ids
stringlengths 6
10
| seqs
stringlengths 16
1.02k
| texts
stringlengths 117
4.4k
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A0A2R5HGC7 | MQPYGTPAYFIWLGLALIPLVIAHAYGKKWMGYQVLFTLAFLWLTFGSTMSIWSILGFGVFETLLIKLYEHYRTREGSANKTWVFVVAVLLSIAPLFVVKLTPVIDPAHPSSIIGFLGISYVTFKTVSTILEIRDGLIKALPVKDFLYFLYFYPTISSGPIDRFRRFQKDMQTPVDREKYVEKLGKGIFFIFQGFLYNFIIGYLIQTYVLHGVAIQAVQNPGFVNMAISAYAYGLYLFFNFAGYSLFAIGISYIMGIDTPINFNKPFLAKSIHDFWQRWHMSLSFWFRDFVFMRFVKFMMVKRWFKQMTTTSNVGYLVNMTIMGFWHGFTPYYVAYGIYHALLMIGYDWWTRFKKKRKIKIPDNRWTRAVSIFITFNAVMIGFLIFSGLPWTALQRALGMHVEIPNF | Pathway: Cell wall biogenesis; lipoteichoic acid biosynthesis.
Function: O-acyltransferase that catalyzes D-alanylation of both teichoic acid and lipoteichoic acid (LTA). D-alanylation of LTA plays an important role in modulating the properties of the cell wall in Gram-positive bacteria, influencing the net charge of the cell wall. Catalyzes D-alanylation from DltC carrier protein.
EC: 2.3.1.-
Subcellular Location: Cell membrane
Sequence Length: 407
Sequence Mass (Da): 47456
Location Topology: Multi-pass membrane protein
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A0A1F4VEU2 | MKLVVGLGNPGEKYEYTRHNAGFLILNAFVAKKVGDGIVWLSETKFNAHVYREEGVIYAKPQTFMNRVGESVSKLVHFYNIDLSNLLVIHDDVDLIKGEFKLKKGSQAAGHHGVEDIFSKLGTSDFFRLRMGVGRPLDKKYEVEDYVLEKFSDEEISNLKDLFEKKIYDKIDGFLNL | 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: 177
Sequence Mass (Da): 20209
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A0A552X005 | MLKALLLIIILALGLIVGPMWSGNAGSVLILAGPYSIEMSLVVATLLVAAFLLLLWLVQAIFRKLSSGKRFTLSWFYKRKQKKAEKQLAQAMHHWLSKNYREAADYAERAAPHLQQPQHGYLLAASAWQALGNLKELQRTLGLAYDSAHHDLNVRLMQLEQMTDSGQALKTARTLLQDHPKHGGVLRACAETYYKHQHLESLRELLPRIQDRDIVPGARLAEFTRASYRSLYQSAGTSSERLRELWKETPSKLRRTPAVRMAYLDVLTHRGFGAIASKVATRGLALNVFTASDLLQFDMREWRQTESLREEVEKQIKQHPEHPNWFVLLGVLAMQESDYGLAERAIQKAISMKPSQLAYRLLGDAYYASGQKESALQAFRQAANLR | Pathway: Porphyrin-containing compound metabolism; protoheme biosynthesis.
Function: Involved in a late step of protoheme IX synthesis.
Subcellular Location: Cell inner membrane
Sequence Length: 386
Sequence Mass (Da): 43714
Location Topology: Multi-pass membrane protein
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D5X7N5 | MSKKIQRITGKTGVIGIFGFPVEHSFSPVMHNAAFQAGGLDYVYVPFEVPPERLAEAVSAIRALKLRGVNVTIPHKERVVQYLDSLSEEARLIGAVNTIVRSGDELKGYNTDAAGFLRSLEEKKVAVQGANVLLLGAGGAARAVAVQLALAGARRVGIVVRNSGWRKAEGIAEIVAGHSCAKSTVALFENAQDLIAEKGNIIINCTPVGMHPNVMEMPPFKLDTIPADSVVCDLIYNPAETLFLKTAKARGLKTVSGSGMLLYQGTLAYELWTRQQAPVDIMRTALEEALQRC | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.
Function: Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).
EC: 1.1.1.25
Catalytic Activity: NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH
Sequence Length: 293
Sequence Mass (Da): 31497
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A0A3B5M660 | RRSAPPGEEILALPDVAVQHELHAAVQSEEEEASADISAPQLFVELNELIVDKDQEMRWKERARWIKFEEDVEEETDRWGKPHVASLSFRSLLELRRTITHGAVLLDLEQNTLPGIAHLVVETMIISDQIRAEDRPSVLRALLLKHRSLAKHAKALNQEPTNSELETLPHPSFITSLLRTKSFILKLIPKDAEAVIVLVGSVEFLEQPAMAFVRLSEAVLLESVLEVPVPVRFLFVLLGPSQSNVDYHEIGRSFATLMSEKVHFTMPVAYFADDRQDLLNGINEFLDCSIVIPPSDVEGKDLLKTVADFQKQLLRKRRDREGKKLPSAHGAEQDSKGTGPEPEVDPLKRSGVPFGGLIHDMRRRYPQYVSDLRDALDTQCVAAVIFIYFAALSPTITFGGLLGEKTEGLMGVTELIISTATLGVIFSLLAGQPLLIIGFSGPLLVFEEAFYKFCQAHDFEYLTGRVWIGFWLIFIVLVIVAAEGSFLVRYISPFTQEIFAFLISLIFIYETFSKLIKEHPLMTVYPSDSTVDVDGPVLNQPNTALLSLVLMIGTFFVAFFLRKFRNSRFLGGKARRIIGDFGIPISILLSVLVDISIPDTYTQVSSGCGVVAVDITEVSSLYVCPSETQCAVWVFRHVSRQERLAHQSVRRQAAVPNMDDGSVRRSRSPRLHPHLHGNTDHLVRLPSDTSGCLHVVYGAFQGQWR | Catalytic Activity: chloride(out) + hydrogencarbonate(in) = chloride(in) + hydrogencarbonate(out)
Subcellular Location: Cell membrane
Sequence Length: 705
Sequence Mass (Da): 78855
Location Topology: Multi-pass membrane protein
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D2Z415 | MTRRIVALDMGTVRIGVAMSDPLGSFAQGVAVWDAEGDWLSDLRDLVTSRDVSTVVVGLPIRENGTKGPSAENVEAKTEAVREAFPDLEIVMWDERYTSTIANRVLIEGDVSRKKRKGQVDKVAATVILQGYLDSLRR | Function: Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
EC: 3.1.-.-
Subcellular Location: Cytoplasm
Sequence Length: 138
Sequence Mass (Da): 15175
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D2R6X0 | MHKLLTVQQHILEEQRRNHPQASGEFSWLLSGITLATKIVAAQVRRAGISADVLGATDSQNVQGETVQKLDVIANQTLLQFLGNRGNVAIMASEENDDPIVVERDRAHGRYVVVFDPLDGSSNIDVNVSVGTIFSVLRREPDPDCSRDTTADVLQPGYKQVAAGYVVYGSSTMLVYTTGHGVFGFTLDPSIGAYLLSHERVTMPDAGTQYSVNEANFEGFPLAYRKFLMQARSGALGRTYSSRYIGSLVADFHRTLLKGGIFLYPPTNSHPKGKLRLLYEANPVALLAEQAGGMATNGTDRILDIEPTSLHQRTPLIVGSKTEVGHLMRMIKEESR | Cofactor: Binds 2 magnesium ions per subunit.
Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Catalytic Activity: beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-phosphate + phosphate
EC: 3.1.3.11
Subcellular Location: Cytoplasm
Sequence Length: 336
Sequence Mass (Da): 36788
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D2Z2L6 | MKQVGIVEYGAGNLGNVMRALKRLGRSGVLLESPDEIPESVSTIVLPGVGAFGPAMDSLRKKGWDRALIEWADRERPLLGICLGMQLFAEGSDENGSHRGLGLIEGKSEKLDMTPLPHMGWNDISTEDPILKPFDGSYLYFVHSYGLKNSKDRAATTEAGKVAFVSAVRKDSVMGLQFHPERSGDVGHAILDRILEELGR | 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 synthesis of IGP and AICAR. The resulting ammonia molecule is channeled to the active site of HisF.
Catalytic Activity: 5-[(5-phospho-1-deoxy-D-ribulos-1-ylimino)methylamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + H(+) + L-glutamate
EC: 4.3.2.10
Subcellular Location: Cytoplasm
Sequence Length: 200
Sequence Mass (Da): 21804
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D2R345 | MPIPVPEVIDTLILDRKKTTMPEPDESSSSPVSATKQAVFAGGCFWCTEMAFEQLAGVSDVASGYIGGSPETANYEAVCTGRTGHAEAIRITYDPAVMTYQTLLDVFFTAHDPTTLNRQGNDIGTQYRSAIFTSDEAELAAARATIARLDASGALPSRIVTTLEPLTEFYPAEDYHQDYARAHPNQSYIMHVSTPKACKVRNYFPKLIRREYLP | Function: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.
EC: 1.8.4.11
Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionine = [thioredoxin]-dithiol + L-methionine (S)-S-oxide
Sequence Length: 214
Sequence Mass (Da): 23549
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A0A194S762 | MARTKPKSTLEPSRNPPTPSLSSTSSSSSFSRPQQPELVPVRHYLPRVPLQLFAVAFSLVAASTSQDKHLAAPARFLQALHREPLKTLPVVCAALAAIQTWFAYSLRSNRIASLARLNHKGTDAPAPAPSRAAAARGTGFRGSLATMWDAAMRGEAPTEALWKKRALRRGAHAKAAIDTSFVGEAIMVTWLGTLAIHACTVLLGAPLTSNLTSTYLFSLLVSILAILPLAIALPLSDTSARFVWLRLASTFTPTDDLELALFAPALGTLVGAWLGAVPIPLDWDRPWQQWPTTPVLGALAGHALGSLVALARIAYGGVVRAAVDVLEEAGQQQQQQQQRGAQQGQGREGGRRKLKGQ | Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 357
Sequence Mass (Da): 38128
Location Topology: Multi-pass membrane protein
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A0A3C0WVB8 | METFPGQCDFGCAQEKIEFPIVFGGTFSPPHKGHLHVLHSCRELFPSSRILVVPSYHTPFKSISEMMPFQERMRLLELAMEDYKDIYPDDNMQGIDVSDIEKNAGKQIATYQLLEMLRRRIDPDGSCGNEFKFGFAIGDDILEKLDKWANPDYLRKHVRFIVFRRILAEASHLAEMRSRLAQEGFDAYYADNDIMEASSTSISQRALTNGRFSEITSSPDDDMLTPRVRGELSKMRDWL | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
EC: 2.7.7.18
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Length: 239
Sequence Mass (Da): 27499
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A0A3D3SCJ1 | AAYGSAADHPYFDLPEIVPLRPITADGTGNRQARLYLLELFHGRTCAFKDMALSVLGGFLRESLSRMGRKEPVLVLTATSGDTGSAALEGLSAIEGIHTAVLYPEKGTSEIQRLQMTTVGLERRFVAGIQGNFDDAQNAVKLIFARAARGEGPLAGVRLSSANSINIGRLLPQIVYYVAAWRALASRGALGAGGLMHVAVPTGNFGDILAAKYAKEMGLPIDRLICASNANKVLADFFETGVYDRRRELLMTESPSMDILLSSNLERLLYMAAGKDPARVSSLMGQLATMGRFAVNDAEKAYLADFSSGWCSDSSAKSAIAQIWESDSLLVDPHTATAVEVAMRLSPRIADDAPIVIASTASPFKFPRACLDALGCEVSGEGDLELAARLAARTGCAMPGSIFSLASKKVLHDRILPVESVEEVLGQYARTKMGAKA | Pathway: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 5/5.
EC: 4.2.3.1
Catalytic Activity: H2O + O-phospho-L-homoserine = L-threonine + phosphate
Sequence Length: 437
Sequence Mass (Da): 46559
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A0A6C1RMF1 | MEYFVEQAASHREAESKIRTKYGDKARIMHHKTIRLGGFLGLFTREGVEVTGYFSHEPPKGRPETSRKSADLEEEKRKILGSVKSEKTIDMVLKELQTIKEKMDQPQQTSVPRTTDHPTLARMEELLQYNDFTPGYIAAMIKRLRATFSIDELDDQEMVEAQLVDWIGESIQIYQPERGDHPTVFVLVGPTGVGKTTTIAKLAAVHGMNGTANGSSQASVRIITIDNYRIGAREQIETYGSIMDIPVACVDSAQEMKKQIALFQDTDVVFVDTIGKSPRQFSQLGEMNEVVRACGGSAQVHLAISATTKTSDLYELLRQFEPFGYRSIIVTKLDETTRIGNVISVLHEKQKPISYLTDGQRVPENLERATVERLLLTLEELHINRRRIAETYAKPNDGESNG | Function: Necessary for flagellar biosynthesis. May be involved in translocation of the flagellum.
Subcellular Location: Cell membrane
Sequence Length: 402
Sequence Mass (Da): 45160
Location Topology: Peripheral membrane protein
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A0A1Y2FD31 | MVGSASSVVANNQGPLSILSVCIASLSMTVANKYIVSGRNFSMNFLMLAIQSIVSAAAVDGAKRGGILDYPDFSWEEARRWAPVSLGLVSLMYSGSKALQHLSIPVYVIFKNLTIILIAYGEMIWFGGTVTSLEFASFVLMIISSLIAASPNISAWLWPPEVLPGLEGVITETSSGLGYLWVVINCLVSAAYILGMRKKIKSMGFTDWQTSFYNNAISIPVLLVASLVTEGWTSDNFSKNFPPADRSYLIFAMILSGGVAVFISFCSAWCIRVTSSTTYSMIGALNKLPVAVSGMIFFNDPVTLRSVSAVSLGFAAGLLYTHAKQLSNEAKKKAQAGELAFPKSCILLRDGELTSNSLPLSLRRPNSLPPFAR | Function: Involved in the import of GDP-mannose from the cytoplasm into the Golgi lumen.
