ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
|---|---|---|
A0A3D1WGZ8 | MKNFNFKKKFGQNFLTDKNLLSSICADAEIGFGDQVLEIGAGMGALTVPLCERASKVVSYEIDNELQPHLLGLGLKNLTLHFEDALEKPLSEIEKDFDGEYKLVANLPYYITSPLIFKFLESNKLKSLTIMVQKEVGDRIVAKQGSKDYGVLSLSCAYFGQAKIMRKVPRQMFTPSPDVDSCIVRLDIEPNKYDLDKQTYFKLIKTAFKSRRKTLLNNLSEGLNVPKNALSGLDFDLSKRAEQLSIDDFVKLGHLLNKFIGEKSHDKR | 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(+) +... |
A0A3D5MPV7 | MLRSDAPGRLRPRGGAPIRHDRRIMTVGELTSYVKGLLDGDPFLADVWVKGEISNFRHHTSGHMYFTLKDATASVRAVMFRKANQRLAFRPENGLEVIAGGRVSVYERDGQYQLYVREMEPAGMGSLYLAFEQLKRKLADEGLFDEALKRELPSLPRRVGIVTSPTGAALRDIVTVARRRYPNIHLVLSPALVQGDGAPADIIRALELLSARDDIDVVILARGGGSIEELWAFNDEALARAIRACRHPVVCGVGHETDVTIADLAADRRAATPSNAAEMAVPRKADLSWKVGVLTGRLERALRALVAERMKAVERLSLSS... | 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... |
A0A2H0SL25 | MKRLIALLIGWRLVLSAVLAVTAGLVVYRADFMYTSLWWYGQPGWPVSSDILWPWANFDGVHYLRIAAEGYTTQARFLPLWPAVIGMVTRALGVHQAYSTGQVLAAVGLSSVTALAAAAALYRLLRLDVTAATARRVVMLWAAWPVAFFLFAVYTEGLFVLLAVLSLYLARQRRWWLAGAALSLLAVTRLVGVLMVPVVLLEFWQAEGLKKLPWQSVAAAKRWRSSWQSWLGQSWPILLSPVTLVGYAWFNWWRWGSPLYFVTAHGQLGNSRTVTGVVLPVQTLVRYARLLVVLSPSQHEWRVAVLELAALVFITAGLWL... | Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 407
Sequence Mass (Da): 45848
Location Topology: Multi-pass membrane protein
|
A0A3D1RFA1 | MEQIEILTEGIEEKEEYKEIIKTVLKQCFKEEELGKHISITITLTNPEYIKSINRKYRNVDNPTDVLSFPMYERDEISTIKKQKYETILGDILISIPKVQEQAIEYEHSFKRELAYMVVHGFYHLMGLDHMNEDEKKEMREKEENILNKLNIIN | Cofactor: Binds 1 zinc ion.
Function: Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.
EC: 3.1.-.-
Subcellular Location: Cytoplasm
Sequence Length: 154
Sequence Mass (Da): 18397
|
A0A1I1G531 | MTASRPSKLSLYLQLIRWNRPAGWLLLLWPTWSALWVAAHGFPGWHLLTVFTLGTFLMRSAGCCLNDVADRDFDRHVKRTAQRPVTSGALSSQEALLVGAVLALLAFGLVLTTNAVTIAWSFAALAVTLVYPYAKRYVSMPQAVLGVAFSFGIPMAFAAVQSRVPLLAWVLLLGNLFWVIAYDTEYAMVDRDDDLKIGMKTSAITLGRFDVAAIMLFYLIFLSIWALALVGIVQSAIYLVAIGLALLQALGHGWLIRKRQRDDCFKAFRLNHWLGFTLFAGVALSYWGR | Pathway: Cofactor biosynthesis; ubiquinone biosynthesis.
Function: Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of ubiquinone-8 (UQ-8) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB,... |
A0A970VHS9 | MTIQQAIKHAADVLEAASIPDPLQDSLLILSSILGLGSLELRLNGDRTLNSEQEQRLSSLLLSRTTRQPLQYLLSEQCFYGLDFYVDHRVLIPRQETETLCELGLAFLKAHTNASALDLCTGSGAIATTLKHEVPLATVTAIDLSEGALEVAKMNAKRNGAEVRFLQGDLLEPVCGERFDLILSNPPYIKSLDCDTLQPEVMLEPRMALDGGDDGYVFYRRIAAKADEFLAVGGMLAVEVGDDQAKQVAALFTSNSNLCDVHIHRDLYGHERIVCAHASSNPT | Function: Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif.
EC: 2.1.1.297
Catalytic Activity: L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-methionine = H(+) + N(5)-methyl-L-glutaminyl-[peptide chain release... |
A0A8D8CE48 | KILTSTSPLSPTALSNRKVLVGGAIVLVAVVAVAIAVPLSINSSGSDDDDQDTNKANDVSPFFGRTILDEVPLIDGHNDLPWNLYSNERNRINNFNLDSDLKKDPRWGPSTSSHTDIPRLLEGKVGAQFWVAYVGCNTQYKDAVERTLEQIDVIKRMVAKYPKYMKY | Catalytic Activity: an L-aminoacyl-L-amino acid + H2O = 2 an L-alpha-amino acid
EC: 3.4.13.19
Subcellular Location: Membrane
Sequence Length: 167
Sequence Mass (Da): 18508
Location Topology: Lipid-anchor
|
A0A970L1J1 | MTNVLSVAAMRAAEENFACKCGGSTRDLMGAAGEGICNAVNDIDASVWSHGKKVAIVCGTGNNGGDGYALALQLHKRGIDSELFLVEYKFTSDSGYYFGLCRELGIPYRVIDGDVDLSDFDTIVDCIFGVGLRGAPEGRIADIIRAINESGGFVVSADINSGICGDSGIVETTAVRSDVTVAIGYPKPGHFLGSARDYIGKLVIADIGVQPVSKPYKLFEAADAAAVFPRRLHNSHKGTWGTAAIIGGSIKYSGAAKLANLAASSLASLKSGCGVARLVVPASISQAVMPYLLESTLCPVPDKDGKMIFDEGAISEAISG... | 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... |
A0A099KU74 | MRFNNIVKSLAIALPLTILSACSSNSDTDEQSQVDTNAQVTQNAEDARKAQEAVRVTAAKRAAEIEEQKRQELAKLRSEHIVYFDFDVSNVNEQYSAILDAHAKFLNANSDVKVLIEGHADERGTPEYNIALGERRAKSVVTYLENMGVAAGQLTVVSYGEEKPMVKERSENAFAKNRRAVLVY | Function: Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity.
Subcellular Location: Cell outer membrane
Sequence Length: 184
Sequence Mass (Da): 20434
Location Topology: Lipid-anchor
|
A0A7C6WAE0 | MNDRLPRHIAFIMDGNGRWALKKGLKRSIGHRYGVKALKRIFEYVFELGINYMSIYALSKENLKRPKEEIQTLIELLNEYIDDCLPQLIKNKIRLNIMGDISILDDSSQQKIKMALEDTKHYSDKALNIAFNYSGRDEIIKAANQAIKDGHGEINQEIFEKYLYTASIPDPDLIIRTSGEQRISNFMLYQSAYSEIYFTKTLWPDFTKKTLDAALDDYKKRHRKFGDIK | Cofactor: Binds 2 magnesium ions per subunit.
Function: Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids.
EC: 2.5.1.-
Sequence Length: 229
Sequence Mass (Da): 26739
|
A0A7C6WA40 | MIKIKTPATSANLGAGFDCMGLALDIYNEIWIKPSDRLIVETDDDLPKDHTNLVVSSMFKTYKYLGQEFSGAHIKQINNIPKTSGLGSSAACVVGGVTAANVLLGNLMSRQDVLDFCAMIDGHPDNVAPAILGGITASVINGQNKVHTFRCLPNGNIKIALAIANFKLPTTKSRNILPKKYSREDLTYSLSRAVSTFAALSLGQFEKLKYIMDDKIHTPYRRPLIANYDQIVKAFEDAGALGVYISGAGPAIAAFVDQNFRPFTPPKEWRLEIRNIVSQGVIVEMNS | Pathway: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 4/5.
Function: Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate.
Catalytic Activity: ATP + L-homoserine = ADP + H(+) + O-phospho-L-homoserine
EC: 2.7.1.39
Subcellular Location: Cytoplasm
S... |
A0A8H6EQ06 | MLPSIFIKSYARCVLWPLARSRVKQSSFRTFTYLHSQLKDYKDVDDEAAHKHLNSTGRSIRNDSGGDKRKALQKYNDLEENKDFDRAIKKLKNLVKDQENLHSEADTLNNKGNKNLRNKMTNDDAVVDEQQKSTTDSESETHTKNVSVEKINLPLKDKVTSFIRSVINGENFRQLKEELTKFSKTRARKQEKYKQSISNRLGQDVTELKKSIGIASRVVNDVTGYSKVNALKEKIAKNDLELKVLREEITRAKDDFSTAIEKRSESQREMNDLLERKSSWVPTDLKRFTELYMNEHELEREVKLKKIRLDELDQKNDETH... | Function: Required for the maintenance of the structure of the mitochondrial inner membrane. Involved in mitochondrial morphology. Causes growth arrest when highly overexpressed.
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 423
Sequence Mass (Da): 49696
Location Topology: Multi-pass membrane prot... |
A0A1J4W053 | MKNNRLIVALDVPNIGEAEKLVKLLSPLVEVFKVGNELFTASGPSAIQMIHSYGSQVFLDLKFYDIPNTVGSACEAAVRYKVFMLNVHSLGGKQMMFQTVQSVHKTAEELGIVPPKVLGVTILTSMKDLDLKEVGITKKLEKEVVGLAALAKTCGLDGVVASAHEIELIRQKTAPDFLIVTPGVRPVWAAHGDQKRVMTPKEAIEKGANFIVVGRPITQSPSPLEATEKVLSEIG | Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
Function: Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP).
