ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
|---|---|---|
A0A2R5HGC7 | MQPYGTPAYFIWLGLALIPLVIAHAYGKKWMGYQVLFTLAFLWLTFGSTMSIWSILGFGVFETLLIKLYEHYRTREGSANKTWVFVVAVLLSIAPLFVVKLTPVIDPAHPSSIIGFLGISYVTFKTVSTILEIRDGLIKALPVKDFLYFLYFYPTISSGPIDRFRRFQKDMQTPVDREKYVEKLGKGIFFIFQGFLYNFIIGYLIQTYVLHGVAIQAVQNPGFVNMAISAYAYGLYLFFNFAGYSLFAIGISYIMGIDTPINFNKPFLAKSIHDFWQRWHMSLSFWFRDFVFMRFVKFMMVKRWFKQMTTTSNVGYLVNM... | 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 t... |
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
|
A0A552X005 | MLKALLLIIILALGLIVGPMWSGNAGSVLILAGPYSIEMSLVVATLLVAAFLLLLWLVQAIFRKLSSGKRFTLSWFYKRKQKKAEKQLAQAMHHWLSKNYREAADYAERAAPHLQQPQHGYLLAASAWQALGNLKELQRTLGLAYDSAHHDLNVRLMQLEQMTDSGQALKTARTLLQDHPKHGGVLRACAETYYKHQHLESLRELLPRIQDRDIVPGARLAEFTRASYRSLYQSAGTSSERLRELWKETPSKLRRTPAVRMAYLDVLTHRGFGAIASKVATRGLALNVFTASDLLQFDMREWRQTESLREEVEKQIKQHP... | 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
|
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-dehydr... |
A0A3B5M660 | RRSAPPGEEILALPDVAVQHELHAAVQSEEEEASADISAPQLFVELNELIVDKDQEMRWKERARWIKFEEDVEEETDRWGKPHVASLSFRSLLELRRTITHGAVLLDLEQNTLPGIAHLVVETMIISDQIRAEDRPSVLRALLLKHRSLAKHAKALNQEPTNSELETLPHPSFITSLLRTKSFILKLIPKDAEAVIVLVGSVEFLEQPAMAFVRLSEAVLLESVLEVPVPVRFLFVLLGPSQSNVDYHEIGRSFATLMSEKVHFTMPVAYFADDRQDLLNGINEFLDCSIVIPPSDVEGKDLLKTVADFQKQLLRKRRDR... | 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
|
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
|
D2R6X0 | MHKLLTVQQHILEEQRRNHPQASGEFSWLLSGITLATKIVAAQVRRAGISADVLGATDSQNVQGETVQKLDVIANQTLLQFLGNRGNVAIMASEENDDPIVVERDRAHGRYVVVFDPLDGSSNIDVNVSVGTIFSVLRREPDPDCSRDTTADVLQPGYKQVAAGYVVYGSSTMLVYTTGHGVFGFTLDPSIGAYLLSHERVTMPDAGTQYSVNEANFEGFPLAYRKFLMQARSGALGRTYSSRYIGSLVADFHRTLLKGGIFLYPPTNSHPKGKLRLLYEANPVALLAEQAGGMATNGTDRILDIEPTSLHQRTPLIVGS... | 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
|
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 synthe... |
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-methionin... |
A0A194S762 | MARTKPKSTLEPSRNPPTPSLSSTSSSSSFSRPQQPELVPVRHYLPRVPLQLFAVAFSLVAASTSQDKHLAAPARFLQALHREPLKTLPVVCAALAAIQTWFAYSLRSNRIASLARLNHKGTDAPAPAPSRAAAARGTGFRGSLATMWDAAMRGEAPTEALWKKRALRRGAHAKAAIDTSFVGEAIMVTWLGTLAIHACTVLLGAPLTSNLTSTYLFSLLVSILAILPLAIALPLSDTSARFVWLRLASTFTPTDDLELALFAPALGTLVGAWLGAVPIPLDWDRPWQQWPTTPVLGALAGHALGSLVALARIAYGGVVR... | Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 357
Sequence Mass (Da): 38128
Location Topology: Multi-pass membrane protein
|
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... |
A0A3D3SCJ1 | AAYGSAADHPYFDLPEIVPLRPITADGTGNRQARLYLLELFHGRTCAFKDMALSVLGGFLRESLSRMGRKEPVLVLTATSGDTGSAALEGLSAIEGIHTAVLYPEKGTSEIQRLQMTTVGLERRFVAGIQGNFDDAQNAVKLIFARAARGEGPLAGVRLSSANSINIGRLLPQIVYYVAAWRALASRGALGAGGLMHVAVPTGNFGDILAAKYAKEMGLPIDRLICASNANKVLADFFETGVYDRRRELLMTESPSMDILLSSNLERLLYMAAGKDPARVSSLMGQLATMGRFAVNDAEKAYLADFSSGWCSDSSAKSAI... | 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
|