Subcellular Location: Golgi apparatus membrane
Sequence Length: 373
Sequence Mass (Da): 40164
Location Topology: Multi-pass membrane protein
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A0A1Y4VB41 | MSDEKKKAGIRGWFRGLQSEFKKITWPDKDRLVRETVTVAVVSVILGIIIATLDMVLQYGINFLV | 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: 65
Sequence Mass (Da): 7395
Location Topology: Single-pass membrane protein
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A0A6P4Y6X5 | MESLVEELTCPVCLELYEQPVLLPCAHSLCKTCAGEVFAEAARKPPQQAAGQEATPKQALCPSCRHEFQLPELGVEGLRRNTTLQNIVDRYREAKNTAAVTKAVPCQMCDQEPPNNAVKTCLDCNNSYCETCLATFHPMRGGLARHTLTEASAAAPKVLMCTEHPQEKVNMYCATDQSLVCSLCKLVGKHKDHEVAAVSDTFQQKKTSIGGRVAGLIQQNAEVECFVDKIQGTMTKAEQNCTDIQERVEAFAQTLTTAIVKRKGILQLKVAVEKDQKLRTLGKQLDQWADTGTGITAAIAEAETLLNEEDPIAFLQASKAVEDRIAAFKFLEERKLNTTDQFVHNTLGVSDLEQRVSALDFLQEAPRMLTDQCTSGPDYITVCWAAGGNTPVDKYKVWHGKAGEGHVLHAQQTVPSTTKSIKLEDLEENTTYTVVVVAINETGHAASQTVSIETRRGGQLQFKLDKNTAEPPMVVAGDGMSVTCSQNVTDVPLRGQAYGFAQGISRPYYEGYGEPGSLRGYNRPPKSKPLLDSSVLGDAAIGNGQRYWEVNVTGSSDFGLGVAYTVQLQQVMRVDRFQRRGPLNLKQQQQYKHVRVSMMYASFCGYGPNGDKTYKFSYVGMDGKVHIIPPDHERNLTKVGVLLDHNAGSISYYDQNHRLITSQAEQFSEPVFPCLVVKDQGGTLSLVQDCVWPDGSVWSVPGPMV | Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
EC: 2.3.2.27
Subcellular Location: Cytoplasm
Sequence Length: 705
Sequence Mass (Da): 77393
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A0A8B5WKV6 | MTALDARRLGVKTIILDPEPAAPARFYADDFVCGRLDDETAIRRVVSAADVTTFEIEHISTDVLLRLEAEHHVFHPCAEVLATIQDKLAQKKVFKRAGVPVPRFAPADTEWTEWPAVWKARRGGYDGRGVQVVDGPADVPSGVPGMLEVMIPIATEIAVLIVRGADTEAVFPVLEMSFEAGANICTEVFAPAAIPRDIAERATKIGRETVSALGGRGVFAVEMFVTPGGELYVNEVAPRPHNSGHLSIEACETSQFEQHIRAVLGLPLGSTGLISPASMRNLLGAADGEIGRTCVSGLDAALAVPGARVHLYGKSECRPNRKMGHVTALARTLADARERAVRAASAIRITGEER | Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5-amino-1-(5-phospho-D-ribosyl)imidazole (N5-CAIR route): step 1/2.
Function: Catalyzes the ATP-dependent conversion of 5-aminoimidazole ribonucleotide (AIR) and HCO(3)(-) to N5-carboxyaminoimidazole ribonucleotide (N5-CAIR).
EC: 6.3.4.18
Catalytic Activity: 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + ATP + hydrogencarbonate = 5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole + ADP + 2 H(+) + phosphate
Sequence Length: 354
Sequence Mass (Da): 37923
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G9WZR0 | MKKITNKEKYRVLEKSDLQNLKDMNEEIKKSRFRQKFHIQPITGLLNDPNGFCFFDDEWHIFYQWFPFGAMHGAKNWYHMTSDDLVSWKNKGLALKPDTVFDNRGVYSGSAIIYDNKLNLIYTGNHKDERDIRHPYQCVAVLEDNEKFVKKDEPIINMSQDYTEHQRDPKIMYVDNKYYIILGAQDKNLKGRALIYVSDDIYNNWKLLGELKVKGYEDFGYMWECPDLIKIEDKYVLIFSPQGLQANGYKYNNIYQNGYIIGKMDFETLEFIPESEFEELDGGFDFYASQSANQNIYENTAVLIAWMGLPDSSYTTDDENWSGCLTLPRELSIKNGKLVQKPARNLKILRDDVITSHISKDYLQKIETPLEIKLDNINSKNLEINIFSDKNNSSNSGFKISFDNKKCEFTIDRGSLSNKINTNQGSTRTIKLNVLDKLDIFIDNSSIEIFINDGEYTMTSRVFPTDEECMLYIKAKDNIKLEMCRLKELMNEEFII | Pathway: Glycan biosynthesis; sucrose metabolism.
Function: Enables the bacterium to metabolize sucrose as a sole carbon source.
Catalytic Activity: Hydrolysis of terminal non-reducing beta-D-fructofuranoside residues in beta-D-fructofuranosides.
EC: 3.2.1.26
Subcellular Location: Cytoplasm
Sequence Length: 496
Sequence Mass (Da): 57986
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D2Z8S0 | MFDALKERLDGVFGKLKGKGKLTEGDVQEALREVRRALLEADVNYKVVKGLVENIRRRAMERSVLDSITPGQQVVAVVYEELMDLMGSEPKPLTISPKPPTLMMMVGLQGGGKTTSTVKLAKRLSKGHKPLVVACDLRRPAAVDQLRVLAESAGVGFYGPEKGESDVLNVIDGALRYARDRLMDVILFDTAGRLTVDDEMMAELDAMKARIAPHEILLVVDAMTGQEAVSVSEAFHSRMDLTGVVLSKVDGDARGGAALAVLATTGVPIKFAGVGEGIDALEVFDAKRMAERIMGMGDVVGLVEKIEQATSEEDVKRLSSSLKKNKLDFNDLLAQFEQIEKMGPLDKVMEMIPGADKIKELKDGEMDPRRIARMKAIIQSMTPEERRSPAVIKGSRRRRIAQGSGTTVQMVNQLLKQQSQMNDLWKKMGKGKGRKKFQMPKLKGFGGLFN | 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 receptor FtsY.
Subcellular Location: Cytoplasm
Sequence Length: 450
Domain: Composed of three domains: the N-terminal N domain, which is responsible for interactions with the ribosome, the central G domain, which binds GTP, and the C-terminal M domain, which binds the RNA and the signal sequence of the RNC.
Sequence Mass (Da): 49336
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A0A813CCM0 | MAGIQAQTRKAAKIFQSETMARRGVLAVALLAVAATVALRSATAFLPVSKPLLRGGAAGALATSAAAVGALPALAEEEGGLLNFGKVELGGGFALNLNIPDINLVNISILVAGLFYFLGPLLSESMASREKEIQSDIDDAIAKYNEASTRLAEAKKAKEQADAVVKEINESIAKDVKEFQATLDAQAKKSMEAQDKAMDSSLKDMESRSASNLEKYIDSAAVKRGLVELQNLSSSQKTKFMDAAINSLCWCKIPVLSFVSCVDFFEASHHGTCPDFEQALVSMGKRGEKWGQYNGYYSYDSRSWAAWPGPKSKPQNNTAAPEFPSYDVEWKQQDIAPVEERRHVVEQQKPSTFTKKVQAAVNIARKQDVKVAKLTEDQAVKERRWKAYTVKMQQAFMQEHAKHRSNLSKLKHELSDALEAQASAQQQLKEVLAEALRGDGQQGSHTAMWEALMAGHKEMDVEEDLQEDEALLYAQRFMQSAARTAEQEHPGLPQFGAGSAAPTTPPHRRSPGLPMTPPAVAAYVPPKTVDPYMVSPGTAAMAAASIAGSPDMPDRMNNNMDAATNQAAAEQVEEVRPEGPHRPPGPKQRSPVKAIPKIATAPLQGPGLSGKLEARRALIPFGGPGGADNGALSTEGHGPPRGPVFHVLDEGDAELFGHEPTDLPGAASPGLGRLE | 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 catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
Subcellular Location: Membrane
Sequence Length: 675
Sequence Mass (Da): 72467
Location Topology: Single-pass membrane protein
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A0A813CML5 | GEAKSYDTITETARSDSQSSDLLTENSHLLDPSSDPEPAESLLALLQDGNDVAICRDGVDAQPTTYAELRQQLEDQSFASFFRRDDRVALVLENGKEMATCLLAVMHRACAVPLNPTFTEAGYASVADAAAQQNTEAVIEMLSQGYRADIQDSDGNTALHYAAWFRLDSLLTPLLEKRARPDIPNNSGECAVHWAAKSSNVMALDAMTRVNRALLSMRDCDGFTAFIVSAQTDNCPVMEWMYLKGVSLEEQDDQGRTALQWACHKGNKKTVQWLLSRSASIVHRDREGMTALHWAAMQGHTIITEMLMEVGAVDLLDVPDCSGETPIELAMRKNKRTLVMAFHKCQIFKLLFGRPHLFQNNYASLFLGFVAFNIILFAFVVAPGIAARNPEAVMTWSILMGLSLLLWVQCLYSDPGWLQPRTINSQSHLMGKDPAKTFDVDQPIESQMAHCDNVLQKLISTCDGEAPQLMKLELEQNKYNYQRQLLREARKRLEEGCGLGDPRSPALGESQPLIAAGFNDAGSRQAQLDRATVTLHERERAAGDSLGRARVEHLLAQGGGEYLSFVEKGDFKQVCVICRTVREFRSHHVKEQGRCVHRMDHYCPWIDNSVGLGNQRSFFVFVTLMFATVLYFYYTVFLYFFDTVFPEISRGSFSELLQSLTSGSLGAEVSPVLVLLTAGVDLFWVYFLTLLMGRTTANMMVNVTTYETLMKPSHVLRRFPKTRGKWWFLQGWNLRSALSNCIIYWTLDTSGDAAAFCGSPQDSFMAPGQATRGKWQELPEEP | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 782
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 87478
Location Topology: Multi-pass membrane protein
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A0A2N1TG32 | MPYNMKKADMKSITEGYGLHPNRKYGQNFLVDDYTTDKLLKIIDIQTGDRILEIGPGLGALTGKMTERCSRLTAVEIDSGICRYLEDSLGSVPNFTLVHGDFLKTELEDNFTKIVSNLPYYCATEILFTVAGKFSARDIFVMVQKEMADRIMSPPGSKVYGALTVTLGYYYRARAVLQLGNDVFHPRPDVGSTFLHLSRREPRELDDAQLEMFHLLVKSAFWGRRKTLLKTLSESPHLRLEKNLVRSVIAEAGIDEKIRGEELSSGDYIRLALLFAKNDNM | 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(+) + N(6)-dimethyladenosine(1518)/N(6)-dimethyladenosine(1519) in 16S rRNA + 4 S-adenosyl-L-homocysteine
EC: 2.1.1.182
Subcellular Location: Cytoplasm
Sequence Length: 281
Sequence Mass (Da): 31769
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A0A1Y3AKR4 | MNSVKIRDEEEFTTNLLENQWPDTVQLDIATGYFNLIRKYQKKLIHQPPPSPTITILMASEEANGFYQGNGLLRYVPYVYTYYVRNFLRKINTMYNPITIRYYNRPNWSFHGKGIWLQTSEYYLTMVGSTNFGYRSVYRDNEAQLVIVTKNDQLKKKFQSEFDHLIEHSHKIRNWQTDLPRIPLLIPFIANIFRSLF | Pathway: Phospholipid metabolism; phosphatidylglycerol biosynthesis; phosphatidylglycerol from CDP-diacylglycerol: step 1/2.
Function: Functions in the biosynthesis of the anionic phospholipids phosphatidylglycerol and cardiolipin.
Catalytic Activity: a CDP-1,2-diacyl-sn-glycerol + sn-glycerol 3-phosphate = 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycero-3'-phosphate) + CMP + H(+)
EC: 2.7.8.5
Subcellular Location: Mitochondrion
Sequence Length: 197
Sequence Mass (Da): 23547
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A0A0G1IHL1 | MISPQQYLENLVKKAARKLTAKLPHFEMESKNISRFGDYSSNVAFSLAKILKKSPIEIARKIKSDLEENRYLDKIEIAGGGFINFFFKKDFWLEMFKNPLAKINPGKGKKVIIDYSSPNIAKPMHVGHLRATLIGDFLARLYKFLDFKVIGWNHLGDWGTQFGMLIAGYKKWGDKKKINKEPIRELLEIYVRFNREIKNNPRLLKQAQEEFAKLERQDKENKKILNWFLRVSLKEFNQLYKKLGILPFSVVKGESEYEKQLIPLINDLKNKGVAILSQGAYIIPLEKYSLPPALVQKSDGATLYLTREIASLIYRVKKYQPDEILYVIGSQQNLHLKQLFAIAQIAGLSGKAKLRHVSFGWVLGPNGKKLATREGEIIEAQKIVDQIINTARKIVSQKRKDLSKKEKEKIARIVGLGGLKYNFLKDGRNSDIVFDPKKALSLQGNSAPYLQYTYVRLKSILAKTKTGKGDFSLFEDKDIEIIKKLTAFEDVLENCLKDSSSHHLAEYLFGLANLANNFYETTPILKDKNIKRRNARLALIKAAAGNLETGLELMGIETLNRI | Catalytic Activity: ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg)
EC: 6.1.1.19
Subcellular Location: Cytoplasm
Sequence Length: 562
Sequence Mass (Da): 64169
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A0A0G1XKI8 | MGKIAAPLGIGVDIEEIKRFRGKKLPRDERFLKTIFTPRELTYCFGKSDPGSHLAARFAAKEAAWKALTAAKKLNSHLAPFLRDVEILNETNGVPRMTFFSPKLRMRSASVSLAHSRTYAIAIVCVS | Function: Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.
Catalytic Activity: apo-[ACP] + CoA = adenosine 3',5'-bisphosphate + H(+) + holo-[ACP]
EC: 2.7.8.7
Subcellular Location: Cytoplasm
Sequence Length: 127
Sequence Mass (Da): 14120
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A0A1V6FZQ0 | MIEINFTLIIQIINFLALIYILNIVLYKPILKVLEERDQRIDGQQADAKKVVEDCQALMVDYNQKLYNAKVEAMNAKNAARNEASEQANGIINDARKKAEETISQMQEQMASEIAMAKKELEPELEVMAATIAQQILGRKAA | 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: 142
Sequence Mass (Da): 16010
Location Topology: Single-pass membrane protein
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A0A4R1BSG7 | MANSALLEDGILDAGLEDAEAKRELARLFDRNFIDLATEADAIRRELHPNDIVTYIVDRNINYTNVCWVACSFCAFYRTKRQEQKGDGYTLSIEQVLQKIQETVDLGGTGILMQGGLHPDIGMEYTTDLIRAIRREFPQVHVHALSPAEIWHLVDKSGLSLEEVLRELKAAGLMSIPGGGAEILTDETRRRISPAKNSTQAWMEVMETWHSLGMKSTATMMFGIDESYEERIEHLLNVRKLQARTGGFTAFIDWVFQPDNTTYLKKHPDFKKASSLDYLKTTAIARIVLDNIPNIQASWVTQPMKTASIALHAGCNDMGSIMIEENVVKEAGAEYHTTEAELRSIIERSGFRPAKRSTLYDRSFEPGISPEDF | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Pathway: Quinol/quinone metabolism; menaquinone biosynthesis.
