ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
|---|---|---|
A0A1Y1S259 | MIPLTNYHTHNSLCDGTGELEEYLATARRKGFAALGFTSHAPLPFINDWTLAEADLETYCSRVRELQKNSDPELYLGLEIDYIPGRMGPAEERWKQYRFDYTIGSVHMIPVDGKAWSIDGPDDEFLHLYRNVYNRDGTAMAVEYYRLLEEMIHKGGFTILGHLDLIKKKNLKMHFLNEEAPRYTDAVLRVLDSLADSGIFMEINSGGLFRGATEGVYPSFSILQEARRRGIPLVINSDAHTPEALDFHFNEACDLARKAGYRRTMMLLNGDWREIPLGEA | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 8/9.
EC: 3.1.3.15
Catalytic Activity: H2O + L-histidinol phosphate = L-histidinol + phosphate
Sequence Length: 280
Sequence Mass (Da): 31913
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A0A6H2FUE7 | MKKTNIRQVVLDTETTGMNLSYPYYIGHRIIEIGIIEIINRNITQNYFHTYINPQKIISKEAFSIHGISNKFLSKKPIFSDILDNFLNFIKGAELIIHNAQFDINFLNYELSLLKKKTPKIEDICIITDTLKIARNIFPGKRNSLNSLCNRFNINISKRNLHGALLDAKLLAHIFLFMTTKQNSFQLEFLKEKNSIFKNKIKFLNAKSKIKKTLVINASKKELKLHQLQLNLIKNKYGFSLWENKNK | Function: DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. The epsilon subunit contain the editing function and is a proofreading 3'-5' exonuclease.
EC: 2.7.7.7
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)... |
A0A9D8KAW3 | MRSDLKDKKIGIVGGTFNPIHLGHLRSAEENREAFDLFRVIFVPSAEPPHKAGNIIDAKHRYRMVKRAIAANHSFSASDLEIKRGGKSYTIDTLIHYKELVGETGEIYFIIGLDAFREIGSWMRFRELFEYAHFVVTDRPDAGSKNPKFTIPGEIKSAFKKGAGGRGGFWTHTSGSKLYFQDISALDISSTTVRRLVKEGRSISYLVPESVEKYINKRGLYR | 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... |
A0A366MJ50 | MSGIAGIVDSRGVAYPLYYALHALQHRGQEAAGISTFDGRAFFMHKGPGQLSDVFCEKVLNRLAGNVGVGQVLYTQKAHRGRTENIQPFNFNFKDHQLSITVSVALINREALRSEYESKGHIFSSTTNAELIAAMIAHELIAGVSAEEAFVNTMQRLSGAYAGVAILDGVLYAFRDPIGTKPLCYGRTEFGHVVVSESVALDILSAAFEADVRPGELLTITEDGVSHRQVLESDHKAYCVFEYVYIARPDSVIDGVLVYDARRKIGACLATNPPKADLVSPVPDSGVAFATGYASESGIPYIEGLLKNRYVGRTFIMPTQ... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2.
Function: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine.
EC: 2.4... |
B1H0L1 | MDNKIKTALTNSDKNNIWHPFTQMADWLNDDPCKPLIIDRAKGSYLYDVDGKKYLDGISSLWVTLLGHKNPRIDKAVKKQIDKVSHTTFLGLTHKPAIDLSEKLLKILPDNLKKIFYSDDGSTAVEIALKMAYQYWQFKNEKRSFFLSLKNAYHGDTIGAVAVGGTDLFHSRFRSLLFKSFFAMSPYCYRCVYRKKEIKFPVTAENFKDHNIQMHCRGQCIKEVESILVKNNKKIAAAVIEPINQAAAGMIIMPKGYLKEYANLCNQYGIPLICDEVATGFGRTGKMFAVEHENIKPDFICLSKGITGGYMPLAVTATTN... | Pathway: Cofactor biosynthesis; biotin biosynthesis; 7,8-diaminononanoate from 8-amino-7-oxononanoate (SAM route): step 1/1.
Function: Catalyzes the transfer of the alpha-amino group from S-adenosyl-L-methionine (SAM) to 7-keto-8-aminopelargonic acid (KAPA) to form 7,8-diaminopelargonic acid (DAPA). It is the only amin... |
A0A357LBR4 | IAAQLAFPNLFYFPDLPWTSFGRLRPLHTSAVIFAFGGNVLIATSFYVVQRTCRARLWGGLAPWFVFLGYNLFIVIAATGYLMGVTQSREYAEPEWYADLWLTIVWVVYLLVFLGTLLKRKEPHIYVANWFYLAFIVTIAMLHVVNNLAMPVSLTSTRSYSLFAGVQDALTQWWYGHNAVGFFLTAGFLGIMYYFIPKRAERPVYSYRLSIVHFWSLIFIYIWAGPHHLHYTALPEWAQTLGMTFSIMLWMPSWGGMVNGLMTLSGAWDKLRTDPVLRMMVVSVAFYGMSTFEGPLMSIRAVNSLSHYTDWTIGHVHSGA... | Cofactor: Binds 1 copper ion per subunit, denoted as copper B.
Pathway: Energy metabolism; oxidative phosphorylation.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
EC: 7.1.1.9
Subcellular Location: Membrane
Sequence Length: 433
Sequence Mass (Da): 49810
L... |
R5FL66 | MNEALFFIEIILTFGCVVAAKKIFGKAGLIAWIAIAMILANLTVVKTIDLFGIEATLGNIMFASTFLAGDMLNENYGRQAAHKGILVGLAGVLVFMVCTQISLLYTPSTSDISQEAMVLLFTLNLRTSIASVAMCVLANWLNVSLYAKIRELTNGKYLWLRNNVTTITCNCIENFLFVLLAFGGIYSMEQILAIALSTCAIEIFLALCDTPFLYLSRGESKLLSKVTASH | Function: Involved in the import of queuosine (Q) precursors, required for Q precursor salvage.
Subcellular Location: Cell membrane
Sequence Length: 230
Sequence Mass (Da): 25102
Location Topology: Multi-pass membrane protein
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A0A1G1LV54 | MQLSKLLQNITKEKIPSDVAHYDIRNVCSDSRKVIPNSLFIALKGFSQNGEDFIPDAVKKGAVAVIKSPSGSQSKSLTSRLPKDPNVFILEVEDTNKTLREIAAKFYDHPSSKVRTIGVTGTNGKTTTTFVIESILQKAGQACGVLGTINYRINREVFPAPNTTPDVIGIQQFLYNLMQKNIPYCVMEVSSHGLDQGRVDLIDFKVGLFTNLTSDHLDYHQTTEKYFLAKAKLFQNLSKGSHAIINGDDPLAKQLKAMTKAKVYTFGVSSDSDFKAVDITTDISHTSFQIKCPQGKMINIRSKLIGLHNIYNILGAVAAC... | PTM: Carboxylation is probably crucial for Mg(2+) binding and, consequently, for the gamma-phosphate positioning of ATP.
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in... |
A0A9D6KDK9 | IPIFGLPGNPVSAMVTFDQFVRPALLHAQGGFRWLRPAIYATLTANIQKEPGRSHFVRGHLTIENGEYKVAPTGDQDSSNLVSLVKANVFIVLPEACGDLEAGKKVLVQIMTAPLF | Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
Function: Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP.
EC: 2.10.1.1
Catalytic Activity: adenylyl-molybdopterin + H(+) + molybdate = AMP + H2O + Mo-molybdopterin
Sequence Length: 116
Sequence Mass (Da):... |
A0A9D8KGZ9 | MLATINWLRDFVDIDMDVEKLADLLTMSGLEVDSVTKIGDDLKGIVVAEIMDVSTHPKGGNLYVAKVSNGAETFQVVSAAPNTKVGLKTALAPPGVVLPTGLKIEKRDFKGVESTGVLLAEDEMGLTHDHTGLIELDPKAAPGKSLAETLNLSDYLIDIDLTPNRSDCLSVIGLAREISALTGAPLRLPKTDVKEEGPDINELTSIEVIDKDLCPRYVARVVQDIKIRMVPFWMRLRINQLGMRDINNIVDITNYILMEYGQPLHAFDYDLLSGNRIVVKRAKEGEKFFTLDAVERTLNKDVLMIADAERSVAIGGVMGG... | 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: 812
Sequence Mass (Da): 90150
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A0A969KAZ6 | MSIVENKVLAPYTSWRVGGPARFFTEATTTSEVRRALRWSQERTLPVLLLGGGTNLLICDEGFDGLVLRYRARSWALENQGTTGLLSLAAGTPIGHLAWIIGSQGWSNLEWAAGLPGSVGGAIYGNAGCYGGSMAGVLRRAWLLIEDQVQEWSVEHFAYGYRSSVLKQPRRFSSRRSEEGEGAPASDPDRTCPRPGAVMPAVILSAELVLKRQDAGSVEETMKAIIANRKERTPVGHSCGSVFKNPPGSQVTAGQLLDQAGLKGTRIGAAEISQRHANYLLNLGGARSDDILRLIELARNTVLRQFGIALELEIQVVGPV... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation.
Catalytic Activity: NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
EC: 1.3.1.98
Subcellular Location: Cytoplasm
Sequence Length: 322
Sequence Mass (Da): 34760
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A0A366MDC6 | MDDRSLLASIRHLIGEEETADDCAAFDLGDGRILVSSTDMLHETTDFPKGMTEFEKGWMSAAVTLSDIASCGAQPVQLLVAVGLDDPSRLVPFMEGAVSCAERFGAKVAGGDIDSHTELTVVTTGFGIVEKAHYCRRSGASPGDVVCITGTPGLAMAALEGDERYRKNLLNPGPQVDAGQKIAAVGASSMMDVSDGLAISLYDMAEASGVGFALDSAKFNLPDVRPGSAREYYLYGGGDFGLLFCISRERLPALDAEYTVIGTVVEENGVWYDGNVAEKRGYAHSW | 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... |
A0A671S4P0 | MAPFHAVKCCQRGLSWIPVIFINLVVCWSYYAYVVELCIYTISNTEEQVIYLLVFHVFFFMFIWSYWKTIISKPASPSKEFCLPKVDKELYEKEENPEAQQEILKRVARNVFIYTCTGSGAIRYCDRCQLIKPDRCHHCSTCDRCVLKMDHHCPWVNNCVGFSNYKLFVLFLAYSMLYCVYIAATVLQYFIKFWTNHLPDTHAKFHVLFLFFVAAMFFISILSLFSYHLWLVGKNRTTIEAFRAPVFRNGPDKNGFTLGFRKNVTQVFGDQKKCWCLPIYSSLGDGYTFPTRLVNADSEQGNAEHQAIKCTVDGQTNPRP... | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 360
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 41708
Location Topology: Multi-pass membrane protein
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A0A968NBI3 | MTDTGVILRAQSGFFWVQTADAVLRCRLRGRLKKDRQSSDIAVIGDQVDVEPTSPNEGAITHVHPRQSSFSRQQPGPRGQWREDVLIANLDQVVLVMACANPDWNARMLDRFLMIAEHNQIAALIVANKTDLLAPAQVAAMVQPYEQIGYPVFATCTPTGAGIASLREHLAGRVSVFTGMSGVGKSSLLNALQPGLQLATGAVSATLNKGRHTTVVAELHALPDLGGGYVADTPGIRELAAWRIPDADVAWCFREMRPFLGQCEFNNCLHTHEPNCAIQAAVATGEISPTRYESYVRILEKQERSG | Cofactor: Binds 1 zinc ion per subunit.