A0A6C1RMF1 | MEYFVEQAASHREAESKIRTKYGDKARIMHHKTIRLGGFLGLFTREGVEVTGYFSHEPPKGRPETSRKSADLEEEKRKILGSVKSEKTIDMVLKELQTIKEKMDQPQQTSVPRTTDHPTLARMEELLQYNDFTPGYIAAMIKRLRATFSIDELDDQEMVEAQLVDWIGESIQIYQPERGDHPTVFVLVGPTGVGKTTTIAKLAAVHGMNGTANGSSQASVRIITIDNYRIGAREQIETYGSIMDIPVACVDSAQEMKKQIALFQDTDVVFVDTIGKSPRQFSQLGEMNEVVRACGGSAQVHLAISATTKTSDLYELLRQF... | 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
|
A0A1Y2FD31 | MVGSASSVVANNQGPLSILSVCIASLSMTVANKYIVSGRNFSMNFLMLAIQSIVSAAAVDGAKRGGILDYPDFSWEEARRWAPVSLGLVSLMYSGSKALQHLSIPVYVIFKNLTIILIAYGEMIWFGGTVTSLEFASFVLMIISSLIAASPNISAWLWPPEVLPGLEGVITETSSGLGYLWVVINCLVSAAYILGMRKKIKSMGFTDWQTSFYNNAISIPVLLVASLVTEGWTSDNFSKNFPPADRSYLIFAMILSGGVAVFISFCSAWCIRVTSSTTYSMIGALNKLPVAVSGMIFFNDPVTLRSVSAVSLGFAAGLLY... | 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
|
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
|
A0A6P4Y6X5 | MESLVEELTCPVCLELYEQPVLLPCAHSLCKTCAGEVFAEAARKPPQQAAGQEATPKQALCPSCRHEFQLPELGVEGLRRNTTLQNIVDRYREAKNTAAVTKAVPCQMCDQEPPNNAVKTCLDCNNSYCETCLATFHPMRGGLARHTLTEASAAAPKVLMCTEHPQEKVNMYCATDQSLVCSLCKLVGKHKDHEVAAVSDTFQQKKTSIGGRVAGLIQQNAEVECFVDKIQGTMTKAEQNCTDIQERVEAFAQTLTTAIVKRKGILQLKVAVEKDQKLRTLGKQLDQWADTGTGITAAIAEAETLLNEEDPIAFLQASKA... | 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
|
A0A8B5WKV6 | MTALDARRLGVKTIILDPEPAAPARFYADDFVCGRLDDETAIRRVVSAADVTTFEIEHISTDVLLRLEAEHHVFHPCAEVLATIQDKLAQKKVFKRAGVPVPRFAPADTEWTEWPAVWKARRGGYDGRGVQVVDGPADVPSGVPGMLEVMIPIATEIAVLIVRGADTEAVFPVLEMSFEAGANICTEVFAPAAIPRDIAERATKIGRETVSALGGRGVFAVEMFVTPGGELYVNEVAPRPHNSGHLSIEACETSQFEQHIRAVLGLPLGSTGLISPASMRNLLGAADGEIGRTCVSGLDAALAVPGARVHLYGKSECRPN... | 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-carboxyaminoimid... |
G9WZR0 | MKKITNKEKYRVLEKSDLQNLKDMNEEIKKSRFRQKFHIQPITGLLNDPNGFCFFDDEWHIFYQWFPFGAMHGAKNWYHMTSDDLVSWKNKGLALKPDTVFDNRGVYSGSAIIYDNKLNLIYTGNHKDERDIRHPYQCVAVLEDNEKFVKKDEPIINMSQDYTEHQRDPKIMYVDNKYYIILGAQDKNLKGRALIYVSDDIYNNWKLLGELKVKGYEDFGYMWECPDLIKIEDKYVLIFSPQGLQANGYKYNNIYQNGYIIGKMDFETLEFIPESEFEELDGGFDFYASQSANQNIYENTAVLIAWMGLPDSSYTTDDEN... | 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
Sequenc... |
D2Z8S0 | MFDALKERLDGVFGKLKGKGKLTEGDVQEALREVRRALLEADVNYKVVKGLVENIRRRAMERSVLDSITPGQQVVAVVYEELMDLMGSEPKPLTISPKPPTLMMMVGLQGGGKTTSTVKLAKRLSKGHKPLVVACDLRRPAAVDQLRVLAESAGVGFYGPEKGESDVLNVIDGALRYARDRLMDVILFDTAGRLTVDDEMMAELDAMKARIAPHEILLVVDAMTGQEAVSVSEAFHSRMDLTGVVLSKVDGDARGGAALAVLATTGVPIKFAGVGEGIDALEVFDAKRMAERIMGMGDVVGLVEKIEQATSEEDVKRLSS... | Function: Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Binds to the hydrophobic signal sequence of the ribosome-nascent chain (RNC) as it emerges from the ribosomes. The SRP-RNC complex is then targeted to the cytoplasmic membrane where it interacts with the SRP recept... |
A0A813CCM0 | MAGIQAQTRKAAKIFQSETMARRGVLAVALLAVAATVALRSATAFLPVSKPLLRGGAAGALATSAAAVGALPALAEEEGGLLNFGKVELGGGFALNLNIPDINLVNISILVAGLFYFLGPLLSESMASREKEIQSDIDDAIAKYNEASTRLAEAKKAKEQADAVVKEINESIAKDVKEFQATLDAQAKKSMEAQDKAMDSSLKDMESRSASNLEKYIDSAAVKRGLVELQNLSSSQKTKFMDAAINSLCWCKIPVLSFVSCVDFFEASHHGTCPDFEQALVSMGKRGEKWGQYNGYYSYDSRSWAAWPGPKSKPQNNTAA... | 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... |
