ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
F4J0A8 | MDSQYFLAFSLSLLLIFSQISSFSFSVDPTRITQLSWTPRAFLYKGFLSDEECDHLIKLAKGKLEKSMVVADVDSGESEDSEVRTSSGMFLTKRQDDIVANVEAKLAAWTFLPEENGEALQILHYENGQKYDPHFDYFYDKKALELGGHRIATVLMYLSNVTKGGETVFPNWKGKTPQLKDDSWSKCAKQGYAVKPRKGDALLFFNLHLNGTTDPNSLHGSCPVIEGEKWSATRWIHVRSFGKKKLVCVDDHESCQEWADAGECEKNPMYMVGSETSLGFCRKSCKAC | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Catalyzes the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in proline-rich peptide sequences of plant glycoproteins and other proteins. Hydroxyprolines are important constituent of many plant cell wall glycoproteins such as extensins, hy... |
Q8L970 | MDSRIFLAFSLCFLFTLPLISSAPNRFLTRSSNTRDGSVIKMKTSASSFGFDPTRVTQLSWTPRVFLYEGFLSDEECDHFIKLAKGKLEKSMVADNDSGESVESEVRTSSGMFLSKRQDDIVSNVEAKLAAWTFLPEENGESMQILHYENGQKYEPHFDYFHDQANLELGGHRIATVLMYLSNVEKGGETVFPMWKGKATQLKDDSWTECAKQGYAVKPRKGDALLFFNLHPNATTDSNSLHGSCPVVEGEKWSATRWIHVKSFERAFNKQSGCMDENVSCEKWAKAGECQKNPTYMVGSDKDHGYCRKSCKACSS | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Catalyzes the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in proline-rich peptide sequences of plant glycoproteins and other proteins. Hydroxyprolines are important constituent of many plant cell wall glycoproteins such as extensins, hy... |
F4JNU8 | MAKKPKQLRNKPRKSFSTQTFTVVVLVLFVILILVGLGIFSLPSTNKTSSMPMDLTTIVQTIQERESFGDEEDGNGDRWLEVISWEPRAFVYHNFLTNEECEHLISLAKPSMMKSKVVDVKTGKSIDSRVRTSSGTFLNRGHDEIVEEIENRISDFTFIPPENGEGLQVLHYEVGQRYEPHHDYFFDEFNVRKGGQRIATVLMYLSDVDEGGETVFPAAKGNVSDVPWWDELSQCGKEGLSVLPKKRDALLFWSMKPDASLDPSSLHGGCPVIKGNKWSSTKWFHVHEYN | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Catalyzes the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in proline-rich peptide sequences of plant glycoproteins and other proteins. Hydroxyprolines are important constituent of many plant cell wall glycoproteins such as extensins, hy... |
Q8VZJ7 | MKSRLKSYRRKKLGLATVIVFCSLCFLFGFYGSTLLSQNVPRVKPRLRMLDMVENGEEEASSMPHGVTGEESIGSIPFQVLSWRPRAIYFPNFATAEQCQAIIERAKVNLKPSALALRKGETAENTKGTRTSSGTFISASEESTGALDFVERKIARATMIPRSHGESFNILRYELGQKYDSHYDVFNPTEYGPQSSQRIASFLLYLSDVEEGGETMFPFENGSNMGIGYDYKQCIGLKVKPRKGDGLLFYSVFPNGTIDQTSLHGSCPVTKGEKWVATKWIRDQDQEE | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Catalyzes the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in proline-rich peptide sequences of plant glycoproteins and other proteins. Hydroxyprolines are important constituent of many plant cell wall glycoproteins such as extensins, hy... |
Q10576 | MRLALLVLATIGYAVADLFTSIADMQNLLETERNIPKILDKYIHDEEERLVQLKKLSEEYSKKNEISIENGLKDITNPINAFLLIKRKIFDWKEIESKMNANKAGNVVSSITDDSYGVRYPTADDLSGAAIGLLRLQDTYRLDTKDLADGKIYADQGNYTFSAKDCFEIARAAYNEHDFYHTVMWMEEAQRRLGDEVEPTVEVEDILEYLAFALYKQNNLKHALKLTEELYKMNPTHPRAKGNVKWYEDLLEQEGVRRSDMRKNLPPIQNRRPDSVLGNTERTMYEALCRNEVPVSQKDISRLYCYYKRDRPFLVYAPIK... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Catalyzes the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins.
Catalytic Activity: 2-oxoglutarate + L-prolyl-[collagen] + O2 = CO2 + succinate + trans-4-hydroxy-L-prolyl-[collagen]
Sequence Mass (Da): 63927
S... |
P16924 | HTDFFTSIGHMTDLINTEKDLVISKLKDYIKAEESKLEQIKKWAEKLDKLTDTATKDPEGFLGHPANAFKLMKRLNTEWGELESLVLKDMSDGFISNMTIQRQFFPNDEDQTGARKALLRLQDTYNLDTDTLSRGNLPGVKHKSFLTAEDCFELGKIRYTEADYYHTELWMEQALKQLDEGEVSSADKVYILDYLSYAVYQQGDLSKAMMLTKRLLELDPEHQRANGNMKYFEYIMAKEKEANKSSTDAEDQTDKETEVKKKDYLPERRKYEMLCRGEGLKMTPRRQKRLFCRYYDGNRNPRYILGPVKQEDEWDKPRIV... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Catalyzes the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins.
Catalytic Activity: 2-oxoglutarate + L-prolyl-[collagen] + O2 = CO2 + succinate + trans-4-hydroxy-L-prolyl-[collagen]
Sequence Mass (Da): 59440
S... |
P13674 | MIWYILIIGILLPQSLAHPGFFTSIGQMTDLIHTEKDLVTSLKDYIKAEEDKLEQIKKWAEKLDRLTSTATKDPEGFVGHPVNAFKLMKRLNTEWSELENLVLKDMSDGFISNLTIQRQYFPNDEDQVGAAKALLRLQDTYNLDTDTISKGNLPGVKHKSFLTAEDCFELGKVAYTEADYYHTELWMEQALRQLDEGEISTIDKVSVLDYLSYAVYQQGDLDKALLLTKKLLELDPEHQRANGNLKYFEYIMAKEKDVNKSASDDQSDQKTTPKKKGVAVDYLPERQKYEMLCRGEGIKMTPRRQKKLFCRYHDGNRNPK... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Catalyzes the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins.
Catalytic Activity: 2-oxoglutarate + L-prolyl-[collagen] + O2 = CO2 + succinate + trans-4-hydroxy-L-prolyl-[collagen]
Sequence Mass (Da): 61049
S... |
Q60715 | MIWVVLMMAILLPQSLAHPGFFTSIGQMTDLIHNEKDLVTSLKDYIKAEEDKLEQIKKWAEKLDRLTSTATKDPEGFVGHPVNAFKLMKRLNTEWSELENLILKDMSDGFISNLTIQRQYFPNDEDQVGAAKALFRLQDTYNLDTNTISKGNLPGVQHKSFLTAEDCFELGKVAYTEADYYHTELWMEQALTQLEEGELSTVDKVSVLDYLSYAVYQQGDLDKALLLTKKLLELDPEHQRANGNLVYFEYIMSKEKDANKSASGDQSDQKTAPKKKGIAVDYLPERQKYEMLCRGEGIKMTPRRQKRLFCRYHDGNRNPK... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Catalyzes the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins.
Catalytic Activity: 2-oxoglutarate + L-prolyl-[collagen] + O2 = CO2 + succinate + trans-4-hydroxy-L-prolyl-[collagen]
Sequence Mass (Da): 60910
S... |
P0A9L8 | MEKKIGFIGCGNMGKAILGGLIASGQVLPGQIWVYTPSPDKVAALHDQFGINAAESAQEVAQIADIIFAAVKPGIMIKVLSEITSSLNKDSLVVSIAAGVTLDQLARALGHDRKIIRAMPNTPALVNAGMTSVTPNALVTPEDTADVLNIFRCFGEAEVIAEPMIHPVVGVSGSSPAYVFMFIEAMADAAVLGGMPRAQAYKFAAQAVMGSAKMVLETGEHPGALKDMVCSPGGTTIEAVRVLEEKGFRAAVIEAMTKCMEKSEKLSKS | Function: Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline. Does not catalyze the reverse reaction.
Catalytic Activity: L-proline + NADP(+) = 1-pyrroline-5-carboxylate + 2 H(+) + NADPH
Sequence Mass (Da): 28145
Sequence Length: 269
Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-proli... |
P43869 | MQHKLIAFIGGGNMAQAIILGLLKQGYPAEQIIVNDPNEEKRAFFANLDVATSENNVGSAIKAEVVLLAVKPQMMAEVCSPLSAVDFSDKLLISIAAGISTERLNALIPSVKSIVRVMPNTPALVGEGMAGLFAPKNTSENYRTFAQDLLGAVGRTVWVNDETQMHAVTAASGSSPAYFFLMLEAMQKALIKMNIDEKTARELVQQSMLGAAKMVTENPQIALSTLRENVTSKGGTTAAALAVFDAQHFNQTIEQAMQACLSRSQEMETLF | Function: Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline.
Catalytic Activity: L-proline + NADP(+) = 1-pyrroline-5-carboxylate + 2 H(+) + NADPH
Sequence Mass (Da): 29124
Sequence Length: 271
Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-proline from L-glutamate 5-semialdehyde: step... |
O25773 | MEILQFIGYGNMAQAILEGAHEILSKRFILEITGRNPEKIAPFLQEKNIQAQIVPYKDAIDIHQKFVFLLFKPYNLKDFNYQGQAKSVLSALAGVGFKALSDAIDSLHYLKCMPNIASKFALSSTAVCEKSPMPLISQKALSVIESFGNCVRVGHEELVDASVATNGSALAFLSLVANSLKDAGIREGLNARGSLELVKMSFKGFAKLLEKERPEMIIEQICTPKGATIEGLSVLEKKGVRGAFIEACHKSVKKMRL | Function: Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline.
Catalytic Activity: L-proline + NADP(+) = 1-pyrroline-5-carboxylate + 2 H(+) + NADPH
Sequence Mass (Da): 28162
Sequence Length: 257
Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-proline from L-glutamate 5-semialdehyde: step... |
Q9HH99 | MENQKIGFIGAGKMGSALMQGTIKAGIVTPENIGASDVYEPFLKDLQAKLGIRVSTDNAVIVRESDILILAVKPQTLSSVLSNLKNEITSEKLVISIAAGVPLSTYEDALLEGTRVVRVMPNIAATVSEAASGIAPGKNATPEDLKAALEIFSAVGTAVQVPESLMDAVTGLSGSGPAFIFPVIEAMADGAVLEGMDRKSALTLAAQTVLGAAKMALETGMHPGELKDMVTSPAGTTIQGIHSLEEAGIRAAFMNAVIRASERSKELGKK | Function: Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline.
