catalytic Activity: alpha-D-galactose 1-phosphate + UDP-alpha-D-glucose = alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose
EC: 2.7.7.12
Subcellular Location: Cytoplasm
Sequence Length: 507
Sequence Mass (Da): 58546
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G0ZGE8 | HLVFLHETGSNNPAGLNSDTDKISFHPYFSYKDLLAFAGLLITLTSLALFSPNLLGDPDNFTPANPLVTPPHIKPEGYFLFAYAILRSIPNKLGGVLALLSSILILMLVPILHTSKQRGLMFRPMSQLLFWTLVADMLILTWIGGMPVEPPYIIIGQVASVVYFLILIILAPSAAWTENKIMKWACNS | Function: Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membra... |
A0A1K1VMB0 | MAFLERITRLMSLALVVIGFVAVALMMLHITADVFLRSAFDVAVPATERIVTRYYMIALALLPLGWVEWSKSMISVDAFSAAYGRVGERFVAVFVPLLSAVIYGVFGMATWLQAMEQFKVGAYIMSLDLVIPLWPTYFLVPLALFMAMLVCLVRIVAGFLPSSSTGTDS | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 169
Sequence Mass (Da): 18629
Location Topology: Multi-pass membrane protein
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A0A2R6AIY9 | MGEDGGLNHILVPKHELLSKEDSEKVLKELGVKLWQLPRIYQDDPAIRHLNPEVGQLVKITRSSELAGEYVVYRVVVSSLTAKSTTTEKKEEKAEKRKTKEKSATKSRTTSKSRKRKRASRHPNLNVLERAKGDGFCQTTKTTIMTLQSH | 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: 150
Sequence Mass (Da):... |
A0A212LGB0 | MSTLPPAPGKAGSELASRVLSAVVLAVVTVGALWAGGWVFAALSAVVAVLILREWMAMSGPFAFRAAPWALMAFLAVTVAMAGDEPLESLGFSALVAAALLLARVTEPRVAWLSLGVLYAGVPAIAAVALRGPDTLTFASTGAVAVIFVLAVVWATDTAAYFSGRLIGGPKLAPRFSPKKTWSGAIGGAVAGVVAGCLVAAAAGIGVGAALVLVALLLSVVGQVGDLAESAMKRHFGVKDSGVLIPGHGGIMDRVDGLVAALAVAVVIGLGRDWLAGGGIAEGLLIW | 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: 287
Sequence Mass (... |
A0A554V8K0 | MGLAALPVIASGLLVQQTLAQRVTVAEAAWWIGGVAAFMLTLFGVGRWLVPHADPVLLPCVAMLNGVGLVLIYRLDLAGLPIGHRSVGPSLESDSAHQVLWTLIGLCVFVAVLWFVDDHRVLGRYGYTCGLAGLVLLVVPAVLPGSISEVNGGKNWIRVHGFSIQPAEFSKILLVVFVAAFLVHNRDLFSQAGRRVAGMTLPRARDLGPLIVVWAISTLVLMFEKGLGVSLLIFGTLLVMLYVGTGRASWLLIGLVLFAVGATASYYLFAHVRVRVEIWNDPFATYATTGYQISQALFGMATGGILGAGLGQGSPDDVPF... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Catalytic Activity: [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-... |
F4GJD5 | MESRAGRLDSRLISCYRAFMTAIHPSYAKVNLHLEVGAKGFDGYHDISTVFHLVSLHDDVSVELRLSDKFSCSVTGLESICRPGEDSLHRAAEAWCHATGRPLSLDIRVTKRIPSGAGLGGGSSNAATLLSILDAAAPGGYSMGRKRLMELGTTLGSDVPFFLSGYTAAIGEGRGERLTPLKAVRDAHALIVMPPFSVSTPHAYLSLDTLRGGDSVSLHRFSFMAGDSSRLSSLLEDDVTKWMFSNDFRLTCGHEDVYDALEALGRKVPGVFSSLTGSGAAWVFISRKLLSLKDIQTQISRLFGVRFVMFSAILLFS | Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 3/6.
Function: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
EC: 2.7.1.148
Catalytic Activity: 4-CDP-2-C... |
A0A259LV99 | MSDVTRETMEYDVVIVGAGPAGLSAAIRLKQLDADLSVVVLEKGSEVGAHILSGAVLDPCGLNALIPDWKEKGA | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Accepts electrons from ETF and reduces ubiquinone.
