ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
|---|---|---|
A0A8J5QXG4 | MTEELSGVTIVVFIAAGVLTILLLFIFAKRQIMRFALRSRRGPHISIGQDAKKSLKRELERRIQVIPRIQHEPQLISDPRHDPTEFTDEEYQVYSRLHLKLIDAARLLKSYPSSRKSSPSRTPIKKNVETKRNILEPRMRPPEEQVLSGSRPNTLTVMALDNTETSV | Function: General regulator of phagocytosis. Required to uptake Gram negative bacterium by macrophages.
Subcellular Location: Golgi apparatus
Sequence Length: 167
Sequence Mass (Da): 19182
Location Topology: Single-pass membrane protein
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A0A7V2WSR1 | MVPEFKKSHAFTIGVELEFQLVDRESLALVPLAPRILESLSDQWKDRIKKEFIQSMLEVNTGVCHTIDDVAQDLRVVTLHLEQKAHEQGALLHPTSLHPFSRALDQQPTQDPRYLEILEDLRLVGQMLITQGLHVHIGVPDGDTAIWIVDHIRAYLPLILSLTASSPFFQGIDTGFQSYRSKLFEQLPRSGIPASLGSWDEYVRLCNMLMEGGIISDVRDIWWDVRPHPYFGTIEVRIGDLPPTFKEILAITALIHALVVYISRNRNLPPPPHRLIIANNKWQAARYGLNGTFVNLDVKTRLTQREAVTHLLARLEDIFL... | Function: ATP-dependent carboxylate-amine ligase which exhibits weak glutamate--cysteine ligase activity.
EC: 6.3.2.2
Catalytic Activity: ATP + L-cysteine + L-glutamate = ADP + gamma-L-glutamyl-L-cysteine + H(+) + phosphate
Sequence Length: 368
Sequence Mass (Da): 41979
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A0A5N9BTM8 | MSNVSRVFIGVDLGDKRIGLSKSDPLGLIASPIKTIPSVNIDKDIQNIVEFANECEAQKIIIGLPLLMSGEKGFQANKASDFVKLLSDNTSIPVQAEDERLSSKEAENILSFNRQKLPTKNKPLDSYAAAIILQRYLDKINRG | 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): 15714
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A0A1H1XW44 | MTSTDPGSTKTFDDLFAELAEKARLREPGSGTVARLDAGVHEIGKKVVEEAAEVWMAAEHEDKDRAAEEISQLLYHLQVMMLALDLEPTDVYRHL | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9.
Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-ATP + H2O = 1-(5-phospho-beta-D-ribosyl)-5'-AMP + diphosphate + H(+)
EC: 3.6.1.31
Subcellular Location: Cytoplasm
Sequence Length: 95
Sequence M... |
A0A6G1YPJ2 | MKLTDATRDYYRKLAKNAGYRSRSAYKLLQLNRSYGIFRPRHAVVDLGSAPGGWLQVAKQQIGVDSLVVGIDTKQVQPLEGVTILRGSIDDAKIIDTVLKLIGGRADIVLSDLSPNVSGIWDLDHSRQISLTRSALAAAIKILKRRGASVFKVFEGELLNGLKEELKNHFQRVYINKPKASRQRSSEQYIVCFGFEPDLCLDIQDHT | Function: Specifically methylates the uridine in position 2552 of 23S rRNA at the 2'-O position of the ribose in the fully assembled 50S ribosomal subunit.
Catalytic Activity: S-adenosyl-L-methionine + uridine(2552) in 23S rRNA = 2'-O-methyluridine(2552) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine
EC: 2.1.1.166
Subc... |
A0A5N9B1L7 | MIYTVSQIQKIHNQLNVPGDKSVSHRALMLSSIALGPSHICNLSFGKDVLSTIKCLKSLGIDISYPKNCSNTLTNCVEIVGKGLTGLSRSAKPLNAGNSGTTLRLLSGILSGQNFSSIIFGDKSLNNRPMKRIIDPLTLMGAKISGRDNNQFAPLEIEGTSLNPPDTMELKVASAQVKSSIILASLISQKKTIIIDPFTTRNHTELMLKYMGVDISQNNSRITIIPSQPKPNNIIVPGDISSATYWIIAACCHPNATIKINNVGINPTRSAILDILKSMGANINISNIKNISGETIADISANSSNLKAIQINHQIIPNII... | 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... |
A0A1Q2D6K9 | MLVKHLMQQNNKYHWWQSDTLVLVAVSGGVDSMVLLELLLQLPEGERPIIGVAHINHKLRTESDDEAHAVQLFCEQHGLPFYLKEWHAGTIITENVEQAARQVRYEFMQQIMEMAGYSVVLTAHHEGDQAETILMRLISGYRLPYLMGIQQTRSFYSGKLVRPLLTVSKSDLYAYAQLHDIPYFEDESNRTTTYFRNRVRHNYLPALANENPQAVQHFIHLGEEVQAYYDVVEELIQPIYASIVQTDSMSWIINVSEFQALSASFQYVISQKLVIELIQAGIVVSQQVEVSLRQLLLSDKPNHTILLKNEWVCQRAYTEA... | 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)... |
A0A1B1BGM6 | MAHNPLAPEWLSSPADANTLTDGLWPSSARRTDDGAITIGGVSAGDLAAQFGTPLYVIDETDARTRAAQLRAAFDAEFARIGTTVRVYYAAKAFLSTEVARWMVEAGLNIDVCSGGELAVALAAGVAPGRIGFHGNNKSRAEINDATRVGVGTIIIDSPVEIERVAEAAGRHGMVQNVRLRVNSGVHAHTHEFLATSHEDQKFGVVFEDAPALVAAIRAQPSLNFLGLHCHIGSQIFGVDGFAESASRLLSLQADLLAGGPVPELNLGGGFGIAYTSVDDPSPVADLAAALADIVAAECARRGIPVPVIAIEPGRVIIGP... | 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... |
A0A1Q3EBM9 | MRHSSILNLHRASNKFRQKYKEPAQRMASSPYPTRTYLPGQFVVSAGSILFRRAPENGELQMCLLYHTIKNEWLLPKGRKDCGESMETTAVRETYEETGYKCKLSPCNMSTRAPAHGVHTKDMIREAEQITEPIAITVRDQGLDGVKIIWWYISELDGDGQKVEGTQMDTESFASQFIDAEEALRTLTFKGDQDIAAKALEIGYEISLQTAIMHIFPKVYVVYYTNSDSEDRQPRSLDELKEKLLKWVNDRAFHFRRRADNFTGATKVRLSGLGAELNKVTGYEEIDALKRQVVEQEARIETTRQAARAAKFNHDEAVVR... | 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: 539
Sequence Mass (Da): 61534
Location Topology: Multi-pass membrane prot... |
A0A0Q4B6Y0 | MEVYKFGGASLRNADAVRAMCDIVRTVPHAHRLVIVVSAMGKMTNALERALDAALHAPEQLQEAVEQIATFHRSMVEQMSADGQGDYSAALQQLADLEILLSHLPNPGFDQVYDLVVPYGELISSLIVAAYLKEQLSVPVQWVDIRTVFRSNSVYRAATVNTAISEPLARQAFSSERPCIFVTQGFIAQGPEGTTTTLGREGSDYSAALLGAFLQAKAVTIWKDVPGFLTADPALFPNASLLPELDYREAIEMANSGAKIVHPKALKPLQNACIPLYVRPFNQPNEQGSAICNLALHDGNPLTQIAIREGQVLLSLSPTD... | Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 1/4.
EC: 2.7.2.4
Catalytic Activity: ATP + L-aspartate = 4-phospho-L-aspartate + ADP
Sequence Length: 436
Sequence Mass (Da): 47688
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A0A1Z5HTJ0 | MYGQGLLKGLGITLKHLFGKAVTEQYPDQRPNLSPRFHGSFALDVEKCIACGICAKACPNNVIKIASSKGENKKRRLDDYKIELGYCLFCGLCVESCPTDAINFTQDFELASYTRQDTVLHLYNRASHETDGSGESDLACCQGTEG | Cofactor: Binds 2 [4Fe-4S] clusters per subunit.
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 (fo... |
A0A5N9CC36 | MSDITSIKDVFRQTEGMLRGVGIDDAFTEARILLQHVLDVDGAGFLLRLDDSLDPRVKNTIDEVVRRRLRREPLAYIVGHIEFYDIDVIVDSRVLIPRPETEILVETALDWLRERHGNPYIVDVGTGSGCVAVTIARHCPQANIVAIDTSRDALEVAMQNIDHYELGGRIIVRHDDLLRNHELPIDLLVANLPYIPTEDIHGLMPEVRDYEPRSALDGGSGGLHIIQNILLQARDFISSTGALIFEIGFGQAAEAKALALRHFPFAEIRLINDFAGVERILAIHLVDDENP | 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... |
A0A7X7ZAQ2 | MSKILITGGTGYIGSHTVVELMESGYDVVIVDNLSNSTTAPLEGIKRITGRKPEFVEADCSDPKQMRTLFERYPHIRSIIHFAALKAVGESVEKPLDYYRNNILSVINLLELLGKRSGNFVFSSSCTVYGQPDILPVTEESPIKKALSPYGNTKRIAENIIEDTVAAMGNINAISLRYFNPIGAHPSAEIGEYPVGKPDNLIPFITQTVRGVWEKLQIFGSDYNTPDGTAIRDYFHVVDLAKAHVVALERLLESKNRKPYEIFNVGAGRGITVLEIVNTFEKVIGQKVNYEFTGRRAGDIEKVWADTTLAEKELGWKAEK... | Pathway: Carbohydrate metabolism; galactose metabolism.