Catalytic Activity: L-proline + NADP(+) = 1-pyrroline-5-carboxylate + 2 H(+) + NADPH
Sequence Mass (Da): 27943
Sequence Length: 270
Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-proline from L-glutamate 5-semialdehyde: step... |
P22350 | MNLGIIGYGNIGELLSQNIISHDFCNLNKLYIANRTLSKINHLKDIDPRISITDDNIEVAKTCEKIIISVKTPDLAIVLDPLKPHITKNQQIIHTCAGTDLEFKDCGLSCVIPTISSTYDEDNPKKGVSIIMHDENVSGENREFVEKLFSKFSQIKVVDSPMDLEIATIAASCMPAFIALGVDLFAGELEEKCNLSKEETFKILAETLNSTAYILKEDIYSPDELINKVATKNGITQKGLDVLDKRPARYL | Function: Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline.
Catalytic Activity: L-proline + NADP(+) = 1-pyrroline-5-carboxylate + 2 H(+) + NADPH
Sequence Mass (Da): 27859
Sequence Length: 251
Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-proline from L-glutamate 5-semialdehyde: step... |
P46725 | MLSSMARIAIIGGGSIGEALLSGLLRAGRQVKDLVVAERMPDRARYLADTYSVLVTSVTDAVENAMFVVVAVKPTDVESVMGDLVQAAAVANDSAEQVLVTVAAGVTITYLESKLPAGTPVVRAMPNAAALVGAGVTVLAKGRFVTGQQFEDVLAMFDAVGGVLTVPESQMDAVTAVSGSGPAYFFLLVEALVDAGVAVGLTRQVATELAAQTMAGSAAMLLERMDQDRHSAEVAPLGAQVDVPAAQLRATITSPGGTTAAALRELERGGLRMVVDAAVQAAKIRSEQLRITSE | Function: Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline.
Catalytic Activity: L-proline + NADP(+) = 1-pyrroline-5-carboxylate + 2 H(+) + NADPH
Sequence Mass (Da): 30237
Sequence Length: 294
Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-proline from L-glutamate 5-semialdehyde: step... |
Q12641 | MAAPQVKSSSELTMAVLGCGTMGISILSGILSSLSSIAQDPSPPPTNPPALPRHFIATVRSPSSVAKVESALSPLVKPSVSTLRVLQSTSNVSAAAEADIILLGCKPYMVSGLLSASGMKDALTVKHTEGHARSQKIIISICAGVTVPDLERVLREDVGLSADNLPIVVRAMPNTASKIRESMTVINTVDPPLPDTVTELLTWIFERIGEVVYLPPHLMDACTSLCASGTAFFALMMEAAADGGVAMGLPRAEANRMAAQTMRGAAGLVLEGEHPAILREKVSTPGGCTIGGLLVLEEGGVRAAVARAVREATVVASLLG... | Catalytic Activity: L-proline + NADP(+) = 1-pyrroline-5-carboxylate + 2 H(+) + NADPH
Sequence Mass (Da): 34215
Sequence Length: 332
Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-proline from L-glutamate 5-semialdehyde: step 1/1.
EC: 1.5.1.2
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P22008 | MSTPRIAFIGAGNMAASLIGGLRAQGVPAAQIRASDPGAEQRAKIAGEFAIDVVESNAEAVADADVVVLSVKPQAMKAVCQALAPALKPEQLIVSIAAGIPCASLEAWLGQPRPVVRCMPNTPALLRQGASGLYANAQVSAAQCEQAGQLLSAVGIALWLDDEAQIDAVTAVSGSGPAYFFLLMQAMTDAGEKLGLSRETASRLTLQTALGAAQMALSSEVEPAELRRRVTSPNGTTEAAIKSFQANGFEALVEQALNAASQRSAELAEQLGQ | Function: Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline.
Catalytic Activity: L-proline + NADP(+) = 1-pyrroline-5-carboxylate + 2 H(+) + NADPH
Sequence Mass (Da): 28094
Sequence Length: 273
Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-proline from L-glutamate 5-semialdehyde: step... |
Q9P7Y7 | MSGFCVLGCGTMGKALLTGIFDSIAENGNDVSDEIIIPNKFYACVKFPKEKEDVQKLFGDRVKVVMGAKENAEMAAISNVLLLSCKPQAAEDVLNSPKMKEALKGKLILSILAGKTISSLQSMLDESTRVIRIMPNTASRIRESMSVICPGPNATEEDIKFAEWVFNGIGRSMKLPEKLIDAATAVCGSGPAFVATMIEAMTDGGVMMGIPFPQAQELAAQTMVGTGRMVLQGQHPAMIRNDVSTPAGCTISGLLALEDGKIRSTIARGIEQATKTASGLGK | Catalytic Activity: L-proline + NADP(+) = 1-pyrroline-5-carboxylate + 2 H(+) + NADPH
Sequence Mass (Da): 29875
Sequence Length: 282
Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-proline from L-glutamate 5-semialdehyde: step 1/1.
EC: 1.5.1.2
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Q63787 | MSAEGYQYRALYDYKKEREEDIDLHLGDILTVNKGSLVALGFSDGQEARPEDIGWLNGYNETTGERGDFPGTYVEYIGRKRISPPTPKPRPPRPLPVAPGSSKTEADTEQPVLTLPDLAEQFAPPDVAPPLLIKLLEAIEKKGLECSTLYRTQSSSNPAELRQLLDCDPPSVDLDVFDEHVLADAFKRYLADLPNPVIPVAVYNEMMSLAQEVPSSEDYIQLLKKLIRSPNIPHQYWLTLQYLLKHFFKLSQASSKNLLNARALSEIFSHVLFRFPAASSDNTEHLIKAVELLISAEWSERQPAPALPPKPPKPTSIANN... | Function: Binds to activated (phosphorylated) protein-Tyr kinases, through its SH2 domain, and acts as an adapter, mediating the association of the p110 catalytic unit to the plasma membrane. Necessary for the insulin-stimulated increase in glucose uptake and glycogen synthesis in insulin-sensitive tissues. Plays an im... |
O00459 | MAGPEGFQYRALYPFRRERPEDLELLPGDVLVVSRAALQALGVAEGGERCPQSVGWMPGLNERTRQRGDFPGTYVEFLGPVALARPGPRPRGPRPLPARPRDGAPEPGLTLPDLPEQFSPPDVAPPLLVKLVEAIERTGLDSESHYRPELPAPRTDWSLSDVDQWDTAALADGIKSFLLALPAPLVTPEASAEARRALREAAGPVGPALEPPTLPLHRALTLRFLLQHLGRVASRAPALGPAVRALGATFGPLLLRAPPPPSSPPPGGAPDGSEPSPDFPALLVEKLLQEHLEEQEVAPPALPPKPPKAKPASTVLANGG... | Function: Regulatory subunit of phosphoinositide-3-kinase (PI3K), a kinase that phosphorylates PtdIns(4,5)P2 (Phosphatidylinositol 4,5-bisphosphate) to generate phosphatidylinositol 3,4,5-trisphosphate (PIP3). PIP3 plays a key role by recruiting PH domain-containing proteins to the membrane, including AKT1 and PDPK1, a... |
Q58346 | MKIGIMSDTHDHLPNIRKAIEIFNDENVETVIHCGDFVSLFVIKEFENLNANIIATYGNNDGERCKLKEWLKDINEENIIDDFISVEIDDLKFFITHGHHQSVLEMAIKSGLYDVVIYGHTHERVFEEVDDVLVINPGECCGYLTGIPTIGILDTEKKEYREIVLE | Cofactor: Binds 2 divalent metal ions per subunit. Most effective are nickel and manganese.
Function: Shows phosphodiesterase activity, hydrolyzing phosphodiesters bonds in the artificial chromogenic substrates bis-p-nitrophenyl phosphate (bis-pNPP), and less efficiently thymidine 5'-monophosphate p-nitrophenyl ester (... |
P07581 | MPFPLVKQDPTSKAFTEASERSTGTQILDVVKAPIGLFGDDAKHEFVTRQEQAVSVVSWAVAAGLIGELIGYRGARSGRKAILANIPFLA | Function: Essential for membrane formation.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 9613
Sequence Length: 90
Subcellular Location: Virion membrane
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Q86XP0 | MESLSPGGPPGHPYQGEASTCWQLTVRVLEARNLRWADLLSEADPYVILQLSTAPGMKFKTKTLTDTSHPVWNEAFRFLIQSQVKNVLELSIYDEDSVTEDDICFKVLYDISEVLPGKLLRKTFSQSPQGEEELDVEFLMEETSDRPENLITNKVIVARELSCLDVHLDSTGSTAVVADQDKLELELVLKGSYEDTQTSFLGTASAFRFHYMAALETELSGRLRSSRSNGWNGDNSAGYLTVPLRPLTIGKEVTMDVPAPNAPGVRLQLKAEGCPEELAVHLGFNLCAEEQAFLSRRKQVVAKALKQALQLDRDLQEDEV... | Function: Calcium-dependent phospholipase A2 that selectively hydrolyzes glycerophospholipids in the sn-2 position . Has a preference for linoleic acid at the sn-2 position .