EC: 1.5.5.1
Catalytic Activity: a ubiquinone + reduced [electron-transfer flavoprotein] = a ubiquinol + H(+) + oxidized [electron-transfer flavoprotein]
Sequence Length: 74
Sequence Mass (Da): 7662
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A0A1E8FBY3 | MDFKKLVLAVVLGSVATTALAVDKNAVRSQAKMMHGPLPAAMPGAENDTPALIDLGERLYFETALSADGTQSCNSCHRIDGGRGGVDNEATSLGVKGSRGDRNSPSVWNAGFHVAQFWDGRAADLAAQAKGPILNPVEMAIPDEQTAISNLKKEGYEALFAEVFKGEADPLTYDNLAKAIGAFERTLITVDRFDKFLAGDDTAITDLEAKGYQTFVQSGCASCHNGATFGGSMYMKMGLVNAYENTHDMGRFAVTNNPADKFVFKVPSLRNITKTAPYFHDGAVAELDQAVSKMAWMQLGRQLSEQELAEIVAFLGALED... | PTM: Binds 2 heme groups per subunit.
Cofactor: Binds 2 heme groups.
Subcellular Location: Periplasm
Sequence Length: 337
Sequence Mass (Da): 36122
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A0A0B1NZD0 | MLHARLFAATPKFRDAHFQPLRTSLSSHASSPGDEPYLDGNPKLDRPLFVQFCANDPNELLAAAKYVAPYCDAIDLNLGCPQGIAKKGKYGAYLQEDQELIFSLVNVLHENLNIPVTVKIRILDSKERTLAYAQNVLKAGASIITVHGRTREMKGHKTGLADWSVIRFLRENLPSDTVIFANGNILKHKDLAHCLEVTGADAIMSAEGNLHDPAIFASPPAIGEEGREYWRAQDGKSGWRVDAIFRRYMDIIYKYVLEIPPPERKPLYLPSDPESDIQVTQMKNGKRGKKLKNRPIQI | Function: Catalyzes the synthesis of dihydrouridine, a modified base found in the D-loop of most tRNAs. Specifically modifies U47 in cytoplasmic tRNAs (By similarity). Catalyzes the synthesis of dihydrouridine in some mRNAs, thereby affecting their translation.
EC: 1.3.1.89
Catalytic Activity: 5,6-dihydrouridine(47) in... |
W0RGL1 | MRRGMSVPNAARWAVWLGVLAGMTAGMLAVRGYLDKAHVALVYLLVVLGASADVGRRLGLVVATLGFLLFNALFLPPYNTLVVANPLDWIVLFAFLATSIVAAQLLARERATAETATARAREIDRLAALGAETLSVPRADDALLAIASVIRSALGVDECEVYQRGLDGRVTPVARAGDVRDGADASARPAGVPAVDDASLVAFLVANRASAVELADGGVRLAHPPDDAHPSDGSGVLGDAIGEAEWLPGVAHVVDGASWAGARALLLSLTARGHTVGVLRLASRAGLRFTPEQARLLTALAYYAALGVERVRLVASAERA... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 557
Sequence Mass (Da): 58709
Location Topology: Multi-pass membrane protein
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A0A6G1DF46 | MTSLSRTLSRGGPMQPAGPRRIRRTQTAVNLGEQIFDSEVVPSSLVEIAPILRVANEVEASNPRVAYLCRFYAFEKAHRLDPTSSGRGVRQFKTALLQRLERENEPTLTGRAHKSDAREIQAFYHHYYKKYIQALQNVSDQVDRAQLTKAYQTANVLFEVLKAVTQQHSVEVDHEILEAADKVKEKTKIYLPFNILPLDPDSGNQAVMKFPETDNVSNQREHLILLLANVHIRRNPKTDPQSKLDDNALNEVMKKLFKNYKKWCKYLGRKSSLWLSTIQQEVQQRKLLYMGLYLLIWGEAANLRFMPECICYIYHHMAFE... | Catalytic Activity: [(1->3)-beta-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->3)-beta-D-glucosyl](n+1) + H(+) + UDP
EC: 2.4.1.34
Subcellular Location: Membrane
Sequence Length: 887
Sequence Mass (Da): 102513
Location Topology: Multi-pass membrane protein
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A0A0N1KGS5 | MPGADCLSTIDCFRKLGVDIRQDGTTVVVEGAGPGGLREPAAVLDVGNSGTTARLLLGILAGQPFHACLVGDESIAKRPMGRVTKPLREMGARIDGREGGNYTPLSIRGGALRPLRYTSPVASAQVKSAVLLAGLFTDGVTSVTEPHRSRDHTERMVRLFGGEVNVDGLTVSVTGPQRLRGAHIYVPGDISSAAFFLVAGAIVPNSEITLKNVGLNPTRTGIIDVLTQMGADMAIDNVRNEETEPVGDMTIRTSMLQAIEIGGDLIPRLIDEIPIIALLATQQKERPSSKTRAN | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7.