EC: 5.1.3.2
Catalytic Activity: UDP-alpha-D-glucose = UDP-alpha-D-galactose
Sequence Length: 370
Sequence Mass (Da): 41373
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A0A2Z3YPM2 | MADPTADLSLSDVTSGEPGRPGRPGDPGVPGGTAVSRTVSGAPDDRGTGGLTHVREDGSAHMVDVTGKNETSRTAVATGRVRTRPDVLDMVFADDSEGLPKGDALPVARVAGIMGAKKTPEIIPLCHPLPLGKITVDFRREDAATHGADAVRIRASVKTRGVTGVEMEALTAVTTAALTVYDMIKAVDRHGVIDDVRVLAKSGGKSGSWDVRDAPADGWGDGSVSGPTDGPVSGPVSGPHGEGA | 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... |
A0A1H1WXE3 | MQTAYPVHDIRRLEEAAIAADPRHDLMQAAAGALAAVVAGELVERRGAVYGARVLLLIGGGNNGGDALFAGALLARRGVAVRALPVLGTPHPAGLAALRRAGGRILEPLAVDEQAETVPQGCDLAVDGVLGIGGRPGLPDRVAAVLDRLNDLRVPIVAVDLPSGVDADTGAVPGAAVTAAVTVSFGAAKPCQLIEPARSRCGRVVDVDLGFGHDDRLTRISALDEDDLARDWPYPGVTSSKYTRGVVGIDAGSDSYPGAGILAAHGAVYAGAGMVRFHGAEESRRVLTGALPNIVYGDGRVQAMLYGSGWGDRPDGADVI... | 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... |
A0A8B9F9L4 | MAALALRCAGQRRLLARLSPSFCVPHVVPMGTTAKEEMSRFWEKNTKSNRPLSPHVSIYKWSLPMAMSITHRGTGVALSLGLGHGEGLQDPAGEPVRGAGAHPDPAVCCGPRGHVKAPPACSILSHLRSCRRWGGAGPEWGYPKGKALPCSSVVDDQSSFVPPPPPGCFCALLCPELQTKLGLCPTGVGSGQASPLSSPGEPELPMPALPQGWGVVLDGVLSPAVSILLLILQNIPIQTALGGRAPRFPPFGMQDASTIPALCRVSPSQ | Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
Subcellular Location: Membrane
Sequence Length: 269
Sequence Mass (Da): 28105
Locati... |
A0A938HUD4 | MDRALELARRALGGVGPRPAVGAVIARGRDVVGEGATEARPGRHAEVVALEAAGERARGATLYCTLEPHAHHGVSPPCTEAIIRAGVTAVVSALQDPSPAVNGAGHRRLAEAGIRVVTDVPDRQRAEASELIAGFAHLTATGRPLVTAKYAMTLDGKLATRTGKSRWLTGAQARARAHELRAAHDALVVGIGTVLSDDPQLTARVPWAAEFKESRPRLRVVVDSRRRLPATAALLGTGGPVLWAVASPTGEDAPAGVATATLPGDHGKVDLGALLDVLGKRGATTALVEGGAALLGSFFDAGLVDRVAVFIAPAIMGGAG... | 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... |
A0A931JZK7 | MGTQSYGHRVLVVDDSAFMRKAIPMLLANEPGLEVVGTARDGQDALDKIRQLQPDAVTLDIEMPVMDGLTALAKIMAMPDPRPVVIVCSTLTTKGSHEALKALRLGATDFITKDPQAIGGSQESFRSDLVGKLRAVLEHRPRRALGVVKTPLPIPTTKPVTLPKQAPTSFSLGSREFGLVLIGSSTGGPPILETVIKRLPQRFSAPVVVAQHMPALFTTSLATRLNEECQVRVEHADSSRPLERGVVYIVKGGMHGVIRRQGGYSLEITDRPTDALYKPSVDVLLGSAATPAGKDALGIVLTGMGADGAIGAKRLHECGG... | PTM: Phosphorylated by CheA. Phosphorylation of the N-terminal regulatory domain activates the methylesterase activity.
Function: Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate resi... |
A0A0Q4B8C1 | MNVQSMFGRIAPRYDLLNHLLSLGADRGWRRRAVACASQLPHGAVLDLACGTGDLTVALAEGLTPQRLVAADFSAQMLELAQRKMARLLPGREVELRRCAAEDLPFGEGEFDLVTIAFGVRNFASLERAMRECCRVLRPGGHLVVLEFTLPGSRVVRGLYGAYSATVMPLVGGLLSGSFSAYRYLPRSIRSFARSGALPRAIGASGMPIVRAECYTLGVVELVVARKPQ | Pathway: Quinol/quinone metabolism; menaquinone biosynthesis; menaquinol from 1,4-dihydroxy-2-naphthoate: step 2/2.
Function: Methyltransferase required for the conversion of demethylmenaquinol (DMKH2) to menaquinol (MKH2).
EC: 2.1.1.163
Catalytic Activity: a 2-demethylmenaquinol + S-adenosyl-L-methionine = a menaquino... |
A0A7X2KEB9 | MRFPPEFLDELRNRVPLEDVIGRHVRLQKKGREFVGLSPFNKEKSPSFTVVPSKGFYHCFSSGEHGDVISFLMKVEGLTFPEAVEKLAGEAGLRMPEQSPESRERSRQAADQRDILEQAADWYAQRLFAPEGRTALTYLRERGLSEETIRRFQIGFSPDSRDALKSHFLQQGQTERALVAAGLLINPDEGGRQTYDRFRGRVMFPISDLRGRIVAFGGRALGDGQPKYLNSPETDLFHKGRNLYGGDLARKAAHDKATVIVTEGYMDVIALHAAGFTGAVAPLGTALTEEQLDLLWRMADEPVLCFDGDKAGQRAAARAL... | 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: 602
Sequence Mass (Da): 67530
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A0A1H1DHJ7 | MVRATLLGVFAVPSGSMEPTLRPGDRVLVWRPADDLASIARGDLVVFDGTGSFDPWVDRGPLGSAWAGLAGSLGLPGGPPGYVKRVVGLPGERVACCDGQGRLVVDGEPLQEPYLAGGGPASRTAFDVVVPPGRLWVLGDARDASADSRAHLGDPGGGTVPVERLVGRVVAVAWPLHRATLLDAQDSAPGRNAP | 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: 194
Sequence Mass (Da): 19940
Location Topology: Single-pass type II membrane protein
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W5J4A6 | MACHDSPPTTTTTASTRGAHEGDKVPSVDLFEDSPANKVNIADLCAGKKVILFAVPGAFTPGCSKTHLPGYVEKATDLKSSGATEIVCVSVNDPFVMSAWGKQHNATGKVRMLADPAAVFTKALDLGADLPPLGGLRSKRYSMVVEDGVVKSLNVEPDGTGLSCSLADKIKL | Function: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events.
Catalytic Activity: [thior... |
A0A1V6HKB6 | MDALVYPSFVKGEVNAPPSKSYTIRAIAAAMLAAGKSTIINPSSCDDALAMLNIAHSFSAEIKFNNQNLEIQGGLKSNPEIIYCNESALTARLMIAIAALSENKITITGSGTLLKRHLGNVNDPLEANGVKFTSNNGFLPVSVQGRLKPGYYLVDGSESSQFISGLLMALPLLNNDSQLIVNNLKSAPYLKMTLEVLRAFNVNIETKGTDVYLISGNQAYCPQNFIIEGDWSGAAFPIIAALLNGEIDITGLLPHSLQADKKLNTILEDIGIKTVCANNKLHLKKSEIPAFVADCTHTPDLVPALVILASQSAGKCRITG... | 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... |
A0A522VTN8 | MLRWVGLSLLVLVLDQLSKLWIDQHFELHESLNLLPVFNLTYVRNTGAAFSLLGDAGGMQRWLFMGLALLASGVLARMLWQLEAGRYWQAVALSLLLGGAVGNLIDRIVYGYVIDFFDFYLGAWHFAVFNVADSAITVGVAMLLIDAFFFGEETA | 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-, ... |
A0A014NJZ7 | MNPENITLLGTKTEYIQHYTPSILEAIPRSLNREEIGIKDNAPLPFSGTDLWTAWEISWLNDKGKPVVAIGEFFIPASSPDLIESKSFKLYLNSFNQSRFPDAEHVSALMKKDLSDVAGAPVELKLYTDINSYNNHITNLPGESLDGLDIAIENYEFDASLLKGSTSPSGEIVSETLHSDLLKSNCLVTNQPDWGSVIIRYEGSKIDREKLLRYIISFRNHNEFHEQCVERIYSDIMLYCQPAKLTVFARYTRRGGLDINPFRSNCEQNLLSARLVRQ | Pathway: tRNA modification; tRNA-queuosine biosynthesis.
