ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
|---|---|---|
R6H008 | MKNRKSGLTAVVTLFLITAVMAGLLALVNSVTAGPIAAAQREKTERALSGVLREGVELGEQLESFPDETGLVEGVYKTSDGYVVEVTPSGYGGEIHMVVGVDGACTVTGIQIVTHSETASLGANAAADNVAGRSFREQFLGAGDQLAVTKDGGSIDALTGATMTSRAVTQGVNAALACAAALEGGSLQ | Function: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane.
EC: 7.-.-.-
Subcellular Location: Cell membrane
Sequence Length: 188
Sequence Mass (Da): 18985
Location Topology: Single-pass membrane protein
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A0A6I8PN26 | MNVGTAHSEVNPNTRVMNSRGIWLSYVLAIGLLHVVLLSIPFFSVAVVWTLTNLIHNMGMYIFLHTVKGTPFETPDQGKARLLTHWEQMDYGVQFTASRKFLTITPIVLYFLTSFYTKYDRFHFIVNTVSLMSVLIPKLPQLHGVRIFGINKY | Function: Negative regulator of sphingolipid synthesis.
Subcellular Location: Membrane
Sequence Length: 153
Sequence Mass (Da): 17565
Location Topology: Multi-pass membrane protein
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A0A933Q1R3 | MFSYRDGQLYCEDTALAGLTKDYPTPFYVYSRKVIKERIATLKDLFAPVDAVLAYAVKVNNNLSILNVIAGEGLGADIISRGELYRYLKAGGDPKKVVFSGVAKTEEELRYAIERGIRLINTESIPEIAAINSIAADYGRKVDIAIRINPDVAADTHHKITTGKKGNKFGVSFETVKKNAAMIRGLTNVRLTGIAMHLGSQIMKAKPYYDAIMKAKDVLTWLKGEGFAVTSLDIGGGIGVPYKKGDAPFDFETYKRDVIPLLASLGVTIIVEPGRYLVAESAALIMKVIYIKEEGEKIFVAVDAGMNDFQRVALYDAHHE... | Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; L-lysine from DL-2,6-diaminopimelate: step 1/1.
Function: Specifically catalyzes the decarboxylation of meso-diaminopimelate (meso-DAP) to L-lysine.
EC: 4.1.1.20
Catalytic Activity: H(+) + meso-2,6-diaminoheptanedioate = CO2 + L-lysine
Sequence Le... |
A0A4R3N276 | MAGRIPPEFIDNLLARTDIVDLIGSRIQLRKAGKDYQALCPFHDEKTPSFTVSPSKQFYHCFGCGAHGTAIGFLMDHDHLPFREAVEELAQRAGLEVPTDGEVVQAGPDYAPLYQLLEQAAALYRQQWREHPQAARAVEYLKTRGLTGEIAARYELGFAPPGYDFLLSRLGRSATERERLMTCGLLAEQDGRHYDRFRERIIFPIRDRRGRVIGFGGRLIGEGKPKYLNSPETPVFHKGRELYGLFEARQANRRLTSLLVVEGYLDVIALAQFGVTNAVATLGTATTADHLQQLLRTAPEIIFCFDGDRAGREAAWKALE... | Cofactor: Binds 1 zinc ion per monomer.
Function: RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.
EC: 2.7.7.101
Catalytic Activity: ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.
Sequence Length: 583
Domain: Contains an N-termi... |
A0A9E7KVY2 | MITSFPILALSIIGILTTSIVLLSYYAFVTKCCLNWHRSGFLGRRPAPSTAFSTSADNLGLDESTMQAIPTFRYRKRAESAWRSSPFRECAVCLSEFQEEERVRLLPSCFHVFHIDCIDTWLQTSANCPLCRSSITAPVPPDHYDPYHSNDEAMEEEVGRIIMILTTPIQ | 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: Membrane
Sequence Length: ... |
A0A0A8UMJ1 | MEFFNPNSKIDFMGARKWTALMSALIFVVSIGALFINGLKWGLDFTGGTQIEVSYPNAANLEGIRENLYKAGFKEAQVISYGTSKDVLISIAPRADVDQTALVDKVMEQLPGATKQRVDFVGPQVGQELATKGALAVIVSLLATMIYIGMRFEYRLAVSSAVALIHDPVLILGVFAMFGIEFDLKALAGLLAVIGYSLNDTIVVFDRVRENFVKIRRATSLEIMNISINQTLSRTIMTSMLTLFVVVALFVYGGETIRGFSLALIIGIVVGTYSSIYVAGALAVAMGLDRKDFLPSQRKEVDDRP | Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA.
Subcellular Location: Cell membrane
Sequence Length: 305
Sequence Mass (Da): 33267
Location... |
A0A6I8NRS5 | MAASGTSASSLRSKDGGSKRWEEFEDMLEERRQSSDLRYALKCYAPVLYKGLNPCKPWAIKTAVLRAEEVQYVVKQLSRETGQSVQSIQETAAQILEEMGHSLRLGAIRLFAFSLSKIFKCLFRKVCVNQDGIQRLQQAIQEQPVVLLPSHRSYVDFLLLSYILYTYDLPVPVIAAGVDFLGMKVMGELLRRAGAFFMRRSFGGDKLYWAVFSEYVKTMLRNGYAPIEFFLEGTRSRTAKTLTPKLGLLNIVMEPFFKREVFDTYLVPISISYDRILEEALYSRELLGVPKPKESTAGLLKARQVLCQDFGCIHVYFAAP... | Pathway: Membrane lipid metabolism; glycerophospholipid metabolism.
Catalytic Activity: an acyl-CoA + dihydroxyacetone phosphate = a 1-acylglycerone 3-phosphate + CoA
EC: 2.3.1.42
Subcellular Location: Peroxisome membrane
Sequence Length: 672
Sequence Mass (Da): 74751
Location Topology: Peripheral membrane protein
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A0A1V6EQI2 | MTNSNQDIPEDHSGPDELSKGGEAELRRHRLAKMERFRERGDDPYKYLYERTHTIQEARSAFEDLEARTAQEELQPLPASLAGRIVARRIQGKSTFMDIRDECGRIQVFLGQKQVGETAYEASKDLDIGDFIGVKGGIKRTHRNEITLFAEEYGLLSKSLRAAAEKYHGLSDVETRYRRRYLDLVANPEVMDIFRKRIRMIDAMRGWLLNHGFLEVETPMLHPIPGGATARPFITHHNTYDADFYLRVAPELYLKKLLVGGFEKVFEINRCFRNEGVDGRHNPEFTTMELYEAYQDYRGLMDETEDMLTHVIETVVGSRQ... | Cofactor: Binds 3 Mg(2+) ions per subunit.
Catalytic Activity: ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-tRNA(Lys)
EC: 6.1.1.6
Subcellular Location: Cytoplasm
Sequence Length: 514
Sequence Mass (Da): 58708
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A0A368V8M0 | MTIKQFSQRPGISINRDSKTASALVWAPFAKTVALEINSTKKIGLSQSTGGYWEGHDLPLSPGDRYRCVIDDEALPDPASLSQPAGVHAPSEVIDLYQHPWDDQNWSGIRPEKLIIYELHVGTFNQEGTFSEIIPHLNRLRELGINAIELMPVAQFPGIRNWGYDGVFPYAVQNSYGGAGMLQLLVDECHKQGIAVILDVVYNHLGPEGNYLNKFGPYFTSKYKTPWGDAINFDDAFSDGVRHFFLENAMMWLRDFHIDGLRLDAVHAIKDFGARHFLAELKQKVEELNAEYHRNHFLIAECDLNDVRYINPFDKGGYNL... | Pathway: Glycan biosynthesis; trehalose biosynthesis.
Catalytic Activity: hydrolysis of (1->4)-alpha-D-glucosidic linkage in 4-alpha-D-[(1->4)-alpha-D-glucanosyl]n trehalose to yield trehalose and (1->4)-alpha-D-glucan.
EC: 3.2.1.141
Subcellular Location: Cytoplasm
Sequence Length: 605
Sequence Mass (Da): 68671
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A0A059X711 | DAGVRLPHLAKYAASIGLSGLEFAVGIPGTVGGGAVMNAGAHGSSISEITESVTVFDTTLWKVVTLTLDDLKFEYRRSAIDPDKHIVLSSRYRMKSDVAENIQARTKHNEEYRWKTQPLGWPNAGSTFKNPEPTRSAGFLLDQAGAKDLRIGNAGVSAIHANFVINLGGATSGEITSLLRSMQDIVHEKFDLRMHPEWKRLGKFTDEELKVWS | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation.
Catalytic Activity: NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
EC: 1.3.1.98
Subcellular Location: Cytoplasm
Sequence Length: 213
Sequence Mass (Da): 23349
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K1YL47 | MNKKTSKNKNNICIDVICGGQSAEHDVSILSAISIINGLLELKNANKIFIIYITQKGEWFRTDVPLKQTPDESFIRTLTKKGNYVSPSVDPNNKVYFGKNKTYELPDLYFPVLHGTKGEDGTIQGLFRLMSIPYVGSDVTGGSCGMDKEVMRRIFQSLKLSLLPWISFNKDEWENNQKLCINNILEKLKYPVFVKPANLGSSIGISKAKNHNNLIKAVNLAFIYDYKIVIEQGINAREIECAVLGNLTPQASEPGEIFPGAEFYDYDDKYLSTNSSNKIPADISPSLKKKIQRDAITAFLGVNAKGLSRVDFFICKETSK... | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation.