Function: One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Helps release RbfA from mature subunits. May play a role in the assembly of ribosomal proteins into the subunit. Circularly permuted GTPase that catalyz... |
F2I4T1 | MLLTDSETLSVLKEIMVLFPDAGPSLNFNSVYQLLIAVMLSAQSTDKKVNEVTPDLFKAFPTPKHLAKASPLDIEPFINKLGLYHSKARYLHAMGQQLIDKYSGQVPSQRKDLESLNGVGRKTASVVLSLGFDQPAFAVDTHISRIAKHHHFVDPNATVREVEKRITKVLPASEWKDAHHALIAFGRTICTARNPQCYRYPQLLPHQEKETKRND | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: DNA repair enzyme that has both DNA N-glycosylase activity and AP-lyase activity. The DNA N-glycosylase activity releases various damaged pyrimidines from DNA by cleaving the N-glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The AP-lyase activity cleaves the ph... |
A0A101SXA9 | MSSTSRRRTSHTPHHRTATLALAGVAALIAAAVQAGAASAAPAAAHRAGRIDPAHAALRLTPSQRAELLRHADAGRAATARSLGLGGKEKLVVRDVVKDADGTLHTRYERTYAGLPVLGGDLVVDTTGSGATRRVVRASNAVLDVARLTPAVPRADAGKQAVRRAEALGSTKSAEVSVRKVIWAATGRPVLAYESVVGGLQDDGTPNELHVVTDALTGKKLFEYQGVRTGIGNTQYSGQVTLTTTQSGSTYTLTDGARGGHKTYNLNHGTSGTGTLFSQSSDTWGNGTTSNAATAGADAHYGAQETWDFYKNTFGRSGIK... | Function: Extracellular zinc metalloprotease.
EC: 3.4.24.-
Subcellular Location: Secreted
Sequence Length: 678
Sequence Mass (Da): 70639
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A0A1F7G403 | MDILLHTCCGPCLTGSYPLLEAGVGAGKAALFWENPNIHPFIEYQQRLASFKTAADHFKLEVIYGDASYGLEKFLRALDNEFGPARCATCYRLRLEATARAAAKAGIAAFTTTLLISPYQNHELLIKTGQEAAAQNGVSFHYTDFRPGFRGSQATARELELYRQKYCGCVFSEHDRYKNDKKYLNPVGAAGV | Pathway: tRNA modification; tRNA-queuosine biosynthesis.
Function: Catalyzes the conversion of epoxyqueuosine (oQ) to queuosine (Q), which is a hypermodified base found in the wobble positions of tRNA(Asp), tRNA(Asn), tRNA(His) and tRNA(Tyr).
EC: 1.17.99.6
Catalytic Activity: AH2 + epoxyqueuosine(34) in tRNA = A + H2O ... |
A0A969FQC5 | MMMRGRADVLLLALALDWLVGEPPDTLHPVVWLGRLAAALEQRAPRGSPPRELLYGAGMAAACLGVAALPALLVTALPLPAPLCLLEATLLKTTFSWRTLHHAGERVRQPLVAGNLEEARAGLRGS | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
Subcellular Location: Cell membrane
Sequence Length: 126
Sequence Mass (Da): 13400
Location Topology: Multi-pass membrane protein
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A0A2G5IJ77 | MLQGSSWQQTSRQATCLGIDVVFVLPFTDLLANTTAEAFASKVIAERLRASVVVVGDNFRFGKGGRGDVDTLKRMGASNGFTVEAVGAVEYDGQTCSSTLVRNHLDIGDRASAEKLLGRPVTWRDACVTPTAAER | Pathway: Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step 1/1.
EC: 2.7.7.2
Catalytic Activity: ATP + FMN + H(+) = diphosphate + FAD
Sequence Length: 135
Sequence Mass (Da): 14451
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A0A2H1W7H0 | GVGLLPYTGHNSSLRAATEKFSKNRKKSSNTLPDTGIEPETSCPAVALAPTQPTRQSTYCLDAQVPDSACTATSYLTGVKTKYGVIGLDGNVTRGSCYSQLHEPNWSESIGQWALEQGLDVGLVTTTRVTHASPAGMYAHTSERNWESDADVPEECLAAGCRDIAYQLVTNSPGRHFKVIMGGGRREFLPNTTNILGSKGRRLDGVDLTDLWHVDKLNMNATHQFVTDRLELLKVFNSDDLPEYLLGLFRDDHMEYHLKAQNQPSLEEMVEVAIKMLSRSSKGYFLFVEGGRIDHAHHDSLAHLALDETVEYSKAVKKAR... | Cofactor: Binds 1 Mg(2+) ion.
EC: 3.1.3.1
Catalytic Activity: a phosphate monoester + H2O = an alcohol + phosphate
Sequence Length: 396
Sequence Mass (Da): 43285
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A0A671RCF5 | MRHQHLLSNYNSHDTRNRTTEANMAAVGRFLKNAWNKEPVITVSCGIGLLACLLPALSPLTKYTGMMNRAIPYNYPVPVRDDGNMPDVPAHPSDPQGKNLDWLKNL | Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
... |
A0A2T2SGM7 | MDDNALPQNGTLQSGSFSENGEGPANNEQIVVGVDIGTTKVCAVVASTDARDRVNILGVGMAESKGSNRGVVVNIDKTVDAVQEAVGEAERAAGISVESVIVGIAGDHVQSFQSRGVITISRRNGEITQDDVQRLLEDTMHVAMPADREILHVVPQEFIVDGQDGVADPVGMSGVRLEANVHIITGLVSAAKNVFRCIEKAGFEVADIVLEPLASSFAVLHDDEQEVGTALIDVGGGTTDVAVFEDNTIRHTAVIAVAGDKVTDDIRKGLGVMREHAERLKRRFGTSLIDYAGEDEMITIPGIGGRSEKSIGRSALAQII... | Function: Cell division protein that is involved in the assembly of the Z ring. May serve as a membrane anchor for the Z ring.
Subcellular Location: Cell membrane
Sequence Length: 451
Sequence Mass (Da): 47554
Location Topology: Peripheral membrane protein
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A0A1Y4BBF4 | MLSLDGWTLFFTVLNVIVLFVGLRLLLFKPVLKIISQREEMIKTQLKEAAAKEQQAEQLKNDYQEKLKDAGHKAEEIIAQAKSRAAREQSEAAVKAKEEAEKMLEKAREEIRTEQEQARKEVQADIAILAMEAARKIMKTGDVHDAAGK | 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: 149
Sequence Mass (Da): 16847
Location Topology: Single-pass membrane protein
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A0A366MH62 | MKSLLISGDRSGAGKTSITLGLAGLLAKDAVVQTYKVAMDYIDTSYLSGVTGRPSYNLDTFVQTDEELAGLFSYGAKGADIGIVEGVRGLYEGRDSFTDVGSTAAIAKRFSLTTILVVDARSITRSAAALVKGFQAFDPDVRIKGVILNNTGGGHHVTKATEAIEYYCGIPVLGAVPRSPEMDLSMRHLGLVPFVEGMRDPGFAKTIEGIIRHVGAHVDLEAVKAIAEDVTPEPNLVTESLASRPAASRRIAVAFDEAFTFYYGELEAVLRSQGCDVVRFSPLHDTLPEADGYIFGGGYPEMFAEELSKNVPMREAILAK... | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 10/10.
Function: Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source. In... |
A0A671MT42 | MSELSSKKQGFKKCRSATFSIDGFSFTIVANETGESSARPLARFARSKSQNALWNAITAGIGIKDKDKRGILIDPRSPEEILADDLPSVDSPDAMEKTAIRLRCLVKQLERGEASVVDLKKNLEYAASVLESVYIEETRRLVDTEDELSDIQSDSVPSEVRDWLASTFTRQMGLMLRRSEEKPRFRSIVHVVQAGIFVERMYRRTSNMVGLSYPPSVITALKHVDTWSFDVFTLNDASGDHALKFIFYELLTRYDIINRFKIPVSALVSFVEALEVGYSKHRNPYHNLIHAADVTQTVHYLVLKTGMVHWLTELEIFAML... | Cofactor: Binds 2 divalent metal cations per subunit. Site 1 may preferentially bind zinc ions, while site 2 has a preference for magnesium and/or manganese ions.
EC: 3.1.4.-
Catalytic Activity: 3',5'-cyclic AMP + H2O = AMP + H(+)
Sequence Length: 696
Sequence Mass (Da): 78808
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A0A6V7XAF6 | MFPDLEYCIPVESSSIHFLKLPDEFYQEILKRISASKSRIVFAALYLGAGQKEQQIVSRLQTACSENVELEISFLLDYFRGTRGEPNDSSTSILKPLLENRNVQVSLFHTPEMRGLLKFLLPGRLNEIIGVQHMKFFIFDDSIIISGANLSDQYFDNRQDRYLVVENCPRLADFFHSISTIMAKHSMQLDKFGKLNFSGSASIHPFTGSNEEIQKSIKTEIFELFDKCKDNVNNLANDTFIYPFLQMGVFDIKQEENIKEINLITAYFNLCDEYADWMLQKRSFLVNIVFGSPRTNGFYGGTGISGSVPLLYLQNSLDFI... | 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-... |
A0A2K6QAX3 | MFVSRNALIETAIFLFQISDDEPGYDLDLFCIPNHYAEDLERVFIPHGLIMDRTERLARDVMKEMGGHHIVALCVLKGGYKFFADLLDYIKALNRNSDRSIPMTVDFIRLKSYCNDQSTGDIKVIGGDDLSTLTGKNVLIVEDIIDTGKTMQTLLSLVRQYNPKMVKVASLLVKRTPRSVGYKPDFVGFEIPDKFVVGYALDYNEYFRDLNHVCVISETGKAKYKA | Pathway: Purine metabolism; IMP biosynthesis via salvage pathway; IMP from hypoxanthine: step 1/1.