EC: 2.5.1.19
Catalytic Activity: 3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate
Sequence Length: 294
Sequence Mass (Da): 31096... |
A0A5C8SYM3 | MHGASVGESLSLVGLVEGMIARGFSVLVTTGTRSAADLIGARLPAGAVHQYMPLDAPRWVARFLDHWQPDLALVAESEIWPNTVVALHARAIPLLLVNGRMSEQSFAGWARAPRTAKALLARIAICLAQTRDDAERFVRLGAPRVSVAGNLKYDAAVQPADRQQVAYLGDMIGDRPVWVAASTHPGEDAAAAEAHAALKDRFPRLLTIVAPRHPYRGGDVAACATAHGLRSA | 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... |
A0A1M7B6R5 | MKIQLWSIGKEHDPYIRDGMAVFQKRLQHYVDFEVKLIPTVKQAASLSIPELKKAEAKIIMDLLQPTDFLLALDEKGKMMTTVQFADFLQQRTNAGTRQLIILVGGAFGIDQTVLQRAQLTMSLSPLTFPHQLVRLIFTEQLYRAYTVLNREKYHHQ | Function: Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA.
Catalytic Activity: pseudouridine(1915) in 23S rRNA + S-adenosyl-L-methionine = H(+) + N(3)-methylpseudouridine(1915) in 23S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.177
Subcellular Location: Cytoplasm
Sequence Length: 157
S... |
V5WI28 | MFGNSSLLKGLIVFEGLDGAGTTTQLRSLEARLEALKRPYYITFEPTDGAVGQVIRTVLGGKEAFQRETLARLFSADRYEHLHGNDGMIAHLDRGDLVITDRYLFSSLAYQGLDLGMEKVWEFNRDFPLPEILLFFDIPPEDGERRYSRRDSLEIYEKLSTQHAVRDNYMEILDHLKQSDCEVIIIDSTKSIDKISDQVWSIVSRHPIVTM | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
EC: 2.7.4.9
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Length: 211
Sequence Mass (Da): 24159
|
A0A7S8CAT9 | MTKELLHMTSTYAKELEQVLLGEKTEEEILLYLKEVEKHSFTPEEVGEMVQTIKNHAIYSPTFESSTLVDMCGTGGDKHHTFNISTAASFVVAGAGLPVAKHGNRKLTSSSGSVDVLEALKIPFSQDLKEHEESLQRNNITFLSAQHVYPALKPLAIARKAFGKPTIFNCLGPLTNPFSVKTQIIGCYREQDQEMIAQVLLEQGKKGIVLTGDQGLDEASLSGETKGIRITENGLESFILHPNDVGLEISPLSAIKGGTPEENAQTMVKLFEGEKGPIYDVVILNACLAIFASGIESTLKTAMGRAIQSISSGAALKVLR... | 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).
... |
A0A7V3M1R0 | MGEMEKRALLASALAILILIAYQVFFVPPAPRPGAERPVEAPAPSPALAPELAAPPAPRRPPMAARQPLREEEIRLETDLLEVLLTNRGGTALSWRIKRYTDGGGQPVDLAPALAPGEPSLSLAAWVEGGRGPDQLLEIVSRPSGAAGEAQTLLFRAVEEGGLVLEKRLTLHPGKYQADLELRLLNQGTGATTPNVRVAWGPGFQATGGNAAGQGGQTVALVGGKRVTEDIGKLKEKEEVLHKGEVSWVAVQGTYFAAALVPAGGSPAAVLGKGAGDRPVAALRFAGTALPAGAERRLVLHFFGGPKEVERLRDLGQDLE... | 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... |
A0A7S8HGV3 | MEQKNNLFYRDTWVDIDLTQIEQNIISIKNTLPKGKEIFAVVKANGYGHGAVEVAESAIRSGVGGLAVAFIDEALVLRNGGITHPILVLGASRPQDVPLAQKNKLTLTVFRQDWLVEAEGWLDSSIPVKVHVKIDTGMARLGVRTMEEFLAMTDWIESHKGIELDGVFTHFAKADEDDQSFMLEQRDKFVQYVEALPKKPKYIHHSNSGATIKIPDDPTNMVRVGIAMYGLLPSEEMKNEMPAGVAESFSLHSRLIHVKKVEAGEPVSYGSTYHTKEAAWIGTIPIGYADGWLRRLQGADVLVGGVRCEIVGRICMDQCM... | Pathway: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1.