EC: 6.3.2.4
Subcellular Location: Cytoplasm
Catalytic Activity: ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) + phosphate
Sequence Length: 374
Sequence Mass (Da): 42... |
A0A6P3E132 | MDEVNYFMNVTGPEHWIIFDFETTDFIWNVLIWMRNYWWKCFYYTAIYLVVIFTGKLYMSNRPKFDLRNALALWSGLLAIFSIIGTIRTMPELFHILYNHGFYYSICSNSYYTHDNVCAFWSSLFALSKIVELGDTVFIVLRKQPLIFLHWYHHITVIYFTWYSYALLMGTSRWYIVMNYFVHSWMYSYYALKAMEIKPPRFIAMMITTMQLVQMVVGFFVTGAAYYYIKIGEKQCHATTFNAACGLVMYFSYFVLFAMYFYKAYLSGNSRTKVE | Catalytic Activity: a very-long-chain acyl-CoA + H(+) + malonyl-CoA = a very-long-chain 3-oxoacyl-CoA + CO2 + CoA
EC: 2.3.1.199
Subcellular Location: Membrane
Sequence Length: 275
Sequence Mass (Da): 32928
Location Topology: Multi-pass membrane protein
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A0A972MCC7 | MANKDLKIIWTKIDEAPALATYSLLPIVNAFTKAAGVVVETKDISLAGRIIANFPDNLTEEQKIPDYLAELGALTQKPEANIIKLPNISASIPQLQAAIKELQEKGYDLPEYPENPQTEEEKALVKRFAKVLGSAVNPVLREGNSDRRSAPSVKRDAQKNPHKMMKPWKENSKTKVSYMNEGDFYGNEKSVITEKGTKFKIELTDKNGNKTILADNLESLDGEVLDATFMSIKKLREFYANQIKDAKDNDVLLSLHLKATMMKVSDPVLFGHAVAVYYKDVLEKHADTIKKLGVNLNNGIEDLYTRIQQLPEAEKNEIEN... | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
EC: 1.1.1.42
Catalytic Activity: D-threo-isocitrate + NADP(+) = 2-oxoglutarate + CO2 + NADPH
Sequence Length: 744
Sequence Mass (Da): 82817
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A0A7J4V8A0 | IMLLRPEQEKSYFKEKPQAKFLAIVIGLLMFAQIIYAVFFAATGKVVDEARRVEIGTIEHIGRELYTTYLLPFESIAFVLLTATIGALVLSKKKLD | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy i... |
K2F4A7 | MQKRKIFIEIGIPSKLRKKLTEKVEKLRELPVKWTKPENLHITLMFLGYVDESVIPEICLKVSQTASEAESFDLSFDKIELGPNPDKAQMIWFSGEANDDLKNLYQEIEKELGIFHIEKKLFRPHITLGKIKKEKWEALKEAPVIQEEFKTFVPVENIFVMGSVSGQEYEVIEDCPLG | Function: Hydrolyzes RNA 2',3'-cyclic phosphodiester to an RNA 2'-phosphomonoester.
EC: 3.1.4.58
Catalytic Activity: a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + H2O = a 3'-end 2'-phospho-ribonucleotide-RNA + H(+)
Sequence Length: 178
Sequence Mass (Da): 20608
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A0A7V1EDS4 | MSEDYQSTTVTSLTDKRPPQNLEAEKACLGSMLLDKEAIEAAIEVLTEDDFYSSQHRIIYSAILQLYNSATPVDIVTLTDSLKFGEDLDKAGGVVNISSLLDEVPTSANIEYYARIIEQKSLLRKLIKAASEVISISYNPDMDVYEIIDEAEKLIFDVAERRASKKNKYYMMSEIIKDSIIAIEKLYHRGDVYTGIPSGYKEFDDLTSGFQNSELIIIAARPSVGKTAFALNIAQNIGIRQKKNVAIFSLEMSKEALVQRMLCSEARIDSQKLRKGFLETEKWAPLTTAAGKLADANIFIDETPGINDMQLRAKARRIQS... | Function: Participates in initiation and elongation during chromosome replication; it exhibits DNA-dependent ATPase activity.
EC: 3.6.4.12
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 465
Sequence Mass (Da): 52581
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A0A931DKH2 | MRASSDTARGLLLGVALDAVLGDPRRGHPVAAFGRVASALEKVLYADSRSRGVLYAGVLVGGAAGAGAVVERLTRGRPAWRTGATAVATWAVLGGTSLGREGRVMARLLEEGDLEGARGRLSHLCARDPAGLDAAALARATVESVAENTSDAAVAPLLWGLVGGVPGLLAYRAANTLDAMVGYRSPRYERFGWAAARLDDVLNWVPSRVTGLLVVVCSGRSEAWRVLMRDGGNHPSPNAGRCEAAFAGALGVRLGGANAYGGRVERRPEMGDGRAPEVRDIRRAVRLSAMVTWAAGALCAR | 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: 301
Sequence Mass (Da): 31315
Location Topology: Multi-pass membrane protein
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A0A496RBN1 | RTLQSIPKNVSIKVMNIILFESEKLPVLLPMGDDRAQHIVKILKLKEGDSFKCGLVNGPSGICSIKGINAEGIVLSWEKKAEKKELYPLTLVVGYTRPISAKRILRETVSLGVAKLVFTGTDTGEKSYRSSNLWKTGEYKRYLIDGAQQAGQTAVPPVLFYPDIKHTLQAVTAGSCSDLLLLDNVSPAGSLSAYNPGMSGGTGPVVLAIGSERGWSDRERLLFSGYGFTAMKLGERILRTETACSAGTAVLLSRLGYV | Function: Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit.
Catalytic Activity: S-adenosyl-L-methionine + uridine(1498) in 16S rRNA = H(+) + N(3)-methyluridine(1498) in 16S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.193
S... |
A0A1F5BXB8 | MKRKLSKTSEFKKVFSEGRRIEGKNLIIFVLKNDYDFNRLGIIVKKEIGKAVVRNKIKRRLKETSRLLNKKLLPGYDIIVMAKNNIREASYFELYYDLEGLLYKEKLFL | Function: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of... |
A0A930X6C2 | MPSLHRLIGACYRKTDALLRPVLFRREKSLVLRRYPALKPVMEAFEARYVRVEYGAHDLSLMERIQRQMTDKDEFVYGTTPWHTFLKIADALNVQPEDVFIEPGCGTGHLCFLMNQIYGVEAIGIETIANFIQTAKTLQKELAEAPHHLLSDKLRFYNLDFFTSDFSRGTIFYVAGTCFPDDYRERLYQKIAREAPEGARLITLTHAIEHPAFALHDQVAGVFSWGRDKALIYTKHKKG | Catalytic Activity: L-lysyl(79)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl(79)-[histone H3] + 3 S-adenosyl-L-homocysteine
EC: 2.1.1.360
Subcellular Location: Nucleus
Sequence Length: 239
Sequence Mass (Da): 27514
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K2FAC0 | MATALYRKYRPLTFSDVIGQGHIVQTLSNAILNNRVGHAYLFTGPRGTGKTTMARIFARAVNCQNPKGADPCLECDVCKNITQGMSLDIFEIDAASNTGVDNIRELRENVKFPPSQAKFKVYIIDEVHMLSTGAFNALLKTLEEPPAHVIFILATTEIHKVPETIISRCQRYDFTRLSLEHIIEKLSTIAKNENVSIEKNALEMIAIASEGGMRDAESLLSQVMALEDKKITAKEVEEILGTTQRQSLE | 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: 249
Seq... |
B4CUD9 | MGCNGELSASASALSVLILILLFPLRGGIKIKSKITIKSLPPVLSPAMLSLAEARSIIEQHVQPLEPQAVPLAAARGRVLREDALAPDDLPAFDRSAMDGYAIDAKDASPKFRVVMEVQAGQVPTRRLHPGECARIFTGAPIPEGASQVIMQEDVERDGEWMTVRERDTKMWIRYRGEDARKGELLLAAGARLQAGELSLLAQLGMVRPRVGRAPRVLHFATGNEIVDPSLTPAHGQIRDSNSTLIAALLADAGVQLMAQNRCGDDLDDLVGAIRQHTAESWDCLLISGGASVGDYDFGARALRELGFTIHFPQMNIRPG... | Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
Function: Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP.
EC: 2.10.1.1
Catalytic Activity: adenylyl-molybdopterin + H(+) + molybdate = AMP + H2O + Mo-molybdopterin
Sequence Length: 445
Sequence Mass (Da):... |
A0A7V1H6W8 | MGSRQSGAAHSALFFCGKNNFNNCEQSMAENCVKLERVTKHFPGCCAIDDLSLSIAEGEFYSLLGPSGCGKTTTLRVIAGFEQPTSGKVYLDNDMVNGVPPNLRNVNTVFQNYAIFPHLNVYENVAYPLRIKKVPKDEIARRVKESLDMVSMQGFDDRFSIQLSGGQRQRIALARALILKPRVLLLDEPLGALDLQLRQQMQGVLKRLQHELGITFIYVTHDQGEALTMSDQIAVMYEGKLQQVGTPKEIYEAPANRFVAQFIGKTNFIEAVFDKKKSDSATVRIDSFIIRCAVKDFFEEQKSVCISIRPERVVIAEKLK... | Function: Part of the ABC transporter complex PotABCD involved in spermidine/putrescine import. Responsible for energy coupling to the transport system.
EC: 7.6.2.11
Catalytic Activity: ATP + H2O + polyamine-[polyamine-binding protein]Side 1 = ADP + phosphate + polyamineSide 2 + [polyamine-binding protein]Side 1.
Seque... |
A0A4R1F991 | MAKVKSDKTFFHGKSESTGVLLINLGTPQEPTKSSVRSFLKQFLSDGRVIEIPKLVWLPILYGFILPRRPEASARNYKKVWMDEGSPLMHYSLRQQKLLQKEMESRFSGPVHIELAMRYGDPDIQAGIDKLQEKGVRRVLILPLYPQYSATTTATSFDEIFKVFSARRWIPELRFVAQYHDHPSYINALAESVKDFWKTNKRSEVLLMSFHGLPKRNLELGDPYFCHCHKTGRLLAEKLDLKESEWKLTFQSRFGKAEWLKPYTDKTLSEMPAEGIKSVDVVCPGFPSDCIETLEEINMENRGYFMEAGGQDYQYIPALN... | Pathway: Porphyrin-containing compound metabolism; protoheme biosynthesis; protoheme from protoporphyrin-IX: step 1/1.
Function: Catalyzes the ferrous insertion into protoporphyrin IX.
Catalytic Activity: 2 H(+) + heme b = Fe(2+) + protoporphyrin IX
EC: 4.98.1.1
Subcellular Location: Cytoplasm
Sequence Length: 370
Sequ... |
A0A1I7Y549 | RNLPNYEDPQQRLLAATYPSPDGPVRVICAYCPNGQSLESEKYTYKLEWFAALHDWLEKELQQYPRLAILGDYNIAPADQDVHDPAKWVGDVLVSPPERAAFERLLALGLHDAYRLFEQSGSPFTWWDYRRFAFRRDAGLRIDHALLSDALKARCTACDIDREPRANEQPSDHAPQTDSGYVLEITLEQEHKIWAYLAISEPDLDAVANIVPPEQFEAGGDVHVMAIAQADDAAQEVQEVLFSMTPNDTVVFLCADPASVQA | Cofactor: Probably binds two magnesium or manganese ions per subunit.