Catalytic Activity: diphosphate + IMP = 5-phospho-alpha-D-ribose 1-diphosphate + hypoxanthine
EC: 2.4.2.8
Subcellular Location: Cytoplasm
Sequence Length: 226
Sequence Mass (Da): 25663
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A0A7S0X5K7 | DDVERAPLPSPRTGPDRPGRGSVHGKSPRITRQLVMWLAAARPKTLTAAVVPWLVGSALAAAGGGETQWLHSLAALLAYFFIQIGTNLVNDACDFDRGADTKERTGPIRVTQAGMFTSRTVHAAGVGCFLFAGVAMSPAIFHRGWPLALLLVSSCAAGYAYTGGPYPLGYHGLGDVTVVVFFGIVATGGIRYIHGGGDFLSVPIAVASVQVGL | Pathway: Quinol/quinone metabolism; menaquinone biosynthesis.
Subcellular Location: Membrane
Sequence Length: 213
Sequence Mass (Da): 22188
Location Topology: Multi-pass membrane protein
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A0A6V7W2R1 | MINNKKILFFVNNQIIKLINNNNLKFQYKYFSTTNLIKNEVKQNFKENSSLIDSFGRFHNYLRISIVEKCNLRCKYCMPEEGVKLTPSSDLLTKDEIIRLAKLFAFEGVNKIRLTGGEPTIRKDLVEIVSELSKIDGIQEIGITTNGIVLNRMIKPLIDAGLTNLNVSLDSLSAQKYAEITRRDGFQKVWRGLILSEQLMPKGKVKINCVVIRGINEKEVISLVEIGRELSFNIRFIEFMPFAGNNYEMKKFVPYREMLENIGKYYGVENIERLIDGPNETSKSYQVKGFVGKFGFISSMSEHFCGGCNRLRITADGNLK... | Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
EC: 4.1.99.22
Catalytic Activity: AH2 + GTP + S-adenosyl-L-methionine = (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate + 5'-deoxyadenosine + A + H(+) + L-methionine
Sequence Length: 323
Sequence Mass (Da): 36924
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A0A4Z2CUY0 | MLIRLWDWENNWTCAQVFEGHNHYVMSLAFNPKDNNTFASASLDHTVKVWNLGSGTPNFTLEGHDRGVNCVDYSTSGDKPYLASGSDDRTVKIWDYQTKACVQTLEGHAQNISSVLFHPELPIILTGSEDGTVRFWHANTYRLESTLNYGLERVWTMTCQRGKQIVGIGYDEGTIAISLGRDEPAMSMDASGKLVCARHAELVQANLRSLNFSGEGGEAIQDGERLPIAFKEMGTSDIYPQTIEHNANGRYVVVYGDGEYIVYTAMALRNKTFGQGLEFVWCQSDAGVYAVRESNAVIKVYKQMKEIRTFKLDYGAEQIF... | Function: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membra... |
H3CI64 | ALDPGGCLQVSETGKESLPGWLHWNASSGTLLGVPLEEDRGVHHISVSTYSDATSSSSEVFSIEVHPEDVLEPDSSLRASADAQTFLCEGEEPVTVLTVIMDADLNKMSSGQRVALLDNMRKFSGVDLQHMKMLPVVNNRLFDMSAFMAGPGNAKKVVENGVLLSWKLGCSLDQTTVPDISSIQGPAKAGTMSAKLGYPVVGWHVANKKQHLPKRVRRQLSNTPTPVLVVPPPTTVVEPPVRIVPTLSSPSAAAPTETSAPPVRGPVPLPGKPTSRFREPVAHTPTLAPPQPTRVAETTSTLPIQPTMTRPTYVEATATP... | Function: The dystroglycan complex is involved in a number of processes including laminin and basement membrane assembly, sarcolemmal stability, cell survival, peripheral nerve myelination, nodal structure, cell migration, and epithelial polarization.
Subcellular Location: Cell membrane
Sequence Length: 774
Sequence Ma... |
A0A6N4R9C1 | MSSGTQSQTTNKLKAPKPAAKVVAPARPSSLLEDYPKLNGLTPAQYIKLQTLCGPRWIDLLFHLPTKMLDRSATPTIAAAPVGETVTLIVQVTRRQPLPPRHIKRPMTIDVTDGSAPLRVMYFNPGYWLERAYPVGETVILSGKIEVDNKGRKLIHPDVWSLPKSEDTASNKINHVARIWPLYPLTAGLGQGWLSRAILTALEVAEDCPLPEWLPASLREQHNLPTFTDALKAAHNPQTEADLQPNSPARTRLALDELYATQLALQHARAANRGQRGIAHGKSDTLTQRLLQSLPFPLTGDQQNALTEIRADLSAPRPML... | Function: Critical role in recombination and DNA repair. Helps process Holliday junction intermediates to mature products by catalyzing branch migration. Has a DNA unwinding activity characteristic of a DNA helicase with a 3'- to 5'- polarity. Unwinds branched duplex DNA (Y-DNA).
Catalytic Activity: ATP + H2O = ADP + H... |
A0A931FBA7 | MADKEILVITGETSGDMHAAKVVARIKELTSGVKFSGLGGRELDYLKLENLLPSEEIKTGSHGFASGITGLFSHIKLAHKITDLVADRDIAVCFLVDYSGFNMYLGRRLRKKLDLPVIHYFPPTAWIWGRWRAKWLASAGVKVAATFPKEADVYREAGAEVKYVGHPLLDEIPESRDQADAREELAELIKLAGRRELQLGERLLAIMPGSRPKEVETHLGPMLAAADQLAHDFALRPVIPVARGIDIEQVEEKIENHRINPVLLSGYSRELLAAADLALVVSGTAVLEAALLGTPQLLIYRADKLTAFLGKYLIGPEYIG... | Function: Condensation of UDP-2,3-diacylglucosamine and 2,3-diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
EC: 2.4.1.182
Catalytic Activity: a lipid X + a UDP-2-N,3-O-bis[(3R)-3-hydrox... |
A0A0G1WQ52 | MALSEKEVIRTAELARITISEDEKKRFGDELTAILDFVRELNEVDTEGVSPMTGGTREENALRPDEPLSDALEGAGADLLNAAPGKKNRYISVPAIFE | Function: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an ... |
A0A1W9VM55 | MEDFKDKNVTIMGLGLHGGGLATAKFFLAEGANITITDLRTKEILKQTIEQLKGEKINYTLGEHIDSDFTNADIVIKNPGVPKTSKYLKLAKRVESDISIFLQRVNTPIIAITGSKGKSSTVSAIYHVLKKFNPKTRLGGNITVSPLTFINDVDETTPVILELSSWQLADLNGKGCLKPKIAAVTNIMNDHQNAYNSLDEYAEDKAVIFQGVTDYAILNYNDKYRDFFKSRLNIKPLYYSNTEEPSHINGIYLDSANQGWSNIEGKRELLLDPQLTLKGEHQRENLLLAALILSLYGVDKKSIRTGLQEFKGIAHRMELF... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).
Catalytic Activity: ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-... |
H3CZE8 | MAKGKFFYAVKKGLQPGVYTTWDECKSQVDKFPSASFKKFASEREAWAFVRGAEPSAPPGTNKAVESGVGLLPKRGPEALEYIPLGKKRSHSGEDEEEAQAKKVKHSGTSSSESTDGFTYMGDAVVVYTDGCCSANGKVGARAGIGVYWGLNHPLNVAERLPGRQTNQRAEIQAACRALELAKEQNIKKLVLYTDSKFTINGVTCWVKNWKLNNWRLKSGGSVTNKEDFEKLERLNAGLDVVWMHVPGHAGYHGNEQADRLSREGAAKPEVQQGNG | Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
EC: 3.1.26.4
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Length: 276
Sequence Mass (Da): 30178
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A0A1V5W8R4 | MKFTVKIAVFSLFISACSDKQDRINTNIHHSQITITYLPPVQKKNKLLPFEVLLVNHGFVNMQHIDSSIQCDLRYSTTHNFVGIDMYGDFNACYVPRDIALRLHRVQKQLQAIDSLYSLVILDAVRPLHIQQIMWDSCSYSGRQKKNFLAPPSQTSLHNYGAAVDVTLAYNGSEVDMGTAFDYAGEAAYTYIEQELLTYNKITREQLYNRTLLRSVMKQQGFIENKYEWWHFGACYRSQVAKKYPLVLSFDSIVPNHQF | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes hydrolysis of the D-alanyl-D-alanine dipeptide.
EC: 3.4.13.22
Catalytic Activity: D-alanyl-D-alanine + H2O = 2 D-alanine
Sequence Length: 259
Sequence Mass (Da): 29923
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A0A1V5W610 | MNLTSLYAIIVAGGKGMRMQNDIPKQFLILSGKPVLQHSLEAFYRYNNSIQCIVVLPKDQISYWQQLCVDYNCMVPHTIAEGGSERFFSVLHGLQYITSHGFVAIHDGVRPLVSNEIIAQGFAYAQQYLAAIPVIDSVDSLRYVEKNTTYVVNREPIKRVQTPQVFETKTLLHAYTLGYDLHCTDDAAVWEKAGNTVFCYKGDEKNIKITTPLDLCTAELLINM | Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 2/6.