Function: Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids.
EC: 5.1.1.1
Catalytic Activity: L-alanine = D-alanine
Sequence Length: 387
Sequence Mass (Da): 42948
|
A0A1F4VRX8 | MTKLTNFKVEAVSEEGSSGIYSISPLPPGFGTTLGNVLRRILLSSIQGAAITEVRITGVSHQFSTIEGIKEDVVNLILNLKQIRFKLHDENPVVVTLSTKGIKSVTAKDFDANPSAEVMNTDAPIAELTSAKATLELQVLVEPGFGYVQRESNEHPKIGVLPVDSAFSPIMHVADSVEPTRVGEDTNYDKLILRIVTDNSITPREALTQAAQLAVAYFAKISGQSVDLDNLNALVAPIERVEESAVALSKKEASIVVDDLDLPLRTINSLKKFGIHNLGDLVGTPELELMNIRGLGETSIKQIINLVATESWK | Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
EC: 2.7.7.6
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Length: 313
Domain: The N-terminal domain is essential for RNAP assemb... |
A0A368C057 | MNLGFISDLHLSETDTSLTNAFVDFLKSHSSNLDQLYILGDLYEVWIGDDDSSSLITSTKNALSKASKAGLEIFFIHGNRDFLLDSSFAESTGISLLPDPFFFDYFGKKIALSHGDMFCVDDTEYQTFKKQVRSPKWKTEFLNKSLVERKSIASSMRDASKKNSSQKDLMIMDVNTNEVTSFFDKHDIDLLIHGHTHKPNIHELDGKNSKLKRVVLGDWDKTGWCFYLDSTSQNLEEFKI | 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 ... |
A0A2P5K6H5 | MNIPDFFFSPCTEVLLLAIILDIIFQEPPGAIHPVVWMGKGIRYLQELPFSNKKIHGIFLVVVMIFTSFIVGIIIVITAQMLPETISLLILAFFLKSTFSFRMLLGTGWNIMNLINSKKSLKAQEELRALVSRDTTGLDKPHMVCAVIESISENFVDTILSPLLYYLILGVPGALAYKSVNTLDSMVGYKNTEFIELGWASAKLDDVLNWIPARLSLIFITLASFFGGNPKNTITVCIRDRTLTSSPNSGWPMAATSGALSIQLEKPGEYKIGREFVLPDTKDIENVIKLITIASMIIYLMLVIIDNPFMR | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
Function: Converts cobyric acid to cobinamide by the addition of aminopropanol on the F carboxylic group.
Subcellular Location: Cell membrane
Sequence Length: 311
Sequence Mass (Da): 34685
Location Topology: Multi-pass membrane protein
|
A0A7C0VSA8 | MKLFFVVLDGVADEPIKEFGNSTPLEAAETPNLDYLASNGITGRIRIMGKYAPETDTGVMALFGFDPLKYHRGRGPLEAYGIGYNFKEGSLALRGNFATVEKNRVVDKRAGRIQSKEARKLVNEINDNVKLEDVKFELLHALNYRVVLIMKTTKFKFSHLITNTHPGYKRLRGHLEVAVKKESKMYRLCKPLVKRKSAILTAKVVNEFIDKTREVLEQSSINKRREKRGLKKANMILFRGAGTELPKLENLKKKYGLKWFCIGDTPAERGIARLLGMELIKGLPEPECDKLSSSSNIKEIKKAVRKDMRIRAKAVKDNLS... | Pathway: Carbohydrate degradation.