A0A813CML5 | GEAKSYDTITETARSDSQSSDLLTENSHLLDPSSDPEPAESLLALLQDGNDVAICRDGVDAQPTTYAELRQQLEDQSFASFFRRDDRVALVLENGKEMATCLLAVMHRACAVPLNPTFTEAGYASVADAAAQQNTEAVIEMLSQGYRADIQDSDGNTALHYAAWFRLDSLLTPLLEKRARPDIPNNSGECAVHWAAKSSNVMALDAMTRVNRALLSMRDCDGFTAFIVSAQTDNCPVMEWMYLKGVSLEEQDDQGRTALQWACHKGNKKTVQWLLSRSASIVHRDREGMTALHWAAMQGHTIITEMLMEVGAVDLLDVPD... | 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
|
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(+) +... |
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-... |
A0A0G1IHL1 | MISPQQYLENLVKKAARKLTAKLPHFEMESKNISRFGDYSSNVAFSLAKILKKSPIEIARKIKSDLEENRYLDKIEIAGGGFINFFFKKDFWLEMFKNPLAKINPGKGKKVIIDYSSPNIAKPMHVGHLRATLIGDFLARLYKFLDFKVIGWNHLGDWGTQFGMLIAGYKKWGDKKKINKEPIRELLEIYVRFNREIKNNPRLLKQAQEEFAKLERQDKENKKILNWFLRVSLKEFNQLYKKLGILPFSVVKGESEYEKQLIPLINDLKNKGVAILSQGAYIIPLEKYSLPPALVQKSDGATLYLTREIASLIYRVKKYQ... | 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
|
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
|
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
|
A0A4R1BSG7 | MANSALLEDGILDAGLEDAEAKRELARLFDRNFIDLATEADAIRRELHPNDIVTYIVDRNINYTNVCWVACSFCAFYRTKRQEQKGDGYTLSIEQVLQKIQETVDLGGTGILMQGGLHPDIGMEYTTDLIRAIRREFPQVHVHALSPAEIWHLVDKSGLSLEEVLRELKAAGLMSIPGGGAEILTDETRRRISPAKNSTQAWMEVMETWHSLGMKSTATMMFGIDESYEERIEHLLNVRKLQARTGGFTAFIDWVFQPDNTTYLKKHPDFKKASSLDYLKTTAIARIVLDNIPNIQASWVTQPMKTASIALHAGCNDMGS... | 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... |
A0A2E4HQS4 | MKIVIKFGGTSVGNGKRINKVCDFVSKLNEKNQIIVVSSALHSTTDELVKLAESAKKGKMELEVFDIITQRHKKTASEIIHDKKIQNELLESISVLLEELEKTVNGVITVKELSNKTLDKILSFGERLAVLIISAKLRDAGIESKSFTGGEIGIMTDENFGNASPLVKVTQHNIKKNLSGLEKTVPVITGFIGVTQQGEISTIGRGGSDYTASLIGMCFDVDEIWIMTDVNGLLTANPKIYPNAKTIPQLSYNEATEMAIMGSKGMHPRALEPAKLANIPVRIKNTFDPEGPSTLINEEVNVKKDEITKAITIINNLAMV... | 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
|
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
|
A0A7S3XYZ3 | KKNKKRKSTPGRRKMAEHNDKRRKVDESKESESSSVKQPVHFLDYGAGNVRSVRNAILKCGYEIVDITRPEDIAEANAIIFPGVGSFGAAMQNLRDKGYLEPLRAHLQAGKPYFGICLGMQTLFEASEETPGVEGLGIIPGTVTKFDSTQCSVPSIGWNGVLKHKQSEIVAPIGEHELVYFVHSFRALMTEANKDWVLTSTTYGGSNYISAVQKGNILATQFHPEKSGQTGLKIFEAFLSRAGQLDPEPTPIEVPADATTAIAKRVIACLDVRSNDAGDLVVTKGDQYDVREEGDGDQGGKGQVRNLGKPVALCARYYQD... | 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... |
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(+) = (... |
R4YS31 | MSTADRWLLPDGIEEVLPPQARGVEQLRRHLLDDFDRWGYDFVIPPALEYLDSLLTGTARDLDLQTFKVTDQLSGRLMGLSADTTPQTARIDAHSWAQEGVSRLCYCRTVFHAKAPSILAGRTPTQIGAELYGEAGAGADIEIISLMLNTLQQAGLQDLHLDIGHVGIFKAFSAKAQLSNVAEEKLFALLKVKCATDLDAWAEEYLTDPALTTAFKAIVRLQGGIEVLDQVAEKLAAVVPEVTGIIEHLKQVCQAIAARYNVPMYFDFTDLRGYNYHTGLVFAAYVPGYGDAVAQGGRYNETGAVFGRARPATGFSADLK... | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
Function: Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine.