EC: 3.1.-.-
Catalytic Activity: Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Length: 262
Sequence Mass (Da): 29484
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R6HZT1 | MVERRFPLFVNLAGRKVLLFGGGPVALRRARTLVAFGPDLTVIAPEPDPAFLSLPVRLERRAYRPGELRGAFLVLAATDDEEVNRAIAAEARARGALANNASDCRDCDFFFPAVVLTEELTLGLTGTGENHRAVKEAAARIREMAL | Pathway: Porphyrin-containing compound metabolism; siroheme biosynthesis; sirohydrochlorin from precorrin-2: step 1/1.
EC: 1.3.1.76
Catalytic Activity: NAD(+) + precorrin-2 = 2 H(+) + NADH + sirohydrochlorin
Sequence Length: 146
Sequence Mass (Da): 15873
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K2BN56 | MSDSNMLLTLLNKGVVDAIVKDDLEKKLKSGKKLRIKLGIDPSGADLHVGHMVVIKKLKEFQDLGHHILLLFGNFTGQIGDPTGKSETRAPKTQEQLEKNAQHYLKQVGKILDVKKVEVVWNADWLASMTFQDVIKLATHFTVAQMLERDMFQERIANNQPISMHEFFYPLMQGYDSVALKADVEIGGTDQTFNLLAGRILQKAYGQEPQNILTVPILEGLDGKKKMGKSENNYIGVNESPKEIYGKTMSIPDNLIVKYFELATDESMEEIVAIKKQLDDGANPRDLKMRLARDIVALYHDEKSAKEAEEEFINIFRNKQ... | Function: Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr).
Catalytic Activity: ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + H(+) + L-tyrosyl-tRNA(Tyr)
EC: 6.1.1.1
Subcellular Location... |
A0A972R393 | MTIYAVGINHHTAPVEIRERFALSDDEISTALRTLHDGILKEAFILSTCNRTELYGVPHDDVETDGYVLQDFLRNLKPEIKVEDRYFFKYFTCGAASHLFNVAASIDSQVLGDVQILKQIKDAYELSLKEGASDTILNTLLHYALRVGKRVRAETSLGIGAISISYAAVQLAGRIFDNLEQKRTLLIGMGETGLLTARHFADRGVRKFMFTNRTRKRAEEIAPKFGAEVVDFSAFPDALREADVVVTATSSPDILITKAMIKSCMKGRYNRPLLVLDISVPRNVDPGAGSVGNVFLNDIDALQGIVDHNISKRKEELPKA... | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2.
Function: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
EC: 1.2.1.70
Catalytic Activity: (S)-4-amino-5-oxopentanoate + NADP(+) + tR... |
A0A933V0I6 | MIIAYIPMLPEIVLVAGALVLFIITLGKRRDALAKNATRVILITATVAAVGTLHAHGSFFYSAYRVDLFSQLMKLILLAAAAMVLYQGRSLRGIDEDVRPEWYFFFSVSTLGLLLLVSSVEFITLFVALELASCTMYLMVPLRNEIGDMREHMEAAVKYVMFGIASTGIMLFGVSYLFGLTGTTALYDMLAHLKETGPEPVVIVAVSLVSAGLLFKLAAVPFHFWIADVYQGASNETAAFIAAVPKLGALAVLLRIAAIAVSAGGMMTTIIAVIAALSMFVGNLSALVQKDVKRLIGFSGIAHAGYLLAGVATMGQDGFA... | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ... |
A0A7C2PVY6 | IKVNSIVQQETLGYTSKEPRWAISYKFPATQMTTRINDIILSVGRLGNVTPIAVLEPIFLAGTTVTRASLHNFDEIARKDVRIGDTAFVEKGGEIIPQVVSIVESRRETGSTPYPVPSHCPECNSLLVKDEEVALKCVNPSCHAQVKRQIEYFASKNAMDIEGLGESIVEQFIKKGFLKDYGDIYYLNKEEIADLEGFGEKSALNLIQSIERSKKAPLHRLISGLGIKHIGSKAARILAETFHSIQNIQSKELDELVEVPEIGPIMAESVTQFFKEPINLEVLSKLEKAGVGFEENPSDSPSVGKDNFFTGKRFVLTGNL... | Function: DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA.
EC: 6.5.1.2
Catalytic Activity: NAD(+) + (deo... |
K8Z8D0 | MEETQITGQVLRIVFQRGDYAIASVRIIGTPPTHLEQRTMVVGTLPELVESETYDFIGHVVEHPTYGWQWQVESFHLHEPDEVEHLVEYFSSERFTGVGKKTAESIIETLGKDAIAKIKEDPSCLDEVPKLRQKQKEVLIKEVQAHYGKDQILLELRNLGLSGPQAEKIYKKEKQRSLAVIQKNPYQLLKMDLRISFDKVDHIARELGIEATDQRRLQAGVEMVLQLHCYRSGDTYLDLRSLLETAQKELEKGQSEPIDIALIQEAISDLLKERKLYFVKEEESQVYLPTFFDAETSIVFALQRLAEAPVPYSEDEIDQA... | Function: DNA-dependent ATPase and ATP-dependent 5'-3' DNA helicase. Has no activity on blunt DNA or DNA with 3'-overhangs, requires at least 10 bases of 5'-ssDNA for helicase activity.
EC: 3.6.4.12
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 803
Sequence Mass (Da): 91217
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A0A933UXP7 | MTHDEIIIGHFEGRLFAWQGDYVRKILEHIVPIPVFTRSIAPENRDDLVKVASHIYTNSFSIDLHFHTTIIDAAIRSGEIDCAVVPLEILPEELPYPLTLAGVVGRVQHREVLISRDKVPFAKLPPGASVGVYSLRQVVQLKHIRGDLSYVIVPPDAETLLSVTGMKDLAAVVYPESDVKRLSYDALITETFSEEMILPALRQSAFGCVTHRENSAVISAMQHVTDAATLRTTRCEEGFMHDFNPPFDAPLAGRASVNGDELRFSVRSIDEITLRVFEDEYTSIGDTDAYAFGRECARRFEQKGGRTPIKRGKAG | Function: Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
EC: 2.5.1.61
Catalytic Activity: H2O + 4 porphobilinogen = hydroxymethylbilane + 4 NH4(+)
Sequence Length: 315
Sequence Mass (Da): 35062
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A0A9E7FEQ6 | MLVVGQVKVSQGNPLVTCLLEGPSGSGKTAMTATIGIETDFPFVKFLTCKNMLVIGTAKEVSFLESLVLRVLSGIVYRDAGQAVPHQINLAIMLVFLKALQNEELKSHRTPTGSRYGLLHSKQPWDVRSTQQRR | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Required for vesicle-mediated transport. Catalyzes the fusion of transport vesicles within the Golgi cisternae. Is also required for transport from the endoplasmic reticulum to the Golgi stack. Seems to function as a fusion protein required for the delivery of cargo p... |
A0A930X7S8 | MPQLTLFNTLSRNKEAFVPLTPGQVKMYTCGPTVYNYAHIGNLRSYIFPDLLKKLLLQLGYSVQHIINFTDVGHLTSDEDLGDDKVEKAAARLGKSAWEISRFYAEAFQQDLQALNIAFPTRFTYATEYIPQQIALLEQLEAKGLSYTLPDGVYYDTASFADYGQLARLDIEGLNEGARVSAEGKQHKTDFALWKFSPADQQRQMEWESPWGKGFPGWHLECTAMIFAELGQTIDIHTGGTDHIPVHHTNEIAQAEGATGQKFVNYWLHGEFLVLDQERRMGKSEGNFITLQTLLDQGFSARAYRYLALTAHYRHFLTFS... | Cofactor: Binds 1 zinc ion per subunit.
Catalytic Activity: ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-cysteinyl-tRNA(Cys)
EC: 6.1.1.16
Subcellular Location: Cytoplasm
Sequence Length: 472
Sequence Mass (Da): 52896
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A0A7V3VV16 | MTVLFWGSSDFSIPALELIYNKYRILSVITNPDTPFGRNLKEIHHTPVKLFAVEKGIPVLQPEDLKDASFQQKVKSIKADISVVVSYGFIIPENLLNISPCGFINLHASLLPKYRGASPIQASLLNGDSVTGVTIQYLSKELDKGDIILQREVNILENDNYITLSKRLSEEGAHLLIEAIELISKGKAERKAQDEKLATMTHRIKKEDGFISFSLMSAKEIFNRWRAYYSWPGIYSMYKNSSASGEKKENSLTISLLEIEKQDRDASTEPGKIIQSDKKALIVKCKEGGIRILKLKPWGKKEMDYISFINGYKPVTGNYW | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
EC: 2.1.2.9
Catalytic Acti... |
K2E8Z0 | MIDFKIAKPEGIVYEGEVERITIPTLSGEITVLENHAPLVSVLDTGEMIVHVSNKETVSISISGGILEIRPDSKVYIMADSAEKSEEIDIERAEEAKNRAQEMLEKEKNLADVDFARLQAIIEKEMNRIHIAKKYRK | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane.
Subcellular Location: Cell membrane
Sequence Length: 137
Sequence Mass (Da): 15451
Location Topology: Peripheral membrane protein
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A0A7C4X6B6 | MKSLYLIDAYAIIYRSYFAFIRAPLRAPDGSNVSSVFGFLKTMFQLWDTYEPKHCAVVFDSRIPTFRHVKYPEYKATRQKAPDDLHAQVPVIEELITQLGIPCLRADGYEADDIIATLSAACTQDKILCRIVSGDKDLLQLVNEYTHVLRPDKDNGFIEVDAREVEALWGVRADQILDYLSLTGDASDNVPGVAGIGEKTAQKLIAQFGSLDAIINNAELIKPDSLKAKILAGLESAKLSRELITLHMDVPGISKDIAMYAVQGLNHDAIYNTLVRLNMKSLIRSEKKSPTISAGELFTSFEPNTTTFREAPASNMQALS... | Function: In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity.
