ids
stringlengths 6
10
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stringlengths 11
1.02k
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stringlengths 108
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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, hydroxyproline-rich glycoproteins, lectins and arabinogalactan proteins.
Catalytic Activity: 2-oxoglutarate + L-prolyl-[collagen] + O2 = CO2 + succinate + trans-4-hydroxy-L-prolyl-[collagen]
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 32448
Sequence Length: 288
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.14.11.2
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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, hydroxyproline-rich glycoproteins, lectins and arabinogalactan proteins.
Catalytic Activity: 2-oxoglutarate + L-prolyl-[collagen] + O2 = CO2 + succinate + trans-4-hydroxy-L-prolyl-[collagen]
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 35570
Sequence Length: 316
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.14.11.2
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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, hydroxyproline-rich glycoproteins, lectins and arabinogalactan proteins.
Catalytic Activity: 2-oxoglutarate + L-prolyl-[collagen] + O2 = CO2 + succinate + trans-4-hydroxy-L-prolyl-[collagen]
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 32915
Sequence Length: 290
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.14.11.2
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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, hydroxyproline-rich glycoproteins, lectins and arabinogalactan proteins.
Catalytic Activity: 2-oxoglutarate + L-prolyl-[collagen] + O2 = CO2 + succinate + trans-4-hydroxy-L-prolyl-[collagen]
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 32279
Sequence Length: 288
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.14.11.2
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Q10576 | MRLALLVLATIGYAVADLFTSIADMQNLLETERNIPKILDKYIHDEEERLVQLKKLSEEYSKKNEISIENGLKDITNPINAFLLIKRKIFDWKEIESKMNANKAGNVVSSITDDSYGVRYPTADDLSGAAIGLLRLQDTYRLDTKDLADGKIYADQGNYTFSAKDCFEIARAAYNEHDFYHTVMWMEEAQRRLGDEVEPTVEVEDILEYLAFALYKQNNLKHALKLTEELYKMNPTHPRAKGNVKWYEDLLEQEGVRRSDMRKNLPPIQNRRPDSVLGNTERTMYEALCRNEVPVSQKDISRLYCYYKRDRPFLVYAPIKVEIKRFNPLAVLFKDVISDDEVAAIQELAKPKLARATVHDSVTGKLVTATYRISKSAWLKEWEGDVVETVNKRIGYMTNLEMETAEELQIANYGIGGHYDPHFDHAKKEESKSFESLGTGNRIATVLFYMSQPSHGGGTVFTEAKSTILPTKNDALFWYNLYKQGDGNPDTRHAACPVLVGIKWVSNKWIHEKGNEFRRPCGLKSSDYERFVGDLGYGPEPRNAPNVSPNLAKDVWETL | 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
Sequence Length: 559
Subcellular Location: Endoplasmic reticulum lumen
EC: 1.14.11.2
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P16924 | HTDFFTSIGHMTDLINTEKDLVISKLKDYIKAEESKLEQIKKWAEKLDKLTDTATKDPEGFLGHPANAFKLMKRLNTEWGELESLVLKDMSDGFISNMTIQRQFFPNDEDQTGARKALLRLQDTYNLDTDTLSRGNLPGVKHKSFLTAEDCFELGKIRYTEADYYHTELWMEQALKQLDEGEVSSADKVYILDYLSYAVYQQGDLSKAMMLTKRLLELDPEHQRANGNMKYFEYIMAKEKEANKSSTDAEDQTDKETEVKKKDYLPERRKYEMLCRGEGLKMTPRRQKRLFCRYYDGNRNPRYILGPVKQEDEWDKPRIVRFLDIISDEEIETVKELAKPRLSRATVHDPETGKLTTAHYRVSKSAWLSGYESPVVSRINTRIQDLTGLDVSTAEELQVANYGVGGQYEPHFDFGRKDEPDAFKELGTGNRIATWLFYMSDVSAGGATVFPEVGASVWPKKGTAVFWYNLFPSGEGDYSTRHAACPVLVGNKWVSNKWLHERGQEFRRPCTLSELE | 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