EC: 4.1.1.23
Catalytic Activity: H(+) + orotidine 5'-phosphate = CO2 + UMP
Sequence Length: 235
Sequence Mass (... |
A0A5C7A9S5 | MITAYVGLGANLGDLRRTLEAALADLADLKDLSVEAVSGAWRSAPVGCEGPDYLNAVARVHTGLAPLVLLEALQAIEQRHGRERPYVNAPRTLDLDLLLYGDETLALERLTVPHPRLHQRAFVLKPLLELDPALSAPGLGDLRSHLPGVADQAIEREDEPLRRPHGPFGPQAATLAGFP | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 4/4.
Function: Catalyzes the transfer of pyrophosphate from adenosine triphosphate (ATP) to 6-hydroxymethyl-7,8-dihydropterin, an enzymatic step ... |
A0A8T3U6I1 | MKKEKSVKKNYQFKRILKKGKITSTEYIRISYQNNNLSNNRLGIAIRKNVKSSILRNRLKRIIREVYRLNNNKLKQGFDVIILINKPIDDYNIMKVNIEKCFTRLRMYEEISY | 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... |
A0A971DX26 | MAEQVLMIALSPTMEEGTVVRWNKKEGEFVNSGDVLCEVETDKATMDYESTMEGTLLKILVQEGEQAAIGEVIAVIGEEGENIDDLLESIKSEKSGIKGGGSSSDQAEESPEIHVKTEKIKADAGTAADSRIKASPLARRIAEINNLPLDRIKGSGPDGRIIKADVEKYMEKKAAPEVSVRSIPPYAVQPSSGDELIPASAARKVIARRLSESKYSAPHYYLTVTAAVDKLIDTRKRINESLPDKISFNAFIIKYAAEAIKKHRMINAAWQDDNILIRKQIDIGLAVALPDGLITPVVRDCGNKGIKEIDGELRKLIEKA... | Cofactor: Binds 1 lipoyl cofactor covalently.
Function: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3... |
A0A5E4TKK9 | MEFISVIYPGPMICGLLAATVWAVFRTRRERARSVRLTTTVSEHEVELEKLAVALADARRQASAALDDAASLRGELEQALLEQTAVLDHTPVSVCFVKDRVIVRCNRGFEKLFGYEAGEPVGKSTRILYATDEEWEEAGRDYEVIGGRVHVGDAKFVRKDGTPIWCADHGAVLDPNDLSKGSVWTALDVTQRKHAEQATREAKEAAEEASRMKSEFLANMSHEIRTPMNGVIGMTRLVLKTDLSPQQRNYVEKIAASAESLLRIINDILDFSKAEAGKIVLEHAPFRLQDILDNLSSLIVLKTEPTGVEVVFRVDKDIPP... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Cell inner membrane
Sequence Length: 961
Sequence Mass (Da): 103762
Location Topology: Multi-pass membrane protein
|
A0A929S874 | MKFNTISSSFGKNLLVRIWGGSHEPYVGADILGFPEGQTLDFAKLERFMARRSPSANKLGSSPRTESDSVIITSGLRDFTTSGEKLSLKIRNQDIDKSAYDLTFDIPRPGHADYPAKVKYGDSLDLSGGGPFSARMTAPLCAAGGITMQYLETQNIFIAGRIYSIAGIKDEDIDYTNPDLSAFLKLNREAIPCFSRSQAAKMQHAIEKAVAENDSVGSVVEAFVWGLPVGLGSPMYQGIESVLAPILFAIPAVKAVSFGSGTAASSMLGSQHNDSFRFENGKIVTPTNNHGGILGGLATGMPLYCKVYFKPTASIMRTQN... | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7.
EC: 4.2.3.5
Catalytic Activity: 5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate
Sequence Length: 471
Sequence Mass (Da): 51323
|
A0A3D1VQ90 | MKKICIVLLTIFLLPFTGCSQQKITSADIFAMDTIITIKLPKDKADEGFALVQEEITRLENTFSVTKSQSEIYQLNHKEGKPVALSEEVFSLIQKAERIKSLTAGAFDCSVYSLMQAWGFFEKSYHTPDEQTLQNLVEALSSPVMNPETFEVSTLSGIDLGGIAKGYSATLLAEKLKNIGVTSGVLSLGGNVQLIGSKPDGSPWMVGITNPFSPQEILFSLSLRDTAVVTSGSYQRYFETEGVVYHHILDPKTGYPANNGLSSVTVITPDGAWADGFSTALYVMGTEEALRFAKTQKDVGFILITDNQKIYVSSSLKSAV... | Cofactor: Magnesium. Can also use manganese.
EC: 2.7.1.180
Catalytic Activity: FAD + L-threonyl-[protein] = AMP + FMN-L-threonyl-[protein] + H(+)
Sequence Length: 333
Sequence Mass (Da): 36360
|
A0A917CPJ6 | MNKNRYYGTHILYRVLIKHEHLKSAMTAVLPKTIEAQDKAWIQHICYMSLRHYFSLSARWQKFLHKPLKDQLVGQLLTLSLAQKFYAQAPDHAIVHEAVNTAGMLKKSWAKGLINTVLKQSLADRDFRSGNAQQQYEHPDWWLALVKKDWPDDWTDIIRANNQPPPLWIRCRPGLTDCPGRPHAQLSNARLINDKQLPHDLLAQGHISVQDAAAQWAAHLLNPQNDERILDACAAPGGKSCHLLELNPNIQLDILEQDPQRLQLIDDNLQRLNLTARRLIQGDATEPDTWYREPKYDKILLDVPCSASGVVRRHPDIKLL... | Function: Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA.
Catalytic Activity: cytidine(967) in 16S rRNA + S-adenosyl-L-methionine = 5-methylcytidine(967) in 16S rRNA + H(+) + S-adenosyl-L-homocysteine
EC: 2.1.1.176
Subcellular Location: Cytoplasm
Sequence Length: 412
Sequence Mass (Da): 47298... |
A0A972CEZ5 | MKRIELKAYAKINLSIDVLRRRSDGYHDVSMIMQLINLFDEIKVEYKEGKEPFEISLSTDMKDLPIDKNNLAYRAAELITTYYCDDKGGKIEIHIAKKIPLAAGLAGGSADAAAVLHALNKLLNLELSLDQLKELGMKLGADVPFCVMGQAAILDFPKDQASTCAHAEGIGELLTPIKPLESWLVLSKPPVNVSTKDIYQSLNVSEIKKRPDNLSLIDGLKEENFEKITSSMFNVLEEVSESKFGEIGKTKDIMARIKGDHKVMMTGSGPTVFAISKDYLTAEKIFNEVREYNKDTFLVNTLN | 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... |
A0A972J5Z9 | MRILAIDYGERRSGLAFSDVSELLCAKAYTIKHYSDGELLDKLLKEIEENEVEKILLGLPRNMDGSEGERAEKSRALGEALKAACGLEVVFIDERLTSVEAHSILQSCGKRERKHKDKVDAVAASLILSTYLDSKR | Function: Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
EC: 3.1.-.-
Subcellular Location: Cytoplasm
Sequence Length: 136
Sequence Mass (Da): 15138
|
A0A9D5M9H9 | MQDITDNCMDRSGFTPVSRIVPDAVQEIRYHFSYNFVGAPIDGYEAPVALMTIPAAEALRRASDRIVRQGYRFKIFDAYRPRRAVRHFVRWLESDDERMKPYFYPEMDKKTLIEEEFIARYSGHCRGSTLDVTLIDMMSGREVDMGGPFDFFGLKSYSACTDGLTEAQLDGRKRLRETMLECGFHAIITEWWHYTLDDEPYPNTYFDFPVRI | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes hydrolysis of the D-alanyl-D-alanine dipeptide.
EC: 3.4.13.22
Catalytic Activity: D-alanyl-D-alanine + H2O = 2 D-alanine
Sequence Length: 212
Sequence Mass (Da): 24807
|
A0A127PPY3 | MKFLFDLFPVILFFGIFKWGEGSSDAALALVNHYLSGFVSGGVVTATQAPVLLATAVAIVATVAQIGYLLLRRKKVDAMLWVSLLIICVFGGATIYFHNETFIKWKPTVLYWAFAAVLLVSQLFLKKNLIRTMMEKQMSMPDQIWPKVGFAWIAFFIFMGCLNLFVAFNFPTATWVNFKLFGGMGLMFVFVIGQSLLLSKYIKESE | Function: Plays a role in cell envelope biogenesis, maintenance of cell envelope integrity and membrane homeostasis.
Subcellular Location: Cell inner membrane
Sequence Length: 206
Sequence Mass (Da): 23171
Location Topology: Multi-pass membrane protein
|
A0A9E2BK33 | MKDLGWRLLTIAVGLPLVLAAIYQGGVWLLGLTLLLALVAGWEFSRLAQQLYGGSWPLPAMLAGAAVILGSYAYGFSGWQLGLLLGLGWLIFWGVVRAVWGGPQKAVAALTGSLVYLLLIPSLYAFMILLREEGGRVYLLWPVVVVWGADAGAYLFGHFLGRHPLVGPLSPGKTWEGFLGGLLVAALAGWGFASQAGWQATLTVVESILLAVVGTLGDVVESAFKRAAAVKDSSRLLPGHGGIWDRFDSLAAALPLAAYFLGLWNL | Pathway: Lipid metabolism.