Subcellular Location: Cytoplasm
Sequen... |
V7N473 | MQCCVLLKYGEMVLKGGNRRWFEQWLLTNLDDALSAWPPEHRPAVRRRGGVLVLFTSPALQDELVALARNLIGISLVQPVWRVPRSARAAETAAVELLRDHCTQDGAPTFAVRCHRRDKRFGLSSEQLAARIGARVRADLGWRVDLSHPELELTVEVDRREMFLGTRTHPGQGGLPVGSSGRAVVLLSGGFDSPVAAYRAMRRGLACDFLHCTGAPFTDASSTYKAYALVRQLTRFQPRSRLYVAAVGRAQRTLAASGAGEAQIVAQRRLYLRLACGLAERIGAQAVVTGDSLGQVASQTLPNLAATEQAATLPVLRPLL... | 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-thiocarb... |
A0A6H1A2G9 | MTTRGPFDVWAPRPERVRLLLGDPAQGPVIAMSRGDDGWWTPDEPLPPAADEPSVDYGYLLDDDPDPRPDPRSRRQPAGVHGLSRLERTSWTWTDESWTGRQLAGSVIYELHVGTFTPAGDLDAAIAKLDHLRSIGVDFVELMPVNAFNGTHNWGYDGVGWFAVHEGYGGPDAYRRFVDACHGAGLGVVQDVVHNHLGPSGNYLPLFGPYLKQGSNTWGDLVNLDADGSPEVRRYILDNVRMWLEELHVDALRLDAVHALSDSSTPHLLEEMAVEVAALSAHQRRPLTLIAESDLNDTVLVTPREGGGLGLDAQWSDDFH... | 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
|
A0A151U105 | MASSLILRASRRFVKPAYAASLLIPTQQFVSQSPTTPSPPFKPTQLQNFNFEFRKSVGCVSNFHLVAYLSTSPSKEDNKQSGNVSSSGAGDTSWIDLYLPRQVQPYARLARLDKPIGTWLLLWPCMWSISLAATPGQLPDFKMMALFGCGALLLRGAGCTVNDLLDRDIDTMYFFLSALILIGDIEIVILCCKLIVERTKLRPVASGLLTPFQGLCFLGFQLLLGLGILLQLNNYRKLTTPNTFDIFIGLNTPYFGCLILVARLLISSHEEVYILGWAAVKGSLDPSVVLPLYASGVFWTLVYDTIYAHQDKEDDLKVGV... | 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, ge... |
A0A2N1JB77 | MSTKHIYEVSNGLVEKAVYGAAASNPSLRVFSPHRVVYDASHALDKVGIIAGGGAGHEPTFTGYVGRGMLTTAVSGDVFASPSAAAISSGVDLTPTEKGLVVIVNNYTGDRLHFGLAAEKARTVFKQEKKGKEVEMVVVGDDVSVGREKGGLVGRRGLTGVAFVCKALGAAAEADWETKKLGEFGRVMVDNIVTCGSSLDHCHVPGREKGDEERGALGPNAIEIGMGIHNEPGVQHIDDKPSSEDLLKHMLKLLLDQNDKDRAYVKFEKSDDPVLVINNLGGMSELELFAIAADVKRLLQSEWGLKPVRVYVGTYITSLN... | 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 M... |
A0A354ZED5 | MIGAFESNSRKAPRSIPMEKRTKIVATTGPACGDLATIRELIREGVDVFRLNFSHKTYDEANNEVTMIREARKALDKPVAIMADIKGPAVRLYGYTEPLAIQPGAELTIESTEAVGIEKLAAKKPMQVYTNLPDIDRICAVGQKVILMDGYFTGKVVRKVPKGIVMALENEGNLRPKAHLTLPGVDYPLPFLSEKDISDINWAVEQDIDYIALSFVRCETDVEEVKRLVQRTALAQGKNTLIKLIAKIESARGLENIDEIIRTADGIMVARGDMGVEMSIENVPIAQKQIIRKCYLAAKPVITATQMMESMMENPMPTRA... | 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
|
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... |
A0A354ZFB4 | MVTIAFPESLKGLHIHLVGAKGTGMTALAEILHTRGALLSGSDVADVFYTDGILHALGVKLFESFDARHVPEETDIIIYSAAYSLAANPELKAAIQRHIPIFSYPQALGALSLHSRSAGIAGVHGKTTTTAMAGILMEALSMPATVLAGSAISNFNGRCTLIRGGDYFIAETCEYRKHFLNFKPSWIVLTSVESDHQDYFPTYESIRDAFVEYVLSLPDNGVLIFCADQPGAVDVADIVLQKRKNISFVEYGFSAKGKYKIRDFQTSAGTNTFMVSDAPKPLQLHVPGRHLVLDAVAAIALAESIFEAQTSRNFGQDEWN... | 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
|
A0A812JXE5 | MVLPAAALNDPRGQEVDETSLSKGRLDWLLQVIKSAPLALASELSHHRALFPLAIAQMTLLADQPLLSTNMSAVANEFGFAGAEKDEKLGGIVSVVFFACGVVSSLIVGRLADVMKRSTLVCLCMLIGSTGTFSNSQAESFTSLLFGRAAVGAAVGGLIPTSFAVIGDMCPAEERPHAIGVVCIISGLGLPVGQSLAGFAGSASGWRAPFAVVGIAGWCVTLLLFFIHEEPARSNDQHLSHDVSSWSALTKPTVLCICSQGVFGCIPWAVIGTFLTDYLAVNDGMGVAGATSVLFCMGVGFIIGTIAGGKLGQHLYKKDK... | Pathway: Protein modification; protein glycosylation.