Function: Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
Catalytic Activity: (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate
Sequence Length: 437
Sequence Mass (Da): 49152
|
A0A973P9W5 | DLVRSRAEVVASREDERRRLRRDLHDGLGPTLAAIGLKAGLAARGVPDDSAAHAALREIATEATASLGDVRRLVEALRPPALDELGLVGAVRSRAATLAGEVAIAVSGDDAPGPLPAAVETAAYRIAVEAMTNVVRHSAATSCLVEITLRPEFVEVTVTDDGQGIDPARAAGVGLRAMRERAAEVGGEVSIGSGVDGVGTRVHARLPIAAMTPPDGRTG | Function: Member of the two-component regulatory system NreB/NreC involved in the control of dissimilatory nitrate/nitrite reduction in response to oxygen. NreB functions as a direct oxygen sensor histidine kinase which is autophosphorylated, in the absence of oxygen, probably at the conserved histidine residue, and tr... |
A0A074VUV9 | MDMSDQGASDYRRDTDQATLKEAPTNRSKASRGSLDITESNNSASNSRPFISSAGPSPPDEGNNGRAQNQHQPYVEDGYAELNPAYSQPGNVRPIWGLADPMPRIIRRGMKPSQQEIQADRPKPGEEDEDVLQPTDSQMEQGIGPKLNLNKLDKSIHDATKERERKYADKYGKKSEPPSEMGQESHTRPAGFLQQLTPPHEAGEDEEELSKASTRRSDTERQQQHSRSEDGHDEEKDEETNDDVAESTSVQRNEGISPINNIEGELHNHHTLWAVLRTKLREPLAEILAVFVLITIGICANVAHNLTNSGSSDSMAWSWG... | Catalytic Activity: H2O(in) = H2O(out)
Subcellular Location: Membrane
Sequence Length: 555
Sequence Mass (Da): 60985
Location Topology: Multi-pass membrane protein
|
N6VGN9 | MEEDEGGYWGDLWEAMESEIESLDKSFTLFAAGDFSPFSMFMAADRVVQAVIIVLILASLVSWTIALAKIVEITLAKRKARRALRFSLNAQTFTHLASDFKNQQEKNLVFLGAGAVFLEETLKEVDLSTQQVVFIKFQGARERRDDDTTLCAFNEGVKERVHLLLARCVLAATGRMACGTAILATIGAIAPFVGLFATVWGIMNAFIGIAQTQTTRLDVVAPGIAEALLATAVGLFVAIPAVVMYNGLTRALNGYRNDLGDIAAAIERLLSRELDQQRQQKSRKQ | Function: Involved in the TonB-dependent energy-dependent transport of various receptor-bound substrates. Protects ExbD from proteolytic degradation and functionally stabilizes TonB.
Subcellular Location: Cell inner membrane
Sequence Length: 285
Sequence Mass (Da): 31252
Location Topology: Multi-pass membrane protein
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A0A2E5CA32 | MLKFLRLIYFPFSVLFTAAITLPVFFLRPYNPKNSSLFLKTFALLTLRPMGFKYTEYDKHNMTNSRPSILVGNHQHNLDVLVASKAFSDHVVVLGKKEILYIPFLGLCFYLGGNIFVDRKNKKRSRKSLDHVKKKLKDKNLSVVIFPEGTRNPEKGLLPFKKGAFHTAIQTQLPIVPFVVSQYAQDMNLNKLNSGHIEVKFLEPIPTEGLTMANMTELMEKTRNAILAGLDEFDQKM | EC: 2.3.1.51
Catalytic Activity: a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphate + CoA
Sequence Length: 237
Domain: The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate.
Sequence Mass (Da):... |
A0A485A9L5 | MTDLVVAKFGGTSVADFDAMNRSVDVARLDENTRVVVLSASAGVTNLLVALAEGLEPAERFEKLESLRQIQFNILERLRYPNVIREEIERLLENITTLAEAAALASSAALTDELVSHGELMSTLLFVEILRERGIASQWFDVRKIMRTNDRFGRAEPDIAALAELTQLQLTPRLAEGLVVTQGFIGSEAKGRTTTLGRGGSDYTAALLGEALNASRVDIWTDVPGIYTTDPRVAPAAKRIDVIAFAEAAEMATFGAKVLHPATLLPAVRSDIPVFVGSSKEPTAGGTLVCNKTENPPLFRALALRRRQTLLTLHSLNMLH... | 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: 393
Sequence Mass (Da): 42341
|
A0A2M7RHH4 | MKLIFASRNPGKIKEIKQLLNELEIEILSVDEAGITEEITEDGKTLEENALKKSRFVAEKSKGWAIADDTGLFIKALDNAPGINTNRWAGENASDRDLIDYTLSKLKGVPKEERKAYFKTVVVLYAPAGKNWIFSGKVKGRIVEEPTGKPRAKLPYDLIFIPKGEKRTFAEMSDKEKNCISHRGIALKKLKEFLAKREKLL | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as ... |
A0A2N3GG08 | MLTSAPNLSTRPPLLRRWYCTGPRRWSARCPLWASKSALTGVTAYSSGVDYRVADLTLAAAGREQIRLAEHEMPGLMALRKRFGDSQPLAGARIAGSLHMTVQTAVLIETLVALGARVRWASCNIFSTQDEAAAAIVVGPNGTPEDLQGVPVFAWKGETLADYWWCTEQILDWGDELPNLILDDGGDATLLVHSGVEFTKAGAVPEAGPDDSAEWAVVLDTLRASKLHWPTLATAIFGVTEETTTGVHRLYEMAKNRTLLFPAINVNDSVTKSKFDNRYGIRHSLIDGINRGTDVLIGGKTAVVCGYGDVGKGCAASLAG... | Cofactor: Binds 1 NAD(+) per subunit.