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+)
Location Topology... |
Q50L42 | MQSIPHSDEADVAGMTHASEGHHGLGTSMLVPKNPQGEEDSKLGRNCSGFEDAQDPQTAVPSSPLLSMASCSSQEGSSPCHLLTVRIIGMKNVRQADILSQTDCFVTLWLPTASQKKLKTRTISNCLHPEWDESFTFQIQTQVKNVLELSVCDEDTLTQNDHLLTVLYDLSKLCLRNKTHVKFPLNPEGMEELEVEFLLEENFSSSETLITNGVLVSRQVSCLEVHAESRRPRKRKKNKDLLVMVTDSFENTQRVPPCQEPCYPNSACFHYPKYSQPQLYAEAPKSHCNFRLCCCGTHRNDPVCQPLNCLSDGQVTTLPV... | Function: Calcium-dependent N-acyltransferase involved in the biosynthesis of N-acyl ethanolamines (NAEs) in the brain . Transfers the sn-1 fatty acyl chain of phosphatidylcholine (fatty acyl donor) to the amine group of phosphatidylethanolamine (fatty acyl acceptor) to generate N-acyl phosphatidylethanolamine (NAPE). ... |
Q50L41 | MPWTLQPKWLAGKGLPLLGAILLRKTEKSEPQWKHRRQETHPYYDLQVKVLRARNIQHTDKLSKADCYVRLWLPTASVSPSQTRTVVNSSDPEWNETFPYQIHGAVKNVLELALYDEDVLDSDNVFSILFDTSTLQLGQPCTKNFTRQQDPKELEVEFTLEKSQTPASEVVTNGVLVAHPCLRIQGTVTGDKTASLGELGSRQIQLAVPGAYEKPQPLQPTSEPGLPVNFTFHVNPVLSPKLHIKLQEQLQVFHSGPSDELEAQTSKMDKASILLSSLPLNEELTKLVDLEEGQQVSLRMKADMSSSGDLDLRLGFDLCD... | Function: Has calcium-dependent phospholipase and lysophospholipase activities with a potential role in membrane lipid remodeling and biosynthesis of lipid mediators . Preferentially hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids (phospholipase A2 activity) . Selectively hy... |
C0HJU3 | NLVQFKTLIMKIAGRSVVYKYFYYGCYCGWGGIGQPRDATDRCCFVHD | Cofactor: Binds 1 Ca(2+) ion.
Function: Snake venom phospholipase A2 (PLA2) that shows myotoxicity and induces paw edema in mice . Exhibits indirect hemolytic activity . Inhibits platelet aggregation induced by ADP and collagen . PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycer... |
P0DJJ7 | DLMQFETLIMKIAGRSGVWIYGSYGCYCG | Cofactor: Binds 1 Ca(2+) ion.
Function: Snake venom phospholipase A2 (PLA2) that inhibits the ADP- and collagen-induced human platelet aggregation (By similarity). Exhibits strong hydrolytic activities and prefers the anionic micelles (dPPC with deoxycholate) to the zwitterionic micelles (dPPC with Triton X-100). PLA2 ... |
P47711 | MKLLLLLLVVMASDLPQAHGHLKQFTEMIKLTTGKNGLTSYGAYGCHCGVGGKGTPKDATDRCCVRHDCCYDRLMKRGCGTKFLNYRFTHKGSSITCSVKQNSCQKQLCECDKAAAYCFAANLKSYSRRYQFYYNGLCRGKTPSC | Cofactor: Binds 1 Ca(2+) ion per subunit.
Function: Secretory calcium-dependent phospholipase A2 that primarily targets extracellular phospholipids with implications in host antimicrobial defense, inflammatory response and tissue regeneration (By similarity). Hydrolyzes the ester bond of the fatty acyl group attached a... |
P14555 | MKTLLLLAVIMIFGLLQAHGNLVNFHRMIKLTTGKEAALSYGFYGCHCGVGGRGSPKDATDRCCVTHDCCYKRLEKRGCGTKFLSYKFSNSGSRITCAKQDSCRSQLCECDKAAATCFARNKTTYNKKYQYYSNKHCRGSTPRC | Cofactor: Binds 1 Ca(2+) ion per subunit.
Function: Secretory calcium-dependent phospholipase A2 that primarily targets extracellular phospholipids with implications in host antimicrobial defense, inflammatory response and tissue regeneration . Hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position... |
P31482 | MKVLLLLAASIMAFGSIQVQGNIAQFGEMIRLKTGKRAELSYAFYGCHCGLGGKGSPKDATDRCCVTHDCCYKSLEKSGCGTKLLKYKYSHQGGQITCSANQNSCQKRLCQCDKAAAECFARNKKTYSLKYQFYPNMFCKGKKPKC | Cofactor: Binds 1 Ca(2+) ion per subunit.
Function: Secretory calcium-dependent phospholipase A2 that primarily targets extracellular phospholipids with implications in host antimicrobial defense, inflammatory response and tissue regeneration . Hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position... |
P14422 | HLLDFRKMIRYTTGKEATTSYGAYGCHCGVGGRGAPKXAKFLSYKFSMKKAAAACFKYQFYPNNRCXG | Cofactor: Binds 1 Ca(2+) ion per subunit.
Function: Secretory calcium-dependent phospholipase A2 that primarily targets extracellular phospholipids with implications in host antimicrobial defense, inflammatory response and tissue regeneration (By similarity). Hydrolyzes the ester bond of the fatty acyl group attached a... |
P48076 | MKGIAIFLVFIFYWTTSTLSSFWQFQRMVKHVTGRSAFFSYYGYGCYCGLGGKGLPVDATDRCCWAHDCCYHKLKEYGCQPILNAYQFTIVNGTVTCGCTVASSCPCGQKACECDKQSVYCFKENLATYEKAFKQLFPTRPQCGRDKLQC | Cofactor: Binds 1 Ca(2+) ion per subunit.
Function: PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. Testis PA2 may be important in the production of prostaglandins, by the release of arachidonic acid, which in turn are necessary for the contractions of the seminiferous tub... |
Q9WVF6 | MRLALLCGLLLAGITATQGGLLNLNKMVTHMTGKKAFFSYWPYGCHCGLGGKGQPKDATDWCCQKHDCCYAHLKIDGCKSLTDNYKYSISQGTIQCSDNGSWCERQLCACDKEVALCLKQNLDSYNKRLRYYWRPRCKGKTPAC | Cofactor: Binds 1 Ca(2+) ion per subunit.
Function: Secretory calcium-dependent phospholipase A2 that primarily targets extracellular lipids, exerting anti-inflammatory and immunosuppressive functions . Hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids (phospholipase A2 activi... |
Q9NZK7 | MKSPHVLVFLCLLVALVTGNLVQFGVMIEKMTGKSALQYNDYGCYCGIGGSHWPVDQTDWCCHAHDCCYGRLEKLGCEPKLEKYLFSVSERGIFCAGRTTCQRLTCECDKRAALCFRRNLGTYNRKYAHYPNKLCTGPTPPC | Cofactor: Binds 2 Ca(2+) ions per subunit. One ion binds at a conserved binding site (GCXCG), whereas the second ion binds at a flexible site and may act as a supplemental electrophile as well as a backup.
Function: Secretory calcium-dependent phospholipase A2 that primarily targets extracellular phospholipids . Hydrol... |
Q9QZT4 | MKKFFAIAVLAGSVVTTAHSSLLNLKSMVEAITHRNSILSFVGYGCYCGLGGRGHPMDEVDWCCHAHDCCYEKLFEQGCRPYVDHYDHRIENGTMIVCTELNETECDKQTCECDKSLTLCLKDHPYRNKYRGYFNVYCQGPTPNCSIYDPYPEEVTCGHGLPATPVST | Cofactor: Binds 1 Ca(2+) ion per subunit.
Function: Secretory calcium-dependent phospholipase A2 that primarily targets extracellular phospholipids . Hydrolyzes the ester bond of the fatty acyl group attached at the sn-2 position of phospholipids (phospholipase A2 activity), the catalytic efficiency decreasing in the f... |
O15496 | MGPLPVCLPIMLLLLLPSLLLLLLLPGPGSGEASRILRVHRRGILELAGTVGCVGPRTPIAYMKYGCFCGLGGHGQPRDAIDWCCHGHDCCYTRAEEAGCSPKTERYSWQCVNQSVLCGPAENKCQELLCKCDQEIANCLAQTEYNLKYLFYPQFLCEPDSPKCD | Cofactor: Binds 1 Ca(2+) ion per subunit.
Function: Secretory calcium-dependent phospholipase A2 that primarily targets extracellular phospholipids . Hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids with preference for phosphatidylcholines and phosphatidylglycerols over phosp... |
Q9QZT3 | MLLLLLLLLLGPGSCLSEATRRSHVYKRGLLELAGTLDCVGPRSPMAYMNYGCYCGLGGHGEPRDAIDWCCYYHDCCYSQAQDAGCSPKLYRYPWKCMDHRILCGPAENKCQELLCRCDETLAYCLADTEYHLKYLFFPSVLCEKDSPKCN | Cofactor: Binds 1 Ca(2+) ion per subunit.
Function: Secretory calcium-dependent phospholipase A2 that primarily targets extracellular phospholipids. Hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids with preference for phosphatidylcholines and phosphatidylglycerols over phosph... |
P76082 | MSELIVSRQQRVLLLTLNRPAARNALNNALLMQLVNELEAAATDTSISVCVITGNARFFAAGADLNEMAEKDLAATLNDTRPQLWARLQAFNKPLIAAVNGYALGAGCELALLCDVVVAGENARFGLPEITLGIMPGAGGTQRLIRSVGKSLASKMVLSGESITAQQAQQAGLVSDVFPSDLTLEYALQLASKMARHSPLALQAAKQALRQSQEVALQAGLAQERQLFTLLAATEDRHEGISAFLQKRTPDFKGR | Function: Catalyzes the reversible conversion of enzymatically produced 2,3-dehydroadipyl-CoA into 3-hydroxyadipyl-CoA.
Catalytic Activity: a (3S)-3-hydroxyacyl-CoA = a (2E)-enoyl-CoA + H2O
Sequence Mass (Da): 27237
Sequence Length: 255
Pathway: Aromatic compound metabolism; phenylacetate degradation.
EC: 4.2.1.17
|
P77467 | MMEFILSHVEKGVMTLTLNRPERLNSFNDEMHAQLAECLKQVERDDTIRCLLLTGAGRGFCAGQDLNDRNVDPTGPAPDLGMSVERFYNPLVRRLAKLPKPVICAVNGVAAGAGATLALGGDIVIAARSAKFVMAFSKLGLIPDCGGTWLLPRVAGRARAMGLALLGNQLSAEQAHEWGMIWQVVDDETLADTAQQLARHLATQPTFGLGLIKQAINSAETNTLDTQLDLERDYQRLAGRSADYREGVSAFLAKRSPQFTGK | Function: Catalyzes the reversible conversion of the epoxide to 2-oxepin-2(3H)-ylideneacetyl-CoA (oxepin-CoA).