Subcellular Location: Membrane
Sequence Length: 849
Sequence Mass (Da): 91829
Location Topology: Multi-pass membrane protein
|
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... |
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
|
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(+) +... |
A0A137PEH3 | MKYQLKYHDNVFDIEAEPYSKISDLRLQAEQHFGLQENTVVLFYGNALEERKCLGQVGIRPGATILVYLRPGSNSALRTQNPIPSKSIYSHQEPIRKGKYISSNDHRSKYNNNSSNYNTGSKNYRSQYNNNDNSKYNTESSNYRREYNNRSNYNTGSNSYRSQYNNNSNYNIGSSSCRREFNNNSSSKYNTESKKNRDCSLCKDKRSQKCTRCGCGICFEKNPENLIRCTKCPKNYHTQCLQISLNSIPKNSWVCPGCIRENGHNPRIDRAQSSHHHSSNNSNFSNYHRTQSSNNLVRDTNVKLEPRSASISNGYHSPNS... | Pathway: Protein modification; protein ubiquitination.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
EC: 2.3.2.27
Subcellular Location: Nucleus
Sequence Length: 7... |
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-riba... |
A0A3B5LHJ7 | TTKTMTNMDYEKPVDYESRSSYSFSVEVLNPIVDPRFLRRGPFKDRASIRVAVLDADEPPRFSRSKYHMDVSENCPPACTVGRVSAVDPDTGLTNNIRFSIDPQSDPEALFRISPETGLITTAMELDREREHWHNITVIASQRGQRPHRCVIRAFFLLLLFTGLCPTASLVLLSQLQPLSRSPSSTLTLYVPLVLRDGTSGLTSTGTVTVSVCPCLRGGALCLPQQSMLPSPGLSTAALLAILACVATLLVSALSLSLRRQKRDSLSPLEEDDVRENIITYDDEGGGEADTAAFDIAALQSQMGLGGYVLGRRDMSPQLL... | 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
|
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 + thi... |
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
|
A0A6N2E830 | MADKERYQMLVIGAGPAGYVAALRGARLGLRTALVDKRPTLGGTCLNVGCIPSKALLDSSEQYHKALHGLEAHGLKLTGVTLDLPTMMKRKDSVVEKLTGGVAMLCKKAGVDVYTGTARLVDAHTVEVSGGGGAGGSGGAGGENGAGSESMSISELTANAVVLATGSVPVELPSLPFDGKQILSSTEALSLETVPKQLAVVGAGAIGLEMASVWARLGSDVTVIELQPNILPGWDPRLSKVLQQEMEKAGVKFHLGAQVEESKQSKKGVSLSVKLKDGSSATVEAQKVLVAVGRKPYSEALGLEALGVAGEKGRVTVDEK... | 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
|
A0A9D9M8Y5 | MQKVFADTRTLDADARKKYSITEEVMMENAASALEKEVLEFLAGCSTPKPVVLIVTGTGNNGGDGYALARRLCGKTLSDGRKINVCIFAPKPPKTEIAVFQKETAVKTGVSFVNTLENTNPDVLVDCFLGSGLSGKLTQDAENLIKRLNEIKAFKIACDVPSGLSAESDTFFIADKTVTMGALKTQLFCENGKDSAGTVVCADLGISRDCFELSDSAVQPEAYLLEKADLLLPHREKNNVNKGTFGHLAVWGGEKRGATVIASKAAFAFGTGLVTVVDNANNGSFTVPEDILCSNTVPSNISAVAAGMGLGAFCDTAVSY... | 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... |
F2IA69 | MADGEKIIQINIEDEMKSAYIDYSMSVIVSRALPDVRDGFKPVHRRVLYGMQDLGVYSNRPYKKSARIVGEVLGKYHPHGDSSVYDTMVRMAQSWSLRYPLVDGQGNFGSVDGDSPAAMRYTEARLRKIAEEMLDDLEKETVDFAPNFDDSLQEPTVLPSKIPNLLVNGASGIAVGMATNMAPHNLGEVVDAIIGYVDNKDIEDEELLQFVKAPDFPTGGIIYGVDGARDALLTGRGRIVIRAKAEIEESGGREQIIVTEIPYQVNKADMIKKTADLVNDKKIEGISDIRDESDRNGMRIVYELKRDAIPNVVLNKLYKY... | 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 ... |
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... |
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
|
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... |
B9YC58 | MNKGNFGTLQDGRSAQWLEIENDKLRVRVSDYGATLVSLWVKDAQLDAVLGFDQVEGYQQSVKYMGAMIGRVANRIKDGQFTLDGQVYTLYRNDKGNTLHGGQEGFDAKLWTVREHTSQTVTLELLSPAGDEGFPGELTVTVTYALAGSRLSITTRTRTTAATPVSLTNHAYFSLNGQHPSLDGHWIQVDADEIGLLDPNGCTRPETLEVEGTVFDLRQPKRLTEILNQHHSQLEIAGGLDHNYVLNGVGFRPVASLVKGGLTMRVLSDMPDMHVYTANFLNSEVGRGGTRYTPHCAVCFETQYYPNSVNDPSKISCILN... | 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
|
A0A662Q0P1 | MTSSRRAKVLSWLLGLDLIGESVLIEGYEVDVEGVKKWIRENEVKRVLVQAPPGLRGVRRKLIDEISGELDMVFVHGGGCWGGCDLAVAHAKAVGADAIIHLGHARFLEKSPIPTFYLECRKTDPAPILAALEKSAKILQGHHKIGVGVTIQWQDSLSPVRKKLEEYGVEALTGPPIPPLRYESQVLGCGYEPLLRLSEEVECYLIVGSKFHGLGLALQTEKTVYSLDPELQRLDDLSAEVEKLLRSRYGYIEMFRRADEVGVVVSVKPGQYRMGAAVKLRETLRKAGKRAEILIMDDVEVNLLRDSGFEGFVNMACPRL... | 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 f... |