Function: Radical SAM enzyme that catalyzes the cyclization of dehypoxanthine futalosine (DHFL) into cyclic dehypoxanthine futalosine (CDHFL), a step in the biosynthesis of menaquinone (MK, vitamin K2).
EC: 1.21.98.1
Catalytic Activity: dehypoxanthine futalosine + S-adenosyl-L-methionine = 5'-deoxyadenosine + cyclic dehypoxanthinylfutalosinate + H(+) + L-methionine
Sequence Length: 373
Sequence Mass (Da): 41989
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A0A2E4HQS4 | MKIVIKFGGTSVGNGKRINKVCDFVSKLNEKNQIIVVSSALHSTTDELVKLAESAKKGKMELEVFDIITQRHKKTASEIIHDKKIQNELLESISVLLEELEKTVNGVITVKELSNKTLDKILSFGERLAVLIISAKLRDAGIESKSFTGGEIGIMTDENFGNASPLVKVTQHNIKKNLSGLEKTVPVITGFIGVTQQGEISTIGRGGSDYTASLIGMCFDVDEIWIMTDVNGLLTANPKIYPNAKTIPQLSYNEATEMAIMGSKGMHPRALEPAKLANIPVRIKNTFDPEGPSTLINEEVNVKKDEITKAITIINNLAMVTVSGMNMVGNIGTAGEIFGILGRNNVNIIMISQSISEANITFLIKQNELQKAVSVLQVGLLGKSSVNNIHSDDEVAVIGIIGAGMKGTHGVATKLFSAISSKNINVKMIAQGSSEQNISFVVKESDCKLATEAIHKQFNMDK | 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: 462
Sequence Mass (Da): 49904
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Q65FJ5 | MNKSVIPSLITVGNFVSGISSILLAFRGYLFLAIIFVLIGAILDSLDGMAARRLNAVSPFGKELDSLSDIITFGVAPAIITYSIVFYDAPILGLPSTLLFPVCGALRLARFNIQSENQDYFTGLPITAAGTILVCLNLFSEILGKKPFILIMLFLSFLMVSKIKVISLKGKKLLKKVS | Catalytic Activity: a CDP-1,2-diacyl-sn-glycerol + L-serine = a 1,2-diacyl-sn-glycero-3-phospho-L-serine + CMP + H(+)
EC: 2.7.8.8
Subcellular Location: Membrane
Sequence Length: 178
Sequence Mass (Da): 19263
Location Topology: Multi-pass membrane protein
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A0A7S3XYZ3 | KKNKKRKSTPGRRKMAEHNDKRRKVDESKESESSSVKQPVHFLDYGAGNVRSVRNAILKCGYEIVDITRPEDIAEANAIIFPGVGSFGAAMQNLRDKGYLEPLRAHLQAGKPYFGICLGMQTLFEASEETPGVEGLGIIPGTVTKFDSTQCSVPSIGWNGVLKHKQSEIVAPIGEHELVYFVHSFRALMTEANKDWVLTSTTYGGSNYISAVQKGNILATQFHPEKSGQTGLKIFEAFLSRAGQLDPEPTPIEVPADATTAIAKRVIACLDVRSNDAGDLVVTKGDQYDVREEGDGDQGGKGQVRNLGKPVALCARYYQDGADEVTFLNITSFRQCVIGDLPMLQVLEKSSETVFVPLTVGGGIRDYEDGEGNKYSALDVASRYFRAGADKVSIGSDAVYAAEEYLEKGAPQGGSSIEQISHVYGAQAVVVSIDPRRVYVDGPGDAPKHTVFELPAPAGPEGKRFCWYQATVKGGREGRDLDAVALAKACQALGAGEILLNCVDSDGQCNGYDLILTKAVREAVTIPVICSSGAGAPEHFSQAFRETDVQAALAAGIFHRGEVRISAVKEHLVAEGIPARSMAQV | 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 glutaminase domain produces the ammonia necessary for the cyclase domain to produce IGP and AICAR from PRFAR. The ammonia is channeled to the active site of the cyclase domain.
Catalytic Activity: 5-[(5-phospho-1-deoxy-D-ribulos-1-ylimino)methylamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + H(+) + L-glutamate
Sequence Length: 585
Sequence Mass (Da): 62915
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L8HDV4 | MTSTLPRRLALEEVNAFNAEDFHRLFDSIFEHSPWVTEGAWQLWTGSYGKVPLRSAVHLWSLFSVALYGASKEDQMRLIRAHPSLGDVARIATDESRSEQRGAGLLSNLTPEEHAELLRLNSAYSSKHAFPFILAVKGHDKHSIVAHLRRRAENATEIEFDEALDQIARIGWFRLLDKIDDGRTPPSTQPPTSLPPTKAGL | Pathway: Purine metabolism; urate degradation; (S)-allantoin from urate: step 3/3.
Function: Catalyzes the stereoselective decarboxylation of 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU) to (S)-allantoin.
EC: 4.1.1.97
Catalytic Activity: 5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate + H(+) = (S)-allantoin + CO2
Sequence Length: 201
Sequence Mass (Da): 22562
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R4YS31 | MSTADRWLLPDGIEEVLPPQARGVEQLRRHLLDDFDRWGYDFVIPPALEYLDSLLTGTARDLDLQTFKVTDQLSGRLMGLSADTTPQTARIDAHSWAQEGVSRLCYCRTVFHAKAPSILAGRTPTQIGAELYGEAGAGADIEIISLMLNTLQQAGLQDLHLDIGHVGIFKAFSAKAQLSNVAEEKLFALLKVKCATDLDAWAEEYLTDPALTTAFKAIVRLQGGIEVLDQVAEKLAAVVPEVTGIIEHLKQVCQAIAARYNVPMYFDFTDLRGYNYHTGLVFAAYVPGYGDAVAQGGRYNETGAVFGRARPATGFSADLKVLAQLGRFAPTQADIVKAPAPYGQQQEQELLDLIAELRAQGTRVEVQLSGELPTNAARIELKDGQWKLIESN | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
Function: Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine.
Subcellular Location: Cytoplasm
Sequence Length: 392
Sequence Mass (Da): 42845
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V7N473 | MQCCVLLKYGEMVLKGGNRRWFEQWLLTNLDDALSAWPPEHRPAVRRRGGVLVLFTSPALQDELVALARNLIGISLVQPVWRVPRSARAAETAAVELLRDHCTQDGAPTFAVRCHRRDKRFGLSSEQLAARIGARVRADLGWRVDLSHPELELTVEVDRREMFLGTRTHPGQGGLPVGSSGRAVVLLSGGFDSPVAAYRAMRRGLACDFLHCTGAPFTDASSTYKAYALVRQLTRFQPRSRLYVAAVGRAQRTLAASGAGEAQIVAQRRLYLRLACGLAERIGAQAVVTGDSLGQVASQTLPNLAATEQAATLPVLRPLLGFDKQEILAEARRIGTAEIAMLPDQDCCQLFLPRRVATHAAVDQLLPVEARAGVDTLVATCWTVCSDSISDLRPPMSSPPRRHPGWANPCARPAGARSRRMRSACPACAARGNAAGWTPWRPPSPRRG | Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
Function: Catalyzes the ATP-dependent transfer of a sulfur to tRNA to produce 4-thiouridine in position 8 of tRNAs, which functions as a near-UV photosensor. Also catalyzes the transfer of sulfur to the sulfur carrier protein ThiS, forming ThiS-thiocarboxylate. This is a step in the synthesis of thiazole, in the thiamine biosynthesis pathway. The sulfur is donated as persulfide by IscS.
Catalytic Activity: [ThiI sulfur-carrier protein]-S-sulfanyl-L-cysteine + a uridine in tRNA + ATP + H(+) + 2 reduced [2Fe-2S]-[ferredoxin] = [ThiI sulfur-carrier protein]-L-cysteine + a 4-thiouridine in tRNA + AMP + diphosphate + 2 oxidized [2Fe-2S]-[ferredoxin]
EC: 2.8.1.4
Subcellular Location: Cytoplasm
Sequence Length: 448
Sequence Mass (Da): 48748
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A0A6H1A2G9 | MTTRGPFDVWAPRPERVRLLLGDPAQGPVIAMSRGDDGWWTPDEPLPPAADEPSVDYGYLLDDDPDPRPDPRSRRQPAGVHGLSRLERTSWTWTDESWTGRQLAGSVIYELHVGTFTPAGDLDAAIAKLDHLRSIGVDFVELMPVNAFNGTHNWGYDGVGWFAVHEGYGGPDAYRRFVDACHGAGLGVVQDVVHNHLGPSGNYLPLFGPYLKQGSNTWGDLVNLDADGSPEVRRYILDNVRMWLEELHVDALRLDAVHALSDSSTPHLLEEMAVEVAALSAHQRRPLTLIAESDLNDTVLVTPREGGGLGLDAQWSDDFHHALHVALSGETSGYYADFEPLEALAKVCERGFFHDGTWSSFREREHGRPVDVEHMPTWRLVVCNQNHDQVGNRARGDRPAEHLDVDQLACAALLTLAGPFTPMLFMGEEWAASSPFQFFTSHPEPELGRATAEGRIAEFARMGWNPDEVPDPQDPETFRRSVLDWDELATGHHAVVLDCYRRLAELRRKLPALTDPDFTSVSCTVEGRVLTMRRRDVLVVVNFGDSAATLPVDHSALVFATPSGAVLDAGVLSLPRHAGALLLRETTPDRGIDRGLNRASTRASHGHHTGGRLSSMTVTEESAPGRLVDVHGDGDRGVVLLWHGRGADSRPELAQLGATIAQHGVRVVVPDWDCDDPDGGRTALLASLSHARRVAEQIGADPQEIVLVGWSLGGTAALGLVTWLDEPVARVVLLAPGDGPNAIVPFTGEPLPEVFPHGAGRPLVQFVSAVDDDIVSPALVRGLASRLTAAGWATSWTDLEADHWSIAMTRFDEVADRGVPTDDPAALATGRRVAEIIASPPGS | Pathway: Glycan biosynthesis; trehalose biosynthesis.
Catalytic Activity: hydrolysis of (1->4)-alpha-D-glucosidic linkage in 4-alpha-D-[(1->4)-alpha-D-glucanosyl]n trehalose to yield trehalose and (1->4)-alpha-D-glucan.
EC: 3.2.1.141
Subcellular Location: Cytoplasm
Sequence Length: 843
Sequence Mass (Da): 91557
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A0A151U105 | MASSLILRASRRFVKPAYAASLLIPTQQFVSQSPTTPSPPFKPTQLQNFNFEFRKSVGCVSNFHLVAYLSTSPSKEDNKQSGNVSSSGAGDTSWIDLYLPRQVQPYARLARLDKPIGTWLLLWPCMWSISLAATPGQLPDFKMMALFGCGALLLRGAGCTVNDLLDRDIDTMYFFLSALILIGDIEIVILCCKLIVERTKLRPVASGLLTPFQGLCFLGFQLLLGLGILLQLNNYRKLTTPNTFDIFIGLNTPYFGCLILVARLLISSHEEVYILGWAAVKGSLDPSVVLPLYASGVFWTLVYDTIYAHQDKEDDLKVGVKSTALRFGDSTKEWISGFGIACLGGLAVSGFNAEIVGWPYYASLAAASGHLGWQIWTVDLSSRADCNRKFVSNKWFGAIIFGGILAGRLSS | 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 coenzyme Q (CoQ) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB, generating the first membrane-bound Q intermediate.
Catalytic Activity: 4-hydroxybenzoate + an all-trans-polyprenyl diphosphate = a 4-hydroxy-3-all-trans-polyprenylbenzoate + diphosphate
EC: 2.5.1.39
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 411
Sequence Mass (Da): 45069
Location Topology: Multi-pass membrane protein
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A0A2N1JB77 | MSTKHIYEVSNGLVEKAVYGAAASNPSLRVFSPHRVVYDASHALDKVGIIAGGGAGHEPTFTGYVGRGMLTTAVSGDVFASPSAAAISSGVDLTPTEKGLVVIVNNYTGDRLHFGLAAEKARTVFKQEKKGKEVEMVVVGDDVSVGREKGGLVGRRGLTGVAFVCKALGAAAEADWETKKLGEFGRVMVDNIVTCGSSLDHCHVPGREKGDEERGALGPNAIEIGMGIHNEPGVQHIDDKPSSEDLLKHMLKLLLDQNDKDRAYVKFEKSDDPVLVINNLGGMSELELFAIAADVKRLLQSEWGLKPVRVYVGTYITSLNAPGFNITLINHKRIQSATGSDLLSLLAAPADAAGWVGVQNGWSDKASQSSLDDDLQESKERLEAKHKSGFSVSGSATSGARAENGPTCDAAQMGKALQSACEAVIEMEPTLTKYDTIVGDGDAGETLRGCGEAVLAALKENKIPLQRPTAALLGLDDVLESNMGGTSGALYALFFTGLVQGLLSSTKDSSEAASVKHWGVAAMSALENLGNYTPARPGDRTLVDALDPFCRTLDEEGKKGTAAVPAVQAAVKAAKDGAERTRDMTARLGRATYVGETKEKVPDPGAWGVWALVEGLLKSLE | Pathway: Polyol metabolism; glycerol fermentation; glycerone phosphate from glycerol (oxidative route): step 2/2.
Function: Catalyzes both the phosphorylation of dihydroxyacetone and of glyceraldehyde.