Sequence Length: 516
Subcellular Location: Endoplasmic reticulum lumen
EC: 1.14.11.2
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P13674 | MIWYILIIGILLPQSLAHPGFFTSIGQMTDLIHTEKDLVTSLKDYIKAEEDKLEQIKKWAEKLDRLTSTATKDPEGFVGHPVNAFKLMKRLNTEWSELENLVLKDMSDGFISNLTIQRQYFPNDEDQVGAAKALLRLQDTYNLDTDTISKGNLPGVKHKSFLTAEDCFELGKVAYTEADYYHTELWMEQALRQLDEGEISTIDKVSVLDYLSYAVYQQGDLDKALLLTKKLLELDPEHQRANGNLKYFEYIMAKEKDVNKSASDDQSDQKTTPKKKGVAVDYLPERQKYEMLCRGEGIKMTPRRQKKLFCRYHDGNRNPKFILAPAKQEDEWDKPRIIRFHDIISDAEIEIVKDLAKPRLRRATISNPITGDLETVHYRISKSAWLSGYENPVVSRINMRIQDLTGLDVSTAEELQVANYGVGGQYEPHFDFARKDEPDAFKELGTGNRIATWLFYMSDVSAGGATVFPEVGASVWPKKGTAVFWYNLFASGEGDYSTRHAACPVLVGNKWVSNKWLHERGQEFRRPCTLSELE | 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
Sequence Length: 534
Subcellular Location: Endoplasmic reticulum lumen
EC: 1.14.11.2
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Q60715 | MIWVVLMMAILLPQSLAHPGFFTSIGQMTDLIHNEKDLVTSLKDYIKAEEDKLEQIKKWAEKLDRLTSTATKDPEGFVGHPVNAFKLMKRLNTEWSELENLILKDMSDGFISNLTIQRQYFPNDEDQVGAAKALFRLQDTYNLDTNTISKGNLPGVQHKSFLTAEDCFELGKVAYTEADYYHTELWMEQALTQLEEGELSTVDKVSVLDYLSYAVYQQGDLDKALLLTKKLLELDPEHQRANGNLVYFEYIMSKEKDANKSASGDQSDQKTAPKKKGIAVDYLPERQKYEMLCRGEGIKMTPRRQKRLFCRYHDGNRNPKFILAPAKQEDEWDKPRIIRFHDIISDAEIEIVKDLAKPRLRRATISNPVTGALETVHYRISKSAWLSGYEDPVVSRINMRIQDLTGLDVSTAEELQVANYGVGGQYEPHFDFARKDEPDAFRELGTGNRIATWLFYMSDVSAGGATVFPEVGASVWPKKGTAVFWYNLFASGEGDYSTRHAACPVLVGNKWVSNKWLHERGQEFRRPCTLSELE | 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
Sequence Length: 534
Subcellular Location: Endoplasmic reticulum lumen
EC: 1.14.11.2
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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-proline from L-glutamate 5-semialdehyde: step 1/1.
Subcellular Location: Cytoplasm
EC: 1.5.1.2
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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 1/1.
Subcellular Location: Cytoplasm
EC: 1.5.1.2
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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 1/1.
Subcellular Location: Cytoplasm
EC: 1.5.1.2
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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 1/1.
Subcellular Location: Cytoplasm
EC: 1.5.1.2
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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 1/1.
Subcellular Location: Cytoplasm
EC: 1.5.1.2
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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 1/1.
Subcellular Location: Cytoplasm
EC: 1.5.1.2
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Q12641 | MAAPQVKSSSELTMAVLGCGTMGISILSGILSSLSSIAQDPSPPPTNPPALPRHFIATVRSPSSVAKVESALSPLVKPSVSTLRVLQSTSNVSAAAEADIILLGCKPYMVSGLLSASGMKDALTVKHTEGHARSQKIIISICAGVTVPDLERVLREDVGLSADNLPIVVRAMPNTASKIRESMTVINTVDPPLPDTVTELLTWIFERIGEVVYLPPHLMDACTSLCASGTAFFALMMEAAADGGVAMGLPRAEANRMAAQTMRGAAGLVLEGEHPAILREKVSTPGGCTIGGLLVLEEGGVRAAVARAVREATVVASLLGGGGAKNVNGTRH | 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 1/1.