Function: Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
EC: 2.7.7.60
Catalytic Ac... |
A0A9D8PNC3 | MEIVMPDIQLLALAPEIILIIVAFLMLFFGPLVGGPNTKGGPKVGGIVSLVALTGAFLINLYIGQDEIVTLGGMIVKDAFSLYFNALVIIAAAFSIIISFGYINRFGIKEGEFYLLILFSTVGMMLMGSSADLLSIFIALELMSIPIYVLVGFRKENLRAREASFKYFILGAISSGIFVYGAALVYGSLGTTNLTAMAEALGSNISPVFLLGSAFIISGFLFKISAVPFHMWTPDVYEGANLPITAYMSVGVKAAAFSAFLRFAVVDLANTGDSWVLAIGFVAVATMSLGNTAALAQKNLKRLLAYSSIAHVGYILVALV... | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ... |
Q4RQD8 | MERFALKQSQLCGSWEMKERLGMGGFGHVYLYQHLESGEKMAVKLCRLELNSKNRERWSREIQIMKKLKHTNVVQAREVPEELTSISINDLPLLAMEYCSRGDLRKVPSGYFIIENHVVVFSEVASLSFVYSFFQILNKPENCCGLKESEVLSLLSDIGSGVQYLHDNKIIHRDIKPENIVLQENDGKLVHKLIDLGYAKDLDQGSLCTSFVGTLQYLVVRETKTQLPLTALRKVWGEAVSYICGLKEDYIRLYSGQRAAILSLLRYNTNLTRYKNLLFSCSQQLRAKLAFFKTSIQQDLEQYSKQSQSGISSEKLLRTW... | Catalytic Activity: ATP + L-seryl-[I-kappa-B protein] = ADP + H(+) + O-phospho-L-seryl-[I-kappa-B protein]
EC: 2.7.11.10
Subcellular Location: Cytoplasm
Sequence Length: 494
Sequence Mass (Da): 56797
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E1QZZ5 | MEELKDIREEIDRIDDGIIDLFMRRMDCAEHVASYKAAHHMPVLDKSRERDLLAKVAERVPHEMRSYIEVLFQLLMEASRNRQDRRLGRQSATADDIERALGAAPELFPARAFVACQGVEGAYQQMAADRIFRHANLAYFDTFDAVFRAVEEGFCRYGVLPIENSTAGSVNQVFDLMMRHNFHIVRTCRLKIDHNLLAKPGTGLEGIHHVYSHEQAINQCGEFISSLRGVQVHACENTAMASRMVAESERSDVAALASRTCAELYGLDVLARSVQDQGNNYTRFACIARDLAIYPGADRSTFMLVVSHEPGALYKILAKF... | Pathway: Amino-acid biosynthesis; L-phenylalanine biosynthesis; phenylpyruvate from prephenate: step 1/1.
Function: Catalyzes the Claisen rearrangement of chorismate to prephenate and the decarboxylation/dehydration of prephenate to phenylpyruvate.
Catalytic Activity: H(+) + prephenate = 3-phenylpyruvate + CO2 + H2O
EC... |
A0A9D8KDX0 | MSVINVAIAGNPNSGKTTIFNALTGSRHMVGNYPGITVEKKEGKIKIEGREVNFIDLPGTYSLTAYSLEELVARNFIVEEKPDMVVDIIDSSNLERSLYLAVQLMEMNVPLILAFNMTDLAELRGIEINVEELSGLLGIPIVKTIGNKKTGLDQLKRTIVMVAEGKIESTPSKIYYEDRVEEEIARLAEIIEKSSLSESGFSPQWLAVKLLEHDTEVEKRLSEDEKWEEIETALEGSRENLLKVLKEDSVNLIAEGRYGFIKGTMKKAVRHIREDHIIVSDKIDKVLLNNLLGIPIFVGVMYIVFQGVFKWAGPFMDLID... | Function: Probable transporter of a GTP-driven Fe(2+) uptake system.
Subcellular Location: Cell inner membrane
Sequence Length: 794
Sequence Mass (Da): 87940
Location Topology: Multi-pass membrane protein
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A0A0K8MED0 | MRFGALLYRYFFRHSSKNAKLLFVMLFFVTSVFLAVVVDYFFPVDTSRFQDISIVVAAEDKPLAHVFQTKDEKWRLGTSLKDVDSCFIKQILYREDRYFWLHNGINPFSLLRATSQWLINGKVISGGSTLTMQVARLLEPRPRTLSSKFIEIFRSFQLEWHFPKSQLLQMYLTLAPYGGNIEGIQAASWRYFGKSAQHLSPSEAALLIALPQAPRRYYHHSFTLSALQARNRILVQLHEAGFFDKATLMAAQDEPLPGQRFALPRYLPHLAYRLKRLLPQQKKIETTVQISLQNKIQHLASQALNIYPSGVNIAVLVVHH... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
EC: 2.4.1.129
Catalytic Activity: [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate = [... |
A0A1V5W9B3 | MTRYKLAIEYDGSQYKGWQILHNEPTIQGKLIEICSKICKTNTIEVYGAGRTDAGVHALGQVAHVDADTNIPPNEFHNQLQAFLPSNISVRAVEIAHNRFHARHHATYRSYLYCITKERTALFKRYVWWIKNSLNVEQMNIAAQEFKGFHNFKSFGKSSKNEESTMVEISHIHIYEVQNCIWIHIVGSHFLWSMVRRMVGTLAEVGKGTLQPNDIKTFLQESSNFPARHTAPPSGLFLEQVYYSKHIDIQKPQFPFII | 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: 258
Sequence Mass (Da): 29735
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A0A5C7EZ96 | MHITFIGGGNMATALIGGLLAKDWSASQIRVVEVDAAARERLTGRFGVATTEAPEVDGSDTVLLAVKPQQMHEVARRLAGRLGSQLVLTIAAGIRLDDLARWLGGYQRLVRCMPNTPALVHCGVTGLYALPQVSREERQRAEAILGAVGRTVWLDREELLDAVTAVSGSGPAYVFYFMEALEEAASSLGLSREQARLLVVETFLGAASLARQSEEPLAALRARVTSKGGTTERAVAVLEEARLRDHIAQAVRAAHARSRELGDEFGKLG | 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... |
A0A4S4BPT7 | MLWMVTGGVGCGKSVYAERWAASLAREAILLSCPTWPNEREDLVGGRPDESALMEEERVVWMRWKADEKLSDRIDQINLKSNPFRADNRVIVLDSLSGWLRRAVREVRQMTLPPAPAEPPRRGRPKRIPETEDLFALRTDRAGKEFRRVVDALLRYHGRSIVVTEQPAPGLADDPWERWYARELAEANRRLAERSAELRMLVSGVAVEIRGPRMKRGNGNDEDLYSNRR | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 5/7.
Function: Catalyzes ATP-dependent phosphorylation of adenosylcobinamide and addition of GMP to adenosylcobinamide phosphate.
EC: 2.7.1.156
Catalytic Activity: adenosylcob(III)inamide + ATP = aden... |
A0A381H8C3 | MIYSLATGGTVSIAALFIAGILPGLLLSFTLMVMCVGFAHKARYPKGERVPFRQALKIFVDTLWGLMTVVIIMGGILSGIFTRDGIGGDRLSVGLLRHYVYLPRLQMV | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 108
Sequence Mass (Da): 11773
Location Topology: Multi-pass membrane protein
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A0A4S4NN58 | MSRPLFIVIEGLDGSGKTTQLEMLRDYLQSRGESCRLTAEPTDLPTGRLIRSILQKEISVDPRTLAALFAADRVEHIFHPESGILDLLAAGHHVIASRYYFSSLAYQSEFVDPGWIAALNRQAKTALPADLTIFLDLEPTESMQRIAGRNGEDELYETLEKLTHVRESFLAAFSVFGEGENIQYVDAGQPVVAVADAIIEHVEALR | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
EC: 2.7.4.9
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Length: 206
Sequence Mass (Da): 22842
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A0A2H6HXQ1 | MNGKNGQTDGNGINGSNGHGIGGGNGHGGSRRALITGVTGQDGSYLAELLLAKDYEVHGLIRRSSTFSTGRIDHIYDDPHRAQVNLKLHYGDLTDSTGLRRIIEEIEPHEVYNLAAQSHVRVSFDQPEYTADVVATGTLRLLEAIRDYMAISNNRPRVYQACSSEMFGSSIPPQNEMTSFHPRSPYAVSKVASYHYAVNYREAYDLFVSNGILFNHESPRRGGTFVTRKITRALTRIKLGLQEKLFLGNLDAKRDWGFAGDYVEAMWRMLQHDRPDDFVVATGETHSVHEFLESAAGVLDMDWRAIVEFDSRYLRPSEVD... | Function: Catalyzes the conversion of GDP-D-mannose to GDP-4-dehydro-6-deoxy-D-mannose.
EC: 4.2.1.47
Catalytic Activity: GDP-alpha-D-mannose = GDP-4-dehydro-alpha-D-rhamnose + H2O
Sequence Length: 377
Sequence Mass (Da): 42265
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A0A2H1X0S9 | TDIKFFFKILALCHSVQVSNEDMKKLSARLSVTGNMQLMNFFKRKKIKTNNTNGSVVDNVTWNSIINENGNKIDYQASSPDEKALVEVAERFDITFLGEEGNDLVLKVGEHTEMYERLQIIEFTSERKRMSVILRDRDGKIWLYCKGAESSVFPLCTNYSCVQETDRDINIFANKGLRTLAIAYREVPEEEYEKVAEAIKRLDGKSAEALQQVTQQYRTLERNLTLLGATGVEDCLQDNVADTLASLRAAGVKTWVLTGDKVETAINVAQSCAHISENDRRMFMIGIEDSTTLQAHIGECSRIINEPSYRDLTLVVDGTS... | Catalytic Activity: ATP + H2O + phospholipidSide 1 = ADP + phosphate + phospholipidSide 2.
EC: 7.6.2.1
Subcellular Location: Membrane
Sequence Length: 504
Sequence Mass (Da): 56835
Location Topology: Multi-pass membrane protein
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A0A932QW80 | MNVADSELIRSILIAKGHQMTSSANDAEVVLMNTCAIRENAHRKIYGRLDILRPLKKQREAEHRPFVVGVLGCMAQNLKEELLMHPVANLVVGPDNYRALPNLIDRIVQTNHHEVEASLSEYETYSDIAPTRIEGVNAWVTIMRGCDNFCAFCVVPYTRGRERSRSIPSILNELEQLVAAGYPQVTLLGQNVNSYCHEGETFADLIVKAAQIPGLKRIRFTSPHPKDFSEKLLYAIAEYPNICNHIHLPLQSGSDRILNLMNRTYTSAEYLGLVKTIRRVIPTTTLTTDMIVGFPTETEKDFQETVQLMDAVQFDNAFIF... | 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 N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that re... |
F9ZAF5 | MADTSNKKNIREESLRDLSDFLTAQGEKAFRAKQIWQWIWQRGVTDFAEMSNLSKATRELLSRHYFFDSLFPQQVQTASDGTEKTAWRLTDGEIVESVLIPGNQKFTVCVSSQVGCQLGCKFCATGTLGFKRNLTAGEIFEQVVRAQQAAEAQGQPLSNIVFMGMGEPLLNYEQVLRAIERITAQDGLAMSPYRITVSTAGIPEKIRQLADDGVRFNLALSLHAAKETTRTFLMPVNKAYPLSEIAGSLKYFVEKTGTRPTFEYLLLKDINDSLEDAKALALYCRQFPIKINIIEYNNVEGSGFHHSPDKNRDAFIRFLE... | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs.