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: 266
Sequence Mass (Da): 28242
Location Topology: Multi-pass membrane protein
|
A0A149VT29 | MILGMSFVISNIVFPEDVVWMRQALALAEKGLFTTMPNPRVGAVVVNNGQKVGEGFHERAGESHAEVFALQQARELTRGATLYVTLEPCSHYGRTPPCVDSVIKAGIQRVVIAMQDPNPLVSGQGIARLKEHGIAVCVGVEEDKARELNIGFISRMERQRPWIRAKVAMSMDAVTALSSGESQWITHDTARRDGHSWRARSCAMLTGAGTVRADNPRLTVRSIESSRQPLRIVIDNRLDTHPDAHIYDNGHAVILTVSSVIERIAQYEKRGVKVLCLEAGENGRVAMESVVKVLHSLQINEVLLETGQRLNGVFLEAGLI... | 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... |
A0A927NKJ9 | MQQQSKVKNLNNNMTISVTQLGNFLKGLLDSEVLLYDLKVEGEISGCRQSSEVVFFVLKDQNSQIDCFCYNPPKIKLAEGQKVIVSGRPNYYVKGGKLSFFATKIEQKEQLGDKFKQFLLLKEKLENLGYFNPLRKKPIVTNCKKIGVITSSEGAVIQDILNVSRRRNPTVDIILYDSRVQGINSEQTIIHGLNYFEKTDVDNVIIARGGGSSEDLSSFNTEVLVHAIAECKKPIISAVGHETDFTLCDFVADYRASTPSVAAEICTQNVQGMLDDLTNRLKSQAVFFSSFINNKSEIISNLKKALFSQIKFVLTCKQNQ... | 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... |
A0A149VR55 | MGRIGAPYGVKGGFHVIPFTDDVDALTHYTTWWVGTEDQCAEQAVAECRVHGNGLVARFNSINDRDIIALERSKLILMPRELLPEPDPDEVYWTDVIGLKVTNLQGQELGCVDRLLETGAQDLLVVRQGSNERLIPFVEPIVVEVNVTQKQVVVDWGLDY | 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 ... |
A0A3D5ZP85 | MKLKLKTDKKTIAKRIIYDAVIPIFVLAALILADYFSKMYFETHYELGETKGEVIKGFFRFRLVHNTGAAFSFAADKPWGQTLFKIITPIAICLFIAFYCFSGRKNVFSRYALVLVIAGTLGNYIDRLAKGYVVDFLSFTLLFGYDFPIFNLADTFLCVGIIIIFIYYIFFDKTLFKDDKVAVSAPSEDLGGGEAMEKIDFGSIAEEETDEKENTTVKESGSSGKTGDMNASVNTEKRKTDGETAGR | 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-, ... |
A0A449HCM7 | MTLAEIAHAVGGRLDAVQDERATVAAATALDSRQVELGGLFAEIGGKRVDEHEFASAAMENGAVAVLATRPTGTLAIIVDDVVAAMSNLAHAVATRYTGRVLAITGSAGTTSTKDLLTQILVRHGSVVATQRSFNNEIGFPHTVLRVEADTDFLVLEMGARGRGHISHLAAIARPQIGAVLGIGSAHIGEFGSREAIAVAKRELVEALDSTGIAVVNADDPLVDAMSEHTRAQVLRFGTGPNADVRATDITLDANAREQFTLRSGDDAAPIRLGVVGEHHLVNALAAAALALSAGVEFDTVADGLDGAGLASGSRMEVTE... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Involved in cell wall formation. Catalyzes the final step in the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the precursor of murein.
Catalytic Activity: ATP + D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-d... |
A0A970EVQ7 | MGELRDYINRGDNIFLVGIGGISMCALADMLRSMGASVRGSDMRDSETVSRLRRDGIEVFIGHDPANIEGAACVIRTAAVHDDNPEIMAARAAGIPVFERAEAWGEIMGDFGQSLCIAGTHGKTTTTAMAVQIALEAGLDPTAMIGGVLPSIGSEHRIGGRDLIIAEACEYRNSFLQFRPTVAVILNIEEDHPDFFSGLDEIMRSFRRFAELVPDSGAVVANADNENVMKCLEGIGRNVITYGIENGDVRAENIEVSGGCCSFDIVHPGGLIPVTLKQLGRHNVYNALAAAASALELGIDGISIGRGLSEFAGTRRRFEF... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation.
Catalytic Activity: ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine
EC: 6.3.2.8
Subcellular Location: Cytoplasm
Sequence Length: 464
Sequence Mass (Da): 50151
|
A0A971CID6 | MSKAKENAVKKTTQAVKKPNSNEKMSTSERIAQWFRDLKSELKKVVWPTKKQTANNTFVALVVTFASAIVLWGFDSLAQVGVKTLISLVG | Function: Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation.
Subcellular Location: Cell membrane
Sequence Length: 90
Sequence Mass (Da): 9969
Location Topology: Single-pass membrane protein
|
A0A2G6GPH0 | MYSDTLFQNEKNMQKRAVLLVNLGSPSSPRIWDVYRFLTSFLNDKRVIDLPWALRLFLVNLIIIPFRVRKSSRLYSQVWTKDGSPLVFHSERLLSKIKTQTDGEFDVFWAWRYGKPGLKKTLQEIESRNYRELMIIPLFPQYASSSSGAVIQKAIEILAQMKRIPKFSVIDYFFDYEQFTDVWVSHLKEYSKKEFDHVLFSFHSLPIKQTEMMHRKGSCKTYACREQISGENRYCYHAQCYAHARLLASRLHLQPDDYTVCFQSRFAKKWLHPFTDELIVEKAKAGTEKLLVIPLSFVADCLETNVEIAQEYKDLFQKHG... | 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: 355
Sequ... |
A0A2H0USY5 | MRNLPTKIHIQNTLTGKETELPIWKNGITRLFVCGPTVYDRLHIGNARTYASFDNFVKFLRYTGIKVRYIQNITDIDDKIIKKAEEEKTTPEEIAQKYTKIFKENMRALDITSVDKYLPATDYIQEIISQVERLIEKNYAYKIEKDLTADKAGGYYFDLSKFPDYGKLAGRTIEQAEDGVSRIDENENKKNRGDFCLWKFPKTNLPLSKKKTKKPILLDGEPVWWAPFGWGRPGWHIEDTAISEKELGPQYEIHGGGRDLIFPHHEAEIAEQESVSGKKPFVQLWMHTGLMTVEGKKMSKSLGNFITVDEFLKNNDANLF... | Catalytic Activity: ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-cysteinyl-tRNA(Cys)
EC: 6.1.1.16
Subcellular Location: Cytoplasm
Sequence Length: 491
Sequence Mass (Da): 56721
|
A0A943GB98 | MTVQTLFVTLRDKLRQAQRQTGLDIDAAAEADEILRVCCGLSRQTRLLEPKRCVSSQQAAQALRAVELRERGEPLGYVLGISPFFGEDFLVRVDKDRTLIPRSDTEILVQALIDRLHPGDHFLDLCCGSGCVGLAALKNSPGTVAFGVDIDAGACRIAQKNAARMGLDARFSVLHGDILQDIPAPGIHVTSDFLGKEKEMPTDAQYHYIVSNPPYIPTPDLAALDIQVQKEPRAALDGGEDGLLFYRTILRRYRGALRAGGAFLFEIGFDQRDALFSLAALEGMRGMCLKDFAGHDRVVVLHQS | Function: Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif.
EC: 2.1.1.297
Catalytic Activity: L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-methionine = H(+) + N(5)-methyl-L-glutaminyl-[peptide chain release... |
A0A355JCB8 | MAEATQKAKKGPGKVATYFREMKSEFKKIVWPSFKQVRNNTGVVITFIILLGVFISLIDLGFTYLLSFMK | Function: Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation.
Subcellular Location: Cell membrane
Sequence Length: 70
Sequence Mass (Da): 7978
Location Topology: Single-pass membrane protein
|
A0A2V2DU61 | MHEGLPESAGALARALRSRELSAREAALACLSRIEEREGTLRAFLTVTREEALAAAQRVDDRLAAGEELPPLSGIPMAVKDNLCTKGVRTTCGSRMLEHFVSPYDATAVARLREVGGVLLGKTNLDEFAMGCDTGTSAFGPTANPVDPSRVPGGSSGGSAAAVAAGEAFFALGSDTGGSVRQPAALCGVVGLRPTYGRISRYGLTGFAPSLDQIGLLTRTVEDCAVLLETVAGFDPHDATSARPSPDGLARAVGEGVRGLSVALVRESEEEASPGVRRELLRAVRCLESHGARVDELSLPFLRDMLPAYHILSAAEASSN... | Function: Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln).
EC: 6.3.5.7
Catalytic Activity: AT... |
A0A2V2CV74 | MPDFVEKEAKTVDEAIQLALDELNIELEDADVEILEEGSKAKLGIFGGKGAKVRVTVNIPDTKIVANFLDEIINRSRSEDDYPKYVITEKEEDGVKVIKVQISGNDVSHLIGRHGETLYAMNYIASLLVNRNKNEFKRVYIDVENYRKHREETLVSIANRAAERVAKYKRPVSLDPMPASERRIIHSALQSNRNVVTESQGEEPNRCVVVKIRPYVKKI | Function: A probable RNA chaperone. Forms a complex with KhpA which binds to cellular RNA and controls its expression. Plays a role in peptidoglycan (PG) homeostasis and cell length regulation.
Subcellular Location: Cytoplasm
Sequence Length: 219
Domain: Has an N-terminal Jag-N domain and 2 RNA-binding domains (KH and ... |
A0A2V2DSC9 | MLDFNVLTIFPEMFESFIGASILKRAIEAGLVRVETHDFREFTQDKHRRVDDYPFGGGAGMLIAAQSVVDCMESLPKSAGKSISIYMSPSGRPLSTDLARELSEYDRINILCGHYEGVDQRIIDECIDMEISIGDYVLTGGELPAMVLIDCVIRHVDGVLGNDESACDESFSLDGLLEYPQYTRPADFRGKTVPEVLLSGHHANIRKWQREQALIKTAQVRPELLETARLDKKDMDFLAEKGFWKDRGEKQ | Function: Specifically methylates guanosine-37 in various tRNAs.