Catalytic Activity: ATP + D-glyceraldehyde = ADP + D-glyceraldehyde 3-phosphate + H(+)
Sequence Length: 621
Sequence Mass (Da): 65400
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A0A354ZED5 | MIGAFESNSRKAPRSIPMEKRTKIVATTGPACGDLATIRELIREGVDVFRLNFSHKTYDEANNEVTMIREARKALDKPVAIMADIKGPAVRLYGYTEPLAIQPGAELTIESTEAVGIEKLAAKKPMQVYTNLPDIDRICAVGQKVILMDGYFTGKVVRKVPKGIVMALENEGNLRPKAHLTLPGVDYPLPFLSEKDISDINWAVEQDIDYIALSFVRCETDVEEVKRLVQRTALAQGKNTLIKLIAKIESARGLENIDEIIRTADGIMVARGDMGVEMSIENVPIAQKQIIRKCYLAAKPVITATQMMESMMENPMPTRAEVSDVANACFDSTSAVMLSGETAIGKYPVQVVRMMRTVIEAVEKEFDYLDFHHDVPPEVQNGDVPAIMSYNAVSVAYRCDAKALIVLTETGHAARLLSRLRPRMPIYAFLTNERLYHQMAINWGVLPFIHSGKGTRLDAVVSEAISICKHKALLKKGDRVVIVAGLPLARQGTTNMIRVETIE | 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: 503
Sequence Mass (Da): 55652
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A0A352ZBQ9 | MRIALLGGSFNPPHIGHIILAEEILGTLDYDRVLFIPANIPPHKEPQGDPGTDMRLAMLHATLEGWSEFAIEPCELKRPGISYTIDTLREISRKYSFDGKPGLVIGDDLAPDFLKVWKDPELILEYADIIVAHREHAEELILPYAHRYIDNLLIPVSSTLVRERIANHGAWRSLVSPGVQEIIETYGLYRNI | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
EC: 2.7.7.18
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Length: 192
Sequence Mass (Da): 21685
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A0A354ZFB4 | MVTIAFPESLKGLHIHLVGAKGTGMTALAEILHTRGALLSGSDVADVFYTDGILHALGVKLFESFDARHVPEETDIIIYSAAYSLAANPELKAAIQRHIPIFSYPQALGALSLHSRSAGIAGVHGKTTTTAMAGILMEALSMPATVLAGSAISNFNGRCTLIRGGDYFIAETCEYRKHFLNFKPSWIVLTSVESDHQDYFPTYESIRDAFVEYVLSLPDNGVLIFCADQPGAVDVADIVLQKRKNISFVEYGFSAKGKYKIRDFQTSAGTNTFMVSDAPKPLQLHVPGRHLVLDAVAAIALAESIFEAQTSRNFGQDEWNRIAAALTSFRGSKRRSEIIGEFRGVLILDDYGHHPTAIRVTIEGIKKFWPQRRLVVDFMSHTYTRTIALQDEFVTSLDEADAVVMHKIYASARERPIPEFDGKTLFHKLCARRADLIPIDLGLVSGKGMASDQELTRRPATPGPNSSSKGGFALYSEEPLDAQNSLLDLLRPGDIFLTMGAGDNWKLGKAIADKLREGRTSQTSEKIQEQP | 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: 531
Sequence Mass (Da): 58204
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A0A812JXE5 | MVLPAAALNDPRGQEVDETSLSKGRLDWLLQVIKSAPLALASELSHHRALFPLAIAQMTLLADQPLLSTNMSAVANEFGFAGAEKDEKLGGIVSVVFFACGVVSSLIVGRLADVMKRSTLVCLCMLIGSTGTFSNSQAESFTSLLFGRAAVGAAVGGLIPTSFAVIGDMCPAEERPHAIGVVCIISGLGLPVGQSLAGFAGSASGWRAPFAVVGIAGWCVTLLLFFIHEEPARSNDQHLSHDVSSWSALTKPTVLCICSQGVFGCIPWAVIGTFLTDYLAVNDGMGVAGATSVLFCMGVGFIIGTIAGGKLGQHLYKKDKKLQAWLTGLTMWGGMLPLFVLFSTDRPDWPFMFHILALVGVFFAAFSPVNLKAVLLNSVATQSRGTVFGVYNIMDDLGKGLGPALVASWVRHLGRRNSFMLGMAFWLPSGLICLLMARTIPHDDLVEGEEQLTAPSENIIGIEQFGIATPRECMVNCQRQRGICNCWSWKDDGFCRTGSALRCTYTASEDDDRWMFGTCPLRGGQNADAAPPTPAEPAKVQDLRGAMSSSGIETQPTRPPAQALSLPEARPPAPLPALGSASQAVAQNAAAEPRTQGIPVATLLPSRDGATMKPEGGSPTLATEPPPDSAEMCPVLMITHKRANYLQRALASIFQQRSDPARFPVIASQDGDDAEVLKTLEEFLRSGRLFKRLQFQPKTFLPTGYERLSHHYGWALGQVFDTFGYQQAIVLEEDLEISPDFFSFFDATRPLLVADPDLFCVSAWSDNGKPDVASNVTAVYRSDFFPGLGWMLLRSFWEEVKDRWPAKYWDDFLRRADVRKGRHCLRPEVSRSHTFGETLCPAFLCRSSV | Pathway: Protein modification; protein glycosylation.
Subcellular Location: Membrane
Sequence Length: 849
Sequence Mass (Da): 91829
Location Topology: Multi-pass membrane protein
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A0A1E7TUS6 | MNSEFSKAQAGSYAFIGGGQMATALISGLIRAGLPPRAIVVFDPDAAQQERLHASLGVDVGGRVDDRLAGAEVVVWAVKPQVLRQAVQQASAHLRAPLHISIAAGIRCVELSGWLASARVIRAMPNTSALIGASVTGLTAAPEAAPADRRVAQDVLATTGHCFWAENDERLNAVTAVSGSGPAYVFHFLEAFQAAAQAVGFDEVTARELVLKTVAGAVQQAQSGDAFGTLRERVTSKHGTTEAALAQLDAARTAQALKDAVAAACTRAEAISREFAQQA | Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-proline from L-glutamate 5-semialdehyde: step 1/1.
Function: Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline.
Catalytic Activity: L-proline + NAD(+) = 1-pyrroline-5-carboxylate + 2 H(+) + NADH
EC: 1.5.1.2
Subcellular Location: Cytoplasm
Sequence Length: 279
Sequence Mass (Da): 28963
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A0A0G0QQZ8 | MSEINTENAQASGNQNDSGTSLSYDLLVFLWEVAKVVLISLAIIVPIRYYLVQPFFVKGPSMESNFHDKDYLIVDEISYSLGEPKRGEAVIFRYPANPKEFFIKRIIGLPGEEVLVRDNKITIFNRENPEGIILKEEYIDSNQVTSGNMRTRLDENEYWVMGDNRMNSHDSRAFGPVNKSYFIGRATLRLFPFDRIGVIKSPTY | 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: 204
Sequence Mass (Da): 23401
Location Topology: Single-pass type II membrane protein
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D2R5T5 | MTSARQTVSYLTSRFREAGIRPEIRHGQNFLVDLNLLDLLADAAQITEDDVVLEVGTGLGSLTSRLAERAAEVVTIEIDERLAAMAEEELEDFDNVTLVLRDALESKHKLSTEVMDIVRAKLAEAPGRRFKLAANLPYNVATLIISNLLASDPCPVSMTVTIQKELADRIVAPHGTKDYSGLSIWVQSQCEAKIVRIIPPQVFWPPPKVHSAILHLEHSQALASQLRDPAYFHSFIRAIFLHRRKFLRGVLAKLFDGQLTKNDIDQLFVEKQLTPETRAEELPVATLVELSHWLLDRGLKVELASDQK | 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(+) + N(6)-dimethyladenosine(1518)/N(6)-dimethyladenosine(1519) in 16S rRNA + 4 S-adenosyl-L-homocysteine
EC: 2.1.1.182
Subcellular Location: Cytoplasm
Sequence Length: 308
Sequence Mass (Da): 34484
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A0A137PEH3 | MKYQLKYHDNVFDIEAEPYSKISDLRLQAEQHFGLQENTVVLFYGNALEERKCLGQVGIRPGATILVYLRPGSNSALRTQNPIPSKSIYSHQEPIRKGKYISSNDHRSKYNNNSSNYNTGSKNYRSQYNNNDNSKYNTESSNYRREYNNRSNYNTGSNSYRSQYNNNSNYNIGSSSCRREFNNNSSSKYNTESKKNRDCSLCKDKRSQKCTRCGCGICFEKNPENLIRCTKCPKNYHTQCLQISLNSIPKNSWVCPGCIRENGHNPRIDRAQSSHHHSSNNSNFSNYHRTQSSNNLVRDTNVKLEPRSASISNGYHSPNSYQNTPITNNLIRDTNEAADTKPPRKIKTETKFHLGKIPGVPVGTSWEWRKEVAEAGVHRPHIAGISGNNTDGAESIVLAGGYIDDEDYGNEFIYTGSGGSTAPLPDPNKKEHQELTRYNYALALSCDAPINNVTGAKARDWRNSKPVRVIRNFRLKKYHPGFAPISGNRYDGLYKLVGYRPEKSKHVNGSIVWRFLFRRDDDEPAPWTPEGLKRSMELGLKINAVLNTSTQKIPSTSSSNQGFNHQNAQNSNQYQNTGSNGNNNTQFVHSFNNLNLNPQNNPYEVSQSTVYNQKRLSQNEDRRRSSDFNDKTDGINISSSTNSHILHSSSTSPNPSHTAVSSSRYNIPDDIQDLIYSDTQNGVIWENIIEAEDEIQFAKMVLSSFKCPMCFELVNNPLTTKCGHNICISCLKARYYDIDNKCPTCKSIIFSELENISEQKKIELTKDVINNYPVNTTLNTILNRIFPSRDLNGSIWS | Pathway: Protein modification; protein ubiquitination.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
EC: 2.3.2.27
Subcellular Location: Nucleus
Sequence Length: 797
Sequence Mass (Da): 90402
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A0A084JFZ7 | MFFNNFLLLFQFITRIPVNISLACEKENFKKATLYFPVVGAILGAIEYLIFYITSIWLPLPMVAIITVIVGIFITGGLHMDGLGDTCDGFFSFRSRERIIEIMKDSRVGSFGVLAMIIDIAVKALGIYYIGTKSIGYMIIVVPMISRLFTVFIALIGKSAKKEGTGNFYIGNTNGVYFTGALTLTLLIGSLFFNIKYIIILLLGGLIVTIIFNLFCNSKIGGHSGDTLGANNEIVELALFILISSMIF | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7.
Function: Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.
Catalytic Activity: adenosylcob(III)inamide-GDP + alpha-ribazole 5'-phosphate = adenosylcob(III)alamin 5'-phosphate + GMP + H(+)
EC: 2.7.8.26
Subcellular Location: Cell membrane
Sequence Length: 248
Sequence Mass (Da): 27296
Location Topology: Multi-pass membrane protein
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A0A3B5LHJ7 | TTKTMTNMDYEKPVDYESRSSYSFSVEVLNPIVDPRFLRRGPFKDRASIRVAVLDADEPPRFSRSKYHMDVSENCPPACTVGRVSAVDPDTGLTNNIRFSIDPQSDPEALFRISPETGLITTAMELDREREHWHNITVIASQRGQRPHRCVIRAFFLLLLFTGLCPTASLVLLSQLQPLSRSPSSTLTLYVPLVLRDGTSGLTSTGTVTVSVCPCLRGGALCLPQQSMLPSPGLSTAALLAILACVATLLVSALSLSLRRQKRDSLSPLEEDDVRENIITYDDEGGGEADTAAFDIAALQSQMGLGGYVLGRRDMSPQLLPFPGQGPQGPGGPSLALRVGEFLRLRLAQVTFDPSQPPYDSVQVYGLEGTGSRAGSLSSLESDGEKEDWGVGLEDWGPQFQKLAQLFKNREKAREDQEKVEEVAKKEREQKEESDKTEKREVEEARDEGKD | Function: Cadherins are calcium-dependent cell adhesion proteins.
Subcellular Location: Cell membrane
Sequence Length: 451
Sequence Mass (Da): 49576
Location Topology: Single-pass type I membrane protein
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R6PI92 | MRELEFLKVIQNTLADSSLIGDDCAYLEEFDICVTQDTLVEGVHFLTHTTTPFKLGQKAVNVNLSDLAAAGARPLYITVSLSLPRASDENFVQSFYQGVQDSCQKYGVKVAGGDLTGADNYFISICAIGKKYNNVKVSRSFAQKGDIILTTGTHGDSAAGLALLQNGINKPKNLINKHLVPLPAIEQSEYIMQTLKDAGIEKLAMMDTSDGLQDAIFKLSKASNLEFDIETIPAGKDLKTTFPKDWKDYALWGGEDFELIFTIPPFLYKYFNTPQFIKIGTVSDRPFSNALEKEFEQKSFKHFEE | 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 + thiamine phosphate = ADP + thiamine diphosphate
Sequence Length: 305
Sequence Mass (Da): 33868
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A0A8H4X903 | MFTRVFMGGYFSKSLARFMIRFSSWWLGAAFIFLYMWTVSVINAVHRGTTAATVSQWYFHRNAGPATPSREIVAAALNHALTTIFGSICESTLLSLLIRAPLIFLPRRLGAAVANIASFWIPTPVVALMNPLTITYSAIHSQNLATSARGLDQMELVSPAIPTTTLTPRALRHRGQPNGLLPYRLAKLLLVATRLIMATGLGFAGWVITAKQLRIQMPDGMGVRGSAYAYVVGLMASFIGYS | Function: Probably involved in transport through the plasma membrane.