EC: 2.7.7.7
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Length: 953
Sequence Mass (Da): 105803
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A0A947QH86 | MRGRGRYIAITAIAFAANFGLDRVTKALAVAFLSGRRALSFLFDTVRIGLAENTGAFLSLGAGWPPAVKYTALLVAPGLLCLYGLFHCAFKETDRMRAALLATIIAGGAGNLVDRALNGFAVVDFLNFGIGSLRTGVLNVADLSITFGAVAFLLHERTSAQRDAPGGKAP | 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-, ... |
A0A2H6GPH1 | MSDLNPVFDNYLKAVHEREARGIPPLPLSDEETQAVCEALQSDSLDSRAMVKPGLEDTAQTLLYMLRERVSPGVTDSSYVKAEFLGGILNGEKISRYISPLDAVEMLGQMGGGANIPFMVEALDAGKDLAAAAAKALSLTILISPLMITKIAELASDGNPFAQNILRSWAEARWFENMPPVPQKVDCVIIRTSGEINTDFLSPAQEAITRDDIPFHALSMLSTSPDDTDFLQRLEGIRKENPGVPILFAGDVVGTGSSRKSASNSLVWWIGNDIPHTPNKRRGGIVMASKIAPIFFNTLRGCGAIPVRCQSGNLLEGKIV... | Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate from oxaloacetate: step 2/2.
EC: 4.2.1.3
Catalytic Activity: citrate = D-threo-isocitrate
Sequence Length: 864
Sequence Mass (Da): 93595
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A0A1F2UHF1 | MAIRKEELGRDERAQAWYKKPIEDIFKELSTGVDGLSQAEAQVRIERYGLNKLVEDEKVPAWQTVLHQFKDPLIYILLIAATITILLQDYIDAGVIIAVVVLNAIIGFVQEYKAEESIRSLKKLLALKAFVVRDGHEQDLDAELIVPGDIISLQSGQKVPADIRLYSVKEFQIDESAFTGESIPVSKSSEPIPREDLQAFEQTNIVFMGSIVTTGRATGVAVNTGRSTQLGQISAAVKAVGTIKTPLQGRIEALSRLIILIVAGFSVAGLVIGLAQGEDIVQLLLTMIAMAVSAVPEGLPVALTIALAVAVNRMARQKAI... | Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Subcellular Location: Cell membrane
Sequence Length: 913
Sequence Mass (Da): 99142
Location Topology: Multi-pass membrane protein
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A0A316ZB43 | MSLALADEVRLVRAALDARERAYAPYSKFRVGAALLLDDGSLVPGANVENASYGAGICAERTALCSWRVSAATPARIVAVGVASDIVASPCPPCGICRQFLREFVALSTPIYMPLAGWKEGDKVEVRTLEQLLPLSFGPDDLDKQK | Function: This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis.
EC: 3.5.4.5
Catalytic Activity: 2'-deoxycytidine + H(+) + H2O = 2'-deoxyuridine + NH4(+)
Sequence Length: 146
Sequence Mass (Da): 15609
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A0A660TNA8 | MENNITLKDSFIEKIDNYSLKHKLISLNDKILCAVSGGPDSVALFYVMLTLMERYKIELSVAHLEHGIRDKESLRDQEFVKSLCKRFDIPFYTKNVRISDFKKSRESIEEGARRIRLDFLKDTCEKIKYNKIATGHTFDDHIETVIFRLINGTGQKGIRGIRVSSDGIIRPLLCVTKREILDFLERHSISYMEDLTNYDVHYTRNRIRYRVIPEIKEINARYREHINNFVKLISEDDTFIEQLVDDYMNGIVRKISNSELRILSEKFYNFPPPIKKRIILRAVNNIGDFIRKFGLKNSIYLPYNVINSITEKKPQSNKIL... | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34)... |
A0A660T324 | MVKAKNSLSALGRKIFLDRYALKDGKKDTLAIDDIVVVVVNKATGQREIGKVSDIDGNNVTVELEDGTKQTLPVEQLDKPLETDPSQMIKRVATALGDGEKEEVRDKWVNNFKWLLDDWRFVPAGRILTGAGTDQNLTFYNCYVIPSPSDSRGGIMETLGHMTEIMSRGGGVGINLSSLRPHHAYVKGVNGRSSGSVSWGALYSYVTGLIEQGGSRRGALMLILNDSHPDIMNFISSKREMGQITNANISVAVSDAFMEAVKENSDWDLVFPDTNDPDYDKIWKGDLTAWKKAGKSVITYKTVKAREIWGSIIESAWSSA... | Function: Catalyzes the reduction of ribonucleotides to deoxyribonucleotides. May function to provide a pool of deoxyribonucleotide precursors for DNA repair during oxygen limitation and/or for immediate growth after restoration of oxygen.
EC: 1.17.4.1
Catalytic Activity: [thioredoxin]-disulfide + a 2'-deoxyribonucleos... |
A0A6P3DXJ5 | MYVKVRTMDGKQEAILTISKLTEVEEFKREIEKELNIKVDLQRLFFRGKQLENGYKLYDYNVNLNDVIQLMVKIQINEVESQATSSTKVTSSSIIKEEIVDNSSKEEKLSEAESLYYKVGDAVDCLDQTYGAWFEAIILKIFKRDDNIIYNMQWEFDDKAPAFNVPESSVRPRARRLLKFDSLKIGQKVMINHNVDDPKVTGLWYDFTILKIDKKKRVQELIGILHIGKDQPLENRKVNPKGEIFAIEEPKFLTDRSPEDEQHMVSSGKRRRIQAYCDACLDNPNKECRECGCRVCAGKEDEHNLLLCDECNSAYHLSCL... | 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: 7... |
A0A930X4Z4 | MHLILASGSPRRHELLQQLAPAFEIQVSDIEEHLNASLPSLGEQVADLARQKALAVAEQQPLSTPVCVLGADTIVCIDHQILGKPRDAEDAARMLNQLSGRWHEVITGVAVIQPRAGQATAEWPCWLDFEISRVLMHPIKASDCAEYIASGEPMDKAGAYAIQGGAGRFVAEFTGTYENIVGLPLELTRRLLQQAGYLQLL | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: H2O + UTP = diphosphate + H(+) + UMP
EC: 3.6.1.9
Subcellular Location: Cytoplasm
Seque... |
K2DP73 | MKKLLPIQYAKILYSLTKDIDKSDLDKAVSEFFQFLKKERILLKTDSILKAFVKYSKEQEGIRFLKIKSAKKLSDAQMKEIVTSFGKNVEVESFVDESLIGGVVVQEGNTVLDGSIKTQLKKLEHKLI | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
A0A2H5YVH2 | MERNVPAPLPAEQRLRRLKRIAILAPAAYMLLLLLGSQLLERLLPSPWAIRLAVIALVLIGIVIFAEWIFRIIARQQATLAQQNAELQALHEAGLAIAADLDLDKVLAQVVDQARRLIGARYGLLVMRDQVGMPPIVFASGLPADRECQLSEITSHGLLDQVLREGRTLRIDDLYLYPGERRFPEGHVTLRMLLGVPIRSGDTILGALYLADREDDTPYSPQDQLRLERFATQAALAITNARLHRRITSLAIAEERERIAREMHDSLAQVLGYVITKASAARELLGQAGRAGDAEQHLRQLEQAARDAYADVREGILGLR... | 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... |
A0A2A9DPY1 | MQQRNPRNQGPQKNRSSLSRPTLRPIPRVLKASRPAAAKSAKGSKPAWTPLTVEETIGRCRVFRDGVCMPTEFSPQGALNEVRDSGGFVWLDVHSPAEEHMEKIAEMFDIDELIVEDAVQAHQRPKVERYEDQLFFVLRTITYSDSEEVRNSRDIIQTGEVQMVVSKDFILTIHHGQPVPGLVDRLDRNMENEEHTPIALGWEVADHIVSEYNTIVDSLDDAVDSLEEDVFSPDSDLDIQPIYQLKREILEMRHAISPLGAALNVLIHQGDVVNEELRTYFRDVLDNQTIARDQVSQFDERLSSLIDAAVAKVSLQQNMD... | Function: Mediates influx of magnesium ions.
Subcellular Location: Membrane
Sequence Length: 381
Sequence Mass (Da): 43326
Location Topology: Multi-pass membrane protein
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A0A4P5UNB7 | MIRSGDHSLIIYALIIYSIGAITDYLDGLIARKWGNTSSFGSFLDPIADKVLTNAALLGLMAIGVIAPWIIIIIIGRDIFITLLRIYADRNGMPIITSTSAKIKTAIQLSSSILILLMLSLESGIQLIDSFGFVVDITMYVIAFLTLYTSVEYCFQNKQLLNHLFLEPRIPGLKSMIATCFGIGYSPFAPGTIASVMSILVTILPISHFQLQIATVIAIILAIPSIQYVETLHGDDSSVIVIDEVIGMWIILSMDFVVYTPAILVLALILFRLFDIFKPFPINIINRKKGAFWVLADDIVAALLTIIFLYIFMIIQIGSN... | Pathway: Phospholipid metabolism.
Subcellular Location: Membrane
Sequence Length: 325
Sequence Mass (Da): 35940
Location Topology: Multi-pass membrane protein
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A0A345UKV2 | MAAARITDHKKEEIRDTADIVDVVSDYVKLKKAGAAFTGLCPFHNEKTPSFYVTPRLGIFKCFGCGEGGDVFNFVMKMEGVGFVEAMRTLAARYNIELPEEESSDSADAQTQLIEGVYHALRFAGVYYHHTLTGEETAAAARDYVGQRGLNAATIRKWGIGYAPEGFDHFYRHAISSGINENYLHEAGLIKYSENNQQPYDTFRRRLMFPIFSPSGKVIGFGGRIMEGGKGPKYINSPQTKVYNKSEVIYGIHLSRNEIRRHDQSILVEGYMDVISLWQHGVPNVIATSGTSITPEQMRRLANYSSNLLMVYDADNAGQN... | Cofactor: Binds 1 zinc ion per monomer.
Function: RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.
EC: 2.7.7.101
Catalytic Activity: ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.