Catalytic Activity: guanosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(37) in tRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.228
Subcellular Location: Cytoplasm
Sequence Length: 251
Sequence Mass (Da): 28250
|
A0A970LEG4 | MKRFTSLFLALILIISFANPILASPENDSVDINVVTSTPEESIALEAKGAVLMGLENGEILFSKDANKRLYPASTTKILTALIALENGDLDEVVTVGNEAYLCPYDSSKAGLDIGEEISLENLLYGLMLPSGNDAAYTIAVHIGRKVKGDPSLPIEDALRIFIDMMNRRSRELGATNSHFVTPDGYHDDEHYTTAHDMALISAEAMKYDVFRKIVSTRMFTIPDWSSLHDPDVENETRYWRNSNALIQPNDQFYYAHANGIKTGYTSKAMHCLVTSASKDGMELLTVVLGSSKNGKWTDSTALLDYGFNNFERYEPFSNG... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors.
EC: 3.4.16.4
Catalytic Activity: Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanin... |
A0A970ZCL7 | MSSYQALYRRWRPRTFSEMVGQDAVRRVLRQQVQDGQISHAYLFCGTRGTGKTSAAKILAKAVNCLNPQQGNPCNACALCTGIEDGSVLDVVEIDAASNNGVDSVREIREEVLYTPAVARYRVYIIDEVHMLTGGAFNALLKTLEEPPPHVIFVLATTELHKIPATILSRCQCFLFARIPQEVIAGRLMEVARDSGIALAQEAAELIARLADGALRDALSILDQCAVGGGRIDVPLVEQVGGLTGRGYLFEVSQALAARQLQEVLRATGHMLAQSKDPSVLTGELLTHLRDLLIYKLVEDPGELLSAPPSEFGQLAALAG... | 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: 553
Seq... |
A0A970JM71 | MIKLRTTAPAKINLTLDVLDRRPDGYHNLSTIMHQVPLEDEIEVMIGQGEGIRATTNLPFIRAETNIAAKAARLFIDELGKLVRISEKNTGILIDIRKRIPVGAGLGGGSANAAAVLKLLNEYFGSPFDEKSLVDIGARVGADVPFCLIGGCALCEGIGEIMTPLARIPSCYIVIVKPRASISTAQLFSEYTVAKSQVRPDTAGAVNALKAGDLCGISSRVFNVLEEVAVKKIKGISEIKRVLMRNGALGASMSGSGSAVFGIFDDKGAADSAASFFEKSHSQVFMLRCE | 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... |
A0A061GZW3 | MLSLSLAIPTVNTLSPPKPKPKSSLVQTASNQTEIFPSRVFVPNRFGYKLQAATTDVANGKISVAGEFSEEEEELPEGLNKELMPKHVAVIMDGNGRWARQRGLPTSAGHEAGVRSLRELVELCCRWGIQVLTVFAFSSENWIRPKVEVDFLMSLFERALKSELETFSRGGIRISVIGDSSKLPTSLQELIHEVEETTKDNSRLQLIVAVSYSGKYDVVQACRSIAEKAKHGNIQLEDINESLIERELETNCTEFPYPDLLIRTSGELRVSNFLLWQLAYTELFFDQQLWPDFGKDEFVEALTSHQQRQRRYGGRHS | Pathway: Protein modification; protein glycosylation.
Function: Catalyzes cis-prenyl chain elongation to produce the polyprenyl backbone of dolichol, a glycosyl carrier-lipid required for the biosynthesis of several classes of glycoprotein.
EC: 2.5.1.-
Sequence Length: 317
Sequence Mass (Da): 35804
|
A0A970IP33 | MSFFGKLFGNENEREIKKIEKIADEIEALESEIQVLNDDELKAKTLEFRQRLVQGETLDDILPEAFAVVREASKRTLGMRHFRVQLIGGIVLHQGRIAEMKTGEGKTLVATLPVYLNALEGKGVHVITVNDYLATRDSEWMGQIYKFLGLSVGLIVHGLDSGERQQAYKSDITYGTNNEFGFDYLRDNMVIYREQMVQRELNYAIVDEVDSILVDEARTPLIISGVGEKSTNLYFAADSFVKTLKRGEDTKEESRSELLSQYWDGSPDENEDDIKKKGDYTVDPKAKSVLLTDTGVAKAEKFFGIENLADPDNMEIQHHI... | Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide c... |
A0A352SY46 | MKFILIALIAYFLGNISFAYILGRVFEKKDVRDYGSGSAGATNALRTFGKKIAAMVLCGDVLKGIVAVLIGRAMGGQAGAYLAGAFAIIGHNWPVMLKFKGGKGVATTVGVMLFVNPFLTLICVAVGIIIIVSTRTVSIGSIIGMASAPIVAVVFVRPFDLKLFLFCVFIATMSIYRHKSNIKRILEGKENKI | Pathway: Lipid metabolism; phospholipid metabolism.
Function: Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
Catalytic Activity: an acyl pho... |
A0A924AB30 | MVNEPFIKRCLILAQKGLGMTAPNPLVGCVIVHNNTIIGEGWHQEYGKPHAEVNAIENVEKKYGSAILKKCKLYVSLEPCVHYGKTPPCANLIIKKQIPEVIVGCRDSFSLVDGKGIQLLKEAGIKVTEGILEKECQFINRRFFGFHENKRPYIILKWAETSDGYIGSTKSKIQISSNAASVLLHKWRTEESAFIVGTNTIINDNPSLTSRLWKGRNPIRIGIDIKLRANNNSEIYNGKADTIIFTALSIKDNCAKVKFIKINESEDVSELLTKLYENNIQSVVVEGGRQLLESFIKHGLWDEARIFKSVHTNKGADIKA... | 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... |
A0A061F7S7 | MERKSTKGFRMCFLCACMLLFILGASAAADNITPNQSIRDNETLVSGDGSFELGFFSPGNSTKRYLGIWYKVSPETVVWVANREAPLANHFGVLNVTNQGTIIILDKKPSIIWSSSGIRTAENPVVQLLDSGNLVVKDGNDSGSENFLWQSFDYPCDTLLPAMKLGKNFVTGRNWSLTSWKSPNDPARGQFSALIDPQGFPQLVVRNGSVILYRGGSWNGKRFTGTPDLEQVESSNLFKFEFELNKNEVYYKGEPYSSLLSRLVVNQSGFLERFVRTKQSNLWAGIYSAPRDECDYYAVCGVYAICITGNSPLCACLDDF... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
EC: 2.7.11.1
Subcellular Location: Membrane
Sequence Length: 825
Sequence Mass (Da): 92338
Location Topology: Single-pass type I membrane protein
|
B5ID06 | MASTIRIVFFGTGGSWPSPERNVMSIGVQIDSEVLLFDCGEGTQRQMMHTNMSFMKIKRIFITHYHGDHFLGLAGLIQTMTLNERKEPLEIYGPERTIDILTKFLNIGYYSPSFKIVLYELKGNESLDFGDYVVKVMKTKHPVPSLAYAIKEKDMPRIDRNRAKALGLNSKILEKLRKNGKIEYEGKEITIDEVSNGVRVGRKIVYSGDTAPMEEMISFAANANVLIHEATVESSLEEQANQYGHSSARQAAKIAKKANVDALLLVHISPRYKDAKIIENEAKKIFPNSRVMNDFDEFIVKVKKVQSS | Cofactor: Binds 2 Zn(2+) ions.
Function: Zinc phosphodiesterase, which displays some tRNA 3'-processing endonuclease activity. Probably involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA.
EC: 3.1.26.11
Catalytic Activity: Endonucleolytic cleavage of RNA, removing extra 3' nucleotides from tRNA pr... |
A0A971VZH7 | MKIILAEHSGTCFGVKKALEVAERFADSNLNVYTLGPLIHNKQVVERLDKKGIRVIDTLDSIEGGTVIIRSHGVPPEIHGQAAGKVVELVDATCPFVRKIQEKVKEYYGKGYQIIIIGDAGHPEVKGVNGWCNYSAIILDKPEDAEKIGYFEKLCVVAQTTITSGLWEEMKSVLEKKGDEIKFFNTICSATSMRQQAAVELAGKVDVMLVIGGLHSSNTQKLYKLCKENCKNTYHIETADDLPLENIKGAESVGITAGASTPDWIIKEVIDKMTEMDKMKQQETNEQTSEEQMLEQAQGVEETTGSLEGNGPEEATAEGV... | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Pathway: Isoprenoid biosynthesis; dimethylallyl diphosphate biosynthesis; dimethylallyl diphosphate from (2E)-4-hydroxy-3-methylbutenyl diphosphate: step 1/1.