Subcellular Location: Cell membrane
Sequence Length: 242
Sequence Mass (Da): 26454
Location Topology: Multi-pass membrane protein
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A0A6N2E830 | MADKERYQMLVIGAGPAGYVAALRGARLGLRTALVDKRPTLGGTCLNVGCIPSKALLDSSEQYHKALHGLEAHGLKLTGVTLDLPTMMKRKDSVVEKLTGGVAMLCKKAGVDVYTGTARLVDAHTVEVSGGGGAGGSGGAGGENGAGSESMSISELTANAVVLATGSVPVELPSLPFDGKQILSSTEALSLETVPKQLAVVGAGAIGLEMASVWARLGSDVTVIELQPNILPGWDPRLSKVLQQEMEKAGVKFHLGAQVEESKQSKKGVSLSVKLKDGSSATVEAQKVLVAVGRKPYSEALGLEALGVAGEKGRVTVDEKFRTSIDGIYAVGDLIHGPMLAHKAEDDGFAVAEIIAGKPGLVDYSTVPNVVYTWPELAAVGSTEAQLKEAGIPFTKGQASFGANGRALAMEETAGFVKILAHAETDKILGAHIVGPWASDLIAEIVVAMEFGGSAEDLARTCHAHPTLSEVVREAALSAAGMPLHSA | 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: 487
Sequence Mass (Da): 50222
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A0A9D9M8Y5 | MQKVFADTRTLDADARKKYSITEEVMMENAASALEKEVLEFLAGCSTPKPVVLIVTGTGNNGGDGYALARRLCGKTLSDGRKINVCIFAPKPPKTEIAVFQKETAVKTGVSFVNTLENTNPDVLVDCFLGSGLSGKLTQDAENLIKRLNEIKAFKIACDVPSGLSAESDTFFIADKTVTMGALKTQLFCENGKDSAGTVVCADLGISRDCFELSDSAVQPEAYLLEKADLLLPHREKNNVNKGTFGHLAVWGGEKRGATVIASKAAFAFGTGLVTVVDNANNGSFTVPEDILCSNTVPSNISAVAAGMGLGAFCDTAVSYLCANPKVPCVIDADLCHSVKLPELLFARKNLANTVLTPHPKEFADVLEICGFGKYVVEQVQQNRIGLAKKFCDKYPDVVLILKGAVPVIAAFKDGAPVVYLNPWGRPCLAKGGSGDVLSGLVGALLAQGYDALKAAQSASLAHALASCKVECDYAMTPFELIECVKKL | 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 is a result of enzymatic or heat-dependent hydration.
Catalytic Activity: (6R)-NADHX = (6S)-NADHX
Sequence Length: 488
Sequence Mass (Da): 51735
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F2IA69 | MADGEKIIQINIEDEMKSAYIDYSMSVIVSRALPDVRDGFKPVHRRVLYGMQDLGVYSNRPYKKSARIVGEVLGKYHPHGDSSVYDTMVRMAQSWSLRYPLVDGQGNFGSVDGDSPAAMRYTEARLRKIAEEMLDDLEKETVDFAPNFDDSLQEPTVLPSKIPNLLVNGASGIAVGMATNMAPHNLGEVVDAIIGYVDNKDIEDEELLQFVKAPDFPTGGIIYGVDGARDALLTGRGRIVIRAKAEIEESGGREQIIVTEIPYQVNKADMIKKTADLVNDKKIEGISDIRDESDRNGMRIVYELKRDAIPNVVLNKLYKYTSLQSSFSINNICLVDGRPRLLNLREMITEFVKFRHEVVVRRTKYDLRKAEERAHILEGLIIASDNIDEVIAIIRSSKSPEEARERLMERFALSDLQSRAIVEMRLRQLTGLEQDKLRAEYADLMALITDLKDILAREERRMQIIKDELIDIRTKYGDARRSRIEYSASEMKIEDLIPDEEVVITISHAGYIKRTNLDEFKVQSRGGMGSKGSTTRDKDFLEHLFVATNHNYLLIFTEKGRCFWMRVFEVPEGNKTAKGRAIQNLLNIEQDDKIKAYVKVKDLTDKEYVQNNFIVMCTKEGIIKKTSLEAYSRPRANGINAITIRENDELLEARLTDGTNEMVLATKAGRAIRFNEAKVRPMGRNASGVRAVTLQNDTDEVVGMICVKDNTETIMVVSEKGYGKRSFLNDPEDGEPVYRITNRGGKGVKTINITDKTGPLLAIKTVADEDDLMIITKAGVTIRMHIDGIRVMGRAAQGVRLINLKGTAAIAAVARVPRSDEEEEFEGEDGIIVAGPVEEISDDSTEPDDSTEDTTETNSED | Function: A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner.
Catalytic Activity: ATP-dependent breakage, passage and rejoining of double-stranded DNA.
EC: 5.6.2.2
Subcellular Location: Cytoplasm
Sequence Length: 861
Sequence Mass (Da): 96625
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B2KEI7 | MKIIFMGAGKMGHAILSSAIQKKALKKADVVVIKRNTGDLKKEGYKVFNSLSELPSGYLADLIVYTVKPNILEDIIEESKPYLKEDGFVISIAAGKTIKTMQNILGTKTAVVRAMPNLPIAVGYGVTGMYASNQVSKKQKDFCDKIFNSSGISFWLKKEADINKVIGAAGSSPAYIYAVISSLEKVCLGYGFSKELSSKISKYLLLGCAKLMQQTGDSPEVLNKKIATPGGTTEAALNFLAKNKILDKLILKAAKKAETKFPF | Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-proline from L-glutamate 5-semialdehyde: step 1/1.
Function: Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline.
Catalytic Activity: L-proline + NAD(+) = 1-pyrroline-5-carboxylate + 2 H(+) + NADH
EC: 1.5.1.2
Subcellular Location: Cytoplasm
Sequence Length: 263
Sequence Mass (Da): 28474
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A0A1Z8VS05 | MNDDNLLIFLTNDDGFKSEGFDFLKKISKYISKNIWSFAPKENQSAKSHAITINKNINVKMINYKEYIVTGTPSDCVILGLEKLKHSLKENMLLISGINQGVNLGYDLLYSGTVAAAREGALNGIKSVAISIDNKNKLAEWSGVECYVPKILDLYIKTKLSNNFFLNINLPNIEKKKIKGIKIVSLGDRKPGKLKKINNNYYTMPSERNISKTAKPNEDEYELKKGYITITIHDRTNLVVNYKDILKLKKIFRKKFE | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates.
EC: 3.1.3.5
Catalytic Activity: a ribonucleoside 5'-phosphate + H2O = a ribonucleoside + phosphate
Subcellular Location: Cytoplasm
Sequence Length: 257
Sequence Mass (Da): 29261
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F2IGK5 | MINFPTCKINLGLHILRRRNDGYHELETAMLELPFNDVLELIESEESTFTTSGLEIPGLGNLVLDAEAEFRIHKSIPTLAFHLHKLIPMGGGLGGGSSDAAFALKLMRDRYAPEIENESLKEMASKIGSDCAFFIDGGLQFATGRGEVLTPLNIDFKNLFVVLVNLGIHVSTKDAYEGVVPNNDRTSLKEILEKPIRMWKDSLVNDFEKSAFAKYAELEDIKNDLYNHGAIYASMTGSGSTIFGIFESEVESIQWSHKVMYEKYLKL | 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-methyl-D-erythritol + ATP = 4-CDP-2-C-methyl-D-erythritol 2-phosphate + ADP + H(+)
Sequence Length: 267
Sequence Mass (Da): 29813
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B9YC58 | MNKGNFGTLQDGRSAQWLEIENDKLRVRVSDYGATLVSLWVKDAQLDAVLGFDQVEGYQQSVKYMGAMIGRVANRIKDGQFTLDGQVYTLYRNDKGNTLHGGQEGFDAKLWTVREHTSQTVTLELLSPAGDEGFPGELTVTVTYALAGSRLSITTRTRTTAATPVSLTNHAYFSLNGQHPSLDGHWIQVDADEIGLLDPNGCTRPETLEVEGTVFDLRQPKRLTEILNQHHSQLEIAGGLDHNYVLNGVGFRPVASLVKGGLTMRVLSDMPDMHVYTANFLNSEVGRGGTRYTPHCAVCFETQYYPNSVNDPSKISCILNPGITAEHCTAFEFDQEDQA | Pathway: Carbohydrate metabolism; hexose metabolism.
EC: 5.1.3.3
Catalytic Activity: alpha-D-glucose = beta-D-glucose
Sequence Length: 339
Sequence Mass (Da): 37375
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A0A662Q0P1 | MTSSRRAKVLSWLLGLDLIGESVLIEGYEVDVEGVKKWIRENEVKRVLVQAPPGLRGVRRKLIDEISGELDMVFVHGGGCWGGCDLAVAHAKAVGADAIIHLGHARFLEKSPIPTFYLECRKTDPAPILAALEKSAKILQGHHKIGVGVTIQWQDSLSPVRKKLEEYGVEALTGPPIPPLRYESQVLGCGYEPLLRLSEEVECYLIVGSKFHGLGLALQTEKTVYSLDPELQRLDDLSAEVEKLLRSRYGYIEMFRRADEVGVVVSVKPGQYRMGAAVKLRETLRKAGKRAEILIMDDVEVNLLRDSGFEGFVNMACPRLSIEDQQALDKPLLLPMEALIAVGAAEWGEVIRTPRYFLMEV | Pathway: Protein modification; peptidyl-diphthamide biosynthesis.
Function: Catalyzes the first step of diphthamide biosynthesis, i.e. the transfer of the 3-amino-3-carboxypropyl group from S-adenosyl-L-methionine (SAM) to the C2 position of the imidazole ring of the target histidine residue in translation elongation factor 2 (EF-2).
EC: 2.5.1.108
Catalytic Activity: L-histidyl-[translation elongation factor 2] + S-adenosyl-L-methionine = 2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + H(+) + S-methyl-5'-thioadenosine
Sequence Length: 361
Sequence Mass (Da): 40096
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A0A525C452 | MIDESILTKAFDAAKKARNNSYSPYSGYAVGSAIICQSDDEHRIFSGTNVENSSYGATICAERAAILNMVSNSGHKKIEAVVVVSAGEPLAVPCAVCLQVMAEFCRPDTLIAIGTPDSGIVKRYTFAELLPHPFLL | Function: This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis.
EC: 3.5.4.5
Catalytic Activity: 2'-deoxycytidine + H(+) + H2O = 2'-deoxyuridine + NH4(+)
Sequence Length: 136
Sequence Mass (Da): 14542
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A0A3D5WUZ3 | MTYQEIQAAAALLRERLGEAPACALVLGSGLGDFVDELERPVALSYKEIPGFPVSTAPGHAGRFVAGYVEGMKVLAMQGRFHCYEGWDASQIAFPVRVLRAYGVKVLLLTNAAGGVNTDFRPGDFMLIRDHINLSGRNPLVGANDERIGPRFPDMSKAYDPALRELAKGAARDLGIGLHEGVYAWFLGPSFETPAEIRMARTLGADAVGMSTVPEVIAAVHCGMRVLGISCITNLAAGILDQPISGDEVLEISAKKRPEFSALVKAIIARIGAEDAALAGMPRGAAWRS | Pathway: Purine metabolism; purine nucleoside salvage.
Function: The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate. Cleaves guanosine, inosine, 2'-deoxyguanosine and 2'-deoxyinosine.
EC: 2.4.2.1
Catalytic Activity: a purine 2'-deoxy-D-ribonucleoside + phosphate = 2-deoxy-alpha-D-ribose 1-phosphate + a purine nucleobase
Sequence Length: 289
Sequence Mass (Da): 30760
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A0A0B5I0G8 | MIKMNLKPSKNKVPRHIGYIIDGNRRFARRLMLKPYKGHEWGAKKVEKLLNWCKEYGIKELTLYAFSLENFDRPKKEFNYLMNLFKEEFTRLKDHPDLKDTRIRFIGRIWMFPKDIQDIMNELAEETKNHDKFTVNFAMAYSGRAEILDATRRIANLIENGKITSREINDKLFSENLYLNSEPDLIIRTSESRLSGFLLWQGAYAEIEFLPNKLWPEFSKKDFVKCLNEYSKRDRRFGK | Cofactor: Binds 2 magnesium ions per subunit.
Function: Catalyzes the sequential condensation of isopentenyl diphosphate (IPP) with geranylgeranyl diphosphate (GGPP) to yield (2Z,6Z,10Z,14Z,18Z,22Z,26Z,30E,34E,38E)-undecaprenyl diphosphate (tritrans,heptacis-UPP). It is probably the precursor of glycosyl carrier lipids.
EC: 2.5.1.89
Catalytic Activity: geranylgeranyl diphosphate + 7 isopentenyl diphosphate = 7 diphosphate + tri-trans,hepta-cis-undecaprenyl diphosphate
Sequence Length: 239
Sequence Mass (Da): 28590
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V9HVF1 | MKLKTLTVSQVNDYLANYIGTNPIFSNMSVGGEVFNLKKTGYGYTFLSLKDDESKLNAITYLEKFDVQEGDFITVSGKISFYKKSGTYSIIINSYEKKGQGNNYEQFKILYEKLEKLGYFKYELKKPIIKFPQKIGIITSAKGAAVKDIISVITRRYPKVSLIIYDSKMQGIDVENNVIQGINTLSDLSVDTIIISRGGGDTDDLSVFNSQLIAKAVFDCDIPIISAIGHEIDYVICDFVADMRAPTPSIAGELSVPNLQEVYDTIDNFEKSIKISYKNIINLYNSKIDSYRFLIQSNTPYKKINQKKLSLLELTSFIEQAYKDKIQSYKDRLFYISSILQENNYNNILSKGFALVEKDDVFIKTVKDLVLGDKLTVRLEDGNISVVVEDIKNIIK | 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 Location: Cytoplasm
Sequence Length: 396
Sequence Mass (Da): 44812
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A0A6C1PKT0 | MARRNRWKSFDAAILRRARRPFLRFFRRTVPTMTAASIRDCLPAGKRIDLGSMTRSPTRVIAGFYLAVALAATYILLGSPLAIDGIGWADAPLIVLIALHYVWGIVLVFSSSGSLPFRRSFVRRLVFVPEVLGAFALLLFLFSYIFALNANMDYVQRFIAAGGNLRLALDTRVERLLVWARVFPLVALNLGVYLLVRVSRYRAVREACRPSHEPRDAIVRPWSLVLVLLSSFLITIAQPSFVSLDGIAMLGWIGFVPLFLVLRSVRFGHGVFYGIVFGVFSTLLTSYWLGTFNLVSLAITVLFFLIYYALFTPVALLAYRLVGRARPLVFPLAFLVLEYLRSIGFLGYPWALAAHTQYAVLPLIQIAALTGVWGVSFVVLLANSAIAEFIGAQIDRRRAATGTVRSRFGWLVATAGVVGAVILYGTVVIAVADVSQASGRSVRIAQIQQSNDPRKSDYEQTFATLRRLTDETMASSPDLVTWSETAFVPNIRHWTTNTSVRRFHVLVRSFLDYQRSLGTWLLTGNDDYEVELDERGAEADRTNYNSTVLFDDRGVRRATYRKIRLVPFTEHFPYRDQLPWVYDLLKEFDVYFWGQGTEMTVFEHPLVRFSTPICYEDVFPNFVRGFVLAGAELLLNVSNDYWSLAEVQAKQHFVAGLFRAVENRRPVVRTTASGLTGSIDPYGRILATIPQFQEATLISDVRIADDQPLTLYTRWGDYFPIATAGVLLVIVTGAGVGRRRRPPTAQAPDASVKAPKRAVPPPPAAAAPATPTAPPKAAVQPTPAAPPKAATIRDGSLREAAKPNAERSRRKKRVNWRAIWDE | Pathway: Protein modification; lipoprotein biosynthesis (N-acyl transfer).