Catalytic Activity: 2-(1,2-epoxy-1,2-dihydrophenyl)acetyl-CoA = 2-oxepin-2(3H)-ylideneacetyl-CoA
Sequence Mass (Da): 28405
Sequence Length: 262
Pathway: Aromatic compound metabolism; phenylacetate degradation.... |
P76083 | MMINVQTVAVIGSGTMGAGIAEVAASHGHQVLLYDISAEALTRAIDGIHARLNSRVTRGKLTAETCERTLKRLIPVTDIHALAAADLVIEAASERLEVKKALFAQLAEVCPPQTLLTTNTSSISITAIAAEIKNPERVAGLHFFNPAPVMKLVEVVSGLATAAEVVEQLCELTLSWGKQPVRCHSTPGFIVNRVARPYYSEAWRALEEQVAAPEVIDAALRDGAGFPMGPLELTDLIGQDVNFAVTCSVFNAFWQERRFLPSLVQQELVIGGRLGKKSGLGVYDWRAEREAVVGLEAVSDSFSPMKVEKKSDGVTEIDDV... | Function: Catalyzes the oxidation of 3-hydroxyadipyl-CoA to yield 3-oxoadipyl-CoA.
Catalytic Activity: (3S)-3-hydroxyadipyl-CoA + NAD(+) = 3-oxoadipyl-CoA + H(+) + NADH
Sequence Mass (Da): 51733
Sequence Length: 475
Pathway: Aromatic compound metabolism; phenylacetate degradation.
EC: 1.1.1.-
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P76084 | MSHKAWQNAHAMYENDACAKALGIDIISMDEGFAVVTMTVTAQMLNGHQSCHGGQLFSLADTAFAYACNSQGLAAVASACTIDFLRPGFAGDTLTATAQVRHQGKQTGVYDIEIVNQQQKTVALFRGKSHRIGGTITGEA | Function: Thioesterase with a preference for ring-hydroxylated phenylacetyl-CoA esters. Hydrolyzes 3,4-dihydroxyphenylacetyl-CoA, 3-hydroxyphenylacetyl-CoA and 4-hydroxyphenylacetyl-CoA. Inactive towards 4-hydroxybenzoyl-CoA and 4-hydroxyphenacyl-CoA.
Sequence Mass (Da): 14851
Sequence Length: 140
Pathway: Aromatic com... |
P0C7L2 | MREAFICDGIRTPIGRYGGALSSVRADDLAAIPLRELLVRNPRLDAECIDDVILGCANQAGEDNRNVARMATLLAGLPQSVSGTTINRLCGSGLDALGFAARAIKAGDGDLLIAGGVESMSRAPFVMGKAASAFSRQAEMFDTTIGWRFVNPLMAQQFGTDSMPETAENVAELLKISREDQDSFALRSQQRTAKAQSSGILAEEIVPVVLKNKKGVVTEIQHDEHLRPETTLEQLRGLKAPFRANGVITAGNASGVNDGAAALIIASEQMAAAQGLTPRARIVAMATAGVEPRLMGLGPVPATRRVLERAGLSIHDMDVI... | Function: Catalyzes the thiolytic cleavage of the beta-keto C8 intermediate 3-oxo-5,6-dehydrosuberyl-CoA with CoA to yield the C6 intermediate 2,3-dehydroadipyl-CoA and acetyl-CoA. Besides it catalyzes also the last step of the pathway, in which 3-oxoadipyl-CoA similarly is cleaved to acetyl-CoA and succinyl-CoA.
Catal... |
Q9L9C1 | MPVKTPSPGDLEPIEKASQDELRALQLERLKWSVRHAYENVPHYRKAFDAKGVHPDDLKSLADLAKFPFTAKGDLRDNYPFGMFAVPREKVARVHASSGTTGKPTVVGYTLKDIDTWATVVARSIRASGGRAGDMVHIAYGYGLFTGGLGAHYGAEKLGCTVVPMSGGQTEKQIQLIQDFKPDIIMVTPSYMLTVLDEMERMGIDPHQTSLKVGIFGAEPWTQAMRAAMEARAGIDAVDIYGLSEVMGPGVANECIEAKDGPVIWEDHFYPEIIDPHTGEVLPDGSEGELVFTTLTKEAMPVIRYRTRDLTRLLPPTARS... | Function: Catalyzes the activation of phenylacetic acid (PA) to phenylacetyl-CoA (PA-CoA). Involved in the phenylalanine metabolism.
Catalytic Activity: 2-phenylacetate + ATP + CoA = AMP + diphosphate + phenylacetyl-CoA
Sequence Mass (Da): 48735
Sequence Length: 440
Pathway: Aromatic compound metabolism; phenylacetate ... |
P76085 | MITNTKLDPIETASVDELQALQTQRLKWTLKHAYENVPMYRRKFDAAGVHPDDFRELSDLRKFPCTTKQDLRDNYPFDTFAVPMEQVVRIHASSGTTGKPTVVGYTQNDIDNWANIVARSLRAAGGSPKDKIHVAYGYGLFTGGLGAHYGAERLGATVIPMSGGQTEKQAQLIRDFQPDMIMVTPSYCLNLIEELERQLGGDASGCSLRVGVFGAEPWTQAMRKEIERRLGITALDIYGLSEVMGPGVAMECLETTDGPTIWEDHFYPEIVNPHDGTPLADGEHGELLFTTLTKEALPVIRYRTRDLTRLLPGTARTMRR... | Function: Catalyzes the activation of phenylacetic acid (PA) to phenylacetyl-CoA (PA-CoA).
Catalytic Activity: 2-phenylacetate + ATP + CoA = AMP + diphosphate + phenylacetyl-CoA
Sequence Mass (Da): 48953
Sequence Length: 437
Pathway: Aromatic compound metabolism; phenylacetate degradation.
EC: 6.2.1.30
|
O33469 | MNMYHDADRALLDPMETASVDALRQHQLERLRWSLKHAYDNVPLYRQRFAECGAHPDDLTCLEDLAKFPFTGKNDLRDNYPYGMFAVPQEEVVRLHASSGTTGKPTVVGYTQNDINTWANVVARSIRAAGGRKGDKVHVSYGYGLFTGGLGAHYGAERLGCTVIPMSGGQTEKQVQLIRDFQPDIIMVTPSYMLNLADEIERQGIDPHDLKLRLGIFGAEPWTDELRRSIEQRLGINALDIYGLSEIMGPGVAMECIETKDGPTIWEDHFYPEIIDPVTGEVLPDGQLGELVFTSLSKEALPMVRYRTRDLTRLLPGTAR... | Function: Catalyzes the activation of phenylacetic acid (PA) to phenylacetyl-CoA (PA-CoA) . Involved in the phenylalanine metabolism . Can also use CTP and UTP as substrate .
Catalytic Activity: 2-phenylacetate + ATP + CoA = AMP + diphosphate + phenylacetyl-CoA
Sequence Mass (Da): 49392
Sequence Length: 439
Pathway: Ar... |
Q8RY79 | MENGSGKVLKPMDSEQLREYGHLMVDFIADYYKTIEDFPVLSQVQPGYLHKLLPDSAPDHPETLDQVLDDVRAKILPGVTHWQSPSFFAYYPSNSSVAGFLGEMLSAGLGIVGFSWVTSPAATELEMIVLDWVAKLLNLPEQFMSKGNGGGVIQGSASEAVLVVLIAARDKVLRSVGKNALEKLVVYSSDQTHSALQKACQIAGIHPENCRVLTTDSSTNYALRPESLQEAVSRDLEAGLIPFFLCANVGTTSSTAVDPLAALGKIANSNGIWFHVDAAYAGSACICPEYRQYIDGVETADSFNMNAHKWFLTNFDCSLL... | Function: Bifunctional enzyme that catalyzes the decarboxylation of L-phenylalanine to 2-phenylethylamine, which is then oxidized to form 2-phenylacetaldehyde, a constituent of floral scent . 2-phenylacetaldehyde is a precursor of 2-phenylethanol, another constituent of floral scent . Catalyzes both the decarboxylation... |
Q9H8K7 | METRTEDGGLTRRPTLASSWDVAGGALTHSLLLTRAGLGPGDFDWEELLAPPAPGQDLVILKRNHNNKDENPCFLYLRCGPDGGEEIASIGILSSARNMEVYLGEEYCGTSRGKNVCTVLDDSEHEKIILYKKNLKLESSTHACKIKLLSFGERQCVFISKVVVHMRSVFANSSTSSPALGSRIDLDKVQTIMESMGSKLSPGAQQLMDMVRCQQRNCIPIGEQLQSVLGNSGYKHMIGLQSSSTLGTLNKSSSTPFPFRTGLTSGNVTENLQTYIDKSTQLPGGENSTKLDECKVMPQNHSFLENDLKNAMASFLPKKV... | Function: ATPase that regulates mitochondrial ABC transporters ABCB7, ABCB8/MITOSUR and ABCB10 . Regulates mitochondrial ferric concentration and heme biosynthesis and plays a role in the maintenance of mitochondrial homeostasis and cell survival .