Function: Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of is... |
A0A943GBU5 | MTNRQGIMRALLWYLCAALAVALDQISKYAATQFLQGKPSVVVIDGALSLTYATNRGAAFSMLSDHRWVFLSLSAIAIVAILVVIWIFRRSHALFGIALGMILGGGVGNMIDRVAQGEVVDFIHVTFIDFPIFNVADCFITIGCVFALFYFIFFDHKQAKPILFEPKNVTDDVSMATSNNGKNVHQNDVPNDVPLDKNSHATISVKTNVETEKTIETQSAHSSHMDSNTHIDLAMQDGVDHTANIVKKADAQPEKNTPPERDDCCGEVHGTDEYESDGVHR | 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-, ... |
A0A927W5D4 | MRNILLTIAYDGTDYAGWQRQPGQMTVQGEIEKALSKICGQDIKIDGCSRTDAGVHALGQRATLRGDFAIPAERIPRAVNGLLSPGGPYSVGAIRILQAKEMETPEFHARFNCVGKTYRYCIETGGMPDPFRRNMAYFLEKPLDLAAMQRGAELVIGHRDFKSFQAAGGNEVPDTVRTIFDCRIWQQPSAGMAGQLQRTAEGTAANPAGKWQDVPGQSLILEVTGDGFLYHMVRNLVGTLVEMGQGRRDPEEMTSILEACDRRRAGHTAPAGGLFLKQIYYSREAMEHGVEATRAAAEQSTFLR | Function: Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
EC: 5.4.99.12
Catalytic Activity: uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA
Sequence Length: 304
Sequence Mass (Da): 33411
|
A0A352A966 | MNKIMENNKISTESMHKSLNVLNVVQYSGLFCANRSMGFNNACIAIGNFDGIHKGHDVLIREMIEISKFNNLNSMILTFKYSDKSMRKSSTNMKYITSFKNKISILKSYNPTNICYIDLDSEISKYSPEKFIKDILIDKYDMKHVVVGYNFRFGHYAFGNTDTLKKYSSECNYDVSILPKIQSKNGLDISSTIIRNYLKDGKIKEANELLTKNYTIFSNDVKFTSNNNCIVSENSEILTPCDGEYKVLVGDKKCTVCISTVDNNRVLTFDSDIKTVSLCEPGENIIFLNK | Pathway: Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step 1/1.
EC: 2.7.7.2
Catalytic Activity: ATP + FMN + H(+) = diphosphate + FAD
Sequence Length: 290
Sequence Mass (Da): 33025
|
A0A1H6Q7V5 | MIEHIFFALGTVKSIKIYDKNSKNYEPLLKHIQERIEYISSHCNFYDDQSDLSHINQQAGESYVTVDQDTYMIIREAKAYSVQYKGFFDITVGSLTRLWHINTNNNEMPLKQDIDRAILKINAQDILLKEDNQIALAHHGQAIDLGSIAKGYCVDLTKELLIKAGVTEAIIQYGGSVAVIGKKKKVGIQNPFKSQGEIMGYIETDACVVTSGTYEHYFMHDNKRYSHLFDLRTGYPIETDMMSLTVVTSSALLGDVLTTVYFNKGVIPRDEDVCVIMNDGRYYLSESLRKEFYAR | Cofactor: Magnesium. Can also use manganese.
EC: 2.7.1.180
Catalytic Activity: FAD + L-threonyl-[protein] = AMP + FMN-L-threonyl-[protein] + H(+)
Sequence Length: 295
Sequence Mass (Da): 33586
|
A0A316QIP1 | MKLLNTAEIGTNQKELEIFIDHEAFEAECEKAYRKNVAKFNIPGFRKGKAPRKMIERMYGTGVFYEDAINAILPSAYPEAVKEAGLEVVSQPEIDIKSLDADGVVITAKVYVKPEITVKEYKGLKATREDVEVTDEAVQTEIDRVRERNARAIEVSDRPAAKDDEVIFDFDGYVDGKPFEGGKAEKYSLKLGSGQFIPGFEDQMIGKSIGEPFDVEVTFPEDYHAKELAGKAATFKCLIHEIKVSELPALDDEFAKDVSEFDTLDEYKADVKAKLQESANKTEDAKVDDQLMSALCENIEGEIPEVMFENEAENLVRDYE... | Function: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
EC: 5.2.1.8
Subcellular Location: Cytoplasm
... |
A0A943IY34 | MRIVPTIKITDDVNKLRIALNRFSKYNIDTIRFIVTKHSLEEHIEFIKLAQSIYVEINDKEFKLMLDIPCPKDKLRFDFMNNEDSVSFQEGEIINIINSRDVQEHEGKKYFFVAADFKNRVPETAIIGDGELLLKLTTISEKIITAVCMNSATIKKGKAIASPTGFLKITDVSITEKVLKIISVLHPEICVLSYIENAEDINNFKMTIYEYAGYIPHIMSKIECQKAVDNAESIVDNSDSIMIARGCLAVNVGIENMIESQDTAILESRKKYKEVCIASNILRSLNSQNWPSRADIADLSYMIIKGVNYFVITDGYCMED... | 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: 340
Sequence Mass (Da): 38900
|
A0A355V316 | MKLEKIVVASGNANKIREIKQIFSNAEIIPMQSLGFDGDIPETGETFKQNAEIKAKFIAEKFCVPALADDSGLCVDALGGAPGVYSARFSGGGDEENRRLLLKKLENENNRSAHFTSAVCLYLPDGTKYFGEGETHGQILFKDTGSNGFGYDCIFYSDDLKKSFGIASAEEKNKVSHRYRALCDLAAKLKKD | 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 ... |
A0A1W1YXU5 | MHRFYTDPARSSGDLVFLAEEDARHALSVLRLKAGQAVEVFLEGQRYDAEITSADRDGVCVKLLSQLPSTEAALSVTLYQGLPKSDKMDFIVQKAVELGVTRIVPVIMSRCVVKLNPKDASHKLERWRKIAREAGKQCGRCITPEITEPCTLSSLPSLPAFPDVNIVPWEESEGHGPLAFSRSHPGLSSLGILIGPEGGIDRDEIAVLNQSGFIPVTLGKRILRTETAGLAAVASLMALYGEME | 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... |
A0A1G1R579 | MNIAALIIGGLVGTLLRYFMGQWMPNLHNGFPIGIMLINFIGCFFLGWLFTVSTGLWHIHQEIRLGLGTGMTGAFTTFSTFTVQSVWLMEHGSQLIAISYILMSILGGIVLTITGVRIANIQLNRKNEVSS | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Subcellular Location: Cell membrane
Sequence Length: 131
Sequence Mass (Da): 14433
Location Topology: Multi-pass membrane protein
|
A0A943WX61 | MRYFLLSVFTAVLDLTSKEVVKNKMPVGQKKQISKKVFLWHIKNKGLAYNKFENDERKVLAVSSLAVGAVGAYLFSLIHRNAGALEKTGSALLLGGGIGNLVDRIKNKNVTDFIYVDFKKAPIFNVADIAALFGGILVVFKAMIDEI | 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-, ... |
A0A942RR27 | MLVAQKRQQQPSFYDQQRTKRKTGVHRQQKLSIAVKKLKMFAVVFIFALASVALITHYTYMIQVNYQIERSLDELNSLQKAQQHLKLEIASLRSPDRLERIALEEIGMKYPDQDQFIILTAGVQ | Function: Essential cell division protein.
Subcellular Location: Cell membrane
Sequence Length: 124
Sequence Mass (Da): 14463
Location Topology: Single-pass type II membrane protein
|
A0A970EYT5 | MDTEKKRIGLFGGSFNPPHNGHVAAAQYAFRSLKLDMLLVIPTSLPPHKDLAKGSPSSAHRYRMTELAFEGMENVEVLDIELRRSGRSYTADTLKEIRRIYPLAEIFLIVGADMFLTIQDWYRPDEIFRTCTICALCRQRGQLAELLEHRDFLAGKFGADCIVLENREVEVSSTEVRKAIMSNGNTDLIPDKVMEYIRENRLYGCKGSDGRTGGSDVKPFPEHIDLSDPNLLDQFRQTDLYRKAISYVDPGRRAHVDGCIIEAVRLSNRWGEDPAKAAVAALLHDVTKSLGREEQLKLFEKYGIIPRTADTLAFGPLHAI... | 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).
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NA... |
A0A7C7EHZ8 | MTIKRYLAKDMNEATTRIKYELGSNAVIVSSRWIRKKGLKGLFSKKVLEVTAAVDQNQDKSDQNTSGLVHTQQTNTPLKSSKELELEREIEELKKMVNSLLEKEKSRKKGGRKTQFSTIMQQHLKKMDLDEKIIKDFAEFCKREGNSSIGFDEASRYFTDLLEKSICPIENVEEKIWAFIGPTGVGKTTTIAKIAAKETLENRKKVGLITMDTFRIGAVEQLKTYADILNLPIEVVSTRNEMSDALKKLQACDLILIDSTGRNSKIKEQLMEAKECLSAASKTYNILVMSATTRSLDLKMILNNYEVIGYDSIILTKLDE... | Function: Necessary for flagellar biosynthesis. May be involved in translocation of the flagellum.
Subcellular Location: Cell membrane
Sequence Length: 369
Sequence Mass (Da): 41755
Location Topology: Peripheral membrane protein
|
A0A3D2FX77 | MNVLVTGGAGYIGSHACVELLNAGHSVVVVDNLVNANAECLRRVERITGKTLEYHEMDLLNRAALNELFDTHRFDCVLHFAGLKAVGESVQQPLRYYNNNLGTTIHLCQTMAAHGVKKILFSSSATVYSPDNTMPVDESARTGGCTNPYGWTKYMSEQILSDTAKADGEWSVMLLRYFNPVGAHPSGLIGEDPRGIPNNLMPYIAQTAAGRREYLSVFGNDYPTPDGTGVRD | Pathway: Carbohydrate metabolism; galactose metabolism.
EC: 5.1.3.2
Catalytic Activity: UDP-alpha-D-glucose = UDP-alpha-D-galactose
Sequence Length: 232
Sequence Mass (Da): 25342
|
A0A972AL14 | MMDTLALVVQKFELFLLLLARCSAIFIASPIFGRRNIPAAFKIGLSLFMSIILLNVVKETPVLAGSILQLAVLIAKEVMVGLVIGLVTYIVFTALYFAGEIIDMKTGFGIVNVLDPQSNTQVPIMGNFLYIFTLILFITIDGHLMLISALARSFDIVPATRMQVTASSVAEFVSILNSTFVIGFKISAPVVAAIMLTDVALGILSRTMPQMNVFMVGMPLKILLGMFMLMIMIPAFAVIIEVLFRNTADSIYRVLLQL | Function: Role in flagellar biosynthesis.