Function: Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation.
Catalytic Activity: a glycerophospholipid + N-terminal S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein] = a 2-acyl-sn-glycero-3-phospholipid + H(+) + N-acyl-S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein]
EC: 2.3.1.269
Subcellular Location: Cell membrane
Sequence Length: 822
Sequence Mass (Da): 91746
Location Topology: Multi-pass membrane protein
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A0A2E4JP80 | MLYLIVSEFVDKMPLFILTGGPGIGKTTTVIRLVEMLKHRGVSIGGIVSREIRKNGVRIGFEFVDINNNETVILASIMNVGPRFGKYNVNIKGCKFAVQVLQEALLNADIIICDELGPMEFKSKEFINCVGSMLDLDKRIIAVVHKKLKHPIVDRFREKADFMINLDIQNRNKVPYLFLDRLE | Function: Has nucleotide phosphatase activity towards ATP, GTP, CTP, TTP and UTP. May hydrolyze nucleoside diphosphates with lower efficiency.
EC: 3.6.1.15
Catalytic Activity: a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H(+) + phosphate
Sequence Length: 183
Sequence Mass (Da): 20765
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A0A4V0YFQ4 | MVMAVMLSGCSGQYLVLDPKGPIGESQRDLIYISAILCAVILVPVLIMTAVIVWRYRENNKKVAYKPKWEHSTKLETLVWGVPTVIIIILAAFTIKYTYDLEPSKAIASEHEPVTIEVTSLDWKWLFTYPDEGIATVNYLKFPEGVPIRFHLTSDQAMNSFWIPQLGGQIYTMSGMAMTLYLQADEAGEYYGSGANFTGEDFSKMTFKADAVSNEDYNAWVQQVKSSSPELTMDGYHKLAEKGTSDEQSFSSFPKGLFQQIVMQYMNGSDMPMHHGNSESAGSDKDMGDMDMDGMDKDMDMGSSEHANH | Cofactor: Binds a copper A center.
Function: Catalyzes quinol oxidation with the concomitant reduction of oxygen to water. Subunit II transfers the electrons from a quinol to the binuclear center of the catalytic subunit I.
EC: 1.10.3.-
Catalytic Activity: 2 a quinol + O2 = 2 a quinone + 2 H2O
Subcellular Location: Cell membrane
Sequence Length: 309
Sequence Mass (Da): 34539
Location Topology: Multi-pass membrane protein
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A0A8B5WXP3 | MSRTTPQRSFHIESLGCAKNQVDSETIISSLIADGWHESPSDEADVIIVNSCGFIAPAKKESIDTAFGFRTAYPGRTIVMAGCLSQRYADDLAQQMPELDGVFGNRDLAGIGAFLDLIAANPRNPVSVAPPVAGVEASEPSVMPEVVGDRRRLLSPAGSVYIKVADGCDNSCAFCAIPLIRGRLRSRDPDVIVAEARLFVSRGIKEINLIAQDLGSYGRDTRDGREIVSLIRRLLEIPGEFWIRPLYVYPERFPKELIRVMRDDDRVVPYFDIPIQHASTRVLRSMGRPGDRNSHGELIRWIRGELPDAVVRTSLIVGFPGEDDEAFDELRGFVAEARVEWLGVFEYSSEEGTPAYRASRGRSRVAKRVAKQRRTELENLQTEIVDERLGRFVGREIDVLVEEPVIGESIVLGRGFMHAPEVDGAVVLRYAGECPRPGSVVRARIIRRTGVDFEAALLTREAS | 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 uS12]-hydrogen + 2 S-adenosyl-L-methionine = 3-methylsulfanyl-L-aspartate(89)-[ribosomal protein uS12]-hydrogen + 5'-deoxyadenosine + [sulfur carrier]-H + A + 2 H(+) + L-methionine + S-adenosyl-L-homocysteine
Subcellular Location: Cytoplasm
Sequence Length: 463
Sequence Mass (Da): 51274
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V9HUU7 | MVSYKVPATSANIGPGFDCLGMAVNIYNTISFEETDKGLEIEVIGDGSDTVPLDENNMAYETAKYFFDKVGYKFKGLKIKIHNYIPIARGLGSSSSIVIGALLCANDIAGTNMSKDEILNIANEIEGHPDNVTPALVGSITASVILGDTVEYKKIIPPDMLDTIVLIPEYEMSTNEARKILPKTYDRQDCIYNISRASLLIMAMITSDYELLSKVVDDKIHQPYRKSLIKEYDFFENIMKSNGALATFISGSGSTLMAFCHKTMSQELYEILKEECKKNNIKGTIKILSPVKEGAIKLEIGG | 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
Sequence Length: 302
Sequence Mass (Da): 33253
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N9D6D1 | MSNASKFGKVAVLFGGKSAEREVSLDSGNAVLEALLRSGVQAEAFDPKHRSVTELVNYDRAFIVLHGRGGEDGQIQGTLEWLDVPYTGTGVQGSAIGMDKIKTKQIWQGTDLPTAPYRIISKDSNIDEIVDSLGLPVIIKPVHEGSSIGMSKVEKKEDFAQAIAKATEHDAIVMAEKWITGCEYTIVVLNGEALPVIRLEPPKDVAFYDYDAKYQRNDVQYGIPSGLSESDEKQLQQLTLRAFQAVGASGWGRVDAMQDEQGNFWLLEINTVPGMTSHSLVPKAAKAVGVGFDELCVAILEQTLQGTAH | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation.
EC: 6.3.2.4
Subcellular Location: Cytoplasm
Catalytic Activity: ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) + phosphate
Sequence Length: 309
Sequence Mass (Da): 33520
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A0A137NYD0 | MSFRAISSKILRAPTASKLFYTPRYFSTSRISLVTKYAESHEWINVENGVGTVGITNHAQAQLGDVVYVEVPEVGAEIEAKSGVAVVESVKAASDIYSPVAGEVIEVNEALSSDPTLINTSAEAEGWLFKVKLSNEAELEGLLDAEAYKKLSDH | Cofactor: Binds 1 lipoyl cofactor covalently.
Function: The H protein shuttles the methylamine group of glycine from the P protein to the T protein.
Subcellular Location: Mitochondrion
Sequence Length: 154
Sequence Mass (Da): 16620
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A0A6I7QSZ7 | MCRDQDDRWLARTLELARQGAGRVEPNPRVGAVIVKAGELVASGFHRNYGSLHAERAALSAAEPDLVRGATLYCNLEPCSHRSPRKKQPPCTEAIIAAGIGRVVIGHRDPNPAVRGEGIRALERAGITVDVRGEDADESPFLRENEVFNTVMALGRPFVHLKAAISLDGRLATTGGDSRWITDGEARTAAHRLRAESDAVLVGRGTVEADDPLLTVRLPAGEVQGSSPAPRPVVLDSLARISLESRLVRERGNELLLCLGPDAPERRRAALEARGVTVLEAEGVGGLDPASVLKCLGTAGIRSVFVEGGAQILTAFLRARLYDRLSLYFAPILLGRGREAVGDLSVATVVQALNFESVRWETIGRQQCFTGLRAGWQEEILGVLRESERERTKGGPQCSRD | 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-6-hydroxy-4-(5-phosphoribosylamino)-pyrimidine + H(+) + H2O = 5-amino-6-(5-phospho-D-ribosylamino)uracil + NH4(+)
Sequence Length: 401
Sequence Mass (Da): 43258
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R4YMV9 | MSQSILWYDYETFGADPSFDRPAQFAGIRTDENLNEIDEPVQFFCRPSPDYLPHPQALMITGITPQQCLQDGLPENEFIDQINQILSVPETCTAGYNSIRFDDEVTRYTLYRNFYDSYAREWQNGNSRWDILDVMRCAYALRPEGINWPKNAEGNVSFRLEDLTAANGIDLGKAHDAVVDVRATIAIAKLLLEKQPKLYRYLFEHRIKHKLASLVDIDHHKPLVHVSGMYGVDRGCMAIVVPICWHPTNKNSFIAFDLSTDPKSLAGLTIEQMQQRLFSKQADLPEGIERLGLKEVHINKSPVLAPAKTLTPDQAARWDISGDVLRENLATLKVLLAEDSSILTNLHGVYTQRDFAEKTDVDTMLYSGGFWSGQDKKAMAQIHATPPKSLASLKVQFQDPRGEEMFFRFRVRNYPEYMAEDDHERWAKHCMDSLLGNGPGLNFEQFSQALQQAAQDYQNDQDKMFVLQELQLYAESIYPDETY | Cofactor: Binds 2 Mg(2+) ions per monomer.
EC: 3.1.11.1
Catalytic Activity: Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Length: 483
Sequence Mass (Da): 55193
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A0A1G6HT77 | MSTLAQRSVLGSSGYPLDQIHIAGIAARGFHGVLESERKAGQDFSADVTLYLDTRAAARGDDLTETVNYATVSQDVADILSGEPVNLIETVAEQIAAAVLARPAVISVDVTVHKPQAPIPVPFVDVVVRIHRDRINAPVVASPLDVAAPDVAAPADSVDDIGADAAVGVGETEPEAAAVVEETVAPRWQAPVPTSTAALPVVISRSAETNGEPLDAPLDAPLDAALAAWAAPAPVLAPAPVLPLAAVLPTADTLPEPVEEHAPEPEPEPEPEPEPEPEPEPEPEPEPEAVEPASAFEIGATAVLPPLDEQALAEQARLSEQARRPEVFGMVDVASVIPTTRVRAYDPAALGSDDVADAPEPIAPREPVAVDEPVATHEQAVPDEQGEAQELSAEHAEQPVEPVAPLEPLEPLEPLESLDATVVLTAVPATAGAQDFFTRSPSVEGSQNASAAPVLPQEPSLGAGSPDETTVLSRTFDRMDTPPDEPVEVVLALGANVGDAQDTLRRAVSELGAVNGLTIMAVGPLARTAAVGGPEQPDFLNTVVLATTTLSPRDLLHACQAIEADHGRERLEHWGPRTLDIDLIAFGALVHSSDDLEVPHPRANERAFVLAPWAHIAPDAVLPGLGGGPVGALAATAPDRDGIRWLALDWLHEPDTAAQPPASITPQGMVRPDTSGVPAVAAPPAPPV | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 3/4.
Function: Catalyzes the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin.
Catalytic Activity: 7,8-dihydroneopterin = 6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde
Sequence Length: 688
Sequence Mass (Da): 71321
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A0A137P4H2 | MTVSETIQDILNIAGFDVNSQEFAQHLDNTELSKFFAKYRSEFFLPKIGNIQPEGKTSDRPEDEVIYLVSNSLGLLNKRTKKLIEEELDVWSKKGVFGHFSHDFQRPWKDIDETSLPMMAKVIGAKVVETSIMCTLTANLHFLLNAFYKPTSTKYKILMEDKAFPSDHYAIISQVKQHGLNPDTDIIYLKPRKGEYLIREEDIFKAIEDENLALILLPGVQYYTGQVFPMEEITRLGQSRGVKVGFDLAHAVGNIPLELNKWNVDFACWCTYKYLASGPGNIGGLFVHERYANASEMNRLIGWWAHNPDTRFKMSNQLELSPGAAGFQMSNPSVTNVVALQGTLSIYNEFDMYKFREQSLLLTDYLELLIKSNSKLKSKIDIMTPEDSARRGCQLSLLLIEEGADLVKIYNELLHYGVMTDERHPNCVRVAPYPLINSFQEIQQFVTILEKVLN | Pathway: Amino-acid degradation; L-kynurenine degradation; L-alanine and anthranilate from L-kynurenine: step 1/1.
Function: Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3-hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3-hydroxyanthranilic acid (3-OHAA), respectively.
Catalytic Activity: 3-hydroxy-L-kynurenine + H2O = 3-hydroxyanthranilate + H(+) + L-alanine
EC: 3.7.1.3
Subcellular Location: Cytoplasm
Sequence Length: 454
Sequence Mass (Da): 51804
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A0A2N3G838 | MLKAAVIGASGYAGAELMRILWGHPELEVVHATANKYAGCPVGSLYPSLAMQYPGDFEEYAPDLFNDCDIAFFGLPHGQSMKVVAEAASAGLKVVDLSADFRLSREDYLKWYGIEHESPELLGKAVYGLPELGRETIAFALVVANPGCYPTSALLGLFPLANAGYIKEKNTVIIDAKSGVSGAGRRPTHATHYPRVADSMSPYAVTGHRHAPEISGWLASMAGGAVDVVFTPHLAPMNRGILSTMYVPLEAGSSIEDIRALYYDTYESEPFVHLLAPGSFPETKAVQGTNNCHVALEVSRSGGTLVVMSAIDNLVKGAAGQAVQNANIMLGIEESAGLLAPGLYP | Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 3/4.
Function: Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde.
Catalytic Activity: N-acetyl-L-glutamate 5-semialdehyde + NADP(+) + phosphate = H(+) + N-acetyl-L-glutamyl 5-phosphate + NADPH
EC: 1.2.1.38
Subcellular Location: Cytoplasm
Sequence Length: 345
Sequence Mass (Da): 36584
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A0A1W9PVM7 | MIAVLMSGGVDSFVAAHLLKKSGADVVGVHFKTGYENADASRLQEIAALAGVPLVFLDCEREFKRKIVDYFIGSYLDGETPNPCIACNRLIKFGVCADYAVSIGAEAIATGHYCSAVRVGNRTVLGRGADTGKEQSYFLAFLSQAQLSRAVFPLGNMKKSDVKKLAHDLSFPFLTQAESQDVCFIRDTGYARFIEEHAGMEFSPGHIQDTEGNIIGRHHGVHRFTIGQRRGINIPSSRPYYVAAIDTRRNLLTVGHREDLFVSEFMVRNVNWLLEPPDGSLDLLVMVRYNQTAVNARVVPVDGGRARVFFATPQFGVAPGQAAVFYDGDTVLGGGIITRDFGRACCNKQKQ | Function: Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34.