Sequence Length: 659
Domain: Contains an N-termi... |
A0A849K076 | MTFADAVTGSDGRPLDQIRLTGVTATGHHGVLPEERAEGQTFRADVVLHLDVRAAAGADDLAATVSYAEVAEDVHDVLCGPPVDLVETLAERIAAVVLEHPAVQAVDVRVHKPEAPIAVPFDDVEIVVRRDREHRPSVPALPAGSPVQVSSSGPAPEPAAPAVPPPPVPPQPVAGTPASAPVPVPSAAVPAPAPSPSAGSVPSASSVPTPAVSVPPAPEGPVAEAPVPAPRAPEPAVPEPSAAGSSPVAEVAIVEPEHVPAPAVDPLDAVPEAPVEAVIALGANLGDAQATLREAVTDIDRVSGVQVMEVSPLARTVAVG... | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 3/4.
Function: Catalyzes the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin.
Catalytic Activity: 7,8-dihydroneopterin = ... |
K1YPE2 | MAIKLAVIGAFGRMGKAICRLALKDATFELCGLIDALDQSKGQTYEQVTGLKTGDLMVVSDFDELKIQPEAIIDFSFHKATMLHLEKVAKKKKKIPYVIGTTGFSGDEVKTIKKYSKVMPLLLSPNMSLGVNILFLLTEVLTKSLGKSYDIEIIEGHHNQKADSPSGTALKILEVIKNNLNDDEYFTVNGRNGLVGKRKPKEIGMHAIRGGSIIGEHCVFFAGTDDEIRIEHRALNRDIFAKGALKCAEFLHKKTPGFYDMKAVLGLA | Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4.
Function: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.
Catalytic Activity: (S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydro... |
A0A496R7K6 | MAEEYLLEMEHIRKEFPGVLALNEVSLRVRSGTVHALMGENGAGKSTLMKVLLGIYRPEDGSIRFDGVTHEVMDIRKSLQYGISMIHQELSPIPYMTVAENIFLGREPVRGKTGWVKSKVQIQQTQELFDELDIDIDPSAKMVDLSIANMQMVEIATAISYNSKLIIMDEPTSAITEKEVAHLFRMINNLRDKGVAIIYITHKMDEVFQISDEVTILRDGTFVDSKLSSKIDKNGLISMMVGRELTDFFPKIDVEITDIKLEVRNLTLPGKFENVSFNVRRGEILGIAGLMGSGRTEVVESIFGIYPPASGQILIDDKEI... | Function: Part of an ABC transporter complex involved in carbohydrate import. Could be involved in ribose, galactose and/or methyl galactoside import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + D-galactose(out) + H2O = ADP + D-galactose(in) + H(+) + phosphate
EC: 7.5.2.11
Subcell... |
A0A972RUR9 | MIPISELDLIKIGEIAKAHGYKGELVIKLSTDFDNLIKTEHIFIEIDGIFVPFFFSYPPKPFKKSSAIVKFDNLDSDKEIKELIKCKILLPKENITHKINDENIFDTLDGYNVYDSDIFIGKAGEFLNIPSNPILTVFNDSNEILIPINDEFLVEIDSINKKIIFNLPEGLIDINS | 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 ... |
A0A1Q7X8L6 | MVSNPEFLREGSAVEDFFYPDRIVFGGADAEAEAVTEELYGPLVHQSFAGGRPEMAPIPVIHTTLQSAEMIKYAANAFLATKISFINEMANICERVGADVSEVARGIGLDRRIGQDFLQAGIGWGGSCFQKDLVALQRTGEEYGYTADLLTATVEVNRRQRLLVIQKLQAELKILKGKRIVLLGLSFKPHTDDLRDAPSLTIAQRLQAAGCKVLATDPVVQVLPEDLDGKIEIFSDPWDALRGADAAVLVTEWPELVGLDLAQMATLMRTPVLVDGRNAFAAAAARAAGLTYIPIGR | Pathway: Nucleotide-sugar biosynthesis; UDP-alpha-D-glucuronate biosynthesis; UDP-alpha-D-glucuronate from UDP-alpha-D-glucose: step 1/1.
EC: 1.1.1.22
Catalytic Activity: H2O + 2 NAD(+) + UDP-alpha-D-glucose = 3 H(+) + 2 NADH + UDP-alpha-D-glucuronate
Sequence Length: 297
Sequence Mass (Da): 32195
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A0A6I8PEQ3 | MWGWWARWPRLRLAVLLLLSGGGWSGWSGWSCWPGARAEGGPEAAAAAAAEEEQDPHAKHLYTGEMFSHGIESAAHFVMFFAPWCGHCQRLQPTWNELGDKYNKLENAKVYVAKVDCTADTEVCSAQGVRGYPTLKLFRPGQEAVKYQGSRDFQTLENWMLQTLSEEPSTPEPPVEPPKAPEPKQGLYELSAANFKLHTTTGNHFIKFFAPWCGHCKALAPTWEQLASIFEHSETVKIGKVDCTQHYELCSGNQVRGYPTLLWFKNGEKVDQYKGKRDLDSLKEYIDSQLQNADDAPEAPKPSEIPPEGAEPTQDEVNML... | Catalytic Activity: Catalyzes the rearrangement of -S-S- bonds in proteins.
EC: 5.3.4.1
Subcellular Location: Endoplasmic reticulum lumen
Sequence Length: 427
Sequence Mass (Da): 47928
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J0USU1 | MSNKPIADMIETIEHFAQTQPSYPVYNVLGQEHTYGDLKADSDSLAAVIDQLGLPEKSPVVVFGGQEYEMLATFVALTKSGHAYIPIDSHSALERVSAILEVAEPSLIIAISAFPLEQVSTPMINLAQVQEAFAQGNNYEITHPVKGDDNYYIIFTSGTTGKPKGVQISHDNLLSFTNWMITDKEFATPSRPQMLAQPPYSFDLSVMYWAPTLALGGTLFTLPSVITQDFKQLFAAIFSLPIAIWTSTPSFADMAMLSEYFNSEKMPGITHFYFDGEELTVKTAQKLRERFPNARIINAYGPTEATVALSAVAVTDEMLA... | Pathway: Cell wall biogenesis; lipoteichoic acid biosynthesis.
Function: Catalyzes the first step in the D-alanylation of lipoteichoic acid (LTA), the activation of D-alanine and its transfer onto the D-alanyl carrier protein (Dcp) DltC. In an ATP-dependent two-step reaction, forms a high energy D-alanyl-AMP intermedia... |
A0A1G1VZE4 | MAVLLNRQTGSDSTNRLPLVAIREGVVFPHTEQVLVFGRKKSVAGVTVAFETNRQVVFVTQKNSTISDPLPEHLYKIGTLSLIERTLKSDGEINAIVKGVSRVRIVNVETGGDYFQAEVSSLPEISEDSREVEAICKHLANEFKKAVNLGKSVEFLSFMKLMGDVKASELADQIASSLDIKTHEKQGLLEMLNVRERLEKTLDYLTHEIKVLEIERKIATKTQKKFDKSMREAVLRERMKTIQKELGEETEEDEEVKELKKKIIEAKMPKIAREKAEKELARLSQMSAHNPESGYIRTWLETIVDMPWSIRSENNVLMKS... | Function: ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield ... |
A0A345UMY2 | MGNFSRILAFDVGHKRTGLAQSDPMHIIASPIGAFGEGELFEKVAAIIAAGPVSHFVVGWPIGQQGQRGASTQRVEQFVKKLNKRFPGIEVTLVDERFTSVMAKQQMIDSGMKKKKRQQKGIVDATAACIILQEFLDQNSNTR | Function: Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
EC: 3.1.-.-
Subcellular Location: Cytoplasm
Sequence Length: 143
Sequence Mass (Da): 15699
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A0A7C5ILD4 | MRLVDLIKNVEISAIIGELNPDFEITSVINDSRKSNSRALFVAYSGYREDVHEFIPAAYEKGVQHFIISKEKKDDFVIFKDAIFILVDSPRKALSQVAKNFYGDPTSQMKVIGITGTSGKTTTTFAIYKALRWMGKKAGLIGTIEYRVGDKIYNSTNTTPDILDLYEIISLMKNENVEYLVMEVSSHSLALGRVDGINFDICGFTNFSQDHLDFHKTMEEYLDAKLKIFDVLSSSNKNRKTLVVNKDIEVFPRIRLKASKYPDIKLKTISLVDRGADYYSRVVRLLPAKTVFELSGRNFEISMIGNTNVYNFSMAIAILK... | PTM: Carboxylation is probably crucial for Mg(2+) binding and, consequently, for the gamma-phosphate positioning of ATP.
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in... |
A0A7C5IML0 | MENKIFCPYSVSFLKSLLREKNIFLSKSRGQNFLIDRNIAQKIVSSIPENETILEVGPGLGALTFLLIENRRVYAVEIDKKIYTELKNHIESKNLILINGDFLKFNLSKIPEKRLYFVSNLPYSISGEALKKFIDEETLNEGILMLQKEFVEKMLATFSTENYCVMSIITYFFLEIEKLFDVSKNCFFPAPEVDSTVIRIKKKKSRYNHKEFGNFLKKAFSQRRKTILNNLKNLNISPEVLEKLEIPASTRPENIHPEKWAILFEYYQVHKSQEE | Function: Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits.
Catalytic Activity: adenosine(1518)/adenosine(1519) in 16S rRNA + 4 S-adenosyl-L-methionine = 4 H(+) +... |
A0A2H5YPR2 | MIYPNVLSLIGNTPLVRLNAVTRGLNASVVAKLELLNPGGSVKDRIGFRMLEEAERRGWLKPGGTIVEPTSGNTGVGLAMAAAIKGYRCIFVMPDKVSAEKVALLRAYGAEVVTTPTAVPRESPESYYSVADRLTREIPGAFQPNQYFNPMNPRAHYETTGPEIWQQTEGKVTHLVAGVGTGGTITGVAWYLKEQNPAIKVIGADPEGSIYTQPENIRPYKVEGIGEDFWPGTFEPSVVDEWITVSDRDSFLTARRVTREEGILIGGSGGTAVWAALQVAQREDDPSTLIVVIIPDSGRGYLSKIYNDDWMRENGFLARF... | Pathway: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine from L-homocysteine and L-serine: step 1/2.