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (D... |
B6HIC2 | MEAPRSDQAHTDATTPMEAIRTTSLGTNNYGPVPDDYLDLPVREVNDGADLREYITETRTGEIIKPIKSNVTGKTEDWKMVTFTIDDPENPKNWSKAFKWYCTMVVAFTCFVVAFCSSVITADVEGPIEEFGIGREASLVVITVFVIGFGLGPMVFAPMSEIVGRRPVYALTLALAVIFVIPCAVSKNIGTLIVCRLIDGIAFSAPMTLVGGTLADLWKSEERGVPMAAFSAAPFIGPAIGPLVGGYLADNCGWRWLYWIQLILAFVAWVMITFTVPETFAPILLKKRAQKLRKAEDDPKYTTETELDARPMGEKLRIFL... | Function: MFS-type transporter involved in penicillin production, most likely through the translocation of side-chain precursors (phenylacetic acid and phenoxyacetic acid) from the cytosol to the peroxisomal lumen across the peroxisomal membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 60841
... |
Q9CQX4 | MVRTKANYVPGAYRKAVASQAPRKVLGSSTFVTNSSSSSRKAENKYAGGNPVCVRPTPKWQKGIGEFFRLSPKESKKENQAPEEAGTSGLGKAKRKACPLQPDHRDDENE | Function: PCNA-binding protein that acts as a regulator of DNA repair during DNA replication. Following DNA damage, the interaction with PCNA is disrupted, facilitating the interaction between monoubiquitinated PCNA and the translesion DNA synthesis DNA polymerase eta (POLH) at stalled replisomes, facilitating the bypa... |
P79106 | MGVNQSVSFPPVTGPHLVGCGDVMEGQSLQGSFFRLFYPCQEAEETSEQPLWIPRYEYCAGLAEYLKFNKRWGGLLFNLGVGSCRLPVSWNGPFKTKDSGYPLIIFSHGMGAFRTVYSAFCMELASRGFVVAVPEHRDGSAAATCFCKQTPEENQPDNEALKEEWIPHRQIEEGEKEFYVRNYQVHQRVSECVRVLKILQEVTAGQAVLNILPGGLDLMTLKGGIDVSRVAVMGHSFGGATAILALAKEMQFRCAVALDAWMFPLEHDFYPTARGPIFFINAEKFQTVETVNLMKKICDQHHQSRIITVLGSVHRSLTDF... | Function: Catalyzes the hydrolyze of the acetyl group at the sn-2 position of platelet-activating factor (PAF) and its analogs, leading to their inactivation . Hydrolyzes propionyl and butyroyl moieties approximately half as effectively as PAF . Also catalyzes transacetylation of the acetyl group from platelet-activati... |
Q99487 | MGVNQSVGFPPVTGPHLVGCGDVMEGQNLQGSFFRLFYPCQKAEETMEQPLWIPRYEYCTGLAEYLQFNKRCGGLLFNLAVGSCRLPVSWNGPFKTKDSGYPLIIFSHGLGAFRTLYSAFCMELASRGFVVAVPEHRDRSAATTYFCKQAPEENQPTNESLQEEWIPFRRVEEGEKEFHVRNPQVHQRVSECLRVLKILQEVTAGQTVFNILPGGLDLMTLKGNIDMSRVAVMGHSFGGATAILALAKETQFRCAVALDAWMFPLERDFYPKARGPVFFINTEKFQTMESVNLMKKICAQHEQSRIITVLGSVHRSQTDF... | Function: Catalyzes the hydrolyze of the acetyl group at the sn-2 position of platelet-activating factor (PAF) and its analogs, leading to their inactivation . Hydrolyzes propionyl and butyroyl moieties approximately half as effectively as PAF (By similarity). Also catalyzes transacetylation of the acetyl group from pl... |
Q13177 | MSDNGELEDKPPAPPVRMSSTIFSTGGKDPLSANHSLKPLPSVPEEKKPRHKIISIFSGTEKGSKKKEKERPEISPPSDFEHTIHVGFDAVTGEFTGMPEQWARLLQTSNITKLEQKKNPQAVLDVLKFYDSNTVKQKYLSFTPPEKDGFPSGTPALNAKGTEAPAVVTEEEDDDEETAPPVIAPRPDHTKSIYTRSVIDPVPAPVGDSHVDGAAKSLDKQKKKTKMTDEEIMEKLRTIVSIGDPKKKYTRYEKIGQGASGTVFTATDVALGQEVAIKQINLQKQPKKELIINEILVMKELKNPNIVNFLDSYLVGDELF... | Function: Serine/threonine protein kinase that plays a role in a variety of different signaling pathways including cytoskeleton regulation, cell motility, cell cycle progression, apoptosis or proliferation . Acts as downstream effector of the small GTPases CDC42 and RAC1 . Activation by the binding of active CDC42 and ... |
Q61036 | MSDSLDNEEKPPAPPLRMNSNNRDSSALNHSSKPLPMAPEEKNKKARLRSIFPGGGDKTNKKKEKERPEISLPSDFEHTIHVGFDAVTGEFTPDLYGSQMCPGKLPEGIPEQWARLLQTSNITKLEQKKNPQAVLDVLKFYDSKETVNNQKYMSFTSGDKSAHGYIAAHQSNTKTASEPPLAPPVSEEEDEEEEEEEDDNEPPPVIAPRPEHTKSIYTRSVVESIASPAAPNKEDIPPSAENANSTTLYRNTDRQRKKSKMTDEEILEKLRSIVSVGDPKKKYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQP... | Function: Serine/threonine protein kinase that plays a role in a variety of different signaling pathways including cytoskeleton regulation, cell migration, or cell cycle regulation. Plays a role in dendrite spine morphogenesis as well as synapse formation and plasticity . Acts as downstream effector of the small GTPase... |
Q8AXB4 | MSDSVDIEEKPPAPPLRMNSNNRDSSALNHCSKPLPMAPEEKNKKARLRSIFPGGGDKTNKKKEKERPEISLPSDFEHTIHVGFDAVTGEFTPDLCGSQMGTGKLPEGIPEQWARLLQTSNITKLEQKKNPQAVLDVLKFYDSKETVNNQKYMSFTSGDKSAHGYIAAHSLNAKTASEPPLAPPVSEEEDEEEEEEEDDNEPPPVIAPRPEHTKSIYTRSVIEPVALTAPAKEASTSPVTPQPENSNSSTSTLYRNTDRQRKKSKMTDEEILEKLRSIVSVGDPKKKYTRFEKIGQGASGTVYTAIDIATGQEVAIKQMN... | Function: Serine/threonine protein kinase that plays a role in a variety of different signaling pathways. Involved in early neuronal development; required for cell cycle exit and differentiation of primary neurons. May be required for the formation of dendritic spines and excitatory synapses (By similarity). Cooperates... |
O96013 | MFGKRKKRVEISAPSNFEHRVHTGFDQHEQKFTGLPRQWQSLIEESARRPKPLVDPACITSIQPGAPKTIVRGSKGAKDGALTLLLDEFENMSVTRSNSLRRDSPPPPARARQENGMPEEPATTARGGPGKAGSRGRFAGHSEAGGGSGDRRRAGPEKRPKSSREGSGGPQESSRDKRPLSGPDVGTPQPAGLASGAKLAAGRPFNTYPRADTDHPSRGAQGEPHDVAPNGPSAGGLAIPQSSSSSSRPPTRARGAPSPGVLGPHASEPQLAPPACTPAAPAVPGPPGPRSPQREPQRVSHEQFRAALQLVVDPGDPRSY... | Function: Serine/threonine protein kinase that plays a role in a variety of different signaling pathways including cytoskeleton regulation, cell migration, growth, proliferation or cell survival. Activation by various effectors including growth factor receptors or active CDC42 and RAC1 results in a conformational chang... |
Q9P286 | MFGKKKKKIEISGPSNFEHRVHTGFDPQEQKFTGLPQQWHSLLADTANRPKPMVDPSCITPIQLAPMKTIVRGNKPCKETSINGLLEDFDNISVTRSNSLRKESPPTPDQGASSHGPGHAEENGFITFSQYSSESDTTADYTTEKYREKSLYGDDLDPYYRGSHAAKQNGHVMKMKHGEAYYSEVKPLKSDFARFSADYHSHLDSLSKPSEYSDLKWEYQRASSSSPLDYSFQFTPSRTAGTSGCSKESLAYSESEWGPSLDDYDRRPKSSYLNQTSPQPTMRQRSRSGSGLQEPMMPFGASAFKTHPQGHSYNSYTYPR... | Function: Serine/threonine protein kinase that plays a role in a variety of different signaling pathways including cytoskeleton regulation, cell migration, proliferation or cell survival. Activation by various effectors including growth factor receptors or active CDC42 and RAC1 results in a conformational change and a ... |
Q9NQU5 | MFRKKKKKRPEISAPQNFQHRVHTSFDPKEGKFVGLPPQWQNILDTLRRPKPVVDPSRITRVQLQPMKTVVRGSAMPVDGYISGLLNDIQKLSVISSNTLRGRSPTSRRRAQSLGLLGDEHWATDPDMYLQSPQSERTDPHGLYLSCNGGTPAGHKQMPWPEPQSPRVLPNGLAAKAQSLGPAEFQGASQRCLQLGACLQSSPPGASPPTGTNRHGMKAAKHGSEEARPQSCLVGSATGRPGGEGSPSPKTRESSLKRRLFRSMFLSTAATAPPSSSKPGPPPQSKPNSSFRPPQKDNPPSLVAKAQSLPSDQPVGTFSP... | Function: Serine/threonine protein kinase that plays a role in the regulation of gene transcription. The kinase activity is induced by various effectors including AR or MAP2K6/MAPKK6. Phosphorylates the DNA-binding domain of androgen receptor/AR and thereby inhibits AR-mediated transcription. Inhibits also ESR1-mediate... |
Q3ULB5 | MFRKKKKKRPEISAPQNFQHRVHTSFDPKEGKFVGLPPQWQNILDTLRRPKPVVDPSRITRVQLQPMKTVVRGSSVPTEGYISGLLNDIQKLSVISSNTLRGRSPTSRRRAQSLGLLGDDQWAADPDMYLQSPQSEHTDPHGLYLSCNGGTPAGHRQVPWPEPQSPQALPNGMAAKAQSLGPAEFQGASQRCLQQLGACLQSSPPGTSPPMATGRRGVKVAKHSSEEARPQSCLVGSAIGRPGGEGSPSPKNQESSLKHRLFRSMFLSTPATGAASSSKPVPLPQNKPNSAFRPPQKDSSSNLVAKAQSLPSEQPMGTFS... | Function: Serine/threonine protein kinase that plays a role in the regulation of gene transcription. The kinase activity is induced by various effectors including AR or MAP2K6/MAPKK6. Phosphorylates the DNA-binding domain of androgen receptor/AR and thereby inhibits AR-mediated transcription. Inhibits also ESR1-mediate... |
Q869N2 | MEQSKRVSMMREKFEAQSNEAESSPPPNRKPPPPNKRVQTNGTSSLNSSGSSFVSPSPSPSPSPQQPVKRPLPSPGVNKQAPPALPTQPRPQQQQPEIPVRPTTPTRTPPNLINSNGTSGGSGFSSSSGNSGYSSSNNNNSNSNSSINMNGNHSNGLNGGSSNPVPMRKVSSPINIANGTTPPPPPQPTPSQQPQQSPSSASHNNTQHNIPSPPPLPNNKPKKLAPTAVPAGLGSIIGGPKTPAISPGSTSPSLGSSNGNIPISTTSTPITPTPPISVPLATSPNNSHKDSISNSNSNNNNNNNNNNNNNSSNATTSPPS... | Function: Regulator of the myosin I component of the cytoskeleton: required for regulation of cytokinesis, phagocytosis and pinocytosis.
PTM: Autophosphorylated at Ser-8. This may stimulate interaction with GTP-bound Rac family members which then further stimulates autophosphorylation and kinase activity.