Catalytic Activity: AH2 + ATP + S-sulfanyl-L-cysteinyl-[protein] + uridine(34) in tRNA = 2-thiouridine(34) in tRNA + A + AMP + diphosphate + H(+) + L-cysteinyl-[protein]
EC: 2.8.1.13
Subcellular Location: Cytoplasm
Sequence Length: 351
Sequence Mass (Da): 38418
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A0A3C0WWK9 | MTKKNLLKGLTLPKTVEYEVVEEDGGNKEYAKIAAYPFERGFGTTIGNSLRRALLSSIQGYAVSSLMFHVRKDGNLTTISNEFEALPGVKEDIVEIIANIKKLALKCSGEDFESQVMTISCKGPGELTGAAFAKNGIEVINSDLHILTMEKDVDMDIDVQIDFGRGYIPADMQKNYVVETYGVIAIDSLFSPVVRVNYSIDAARVGQRNDFEKLVLEVWTNGAISAVNAVGQAAFIVSEYLQKFINFDKSEVLNSQEIEKCENDRIELLKSSIDRLDLNSRSMSCLKRININFIYELVQKNEDELLREKNFGEKSLGEIKEKLQNLGLSLGMTGLEL | Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
EC: 2.7.7.6
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Length: 337
Domain: The N-terminal domain is essential for RNAP assembly and basal transcription, whereas the C-terminal domain is involved in interaction with transcriptional regulators and with upstream promoter elements.
Sequence Mass (Da): 37548
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R4YKJ2 | MDKVFIRGLKIETVIGVFAWEKQVQQPLIFDLTMDWDITKAAETDDLAYALNYAAVSDRVIEFVQGNQYDLLERLLVQLAETLRTEFSISKIKIRVEKPAVAPDAIAVGLEIERG | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 3/4.
Function: Catalyzes the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin.
EC: 4.1.2.25
Catalytic Activity: 7,8-dihydroneopterin = 6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde
Sequence Length: 115
Sequence Mass (Da): 13027
|
A0A6B2C0I2 | MKVGFEIHIQINSKRKLFCNCNPKSDESSQIEFRRRLRVSTSELGEIDPAAAFEIKKGLDIIYVSGDKTSCLVEADEEPPHEPDPYSVEVAIKISNMLNSFIVDEIHFMRKIVVDGSNTSGFQRTAIIGLNGSYTFRGKNVRIQTICLEEDAARLLEKGEGYVKYELKRLGIPLLEITTEPLEISPEEAKAFAESLGRTLKLTGLFARGLGTIRQDINVSVEGGCVVEVKGVQKLEQIQKVIEFEEKRQKMLLEIAAKLKERGISEENFVSIEPVEVSDVFKNHLNIPSVKKFFKDYAFALKAPGLKGLFSYETVPDSRLGLDLADICRLFGFKGIIHSDEISKYDFGQDILKELEDKLGISKNDGFVIVFGDKEKAVLCLQMVKERLKMALKGPVAETRYATEKGTTRYLRPRPGASRMYPETDIPTIKITQEMKDKYRIEIKSWEKAVEEFSSRHSINKEMAEQILDSEFVDFFENVVENYKNVPTTLLASLIVQILIPYQNSGKVIEYDEFLNLLAEFSKGNISKEAVMDVARYMLEKGVNLESALKEMNIKKLSVEELRKIIKEKIDEALQENVEPSKLYGTVMGRVMSLVRGKIEGKIVNEEVKKALENLNKA | 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). The GatDE system is specific for glutamate and does not act on aspartate.
EC: 6.3.5.-
Catalytic Activity: ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate
Sequence Length: 618
Sequence Mass (Da): 69958
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F2IK29 | MTKKCNFGLMSKRIEKTGKKGLRTSYISTVIGISLVLFMIGLVLAGVIGLDSLQKQARENLHGDLFFKSEYNAADIKQVEQELKSWDCFKEVVFVSPERAIEEFKGADQNSDEILAIFEGENPLPPTINFRPVSSYVTKKGMKEIETRLNTKFGDMLAEVNYDKAALEEVNLGFKQFAFLILLVASLLIVIAVAMINNTIRLSLYSKRFTIKTMQLVGARSGFIRKPFLKQAIFQGLVSGIIGMAFLMTVFFALNNILDVVEINLKLVDILLLFASLLIIGCVLTIVSTWFALNKYLRAKLDDLY | Function: Required for cell division and gliding motility.
Subcellular Location: Cell inner membrane
Sequence Length: 305
Sequence Mass (Da): 34234
Location Topology: Multi-pass membrane protein
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A0A1F4VDY6 | MLSTQPYKGVRDFFPDDIKVRNYIFDTWRKVCLSFGYEEYDGPFLEPFELFSAKTGDEIVNNQLYSFEDKSGRKVAIRPEMTPTVSRMAAEKIRMQTPLPLKWFSIADFYRYEKPQKGRGREFYQLNVDIFGEESVNAELEILLLNKGIMEKFGATDKMYEVRFNNRFLMNYLYERIASLTVPEIKAVQKAVDKKAKISNSEFESLLEKDIDKSKIKKVHEVLNLTISDIKKLKDLPDKASNLLKLMEMAQKVGIKNIIYDPALVRGLDYYDGNVFEQYDLTKGNNRSMFGGGRYDGLISLFIDKKVPAVGFAPGDITLMEFLKSWNLLPETGSLVNLLVTVFPGNKACLEKSLEVSEKLREYINVETYLNPDMELTKQLKYADRKSIPFVLIIGPDELAKELLLIKNLKTEEQSKMKSLQDVVKLIKS | Catalytic Activity: ATP + L-histidine + tRNA(His) = AMP + diphosphate + H(+) + L-histidyl-tRNA(His)
EC: 6.1.1.21
Subcellular Location: Cytoplasm
Sequence Length: 429
Sequence Mass (Da): 49427
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A0A6N2E7Y0 | MIEVLDTGLEMLGMSQESPDRRTSLLRYLSELRLWNRKLGLVEAEGDELVVRHVLDCLTPLSIIKSNSPGTVADLGSGAGLPGIPLAIYMDSSEFALVERSGRRVGFLKNVVALLRLKNVSIYESDFTRHTPTQAAQAGYDLISFRAFRPFSEDLIVGIRRILSPGGVVAAYKGRDENVAEDARLLQAAGAVTETIPLEVPFLKHERNLLLARFPSES | Function: Specifically methylates the N7 position of a guanine in 16S rRNA.
EC: 2.1.1.-
Subcellular Location: Cytoplasm
Sequence Length: 218
Sequence Mass (Da): 23978
|
A7TIX7 | MSGQILDKNTIDILSRECIRARESSYSPYSKFRVGCSILLTNGKIIRGCNVEVASFAGTICAERTAIVKLISDDEDNNGNSTKLQQVECIGIIGDTKEGVITPCGICRQVLREFLPSKTKIVMFNNDGTQNEILTLEDLLPYSFGSDSLGT | Function: This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis.
EC: 3.5.4.5
Catalytic Activity: 2'-deoxycytidine + H(+) + H2O = 2'-deoxyuridine + NH4(+)
Sequence Length: 151
Sequence Mass (Da): 16502
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A0A2S9V825 | MSSPSKPPFILVDGSSYLFRAFHGLPPLTNTKGQDTGAIYGVINMLKSLIKQYNPTHIGVVFDAKGKTFRDDIYPEYKANRPPMPDELRSQIAPLHDIIKAMGLPLIIEDGVEADDVIGTLARQAGEQGIDTLISTGDKDMAQLVNEHVTLINTMNNQLMDVQGVQDKFGIPPELVIDFLALKGDKVDNIPGVPGVGDKSAQGLLNGIGGIEAIYQNLDKIAELDFRGAKTLGKKMAEYEEQARLSYKLATIDVDLNLDYSPQTLTPEQADNDKLADLYSEYEFKRWYTEVTSSQATPAATDSDSQSKETDEEDSAAADIETDYTTILDEATFKQWFERIQLADIVAFDTETTSLDYMEAELVGMSFCMEPGVAAYLPVAHDYPDAPEQLSRDWLLQQLKPWLEDASRIKVGQHLKYDKNVLANYDITLDGIGFDTMLESYVLNSTGSRHDMDTLAQNYLNHRTVHYEEIAGKGAKQLTFNQIELEQAAFYAAEDADITLRLHEVLWPKVAAEDTLKKILQEIEVPLASILARMEQQGVLIDSQQLSQQSQQLATRIMELEKEVHEMAGEAFNLGSTKQLQHILFEKMELPVVKKTPKGAPSTSEEVLQELALDYPLPALIMEYRGLTKLKNTYTDKLPKMINHRTGRVHTSYHQAVTATGRLSSTDPNLQNIPIRNEEGRRVRKAFIAREGYKIVAADYSQIELRIMAHLSGDKGLLDAFAHGKDIHRATASEVFNVAEDDVTDNQRRSAKAINFGLIYGMSAFGLAKQLHVSRQEAQEYMDLYFKRYPGVLEYMDRTREFAKEHGYVETVFGRRLYLPEIKSSNGARRKGAERAAINAPMQGTAADVIKMAMIQVDDWNRSTDNDDVVMIMQVHDELVFEIKQDTLDTNVATIVELMEQAATLSVPLKVEAGNGENWEEAH | Function: In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity.
EC: 2.7.7.7
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Length: 923
Sequence Mass (Da): 103323
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A0A137P308 | MFSTSEKNIQGVFTSTMYYAIKQSIGPLIGTIFISSFVGLLWIFFLCNFIKPFMWFTFLSVPVISFVIFLWMLFNGIFGIDNTLIAANQSKLLSIIPLIITGGHCLFIHRYHALINHCIDIIKVSCIILRQSLDIFGVSLFCLSIQILFSSFWLILFDRLFLLGSSTTIEGKANWAQDANLIYLVPFYLFYYWWTTCIIDGVERSSIAGTVSHWYFHQEETQFINGFNATHISFRRALTTSFGSICFGGLIASVVRFIQFLRQLNDQIPQSVNFLTTILRWVMWPIVLVSDLVEK | Function: Probably involved in transport through the plasma membrane.
Subcellular Location: Cell membrane
Sequence Length: 295
Sequence Mass (Da): 33913
Location Topology: Multi-pass membrane protein
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A0A3B5KQ85 | MVRRVAVVGAGSSGLACVKVCLEEGLDPVCFESSDDIGGLWKFKESPEPDRSSIYRSLVVNTSKEMMCFSDFPMPDDYPNYMHNSQLLQYFRLYAEHFHLLQHIRFQTTVRSVTQRPDFSESGQWDVVTMNKNNEEERHIFDAVLVCSGHYTHPVLPLSDFLGHETFLGRLLHSREYRDADSFRGERVVVVGFGNSGGDVAVEISRSAEKTFLSVRDGFWVMSRMAHRGLPVDMALISRFNILLLQLLPKTLINWAAERALNQKYDHELYGLKPRHRLLDKRPLVNDDLPGRILQGALIMKPNIRAFKDSGVTFEDGTVEDNIDAVVFCTGYKGIFPFLPSALSEGPHSELTLYKRVFPPSLQQPTLAVMGFFQVRGPIMPIVEMQVRWAVKVFSGLTRLPLTQKMLEVTETERRLNLPR | Catalytic Activity: H(+) + N,N-dimethylaniline + NADPH + O2 = H2O + N,N-dimethylaniline N-oxide + NADP(+)
EC: 1.-.-.-
Subcellular Location: Membrane
Sequence Length: 420
Sequence Mass (Da): 47812
Location Topology: Single-pass membrane protein
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A0A146KIX5 | GRTLKAQYTRNLMLEEVNPITDRKKRKFRDLLCVIIFIAFWIFIILLIVLNKIWTQYQNSTLLLEPHDFMRRRCGQSSNNQKDKLATDYSKLITQQDQFVQFCTVFQQVYTGVEPYDCQWLNQSQNISAIYNSRTFFNKISQTAVDTTLQSAGFSVNDVKICVAPAYLEASSSAANCNPPLEAAYVCAHDFVNFAMELISNPVLKNDIDNLVNKQFYTQSMINQIMNDVGFNNQFIIKFCQSIPAYVGNNSIRDDFAQNAIQQLFNIKTCSRSNLFFENQLFKDIGNYISDFSNNFLMQISSRWQWILVGIGSGILFMILFLVFVRYFVGIIVWLCIIASIASCAVGSYFLFDHANILKISNEFRLQYFGFEDAAILYQYKLYLALGIAVAVVGGLLALLTLIFLRTIRIAIAVIKQSMVCIAKVPIIFIFPLFTLIFVAIHLAWSVSASYLMYLSGSYDASTNMFNFETISRDSEMQVVKEWDYTNSSYFAAMVFAAIWGVFFFYNLLEYSISAMVAQWYFNRERTSKSLSGSTAKTIIFTLKSMGTIVITSFITSFVVFIRFVFEYILKRLKAANKIADTKVVKAAIWFTRCCLKCLQKIVMWFNRNIQVYAAISGEGYCKSLGGAMKLLIGKLMSNLFTKGLTSLFIFIGKILITAVGGVVTGVIIYYSYNSIEIAPALLSSLVSFVLSYYVLEIVKLVIDTIYFCYLYEETFMQRERESGMKPYAPGDLIKLLI | Function: Choline transporter.
Subcellular Location: Cell membrane
Sequence Length: 738
Sequence Mass (Da): 84200
Location Topology: Multi-pass membrane protein
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C4GIC9 | MRRLLFCLITSLALIAPSADAKARAAKNAEGRAIKTVMPVYPPLAQENGIEGRVKLRVQVAPNNRIRLVEVAESSGSPLLDEAAVAAVRQYRFQAASRDGKRVATTFFPIFINLNWSDKRAGADSRPALLCPCIKRQPEKHKTAWYSAKRFFYWIDSLSGCLTLHNCLMLPPSPLRSAERSILFSGKSVRLSDDVRSTASSHAPKKGCGVREVRTANLHVEVAFLLLTFLWRSKEK | Function: Interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates. It could act to transduce energy from the cytoplasmic membrane to specific energy-requiring processes in the outer membrane, resulting in the release into the periplasm of ligands bound by these outer membrane proteins.