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
|
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,... |
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... |
V9HVF1 | MKLKTLTVSQVNDYLANYIGTNPIFSNMSVGGEVFNLKKTGYGYTFLSLKDDESKLNAITYLEKFDVQEGDFITVSGKISFYKKSGTYSIIINSYEKKGQGNNYEQFKILYEKLEKLGYFKYELKKPIIKFPQKIGIITSAKGAAVKDIISVITRRYPKVSLIIYDSKMQGIDVENNVIQGINTLSDLSVDTIIISRGGGDTDDLSVFNSQLIAKAVFDCDIPIISAIGHEIDYVICDFVADMRAPTPSIAGELSVPNLQEVYDTIDNFEKSIKISYKNIINLYNSKIDSYRFLIQSNTPYKKINQKKLSLLELTSFIEQ... | 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... |
A0A6C1PKT0 | MARRNRWKSFDAAILRRARRPFLRFFRRTVPTMTAASIRDCLPAGKRIDLGSMTRSPTRVIAGFYLAVALAATYILLGSPLAIDGIGWADAPLIVLIALHYVWGIVLVFSSSGSLPFRRSFVRRLVFVPEVLGAFALLLFLFSYIFALNANMDYVQRFIAAGGNLRLALDTRVERLLVWARVFPLVALNLGVYLLVRVSRYRAVREACRPSHEPRDAIVRPWSLVLVLLSSFLITIAQPSFVSLDGIAMLGWIGFVPLFLVLRSVRFGHGVFYGIVFGVFSTLLTSYWLGTFNLVSLAITVLFFLIYYALFTPVALLAYR... | 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-[lipopr... |
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
|
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: Cel... |
A0A8B5WXP3 | MSRTTPQRSFHIESLGCAKNQVDSETIISSLIADGWHESPSDEADVIIVNSCGFIAPAKKESIDTAFGFRTAYPGRTIVMAGCLSQRYADDLAQQMPELDGVFGNRDLAGIGAFLDLIAANPRNPVSVAPPVAGVEASEPSVMPEVVGDRRRLLSPAGSVYIKVADGCDNSCAFCAIPLIRGRLRSRDPDVIVAEARLFVSRGIKEINLIAQDLGSYGRDTRDGREIVSLIRRLLEIPGEFWIRPLYVYPERFPKELIRVMRDDDRVVPYFDIPIQHASTRVLRSMGRPGDRNSHGELIRWIRGELPDAVVRTSLIVGFP... | Cofactor: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein uS12.
EC: 2.8.4.4
Catalytic Activity: [sulfur carrier]-SH + AH2 + L-aspartate(89)-[ribosomal protein uS1... |
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
S... |
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): 33... |
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
|
A0A6I7QSZ7 | MCRDQDDRWLARTLELARQGAGRVEPNPRVGAVIVKAGELVASGFHRNYGSLHAERAALSAAEPDLVRGATLYCNLEPCSHRSPRKKQPPCTEAIIAAGIGRVVIGHRDPNPAVRGEGIRALERAGITVDVRGEDADESPFLRENEVFNTVMALGRPFVHLKAAISLDGRLATTGGDSRWITDGEARTAAHRLRAESDAVLVGRGTVEADDPLLTVRLPAGEVQGSSPAPRPVVLDSLARISLESRLVRERGNELLLCLGPDAPERRRAALEARGVTVLEAEGVGGLDPASVLKCLGTAGIRSVFVEGGAQILTAFLRAR... | 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... |
R4YMV9 | MSQSILWYDYETFGADPSFDRPAQFAGIRTDENLNEIDEPVQFFCRPSPDYLPHPQALMITGITPQQCLQDGLPENEFIDQINQILSVPETCTAGYNSIRFDDEVTRYTLYRNFYDSYAREWQNGNSRWDILDVMRCAYALRPEGINWPKNAEGNVSFRLEDLTAANGIDLGKAHDAVVDVRATIAIAKLLLEKQPKLYRYLFEHRIKHKLASLVDIDHHKPLVHVSGMYGVDRGCMAIVVPICWHPTNKNSFIAFDLSTDPKSLAGLTIEQMQQRLFSKQADLPEGIERLGLKEVHINKSPVLAPAKTLTPDQAARWDI... | 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
|
A0A1G6HT77 | MSTLAQRSVLGSSGYPLDQIHIAGIAARGFHGVLESERKAGQDFSADVTLYLDTRAAARGDDLTETVNYATVSQDVADILSGEPVNLIETVAEQIAAAVLARPAVISVDVTVHKPQAPIPVPFVDVVVRIHRDRINAPVVASPLDVAAPDVAAPADSVDDIGADAAVGVGETEPEAAAVVEETVAPRWQAPVPTSTAALPVVISRSAETNGEPLDAPLDAPLDAALAAWAAPAPVLAPAPVLPLAAVLPTADTLPEPVEEHAPEPEPEPEPEPEPEPEPEPEPEPEPEAVEPASAFEIGATAVLPPLDEQALAEQARLSE... | 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 = ... |
A0A137P4H2 | MTVSETIQDILNIAGFDVNSQEFAQHLDNTELSKFFAKYRSEFFLPKIGNIQPEGKTSDRPEDEVIYLVSNSLGLLNKRTKKLIEEELDVWSKKGVFGHFSHDFQRPWKDIDETSLPMMAKVIGAKVVETSIMCTLTANLHFLLNAFYKPTSTKYKILMEDKAFPSDHYAIISQVKQHGLNPDTDIIYLKPRKGEYLIREEDIFKAIEDENLALILLPGVQYYTGQVFPMEEITRLGQSRGVKVGFDLAHAVGNIPLELNKWNVDFACWCTYKYLASGPGNIGGLFVHERYANASEMNRLIGWWAHNPDTRFKMSNQLEL... | 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-... |