Function: Catalyzes the NADPH-dependent reduction of 7-cyano-7-deazaguanine (preQ0) to 7-aminomethyl-7-deazaguanine (preQ1).
Catalytic Activity: 7-aminomethyl-7-carbaguanine + 2 NADP(+) = 7-cyano-7-deazaguanine + 3 H(+) + 2 NADPH
EC: 1.7.1.13
Subcellular Location... |
A0A1F9QWD1 | MNLFLEVTGKRKNGYHTLSTLFAKINIYDVLDFKFANGGKPILEIVDEFHACRLSAGPDNLVMRAAKAFYRSFRIGVGVHITLTKRIPMGAGLGGGSSDAAGTLLGLAQFFQIKLTAARKKKLHDLGVELGADVAFFLKDSPFCLATGIGDRLRPMKIPRSLPYMVLAWPGFPSPTGPVYKALAARRRPDILTRLSQLDKLVRRLKRGRPVDEWGGLLFNRLEQAELPVLADVAQARRIMEAAGVEGVRMSGSGSSVFGFVSSHAEGERIVRRLRVYPWKVFLTSCLG | 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... |
C5E4M9 | MKLDIKKTFSNRSDRVKGIDFHPSEPWVLTTLYSGRVEIWNYETQTEVRSIQATDSPIRSGKFIARKNWIIVGCDDYRIRVFNYNTGEKVVDFEAHPDYIRSIAVHPTKPYLLSGSDDLTVKLWNWEKNWALEQTFEGHEHFVMCVAFNPKDPSTFASGCLDSTVKVWSLGQPTPNYTLTTGQERGVNFVDYYPLPDKPYMITSSDDLTVKIWDYQTKSCVATLEGHMSNVSFAVFHPTLPVIISGSEDGTLKIWNASTYKLEKTINLGLERSWCLATHPTGKKNYIASGFDNGFTVLALGKDVPTLSLDPVGKLVWAGG... | Function: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membra... |
K2KYL0 | MDASTTITLPAPAKLNLFLHITGRRNDGYHQLETLFQFLDVGDRLRFQPRSDQQIELLDDSGIATDDNLVMKAARLLKHYAEQHQQPVTGVSIGLQKLLPAGGGLGGGSSDAATTLLGLRHLWQLSISDTELRQLALSLGADVPIFIYGQAAFARGVGEQFFPASPACPWYLVAKPNDLHIATAELFQHPDLPRQTASIDFADWYFANSHNDFQQLVCQRYPEVAKLLSWLLEYAPARLTGTGACIFGSFATEAEARAAHAQLPANCSAFVARGLNQSPVIDALANAAGAS | 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... |
A0A8B9F2D1 | MRSSWRESHLQVGPGPQNLPCLPTYTAKDHTTYSKRATELRNITRANLANGLYRSSGGPSGLSICMYSKLNHLPEALQILNNRPIGKMETPLMRMTTPNLQIKPLTVAETLTYWEIMEGALAPYRATLDAAGLYSLQMHSLNIRGICVIDTGIGVYIPSGYFGLIAPRPALAIKGIQILGGITDSDYQGEIKVILLNSGDQDILIQTGDHVAQMLILPVLKM | Pathway: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 2/2.
Function: This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA... |
A0A5N9AJP6 | MIKNRNILVAIVGPTAVGKSNLAIRLAKSLNGEILNGDSRLVYRQMDIGTDKPSLANRSEVKHHLIDILNPDDTYNLSLYLDQARSIVDDTNNMDKVPFLVGGTGQYIWGLIDGFRSPNVAPNNVLRYQLQQKAQDQGSIALWNQLELVDPLSASKIDYRNTRRIIRALEVYLGTGIPISQAQNKNTNLYESLIIGLTMDREHLYNKIDSRIDQMIANGWIEEVKHLLGQGYSPDMASMYSIGYRDITKHIEGQMDLDDTISKIKTDTHRLARSQYAWFKPTDPRIQWFDASGESSYELILQMAISHISKSTHGDVIIS | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
EC: 2.5.1.75
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylall... |
A0A5N9FXH1 | MAFPDKLEKNHQQKSYFNSPTKYPQRDRGSYNSTVRSQELILFMKIVFMGTPYFAIPVLDAISADGHDIVAVYTQPDRTSGRGRKVTMSAVKEHAVSKNFQVLQPGNFQADPSQIPILADFKADIAVVAAYGTLLPSEILDMFPYGCINLHPSLLPKYRGASPVSTAILEAEKVTGITIIQLDSGMDSGPILAQKEAPIGEGTLCNELTEKLFYIGADLIVETISNLAKGVIKPRQQDNENATYTKKLVRKDGLIDWKDRAGVIWRKIKAHHPWPGSYTHFNGKNLKIIEARISENYKLGPGCVSIHDNAVYIGTSDDSL... | 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... |
B1NS71 | FFNKKTNRNLLDGQNVETAWTIIPVFVLILIAMPSLRLLYLMDEVSDPSITMKTIGHQWYWSYEYSDFSEVEIDSYMLPLDEMASGMTRLLEVDNRAMLPMNTQVRILVTAADVLHSWTVPSLGVKVDATPGRINQTSFFMNSPGLFYGQCSEICGANHSFMPITIESVSTKTFLKWI | Cofactor: Binds a copper A center.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreducta... |
A0A2A2R6J0 | MPLYLVMGVSGCGKTTLAQRLAETVGGTWLDADNFHSPGNRAKMAAGIPLTDEDRWPWLEALNEELGRAESAGETLFLACSALRQIYRDRLARGLSSLKIIYLQGSIELIHSRIAQRTGHFMPATLLASQFALLEEPTDALILSVDQPVEDMLREFVRALY | Pathway: Carbohydrate acid metabolism.
EC: 2.7.1.12
Catalytic Activity: ATP + D-gluconate = 6-phospho-D-gluconate + ADP + H(+)
Sequence Length: 161
Sequence Mass (Da): 17833
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A0A3P1SKR4 | MRLFLSIDPPRTVREAIHSCCPALKQIKLEPAEQLHLTLLFLGEQPPTTVDLIEQASQYLTTAPFELRLAGVGQFRSGIIWLGVQPQPALMKLQQKLSQRLTNDGIDLETRVYHPHLTLARSRKPLRNQQLRAFLDTFQDRSFSFQANSILLKQSQLYSTGARHECLAEWHFS | 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: 173
Sequence Mass (Da): 19819
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A0A6V8L1B4 | MVTEMVGSGRCVVAVDGPSGSGKSTVSRRLAAALDASYLDTGAMYRAVTWAVLQSGVDPHDADAVIKVAGDIELAVGTDPQAPHIQVNGTPVDRSIRGPEVTGAVSAVAAVPWVRQLLVAEQRKLIAAAPRVVVEGRDIGTVVAPDADLKVYLTASADARARRRSAETLADVAATAADLHRRDKLDSTRAADPLQQADDAVVLDTTELGIDEVVSRLLALLDWRVGRDLRRARAGRARDHRPGAGGRRCRPPQRRQVHARQPHHRPPPSRRRGHPGVTRDRVPYDAQWSGRQFTVVDTGGWEPDAKDRAAAIAAQAEIAV... | Catalytic Activity: ATP + CMP = ADP + CDP
EC: 2.7.4.25
Subcellular Location: Cytoplasm
Sequence Length: 796
Sequence Mass (Da): 85035
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A0A202DGG8 | MGLKEFIQESKRVLRVTKKPTKEEYKTIVKVSGLGILAIGFIGFLITFVKQVVLG | 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: 55
Sequence Mass (Da): 6153
Location Topology: Single-pass membrane protein
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A0A9D9K7Y4 | MSEHTFDRIELSEDEILALLRSLRHKDGNWIAWGKACYQLHKAGYDPQNIFEETGFETAVQNQVIVAAQVYDSIVKEGVSDAVRAYCEGPRSDVLYEFRVLNQTQRAEAVELAWEKQLDIDSAHDVTRAVKAIDRLSKLPEGFTRKPGDAVAYQCWRQARQKKDLAERTRPIARGLKFAQTAGARLQLETLLSEISAPPQRKAPLLPLYRVDEELELPRIVPVAGTLPLSASAMESVPQVESIEPFRVTTVASQTVCVPIPGWQAVLQAGDPVALFTHSADLPNAPEGSDEMMLVLVDRSDRQWNPNSYFLAETGNGLEI... | Function: A major RuBisCO chaperone. Acts after GroEL-GroES chaperonin to fold and/or assemble the large subunit of RuBisCO (ccbL, rbcL). Cooperates with RbcX in RbcL folding, plays the major role in assembly of dimers into RbcL(8)-Raf1(8) intermediate complexes. RbcS replaces Raf1, leading to holoenzyme formation.