EC: 2.1.1.192
Catalytic Activity: adenosine(2503) in 23S rRNA + 2 reduced [2Fe-2S]-... |
A0PZR1 | MSKVKVARFASQVMIITILSKLMGFWRDALIAKEFGTTYETSAYMMSLNVSSILFGLMGLAITTTFIPMLTRSLREKGKDDMYEFGNTVINIIIILTTIIGVLGWKFAPQIVKIVACGYTGEIYDLTVQLTRLSVINVVFIGLTSGYTAILQTMDNFAAPSLVGVAMNICIIIYLLFTKNTTIEGLTIATIIGNGSQILVQIPWLIKNKYKYSCKINFKDPRLKEMMTLILPVLIGIGINQINTLVDNNVASNLNEAAVSVIQYANRLNSLVYGIFATSIITVIYPTLAKYINAGEIKEDFKKYLSKAINNINLIMFPAT... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Involved in peptidoglycan biosynthesis. Transports lipid-linked peptidoglycan precursors from the inner to the outer leaflet of the cytoplasmic membrane.
Subcellular Location: Cell membrane
Sequence Length: 515
Sequence Mass (Da): 56524
Location Topol... |
A0A4R1HAJ2 | MSIRAVSFLALALLLATACQPQPEVVYRQQLFAFGTLIDITTQGVDAAQSRAAVQAVDAMYQQQHRDWHAWQRGALDDLNNAIAAGKSWQTDSSIVKLIRMGQNFERLSGGLFNPAIGELLALWGFQQDEPEGPPPSPQRINAWLSHKPSSLQLTIDGNIVSSQNPHVRLDFGGFAKGYSVGKAVELLEGRGIHNLIINAGGDLCLRGNRGGNKPWRIGIRHPRNTGTLATLELQGAACVFTSGDYERYYIYQGRRYHHILDPRSGYPATATRSVTVIADDPALADAAATALLIAGAEHWQSVAVNMGVTDVLRIDDQDV... | Cofactor: Magnesium. Can also use manganese.
Function: Flavin transferase that catalyzes the transfer of the FMN moiety of FAD and its covalent binding to the hydroxyl group of a threonine residue in a target flavoprotein.
EC: 2.7.1.180
Catalytic Activity: FAD + L-threonyl-[protein] = AMP + FMN-L-threonyl-[protein] + H... |
A0A1H4CIQ7 | MPKGFSLQELAEYTDSDIRGDAQLRLYSVASIEKAVSGDLSYIRDAKYRHYLQTSEASALILPTDMAQTYQGNCLVNPNPYLAYAKAVTLLYPAVRPAVLIHPSVVIGDGVELGADVVIEAGCVIGDGCVIGDGSWLHANVTLYADTYIGKRCIIHSGAVLGADGFGFAPDQKTWFKIPQVGNVVVGDDVEIGANTTIDRAAMGSTVIGNGVKLDNLIQIGHNTQIGDYTAMAACTAVAGSVQIGRYCQIAGMCAIAGHLSITDHVVVTGTSMVSHSITKPGVYSSGTTIEENAVWRKNAVRFNQLDKLARRLQELEKQL... | Pathway: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
Function: Catalyzes the N-acylation of UDP-3-O-acylglucosamine using 3-hydroxyacyl-ACP as the acyl donor. Is involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.... |
L2GW45 | MSSTVYASFVNSILSTLYPILTIYSYYVLVGKYCIDAKRFDSVVVLIMFLIYHVLLIYTLIFYMRILAIDDTSTANRFPSKVANKQAITSRYFNPFIEEEIIQKRLKMLKTCNICVTYKPPRTHHCSICQKCFLRFDHHCGLLGVCIAFHNYKFFYLFVIMNIIYCLFLIILLMFELIKNRQLPTASFSHFIVLTSLLFVEMCVSLQMFIYHTILIRKNETMIENKALNAFLRGDQGVRFVYQEGPLVNEEEVLERDEMNPYNMGVYENWEQIFGKNTWEWFLPTFTTLGDGINFPKKIGRD | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 302
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 35573
Location Topology: Multi-pass membrane protein
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A0A6V7V4Z8 | MDEKHQQQSPIIMDNLINNNGENSSSKISSPLLDTGQSEDPSICPYCNKKFRKPRVLDCLHSMCEDCIIAQLDDGRNNQQRNSKNILNSFMELELEDSVAGRRPTPPGVICCSVCNQETHIGNDPMFVNLMLLDFVKIREYGFNDANDTGRICEACKSEEKAVANCIHCCSDLCPKCVQVHRDMKMFDGHKVVMFSEKDKLSNQQEGLLKEGGMETIKLALCNKHKGDFELICPSCDELLCKQCAFEHVEHNVSPLNDLVFKWYKQSIHDLAKQAENKGRTTLDARSAIPDRKFLLQQSYHKCRDKIEDAFQFYARVIDE... | 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: 983
Sequence Mass (Da): 110621
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A0A9D8KFE6 | MSEILKFKSPAKVNYFLKVGEKLPNGYHKIATVMSAIDIYDHITVAFEGSRIEIESDNTKVPQGPSNTVYRAIEALLKEANVDIGIKVNIQKNIPLESGLGGASSNAASVMLKLNDHLNLGLGLDELLTLGVKIGSDVPFFIFGSPALVTGIGENLKKIEGIPETWMVVVKPPGSVSTKLAYKMIDLVLTFNKKSIIIPKFNGTLGGLIEGMVNDFETVVGVEPIVNDKRNDRDRDGGGYSVYLPEVGRIKREIERLGSLKAMLTGSGSSVFGVFGNRIEAKRAFEEIRSKNDWTVFLAQNLFY | 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... |
A0A951BRS6 | MTGSTSRSTRRAPSACSTASWKRRERTGAEASVSGLGPALESVALDVPEAAVPAYEAALRTACGSVGLFRDEASGTWRLEGVKPAGAGEAALAAGLALAAAATGVDARARRGPIAAEGWLARSMAGFPEQTVGRFAIRGSHLPDRPRAGRITLRLDAGVAFGSGEHGSTRGCLLALERVARRRPGRTRVWRILDLGTGSGVLALAAARLLRRPVLAVDVEPWSVRTAAANAGRNGLRPRIRCRLGDGWRDRAVRAGQPYDLVFANILARPLCAMARDLAAGLAPGGRAILAGLLVSQARQVLAAHRRQGLVLEWMVNEGG... | Function: Methylates ribosomal protein L11.
Catalytic Activity: L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
EC: 2.1.1.-
Subcellular Location: Cytoplasm
Sequence Length: 335
Sequence Mass (Da): 35275
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A0A671Q3P0 | KKHLLLSILKTVVVIKNLLQFEDMIKCTVPDSSPLLDFADYGCFCGLGGTGTPVDQLDQLVSFVIFSENVYIIYIYITLFVLNHFVLIIFFL | Cofactor: Binds 1 Ca(2+) ion per subunit.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+)
EC: 3.1.1.4
Subcellular Location: Secreted
Sequence Length: 92
Sequence Mass (Da): 10435
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A0A0N1CTT3 | MIEMKDIMKKYSNGTTAIRNLSISIDQGEFVYVVGPSGAGKSTFIKLMYREEKATKGVLNVAGYDLVGMKSREIPLMRREIGVVFQDYKLLPRKTVFENVAYAMQVIGRKPRDVKKRVMEVLDLVGLKHKVRVFPSELSGGEQQRVSIARAIVNTPKVLIADEPTGNLDPENSWEIMKLLDRINAQGTTVVMATHNSTIVNTIRHRVIAIENGRIIRDQAEGEYGYDD | Function: Part of the ABC transporter FtsEX involved in cellular division.
Subcellular Location: Cell membrane
Sequence Length: 228
Sequence Mass (Da): 25641
Location Topology: Peripheral membrane protein
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A0A1Y1RZY8 | MSAIPPERLVFHSLHAAVDWILKHPNAREDLQKAIDKGALSLRQGKLTAFPTETVYGLGADALNRDAVKLIFKAKQRPFYDPLIVHISELQQLDTLVLEFPEKARRLAEAFWPGPLTLVLKKDSRVPDIVTAGHPTVAIRMPSNPWARELIHRAGTPVAAPSANLFGRTSPTTAAHVAEQLSGSYEVLIDAGACRVGLESTVLSLAGERPLLLRSGGVSREQIEEIIGPVEVPAKTRAGDAESPGMLPNHYAPVTPLLMVEDVRDYAENRDIGCILFEKPDIDFQGPTVQVSGNRNADEIAVNIYAALRSLDGKGLRLIV... | Function: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine.
Catalytic Activity: ATP + hydrogencarbonate + L-threonine = diphosphate + H2O + L-threonylcarbamoyladenylate
EC: 2.7.7.87
Subcellular Location: Cytoplasm
Sequence Len... |
A0A109ULC2 | MQRNQLADAGIGLGETLGQVVALHGPTGNADQGRRLVLNELRLRALDLHDDPALEVLDLRGCGRQHYLHLQLDRLPHLREIYLPCLAEGAILHLFNLDVPASLTVHGRVREIDADWQKGTLRLTHRQRSWEGVQLLGHDAKPDDLVDPPLAFPLNVVLSSELLQAATMDGALCLSGQGEWMDGFQPLRMGQRLWIVPSWHQPPDPDAVNLHLDPGLAFGTGTHPTTALCLEWLDGLSLTGELDERAVLDIGCGSGILAIAALKLGAGQAIGTDIDPQALQASRDNAARNAIADEDLRLCYPEELAESGTATTFPVVIANI... | Function: Methylates ribosomal protein L11.
Catalytic Activity: L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
EC: 2.1.1.-
Subcellular Location: Cytoplasm
Sequence Length: 384
Sequence Mass (Da): 41441
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A0A1F3EPK3 | MAHSDGDVLLHALCDAMLGAAKMGDIGRHFPDTSSDYKNIDSKILLAQTNELIAAKNYRVGNLDVTVAAQQPKLKPFIPEMEETIARILGIDVDAVSIKATTTEQLGFEGREEGISVHAVVLLETLS | Cofactor: Binds 1 divalent metal cation per subunit.
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 4/6.