A0A2N3G838 | MLKAAVIGASGYAGAELMRILWGHPELEVVHATANKYAGCPVGSLYPSLAMQYPGDFEEYAPDLFNDCDIAFFGLPHGQSMKVVAEAASAGLKVVDLSADFRLSREDYLKWYGIEHESPELLGKAVYGLPELGRETIAFALVVANPGCYPTSALLGLFPLANAGYIKEKNTVIIDAKSGVSGAGRRPTHATHYPRVADSMSPYAVTGHRHAPEISGWLASMAGGAVDVVFTPHLAPMNRGILSTMYVPLEAGSSIEDIRALYYDTYESEPFVHLLAPGSFPETKAVQGTNNCHVALEVSRSGGTLVVMSAIDNLVKGAAG... | 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 = ... |
A0A1W9PVM7 | MIAVLMSGGVDSFVAAHLLKKSGADVVGVHFKTGYENADASRLQEIAALAGVPLVFLDCEREFKRKIVDYFIGSYLDGETPNPCIACNRLIKFGVCADYAVSIGAEAIATGHYCSAVRVGNRTVLGRGADTGKEQSYFLAFLSQAQLSRAVFPLGNMKKSDVKKLAHDLSFPFLTQAESQDVCFIRDTGYARFIEEHAGMEFSPGHIQDTEGNIIGRHHGVHRFTIGQRRGINIPSSRPYYVAAIDTRRNLLTVGHREDLFVSEFMVRNVNWLLEPPDGSLDLLVMVRYNQTAVNARVVPVDGGRARVFFATPQFGVAPG... | 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 Lo... |
A0A3C0WWK9 | MTKKNLLKGLTLPKTVEYEVVEEDGGNKEYAKIAAYPFERGFGTTIGNSLRRALLSSIQGYAVSSLMFHVRKDGNLTTISNEFEALPGVKEDIVEIIANIKKLALKCSGEDFESQVMTISCKGPGELTGAAFAKNGIEVINSDLHILTMEKDVDMDIDVQIDFGRGYIPADMQKNYVVETYGVIAIDSLFSPVVRVNYSIDAARVGQRNDFEKLVLEVWTNGAISAVNAVGQAAFIVSEYLQKFINFDKSEVLNSQEIEKCENDRIELLKSSIDRLDLNSRSMSCLKRININFIYELVQKNEDELLREKNFGEKSLGEIK... | 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 assemb... |
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-dihydr... |
A0A6B2C0I2 | MKVGFEIHIQINSKRKLFCNCNPKSDESSQIEFRRRLRVSTSELGEIDPAAAFEIKKGLDIIYVSGDKTSCLVEADEEPPHEPDPYSVEVAIKISNMLNSFIVDEIHFMRKIVVDGSNTSGFQRTAIIGLNGSYTFRGKNVRIQTICLEEDAARLLEKGEGYVKYELKRLGIPLLEITTEPLEISPEEAKAFAESLGRTLKLTGLFARGLGTIRQDINVSVEGGCVVEVKGVQKLEQIQKVIEFEEKRQKMLLEIAAKLKERGISEENFVSIEPVEVSDVFKNHLNIPSVKKFFKDYAFALKAPGLKGLFSYETVPDSRL... | 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 g... |
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
|
A0A1F4VDY6 | MLSTQPYKGVRDFFPDDIKVRNYIFDTWRKVCLSFGYEEYDGPFLEPFELFSAKTGDEIVNNQLYSFEDKSGRKVAIRPEMTPTVSRMAAEKIRMQTPLPLKWFSIADFYRYEKPQKGRGREFYQLNVDIFGEESVNAELEILLLNKGIMEKFGATDKMYEVRFNNRFLMNYLYERIASLTVPEIKAVQKAVDKKAKISNSEFESLLEKDIDKSKIKKVHEVLNLTISDIKKLKDLPDKASNLLKLMEMAQKVGIKNIIYDPALVRGLDYYDGNVFEQYDLTKGNNRSMFGGGRYDGLISLFIDKKVPAVGFAPGDITLM... | 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
|
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
|
A0A2S9V825 | MSSPSKPPFILVDGSSYLFRAFHGLPPLTNTKGQDTGAIYGVINMLKSLIKQYNPTHIGVVFDAKGKTFRDDIYPEYKANRPPMPDELRSQIAPLHDIIKAMGLPLIIEDGVEADDVIGTLARQAGEQGIDTLISTGDKDMAQLVNEHVTLINTMNNQLMDVQGVQDKFGIPPELVIDFLALKGDKVDNIPGVPGVGDKSAQGLLNGIGGIEAIYQNLDKIAELDFRGAKTLGKKMAEYEEQARLSYKLATIDVDLNLDYSPQTLTPEQADNDKLADLYSEYEFKRWYTEVTSSQATPAATDSDSQSKETDEEDSAAADI... | 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
|
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
|
A0A3B5KQ85 | MVRRVAVVGAGSSGLACVKVCLEEGLDPVCFESSDDIGGLWKFKESPEPDRSSIYRSLVVNTSKEMMCFSDFPMPDDYPNYMHNSQLLQYFRLYAEHFHLLQHIRFQTTVRSVTQRPDFSESGQWDVVTMNKNNEEERHIFDAVLVCSGHYTHPVLPLSDFLGHETFLGRLLHSREYRDADSFRGERVVVVGFGNSGGDVAVEISRSAEKTFLSVRDGFWVMSRMAHRGLPVDMALISRFNILLLQLLPKTLINWAAERALNQKYDHELYGLKPRHRLLDKRPLVNDDLPGRILQGALIMKPNIRAFKDSGVTFEDGTVE... | 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
|
A0A146KIX5 | GRTLKAQYTRNLMLEEVNPITDRKKRKFRDLLCVIIFIAFWIFIILLIVLNKIWTQYQNSTLLLEPHDFMRRRCGQSSNNQKDKLATDYSKLITQQDQFVQFCTVFQQVYTGVEPYDCQWLNQSQNISAIYNSRTFFNKISQTAVDTTLQSAGFSVNDVKICVAPAYLEASSSAANCNPPLEAAYVCAHDFVNFAMELISNPVLKNDIDNLVNKQFYTQSMINQIMNDVGFNNQFIIKFCQSIPAYVGNNSIRDDFAQNAIQQLFNIKTCSRSNLFFENQLFKDIGNYISDFSNNFLMQISSRWQWILVGIGSGILFMIL... | Function: Choline transporter.