Sub... |
A0A1Q3DWS4 | MEFFNDVGADPLKPSLFELVAQEQLRDLLQPALKYVLSVFAQRYPRYLLRIVNKHEECYALFMLVVERHYLRKHGASFSENFYGLKRRRRPYIEPERAKAATGGVPEAEKLRSREIRRSLLFLVGLPYLRAKAQDYYEELGGGANSDILDEGMDARQLRALTDQSYKGWLRRAFKAAYPWLNTSFEVWLLICADLVLKTLGQQVYPQGQKYLKLNQKASYSGSVV | Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Membrane
Sequence Length: 225
Sequence Mass (Da): 26078
Location Topology: Multi-pass membrane protein
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A0A1H1PFB7 | MINNTVGELAELIGARVVGEGDLQAPVGDLVYDSRSVSPGSLFVAFLGERVDGHDYAVRAWQAGAVAAITQRPVAGGLCLVVDDPQTAMGLIGRHVVAAAKRGGLRVIGITGSAGKTTTKDLLAQILERAGSVVAPRESMNNEIGLPVTASWVTTDTQFLVSEMGAKGIGHIGYLCSITPPDIGLELNVGVAHLGKFGSQDAIAEAKGELVEALPADGRAVLNAGDPRVWAMAGRTTAPVLGYAVEGDRLPDGVVPEVYASALAADDLDRWAFELRIGDRTMPVRLRILGRHQVGNAVAAAAAGHAAGVDPQLIADTLSG... | 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... |
A0A5N9GK61 | MRDGLSIAIDGPVAVGKTVVGRALAARLRYRFLDTGVMYRAVTWVALGRDKLAHTSAEQDLVDIAMHLCIDILGHPHEQQVLVDGADVTDSLRSLAVERKVSSVAQIPGVREALVAKQRALANSGSIVMVGRDIGTVVLPNADLKIFLKASVPERAQRRYAQIQSGGSESDLELVQQYMEERDRIDTQRAHSPLQMAQDGIPISTDSLSVDDVVEHILNLLHQSYYD | Catalytic Activity: ATP + CMP = ADP + CDP
EC: 2.7.4.25
Subcellular Location: Cytoplasm
Sequence Length: 227
Sequence Mass (Da): 24875
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A0A3E1EWP2 | MSFNVTILGSGAAVPTLKRGTTSQLVTCNQRTILIDCGEGTQIQMRKFKVKFQNIQVILISHLHGDHVFGLPGLISTMQLLGRQDPLKIIGPKGIKEFLLNQFKLSGLYNGFPLEFTELETNAKQIVFEDKCLEIHTFPLKHRIQTQGYRINEKPGKRRLDVEAFEASGASRSYIQKLIAGDDIMDNEGRIVKSEDVTFPPKPIKSYAFCSDTAYLPELIDSLKDVDLLYHEATFLDKESERAVETFHSTAKQAATIALKSNAKRLILGHFSARYKSMENHQLEAESIFERVYIPTDGEIFHV | 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... |
A0A7S4QZM8 | GPQGEGGGRGGGGGPSTAGTMFARSRVVQAVSQLPVLMVLSVFGFEWYSHNVLLAPRVLVQEVGAASALLSAVLFNVAWALALWSFLRCSLTDPGRVPEEWRRRNRGYSVLDGEPGGDPSLLHGLRQWRPAVVTTCRHCHQRRPERAHHCGICQVCVLRLDHHCPWVGNCVGFRNHKFFLLLGAHGCLACVGLCTSARQQLQALVWGGPGLEVLLAKATPREAFAVCFSIMMSLVLGFLLGALFLSNAALVAQNKTAIEVNYQGPNPYSLGPLRNAEQLLGSFDLWWFLPVDPARPHCDGVTFPTRGLSAAAAHSV | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 316
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 34134
Location Topology: Multi-pass membrane protein
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A0A8C5D6A1 | MRATWCHHVGDHWGKDSLLCNLPFRQILETHLNFQNYIEKLQMLLYLEEIWMKDNIKKYNISDAVFHKEMELFTLEMSGFSENRPSVRQGDILSVYPVGNKEMRYWGSVHSVQHNSVKIKFSMDQFVEGMKFNVEFTVKNLIMRLQHRALELAYEDRLMSVLFPNPKHCASCLCFFLPVDRLFNTQVEDNPRQYQAIQHIMAGSSRPAPYLIYGPPGTGKTVTMAEAIKQIANNCTSTSIKILACASTNSACDVLCENIVGGNEDKSKVYRMYAKYCDSRLVPEVLKAYSNLDRQTFVFPEKKELMKYKIIVTTPYTAGR... | Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
EC: 3.6.4.13
Subcellular Location: Cytoplasm
Sequence Length: 639
Sequence Mass (Da): 73416
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A0A1V6N4R2 | MKFAHLSDTHLGYRQYGLIEREDDFYNVFNEIVDKIIDERVDFVIHSGDLFEIAKPSPNALLIFQEGLMKIKESGIPFFAIAGNHDTILRQNALPPQILFKKLGLTLISPNNPIVNSSFLRENDIFIGGTPYISKSQTPLLKSLLNDLSKKSEGFSKRILVAHQGIDKYIPFDYELEISDIPTSFNYYAMGHVHNRIIDDFGQGKLVYPGSTEIWRSNEAIDYKKNGKGFYIVDTSENDAENRFDVDPINIELPREFISKNIEYGKLDSELNSLGSYISSLNNKPILNITIEKGNFNTSDVYKKLNNILSKITLMFRPTF... | Cofactor: Binds 2 manganese ions per subunit.
Function: Part of the Rad50/Mre11 complex, which is involved in the early steps of DNA double-strand break (DSB) repair. The complex may facilitate opening of the processed DNA ends to aid in the recruitment of HerA and NurA. Mre11 binds to DSB ends and has both double-stra... |
A0A0K1EEN5 | MTSEEAFPIGLSLRVAAIALGLAGPLGIGIAWVQARHRYPLRWLVEALVLLPLILPPSVIGYFLIVVFGRRGLVGPLLEGTFGVRLVFSPAGAVLASTVVALPLVVKTAQPAIEAVPPELEQVAKTLGLGPLSLLFRVTLPVAYRGVLAALVLGYARALGEFGATLMFAGNIPGLTNTMPLELFAAYQGGDDARAGLYVIVLTGMSLVVAFVAARLSPREITG | Function: Part of the binding-protein-dependent transport system for molybdenum; probably responsible for the translocation of the substrate across the membrane.
Subcellular Location: Cell membrane
Sequence Length: 223
Sequence Mass (Da): 23306
Location Topology: Multi-pass membrane protein
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A0A926ERL5 | MRMVIGGKAQGKLAYVLSHENLLQDEIIDGRTCPLQAPFRGKALYALHELVRRVLKDGNDPREVVVSILRENAELIIITDEIGGGIVPMEPFERQWREEYGKICCMLAKKAQKVERVYCGIPMVIKE | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 5/7.
Function: Catalyzes ATP-dependent phosphorylation of adenosylcobinamide and addition of GMP to adenosylcobinamide phosphate.
EC: 2.7.1.156
Catalytic Activity: adenosylcob(III)inamide + ATP = aden... |
A0A6P1YS40 | MSVTSGPSMRTPRRAVSGLGSARSGTGHFWRQRVTAAANLLLVLIAVPVFVCVAGQDQETVRATLGHPLVAIALLLLLLSTAVHMRIGMQVVIEDYVHSEGLKILALIANTFFTIAVGCAGAFAILKISFGG | Pathway: Carbohydrate metabolism; tricarboxylic acid cycle.
Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH).
Subcellular Location: Membrane
Sequence Length: 132
Sequence Mass (Da): 13855
Location Topology: Multi-pass membrane protein
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A0A5N9AW82 | MTSESKFRVFIAFKVDQKVTQLADDVIRHLKAAYQEGFRAVKPSGFHITLVYLGDIERGLMLSINKEITDVCDLTPPIRFAVKGLGVFPNWSRPNILWLRIIDPKRELGTFRKDIVKAISGFDFPKVDSVFRPHITLGRFKQKLKSADIHELKRIAALLKQDEPLRCTTMNLFVLESTPTSRGVLYKPISEHSLGE | 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: 196
Sequence Mass (Da): 22352
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A0A5N9AXD6 | MEAQIKVKRFNPENGAKPFFQDYSIDVSEDSTILDGLIKIREEQDGTLALRCSCRASICGSCSMKVNGSAKLVCKTRIKEVSPQGETVTVEPMGNFPVIKDLVTEMDSFWSKVKSIDPYVKTNFEPEAEHIASNESMTHLLGVMNCIMCGACVSECTALEVDSTFTGPAALAKAYRFVADPRDEDKKERLGKLNESSGVWDCSRCLACVEVCPKDVAPMERIVKMRDLAIEEGYTNTSGYRHTESFSDSIKKHGRLDETRLALESTGLLNISGLIDLAVIGIKSLFKGKIPPPLPHRPKEADKVTNIAKRLDSEESEE | Cofactor: Binds 1 [2Fe-2S] cluster.
EC: 1.3.5.1
Catalytic Activity: a menaquinone + succinate = a menaquinol + fumarate
Sequence Length: 318
Sequence Mass (Da): 35107
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A0A351KWD0 | MKHHPVYTHERGRTDWLLERGTALVLMFLIPWLGLHLAFLPGLNQGRLVEWVHSPWNAIALASLIVMAALHAGLGIRSILMDYIATPSLRGLSLLITRILLVFSSVTGLGALWVLHTGVAP | Pathway: Carbohydrate metabolism; tricarboxylic acid cycle.
Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH).