Pathway: Amino-acid biosynthesis; L-homocysteine biosynthesis; L-homocysteine from S-adenosyl-L-homocysteine: step 1/1.
Function: May play a key role in the regulation of the intracellular concentration of adenosylhomocysteine.
EC: 3.13.2.1
Subcellular Location: Cytoplasm
Catalytic... |
A0A7C4A7V7 | MGPEGTQERKRNIKSLSLADLAELMDSWGQPAYRVRQLARWLYQRGESDFEGMTDLPLSLRQKLKDSYYVGQLRVVGEEKSADGTRKLLIELEDGEHIESVLIRDKNRLTACLSSQVGCPLGCLFCRTGRFDYRRNLESHEIVGQVLALQGVLEVGERITNLVFMGMGEPLLNLSALKESIALILSQDGLGFSPRRVTVSTAGLPAGLVEMGAWGFKTKLALSLNAADDETRSALMPIGRKYPLASVLSACRSYPLPRGCRLTIEYVMIDGVNDRDRDAEGLARLLGGMPTKINLIPLNPWPGCPFRPPSPDRIEAFQRI... | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs.
EC: 2.1.1.192
Catalytic Activity: adenosine(2503) in 23S rRNA + 2 reduced [2Fe-2S]-... |
A0A7C7JL89 | MKSNILALKYRPKNFDELVGQEAIARTLKNSLANGATHHAYLFSGLRGSGKTSSARIFAKTLLCDKAPTPLPCEECESCKMANSGSHLDIIEMDGASNRKIDDIRDLIEQTRYRPSIGQYKIFIIDEVHMLTKEAFNALLKTLEEPPSYVKFILATTDPQKVPQTILSRTQHFEFKKIPDKKIENHIISILQKEGIEFEKEAISAIVRNGSGSLRDTLTLLQQAIEYSNRNITLQSVAEMLGLIDVSILETLLSAIVHKDRDAILETLQNINDSETEHILDEFSNFLKGKIFLGEVEDTILQRIASSIEEGKKLLFSGVD... | 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: 499
Seq... |
A0A0P8A6X4 | MKPPVLNRSIPWSRQLLEWVAIALIYFLSAQLSLRFAALPGNISSVWFPTGLILGLSLWRWQWRAVPGVFLGSMLSTSLDLSLSPTPLGLVSILFCGLIHGSSNALELSVVLSLLQAWIPQKNILQRVSHVGLFILSLIPASLIGATLGIFPLVVIGLIPPPEVPRSFIIWAWSAVLSQLLITPVFLAGMAAPTQWRPKPGRHRTLEITLFIGVSVIILIGTFGVGYPAEYALIPLCVWSVLRFGKFETTLFVFGISLIAIFTTVQGLGPFAGHSTYIAFTLLQSFMGATILTSLVLSASNDEHHQVEQQLRDSNRELHK... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 765
Sequence Mass (Da): 85298
Location Topology: Multi-pass membrane protein
|
A0A0C9RBD6 | MGLSSIVRNILLGIPIGVTFVNTVGYVARVEGISMQPALNPNAKEYDYVFLNCWTVHNYNINYGEIISFKSPKNPEQKLIKRVIGLEGDEVRTIGYHTSILRFFVSGARRSLLGRR | EC: 3.4.21.-
Subcellular Location: Membrane
Sequence Length: 116
Sequence Mass (Da): 13073
Location Topology: Single-pass membrane protein
|
X6CJL6 | MAAIVFVAALMLDLGTKMWVRASLPSPDGLDPLPFLALRPRYNEGTTFGLLSGGTTTDLMVLVTVTVLAILGLWWWVARAKGPQVIIGAGLMAAGALGNLVDRLTIGMVTDFIGLHVGGWYSVIFNMADIWVVSVQCWCSLAHVRDARRVPGKHEPGANLHSDRATGVRKNCLEQRKLVGCHVLPCNIRRILSVVCEHLGKASSFGAVPLSDLQHRKLGSNGLEDRSFGRFGRAWSHISRHGVLEPIRLVHRHGLGASLGFV | Pathway: Protein modification; lipoprotein biosynthesis (signal peptide cleavage).
Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, ... |
A0A972VUW5 | MNISDRWLLPDGIDEVLPPEALNLERVRRRLLDIFAVWGYDYVIPPMVEFLESLLTGTGRDLDLKTFKITDQMSGRMMGIRADITPQVARIDAHSQNKKGVARFCYAGTVLHAQANNMLASRAPLHVGAELFGDSGSPADLEIVSLMVESLHGLGMPSVVIELGDVGIFRLLVQQFKISPETEEKLFALIQKKAMVELETCVQELDLDAGHKQIILELPGLCGNSGVLARAEAVFGGYPQIMQRLASLGEVARGVESRFSGIQIYYDLSELRGYNYHTGIVFAAYLGEARRRVAQGGRYDSIGSVFGRDRGATGFDVDVK... | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
Function: Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine.
Subcellular Location: Cytoplasm
Sequen... |
A0A011NYU3 | MSAVSSVPVIAVSSGEPAGVGPEICLRLADCALDARFPARIVVLADRSLLAERAAALNFPGRLRDWQPDLSPQAGTLDILHLPLAAAATPGRLDAANSPYVLALLDRALDGCQSGEFAAMVTAPVHKGVINDAGIPFSGHTEYLAQKTATPRVVMMLAGGGLRVALVTTHLPLRDVPAAVTQDAVEETLRILHREMAAKYGIARPRILVAGLNPHAGEGGYLGHEEIEVITPVLERLRGEGMSLLGPLPADTMFSPPVLERGDCVLAMYHDQGLTALKYASFGQGINVTLGLPIIRTSVDHGTALELAGSNGAGTGGERT... | Cofactor: Binds 1 divalent metal cation per subunit. Can use ions such as Zn(2+), Mg(2+) or Co(2+).
Pathway: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 4/5.
Function: Catalyzes the NAD(P)-dependent oxidation of 4-(phosphooxy)-L-threonine (HTP)... |
D2RLL1 | MANIVLIGMPGAGKTTIGKKLSKVLGRPVIDADDVVVQQTGRTIKSLFQEGENVFRDAETAAIRSLAAKDGIIISCGGGVVKRPENMAYLQETGKIFFLNRDLAAIAGCVDKVSRPLLNSAEDRLTQLYRERMPLYLKYCDYAIPVDEDFDKTTKYIIDLIRKLGI | 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... |
A0A8T3ZHM0 | MVERKRKTAEDMAREQKEISISEFFEKNKHLLGFDNPTKALLMCTKEAVDNALDACEEAGIVPDVTVKVRQMKDEKYRITIQDNGPGIVKQNIGKAFGKLLYGSKFHRLLQGRGQQGIGISACVLYSQLTTGANTKVWSKTESDKRMHYYELQINTRKNEPEIMKEEILDPSFEHGVRIEMDVTGRYRKWVEDYLKQTSIANPFAKIAYTAPDGTKTIYPRSVNELPKAAKEMKPHPYGIEFGIIQRMLAVTASRSLVAFMTNEFSSVGNQTAREICKVAKLDANAKPQELDREQIEKLLAAMQKVKVQRPPTDCLSPVG... | Function: Relaxes both positive and negative superturns and exhibits a strong decatenase activity.
EC: 5.6.2.2
Catalytic Activity: ATP-dependent breakage, passage and rejoining of double-stranded DNA.