Catalytic Act... |
Q8K9U6 | MESITISKIQNWKKNQIKFAAITAYDFSFSRLFEKEGIPIMLVGDSLGMTIQGHNSTLPVKIQDIKYHTKAVRRGAPNSFLLSDLPFMSYYSIEETLKNTAKIIQSGANMIKIEGGKWLVETVKELSKRSILVCGHIGLTPQSINFLSGYKIQGKEKNDAQRIIDEAFILEEAGIKMLVLECIPSLLAKKITENLSIPVIGIGSGHHTDGQILVMQDLLGITDGKKLKFVKNFLCHNGSIQNAIKQYINEVKNGNFPSEKYSF | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5... |
Q2SYZ1 | MTYLQESSRPAVTVPKLQAMREAGEKIAMLTCYDASFAALLDRANVDVQLIGDSLGNVLQGQTTTLPVTLDDIAYHTACVARAQPRALIVADLPFGTYGTPADAFASAVKLMRAGAQMVKFEGGEWLAETVRFLVERAVPVCAHVGLTPQSVHAFGGFKVQGKTEAGAAQLLRDARAVEEAGAQLIVLEAVPTLVAAEVTRELSIPTIGIGAGAECSGQVLVLHDMLGVFPGKRPRFVKDFMQGQPSIFAAVEAYVRAVKDGSFPGPEHSF | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5... |
B1Y4K8 | MSSHAEPTPVARNRKPLTLPALRAMQQRGEKIAMLTAYESTLARVADEAGVDTILVGDSLGMVVQGHASTLPVTLDEMAYHTRCVARGLQGGAAWLVADLPFASYHQGPSQAMAAAATLMQAGAQMIKLEGGGWTAETVRFLVERGVPVCAHLGLTPQSVHALGGYRIQGRDEAGAAELRRQATELTQAGAAMMVLELMPSAVAAAVQADNPQLMTIGIGAGPATAGQVLVVHDMLGLTRGKLPRFVRNFMHSEAGQNLSVEDAIRAYVAAVKDASFPDPVAHAYASAS | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5... |
Q72MN0 | MKNIHKIFSPEKKGKEKISVVTCYDFSFARILNETEIDSILVGDSLGMVFQGNTSTLPVTLEEMIYHTKAVRRGAPDKFLIADLPFLSYQTSIEEGIRSAGKIMKESDCDAVKIEGGSEFICELVSILKQIGVPVMGHLGLTPQSVHVFGGHRVQGKGEESSSKLLKESISLFESGVFSMVLEMIPAELGKKVSQEVGVPTIGIGAGSDCDGQVLVLNDLLGLDINFQPKFLKKFSNLHSIVKEAIADYDKEVKSGEFPGKDHSF | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5... |
Q8Y601 | MKRPVDFFAMKENGEKITMITAYDYPSAKNVEQAEADMILVGDSLGMVVLGYDSTVPVTIDDMIHHTKAVKRGATDTFIVTDMPFMTYHGSVNETIQNARKIIQESGAHAVKLEGAGEVVNKIARLTEAGAPVVAHLGLTPQSVGLTGSYKVRAKSAQEAQELMDNALAVEAAGAIAIVLEAIPRQLAEKVSKALSIPTIGIGAGLETDGQVLVYHDIIGYGISRRAKFVKAYADIDETIEPALASYVKEVKAETFPEVKHSFTMAEEDLKGLYGRE | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5... |
A0L3M6 | MKKRVRVPDLVRMKQQGEPIVALTAYDYTLARLVDAADVDLVLVGDSLGMVVQGHETTLPVTLDEMIYHTRAVARGCQRALVVLDMPFGSTQNGPERTFEQAARAMKESGAAAIKLEGGQAMAATVAYLTERAIPVIGHLGLTPQSVHAFGGFKIQGRDQAAAQRIADDALALQQAGAGAIILEGIPAALAQQVSQSLTIPTIGIGAGVGCDGQVLVIYDMLGLYGDLAPKFVKRYLDGVPVIGGAIGAYVQEVRNRQFPTPDHSFEK | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5... |
Q2LTJ5 | MSTQSKGRKITTSVIRGMKKKGEKITMLTAYDYAMASLLDEVGVEMLLVGDSLGMVVLGYESTLPVTMNDMLHHTRAVSRGANNAMVVADLPFMSYQCSVEEAVRNAGRFLQEAGAHAVKLEGGREIAESVKRMTVSGIPVVGHLGLTPQSVQQFGGFKVQGKGDAAAQRIMEDAKIIEEAGAFSVVLECVPAPLAQRITDDLAIPTIGIGAGAGCDGQVLVVNDMLGIYERFTPKFVKKYANLSDNIRGAVKQYIEEVKNGTFPDQDHSFL | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5... |
Q31KK8 | MPITPRHLRQWKQQGRPIVALTAWDFAIASILDEAGIDLVLVGDSLAMVALGHPTTLPLSLEDMIHHVQAVQRGCRNALIVSDLPFLSYQTSPEDAILAAGQLLKVTEAQAVKLEGGYPRLLETVQRLVEVGIPVMGHVGLTPQSVRQLGYRQQGQTPEAQQQILDQALALEAAGAFAIVLEHIPDRLAAMITAKLSIPTIGIGAGPNCDGQILVTADLLGLTPSQPPFAPAYLNLRQAIGSAVQRYAREVRDRQFLQSQPAEQEPLS | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5... |
Q2JRY1 | MAALSIHHFRQAKQAGQPLVALTAADYATAQILDRAGIDLILVGDSLAMTSLGHSSTLPLTLEQMIHHAQAVRRGVERAFLVADLPFLSYQVCKEQALLSAGRLMKEAGVNGVKLEGGYPDMVETVAFLVQRGIPVLGHIGLTPQAKHQLGGYRQQGKTPSEAERLRQEALSLERAGAFALVLEHMPAELAAQITQQVGIPTLGIGAGPACDGQILVTHDLLGLSERIPPFAKAYANLREVIREAVEAFVGDVHQRLFPPT | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5... |
Q0IC75 | MRPAELIRFKQSGRAITMLTAWDALSAALVEEAGADVVLVGDSLAMVVLGHATTLPVTLEHMLHHTQAVCRGMSKPLAQQPLVVCDLPFLSYQCGLDRAVAAAGTILKESDAAAIKLEGGEPEIVAVVDRLVRMGIPVMGHLGLTPQAVHRLGYRRQGIDPRSQDKLHRQAQALQDAGCFSLVVEHVPSELAGRLRRTLSIPVIGIGAGPDCDGQVSVTADLLGLTPSQPPFTPARMQGRELSINALKSWLKEQRDQRATPTTPPPPPAPDC | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5... |
Q0B0P6 | MARVTVSVLKDKKKRKEKISMLTAYDYSLAGMVDEAGIDMILVGDSLGNVVLGYDNTLAVTMDDMIHHSKTVVRASKNAMVVGDMPFLSYHISKKEAVRNAGRFIQEAGCSAVKLEGGSERVDTVKAILDAQIPVMGHIGLTPQSVHQFGGFKVQGKDLETAKKLVEDARALDQAGVYCIVLECVPSELARRVTEEISVPTIGIGAGPYCDGQVLVINDMLGMFRGFTPKFVRKFANLEPLIMEALKNYKAEVEAGTFPAEEHCFTIKEEVLDRLY | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5... |
Q5JCY6 | MREITPRKIIEMKGKEKIAMVTAYDYPSALLADKAGMDIVFVGDSLGMVVYGEPNTLNVSMEQMVFHTRAVAKAVKRALVLADMPFGSYEVSVEEGVKNAMRLIRAGADAVKIEGGYDHKKLVKKLVRMGIPVMGHTGLTPQRYLRLGGYRLMGETEEEIEEILRDAKALEKAGAFAVVLEFVLADVAKLVTEEVSIPTIGIGAGPHVDGQVLVWHDLLGIYENVPPFVKKYADLASIIQLALENYRGEVKEGRFPAKEHYWEFLDKDDFERKKMKALERLEDE | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5... |
Q9X251 | MNVEKLKKMKGKEKIVMVTAYDAPSARIARDAGIDVILVGDSLGNNVLGYENTIPVTMEEMLIHVAAVKRGAPDAFIVADMPFLSYQTSVEKAVENAGKFLKVGANAVKIEGGEEFGELVQKLVESGIPVMGHIGLTPQFVNRFGGYRVQGKTEKNREYLLRSARELEKRGAFAIVLELVVEEVAKEITESVSIPTIGIGSGRFCDGQVLVWHDLLGLNPDFAPRFSKKYANLYEVILKALQEFRREVKKGLFPTEEHSFTDKSKGGVSS | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5... |
Q3A9L1 | MRFFTEIKPLKTYVAEQKREGKIIGFVPTMGYLHDGHLSLVRKAKLQADVVIVSIFVNPLQFGPNEDFAKYPRDLERDLALLQEEGVDCVFAPSAEEMYKEGFSTFVEVNGEITEVMCGKSRPGHFKGVATVVTKLFNIVTPDLAFFGQKDAQQLFIIEKLVRDLNLNVEIVSVPTRREEDGLAMSSRNTYLNPEERKAATILYRALKRGEELVLAGERNPERLKKLIEEFIKTEPLARIDYVEVRSVPDLKAMDVIKGKFIIALAVYIGSTRLIDNFILEVD | Function: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
Catalytic Activity: (R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+)
Sequence Mass (Da): 32102
Sequence Length: 283
Pathway: Cofactor biosynthesis; (R)-pan... |
Q9A6C8 | MTSPIIVRTVAEMREHVRAWKAAGQRVAVVPTMGALHEGHLSLVRLAQQHAERVIATVFVNPKQFAPHEDFDAYPRGEAADAEKLALVGCDLLFAPNATEMYAPGFSTLVSVSGVSEPLEGAARPQFFGGVATVVAKLFIQSQADVAVFGEKDYQQLQVVRRMARDLDIPVEIIGAPTARAEDGLALSSRNAYLSAEERAAAVALPTAMKAAAAAVAQGGPIEDAERSAVAALQAAGFGQVDYVEIREASDLSRLGPGPIGEASGRILVAAWLGKTRLIDNMAVG | Function: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
Catalytic Activity: (R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+)
Sequence Mass (Da): 30052
Sequence Length: 285
Pathway: Cofactor biosynthesis; (R)-pan... |
Q3J5N0 | MPPVLRTVAELRARVSDWKAAGETVGVVPTMGALHEGHLSLARRARAACDRVIVTIFVNPRQFNNPADLEKYPRTEAQDAALLASVGVDAVFAPGPEEVYPRGFATNVSVSGVSEPLEGAHRPGHFDGVATVVAKLFGMTRADRAFFGEKDWQQLMVVQRLVADLNIPVTIEGCATVREADGLALSSRNRRLSVEGRARAPALVRAMQAAAEAMRGGRAIPEALAEARAAVLAAGFETVDYLELRTADLLLPMERLQGEGRLLAAATLDGVRLIDNIPV | Function: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
Catalytic Activity: (R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+)
Sequence Mass (Da): 29877
Sequence Length: 279
Pathway: Cofactor biosynthesis; (R)-pan... |
B8G643 | MQVVHTIAEARRARAAFDELGFVPTMGYLHQGHLALVERARAECPAVAVSIFVNPTQFGPHEDYARYPRDTARDLALLEAAGVDLVFIPTVEEMYPAGFGTYVIQPAADEVLEGAARPGHFRGVATVVCKLFNIIQPTKSYFGQKDAQQTVVVRQMVRDLNIPVEIVIVPTVREPDGLALSSRNVYLTPEQRAAAPVLYRALRAAAERYAAGERSGEVLRAVMREVLSTEPLAKPEYVSVAHPHTLRELDQIGPEGALLSMAVRFDQVRLIDNWLLL | Function: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