Subcellular Location: Membrane
Sequence Length: 121
Sequence Mass (Da): 13333
Location Topology: Multi-pass membrane protein
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A0A3B9QX08 | MGHTVACPGYAGECRGFGPGTQGKYRRQRYPRTVQIIEYPVSLVMKAWHVFLTWLGMDAVSSWPLTIVLLVVTVRLILLPFAYRALYSSRMLINLRPALHALEVEYKGVKDRDRIREKMAKRKQLQQDDGYRMRDGCLPALIQIPFFLGLYRILLTVSRPTDLESGTHQSIGALNGTDVGQFLQAEVFGVPLPAYSVMTDERFDFLGTSSSEVFHIALPLCLIASVLTTSNTAYSLKRNWMTLDEDSAVARGLFKFMVLLLPVMLIFPLAFGLAGPAPVAIMCYWVMNNLWTVAQSVTLQLIMDRKAPYTEEFLAHRKEI... | Function: Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins. Aids folding of multispa... |
A0A3D6B1S3 | MKNTVFKGCATALLTPFKDDRSVDFDAYATLVRRQVEGGVDFLVPLGTSAETPTLNREEKKEILKITKKEAPRLPLLVGCGSNSINATLENISSIEYADALLIVVPFYNKPTQEGIYQYYKALAEKTELPIIMYNVPGRTGVNMSAETALRIAFDVKTVIGIKEASGDISQVKTIIERCPENFTVLSGDDDMTFDLINAGAQGVISVASNVLPAQVSQMVHLALEGHKAEARQLNEKLYPLFKGCFVESNPIPAKEALHQLGLCSAKMRLPLTEASEKTKELIYNILKEWR | Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4.
Function: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
Catalytic Activity: L-aspartate 4-semialdehyde + pyru... |
A0A1V6N3L2 | MKLKILPPTLRINNRYLVLDIKSEIKISKDELVSAIWYACLRLYGEIGTSDFNLWLMKFYDISNYSSKYYKIDDNIINSGIDTNINTNSNKINNNINNNINTKINTKINTKINTNNGNNKINTDNLNNSSNNNNNKVNTNSNSNNNFANYDEEGPSYYHFKVVLRCKRGCEDKVRGSLALLSNYNNNKIAITTMGISGTISSSIENFIK | Function: Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
EC: 3.1.26.5
Subcellular Location: Cytoplasm
Sequence Length: 209
Sequence Mass (Da): 23774
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A0A1F9QWC6 | MRMSETRIKLGVNIDHIATLRQARKDIDPDPVAAAQVARQAGADMIVCHLRRDRRHIQDADLFKLCRLKGETHVEIADDKRIVDLVLKARPGSVCLVPERPGEVSTEGGLDVARNFKSLEKTVARLKRAGVEASLFIAPEAGNVRAARNLGADVVEFDASDYSAAPNQPKRRSELERLELATYMAWEMGLTVHAGHGLDYHNVAPLARMPHLNALNIGYSIVARSVFVGLKTAVGEMRRMVD | Pathway: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 5/5.
Function: Catalyzes the complicated ring closure reaction between the two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and 3-amino-2-oxopropyl phosphate (1-amino-acetone-3-phos... |
J4QE84 | MKELTYFNGEFVEPGAKVISIDDRGYLFGDSVYEVVRVTKGRCFALSYHQDRLYRSMREMDIPVKMTPDDLTELHEILIEQSEIKEGYIYLQISRGVAPRHHAYDRSKLEPQMLMSIHNLDMDAVNKLESGVKAIALPDERWGHVDIKTTNLIPNILAQTKAEKKFAYTAMLFRDGICTEGATSNVFAVKDGIIYTHPSDNHILKGITRQMVITRVAPSLGITVIEKEFDRAFVDDADELFFTNTTGGVIPIIKLDRNPVADGKPGAVTMKLRHGLEKLMEEGLA | Function: Acts on the D-isomers of alanine, leucine, aspartate, glutamate, aminobutyrate, norvaline and asparagine. The enzyme transfers an amino group from a substrate D-amino acid to the pyridoxal phosphate cofactor to form pyridoxamine and an alpha-keto acid in the first half-reaction.
EC: 2.6.1.21
Catalytic Activit... |
A0A1H1XNN3 | MSRAAEGPIGIFDSGFGGLTVARAVMDQLPNEDLIYLGDTARAPYGDQAIADVREYTLECLDHLVEQGVKALVIACNAGSAATLRDARERYRLPVVEVVLPAARRAAAATRNGRVGVICTEVTKTSMAYDDALGVAVGVEVVTAACPAFVPFVEAGVTGGPELLAAAESYLTPLRDAGIDTLILGCTHYPLLTGVISMVLGDRVTLVSSADECAKQLYVTLATAGLAHDAPRQTSRRFLTTGDPDSFSALGRRLVPDLITDVDQFSGGVRRA | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Provides the (R)-glutamate required for cell wall biosynthesis.
EC: 5.1.1.3
Catalytic Activity: L-glutamate = D-glutamate
Sequence Length: 272
Sequence Mass (Da): 28582
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A0A359H073 | MKLFRAIARVVFGLTFLFSGFVKLIDPVGGGLIVAEYFKIIGIESNTAFPIIFGAFMAGAEMLIGISLLLGLRMKFACKASLIFISFFTILTLFLALFDPIADCGCFGDVIKLTNWQTFNKNIVLLILAILLYFERDNFIPIAPKYWELGFVGVYAVMIVFISFYSFRHLPVIDFLPFRVGTDIREEVLNPGISDEPAFETTLYYSKNGKMQSFSLDRLPDSTWTFTHSMSTPVNPDLKKEIVDFAISDKEGSYVTDSLLSFKNVFLFSVPFPHKLAMEDFFAMKELYDSLSVKGVHIYALFGSSYIDIKNAVAGNKIPF... | 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: 759
Sequence Mass (Da): 84611
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A0A8J5RAI6 | MYSRNTIVIFIYLNVLNTINCDSNVGVNFYVDGNGFHRTINYQVEAKKYINYDCHVALYLELPQELYVNIDELADLQRFTNMRACAVGETNVELFAEEAKPQSVSFCTALNFDATTLNLTIHQRYQRAKEKEDYANVILPFPKLLLGCKKRIKEYQVSLIDLCDSCVGFAIKWREIPYQTETKNYMWIIPIGELTHRSYVTYITLFTSVIGTLIILKALFSVNPTDHVKNN | Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Function: Essential component of glycosylphosphatidylinositol-mannosyltransferase 1 which transfers the first of the 4 mannoses in the GPI-anchor precursors during GPI-anchor biosynthesis.
Subcellular Location: Endoplasmic reticulum mem... |
A0A8J5R7B9 | MTQAQELSKRPHIVVATPGRLADHLESCDTFSLNKLKFVVLDEADRLLGGDFDEQIKTIFAALPKQRQSLLFSATMTDALEQVKQVARNNVFQFEDQDDSGMATVKQLDQRYVVCPRDVRDAYLVEVIRTFKGINPNGSIMIFTDTCKNCQLLSMTFNTVGFENVALHAMIKQRERLSALNKFKSNCVKILIATDVASRGLDIPLVELVINHTIPNVPKEYIHRVEKEIATIFTQVSTTKREAEIVLDETDFYEKKMINKRKKLIMEGKTDEEIDKILAPKKKHRKKDKKMKTIKTIENKLTDV | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 304
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Sequence Mass (Da): 34759
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A0A0P7WEB3 | MNTDIGVYWIQEALTAAVVLSTPLLVGALAIGLAIAIFQAATSIQEMTLSFVPKMLVVVIIMFLLFGFMLQYAINFTERVFDFIPQIAR | Function: Role in flagellar biosynthesis.
Subcellular Location: Cell membrane
Sequence Length: 89
Sequence Mass (Da): 9842
Location Topology: Multi-pass membrane protein
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A0A094P8N7 | MTWIYLAALLFSLIGMVVLDRRFTLFFWADARRAAIVLPAGVLFFLLWDLAGIGLGIFFRGPSSLVTGIVVAPELPIEEIAFLTLLCYLTMNVFAGITKILMRRDHP | Pathway: Carotenoid biosynthesis.
Subcellular Location: Membrane
Sequence Length: 107
Sequence Mass (Da): 11990
Location Topology: Multi-pass membrane protein
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A0A5N9AL48 | METITLQISKSDTAKRVDIFLSERTTDLSRSQISNFISQGLVTVDGTPAKASYRVKSGEIIQLLIPPLPPTSLIAEDIPITVVYEDSDVLVIDKPAGMVVHPAAGNWSGTLANALLKHIPDIAGVGESGRPGIVHRLDKETSGLMMVAKNTSAHRNLSKQIKDRYISKVYTCLIRGNLKLYQGTISGNISRDTHNRKRMAVVESGRTAETSYKVMQTYNGYSLVEAYPKTGRTHQIRVHFSSIGHPITGDKLYGGTNKLLRRQFLHSTRLGFWLPSNQHYVEFESKLPYDLQMYLDGLVLESL | Function: Responsible for synthesis of pseudouridine from uracil.