EC: 4.2.1.22
Catalytic Activity: L-homocysteine + L-serine = H2O + L,L-cystathionine
Sequence Length: 467
Sequence Mass (Da): 51122
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K2CIN4 | MYQLQQAIGLLGGTFDPIHFGHLRTALELYQALELAEVRLIPCFQPVHRKLPVASPKHRLAMVQAAIIDEPALKVDDCEIQRKGPSYTIDTLEALHKKLPDTPLCLIMGIDALLGFPSWHRWEDILTLAHLVVAHRPHYQLPQTGIVAQLLKQRLKHNFSAIHECMAGNIILHPVTALDISATDIRKQIAMGRNPRYLLPSAVYQYIEKHGVYSISRI | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
EC: 2.7.7.18
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide... |
A0A7V3VW33 | MSGGKALSYWDHLEIFRIKILTVIVFLVVASFFSFFFIDKILQILQRPIQGLPVTLNYFKPYEKMLVYIKISFYSGFVLTVPFGLFQIGSFIYPGLKKKERRLFALSFVLIPFIFITGILFSYFYMAPAAFRFFVSFGIGDSFKFLWSVMEYYDLFVGLLFACGLIFQLPLILIVLMKLGVLKVEKLVFFRKYIILAIAIIAAILSPPDVLSMFLIGIPLYLLFELSVFIGRFVARR | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes.
Subcellular Location: Cell membrane
Sequence Length: 237
Sequence Mass (Da): 27411
Location Topology: Multi-pass membrane protein... |
A0A8U8C925 | NPVQPMTRARFLGGCAWLLGALALLQTLYLRSLPPPAHPPPPIPPPPGRAAAALGGARGGSWAGPLSLAAFGEPRAGLRELLAALGGPCRALRGRLRLHVVQGAARPPPRVPPPQSPPQNWPGGCRGALARLAAADPPSYALGVPYPGNLLRNVAWQGAPSPGLREGFLELLDPHAQIAPHDPHDPHAPAPPWARTLFVLPAFEVRGSRPPPGSKAELLRLWGAGEARPFYGGLCPRCQAPTAFGRWRGLPPAPPGPPRLRVAYEVPWRDPWEPFFVAPARGVPPFDEGFLQYGFNRISQACELHVAGFRFAVLDGAFVT... | Pathway: Protein modification; protein glycosylation.
Catalytic Activity: 3-O-[beta-D-Xyl-(1->4)-Rib-ol-P-Rib-ol-P-3-beta-D-GalNAc-(1->3)-beta-D-GlcNAc-(1->4)-(O-6-P-alpha-D-Man)]-Thr-[protein] + UDP-alpha-D-glucuronate = 3-O-[beta-D-GlcA-(1->3)-beta-D-Xyl-(1->4)-Rib-ol-P-Rib-ol-P-3-beta-D-GalNAc-(1->3)-beta-D-GlcNAc-(... |
A0A971GSV2 | MKKNKVDHPLLFKAVMLAAGLFLGLFCARIFFTVMTVNTDSMEPSVRRGSTVLLSAFSPVRTGDIVAIENPAQSDRLLLLRVLAEGNDTVEIRNRVIYINDNRFEPRWKIIRGDITALPMKFCYRDNMPPLRLGRNEYFLMSDSYDEGYDSRVFGKIDASAIAGKAVYILR | Catalytic Activity: Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.
EC: 3.4.21.89
Subcellular Location: Membrane
Sequence Length: 171
Sequence Mass (Da): 19415
Location Topology: Single-pass type II membrane protein
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A0A972L479 | MICFPNAKINLGLRILQKRDDGFHDIQSCIVPIPLCDVMEIHESGQFKIEVFGAVMGANPKDNIIYKTWEKLNDSFDIPAFEVKLIKNIPLQSGLGGGSSDAAFFLKEVNAAYGLGITDDGMEMFLESLGSDCPFFVRNRIAMAYSKGEALKGCELDLSGLHLTIIKPDHNISTSTAYGKVVPNSHEKPLSELLKLPLPTWKDNVFNDFEKTVVAQMPELSSIKGLLYDSGAEYVSLSGSGSAIYALSVDKLDVSGVGGGFIRQAAF | 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... |
F6YAR7 | MAASGHEGGEDGRTRGGEVCPPGAAVAPPPLSPALVVPLWSASAAVAGWVARSLARAAGSRPSPLGSARARPPARPPLPLGLSSAPAAAMLGAALRRCSASAGLRSLLRSPRAPASTAAVQTARCYSHGSHETDEEFDARWVTYFNKPDIDDWELRKGMNTLVGYDLVPEPKIIDAALRACRRLNDFASAVRILEVVKDKAGPHKEIYPYVIQELRPTLNELGISTPEELGLDKA | 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... |
A0A1G2BMN2 | MLPSKNRLSKTSDFKELALKGRPFYSSFLTLKILKESGLTSRFGVVVSARVSKKATVRNKIKRRITEIVRLNLNNLAAGFKIMILVKPAAASKNYREIKEEIGKLLKQARIL | Function: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of... |
A0A7W4UGR0 | MSTENPAPASGEPSAPTVPAAPGASLAEVRVDEPDGRPARPRVRTDPRTWPGWAQALSLYAATRAFSAVVLVLVAQLQVENYWTGARPSYLQFTGLMWDASWYRGIAEDGYPAELPRGEDGLVQQNPWAFFPLFPMLVRGVMLVTRADWYVVAPLVALVLGCAAAVVVHRLVERGAPRAVAARPGLPLATVALLGLFPTAAVLQVAYTESLALLLVASALLLVVERRYAWASLVVLALGFTRAVALPMAAVVVVHALVRWWGARRGTDRLGARGVAGIGLLAVTAAVSGVAWPLICGWTTGEPDGYLQTQGAWRGVREIT... | Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 443
Sequence Mass (Da): 47797
Location Topology: Multi-pass membrane protein
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A0A522D8H9 | MMEDLESSPVLTRVHDALAARYPESLSEWTFEKGELTAIVRSDALVEVLVCLKGELGFIALNDMIGLDNMNIGDGRKRFSVLYQLYRFPAADRIRLRVDIGEGETLPSIYFLYRSSDWAEREIYDMFGIVFKGHPDLRRIYMPEEFDGHPLRKDFPLEGRNP | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ... |
A0A3B9UH16 | MIDLTAQTTFRLPFQAATVIELASLETAATQLQDIDAPALVLAGGSNWIQLDPTFLGTVIRPRLMHCHAETVQDEVRLRVGAGVLWHQLVMDTLASGWYGLENLALIPGWVGAAPIQNIGAYGVELSSVCTAVLAWDFVRQKQVMLTNDDCAFAYRDSLFKRDSTRYCILEVHLTLHRRARTSVDYGAIRDAVSAAGGDLQNPLDIAHAVIAIRQSKLPDPQVIPNVGSFFKNPVVSVAQRDALLKRHPDLPHFPDSDGVKIAAGFLIDQAGWRGRWIGSVGVHADQALVLVNNGQPVLADLRTLVKQVRSEIKARYHIH... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation.
Catalytic Activity: NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
EC: 1.3.1.98
Subcellular Location: Cytoplasm
Sequence Length: 333
Sequence Mass (Da): 36409
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A0A935RE71 | MKPPRKPAAGPPRRPSAPPLTHFDAGGQAHMVDVGGKDETTRVARAQGHIRMAAATFALVSSGSAKKGDVLGVARIAAIQASKRTSDLIPLCHPLALTRVAAEFTLDARRHCVTLDVTAETVGRTGVEMEALTAVAVGLLTIYDMCKAADRGMIIEDIRLLEKTGGKSGHWIADAECK | Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
Function: Catalyzes the conversion of (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP).
EC: 4.6.1.17
Catalytic Activity: (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate = cyclic pyranopterin phosphate + diph... |
K1ZBJ3 | MIESTLSKRYARALLELAQKESTEKLYLESLQNLSELVNSHPHLRIALENPFFDLASRLRVVEALSVKMGFDRIFINFLKILTKNGRMNFLKDIVVAYQNLYFQKEGMLEAVVTTAKEMPTSFYDQIKTILGKKTGKKIMCQPNINVSVLGGVSITLDGKMYDGTILSDLNRLGYRLKNVSAGHF | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
A0A0C9V4E2 | MPPVPKKAQKIGRALKTAARLPARVSGGRGSGRNNYSPSPGEHPVVFLRLQVLGCKDLCSRGKNSSCDPFVVVSLLNTRQHTPVIKRTANPEYILKDATFDFPIYLSLADRLGTVEIVVWDKDGLLKKEYLGEVALPLEDWFNEGNAFGFSDNNNKSSSLNLVSTRATTHASGSVQIKLGFVSPPNTQSLMGFEEVFAELIKRSRPSLVSAPPTKFRKSWSTNKRVDYNFSAANDIVGIVMLEIQGATDLPRLKNMTRTGWDMDPFVVTSFGKKVFRTRVIRHSLNPTWDEKLLFHVRRYETSFKVQLTVLDWDKLSSND... | PTM: Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme... |
A0A109QJ99 | MKWKMTSLFLVPLILMTVAFTFINLAAVIYFSSAEPEKNAFISFFPYEEYTRKFGRFIVFVDDKPQVSPEGKKELSKKRAWIQILNANGTEVYNLNKPEAAPKHYTPGELVHYYRYTASIQDSTLFVSWVTHEDTKWTYILGFHYHTISRYVMSFSPFKMINFWKEVILAVFVLTFLMVITIGYFFGRKLTRPLVEIIGSIQALAQGHYSIKYNIRGLYKDVYKSLNQLADALKASEVQRMRLEKMRDEWVTNLSHDLKTPLASIKGFGEVLADSDYEISPDERRKYADIIVGKTSYMEKLLEDLRLTYQLKNNLLPLQK... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 475
Sequence Mass (Da): 54839
Location Topology: Multi-pass membrane protein
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A0A496QWI6 | MFQYYRTNKSRENDALQENGFEECIMRKRTKIVCTIGPACKDERVLRGMIENGMNVARLNFSHMEREEADRIIALLKNLRSKLHIPLAIMLDTKGPEVRLYGYREPVPLSQNDIITIKSYEKPDLHSKETGNKFHFYTNLPSAGSLCRIGSRVLLMDGFIEGEIIDKNETCVKVRIRNSGLLRTKAHFAIPGTEYPLPFLSEKDREDIIFAAEKGLEYIALSFVGSANNIFTVRNLIHDRFPGSAIQLIAKIENKAAIDHLDEIISHADGIMVARGDLGVELDMAEVPVMQKRIIEKSYLRGKPVITATQMLESMINNPI... | Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5.