Subcellular Location: Cytoplasm
EC: 1.5.1.2
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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 | MSAEGYQYRALYDYKKEREEDIDLHLGDILTVNKGSLVALGFSDGQEARPEDIGWLNGYNETTGERGDFPGTYVEYIGRKRISPPTPKPRPPRPLPVAPGSSKTEADTEQPVLTLPDLAEQFAPPDVAPPLLIKLLEAIEKKGLECSTLYRTQSSSNPAELRQLLDCDPPSVDLDVFDEHVLADAFKRYLADLPNPVIPVAVYNEMMSLAQEVPSSEDYIQLLKKLIRSPNIPHQYWLTLQYLLKHFFKLSQASSKNLLNARALSEIFSHVLFRFPAASSDNTEHLIKAVELLISAEWSERQPAPALPPKPPKPTSIANNSMNNNMSLQDAEWYWGDISREEVNEKLRDTADGTFLVRDASTKMHGDYTLTLRKGGNNKLIKIFHRDGKYGFSDPLTFNSVVELINHYRNESLAQYNPKLDVKLLYPVSKYQQDQVVKEDNIEAVGKKLHEYNTQFQEKSREYDRLYEEYTRTSQEIQMKRTAIEAFNDTIKIFEEQCHPQERYSKDYIEKFKREGNEKEIQRIMHNHDKLKSRISEIIDSRRRLEEDLKKQAAEYREIDKRMNSIKPDLIQLRKTRDQYLMWLTQKGVRQKKLNEWLGNENTEDQYSLVDDDEDLPHHDEKTWNVGSSNRNKAENLLRGKRDGTFLVRESSKQGCYACSVVVDGEVKHCVINKTATGYGFAEPYNLYSSLKELVLHYQHTSLVQHNDSLNVTLAYPVYAQQRR | 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 important role in signaling in response to FGFR1, FGFR2, FGFR3, FGFR4, KITLG/SCF, KIT, PDGFRA and PDGFRB. Likewise, plays a role in ITGB2 signaling. Modulates the cellular response to ER stress by promoting nuclear translocation of XBP1 in a ER stress- and/or insulin-dependent manner during metabolic overloading in the liver and hence plays a role in glucose tolerance improvement (By similarity).
PTM: Polyubiquitinated in T-cells by CBLB; which does not promote proteasomal degradation but impairs association with CD28 and CD3Z upon T-cell activation.
Sequence Mass (Da): 83531
Sequence Length: 724
Domain: The SH3 domain mediates the binding to CBLB.
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O00459 | MAGPEGFQYRALYPFRRERPEDLELLPGDVLVVSRAALQALGVAEGGERCPQSVGWMPGLNERTRQRGDFPGTYVEFLGPVALARPGPRPRGPRPLPARPRDGAPEPGLTLPDLPEQFSPPDVAPPLLVKLVEAIERTGLDSESHYRPELPAPRTDWSLSDVDQWDTAALADGIKSFLLALPAPLVTPEASAEARRALREAAGPVGPALEPPTLPLHRALTLRFLLQHLGRVASRAPALGPAVRALGATFGPLLLRAPPPPSSPPPGGAPDGSEPSPDFPALLVEKLLQEHLEEQEVAPPALPPKPPKAKPASTVLANGGSPPSLQDAEWYWGDISREEVNEKLRDTPDGTFLVRDASSKIQGEYTLTLRKGGNNKLIKVFHRDGHYGFSEPLTFCSVVDLINHYRHESLAQYNAKLDTRLLYPVSKYQQDQIVKEDSVEAVGAQLKVYHQQYQDKSREYDQLYEEYTRTSQELQMKRTAIEAFNETIKIFEEQGQTQEKCSKEYLERFRREGNEKEMQRILLNSERLKSRIAEIHESRTKLEQQLRAQASDNREIDKRMNSLKPDLMQLRKIRDQYLVWLTQKGARQKKINEWLGIKNETEDQYALMEDEDDLPHHEERTWYVGKINRTQAEEMLSGKRDGTFLIRESSQRGCYACSVVVDGDTKHCVIYRTATGFGFAEPYNLYGSLKELVLHYQHASLVQHNDALTVTLAHPVRAPGPGPPPAAR | 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, activating signaling cascades involved in cell growth, survival, proliferation, motility and morphology. Binds to activated (phosphorylated) protein-tyrosine kinases, through its SH2 domain, and acts as an adapter, mediating the association of the p110 catalytic unit to the plasma membrane. Indirectly regulates autophagy . Promotes nuclear translocation of XBP1 isoform 2 in a ER stress- and/or insulin-dependent manner during metabolic overloading in the liver and hence plays a role in glucose tolerance improvement (By similarity).