Subcellular Location: Cell inner membrane
Sequence Length: 236
Sequence Mass (Da): 26248
Location Topology: Single-pass membrane protein
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A0A9E4DEP7 | MIVPSIDLMGGQAVQLIGGETRAIDAGDPFPIAERFAVAGEIAVIDLDAAMRQGSNAGLIEGLVRRFPARVGGGIRDVETALSWLDTGAVSIILGTMAVPEVLKDLPKARLIAALDARNGEVVVEGWKTGTGRGILERVAELKGLVAGFLVTFVELEGRLGGTNLDLAKEIVAAARPARVTIAGGVTTPEEVADLDAIGADAQVGMALYTGRMDLGEAVAAPLRSDRPDGLVPTVVADAHGVALGLVYSSRESVKTAVNERRGVYHSRSRGGLWRKGETSGATQELLRVDADCDRDALRFTVRQAGAGFCHTGARTCFGEDRGLPRLARRLHERRAGTVPMGSYTKRLFDDPDLLAAKITEEARELVAAASRDEVVWEAADVLYFTLCRLAAEGIDLAEVERHLDLRERVVRRRG | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9.
EC: 3.5.4.19
Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-5'-AMP + H2O = 1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide
Sequence Length: 415
Sequence Mass (Da): 44289
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A0A812M9G5 | MWLIWWDPCGLFCYLFGELVMVLSNYVVLVYILGPWTQWNTVGIVNGVLFQTVVCLVFVAHWRAMFVCPGVTQLNSATPADCQPDQSDPTWWTKPKRKYCTKCKAIKPPRAHHCSVAGRCVVKMDHYCPWVNNTVGQNNHKFFLQFLVYVFIGTAYAALASLAYGLAVWQGWTPWPKWSVLDIGLVVAQVVLDAFFAIFVCAMMSDQFEAVCTDTTGIEAMKRWEERDWTLMQGLTNVMGGPLGLHWFIPTLPQGKALYQWSATDDLDAYDIRDPSIKNFFRQLDFEARLQELNAAKGEEGQADAPSKPSLPNLQELIGQDLKRVYDEQGRAMLVPGDVAQRLQARKAARAEEDMDMSSVGI | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 362
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 40921
Location Topology: Multi-pass membrane protein
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A0A1J5DRY6 | MEIQIQFRRRTPGLSAAKIRRKAAALLDALGCPSKELSILFTDDGHIAKLNGIYRKKEGPTNVLAFPQGSPDDLFTDMLGDVVISVDTAGREAESLGEPFEITIQRLMIHGLLHLLGYDHERSGEAAEEMEKEERRLLAMIREDN | 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: 145
Sequence Mass (Da): 16188
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W0U4J5 | MSEERIPKRSEVPEQFKWALEDIYATDEKWAEDLQKLKAMPERITAFKGRLSESADTLYDFMQLSDEISVLCDSLGNYAQRRSDEDTANAKYQGFLGQLMNAYVAVNSAGSFETPEIISIEEDKLQKFYEDKPELKLYKRALDKLRRKKAHILSEAEEKILALTGEMGQSPENIYSMFSDADLRFPDAVDKDGKAHQVTHGSYIPLVQSEDRVLRKSAFESMYGTFDKFKNTCAATLSAQIKAVNFYAKARRYDSSLEAALDGTEVPVSVYKNLIEAVHDNMHYMYDYVALRKKLLGVDELHFYDLYTPVVPDADMKITFEEAKETVLKALAPMGEDYLAILKEGFENRWIDVYENEGKTSGAYSAGARVHPYVLLNHKDTLNCMFTLAHEMGHAIHSYLSNKNQPVVYSDYVIFVAEVASTCNEALLMQYLLKNTEDKKQRAYLINYFLEQFRTTLYRQTMFAEFELKINEMVAAGESLTAEGLNELYGQLNKLYFGDGIVLDDEIKLEWARIPHFYYDYYVYQYATGYSAAIALSQRILKYGKPAVKDYIGFLKGGCSTDPISLLKGAGVDMATTQPINEALAMFGELVKEMEEAMS | Cofactor: Binds 1 zinc ion.
Function: Has oligopeptidase activity and degrades a variety of small bioactive peptides.
EC: 3.4.24.-
Sequence Length: 599
Sequence Mass (Da): 68223
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A0A928CJJ4 | MTNNIYDYSYQMRRNLQKKIGFIFIFLLVIFILVAITSSFFIFSKFIKSDSMSPTLEKNNIVFISPFASPSNPIFSDKNIFERGQLVQIKPLETTEISFFKQILDKIVLFFTFQKVAPFSDSTNMTHSSLIRRVIGLPGDTVYVKNCVVYVKPADSSHFLTEFEVSQKKYDIISTNSNNENIDLLKDSKEITLGNDEYFVMSDNRVSSIDSRLWGAIKSDQIQGKVLLRYFPLNKISGF | 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: 239
Sequence Mass (Da): 27494
Location Topology: Single-pass type II membrane protein
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A0A4P9A1A1 | MEKLDEVRALLLSRVTEVAEPRSVLRSAELRELYGIIATLPAEERGAFGKKVNELKQELERAITAREDELSKVDLPPIDVTAPMDVNAPRPELLPSERGTIHPLSAEIERISDIFNRMGFVTEESREIDDQFHMFESLNFPKGHPARDDYDTFMTEETDANGDRLIAPAHTSTMQNRVLKKYHGNLEKGEAIAAIVPDRVFRNEDLDARHEHTFYQVEGVYVAKGVNVGNLIATLQEFLQEYYGKKLDVRVNPFYFPFTEPSFEFALSCPFCEGKNPDCKVCSGEGWIELLGCGMIHPNVLKAADIDPNEYTGFAFGCGIDRLVMMKYGIEDVRHFESGKLDFLEQF | Cofactor: Binds 2 magnesium ions per tetramer.
Catalytic Activity: ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + H(+) + L-phenylalanyl-tRNA(Phe)
EC: 6.1.1.20
Subcellular Location: Cytoplasm
Sequence Length: 347
Sequence Mass (Da): 39345
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A0A6I7PIT0 | MNSGSKTSTRKRTMGRRTILLDLAYDGTDFCGWQVQRSDRTVQGELERALAELHGQRVVLHAAGRTDSGVHATEQRAHFHTSMDSVPSERFRDAINSKLPLDVRVLRSRRVADEFHARYDAVLRTYHYHLLVSPVQLPRYRNYCHRISRRPDMATLNRLAAQLIGEHDFSSLGLPPGDGGHARRRVEAAAFVSRPPFIVFQISANAFLWKMVRTIVATILACESCGEDAFVDILQARDRSRAQLAAPGRGLFLHKVRYHESFAID | 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: 265
Sequence Mass (Da): 30017
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A0A1R1YJH0 | MIASTKSIFRPCIDLHNGQVKQIVGGTLTENDQQVKTNFVSSNPSSYYAELYKKHSLIGGHLIKLGPGNDLAAIEALKSWPNGLQVGGGINIENAQKWLDLGASKVIVTSWLFTDKKFDLNKLKALCDKIGKDRLVVDISCRKDDIGWVVAIDKWQTRTDLYLNKNTIDLISHEFLVHAADVEGLCQGIDEELVKCLLIYSFSLLLCSCLGIWVDIPTTYAGGANSKNSI | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 4/9.
Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide = 5-[(5-phospho-1-deoxy-D-ribulos-1-ylimino)methylamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
EC: 5.3.1.16
Subcellular Location: Cytoplasm
Sequence Length: 230
Sequence Mass (Da): 25340
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K6WYS1 | MEQLSGADAAFVYCETAGAAHVTFFAIYDPSTGPGKIVGFDDVFAHFGSRLGVASFFRSVLVRVPFDLDHPYWVRDENFEVGHHLHHVTLPGPGDWRTLCDQVSRLHAEPLDLHRPPWDCYVIDGLGEISGIPDGSFALCLKVHHSALDGLTGLTLVMQLHELTPETSPPPEDVWVPESRPSSLHLLARSAVTVARRPAQLASAAEHSIPAVGRLPGATLRRLLPRHGSEYLPALYAPRTRFNGHTDSTRNFDGRSYDLAAVKAVRTLVPGATVNDVVIAGIGGALRRYLLANGELPEKSLTTVIAISLHHATGRPHGVNRLGVARVTLGTNIADPIARLKVVQRSSAHAKATVATVGEPVLDYLEFVPGGLVVTALRAGMAAHLGIVMEQARIANTLVSSLRGPDFPLYLVGARMLAGYALSPFAQGGGLLHNVISYCGRVTVSINGSPLLLPDIEHYGDCLDASLAEVLAAAKIAP | Pathway: Glycerolipid metabolism; triacylglycerol biosynthesis.
EC: 2.3.1.20
Catalytic Activity: a 1,2-diacyl-sn-glycerol + an acyl-CoA = a triacyl-sn-glycerol + CoA
Sequence Length: 478
Sequence Mass (Da): 51069
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A0A2V2U9A9 | MQLTIIRIEEYGPWTITLGSDREARLQMLQANFYYDLQRLFSAKDCLVYLNRFDEYFAITNGLSVADHLVIESELSSLYKKLKLSMTIGNGETPYQANLDAYNTRKMGELGTDKARIFASAAVQSSMSNSIPGVNEFVQIMHIDMNNSAEIGSKLSPYEMTCLIIKIYARLSEEFVKKESLTFFLGGDNFMVVSNAATKQDAEETIMKVTQGTNIRLNCGIGIGRTGRKAANAATKALDTIRDLRHVGKDLPVYEVECL | Function: Catalyzes the formation of 2-amino-5-formylamino-6-ribofuranosylamino-4(3H)-pyrimidinone ribonucleotide monophosphate and inorganic phosphate from GTP. Also has an independent pyrophosphate phosphohydrolase activity.
EC: 3.5.4.29
Catalytic Activity: GTP + 3 H2O = 2-amino-5-formylamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one + 2 H(+) + 2 phosphate
Sequence Length: 259
Sequence Mass (Da): 28973
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A0A229T432 | MSLVTTHVLDTAAGRPAAGVPVRLETGDGTPIARGRTDDDGRIRDLGPDELDPGVYRLVFDTGAHLGPDAFFPEVTVSFRISDGTQHHHVPVLLSPFSYSTYRGS | Function: Catalyzes the hydrolysis of 5-hydroxyisourate (HIU) to 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU).
EC: 3.5.2.17
Catalytic Activity: 5-hydroxyisourate + H2O = 5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate + H(+)
Sequence Length: 105
Sequence Mass (Da): 11274
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A0A812YER3 | MQSNRVAATDFENPVGIEIPPPNAKPANERTKKNVITILGVVAFIFLVTTILFAVLYAVEANRDEDSSRGECPVQGAYVPETGDLAEFSNNVDRVKEMFDTITPEELLAVRNFAVQEWGLTPIADRSSEQFDEDYLLTTELAPAPKAAAKDYIDGVSDTSPGRYAHAFVVKGSEATPMVHVYLVGPLGGTLTATELTAPNHPYPVPFNMSALNGMVETFIADLDAENFWTTAYGLTADDIWWTDSSPRGYDRASRKTWHWFNAWGEGQYIYPLGLTVLIDHQDLDPQNWSIERIVFNGQGPYATVADLITASADSGFEWPSRPIDSSFGSLKRRDGAPRRPRERLAMPDIVYPQGRRFGVDGSMVSWMGWQFHVNWNIFGGLQLNDLRFRTDRIVWEVSLQDAYAKYSGYQPLQSLSQYNDVGWGQGYASFELIKGVDCPRDALYLPRNFLVDSDTVTQLKDAVCIFERPTSIAAQRHYDQDYEGSYVFAAGYPGSELVVRTTHTVYNYDYIISVVFYLDGSFETFSHATGYLQAEWYLDNGNENPFSTRIHDNTIGSIHDHLFSWKLDMDILGTNNRLTRSELKVGTTALPWGGDLPGSSVQQVYKEMVQVTTETEGSSTYDVSLDAPVTFLFHANQANDWGVMRSYGLVVHTAAKQHITNAPWLPANEWTKHHITVTQRKDSEPRSGAPFFDMQAPAEPLFRFGDFTNGDSLVDQDLVAWICTGLVHVPHSEDVPVTYTIGNSVGFRFRPYNYFRESPLTDLTRYFYVSKENGVEVDTTNIAAGEECFEPTPERDWVGEPIEL | PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue.
Cofactor: Contains 1 topaquinone per subunit.
EC: 1.4.3.-
Sequence Length: 805
Sequence Mass (Da): 90395
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A0A0G1WCV5 | MVYYFNVKRVFISIPLTEVVRRQLRDLIGVLKVKMAGVHWVDPRQAHVTLRFIGEVEKSELIALSDIVSKCTADVRPFKLEIQEFEFLPSAKRARVVALSVMENVLLDSLTAALSTRLEAFGLVPLDVQPFRPHVTIGRTRAGVLNAVQYSLIHFSATCPVHTIDIMKSTLTTDGPVYTLVKQIFI | 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: 186
Sequence Mass (Da): 20919
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A0A3N5TDP6 | MQNTNDVRILSCVTLQSPEELKKEYPITASAAETVVTGRRAIESILVSAATGTGKDSRILAVVGPCSIHDPAAALDYASRLVSLQKRIARHILLVMRVYFEKPRTTVGWRGLILDPGMDGTGDINKGLKIARKLLVEINSMGLPTGCEMLDPIVPQYTADLVSWASIGARTTESQTHREMASGLSMPVGFKNGTDGGLETAINAMV | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 1/7.
Function: Stereospecific condensation of phosphoenolpyruvate (PEP) and D-erythrose-4-phosphate (E4P) giving rise to 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP).
EC: 2.5.1.54
Catalytic Activity: D-erythrose 4-phosphate + H2O + phosphoenolpyruvate = 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate + phosphate
Sequence Length: 206
Sequence Mass (Da): 22109
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A0A2N1J771 | MRELKMRNQTTLLYSTAGLILTLGLSYAAVPLYRAFCAATGYSGTPMTDRERYSDASRLHPTYSDPFNETKDTERIRISFSATHSDQIPWSFVPEQPEIYVLPGETALTFFKAHNYSDKDIIGIATYNVVPDRIAPYFAKIECFCFEEQKLLAGEVIDLPVFFFLDKDMLEDGETRDVKDVILNYTFFSARRNPVNGQLEPDTDLSKYRVGKDA | Function: Exerts its effect at some terminal stage of cytochrome c oxidase synthesis, probably by being involved in the insertion of the copper B into subunit I.
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 214
Sequence Mass (Da): 24404
Location Topology: Single-pass membrane protein
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