Subcellular Location: Cell membrane
Sequence Length: 258
Sequence Mass (Da): 28233
Location Topology: Multi-pass membrane protein
|
A0A972CD45 | MKFIDEFKNFAFKGNVIDMAVGIVVGGAFSAIVNALVTYIIMPLISYGTAGLDFTDMKIVLRPAAVVDGVEVAECAIGYGQVIQSIIYFLLVSLALFIVLKIIFNFRSKVNAAAGAAATALKKPAPASAAPLQPQTSPEQAQAAADQAALDAASKAASIEAREANIELLLSEIRDLLKNQSNNQSANNS | Function: Channel that opens in response to stretch forces in the membrane lipid bilayer. May participate in the regulation of osmotic pressure changes within the cell.
Subcellular Location: Cell membrane
Sequence Length: 189
Sequence Mass (Da): 19862
Location Topology: Multi-pass membrane protein
|
A0A972EGM3 | LHLIGPLGFSIEEKQVKRAGLDYWDMLDLRYYNSYNEFLEKNPDAKIYYLTTKSEKKYSEIEYPKNDCFIMFGKETAGIPEKILNQNRDNCVRIPMLNSERARSLNLSNSVSIVVYEVLRQHNYPNMK | Function: Could methylate the ribose at the nucleotide 34 wobble position in tRNA.
Catalytic Activity: 5-carboxymethylaminomethyluridine(34) in tRNA(Leu) + S-adenosyl-L-methionine = 5-carboxymethylaminomethyl-2'-O-methyluridine(34) in tRNA(Leu) + H(+) + S-adenosyl-L-homocysteine
EC: 2.1.1.207
Subcellular Location: Cyto... |
A0A927NLU5 | MNIVYFGTPDFSAKVLASLINSEHKVVAVVTQTDKKVGRKQILTECPVKILAKQYNIPVFQFEKIRKEGFEPLSKLNADVFITCAYGQIISKEILEISKFGTINIHFSLLPNYRGASPVQWALINGEKEIGVTIMRTDEGIDTGDIILSDSIKVENEDNAETMLNKLADLSVPLVLKVFKQLEDNTIKYIKQGDNFTYYPMLKKEDGKIDFNKTSRDIVGLIKGLYLWPNAYFYFNDKQVKVFKAESVDFIGGNINGEVVCANKTGLIIKCGVGYLKVLELQIEGGKRLDYKSFLNGNKIEIGKVLV | 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... |
A0A2M7T118 | MNTELMETIKLTGAVGGFPEFLPAQQRAADEIISIIKTQYESYGYTPLETATVEKIETLLAKGIAAKEVYGLRRLNAEDGEGDKELALRFDLTVPLARYVVQNQNELVFPFRRYQIQPVFRGERPQKGRYRQFHQADIDILGQETLPLSADAEVIACATQTLAAILPKGEEFILRINNRKLLQGLVAWAGSADIPAAIKTIDNAEKVGWPKTIEGLIQTAIAAPKAEDLAALLQASNLENLTKLGLSGEAEEGLTELQTVLSLAKTLLPPALHGNLKADLTIARGLDYYTGTVVETVVASAKELGSVCSGGRYENLTASL... | Catalytic Activity: ATP + L-histidine + tRNA(His) = AMP + diphosphate + H(+) + L-histidyl-tRNA(His)
EC: 6.1.1.21
Subcellular Location: Cytoplasm
Sequence Length: 444
Sequence Mass (Da): 47916
|
A0A927RM79 | MSQNKERDQEFQEFLRALKDKNDIVEVIRSYVALDRKGGNHWACCPFHHEKTPSFAVNESEQFYHCFGCGVSGDVLRFVREIESTDFMGAVRILAARAKMTVPENNFDTEKAQEMKKKRDTLASIMLDSARFYLGNLYSGDSRADVHLQYISKRGLSPTTVKKFGLGASLDFYSLPEYLQDKGYTRQDLLDSGAVSEAKNGKLVDGLAKRLIFPIINAFDEVIAFGGRRLEQSDFGKYLNTRDTMLFNKKKTLYNVNLLKKLKREQTIKDVIIVEGYMDTISLYQAGFKNVVASMGTSLTKEQARLVKRYTENVYISYDG... | 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: 605
Domain: Contains an N-termi... |
A0A7C7AB04 | MFYYIIRAILIPFLFLLFFPKITGKENLPKEGSVIIYSNHTSFLDPILLGCVLPRRIYFMAKQELFRFPPLAYIIRALGAFPVKRGTADITAIKKALQTLKEGKVFGIFPEGTRSKSGDLKDFNHGIAAIAQKSRAITIPVIIKGNYKVFRQVRVIIGKPLDLHEYYGQKPNSELLTKMSDYMTEAIKSLASESENN | 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: 197
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):... |
A0A2V2G5Z1 | MLKHVGCIAFLGSTPYFFGDFMDKNIFTIDSDCSGMTVKEYILGYLGYSVGVLKKLKYSGKITVNGKEVFVNHVLSCGEILQLIYPEENSDSIEPVYHPLDILYEDENYLAVNKPSAMPVHPSLYHVSDTLANAVMYYYRDRSFTYRVLTRLDADTTGVVIIAKNMCAASKFPSSGVEKKYLAICCGVPEANEGIIDAPIGRIGDSIIKREVRSDGKNSITKYRLIKENNGKSLIGAVPVTGRTHQIRVHLSYIGCPLYADYLYGTEIAGERPRLHCESVVFTDPFTQIKREITAPLPEDFFIR | Function: Responsible for synthesis of pseudouridine from uracil.
EC: 5.4.99.-
Catalytic Activity: a uridine in RNA = a pseudouridine in RNA
Sequence Length: 304
Sequence Mass (Da): 34013
|
B5ICY4 | MLEKELNLQFFHKNGWKRYKCKKCGVYFWSKVPRETCTEAPCGEYEFLKEPIFSREFTVESMRRSFIEFFKRNGHEEIKRYPVVARWRDDVFLVNASIYDFQPHVTSGLAPPPANPLVISQPCIRMVDVDSVGKTGRHLTGFEMMAHHAFNYPDNPIYWKDETVEYALKLIEELGGEPDNVVFKEKPWIGGGNAGASFEVIYGGLELATLVFMNLKEDDNGDIELNGTRYSEMPVKVVDTGYGLERFVWASKGTPTIYDAIYPEMISMLEDRIGISRNDRKNEILRQFALLSPRIEIENENELINEVLKATRASMKEYKE... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.
EC: 6... |
A0A972AEZ7 | MGDAVYEALARSYIVANSQSTVGRLHLDKLEIVNASAQFRAAKVIFDYLTEDERQIFLRGRNAHNAHIPKNKSAEEYRYATALEALFGYLYLSGKTDRLYILFDIIMRDINERKDNKKENE | Function: Involved in correct processing of both the 5' and 3' ends of 23S rRNA precursor. Processes 30S rRNA precursor transcript even in absence of ribonuclease 3 (Rnc); Rnc processes 30S rRNA into smaller rRNA precursors.
EC: 3.1.26.-
Subcellular Location: Cytoplasm
Sequence Length: 121
Sequence Mass (Da): 14006
|
A0A1W2BCK3 | MRHFWQGEWVGDEAVALRLDTLDDRTQQVITGPRLNPLVVLAAAEKLDLEQHRASLVSWGLDEVEVDETLDALRHALSRDSLERKLKRELGNLDPARMVRFDFRTPTYEAWVPLGLLAHVTAGNAPAAGVLSAVEGLLSGNLNVIKVASDDSGFTAEVLAALASHDQTGQIAARLVVLHFSSSRTDWMTRMLGAADAVAVWGGEEAITGVTELVKPGARVIDWGPKLSFAYLTRDSWSDVDTLRALAADVCRLEQQACSSPQVIYLDTEDSSQVFAFAERFASVLEQAGPPTREPSQAEWAEITNTVLVTQLEEHLGFTK... | Pathway: Lipid metabolism; fatty acid reduction for biolumincescence.
Function: LuxC is the fatty acid reductase enzyme responsible for synthesis of the aldehyde substrate for the luminescent reaction catalyzed by luciferase.
EC: 1.2.1.50
Catalytic Activity: a long-chain fatty aldehyde + CoA + NADP(+) = a long-chain fa... |
A0A971VS45 | MDIKIIPRALTGKVKAISSKSDAHRLFFAAAAAEEETSIVINGKAGEDILATINCLKALGAEIHERKTDADETEYTVIPAGRVESDILPTLDCGESGSTARMLLPLATYISPKGFKMTGRGRLPERPMTPLIDELIKKGCEFTSKSIPLEVKNTPAGGVFKIAGNISSQFISGLLFLLPLLPDGGIIEIDPPLQSAGYVDMTVKTLSLFGVKVERNDNRITVKGGQRYISPQKAYAEGDWSSAAFWLCAAALNGSITVTGLDAESAQKDKYVFDILSRMGAKCSQTDGEFTISANSLKGTEIDASEIPDLVPVLSVVCAA... | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7.
Function: Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-ph... |
A0A356B0H6 | MTRLRRYMTEALIEAKKAYSIGEIPVGAVIVKDDQIIARAHNTVEQNNNPTHHAEMNAIEAACAALGYRSLHDCEMFVTLEPCPMCVGAIMQARVGKLYFGASDETAGAVVTKIDLLDKHFGNRKTQYDFPVMEDESKNLLTGFFKEVRSKFSLNDGTNVYKLSGMYFDNDTVLLSKTLLGAYIIRNLNGERLVAKVVETEAYCGIDDKGSHTYGDTRTNRTEIMYGHPGHAYIYLIYGMYNCLNLVTRPKDIPSCILIRAVEPVEGLETMSQLRYNKPYEELDKKKRIGLTNGPGKLCIALGLSREQNGLDLTGDELYI... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the deamination of adenosine to inosine at the wobble position 34 of tRNA(Arg2).