PTM: Phosphorylated in response to signaling from activated receptor-type protein kinases . Dephosphorylated by PTPRJ . Dephosphorylated at Tyr-655 by PTPN13. Phosphorylation of Tyr-655 impairs while its dephosphorylation promotes interaction with FBXL2 and SCF(FBXL2)-mediated polyubiquitination .
Sequence Mass (Da): 81545
Sequence Length: 728
Domain: The SH2 2 domain is required for interaction with FBXL2 and PTPN13.
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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 (pNP-TMP) and p-nitrophenylphosphorylcholine (pNPPC). No catalytic activity was found toward cAMP or cGMP, nucleotides or phospholipase substrates such as phosphatidylcholine. The physiological substrate is unknown.
Sequence Mass (Da): 19039
Sequence Length: 166
EC: 3.1.4.-
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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 | MESLSPGGPPGHPYQGEASTCWQLTVRVLEARNLRWADLLSEADPYVILQLSTAPGMKFKTKTLTDTSHPVWNEAFRFLIQSQVKNVLELSIYDEDSVTEDDICFKVLYDISEVLPGKLLRKTFSQSPQGEEELDVEFLMEETSDRPENLITNKVIVARELSCLDVHLDSTGSTAVVADQDKLELELVLKGSYEDTQTSFLGTASAFRFHYMAALETELSGRLRSSRSNGWNGDNSAGYLTVPLRPLTIGKEVTMDVPAPNAPGVRLQLKAEGCPEELAVHLGFNLCAEEQAFLSRRKQVVAKALKQALQLDRDLQEDEVPVVGIMATGGGARAMTSLYGHLLALQKLGLLDCVTYFSGISGSTWTMAHLYGDPEWSQRDLEGPIRYAREHLAKSKLEVFSPERLASYRRELELRAEQGHPTTFVDLWALVLESMLHGQVMDQKLSGQRAALERGQNPLPLYLSLNVKENNLETLDFKEWVEFSPYEVGFLKYGAFVPPELFGSEFFMGRLMRRIPEPRICFLEAIWSNIFSLNLLDAWYDLTSSGESWKQHIKDKTRSLEKEPLTTSGTSSRLEASWLQPGTALAQAFKGFLTGRPLHQRSPNFLQGLQLHQDYCSHKDFSTWADYQLDSMPSQLTPKEPRLCLVDAAYFINTSSPSMFRPGRRLDLILSFDYSLSAPFEALQQTELYCRARGLPFPRVEPSPQDQHQPRECHLFSDPACPEAPILLHFPLVNASFKDHSAPGVQRSPAELQGGQVDLTGATCPYTLSNMTYKEEDFERLLRLSDYNVQTSQGAILQALRTALKHRTLEARPPRAQT | 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: Peripheral membrane protein
Sequence Mass (Da): 91952
Sequence Length: 818
Domain: The N-terminal C2 domain mediates the association with lipid membranes upon calcium binding (Probable). An additional second C2 domain may stand in between the C2 domain and the PLA2c domain (Probable).
Pathway: Lipid metabolism; fatty acid metabolism.