Sequence Length: 558
Sequence Mass (Da): 63269
|
A0A2M7RFN5 | MQKIIVILGPTASGKTHLAINLAKKFEGYIISADSRQIYRGMDIGTDKLPEKERRGVEHRMIDIVDPNQEFSLAQYQKRVFSIIKQSDKLPFLVGGTGLYIKAVVDNLDIPKSGPDKVLRKKLEEKSNEELLKELIKLDVAAARTIDENNRRRLIRAIEVCRTTGHKFSKQTSKQKPIVNALQIGVSAPREELYQKIDRRVDEMIKEGLIEEAKKLGERYGWDIPSMSAIGYRQLGLYFQKRITLKEAVELIKKDTRNYARRQLTWFRKDERIHWIKSQPEAEKLIKNFIKKIPRA | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
EC: 2.5.1.75
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylall... |
Q7VQF5 | MINDTSRIHIAFLGPKGSYSHIAAKKYANYHFNKITEYSCQNFSDILHVVENNQVDYGILPIENSNSGLINEVCDLLLTTHLILIGDITIPIQHRILVNNYNSSLKQIQTIYSHPQPIQQCSNFLKKFPHWKIILCESSSIAIKKVAYLNQPNIAALGSTQGGIIYGLHPLLLSPYIISNYPLNSTRFIILKNENLLFTNTTAILEKIMLIISIDTKLNKLYSILKILQFYKIKINFLRLCCSLLPNNTTNSIILEITAHFHHTYTQQALIKIYNIAYSLKILGCYSTIAYQPYQQYT | Pathway: Amino-acid biosynthesis; L-phenylalanine biosynthesis; phenylpyruvate from prephenate: step 1/1.
EC: 4.2.1.51
Catalytic Activity: H(+) + prephenate = 3-phenylpyruvate + CO2 + H2O
Sequence Length: 298
Sequence Mass (Da): 34028
|
A0A2M7GVH4 | MNPGFGAPELIVLAVLALIVVGPKDLPMMFRRVGRFVGQARQMARDFQRSFDDMGREAEMSELRREIEALKTGNPVAKAKRDIDEVKRDLASLEHETVVGRKLAAAEKDHSIGGGKKPAAKDELAPSEPSQPTVQPYKSPKKKTKKPVADE | 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. Together with TatC, TatB is part of a receptor directly interacting with Tat signal peptides. TatB may form an oligomeric binding... |
A0A2M7NXY8 | MGRVLIGRIGRRHGLGDEFYMTAFMPLPEDLNSVFLEENSDNPGGNSREIGIESLKQARHGGHSAADKWLVTFTGADDSLTGKCISCEKWELDGGFFWREDLVGCEVLEPSGIKLGRLSEIIDDASQVWIRIERESGETISVPFLERFVKEVDTKGKKIIAVFPESVIVRDE | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but ... |
A0A5P6P554 | MHAPVHPRVGSRQVFAIAGPAMVANLTTPLIGVVSTTAIGRLDDAALLGGVAMASVIFDCLFWLFGFLRMSTLAFTAQALGSGETRELTAILMRGFIVAGLIGATLIALQLPLAAALFDLMGGSEGVTRAAKSYFMIRIWSAPLALANYVILGWLVGQARANPALLLQVAINLVNMVATVLLVLVYDTGIAGAAVAALLSETIGFVLGVIVCRRFADGGLAVPRATLFDRDKLMRLLSVNSDILIRTAALIAVFLFFTAKGARAGDVTLAANSVLNNFLLVSAFFLDGLANAAQQLCGRTFGARDARGFADSTRLVLLWG... | Function: Multidrug efflux pump.
Subcellular Location: Membrane
Sequence Length: 460
Sequence Mass (Da): 48946
Location Topology: Multi-pass membrane protein
|
A0A8T3X1N8 | MEIKIIENENGKLKAEINDNSTLVNAINEKILTQRGADVSAFTTGHPYLGKPVLMVRGKDPEKAVIAAAEELIEDAKALKKQLGKQ | 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: 86
Sequence Mass (Da): ... |
A0A8T3ZH24 | MNIYIETYGCSANQSESEMMAGMLARSGFHITGSMDAADILIINTCVVKKPTEDKILERLRQLSAKYPEKKILVAGCMPEVLPEKIREAAPQASMLGTHYIADVSNVIKKLSDGISVEKVGKTQKEKLCLPRIRKNDSIAIVPISSGCLSNCSYCIVKRVKGSLFSYSNEKIIREILSAKKAGCKEFWLTAQDCGCYGLNAEADKKGNGLPELLKSIVSIVPGKYWLRVGMLNPRHLKKICPELIEAYKDEHIFKFLHLPVQSGSNATLEKMKRGYTVKDFKKIVSAFERELPSLQLWTDVIVGFPGETDEDFFATYELI... | Cofactor: Binds 1 or 2 [4Fe-4S] cluster. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the methylthiolation of N6-threonylcarbamoyladenosine (t(6)A), leading to the formation of 2-methylthio-N6-threonylcarbamoyladenosine (ms(2)t(6)A) at position 37 in tRNAs... |
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