Subcellular Location: Cell membrane
Sequence Length: 738
Sequence Mass (Da): 84200
Location Topology: Multi-pass membrane protein
|
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 rele... |
A0A9E4DEP7 | MIVPSIDLMGGQAVQLIGGETRAIDAGDPFPIAERFAVAGEIAVIDLDAAMRQGSNAGLIEGLVRRFPARVGGGIRDVETALSWLDTGAVSIILGTMAVPEVLKDLPKARLIAALDARNGEVVVEGWKTGTGRGILERVAELKGLVAGFLVTFVELEGRLGGTNLDLAKEIVAAARPARVTIAGGVTTPEEVADLDAIGADAQVGMALYTGRMDLGEAVAAPLRSDRPDGLVPTVVADAHGVALGLVYSSRESVKTAVNERRGVYHSRSRGGLWRKGETSGATQELLRVDADCDRDALRFTVRQAGAGFCHTGARTCFGE... | 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 Len... |
A0A812M9G5 | MWLIWWDPCGLFCYLFGELVMVLSNYVVLVYILGPWTQWNTVGIVNGVLFQTVVCLVFVAHWRAMFVCPGVTQLNSATPADCQPDQSDPTWWTKPKRKYCTKCKAIKPPRAHHCSVAGRCVVKMDHYCPWVNNTVGQNNHKFFLQFLVYVFIGTAYAALASLAYGLAVWQGWTPWPKWSVLDIGLVVAQVVLDAFFAIFVCAMMSDQFEAVCTDTTGIEAMKRWEERDWTLMQGLTNVMGGPLGLHWFIPTLPQGKALYQWSATDDLDAYDIRDPSIKNFFRQLDFEARLQELNAAKGEEGQADAPSKPSLPNLQELIGQ... | 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
|
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
|
W0U4J5 | MSEERIPKRSEVPEQFKWALEDIYATDEKWAEDLQKLKAMPERITAFKGRLSESADTLYDFMQLSDEISVLCDSLGNYAQRRSDEDTANAKYQGFLGQLMNAYVAVNSAGSFETPEIISIEEDKLQKFYEDKPELKLYKRALDKLRRKKAHILSEAEEKILALTGEMGQSPENIYSMFSDADLRFPDAVDKDGKAHQVTHGSYIPLVQSEDRVLRKSAFESMYGTFDKFKNTCAATLSAQIKAVNFYAKARRYDSSLEAALDGTEVPVSVYKNLIEAVHDNMHYMYDYVALRKKLLGVDELHFYDLYTPVVPDADMKITF... | 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
|
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
|
A0A4P9A1A1 | MEKLDEVRALLLSRVTEVAEPRSVLRSAELRELYGIIATLPAEERGAFGKKVNELKQELERAITAREDELSKVDLPPIDVTAPMDVNAPRPELLPSERGTIHPLSAEIERISDIFNRMGFVTEESREIDDQFHMFESLNFPKGHPARDDYDTFMTEETDANGDRLIAPAHTSTMQNRVLKKYHGNLEKGEAIAAIVPDRVFRNEDLDARHEHTFYQVEGVYVAKGVNVGNLIATLQEFLQEYYGKKLDVRVNPFYFPFTEPSFEFALSCPFCEGKNPDCKVCSGEGWIELLGCGMIHPNVLKAADIDPNEYTGFAFGCGI... | 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
|
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
|
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... |
K6WYS1 | MEQLSGADAAFVYCETAGAAHVTFFAIYDPSTGPGKIVGFDDVFAHFGSRLGVASFFRSVLVRVPFDLDHPYWVRDENFEVGHHLHHVTLPGPGDWRTLCDQVSRLHAEPLDLHRPPWDCYVIDGLGEISGIPDGSFALCLKVHHSALDGLTGLTLVMQLHELTPETSPPPEDVWVPESRPSSLHLLARSAVTVARRPAQLASAAEHSIPAVGRLPGATLRRLLPRHGSEYLPALYAPRTRFNGHTDSTRNFDGRSYDLAAVKAVRTLVPGATVNDVVIAGIGGALRRYLLANGELPEKSLTTVIAISLHHATGRPHGVN... | 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
|
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-ribosylam... |
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
|
A0A812YER3 | MQSNRVAATDFENPVGIEIPPPNAKPANERTKKNVITILGVVAFIFLVTTILFAVLYAVEANRDEDSSRGECPVQGAYVPETGDLAEFSNNVDRVKEMFDTITPEELLAVRNFAVQEWGLTPIADRSSEQFDEDYLLTTELAPAPKAAAKDYIDGVSDTSPGRYAHAFVVKGSEATPMVHVYLVGPLGGTLTATELTAPNHPYPVPFNMSALNGMVETFIADLDAENFWTTAYGLTADDIWWTDSSPRGYDRASRKTWHWFNAWGEGQYIYPLGLTVLIDHQDLDPQNWSIERIVFNGQGPYATVADLITASADSGFEWP... | 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
|
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
|
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.... |
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
|
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.