Function: Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP... |
F9ZC24 | MIQETIKNFLQQHHISRDAGFILAVSGGADSICMLHAFKYLNLKMLVLHCNFSLRGKESDMDEQFVKRFCDSYGIAHSVKKFDTLKYARENGLSVEMAARELRYTWFREMKEKKKMDYIVVAHHADDVAETVLINLCRGTGIKGLTGIKSINGDILRPLLPCSRTDILKYIEDHQLGFRTDSTNNSLDYVRNKIRHQIIPVLKEINPSFLDTMTENCETLKETEEIFQYGIHRFQEEILDCEEDELLIHISKTLATPAPYTFLYETLKPFGFNKVQIRDILNTHTAIPGKQFIAGHHTLERGRIFWRLYDNSKCSRTIVS... | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34)... |
A0A0C1S0S2 | MNIKIFSGNSVIKLSKNISKHLHTNLGDASVGKFSDGEINVQINESVRGKDVFIIQSTCYPANDHLMELILMIDALYRASSKRITAVIPYFGYARQDRRVGSSKTPITAKIVANILSCVGTSKILTVDLHTDQIQGFFDIPIENISGNDVILKDIESKKLYDPIIVSPDIGGIFRARMVSKLLNNMEIAIIDKIRSRANVSEMVHIIGNVKNRDCIIIDDIVDTGSTLCQAAEILKKNGAYKIFIYVTHPVFSGNSLKNITKSSIDEMVVCDTIPVSEKINGLGKIRSLTLSFMLAESIKKINNEASYCSIKTFNK | Cofactor: Binds 2 Mg(2+) ions per subunit.
Pathway: Metabolic intermediate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate from D-ribose 5-phosphate (route I): step 1/1.
Function: Involved in the biosynthesis of the central metabolite phospho-alpha-D-ribosyl-1-p... |
A0A101ST62 | MSELAVRAEKLDGADELAPLKSRFVLDGAVYLDGNSLGALPAHVPGRVEDVVRRQWGELRIRSWEESGWWTAPERIGDRIAPLVGAAPGQIVVGDSTSVNVFKALVAAVRMADEGRDEILVDATTFPTDGYIAASAARLTGRTLRAVTPAEVPAALGARTAAVLLNHVDYRTGRLHDLPALTAAVHAAGALAVWDLCHSAGALPVGLDEHGVDLAVGCTYKYLNGGPGAPAYLYVRSDLQDRFDSPLPGWNSHADPFGMDPSYAPAPGAPRGRVGTPDILSMLALEAALEVWDGVSVEAVRRKSLALTDFFLECVTACTE... | 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.
EC: 3.7.1.3
Catalytic Activity... |
D8IGA2 | MNDTSIIVLVQQTLWTFMLLSAPVLGVSIIVGLIISIIQATTSIQEQTLTFVPKMIAMLAVIYFLASWMINYISGFTVRLFNILPTIAR | Function: Role in flagellar biosynthesis.
Subcellular Location: Cell membrane
Sequence Length: 89
Sequence Mass (Da): 9920
Location Topology: Multi-pass membrane protein
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A0A317PNI2 | MSTLLLALGLIFVLMALRVPVAVSIGLAAMTATAAELGWRVFPVSAQVMVDGISSFVLIAAPFFMLAGEIMNRGGLTQRIFRLANALVGSLPGGLGQVNVMASMLFAGMTGSAISDAVGLGTMEIRAMKERGYDARLSASITAASSIIGPMIPPSVPIVIYGALAGVSIGSLFLAGLVPGILMGVALMLAILVYDRLGLCPREPRAPGSELRAAALAAVPSLALPVLVVGGIYSGLFTPTEAAVVSSAYAAVLALIYGELRIADFKQIITGVASATGALFLIVATTALLGWIVTRSGVMIEVALWLGGAVDSQTQLLLIV... | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 432
Sequence Mass (Da): 44676
Location Topology: Multi-pass membrane protein
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A0A2X2WNH6 | MVSFRKEMLSNISDLLKHQDAIKFMTEEKKGKVCVFGSFNVDIVSYVARLPHPGETIVSQSCSFGPGGKGANQAIAASNAMCKVDFITKVGNDQLSSHAYSHLEASNIDSLTIYVSDSAPTGNALIYVSELDGENMIAINQGANVTIIDEEIINSHKNILNSNILLVQLENNLSATINAIKYARENDVTVILNPAPFTSDAKIMLPFVDIVTPNQTEATLLSGINITDIETAKKAAERIAQMGPQCVIVTLGNKGALLYDKGQFYMIPAYPAMVVDTTGAGDAFNGALAASLSKGETIKHACHYAAAFSSLAVELNGASN... | Cofactor: Requires a divalent cation, most likely magnesium in vivo, as an electrophilic catalyst to aid phosphoryl group transfer. It is the chelate of the metal and the nucleotide that is the actual substrate.
Pathway: Carbohydrate metabolism; D-ribose degradation; D-ribose 5-phosphate from beta-D-ribopyranose: step ... |
A0A0X8HCA8 | MTRRLLIRATGAARPGQLAGLGQAMARSGARLLDINQSVTFGMVSLEALVGLDRESDLESALSAAGDTLGLEIQAIQVSAEDYQRWSVQASEPRLILTLLAPHLPAGILAEVGALTAEHGLTVELIHRLSGREPLDGGVPRDHHTQGACVECWLRGEEVDLDALREKALALGAMHGVDIAIQEDSIWRRHRRLVCFDMDSTLIKAEVIDELARRHGVYDEVAEITERAMRGELDFQQSFRERMAKLKGLDETVLAEIADTLPMMDGVERLMYHLKRLGYRTVILSGGFTYFARHLQEKLGFDEVHANELLIENGKVTGEV... | Pathway: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 3/3.
EC: 3.1.3.3
Catalytic Activity: H2O + O-phospho-D-serine = D-serine + phosphate
Sequence Length: 408
Sequence Mass (Da): 45026
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A3DVI8 | WXAGMIGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTIEAGVGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGISSILGAINFITTAINMKPPTLSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPV | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
A0A6N4R9U3 | MKFSTGTLVVVGVIVLGLITAVTGGIGVYMAQRGPLEQPVKVIVDQGMGVRAIASRLGQANVIAHPDAFVVMVKATGMAGTLKAGEYAFEPGISLRAVVNKLALGDTENRSVTIPEGWTVKQAIDRLEAVEGLTGHAVRPEEGRIFPDTYAFRFGAERAKVLDTMTARMDKELANAWAARDTTLPLKSPEELLILASIVQKEAANDDEMPMIAAVFYNRLSKGMRLQSDPTVMYGAELEGDRLKRKDLTEPHPFNTYLFAGLPPTPISNPGKSALMAVARPARTEAIFFVADPSLTMHVFSVTYDEHRRNVARYWKDVKK... | Function: Functions as a peptidoglycan terminase that cleaves nascent peptidoglycan strands endolytically to terminate their elongation.
EC: 4.2.2.-
Subcellular Location: Cell inner membrane
Sequence Length: 349
Sequence Mass (Da): 37834
Location Topology: Single-pass membrane protein
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D8IDD5 | MKKVNVCLLGASGAVGKEMLKILQERKFPVNELRLLGNKTAGQKVIFNNKEYTIEKPTKDSFKDMDITLVAVGSDESKKLSPLAAKAGSVVIDNSSAFRMDKNVPLVVPEVNPEDVKLHKGIIANPNCSTIIALVALAPLHKFAKIKRVIASTYQAVSGAGKEGMEELQQQVYDYAEQKKLNIKAFKYQILFNLIPQIDAFDSKTGYTKEELKMTNEGRKILHAPDLQVSCTCVRVPVLRSHSESITIETEKKLTAKKAKELLSKAKGVKVVDNPSQFKYPMPLDTTDQDNIFVGRIREDISAKNSLTFWCAGDQIRKGA... | Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 2/4.
Function: Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate.
EC: 1.2.1.11
Catalytic Activity: L-aspartate... |
A0A1W9VIL2 | MVLLLAPLLLYLLLKSGKVKLALGYFTQKDLDYAKKCKKDKVLKKKESKRLRKERNVFQNIWFELLDPLFWAIIWVLILNNFIAQLYVIPSSSMVPTFLEKDRVVASKLFSGPGIPLTNYQVPEVSNPKPGDIVTFNNPKVDDSTSDIHYKNVFTRIFQPFVYMLTLTKLDIDADVNGNPKVRQLVKRVIGVPGDKLCMVNDKVYKKVDGGEWFLMSDIPGQKEWGQNALFSLTNKNSMMEIKISFCFGY | 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: 250
Sequence Mass (Da): 28696
Location Topology: Single-pass type II membrane protein
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A0A8H2QYN3 | MKTIGVLFGGKSVEHEVSVITGVQVMENLSKDYCVVPIYVKKDGQWLGGESLKDFKSFKNQDFSQAYPVYFKAGIPSLFHLQRQKGGLLKGDQLVEEERKIDCIINALHGTNGEDGSMQGLLEQWSVAYTGCQVPGSVLGMDKVLMKERFSHCGIQQVAYTWFKARDWKENRDQVMEKIEKIGYPLMVKPSTLGSSIGISKVKEEKDLEAAVDLALSYDKKVVIEHAVDHLRELNISVLGANGSYDLSPIEEPKSINDLLTFDEKYIHSNNKAGGKTSGKGGRNIVVPEEKVLEAIHTMARSAMDAIDGAGVVRIDFMME... | 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: 387
Sequence Mass (Da): 43... |
D8I9T8 | MSISSKPIAVFDSGFGGISVLKKLLNILPNENYIYLGDNHNIPYGDKSKEEITQLSIKILDFLIKQNCKMAVIACNTITASSYDVLKEKYNIPIIEIISNGVEDIIDNTKNNNISIMATEFTVHSNMYHDKILDYNDKIKVTQVACQKLCPMIENNWYSYDDRILVLEEYVKKIDDNSDTLLLACTHYPFIIDDIKSVVNRKKTNIKNIIDPSTKIALSIKKYLIDNNLLNTSGGKLKFFTTGDKKDFNDFVSRYIKINYELERIVL | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Provides the (R)-glutamate required for cell wall biosynthesis.