EC: 5.4.99.-
Catalytic Activity: a uridine in RNA = a pseudouridine in RNA
Sequence Length: 303
Sequence Mass (Da): 33670
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A0A5N9CC69 | MPGPFHIGQINDTNVAIHYSSLIGFGLVAWFLADSVFPTFYPGWSPTKYWFTSSISAMLLLISVLIHELAHSFAAKSRGHQVLQITLFIFGGVTYIRDRTIKLQEHIFIMVAGPFASLCVSIPLLFSLAYLNETGENSALGAILAFTGIANGFIVIINLIPGSPLDGGQILRSLISRSTNSMIGANNISVRVGQISGWLFVCFGLFQLLHSSYISGLWLTFFGWFLLLAATHEWKSKSTENDLSPISVSQLMYRAPKTTSPTSSIKNLLDGFFVESGETLIAVVENDVFQGFVELTDIIRIPPTEWDVTLVRSIMKSSAP... | Cofactor: Binds 1 zinc ion per subunit.
Subcellular Location: Cell membrane
Sequence Length: 374
Sequence Mass (Da): 41473
Location Topology: Multi-pass membrane protein
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A0A455UXA0 | MAPEGEATLSATLYMGPKVQDYLEQVAPNLKLTVDYGWLWFIANPLFWLLDKIHDIVGNWGWSIVLLTVLVKLVLFPLSAKAYKSMARMRKLGPEMQRLKEMYGDDRQKMSQEMMKFYQKEKINPLGGCLPILVQMPVFIALYWMLLESVELRHAPFIFWIQDLSVKDPYFILPILMGISMFVQQMLNPTPPDPMQAKIMKMLPIIFTFFFLWFPAGLVIYWVVNNIISVAQQYFITRSIEKDPSVGKGMRTK | Function: Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins. Aids folding of multispa... |
C1DSJ3 | MLHDGVAVLSLDRPPINNLSFELRTHLLQALDAANADPAVEAIVLHGNDKVFSGGVDINEFGSDLATRSPSLPELIRAVENSRKPVVAALGDLCLGGGLELALGCHYRVFSASARIGLPEVTLGLLPGAGGTQLLPRAIGLDAALNLILSGRQQAAADFRDTALVDELATEDLRAAAVDFARRLSADTVPWPRLRDRPLRVEVEDELYIHFVRDRLKGQKGQGPAPLAALEAVAAAGRLPVDEGLEEEGRLFAGLHAGPQSRALCHAFLAERAAGKIPGIDDSTPTIPVERVGVVGAGTMGTGIAIVFLNAGFEVALLES... | Pathway: Lipid metabolism; fatty acid beta-oxidation.
EC: 1.1.1.35
Catalytic Activity: a (3S)-3-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + H(+) + NADH
Sequence Length: 697
Sequence Mass (Da): 75031
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A0A2M4CLN7 | MAFSKIFICSLIVIHVCSVLSQTDPVCTTPTRKAGFCVAIERCRNIHYILRSPTPPIKGIQSYIDRAACTLPGVVRSICCQPTEIVHRRPLLPEDCGDSIFQKLSQGNETDPFDYPWMVALRYSKNGLLKDGCGGSLINSRYVLTAAHCVQPRDGWMLSKVRLGEQDRSKPIDCIVYSNGEKSCADPPIDVEIESTVLYPQYNSLVLLHDIALIRMVHEVSFSDSIQPICLPVRQDVRNLLLPRYIVTGWGMTANKSSSNVLLQAVVEPVPIPECQRTIAEHGFFVDLSEDYHMCAGGKDRVDACRGDSGGPLAFYVRNV... | EC: 3.4.21.-
Subcellular Location: Secreted
Sequence Length: 362
Domain: The clip domain consists of 35-55 residues which are 'knitted' together usually by 3 conserved disulfide bonds forming a clip-like compact structure.
Sequence Mass (Da): 40008
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A0A1H1DAS4 | MSAASVVLAAAEAESHTEPTAELPILPHLGELVVGGICFAIILFLAWRYAVPRLEAVYAQRRQAIEGGMEEAQATQAEAERTLEEYRAQLAEARAEAARIREEARTEGAVIVAEMRERASAEAARITESAQRQVEAERQQAVAQLRAEMGVLATDLASRIVGESLADDARRSRVVDRFIAELEEVDTSSAAPSDGSTSEPRVGSRPSRAGEEPSGGLLSAITRKVRGT | Function: Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).
Subcellular Location: Cell membrane
Sequence Length: 228
Sequence Mass (Da): 24479
Location Topology: Single-pass membrane protein
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A0A4S8P3Q0 | MPDRERRRHPDLEHENAGTLIVVVGPSGVGKDSLIAVARRHFRDDPDIRFVQRVITRPADSGGEDHRPASMDAFTKAKSAGDFAIDWEAHGLRYGVPISILADLRSGATLVVNGSRSALPQFEERFAKLVVVNVTARPDALAARLAARGRETAAEIEARLNRTTEPPPSGAHVVTINNSGALEAGAQKLIDLIGRLAHQTA | Pathway: Metabolic intermediate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate from D-ribose 5-phosphate (route II): step 3/3.
Function: Catalyzes the phosphorylation of ribose 1,5-bisphosphate to 5-phospho-D-ribosyl alpha-1-diphosphate (PRPP).
EC: 2.7.4.23
Cat... |
A0A353VQ52 | MLLKDFLNAGVARLEPLYPTKEARNIMLMLCENRIGTKSYTHIVEPEYQIKDKFLDGLNADLERLAAGEPVQYVLGFADFCGLRFKVTPEVLIPRPETELLCREAIKIGSRMQRMRKAYGKQARPVRVLDLCTGSGCIAWTVALNIPGAEVIGVDISEGAVAVASSQDFAMTIKETEAAAPRFVVADVLAESHPFVDGDFDLILSNPPYIMESQKAQMRANVLNYEPSTALFVDDGNPLVFYRSIAALSRTCLSAEGKGLTEINELFGPETAKVFSDAGFSKTEVVKDFYDKNRFVFYSK | 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... |
A0A259CXI1 | MTTNTTAFPHYESAIAELEAIIAQLESSQLPLEQSLAAYQRGTELLKQCQQSLTQAEQQVRILTEANTLVAYNAVNE | 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... |
A0A1B9F7T9 | MIRLFVAIDIPDSIKEIVESHYREIQCKFKEKRIRSVKWVDPRLWHITLKFLGEIPEQKLPMCQKIIEQCGQLHNTLKLRLRHIGCFPGLQRPRVVWAGIEDNAKCLESMHLFLDKSFESIGIPREQKKFHAHLTFCRIKNSSPCVAGTLVDILKTGLETPWFEVGYISLYKSKLTPNGPIYTPITRAKLGRQ | 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: 193
Sequence Mass (Da): 22423
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X8JJG6 | MRPPYGNYNDNVRRAAGVRGQKLVTWDFDSGDSVGATPAQSKAMYDKIIAQRPSSILTLNHETHERTAHEVIPYVVPRLQAAGYKLVTVAECMGMQPYQSVGSPQTPDVGLEQIILQNI | Catalytic Activity: [(1->4)-N-acetyl-beta-D-glucosaminyl](n) + n H2O = n acetate + chitosan
EC: 3.5.1.41
Subcellular Location: Cell membrane
Sequence Length: 119
Sequence Mass (Da): 13126
Location Topology: Lipid-anchor
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A0A1B9F4P1 | MREIDITKAIIDKHIEELNKCLCSDVVIVGAGPSGLVAGSILAQKGYTITIFEKRLAPGGGIWGGGMGFKYVIIQKEALDIVEEFNIPYEKYSDDLYAVDAINFASGLILEAGKRGVHIFNLIAVEDLLVREGRVQGVVINNTFAKMNQFPIDPLTIEAKAVVDATGHEHEVVKTLSQKNDVTLNTPTGKPLGERSLFAETAEKAVVTNTKEVYPGLYVCGMATAAVYGGYRMGPIFGGMLMSGKKLAGLLEEALKA | Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
Function: Involved in the biosynthesis of the thiazole moiety of thiamine. Catalyzes the conversion of NAD and glycine to adenosine diphosphate 5-(2-hydroxyethyl)-4-methylthiazole-2-carboxylate (ADT), an adenylated thiazole intermediate, using free sulf... |
A0A0Q4B4Y5 | MFITLQDSQYSIKDQVGDYLAGGGQLVQFRVKGHLPRGLEREAGMIQRKCEQAEARMIVNDYVDVAQEVGAWGVHLGQDDASPKAARATLRPDAVVGATAHSWEEVLALKNAPIDYIGLGPLHFTSTKTNLAQILGYQGVEDILGKMLSANINIPVYVVGGVENQDVRPLIKMGAYGVAVSGSIALASDIVFATQKFLESIAKGIR | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)-thiazole: step 1/1.
Function: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-met... |
A0A0P7X5Y3 | MAKEVDVCVIGSGPGGYVAAIRASQLGFKTAIIEKRDLGGVCLNIGCIPTKALLKSAETLDNLKHAEEFGFTVSEVKADFDKIIKRSRGVADKQSKGIQFLMKTNKIDVIMGHGAFTSAKELAVTDGDGKTVETVKAKHFIIATGARSRELPNLKFDGETIINSERAMKLENQPKRMVIVGAGAIGVEFAYFYKTLGTEVTIVEMQKTLVPIEDEEIGKELGKIYKRAGYKLMLESTVEKVEKKGKNVVVTVKTPKGTETLETDVVLSAVGVVGNIENLGLEKIGVKTEKGAIVADKVTYETSVKGIYAIGDVAGAPWLA... | Cofactor: Binds 1 FAD per subunit.