Catalytic Activity: adenosine(34) in tRNA + H(+) + H2O = inosine(34) in tRNA + NH4(+)
Sequence Length: 363
Sequence Mass (Da): 40970
|
A0A9E0BZW1 | MQDEFQQTGPEHQSFNLKQFLYEKVIHYWYIYILSMVVVLIIANFYLWYATPVYTSTTSVMLGMDDKKYANEDLLAQLGSIENTGSIESQMQIIKSRNIITRTIQQLDFRFSYYLEGDIKTSELYKNCPFELVVDSSIISQNFPNLTLKATSISKFELNYVNPKNNSSQTVNGTFDTPISTDLGTLTFVLKAPKLLKFYKNSLDSKNLYKIYSNTSEDLVRSYSQRLNVSQIKGTRMLLISVDDAVPQKGCDFLNKLTDVYLVYGVEQKNEDSRNSLRFIDGQLDVINNDLLKSEGKLEEYKTENGFVDLLNMTGLIQSD... | Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
Subcellular Location: Cell inner membrane
Sequence Length: 807
Sequence Mass (Da): 91597
Location Topology: Multi-pass membrane protein
|
A0A3C1A559 | MPEIILENNQDKLAIEDDIRETIERVILKTLEVENCKFDAQVSVTIVDLAEIRRINRDMRNIDSETDVLSFPMLEFDENRNMIEDDYDLDDGKLLLGDIVICAERAKSQAEEYGHSFLREMAFLTVHSMLHLLGYDHMEKEEEKEMFSRQEDILNILGIKRGGV | Cofactor: Binds 1 zinc ion.
Function: Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.
EC: 3.1.-.-
Subcellular Location: Cytoplasm
Sequence Length: 164
Sequence Mass (Da): 19107
|
A0A095XHZ9 | MNIVFMGTPDFAAVSLKKLIESGHNIDLVVTQPDRRKNRGKKIICSPVKELAIANEIPVIQPVKLRNDEEAKEKLRKAHEKADIGIVVAYGQILPKEVLEMPRKGYINVHASLLPKLRGASPIQTAILYGDDPTGISIMKLEEELDSGPVYSKVEVDIEGRTAGELESHLAEIGAELLVKTLSEFDDINPEVQNHSDATFCGIIKKQDGHIDFSKSAAEIERMCRAYDPWPGTFANIDDKTYKFWKFELADATKNSGCSLNSDNSSSDGAKPGEIVYVDDDSFVIACGSDGVERIRVLEIQAPGKRRMRTDEFLRGNKII... | 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... |
A0A356AUI4 | MADKVIKKGDNKNVAKKKASLRFFKDLKNELKKVTWLSWPKLVKNTLTVIAACLVIGAIIWIFDAAIGSIVKWSILR | Function: Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation.
Subcellular Location: Cell membrane
Sequence Length: 77
Sequence Mass (Da): 8698
Location Topology: Single-pass membrane protein
|
F8ACH6 | MTEEEILAFFRKKSKPVHREVICGIGDDCAVISRGSFWELLTTDTMVENVHFDFAYFDPYFVGRKLAAVNLSDIAAMGGEPAYALLNLSVPGISERELPLFWEGITTKLANYGAEVIGGDVTRNPERWHLTLTLIGHAPSGGVIFRQGARPGDLIFVSRPLGASAGALELWQQGFEPPESLKRAHLDPEPEIRLGKVLAQENLASAMMDISDGLLLDLARLCRANSLGAEIEAEKIPVHEALNEVSLSQEPIFYALSGGEDFALLFTVPPEKERFLRLKLGSQRLFQIGYIIEEQIIYLIKNGQKEKVSPSGFDHFA | Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine diphosphate from thiamine phosphate: step 1/1.
Function: Catalyzes the ATP-dependent phosphorylation of thiamine-monophosphate (TMP) to form thiamine-pyrophosphate (TPP), the active form of vitamin B1.
EC: 2.7.4.16
Catalytic Activity: ATP + thi... |
A0A971KL48 | MLDIHKRTWAEVGVSAINYNYGRIRKLVSENCKICGVVKANAYGHGLVEVSKMLQAYGCDYLAVACLDEAELLREKGIKLPILILGHTFPDFIERVADCDAIQSLFSLETAKEYSRILEKAGKSLKVHVKLETGMGRLGFDAKNGVDDICRAISLPKLQAEGVFTHFAVSDEPDGGEYTKKQFESFMSAVSQVEEKTKKPFAIKHCANSGAILNHPEMWLDMVRPGILLYGCYPKERSEVLPITHSMEFKTRVSHIFDLEKGESVSYGRDFIADKKMKVAVLPVGYGDGLRRELSGKIDVIVNDRRCPQIGRICMDSCMV... | 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: 375
Sequence Mass (Da): 41881
|
A0A970XHE1 | MYDFFEGTVAAKTQEAVVLEVSGVGYELFVSKKTLARCPRAGERMKAFAHLSVRDDAMVLYGFASVEEREMFKKLIAVTRVGPKLALSILSIMGPSELAIAVMTGDVAALIAVPGIGKKAAERIVLELKEKVSHSLQEAGQEPVFAEVGDAAGEAVRALVSLGYSPPEAAAAVSKADQGGADPEQIVLAALRKLGEKI | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an ... |
A0A943RZ11 | MNGKVIAFEGIDGSGKGVQIAEIARRLKKLKNEVLVQDFPVYSSFFGREIGKMLSGEHSVRADIVDPKSMSLWYALDRYESLKNLNKMDYDYVLFNRSTLSSAVYQSIRIGEDKRDEFIQWLFELEFDKLGIWKPDLYFIFDVTEEQSKKNVAQKEQRSYLKSKYDVYEESQDIMNQARNVYLRQARRYDNIFIVPCMDDKGNFKSIDEIASYVMEKILNSYV | 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: 223
Sequence Mass (Da): 26200
|
A0A2M7D7A5 | MPTKRQKQILDFITSFKKKRGFSPSLEEIKRHLKLSSVSTIHFHIKRLKEEGYLDKGENRPRSILVYESQQMVKIPLLGSIAAGQPIEAIQEKEIIAVPKTKLPRSGNLYALKVIGNSMIDENINDGDVILVKEQSTADNGQKVVALIDNHEATLKTLYKEKRQIRLQPANKEYEPIIIKNGEREIIIQGLVIDVIKNEILSPEIKERFEIEKHFKKFEKLPLNKIICGDAVEELKRLPNNSIDLIIADPPYWKVINEKWDYKWRTENDYIFWCKQWLKELSRVVKKIGCFYLFGYFRTLSYLLPEIEREGFSLRQQIII... | Function: Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually ... |
C1AE20 | MMSRSHGWVAALLSVLMPGLGHLYAGRALRAIAAFILLQVLGFGLVYLTLVASTAPLRVVLIVLLLAGFLAVVLDAARVARRDTSEPRRRVQRWYVLLPVCLGVGFIVQPWIFGLTKRHIVEAHRFPGGSMAPTILPGDYLLSSPRAPNPVTRGELVVYQASGQRNIHRVVGLPGDTISMRDFQFIVNGTLAHEPYAHAEDGSGSLTDPQFEWQRGHLRDRTDAAGYQATYGTWGPLVVPDGAYFVLGDDRANSFDSRYRGFIATDALVGRPVWIYFSRDPDTGIIRWSRIGLGVGA | 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: 297
Sequence Mass (Da): 32590
Location Topology: Single-pass type II membrane protein
|
A0A2G6PI77 | MSSSQRILVTGGEGQLAQALRWVLAQGTEGGAQWIFPTRAELDITRPSSVAAALREHQPRWVVNTAAYTAVDRAEQEPERAMLVNATAVDYLARAVRRHNADTGMDTRLLHLSTDYVFGSGGNRPFREDEVPHPQGQYAVSKRQGELRALSSGIATVLRTSWLYSPFGHNFYLTVRERLRQGQELRVVYDQVGTPTSALSLARAICSLVADARCTPGVLHYADLGIASWYDFACEIRTLTGGPEILPIRSENLKQPAPRPAFSVLDTQRARGELSLTARHWREALRECHQATG | Pathway: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
Function: Catalyzes the reduction of dTDP-6-deoxy-L-lyxo-4-hexulose to yield dTDP-L-rhamnose.
EC: 1.1.1.133
Catalytic Activity: dTDP-beta-L-rhamnose + NADP(+) = dTDP-4-dehydro-beta-L-rhamnose + H(+) + NADPH
Sequence Length: 293
Sequence Mass (Da): 32449
|
A0A2M7HDB5 | MSALIIGGGGYIGSSVAYYSHARNWDSVIVDNLSTGHADLAANAGCLLVEADLRDRQKVFALLQKCKPDIVLHFAARSLVAESVAAPSMYYGNNVVGTINLLDAMLASGVQNIIFSSSAAVYGIPHEIPITEEHSLLPISPYGWSKMMIEMMLADYSRAYGLQYVSLRYFNAAGAIPGAGIGERHEPESHLIPNILRSMLRKDGKVFEIYGNAYSTADGSCVRDYIHVEDLARAHIQAAQYLLDGGESTAVNLGNGKGYSVLDVIESAKRKLGSNIPYNIKPPRSGDPAVLVASAEKAGRILDWKPLWVSLDDIIGSAWE... | Pathway: Carbohydrate metabolism; galactose metabolism.