EC: 5.1.1.3
Catalytic Activity: L-glutamate = D-glutamate
Sequence Length: 267
Sequence Mass (Da): 30558
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A0A0N1LZ49 | MKQSKLLIPTLRETPSDAETLSHQLLVRAGYIRQAASGIYVYLPLAQRVLEKIKTVIREELAAIDAIEMAMPALLPFEPWVASGRAERYGRALYHLEDRNAREMVLGPTHEEPFMELIKNEVTSYKKLPLNLFQIQNKYRDEQRPRFGLIRSREFLMQDGYSFHADAESLDTTYRQYEAAYHAIFRRCGIDYRTVLGDNGVMGGHDSKEFLALSGIGEELLCYSTESDYVANWKLATSLYASKKSHETFLPLDTIQGNKEWSIDEAAEAAEIDDSKIVKSHVFLVDEQLVMVLIRGDHTINETKVKLFLSGEQITPLSAA... | Function: Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has... |
D8IAD0 | MNNNKKIMLSGIQPTGSLHIGNYLGALKNWADILDDYYGFFCIVDYHAITIEYDVKEMQKRIINAAVEYLASGLDPKKCSIFVQSDVRAHTELAWIFNSIIPVAELERMTQYKDKSRKNVENINAALLTYPSLMAADILLYHPDIVPVGEDQEQHVELTRMIVRKFNNRFGEYFKEPDTYHGKVLRILGLDGVNKMSKSLNNHIALSLTAEETEKLIMQKAMTDTNRKLKTDKGNPDICNVYSYHKIFSSEEEQKEVCEGCKNASIGCVQCKRMLAANINKELAPIRENINKYSNDLDYVYDVLKEGAKNASEVAEKTLY... | Function: Catalyzes the attachment of tryptophan to tRNA(Trp).
Catalytic Activity: ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + H(+) + L-tryptophanyl-tRNA(Trp)
EC: 6.1.1.2
Subcellular Location: Cytoplasm
Sequence Length: 334
Sequence Mass (Da): 38194
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A0A4R1HNW4 | MVARAETTTSNDGQLPDVDAWLSSVSFGRDESAQQMIRAALDRAQKAHRDQTRASGEPYLVHCLAVAEIVHHLQLDHEAVTAAVLHDVVEDTDVSLDDIREEFGEKVAHLVDGVTKMGRISEIREPLSLQQQLDHGRAENVRKLLLAMAEDVRVVLIKLADRLHNMRTLRHLSEERQKRIARETLDIYSPLANRLGIWQVKWELEDLALRYLDADAYHRIAALLDGRRIDRERHIELVKESLIEEFDRAGIQADVVGRPKHIYSIWRKMRRKNVDFHQIFDVQAVRVLVDTTAECYTVLGIVHGLWRHVPHEFDDYIANP... | Pathway: Purine metabolism; ppGpp biosynthesis; ppGpp from GDP: step 1/1.
Function: In eubacteria ppGpp (guanosine 3'-diphosphate 5'-diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance.
EC: 3.1.7.2
Catalytic Activity: gua... |
A0A7J8E4V4 | MEPSPATVGSETTRLVSPRDRGNAGGGLRLKSLFTEPLPEEPKSVEMASHHCHRDPLPQGLTPERLRAQRQLCAACAVCCIFMAGEVVGGYLAHSLAIMTDAAHLLADVGSMMGSLFSLWLSTRPATRTMTFGWHRSETLGALASVVSLWMVTGILLYLAFIRLLHSDYHIEGGAMLLTASIAVCANLLMAFVLHQAGPHHSHGSRGAEYAPLEEGPSEPLSLGNTSVRAAFVHVLGDLLQSFGVLAASILIYFKPQCKAADPISTFLFSVCALGSTAPTLRDVLRVLMEGTPRNVGFEPVRDTLLSVPGVRAAHELHLW... | Catalytic Activity: 2 H(+)(out) + Zn(2+)(in) = 2 H(+)(in) + Zn(2+)(out)
Subcellular Location: Membrane
Sequence Length: 384
Sequence Mass (Da): 41327
Location Topology: Multi-pass membrane protein
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A0A9D8PRS8 | MFNETVIRDTRAVVDLDRIRESVSGIRKLVGDGVEIMAVVKADGYGHGAVRVAKKALRSGAESLAVAYPEEGAELRDNGITAPVLVLGLTSPKIKGAMEKVVGCGLTQTVADTELPRALNAATPEGKRVPVHIKVDTGMGRIGIGIEDVIEYILFLKGLKKIEIEGIYTHFPSSDEADKGFTKRQIEAFLRLLKELKGMGIDIPKAHMANSGGILAHPKSHLTSVRAGIMLYGLYPSGEVERSIPLTPAMSFITRVRYLKKVPKGTTISYGRSFVTERETAVATLPVGYADGYLRILSNRRHVLVGGKQAPIIGRVCMDM... | Pathway: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1.
Function: Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids.
EC: 5.1.1.1
Catalytic Activity: L-alanine = D-alanine
Sequence Length: 379
Sequence Mass (Da): 41270
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F9ZBY2 | MIHSIGLTGGIGSGKSTIAGILKQLGYPVYLADPEASRLINRSVEIRNDLTGLFGADLYTPRGMLDKKLLADIIFKNPQALSQVNRIVHPRVIRDFQHWREQQNSPLVFFESAILFEAGLTRHFDFIICVTASEATRLKRVILRDATNEDKVKERMQNQAADTEKCKNSDFIIYNDEDHMVVQQVLDVLNKLNLKIQ | Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
EC: 2.7.1.24
Subcellular Location: Cytoplasm
Sequence Le... |
A0A968NCZ7 | MDCAIPIDSTDSNRPDPLAQIVVVLHRPQAVVNIGATVRAMKNMGVGQLRLVQPVAYTPDQISALAHRSADLLHGTHHYPDLASAIGDAVYVVGTSARQHRDYPVQPDLRRAAHTLLQATQRGTVALVFGTEDNGLQRAELDLCQQVLHIPTDPAYASLNLAQAVLLVLYELRMAAVGMPAPAVPAAPAPTAAELADLEQAWVTALTELDFFETRNPAIPLRRLRRLLHRAQADRREVAMLRAIAHRITRRLRERGQ | Function: Catalyzes the formation of 2'O-methylated cytidine (Cm32) or 2'O-methylated uridine (Um32) at position 32 in tRNA.
Catalytic Activity: S-adenosyl-L-methionine + uridine(32) in tRNA = 2'-O-methyluridine(32) in tRNA + H(+) + S-adenosyl-L-homocysteine
EC: 2.1.1.200
Subcellular Location: Cytoplasm
Sequence Length... |
F9ZA27 | MNLVIDIGNTRSKYAFFQEDRLIGVNYRLDSILEDIRVWKEKGEKVWIFLTGSGHIDSEMQLAIKEQADYWLEASPALEVPLKIGYATPETLGFDRIAICVGAKSYYPGASLLVIDSGTCITYNYVSAEGVFLGGNISPGLEMRFNGLHRFTARLPLVTPTETYGGIGQSTEEAIRNGVMSGMLFEVQQYIECFLGQYPEGHVLITGGNAHFLERHLTPDILFCKYLSFVGLNEILKYVKKSNY | Cofactor: A monovalent cation. Ammonium or potassium.
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5.
Function: Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
EC: 2.7.1.33
Subcellular Location: Cytoplasm
Catalytic Activity: (R)-pant... |
A0A931ANW0 | MNNKMPEMIQLVIFGGTGDLSRSKLIPGLYKLYKRNSLPDQLSILGLARSFSSRKAYLQSLEQSLKEENPEIYTKESWNNFKEYLDYLQMDFTEDIGYNKLYHHLNDQEGNQAGRHCIYYLATAPEFFPMITENLKEHRLSKSREPGWPRLVIEKPFGYSLSSARDYNSQICQVFPEENVYRIDHYLGKEMIQNILTMRFANMFFEPIWNKHYIDNIQIVSTETSGIKTRGKYYDNAGALRDMVQSHLLQMLALITMESPADMSTESIRQEKIKLLKTLADSPSLGDLRDNLVIGQYKSGIIGDRTVPGYQDEDNIASNS... | Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 1/3.
Function: Catalyzes the oxidation of glucose 6-phosphate to 6-phosphogluconolactone.
EC: 1.1.1.49
Catalytic Activity: D-glucose 6-phosphate + NADP(+) = 6-phospho-D-glucono-1,5-lac... |
A0A2N2KYM3 | MPKGRLYLVPTPVGNLGDMTLRAIETLRNVALIAAEDTRTARKLLNHFEIAAPKLISYHKFSEKSRSPEILGVLTRGEDVAIVSDAGSPGISDPAEIIVKDAIARGFEVIALPGATALIPALTASGLPCGAFLFLGFLPTHSRERKDILKQIKDSPVTAILYEAPHRLRTTLTELYKAIGKRKVVIAREISKIYEEYIRGNLDDVLEDYQVTEKGEFVILIEAIAPDSAPDPLALKSLILAELESGKSPSEIVKALSPDYPKNLIYKLILEMKEHKA | Function: Catalyzes the 2'-O-methylation of the ribose of cytidine 1402 (C1402) in 16S rRNA.
Catalytic Activity: cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = 2'-O-methylcytidine(1402) in 16S rRNA + H(+) + S-adenosyl-L-homocysteine
EC: 2.1.1.198
Subcellular Location: Cytoplasm
Sequence Length: 277
Sequence Mas... |
A0A1G1LN04 | MSRHKTLHLHSPAKLNLYLRVLNKRKDGYHNIVTLFERIDLFDVLTFRCNAGGGIKIYCDHPDVPKGAKNLVYKAAQMLKKEHRVSAGVDIRIKKQIPVAAGLGGGSSNAATALLALNRLWRLSLTQKELLGYAKRIGADVAFFIHDCRWALGEERGDEIRRIPLKTRLWHILVVPRIKMYTKAVYEAFQPAKTDITYRKSEGYSTGPVPRNLLTNQKQNVNILIRHLRQNDLRGVGQFILNDLESSSFRLCSNLKELKETVLNHAPLGGLLSGSGPSIFGLVKTKKEAEKIRSVLRKKYSQSFVVGSL | 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... |
F2I8Q2 | MAESLTDRFIRYAKVNTRSDMYSETFPSTQSQLDFLEVIAGEMEELGLSQVDFDRQRACVTATLPATTEADLPVIGFVAHVDTADFNAENIQPQVHEDYDGQDLVLNEAEGIVMEVAEFPFLKDYVGQTLITSDGTTLLGADDKAGMVGIIGAMEYLLAHPEIEHGKVRIAFVVDEEIGLLGAYRFDVEGFGADFAYTPDSGRVGKIEGETFNAAQVEVWIEGKSVHPGSSKGNAINPLHLGAQIVNDLPKDQVPEKTDGYEGYFMLTQQNGDLGQVHQVFIIRDHDEAKFQERKEIFAQVVDKINSQYKRPRIRYEISD... | Cofactor: Binds 2 Zn(2+) ions per subunit.