EC: 1.8.1.4
Catalytic Activity: (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + NAD(+) = (R)-N(6)-lipoyl-L-lysyl-[protein] + H(+) + NADH
Sequence Length: 473
Sequence Mass (Da): 50853
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A0A1G3PKC6 | MSGKHTYTEEGKFAGSRLDAAVAALYPDYSRSFLKTAEIEPSVNGKPAKWSHKLKPGDIVEFEIPEIKHLELVPQDVPFDILYSDDDIAVINKPYGLPVHPSHGHPDKTLVNGLLFRLGDKITGVGGADRPGIVHRLDMDTAGLMVVAMNDHSHRVLSEMFRERKVGKIYHAIVKGHLPGKGRFEHPLGRSHSNPLKRAVIPVADGGKPAITEYKVLEYLDEHAYVEIVLLTGRTHQIRIHFAYEGHPIAGDPLYSRHPKAYGLSGIALCAKELSFTHPSTGKEMSFKIELPGEFSALLERLRKSLP | Function: Responsible for synthesis of pseudouridine from uracil.
EC: 5.4.99.-
Catalytic Activity: a uridine in RNA = a pseudouridine in RNA
Sequence Length: 307
Sequence Mass (Da): 34021
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A0A0G0L963 | MEFFDFKRRLVSNIKDACEKTCLMYDLNFSDLNLEEKAILENTTNLDFGDYTTNVAMVIAQKYGVNPVEIGQKISDHLKKSADLRSIVKSIDVVRPGFINIILKEKILLDSTNEILDVNQFKQKLVSLQTNKQILVEHTSPNTNKSLHIGHLRNNLLGMTVIRLLRAIGNDVISDCLYNDRGIHISKAMWGYLKNGHLKEPWRELIVYWHTHKNEWPTPQLLNLKPDHFIENFYKIGVESEDNEVFMKEMREMLVAWEEGDTLVRDLWKMLNNWVYEGFAITYKLIDSIHDNNWYESEFYKDAKKTVDTGLKKGVFRRLE... | Catalytic Activity: ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg)
EC: 6.1.1.19
Subcellular Location: Cytoplasm
Sequence Length: 609
Sequence Mass (Da): 70580
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A0A455V7V9 | MSDNLRLHGFNNLTSSLSFNIYDICYAKTEEQRAAYIDYIDELYNAERLTQILKDVTNIIGAHVLNISRQDYEPHGASVTILIAEHELDEPTAGQIEPGPGPLPETVVAHLDKSHVTVHSYPESHPDNGISTFRLDIDVSTCGHISPLKALNYLIHSFDSDIVTMDYRVRGFTRDVDGKSCLLTTTSPRSRTTWRKTPSRPIR | 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... |
A0A7V8AWZ8 | MDIKNQILNILADIAGDSIVKDNLDIAIFEEGIIDSFKTIELLLAIENQLGIDVSITDFDREAWATPNKIIALLSAKQ | PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine of apo-DCP.
Pathway: Cell wall biogenesis; lipoteichoic acid biosynthesis.
Function: Carrier protein involved in the D-alanylation of lipoteichoic acid (LTA). The loading of thioester-linked D-alanine onto DltC is catalyzed by D-alanine--D-alanyl c... |
Q5NUL4 | MSIGPKNNLDDVLKKRGSISDPNTLSSLPVLVPKAKSKFKPSTNATPSSSTAALGHNALPSFRTPGFGKPKARKSEPETSTAREVIDLSCSSPSPRSKRQLETQHITDAFPSKRRRSGLFDDKENLSFINGDINGKGKAKEMDDVEGLVDVCSKESTERASLTKRDLYDPFDQLDIDFPSFKRNPRLNQHPQHPTQDHKDLESKSVADLRGLLEFVLSLQHTNNCSIEQYRKSRNSRVDIVTLEGIETLFSSRINAIRQILESKEGTYCDPCLVTSPYFDGIHNSSSVSIASSETLNGLSSDHNRSSSDPILDSFEDDIE... | Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
EC: 3.6.4.12
Subcellular Location: Nucleus
Sequence Length: 945
Sequence Mass (Da): 106646
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A0A2W6Y3J8 | MKKELLRIGILCSIFGFTLSANAQEYIDKKITEKNGNVSLATFKSGSNLKSANKADLFKTILKLPAGSELKLTKSEKITAGNFLDEKYELYYNNVKVEFGVYNLHYKNGELTSMNGDIFTTNNVITSPKISSQAALDKAIQSVGAQKYMWDDAESNVDNYKKPAGELVLLPLQQADESYKLSLAYKFDVFASQPMSRAYIYVDASNGQVLLSDAIIKHANGRNHNILKNELDTEKITSEVKDSELKNTVSKLAAGNAATRYSGTQSIETSLNTAGDNYILYDTTRGNGVRTYNLKKNTSISNTDFTDADNDWSATEFDNS... | Function: Extracellular zinc metalloprotease.
EC: 3.4.24.-
Subcellular Location: Secreted
Sequence Length: 645
Sequence Mass (Da): 70944
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A0A0K0Y8S7 | MIKEFKDFIAKGNVMDMAVGIIIGAAFTAIVGSLVADIINPLIGIFMGGVDFGGLSASVGDAVFTYGNFIMAIINFLIIAFVIFMLVRSVNKMKKAEEEAPAEPAGPTQEELLADILTALKK | 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 inner membrane
Sequence Length: 122
Sequence Mass (Da): 12942
Location Topology: Multi-pass membrane protein
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A0A1G3PPR0 | MKRKEILEAIKKAGEMKFAALQELFEADNKNKRKRLRIVLDEYNTKGVIHYSRDTGDISWSGAVEPAEEEQERKHEQKKPKKRELFGKSVIAPRPVKDAADDFPRVVEKYHIRAEFPRAVFAEAERIPSEIPVSELARRVDMRDSMVVTIDGIDAKDLDDAVSLEVRADGWRLGVHIADVSNYVPADSKLDSEALKRGNSYYFINKVVPMFPEVLSNGLCSLNPFEDKLTMSAFIDLSREGEVLSYDVKESVIRTRYRLNYTDVQRYFDGELTPEDPELCETLDRMYELFQILYKKRIADGSIDFDFKEQKVSIDENGEP... | Function: 3'-5' exoribonuclease that releases 5'-nucleoside monophosphates and is involved in maturation of structured RNAs.
Catalytic Activity: Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.
EC: 3.1.13.1
Subcellular Location: Cytoplasm
Sequence Length: 618
Sequence Mass (Da): 716... |
A0A3D0FRV3 | GLISSDKLSELYRAADQLAMARPLQYVLGFCEFSGLNFHVEDGVLIPRPETEELVRWIGEDRDYADIKEEFAIFDAGCGSGCIGIALANLFPNAKVCMCDISDKAIEVSKFNCRTVLNKAKWPRVNIFKYDLLGYMPLENHIQESSLDIIVSNPPYVRQSEKQLMHRNILEFEPSNALFVSDKDPLLFYRVIAERGRKMLKTSGKIYFEINEAFGYETMQLLQSLGYENIELKKDLNGRDRMVRASSSRYRESRRDDPPHVEK | 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... |
A4XIV0 | MSIRALQKETLKKGEKNLKIKVFPEDFIVKEEINIEIKPSGKYKIYLLKKKHWNTVDALRFISRENKIPFEKIGCAGRKDRHALTYQYISVPREYDINFNKENVKLEFLGYSDDFVSPMTLKGNYFEVVIRKIKNKDERIFQRLDEIKKFGFPNYFDDQRFGSAENEQEFIGEKIAKKHYNGALKLYFTTIHPEDKREEKERKKKIFELWGDFEKILPLCKTKVEKDIIKTLMKGKSRHYLIEAVNLIPKEEMSMFFSAYQSYIWNRTLSTVLPYYTDLLRPVKGKIMEYLIYRTLSEKALDELKNLQIPTVSSKIPYVN... | Function: Responsible for synthesis of pseudouridine from uracil-13 in transfer RNAs.
EC: 5.4.99.27
Catalytic Activity: uridine(13) in tRNA = pseudouridine(13) in tRNA
Sequence Length: 405
Sequence Mass (Da): 48160
|
A0A258M4C8 | MQVDLSKHDVRTVGDEALLLARVAPTIVSHNRLAGAQMAFALGATHIVMDDGFQSPGLVKNATLLVVDAEAGIGNGLTIPAGPLRARFRDQLERADALLVVGDGPAERGLPNSRRKPILRAHMEPDAETIKRLFGQNVIAFAGIGRPDKFFNTLTDNGVHVVQQHAFPDHHPYTVAQVASMVERAHFRQLKLVTTAKDYARLQRPAFAAFKDMIEVLPVRLKFDDPTEVDAIIRNAEVRSMLFQPPEPATPVETPAEPQAAAGTETPPAEPAQPTPPPQPVQTGPFTG | Pathway: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 6/6.