Catalytic Activity: (R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+)
Sequence Mass (Da): 30594
Sequence Length: 277
Pathway: Cofactor biosynthesis; (R)-pan... |
B3QSB4 | MKIIETVSEMQHFSESLRIAEKRLGVVPTMGALHDGHLSLVKLALKHADVAIMTIFVNPLQFGPSEDFAKYPRTFERDAMLAEKAGVSCIFAPTPETLYPSGFQTHVTVDEITQGFEGELRPGHFRGVTTVVAKLFNITKPHVAVFGEKDAQQLAAIRKMQKDLNFDVEIVPAPIVRETDGLAKSSRNIYLNPAERKQAVVLNESLEIAKSAIQHGERNVKTLLEVLNRHIQSAPLAEPDYIAIVDAESFQPVQEELLAEETYLVLLTVRFGSTRLLDNCRIEL | Function: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
Catalytic Activity: (R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+)
Sequence Mass (Da): 31641
Sequence Length: 284
Pathway: Cofactor biosynthesis; (R)-pan... |
Q8KBY5 | MQIINDPAEMQKIAEKLRLQHQYIGVVMTMGALHEGHLSLVKLAKAHAGTVIMTIFVNPTQFGPNEDFYRYPRPFEQDAALARSAGVDYLFAPSTEAMYPDGYSTSIDPGPIATRFEGASRPGHFGGMVTVVVKLLGITRPHLAVFGEKDAQQLAIIRRVVTDLNIGTTILGAPIVRESDGLATSSRNIYLSSNERQQATVLYRAIRYAKMEIDKDRTDLEAIAGEAEALVRSEPDAEPDYLCFVDDATFEPVTQAVTGKAYRLIMAVRIGSTRLIDNWRFDYQ | Function: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
Catalytic Activity: (R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+)
Sequence Mass (Da): 31471
Sequence Length: 284
Pathway: Cofactor biosynthesis; (R)-pan... |
A0M787 | MQVFREKQLLIQAIQKVKSDGKSIGLVPTMGALHEGHLSLVTNALKDSDQVIVSIFVNPTQFDNPEDLEKYPRNLNKDIELLEKETSDIWVFSPTANELYGDKILSQNFDFEGLESVMEGEFRAGHFNGVGTVVKHLFEVITPDKAFFGEKDFQQLQIIRKLIEKTGLPVEIVGCPILREDSGLARSSRNERLSFQNRKEAAFIYEVLQNANRLFGTESAEHTTNWVENQFKNNQHLKLEYFEIADSETLKKVNKKEKGKQYRAFIAAYSDGIRLIDNIALNN | Function: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
Catalytic Activity: (R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+)
Sequence Mass (Da): 32284
Sequence Length: 283
Pathway: Cofactor biosynthesis; (R)-pan... |
O24210 | MAAPREPEVIRDKAAMRAWSRRRRAEGKTVAVVPTMGYLHQGHLSLISAAAAAASADPVAIVVTIYVNPSQFAPSEDLATYPSDFAGDLRKLASTGVVDAVFNPPDLYVRGAGRRGAASGGAISCLEEAAGDGHETWVRVERLEKGMCGASRPVFFRGVATIVSKLFNIIEPDVAVFGKKDYQQWRVICRMVRDLDFAIEIIGSEIVREADGLAMSSRNVHLSREEREKALSISRSLVDARTGALKGNTDCKQIKNKIVQTLTETGGQVDYVEIVEQESLVPVEQIDGPVVICVAAWFGKVRLIDNIEIDTRS | Function: Catalyzes the condensation of pantoate with beta-alanine to form pantothenate. Essential for panthotenate biosynthesis (Probable).
Catalytic Activity: (R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+)
Sequence Mass (Da): 34039
Sequence Length: 313
Pathway: Cofactor biosynthesis; ... |
Q4FLP6 | MFYLLIFLLQMKLIKLKTDLIKAIELDRRLGFVPTMGSLHEGHKTLIKTSQKNCKKTLVSIFINPTQFNNKKDYKTYPKNLKQDLSYLKKLKVDYVYLPTIKQIYWKKNNEIKLNKSQKILCAKFRKGHFEGVLNVLDRFIELISPQKMFMGEKDFQQFFLVKNYIENKYNTKVHVCKTVREKNKLALSSRNSLLNKKSFINSGIIAKKLLSLKNEIKKNKKNYKKMIFYLKEELSKNFDIKIEYLECRNTHNLSTNIMNKPFKLFVAYYINNVRLIDNF | Function: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
Catalytic Activity: (R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+)
Sequence Mass (Da): 33382
Sequence Length: 280
Pathway: Cofactor biosynthesis; (R)-pan... |
A4SWJ8 | MKIISDIQELRDHLRGQNRASFVPTMGNLHEGHLSLMRLARQHGDPVVASIFVNRLQFGPNEDFDSYPRTMQADIEKLEKEGVYILFAPTERDLYPQPQEYRIDPPQQLGDILEGEFRPGFFKGVCTVVLKLFSCVQPKVAVFGKKDYQQLMIIRQMAKQFALPVEIIPGETIRAEDGLALSSRNGYLSVEERAEAPELQRVLQQVREQVLGLKHRDVSSLLEIEKKAIATLAGRRWEPDYIAIRQQGDLAPASNEQLQAGEPLVILTAAKLGKTRLIDNLEI | Function: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
Catalytic Activity: (R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+)
Sequence Mass (Da): 32025
Sequence Length: 283
Pathway: Cofactor biosynthesis; (R)-pan... |
B0C321 | MHRTFLFSKIHHCTLTETNLEYVGSISIDQTLLDAAGIVPYEQVQVVNMNNGERLVTYAIPAPADSGAVELNGAAARLGTRGDRVIIMTYAQLTSEEIEGFEPRVVLVDQENRVIEDAPVVNASTPELCLT | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.
PTM: Is synthesized initially as an inactive proenzyme, which is activated by self-cleavage at a specific serine bond to produce a beta-subunit with a hydroxyl group ... |
A3DDV5 | MFITLMKSKIHRATVTEANLDYVGSITIDEDLMEAADIMENEKVQVVDNNNGNRFETYVIKGERGSGMICLNGAAARLVHPGDLIIIISYGIFDREEAKTFNPKVVFVDEKNKIINIKSEEKHGEI | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.
PTM: Is synthesized initially as an inactive proenzyme, which is activated by self-cleavage at a specific serine bond to produce a beta-subunit with a hydroxyl group ... |
Q6F8I6 | MLSRLLKCKIHRAVVTHAELHYEGSCAIDGVLMDLAGIREYEEIHVWNVTNGKRFTTYAIRGEDHSGIISVNGGAAHQAEVGDLVIIATFGDFTEVEANAHKPRLVYANPDNTVNHTANCIPVQVA | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.
PTM: Is synthesized initially as an inactive proenzyme, which is activated by self-cleavage at a specific serine bond to produce a beta-subunit with a hydroxyl group ... |
A8ERX9 | MTFEMLYSKIHRATVSDANLNYVGSITIDEDLMKAANLRVGQKVDIVNINNGERFQTYIIKGKAGSKDMCLNGAAARKVEIGDKIIVIAYATFSEAELENYKPTVVLVDDKNNIELITHELEGGKYV | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.
PTM: Is synthesized initially as an inactive proenzyme, which is activated by self-cleavage at a specific serine bond to produce a beta-subunit with a hydroxyl group ... |
Q31FF9 | MQITLLKSKLHRVTTTHSELDYEGSCAIDGHFLEVAGIREYEQIQIYNVNNGNRFTTYAIRAEENTGIISVNGAAAHKAAPGDLLIIATYASMDEKEAEEFKPIMVYFDEKNQITHTRNTIPKQMQQLA | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.
PTM: Is synthesized initially as an inactive proenzyme, which is activated by self-cleavage at a specific serine bond to produce a beta-subunit with a hydroxyl group ... |
C5CEQ3 | MFRIMQKSKIHRATVTDKNLNYEGSITIDYRLMKLADIRENELVQVVNINNGERFETYVIKGEEGSGVIALNGAAARLAEIGDRVIIISYAIYNDDEYKPPKIVKVTEKNEPIEK | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.
PTM: Is synthesized initially as an inactive proenzyme, which is activated by self-cleavage at a specific serine bond to produce a beta-subunit with a hydroxyl group ... |
B1Y852 | MFRTLLKSKIHRAVVTHCELHYEGSCGIDEDLLDAANLCENEQIHVWNINNGERFVTYVIKAPRGSGIISLNGSAARRASAGDLVIIAAFAQVHEEQVPTHQPKLVFMDEANRIKELRSEPQNPPQTSPLR | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.
PTM: Is synthesized initially as an inactive proenzyme, which is activated by self-cleavage at a specific serine bond to produce a beta-subunit with a hydroxyl group ... |
Q8CVE9 | MQITVMKGKIHRATVTDADLNYEGSLTVDMDLVDAAGMRVYEKVSVVNVNNGARFETYIIEGKRGSGEICLNGAAARLGMKGDKIIIITYAQVEEQELASDYTPKVVHVDEKNRKR | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.