EC: 2.7.1.40
Catalytic Activity: ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate
Sequence Length: 614
Sequence Mass (Da): 68841
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A0A496QX35 | MRKKSLAERIRALFSPGKGGKEILEELEDSLIEGDIGAKTAMEIIDELDNCAEVHLSTREELQNTLKELLIEYLKEAPLVPEKGKINFFLILGVNGTGKTTTIAKLAYYFSRELGKEKILLSAADTFRAAAIDQLKLHGERLGIPVISQNPGADPGAVIFDSIQSARARGCEVVLADTAGRMHNRANLIRELQKIKKIVDTKVPGIVSKNILIIDATTGQNGFRQAEIFHQAVGIDSIILAKYDATSKGGIAVSISRNLGIPFSFLGTGEKYTDLEEFRIDTYLDSLIGEE | Function: Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Acts as a receptor for the complex formed by the signal recognition particle (SRP) and the ribosome-nascent chain (RNC).
Subcellular Location: Cell membrane
Sequence Length: 291
Sequence Mass (Da): 31843
Location T... |
A0A4R1F909 | MSKPRNLSTLSTVSTLYRTDQTRELDRIAIQDFGIPGFTLMQRAAQATFDAILNSYPDCKSVCVLCGAGNNGGDGYVIATLAIKAGLKTTLIQLGDVNAIQGDALLAKDVFIKAGGISAEFEETLLNADVIVDAILGTGLTRNVKDDWIGFFDAVNQSSAKKVAVDIPSGLSSDTGQILGACIKADLTVTYIGLKRGLFTGQARDQVGQLIFDNLGVPTSVYEQLSTKSNTHLIPENIITNTITPRPRCSHKGNFGSVLLIGGGEGMPGAIRLAAEACLRSGAGLVHVATHPSHAHYINATRPEMMVKGVEEPQELDELI... | Cofactor: Binds 1 potassium ion per subunit.
Function: Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that... |
A0A2H6GNR9 | MSTEVGVLMGGRSAERDVSLVTGNSICSALLERDVDAVTVDTAGDWRSEMLRKKVDVAFIALHGRGGEDGTIQGALELMDIPYTGSGVLASALAMDKIQTKRILDACGIPTAPYVSMGPGDYDHEINMPFPVVVKPSREGSTIGISIVREKGTLKKAIRDAARHDPYVLIESFVPGEEYTVGILNGKPLAVVQIVTANGFYDYETKYVTGADEYRVPAPLDPEMTELVRSTGLETSHALRCSGAVRVDLRGQDGNFKVLEVNTIPGMTPTSLLPKSAQGMGIDFQSLVLEMLKTAGEGSK | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation.
EC: 6.3.2.4
Subcellular Location: Cytoplasm
Catalytic Activity: ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) + phosphate
Sequence Length: 300
Sequence Mass (Da): 32... |
A0A6I8PR41 | MSPLGPWASHFTSPCLSSLICKIRIKSVSPTWDGDCVQPDLLISTPALSTPPVPAERSPHRPILQAGLPANTTAVVGSDVEFFCKVYSDAQPHIQWLKHIEVNGSSFAADGVPYVQVLKTADINSSEVEVLYLRNVSAEDAGEYTCLAGNSIGLSYQSAWLTVIPGKGRGGPGKEELLRDAAGPEVKYTDIIIYTSGSLAVAMVVVIVALCRMQSQAGKPSREPLAVHKLSRFPLIRQFSLESSSSGMSSTSLMRVPRLSSSCTPMLAGLVELDLPLDAKWEFPRDRLALGKPLGEGCFGQVVRAEAYGIDRDRPDKVET... | Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
EC: 2.7.10.1
Subcellular Location: Membrane
Sequence Length: 622
Sequence Mass (Da): 68571
Location Topology: Single-pass type I membrane protein
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C9PWY9 | MQPIINHFTDNDAYTFSCQYYVLQTYPRAEVEYTFFDRNHTSYPEGFADKVKEQINLMKNVRITEEEIAFMQQRMYYLPQWYFTFLRGYKFNPDEVHIQQSPDGQLAISIRGKWYSTIMWEMPVLSIISELMHQHRGDLERYDATVEYERATEKAKQILRGGLVLGDMGTRRRLSFHHHDNVIRALKATAEAGGENVDGVFVPWKGRIVGTSNVYLAMKYELVPMGTMSHQIIEFEENVSGIFECNFNVMRKFSDVYDGDNGIYLYDCFGDKVFFNNLSKRMALMFVGLRVDSGVEEEQTEKIIEKYKQLGINPATKQVI... | PTM: Transiently phosphorylated on a His residue during the reaction cycle. Phosphorylation strongly increases the affinity for substrates and increases the rate of nicotinate D-ribonucleotide production. Dephosphorylation regenerates the low-affinity form of the enzyme, leading to product release.
Pathway: Cofactor bi... |
A0A369A3H1 | MKHFNFLSFPIVVLLLACNSNSNDFVQRINRGNAQGTTYNIQYLVKTGTDYQINIDSIFRFVDSEMSTYIPNSTISKLNKGENAPISEHFFKVLKKSEEVYELTGGFFDVTVFPLVNFWKIENKDENVIPDSSKVDSVLHITGFKKVVFTENSVSLPKGMSLDLNAIAQGYTVDLIAEFLESKGVENYMVEVGGEVRAKGKTINENIWKIGIEKPTESTDQTAFQTVIVLKDKSLATSGSYRKYKTMPDGSRLSHVINPITGYPANHNLLSVSVVADDCMTADALATALLVMGLEDAKQFAKAHPEWDYYFIYFDKYKGY... | Cofactor: Magnesium. Can also use manganese.
Function: Flavin transferase that catalyzes the transfer of the FMN moiety of FAD and its covalent binding to the hydroxyl group of a threonine residue in a target flavoprotein.
EC: 2.7.1.180
Catalytic Activity: FAD + L-threonyl-[protein] = AMP + FMN-L-threonyl-[protein] + H... |
A0A369A1E8 | MQEHIPYIHRCFQLAKNGEYTARPNPMVGSVIAFKGKIIGEGWHHKPGEPHAEVMAINSVADQLLLPHSTLYVNLEPCSHFGRTPPCSLLILEKGIPKVVISNTDPNPLVCGKGVQMLREHGVEVITGVESSLGYEINKHFFTFHTQKRPYVYLKWAESLDRFIAPINQPVNKPFIISSKQSLRLAHRLRAGTQSILIGSETALKDNPSLTTRLVKGPDPLKLVIDRYRKLPESLNIFRTPAPAIRIVDSRFAKEEDIAIQMDKDWNWLGALLDQLYKKGVQSLQVEGGTRVLSAFIAKNLWDEIWLIKSHTRLFDGIPA... | Cofactor: Binds 1 zinc ion.
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 2/4.
Function: Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5'-phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)-pyrimidinedione 5'-phosphate.
Catalytic Activity: 2,5-diamino... |
K1YQF2 | MNSPAKINLYLHIVGHRDDHYHLLESIFVFTQWGDDIAIMPRKTITLSITGPSALPLKYFPLEQNLCYRAAILLQKKFNIAEGAHIILQKNIPVSAGLGGGSSNAATVLKLLNQQWKLNLSQDILCELGATIGADVPACIHATSAFVSGVGEKIQPITLSFAGYPVLLVNPNQPLSTQKVFQQFHHDAQAFTPSQSYQNTLEWISKQRNDLEKPAMQLQPAIRAILEKLEQQPSCKLARMSGSGPTCFGIFETVIAAENAKLQLQKQFPLYWMKATVLC | 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... |
A0A9E7HZ65 | MRAQACGSSANRPQSAHFSGFVDRAKLIRTLTTPVKLIKCLRSIKEHAFEASPYPVIITLEDHLTPNLQAKVAKIKEKEHEGQKVDEEAWSEEVSDHEAITNDHELNEHYQEEDPEEGNGKPPIKYKRLIAIAAKKMQGDLTEALKIDPHKVTRLSLSELALEKAASSHGTELIRFTQRNLLRIFPKGTRVTSSNYKPLLGWMHGAQMVALNMQGYGKPLWLVHGMFKANGGCGYVKKPDILLNDDPDQLFDPKATLPLLKTLKVRIYTGDGWRFDFHKSHFDTFSPPDFYARVGIAGVPVDTSTTMKQTKIINDCWMPV... | Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + H2O = 1D-myo-inositol 1,4,5-trisphosphate + a 1,2-diacyl-sn-glycerol + H(+)
EC: 3.1.4.11
Subcellular Location: Cell membrane
Sequence Length: 394
Sequence Mass (Da): 44811
Location Topology: Peripheral membrane protein
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K1ZYP2 | MFSKRKQLLLHICCGPCVSGIVDFLRKQNFDVTGFYYNPNIYPYGEYKKRLDTVTEFASKINLEIVHLGFSKNSYTKQVAAFYDITKDHTQKPGRCLLCYKMRLEETARKAKELHIKNFSTTLLISPYQNIDAIQQMGNSISKNHGLNFFPDHHSKKKFKGFRRFFTFCKRIAKRHNMYSQKYCGCLYPKKEAVAERKKVR | Pathway: tRNA modification; tRNA-queuosine biosynthesis.
Function: Catalyzes the conversion of epoxyqueuosine (oQ) to queuosine (Q), which is a hypermodified base found in the wobble positions of tRNA(Asp), tRNA(Asn), tRNA(His) and tRNA(Tyr).
EC: 1.17.99.6
Catalytic Activity: AH2 + epoxyqueuosine(34) in tRNA = A + H2O ... |
A0A1I3AYB6 | MSEWSLVISGGGSGGHLFPALAVVEELRKRPNGPSRVLFLTSQRAIEKTILDPYGVEQIALPAVESHQFRSRPIRSLWNLRAAVSQASATLRSLPRPVVLGAGGYGSIPGGLAAWWMKCPLVLLEQNIVPGRATSLLSRFAQVICTSFENSERHFPERPKIVCTGNPVRADVAGQTKYEPDLDRKILLVLGGSQGAAFLNRSLLRFGQHNGGALEGWSIVHQTGESDCELVRQTYRDLGIAAEVAPFFDDLADRYQAASLVVTRAGGTTLAEIACAGLPAVIVPYLGSLRDHQLRNAQLFVRGGGAMLVEQLGTASDEQD... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II).