Subcellular Location: Cytoplasm
EC: 3.1.1.4
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Q50L42 | MQSIPHSDEADVAGMTHASEGHHGLGTSMLVPKNPQGEEDSKLGRNCSGFEDAQDPQTAVPSSPLLSMASCSSQEGSSPCHLLTVRIIGMKNVRQADILSQTDCFVTLWLPTASQKKLKTRTISNCLHPEWDESFTFQIQTQVKNVLELSVCDEDTLTQNDHLLTVLYDLSKLCLRNKTHVKFPLNPEGMEELEVEFLLEENFSSSETLITNGVLVSRQVSCLEVHAESRRPRKRKKNKDLLVMVTDSFENTQRVPPCQEPCYPNSACFHYPKYSQPQLYAEAPKSHCNFRLCCCGTHRNDPVCQPLNCLSDGQVTTLPVGENYELHMKSSPCSDTLDVRLGFSLCQEEVEFVQKRKMVVAKTLSQMLQLEEGLHEDEVPIIAIMATGGGTRSMVSLYGHLLGLQKLNFLDASTYITGLSGATWTMATLYSDPEWSSKNLETVVFEARRHVVKDKMPALFPDQLYKWREDLQKHSQEGYKTTFTDFWGKLIEYSLGDKKNECKLSDQRAALCRGQNPLPIYLTINVKDDVSNQDFREWFEFSPYEVGMQKYGAFIPSELFGSEFFMGRLMKRIPEPEMCYMLGLWSSIFSLNLLDAWNLSHTSEEFFYRWTRERLHDIEDDPILPEIPRCDDNPLETTVVIPTTWLSNTFREILTRRPFVSEFHNFLYGMQLHTDYLQNRQFSMWKDTVLDTFPNQLTQFAKHLNLLDTAFFVNSSYAPLLRPERKVDLIIHLNYCAGSQTKPLKQTCEYCTEQKIPFPSFSILEDDNSLKECYVMENPQEPDAPIVAYFPLISDTFQKYKAPGVERSPDELELGQLNIYGPKSPYATKELTYTEAAFDKLVKLSEYNILNNRDKLIQALRLAMEKKRMRSQCPS | 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). Similarly can use plasmenylethanolamine as a fatty acyl acceptor to form N-acyl plasmenylethanolamine (N-Acyl-PlsEt). Both NAPE and N-Acyl-PlsEt can serve as precursors of bioactive NAEs like N-arachidonoyl phosphatidylethanolamine also called anandamide . Has weak phospholipase A2 and lysophospholipase activities . Regulates intracellular membrane trafficking that requires modulation of membrane curvature as it occurs by enrichment in lysophospholipids. Promotes tubule formation involved in clathrin-independent endocytotic trafficking and cargo recycling .
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphocholine + a 1,2-diacyl-sn-glycero-3-phosphoethanolamine = a 2-acyl-sn-glycero-3-phosphocholine + H(+) + N-acyl-1,2-diacyl-sn-glycero-3-phosphoethanolamine
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 100157
Sequence Length: 875
Domain: The N-terminal C2 domain associates with lipid membranes upon calcium binding. It modulates enzyme activity by presenting the active site to its substrate in response to elevations of cytosolic Ca(2+) (By similarity).
Subcellular Location: Cytoplasm
EC: 3.1.1.4
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Q50L41 | MPWTLQPKWLAGKGLPLLGAILLRKTEKSEPQWKHRRQETHPYYDLQVKVLRARNIQHTDKLSKADCYVRLWLPTASVSPSQTRTVVNSSDPEWNETFPYQIHGAVKNVLELALYDEDVLDSDNVFSILFDTSTLQLGQPCTKNFTRQQDPKELEVEFTLEKSQTPASEVVTNGVLVAHPCLRIQGTVTGDKTASLGELGSRQIQLAVPGAYEKPQPLQPTSEPGLPVNFTFHVNPVLSPKLHIKLQEQLQVFHSGPSDELEAQTSKMDKASILLSSLPLNEELTKLVDLEEGQQVSLRMKADMSSSGDLDLRLGFDLCDGEQEFLDKRKQVASKALQRVMGLSEALHCDQVPVVAVLGSGGGTRAMTSLYGSLAGLQELGLLDAVTYLSGVSGSSWCISTLYRDPSWSQKALQGPIKYASERVCSSKIGMLSPKQFEYYSREKRAWESRGHSMSFTDLWGLIIEYFLNQEENPAKLSDQQETVSQGQNPYPIYASINVHKNISGDDFAEWCEFTPYEVGFPKYGAYVPTELFGSEFFMGRLLHFWPEPRICYLQGMWGSAFAASLYEIFLKLGGLSLSFLDWHRGSVSVTDDWPKLRKQDPTRLPTRLFTPMSSFSQAVLDIFTSRITCAQTFNFTRGLCMYKDYTARKDFVVSEDAWHSHNYGYPDACPNQLTPMKDFLSLVDGGFAINSPFPLVLQPQRAVDLIVSFDYSLEGPFEVLQVTEKYCRDRGIPFPRIEVDPKDSEDPRECYLFAEAEDPCSPIVLHFPLVNRTFRTHLAPGVERQTAEEKAFGDFIINGPDTAYGMMDFTYEPKEFDRLVTLSRYNVLNNKETIRHALQLALDRRRQAGGRVGG | 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 hydrolyzes sn-2 arachidonoyl group from membrane phospholipids, providing the precursor for eicosanoid biosynthesis . In myocardial mitochondria, plays a major role in arachidonate release that is metabolically channeled to the formation of cardioprotective eicosanoids, epoxyeicosatrienoates (EETs) (By similarity).