PTM: Is synthesized initially as an inactive proenzyme, which is activated by self-cleavage at a specific serine bond to produce a beta-subunit with a hydroxyl group ... |
O67619 | MVMKFLIVGVGAIGSAYLAFLTRAGHEAAGLVRRNPVNRIKVEGIWGEFEIPVKTFTKVEEVPFIPDIVIISVKSYDTEEALKKVKPVVGENTFIMIAQNGYGNYEKAVEIYGEGKVILSRIIFGSKVIKPGHIRITVSADEVVIGDPSGKIDEEFLKNLARTFTEAGIPTRYERDVYKYLVDKIIYNSALNPLGALFEVNYGSLAENPHTKELMNRVIDEIFQVIEKAKLPCFWKSADEYKKVFYEKLIPPTAEHYPSMLEDVKKGKTEIEALNGAIVELGKKYGVSTPTNEFITKMVKAKELFNLKDT | Function: Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid.
Catalytic Activity: (R)-pantoate + NADP(+) = 2-dehydropantoate + H(+) + NADPH
Sequence Mass (Da): 34776
Sequence Length: 310
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step... |
F4KIN4 | MESRCKKGYFRLAVIGLSKAKDCWEKNACAVTFIGDGGTSEGDFHAGLNFAAVMEAPVVFICRNNGWAISTHISEQFRSDGIVVKGQAYGIRSIRVDGNDALAVYSAVCSAREMAVTEQRPVLIEMMIYRVGHHSTSDDSTKYRAADEIQYWKMSRNSVNRFRKSVEDNGWWSEEDESKLRSNARKQLLQAIQAAEKWEKQPLTELFNDVYDVKPKNLEEEELGLKELIEKQPQDYMMLKELIPNWILGIGTLALRYDFQETLFNGWHAIAELQQLKLKIKLNSLLNDQADTESLKAARNSALNVIQAMIIHLVLTLKGR... | Function: Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid.
Catalytic Activity: (R)-pantoate + NADP(+) = 2-dehydropantoate + H(+) + NADPH
Sequence Mass (Da): 41601
Sequence Length: 365
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step... |
O28578 | MRVQRVQIMGAGALGSLVGALIQLAGYDVIFVARGKQLEALKKGLRVSGLKNAELKVYCTSQPEDADITFVTVKAYDTETVAKKLAEVDAGVVCSLQNGVGNEEILAKYCRKVLGGVTTYGANLKDYGHVVYAGEGYTYVGEMDGRVSGEAEMVAEVLRDAGMRAEAVNDIEFRIWAKAVVNAAINPITAICRVKNGEVVRNPHLWEVARAVADEGRQVMARMGYEFDAASEVRKVAEMTAENRSSMLQDLERGKRTEVEFINGAIVKKGEEFGIDCAVNRTLLNLVRGVESGL | Function: Catalyzes the NAD(P)H-dependent reduction of ketopantoate into pantoic acid.
Catalytic Activity: (R)-pantoate + NAD(+) = 2-dehydropantoate + H(+) + NADH
Sequence Mass (Da): 31885
Sequence Length: 294
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis.
Subcellular Location: Cytoplasm
EC: 1.1.1.169
|
O34661 | MKIGIIGGGSVGLLCAYYLSLYHDVTVVTRRQEQAAAIQSEGIRLYKGGEEFRADCSADTSINSDFDLLVVTVKQHQLQSVFSSLERIGKTNILFLQNGMGHIHDLKDWHVGHSIYVGIVEHGAVRKSDTAVDHTGLGAIKWSAFDDAEPDRLNILFQHNHSDFPIYYETDWYRLLTGKLIVNACINPLTALLQVKNGELLTTPAYLAFMKLVFQEACRILKLENEEKAWERVQAVCGQTKENRSSMLVDVIGGRQTEADAIIGYLLKEASLQGLDAVHLEFLYGSIKALERNTNKVF | Function: Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid.
Catalytic Activity: (R)-pantoate + NADP(+) = 2-dehydropantoate + H(+) + NADPH
Sequence Mass (Da): 33287
Sequence Length: 298
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step... |
Q9ABG6 | MTSIAVIGPGAVGGTLAAWLAQKPDHVVTVCVRTPFEALAVETPEGAISATPRVATSPESLAPVDWVLVTTKTYDTDATWTWLDALVGPQTRVAILRNGVEHVAPFVGKIAAERLVPAVVDIPAERSAPGRMLQRRNGWIKVPVGPAGEAFAALFAHTPIELHVVEDFVTEAWKKLALNCAGAVNALVLKPAGIAHDEGAAQVMRSLVRECVAVGRAEGADLSDDLPDQVIAGYRAADPGSVNSLHADRAAGRAMELDARNGVIVRRGAAHGIATPANAMVVALLNAAAL | Function: Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid.
Catalytic Activity: (R)-pantoate + NADP(+) = 2-dehydropantoate + H(+) + NADPH
Sequence Mass (Da): 30189
Sequence Length: 290
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step... |
P0A9J4 | MKITVLGCGALGQLWLTALCKQGHEVQGWLRVPQPYCSVNLVETDGSIFNESLTANDPDFLATSDLLLVTLKAWQVSDAVKSLASTLPVTTPILLIHNGMGTIEELQNIQQPLLMGTTTHAARRDGNVIIHVANGITHIGPARQQDGDYSYLADILQTVLPDVAWHNNIRAELWRKLAVNCVINPLTAIWNCPNGELRHHPQEIMQICEEVAAVIEREGHHTSAEDLRDYVMQVIDATAENISSMLQDIRALRHTEIDYINGFLLRRARAHGIAVPENTRLFEMVKRKESEYERIGTGLPRPW | Function: Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid.
Catalytic Activity: (R)-pantoate + NADP(+) = 2-dehydropantoate + H(+) + NADPH
Sequence Mass (Da): 33871
Sequence Length: 303
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step... |
Q9HRF0 | MRVVVQGPGSLGSLVGGVLAGGETAVTLLGHQSEHLTRVREDGLRVVQPDGTTRVTRPSVATDPSVVADADLVVVCVKSYDTASAARALGRQCDGAMVLTLQNGLGNAAVLAEHVPADTVLVGTTTHGAARTEPGVVRHAGGGETTIGRYRGANDARVASVAAAFSTGGMETTVTASPQRAVWEKVLVNVGINAATALADVDNGALVECPPGERVLERAVTEGVRVAEAEGVSVSESVVERARQVAARTASNESSMRQDLAGGARTEVESLHGAVVERARDHDIAVPVIRTLADLVRLAQRDG | Function: Catalyzes the NAD(P)H-dependent reduction of ketopantoate into pantoic acid.
Catalytic Activity: (R)-pantoate + NAD(+) = 2-dehydropantoate + H(+) + NADH
Sequence Mass (Da): 31124
Sequence Length: 303
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis.
Subcellular Location: Cytoplasm
EC: 1.1.1.169
|
Q8Y5L2 | MANQLKVGIIGAGAMGLLYAANFANISELTLFTRRKEQSDLLNQKGLSLKDNSELKNIHIQATVITDAEKLSEQELLIIAVKQYSLKTILPLLRSIPERVPLLFIQNGAAHLDSMPLLGNKRTILLGISEHGAGREDDTTVIWRGHGRTKYSIYQGELNEAVIKILDSNPDFPVEKHASYLDIINEKLFINAVINPLTAVLQVQNGKLLENKEWHELLKTIVKEIQTVLPVENALEKVEVICQVTATNFSSMALDRMNNRMTEIDGIVLPILEKGESLPTLHALYHLIKGLEGESDV | Function: Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid.
Catalytic Activity: (R)-pantoate + NADP(+) = 2-dehydropantoate + H(+) + NADPH
Sequence Mass (Da): 33042
Sequence Length: 297
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step... |
P9WIL0 | MATGIALVGPGAVGTTVAALLHKAGYSPLLCGHTPRAGIELRRDGADPIVVPGPVHTSPREVAGPVDVLILAVKATQNDAARPWLTRLCDERTVVAVLQNGVEQVEQVQPHCPSSAVVPAIVWCSAETQPQGWVRLRGEAALVVPTGPAAEQFAGLLRGAGATVDCDPDFTTAAWRKLLVNALAGFMVLSGRRSAMFRRDDVAALSRRYVAECLAVARAEGARLDDDVVDEVVRLVRSAPQDMGTSMLADRAAHRPLEWDLRNGVIVRKARAHGLATPISDVLVPLLAAASDGPG | Function: Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid.
Catalytic Activity: (R)-pantoate + NADP(+) = 2-dehydropantoate + H(+) + NADPH
Sequence Mass (Da): 31033
Sequence Length: 295
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step... |
Q8YX96 | MNERKYAILGTGALGGYYGAKLQKAGSDVHFLLKSDYEKVNQDGLLVESKDGDFTLPQVNAYNDVAKMPKCDVVVVALKTTQNHLLPKLLPPIVKNDGIVLVLQNGLGVEEEIAEILPQVHIIGGLCFLCSNKVGAGYIHHLDYGQITLGEYAHGYSNMGITDRMQQISHDFQTAGISIELLEDLLLGRWKKLVWNIPYNGLSVVLNARTDELMADTYTRTLVEQLMYEVKAGAKSMGRNIPDSFIQTMLDYTVKMKPYRTSMKIDYDECRPLEVEAIVGNPLHKAQEVGVNLPQINCLYHQLKFLDGRNRTGQLTVDS | Function: Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid.
Catalytic Activity: (R)-pantoate + NADP(+) = 2-dehydropantoate + H(+) + NADPH
Sequence Mass (Da): 35574
Sequence Length: 319
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step... |
Q9HW09 | MTWHILGAGSLGSLWAARLGRAGLPVRLILRDRQRLRRYQQAGGLSLVEDGQASLYPIAAETPDGGQPIQRLLLACKAYDAEEAASSVAHRLAGNAELLLLQNGLGSQQAVAARLPRSRCLFASSTEGAFRDGDFRVVFAGRGHTWLGDPRDTNAPAWLTQLSQAGIPHSWSDDILERLWRKLALNCAINPLTVLHDCRNGGLRQHPEEIAALCDELGQLLHASGYDAAARSLLEDVRAVIDATAANYSSMHQDVTRGRRTEIGYLLGYACQHGQRLGLPLPRLGTLLARLQAHLRQRGLPDR | Function: Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid.
Catalytic Activity: (R)-pantoate + NADP(+) = 2-dehydropantoate + H(+) + NADPH
Sequence Mass (Da): 33062
Sequence Length: 303
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step... |
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