Function: Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form te... |
A0A836TRT4 | MSPTNQLNYIFYLGSLSLAFMLRILPLPPSVQLIAPDWVLLVLIYWLLSEPHKIGIFHAFLIGLLVDVLTGRILGQHPSGYIFAAYLCLTLHKRLQNIRLIQQCFFIFFILFITQSIILWTEIFQHPLPYNTAFWLPALSGTLFWPVIKYLLRRCQQGFH | Function: Involved in formation of the rod shape of the cell. May also contribute to regulation of formation of penicillin-binding proteins.
Subcellular Location: Cell inner membrane
Sequence Length: 160
Sequence Mass (Da): 18660
Location Topology: Multi-pass membrane protein
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A0A926EPH8 | MFTDLKYGIDVFRTITPNDILDIVIVAFLIYQCIKLVRETRAAQLVKGILALLLVNIFATELELKTLGFLMENILQIGLFALVVVFQPELRRALEQVGRTRITDLNVFSSGLSEQQTRDRWMHTINAIVDGCSSLSRQKIGALIVVEQKTKLGDIIKTGTIIDSDASAELIGNIFFPNSPLHDGAMIIRDGRLYAAGCFLPLSDNSQISRELGTRHRAALGMSELSDAVVIVVSEETGTITLCRNGKLDRGFTAESLTKVLIGALIPDSTDPSEKKSERKVRRKGKKKA | Function: Catalyzes the condensation of 2 ATP molecules into cyclic di-AMP (c-di-AMP), a second messenger used to regulate differing processes in different bacteria.
EC: 2.7.7.85
Catalytic Activity: 2 ATP = 3',3'-c-di-AMP + 2 diphosphate
Sequence Length: 289
Sequence Mass (Da): 31887
|
B9K379 | MSNSCQLVFPSHIERLPRYRPAADLAVVSETSAEPLVNLASNENPYGTNPGFADALNEITRFNLAEYPDPDALRLKTAIAAKNHVSIDQLIIANGSDELIDLSARTLLAPGTNAIFDEYSFVAYRKATYLAGATGVSVRPSGWNADLNEMLRVIDTNTRMIFLANPSNPTPGFISTAEFDSFISRVPATVLVVLDEAYIDFVEPNERIDCKLLLQSRSNVFITRTFSKAYGLAGVRVGYGIGSPTLINMMNRIRQPFSVGVLPQLAAVNALANEGFVNETRAKNIEQKARLSEGLSDLGIEHAASKGNFIIVKLRAPSAA... | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
EC: 2.6.1.9
Catalytic Activity: 2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Sequence Length: 368
Sequence Mass (Da): 40256
|
A9HB14 | MGKMNNFGRNLALWVIIIVLLLLLFNVFQPGSVQHASQQLAYSDFIGDVNGGRVRSVIVQDHNISGTLTDGTSFETYTPQDPTLIPRLTEKGVEVVAKPLDSDSNPFLRYLINYAPILLMFGAWIFIMRQMQAGGGRAMGFGKSRARMLTEKQGRVTFDDVAGIDEAKSELQEIVDFLRDPQKFTRLGGKIPKGVLLVGPPGTGKTLLARAIAGEANVPFFTISGSDFVEMFVGVGASRVRDMFEQGKKAAPCIIFIDEIDAVGRHRGAGLGGGNDEREQTLNQMLVEMDGFESNEGVILIAATNRPDVLDPALLRPGRF... | Cofactor: Binds 1 zinc ion per subunit.
Function: Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.
EC: 3.4.24.-
Subcellular Location: Cell inner membrane
Sequence Length: 646
Sequence Mass (Da): 70055... |
A0A5N9GR87 | MAGRSLPSAKRYAQAAFDIAQASDSMQKWDEQLSMLAQASGVPEFALLMQAPEINPEERSKALESVLPSLSDGTRNLLMLIAKRGAVKVLPQVYSRFQELSDAAQGVVRVQVTSAIDLTDADQKRITEQLATSLGKEVRITTAVKPELLGGLVIRVGDRVIDGSAQQRLQALKGTLARGIV | 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... |
A0A5N9AZ08 | MNFMERAVLLSRKALGHTSPNPPVGALIVKDGMIVGEGWTQSPGPGGWHAEREAIVKAGKKSSGGVLYTTLEPCNHQGRTPPCTQEIIKSGIKEVHVSLLDPNPEVNGDGVDRLKLAGIKVLIGEGKEQSGEILVPYLKFVTKGMPFVTVKYAMTLDGKIATYTGDSQWISGTKSRQYVHQLRSENDVILTGIGTVLADNPRLSVRDKSIPTYDFKQPLRVVVDSKGQIPLDSAVFSEHGETLLAVTERFAPSTKSKFRGKEIDVESIPEDENGRVDLKILLARLSNLGMITVLVESGPKLLGTFFDTGLVDKVEVFIAP... | 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... |
A0A7G8HG05 | MAVIADRCPGVQVTVVDINQARIDAWNDADLSKLPVYEPGLDAVVGRARGRNLRFSTAVDEAIAAADMVFISVNTPTKTKGLGAGQASDLRWVEACARQVAKSATGHTIVVEKSTLPVRTAEAIKAILASAEASGGDRSFAVLSNPEFLAEGTAIPDLESPDRVLIGGEHPEAIDALACVYSHWVPQERILRTNLWSSELSKLTANAFLAQRISSINSVAALCEATGADVREVARAIGTDSRIGPKFLNAGPGFGGSCFQKDILNLVYLCRHFGLPDVADYWESVVQLNTWQQHRIARLVVQKLFGTVTGKRLAILGFAF... | 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: 457
Sequence Mass (Da): 49285
|
A0A5N9AH49 | MKIVSKVSEMLAIQKDLLRPVGLVPTMGALHIGHESLINQSLKDNNSTVVSIFVNPSQFNAAADLEKYPKPLNADLALLEKAGVDIAFLPDNEEMYPKGFETWIEAEKTSVILEGQSRPGHFKGVATIVTKLFNIVKPDKAYFGQKDAQQLNIIKRLNEDLNLFVSIIDMPTIRDENGLAVSSRNAFLTDAERDAAHILFQSLSQAKEMIMEGKYDAGIIRNRITKMLGGSDLISVDYVSISKLRSLEELTIIEKPVLISLAVIINNTRLIDNIIVE | Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1.
Function: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
Catalytic Activity: (R)-pantoate + ATP + beta-alanine = (R)-... |
A0A5N9DRF6 | MSSKPTANTTESRRKGTAFFSDSFNELRRVTWPSREETVRLSIMVIVVAAIIGTFLGLFDLLFARLFDVILGT | 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: 73
Sequence Mass (Da): 8199
Location Topology: Single-pass membrane protein
|
A0A5N9DT99 | MLQEQIKMIVGLGNPGHIYANTRHNLGFMVVDNLVSQSKIIKRTNTSFGLMVESRISGKKVRLFKPASFINNSGPNIKLAMHKHNIGPTEILVVLDDLNIEIGKLRIRLTGSSGGHNGLKSIISSLETISFPRLRIGIGPPTNSGNQIDHVLGIIPDHEHEIISTTIEKACKAITCSLNTNLDSAMDSYN | Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Catalytic Activity: an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+)
EC: 3.1.1.29
Subcellular Location: Cytoplasm
Sequence Length: 190
Sequence Mass (Da): 20746
|
A0A836PP88 | MKVCLQWVMVCSLVVFLAGCSSLNEKTGGAFGSDAVTSGYSEDGEIRDERLGDLEEITNGSLMGGEFNDPDSLLSKSVIYFMFDSSEVQPVFAEVVTAHAQYLVANSAQRVILEGHADERGSPEYNVALSERRAKAVARMLEMQGVFPEQIEIISYGEMKPSAEGHDQAAWQLNRRVEITYQAQS | 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: 185
Sequence Mass (Da): 20338
Location Topology: Lipid-anchor
|
A0A8C5EDQ6 | MTSNSNLSTMRRLVEQLKLEASVERIKVSQAATELQQYCLQNAGKDALLVGVPTGSNPFREPRSCAVQIKNDRELLCKLPNNPVVDGQIQQFNETPQYF | Function: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction.
Subcellular Location: Cell membrane
Sequ... |
A0A3N2KUR5 | MKRNIFTALLLAVMALVFPLGMAASEETPLDSVVEKDSSVDAQGIIFDHLGDRYGWEVPFNHHKSIPLPVIVWGSDGLHVFSSARVDHGAVYRDGNAEFKVAGKDSPYKGKVVELVNGQEVKPAVDISITKNVCGVFISVLLVIWCILSVARWHKSQGMKGPRKMTGAIELVILFIYDGVIKPTLKNKANKFAPYLLTVFFFILVMNLLGLIVIFPGGANLTGNIAVTLVLAIITFLITNIFATKHYWKEVFNPDVPWWFKWPIPIMPVIEIFGIFTKPAALTVRLFANMMGGHMIVIVLTLLIFIFAAMGPVVTGATAV... | Function: Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.
Subcellular Location: Cell membrane
Sequence Length: 390
Sequence Mass (Da): 42870
Location Topology: Multi-pass membrane protein
|
A0A5N9GLB1 | MKRHVTLKKDFIAIARQGRIWHSHLLLLRTLERNGQQARFGLSVSKRVGKATVRNHVKRRLREILRDVSLNPGWDIVITARPVTATSRFSVLKDELLNLLATSGVVDPKGLGRTRYV | 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... |
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