EC: 5.1.3.2
Catalytic Activity: UDP-alpha-D-glucose = UDP-alpha-D-galactose
Sequence Length: 327
Sequence Mass (Da): 35499
|
A0A356MIU2 | MKLLLMGPVGSGKGTQAALISEKYNIPHISTGEIFRWNIKNNTQLGQLVKPYIEKGELVPEDITFEMVEDRLSKDDCRNGFILDGYPRNIQQAHALDTITTLDKVIMINISEDIIIARLSNRRMCSQCNQPTRVEWLVDGKCEKCGGEVYQRDDDKPEIIKNRLEKQDISKEMIEFYENKGIFYSIESTNVVEKTFALIDEVIKK | Pathway: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from ADP: step 1/1.
Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Catalytic Activity: AMP + ATP = 2 ADP
EC... |
A0A8D8CXN6 | GTCVWFPVYGLHHDPKYYPNPERFDPERFNDENKRNINLGAYLPFGSGPRNCIGSRFALMEIKAILYHMLLKFSCEQSENTQIPLQLEKGLSNLATERGLHVNLRLRSDVK | Function: May be involved in the metabolism of insect hormones and in the breakdown of synthetic insecticides.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 111
Sequence Mass (Da): 12837
Location Topology: Peripheral membrane protein
|
A0A315ZAI3 | MVKAASFESGYLKVSSTHQIYFEEVGNPLGTPVLYLHGGPGAGLPNNYHSYFDLKRCRVIGMDQRGSGRSEPLGCLEENTIQHLVEDINVLREYLGLTDWVLFGGSWGCTLALAYALKYPENVRGLFLRGVFLGTNKEIQWFYHKGANLFYPEEWKYFDIRSEEAINSSSNLISQYYYDLCLSDKPIYEKKEIARRWIFWEVRLAMFEGSECAKEEWIITDELLAFAQLEVHYFYHSCFFPYQNYILERLSLSDLKEVPTTIVQGRYDLVCPPRYAFDLHQKMTASKLVWIEKGGHASYEKHTKFKMIEEFKLLLDKVQY... | Catalytic Activity: Release of N-terminal proline from a peptide.
EC: 3.4.11.5
Subcellular Location: Cytoplasm
Sequence Length: 325
Sequence Mass (Da): 37999
|
A0A316LQZ0 | MTQENFRKKKKYGQNFLVGDTVVRKIVAGSGITADCGVLEIGPGAGALTKELLGAAGRVLSVEIDDELIPVLQSRFGSDDRFRLIHGDILKTDVAALLREHFDGMPVCVCANLPYYITTPILMLLLEGRFGFRSITVMVQKEVAARLCAGKNDGCRGAITLAVQYYASVRRLFGVPAGCFSPPPKVDSAVVRMDPYPVPPVDTGDEKLFFTLIRAAFTQRRKTLLNALSAVFGDRADKTRLAAVLAEAGLAPDIRGEKLGIEEFANLTKKMININLKTEEHHV | 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(+) +... |
A0A928RPH7 | MFLDRVKISIKAGNGGKGSSSFLRTKLTANGGPDGGDGGRGGHIVFKATNDMNTLYSFRFKKKFVAENGEDGHQKNKTGRMGKDEVILVPTGTVLINPKTDKIVADLNQHGAEFIALRGGNGGHGNAYYKSSVKQAPTFSQMGEVVEQKEIILELKTIADVGLVGFPNVGKSTLLSVISNANPKIANYPFTTIYPNLGVCEVLGETFVVADIPGLIEGASQGLGLGHYFLKHVERVRLIVHLVDISESEGRKAEEDYEIINKELASYSADLPKTKQIVVFSKCDLIEEEELQAKVKSFVKKHKIKDYLCISSYTRDGVED... | Function: An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis ... |
A0A3R7WQ57 | MFGQITEQFQTIFKNIRGLGKITDKNINETVRQVRRALIDADVNFKVVKSFVAEVEEKAQGTKVIKSINPGQHFIKIIKDELISLLSSEGSNLNIDGKPAIILLAGLQGAGKTTTAGKLAFKLKEEGRSVLMVAADVYRPAATDQIAKIGKQVGVSVFRGQGKDPLKICIDGIKEARSLKNDVVIIDTAGRLHIDKDMMKEIQEIAYHSQPNEILFTADGMTGQDAVKSALAFHEAVPLSGVVLTKMDGDTRGGAALSIKKITGVPIKFIGVSESFEGLETFDPKRLADRILGFGDVVSLVEKAEKIFDREKAEQMNRKI... | Function: Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Binds to the hydrophobic signal sequence of the ribosome-nascent chain (RNC) as it emerges from the ribosomes. The SRP-RNC complex is then targeted to the cytoplasmic membrane where it interacts with the SRP recept... |
A0A3D1XBL8 | MTDKNVSPELSAAEFSKLFRKALEMNGLEEVLSTEKAESDFYTLARLLLDFNSHTNITAITDTKGLILAHFVDCLTVAPLIPRGASVADIGCGGGFPTIPLAIVRPDIKIHAIDSTQKKLNFVSSAANELGLRNITPLCIRAEDGANDPLMRESFDFVTARAVSALPVLCELCLPYLKNGGTFCAMKGPRGAEELAASKNAVRKLGGAVCSAKKLSLIPPAGGDVLERMLILINKVSPTPECYPRAYGKIKNKPL | Function: Specifically methylates the N7 position of a guanine in 16S rRNA.
EC: 2.1.1.-
Subcellular Location: Cytoplasm
Sequence Length: 255
Sequence Mass (Da): 27328
|
A0A9E2G4T1 | MLNEWVEVSLPVTTEQEDEVAALFVWAGAMGVEVRDTTTLFAEDRGTTRVVAYIEQGTEKAFMDLLNPVLAASLDQPEEELAERFRMLPITRQEWNEFWKKTFDVQRIGHFVIRPSWKEVVPEPGDTVFVIDPGMAFGTGLHATTRLVMEAIEQLHASGFRPTRILDMGAGTGILSMAAASLFPEARIWAVDNDPDAVETAAEVIANNGLSDRIQVGLSWSEAPVDLVLANIQRDVLLELNPLFQRNLDPGGRMVFSGILNDQIDEIREKTNLPVVRNWHEGEWELVVFEKPATGG | Function: Methylates ribosomal protein L11.
Catalytic Activity: L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
EC: 2.1.1.-
Subcellular Location: Cytoplasm
Sequence Length: 296
Sequence Mass (Da): 33026
|
A0A7C6XQ45 | MNIGLISLGCDKNRVDSEKVLYYLKENGFNITNDLNNADALIINTCAFIDEAKEESISVILDSIEIQKKNNIKIVLIGCLASRYFEVLKKEFPTINIVCLDRYENILEVLQNENPVFLSCNNKSLKYEKTSFDLVNIGRVSTTPKHIGYLKIADGCDNFCSYCAIPFIRGRYRSIPLEILIEEAKFLQNSGVKELMIIAQDTTKYGIDIYGEYKLRDLLNELIKLNFWKIKILYAYPELIDDKLIKFISENEKIAKYIDMPIQHINDDLLKSMNRKITKKEIISKLRMIKSINPNIAIRSSFIVGYPGENKAKFLELYEF... | Cofactor: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein uS12.
EC: 2.8.4.4
Catalytic Activity: [sulfur carrier]-SH + AH2 + L-aspartate(89)-[ribosomal protein uS1... |
A0A971AHY6 | MKILIKNVRIITMDANMNEYDQGCIGVEGAVIAYIGGEEQLPQDFKADKVIDGKGMLALPGFVNAHTHSAMSIFRGYANDIPLMEWLSEKIWPMEDRLMPGDAYWLSLLSIAEMIMSGVTVFADMYMFMDQTAKAVARSGIRAVLARGLQGPDPKAEQRLAENRRLWEEWNGQAEGRIRIMVGPHAVYTCDREYLEKCMDLAQELGAGIHIHLAETRHEVEECRRKYGKTPVEYLEGLGLFKHHTLAVHCVHLSREDMDILKDNGVHVVHCPISNLKLGSGVAKTVDLVDKGINVALGTDSAASNNSLSIMREMNFAALL... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the deamination of 5-methylthioadenosine and S-adenosyl-L-homocysteine into 5-methylthioinosine and S-inosyl-L-homocysteine, respectively. Is also able to deaminate adenosine.
EC: 3.5.4.28
Catalytic Activity: H(+) + H2O + S-adenosyl-L-homocysteine = NH4(+) + S... |
A0A7C6XU49 | MGIIDYGAGNLHSVAGALKQLGVSFVVSGDREELDSADALILPGVGAFPAAMEKLGSLGLVDFIRASAERKPLLGICLGMQLLLSMSHEFSDTEGLGLLPGEVARLSAADCDSRFKIPHMGWDLISPDMSDPLMKGLGSSAYVYFVHSFKAVPDDESDISAFCRYGEPIASVIHRGNVWGTQFHPEKSGERGMKILKNFCSMV | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 5/9.
Function: IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisH subunit catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the synthe... |
A0A927S9C1 | MTRITNDCHVHSNYSEHPSVDKTSPWLNMEKAVELGLERLYFSEHVDMDYPYQEETNVEYDPCVNMQAYYENLKKMEEAYRGKVRPMFGVELGLMEGNLDKIREYIKGYELDQVLASIHTLHGVGPNFHKAPAWEGWTKSTVQQLYLETMIRLSKEYGDFDCVTHITYYSRNCPFEEKEFYYNEAPDHYDALFKMLIESGKGMEINTSAYRKFGFFLPGLEILKRYREMGGEILTIGSDGHGKDKIGLDLDLAGEMAKEAGFTYYTIFESRKPRFIKL | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 8/9.
EC: 3.1.3.15
Catalytic Activity: H2O + L-histidinol phosphate = L-histidinol + phosphate
Sequence Length: 278
Sequence Mass (Da): 32422
|
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.