EC: 3.4.11.4
Catalytic Activity: Release of the N-terminal residue from a tripeptide.
Sequence Length: 406
Sequence Mass (Da): 45128
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D4G7K8 | MQKKLSWKTVGFGKQNIVLIHGFGFNSEVWKNTIHQEDRNFRFHLIDLPGHGCNHQVLIESVDQVIEKIWENSPKRAIWLGWSLGGLIASEIALRYKDQVRALITVSSSLYFIQEKKDHLLWPGITEKSLKNFKNQLSENFEETIRRFLFIQNLGSNLLKKDLKSLKNSILSYPRPNLESLSFWLNVLRKIDLRKVMSKFKKPFLRIYGEFDQIVPKSVIPLINFLIPNSQSVLIKGSSHAPFISHSEIFNKIIFYFYRNHR | Pathway: Cofactor biosynthesis; biotin biosynthesis.
Function: The physiological role of BioH is to remove the methyl group introduced by BioC when the pimeloyl moiety is complete. It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway through the hydrolysis of the ester bonds of pimeloyl-ACP esters.... |
A0A0C1RZP5 | MNIKQIIQEKIRSIVTFENFCDSVEVRVRFSKNRKTFGDYQIEGLSNILKSNRISLETFKRKLCYLFSKEEYIKSIKIIEPNFINIFLHERWISRQIDTIFSKDRLGISQDNYQKKIVTIIDYSSPNMAKNMHVGHLRSTIIGDTVVRVSKFLGKKVIKANHIGDWGTQFGMIIAYLKEILRKNCVKNITLEKIEDIYQRSRKIFDQNGRFSHISRRYIQQLQSGDDELLTLWNDLVQITILENQRIYDLLGVSLNKGDIVAESFYKDMLQDIVEDLKQKKIAVIHNGAVVVYLDDFKNHHGRSSAVMIQKSDGGYLYAT... | Catalytic Activity: ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg)
EC: 6.1.1.19
Subcellular Location: Cytoplasm
Sequence Length: 582
Sequence Mass (Da): 68229
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E1QXY9 | MAMEPEAWTIRRMLDWTIGYLERRSDGRPRLSAEWMLSNVTGLSRVQLYTSFDRPLSADELARMHDAVVRRGAGEPLQYVTGEMPFRHIVLHCEGGVLIPRPETEVLVDAVLAHVDVAAAAGHDAQVLEVGTGTGCIACSIASERPGSHVVATDLSPAAAALAMRNRDALGLARAVDVITCDLASGVDPALKGTFDVLVSNPPYIPSDVVPTLPREVVGFEPHLALDGGADGLDVFRRLLEVAPDMLRPGGMLACELFETNAEVAAELCRRQGGWARVEVREDLTHRPRVLVAVREGDLAAGGVMVRPRKLLAVDQDRPE... | Function: Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif.
EC: 2.1.1.297
Catalytic Activity: L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-methionine = H(+) + N(5)-methyl-L-glutaminyl-[peptide chain release... |
A0A2H1VBT9 | MCEVVFQCSSDTELALELNEPVFLEDDDYATRAPASPTTVPNVRPYRPPSTGSNILKSPRARRVRTTSMSQPNKRTTAESILHADRRTIYTAGRPPWYNCTGGQEVEPFLIGICGASASGKTTVATKIIESLNIPWVTIVSMDSFYKVLNEKQHQAANRNEYNFDHPDAFDIELLISVLQRLREGKKVEVPIYNYVTHSRENRTKTMYGANVIIFEGILAFYNAEVTKMLDMKVFVDTDADIRLARRLRRDIVQRGRDLEGVLKQYMTHVKPAYQSYIAPCMAHADIIVPRGGENKVAIHLIVQHVHKQLQLVSYCNTFW... | Pathway: Pyrimidine metabolism; CTP biosynthesis via salvage pathway; CTP from cytidine: step 1/3.
EC: 2.7.1.48
Catalytic Activity: ATP + cytidine = ADP + CMP + H(+)
Sequence Length: 342
Sequence Mass (Da): 38662
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H3D6L8 | MVRRVAVIGAGSSGLACAKACVEEGLEPVCFERGHDIGGLWNFREWSEPGWAGVYRSLVANTSKEMMCFSDFPMPADYPNYPHNSQMLQYLRLYAEFHLLPYIRFQTTVTRVTRRPDFSQSGRWDIETVTSDGEEEKHVFDAVLVCSGQFGYPSSPLEDLPGHQDFPGERLHSRDYRDPEAYRGKRVLVVGIGNSGGDIAVEISRCAEMTFLSTRRGAWVISRMSRQGLPVDISSITRFNQVLMELLPWSLLNGLLERALNQKYDHRLYGLQPHHRFLDRKVLINDELPGQILKGRLSVKADLRAFQGSGVLFEDGSVEE... | Catalytic Activity: H(+) + N,N-dimethylaniline + NADPH + O2 = H2O + N,N-dimethylaniline N-oxide + NADP(+)
EC: 1.-.-.-
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 537
Sequence Mass (Da): 60277
Location Topology: Single-pass membrane protein
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A0A1M5R7R3 | MGPVPVRSASPGAARRPGRRGPADYRRARRAARARPDRGAPLSEQPEDAARATPARRPRTRLLLTLAALLFLADLATKLLVVATIDRGENIRLLGGLVYLTHARNTGAAFSFAEGFTVVFTLIAVVVAVVIVRAARRLFSTAWAVALGLVLGGALGNLVDRVFRDPGFLRGGVVDFVSVFAPNGEFYPIFNVADSGIVVGGLLGAYLALRGVEFDGTRSRDRGDGAVTSS | Pathway: Protein modification; lipoprotein biosynthesis (signal peptide cleavage).
Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, ... |
F2I584 | MAFNNMYHIIDRDDWHAYRDEITSDINVKLTEKQLEALLAFNDHLTLEDANDIYQPLTQLISIYFKNYQSLIIERNQFLGINDKIPPFIIGISGSVAVGKSTTARLLQLFLSQFFPYLDVELITTDGFLYPNEQLEHWDLMHRKGFPESYDMHELKKFFMAVKSNKQRLKVPLYSHESYDRINAYREIKSPHILIVEGINVLQFLGSDQFFIGEYADLSIYVDADTELIEKWYMERFILLRENALKDPDHYNQRYSKMSLDDALRSAKRTWENINLVNLEDYILPTRDRADIVIHKIENHYIDSIRMRRY | Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5.
Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+)
EC: 2.7.1.33
Subcellular Location: Cytoplasm
Sequence Length: 310
Sequence Mass (Da): 36851
|
F2I5J0 | MKDNKHSGRLSNILNQSNIFVPLVIAAILVFLAVGMLMHNNPLIALISFLLVIFAIILVYVAFRLIEQELNKQVYDLTDDIQTIENEILLQIPLGIILFEEDDTIRWMNPYMQNYFNSSDTLGNKIDDVDSVLSDIYHQLKERDEDDVTGHPISWDDHYLSVGLLEDQNAMYMLDITEYGRIADVADKNRLVIANILIDNYDETIASYSDRRKSTVDNFMTKQLFAWAKKFGSFIKRLDDDRFLLVTTYGELMEMEEDRFSVIDTIRETTSKGNFPLTISMGISYQEEDDEAPDIGKINEIAQSNLDLALSRGGDQVVIK... | Cofactor: For phosphodiesterase activity, probably binds 2 Mn(2+) per subunit.
Function: Has phosphodiesterase (PDE) activity against cyclic-di-AMP (c-di-AMP).
EC: 3.1.4.-
Catalytic Activity: 3',3'-c-di-AMP + H2O = 5'-O-phosphonoadenylyl-(3'->5')-adenosine + H(+)
Subcellular Location: Cell membrane
Sequence Length: 676... |
Q3YRP0 | MLCKLKYIVSNFGEYRLLLRLHSVEIIFLAMFPALASIALVSHSVLRACGYMILCVIGAFIMRPAGCIINDIFDRKIDSKVKRTRNRPLANGNLSVVQALKVLGVLLACACLLLACTNMYTVKLSIISMILIVLYPLSKRFFTWPQLLLGIVFNSGVLLGCTMTIGHLTLSAVLLYIGCVFWTIGYDTVYAAQDKEYDIELGLQSTAIKFGNDIRLWIGRLYIITITMWISAGIISMLHPIFYIAILIIGAIFYYQYKKSDFDNPEKCMYMFKVNVYVGLILFLGIVLGRVI | Pathway: Cofactor biosynthesis; ubiquinone biosynthesis.
Function: Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of ubiquinone-8 (UQ-8) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB,... |
D8IAW5 | MSENQNNSENTQNEKNSSVEKNAEKENRKEKLNTLRNMGINPFPNSYDVTYKSKDIAEQFEELEKNETEVAVAGRIMLYRVMGKSSFLTIKDSKGTIQAYIQKDKLGDEFYNTVFKKLIDIGDIVGVKGTVFKTKTGEITIYASELKLLTKSLNPLPEKFHGLTDTELRYRQRYVDLIMNDDVKEAFIKRSKMISAIREIMIENNFLEVETPMMHPLIGGAKAKPFVTHHNTLDMTLYLRIAPELYLKRLIVGGFDKVFELNRNFRNEGISTRHNPEFTMMEAYMAYANFHKVMELVEEVFSKVCFKLNGKYTSQYKDYE... | Cofactor: Binds 3 Mg(2+) ions per subunit.
Catalytic Activity: ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-tRNA(Lys)
EC: 6.1.1.6
Subcellular Location: Cytoplasm
Sequence Length: 510
Sequence Mass (Da): 58568
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A0A2H1VZ36 | MLLIKLWLWLLFLFKTNEALLCYNCSTTQREWSRCGGDFVPTNLGFNSTRMFLVNCTGENAMCFVRSWNARARHAWIVQRGCYLPTGDDTLPRSVNIPTRAMSCKHERHAEAEYKVCLCRADWCNSASSLVPSIAQYFYKSLTYIVGNIIIIFWTNKLPIFI | Function: Required for homeostatic regulation of sleep under normal conditions and after sleep deprivation. Important regulator of the Sh K(+) channel, acting as a signaling molecule that connects sleep drive to lowered membrane excitability, possibly by enhancing K(+) channel activity and thus reducing neuronal excita... |
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