Catalytic Activity: di-t... |
A0A1I3SWF9 | MGLGHFGGGLGAVKYLLDRGAMVTVTDLRSADELADSLSQLDVSQLEALVLGEHRDNLFTRAELLVVNPAVKPGNRYVELARTVGVPITSEINLFWQHCRGKKLVVTGSTGKSTTASLIHQFLQAAGVPSRLGGNIGVSLLPLVDEITPDEWVVLELSSFQLAALDELRPRPDIAVVTNFFPNHLDWHGTLDAYREAKQTAVCWQTKNEIAVLNADDADSALWPTDAKVVWYGKECWRDRPGVVVGDNHLIVRSSSGGWKIELTDLAPYLRTPHGLMNVAAAFGAVTVALGIPVDKLAGALLNFQGLPHRMQTVAEIEGR... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).
Catalytic Activity: ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-... |
A0A9E7EUB2 | MCCPCCCLYLFIGVNHDFPAMCYPLLIRSMGIVVCLVTTPIATDGWYCNYQFDCSPSTFTIFSFGVTRSRSKAVIQGVISCVAIGLWADLVIGFVTEYYTRNAYGTIQDGADSCRAGAATNVIFGLALGYKSVIVPNFATAVSIFVRFSLGAMYGIAVAALGMLSSIATGPVIDAYGLTSDNIAGGIAQMDGTSHRIQERTDALDTAGNTTAALGRGGNLCLGDSDKNNLDSSFGKTATHKFQALQLIQLPWSLLQSSSYFHCGCSDTKGLQWVDCWCDASLLVLSHDHEECRQCSSEEGGGGALVMLTPLIIGILFVME... | EC: 7.1.3.1
Subcellular Location: Membrane
Sequence Length: 490
Sequence Mass (Da): 51788
Location Topology: Multi-pass membrane protein
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A0A924DVD5 | MTEGNVLPGSNPEEPVNETVRVEAFSDAVFAIAITLLGLELKVPHLNPVTAEGFWRGILALWPSYVAFVTSFATILIMWINHHGILKQTRRTDTAFMMANGLLLMLITAVPFSTACLANFLTTPAAQMAAGLYAGTFALINIAYLLLWLASAHHKRLLHAHISERHARRITRTLLAALPLYLMAMGVAVANPYASVVLCAALLPVWAVISYDYRPPPETVKSGPRRIRIGPWHRPPPGPAPPEPATEPDALPPAAS | Catalytic Activity: K(+)(in) = K(+)(out)
Subcellular Location: Membrane
Sequence Length: 256
Sequence Mass (Da): 27818
Location Topology: Multi-pass membrane protein
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A0A660TGS5 | MRMKKLQSLLKGVDIINRRGSTGINISGIAYDSRKVQPGSLFVAIAGFHTDGHRFISEAVKRGASAVVYSTPLPSLVSASSAQGFPAVNVPSADTQHKDRMPAADKSRAYIQVKDSRKALSRMASNFYGNPSKKLKVIGVTGTDGKSTTVWLIHQLLEKLDKKSGLISTVNFKTGNRLKKNSMRQSTPESLEIQSMLAEMVANSLEFAVVESTSHGLSECTARLYDVAYDAGVLTNVTHEHLEFHGTVEQYRYDKANLFRKSSLFNVVNADDSNYRYFKNVSSVPVYAYSIKRENTEIYACAIKTYLHYSEFTIHYGNER... | PTM: Carboxylation is probably crucial for Mg(2+) binding and, consequently, for the gamma-phosphate positioning of ATP.
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Catalyzes the addition of an amino acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosyn... |
A0A930X9M4 | MQLVLVGANYKSAGLDTRELLTFSKVQLSALLDTLSETAVIEEALVMSTCNRSEVYVISRHPEAARQLILDAISELAGVPENTLETLLYTYYNKFAATHLFDVACGLDSMVLGEDEILRQVKTALDIAQLSHSSGPILNQLFRAAVTAGKRVRSETAINQGCTSLSAVAARLLRRHLEQKPAHLLIVGAGQMARTLIRNLEDTDIQISLANRTRSNAEALAESSKQAIQLLNLDQLASILPQVQAVVTCTALPDFLITPDFLPNQALMMIDLAVPRNIDPGVTQQPGITLYDVDSLQNQVEDSLLRREQNIGQAQSIIGE... | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2.
Function: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
EC: 1.2.1.70
Catalytic Activity: (S)-4-amino-5-oxopentanoate + NADP(+) + tR... |
K1YSQ1 | MTNKLSGLLDLRTMQELTDSLYAAAGIPSALIADDGSVLTRSGWQEICRDFHCRHPEGRKNCNCTTIRSPEIPVAKATHAVSKCPFGLFHAVTPIIVDGNFFGHFFAGPFLHHQPDHDEIEYFKQQAERFGFDEQAYLNALHKVPVFAPERVASVMEFLGHFAGIITRAGLANGRRTTFSPPPIQANGQLAEKEKEHNSPQHALLQYPELTQILLDTIPAAVYYKDSEGKYLGCNTIFCDFILGLPKAEILGRKRFEVATIPAGLAAIYHQKDLELLANGISQRYEAAVRCADGQIRDFLFHKAVFRDSTGTACGIIGVM... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Cell inner membrane
Sequence Length: 972
Sequence Mass (Da): 107178
Location Topology: Multi-pass membrane protein
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A0A1B2YNS9 | MALTISVLAKFSDRVTQTLSLELVPVQLNPTELITDSQPQFMDVTVETDGYDMLKYAFQHLTYKIDVTTLDKSNSTYTWTADLKDFKGSDFFDESFEIIALSPKVVRFNYDTQSQKRVPVTVVARTQFSVGYDMLNPLTSRPDSITIVGAKTSLDTIDRISTLNIEMTAVKSDINQSVELRIPPNLKPSSNVVQVFGTVEKFTEGKINVPVSVVNLPEGFTVSIFPKEIPVVYYTNLRTYDSITATDFKVVCDFNNFNIDSKVLVPTLASHPKSIKNASLEINKLEFVMTKKMTKVIGLTGGIGSGKTTVSKMFESVGVP... | Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
EC: 2.7.1.24
Subcellular Location: Cytoplasm
Sequence Le... |
K1Z4I5 | MAKKALKKKSESVDFAKAFSELEEITKWFESGSIDVDEGLKKFERGIELSKQCQKKLAEVQNRIEELKNSNK | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
EC: 3.1.11.6
Subcellular... |
A0A7G9G425 | MRYLTDSSQMKAIDSYNIEELGIPSLVLMERAAYAVSAEAEQMSSQNGSVLVICGMGNNGADGLAAARMLKLHGRKVKVLLCGKASHSTKEHSIQLAITEKLGIPAVTADSRQEYSIENGFELIIDALFGVGLSRPLNKTFIELTDAIERARISGAKVLAVDIPSGVSASDGQILGAAVKADATVTFGFEKLGLVLYPGAFYCGKKKVADIGFSLPNGMESRMAYTFGPEDLRRLPKRPADGNKGTFGKVLLAAGSKRMSGAAYMSALASYRSGAGLVQIYTVKENVQVLKTMLPEAIVTGFDREHPDMEELADLCRWAD... | Cofactor: Binds 1 potassium ion per subunit.
Function: Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that... |
A0A936P9F6 | MNPMFRFAKAPGVDPAHPIIQDVSAEVLKYLSIVVVLGSLAFVVLVRFISPEQTMRAIVPLLSLPLFGGVWLLMKHGRPYAATRLLVVGIWAVTALICIFASGVRTPIVIVYPVLIIYAGWRLGPKSGAVLAGLVFLTLAGLGWAEWAELLRPRPTAPALYVLVQSLVIAIALAVVAGAVSAQERRIAAVASLGRELDESRAELVRAQAVGRIGSWVLDVAGNRVRLSAEACRIFGLPEGSPGSVGAYLARTHEDDRDAAKAAWRAGLAIGVFDHEHRVRIHGEIRWIRQQAEIEFDAEGKPRTVFGVTQDITERKRAES... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Cell inner membrane
Sequence Length: 994
Sequence Mass (Da): 106405
Location Topology: Multi-pass membrane protein
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A0A7J4VGG7 | MITNLVREHLRNLKPYRSARDIYKGNGYIFLDANENPLISSEEGLERYPDPGQTGLRLKLAEKTGIPAENLFFGVGSDELIDLIVKLICDPGKSEALTAGPTYGMYKTVCDIHNIKLNTVLLEAGTFQLNAEKLLAAVTPETKLIFLCSPNNPTGNLLVKEEVLRVVKGFSGLVVVDEAYIDFSGSEGFLREAVEYPNLCVIRTFSKAFGLAGARIGWLAGSAGLVEWLFRIKAPYSINKLTEQKALEALGQYEIIRKRLTTVTDLREKSAAVLSALPFVEKVYPSDANFLLIKVSDPKGLCSSLAEKGVIIRDRSDQPM... | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 6/9.
Catalytic Activity: 2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Subcellular Location: Cytoplasm
Sequence Length: 549
Sequence Mass (Da): 6020... |
K1XRP9 | MKPSKSLKVKEKSSGMRIDVFLSQELKISRAQVQKYIKSGFIFVDGELAKSSSRTSKGQKIEITIKPENNSDKKLPELNIIYEDDDVLVLNKQSGVVVHGASGVHEPTLADSVVAKYPKIARVGENKMRPGVVHRLDRGASGVIVFAKNKKAFLHLKDQFQSRTAKKIYIVLVHGQMPKNFGTLRVNIARSERTGKMVSRPMSQEGKEAITNYSVTKNYRNYSLLEVHIETGRTHQIRTTMQASGHPIAGDTLYMNRKLKQAEINRPFLHASFLTITLPSGEVKTFSAELPVELKKYLETLT | Function: Responsible for synthesis of pseudouridine from uracil.
EC: 5.4.99.-
Catalytic Activity: a uridine in RNA = a pseudouridine in RNA
Sequence Length: 302
Sequence Mass (Da): 33864
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