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 96364
Sequence Length: 855
Domain: The N-terminal C2 domain associates with lipid membranes upon calcium binding. It modulates enzyme activity by presenting the active site to its substrate in response to elevations of cytosolic Ca(2+) (By similarity).
Subcellular Location: Cytoplasm
EC: 3.1.1.4
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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-phosphoglycerides .
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+)
Sequence Mass (Da): 5544
Sequence Length: 48
Subcellular Location: Secreted
EC: 3.1.1.4
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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 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+)
Sequence Mass (Da): 3263
Sequence Length: 29
Subcellular Location: Secreted
EC: 3.1.1.4
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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 at sn-2 position of phospholipids (phospholipase A2 activity) with preference for phosphatidylethanolamines and phosphatidylglycerols over phosphatidylcholines (By similarity). Contributes to lipid remodeling of cellular membranes and generation of lipid mediators involved in pathogen clearance. Displays bactericidal activity against Gram-positive bacteria by directly hydrolyzing phospholipids of the bacterial membrane. Upon sterile inflammation, targets membrane phospholipids of extracellular mitochondria released from activated platelets, generating free unsaturated fatty acids such as arachidonate that is used by neighboring leukocytes to synthesize inflammatory eicosanoids such as leukotrienes. Simultaneously, by compromising mitochondrial membrane integrity, promotes the release in circulation of potent damage-associated molecular pattern molecules that activate the innate immune response (By similarity). Plays a stem cell regulator role in the intestinal crypt. Within intracellular compartment mediates Paneth cell differentiation and its stem cell supporting functions by inhibiting Wnt signaling pathway in intestinal stem cell (ICS). Secreted in the intestinal lumen upon inflammation, acts in an autocrine way and promotes prostaglandin E2 synthesis that stimulates Wnt signaling pathway in ICS cells and tissue regeneration (By similarity). May play a role in the biosynthesis of N-acyl ethanolamines that regulate energy metabolism and inflammation. Hydrolyzes N-acyl phosphatidylethanolamines to N-acyl lysophosphatidylethanolamines, which are further cleaved by a lysophospholipase D to release N-acyl ethanolamines. Independent of its catalytic activity, acts as a ligand for integrins. Binds to and activates integrins ITGAV:ITGB3, ITGA4:ITGB1 and ITGA5:ITGB1. Binds to a site (site 2) which is distinct from the classical ligand-binding site (site 1) and induces integrin conformational changes and enhanced ligand binding to site 1. Induces cell proliferation in an integrin-dependent manner (By similarity).
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + H2O = a 1-acyl-sn-glycero-3-phosphoethanolamine + a fatty acid + H(+)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 16153
Sequence Length: 145
Subcellular Location: Secreted
EC: 3.1.1.4
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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 of phospholipids (phospholipase A2 activity) with preference for phosphatidylethanolamines and phosphatidylglycerols over phosphatidylcholines . Contributes to lipid remodeling of cellular membranes and generation of lipid mediators involved in pathogen clearance. Displays bactericidal activity against Gram-positive bacteria by directly hydrolyzing phospholipids of the bacterial membrane . Upon sterile inflammation, targets membrane phospholipids of extracellular mitochondria released from activated platelets, generating free unsaturated fatty acids such as arachidonate that is used by neighboring leukocytes to synthesize inflammatory eicosanoids such as leukotrienes. Simultaneously, by compromising mitochondrial membrane integrity, promotes the release in circulation of potent damage-associated molecular pattern molecules that activate the innate immune response . Plays a stem cell regulator role in the intestinal crypt. Within intracellular compartment mediates Paneth cell differentiation and its stem cell supporting functions by inhibiting Wnt signaling pathway in intestinal stem cell (ICS). Secreted in the intestinal lumen upon inflammation, acts in an autocrine way and promotes prostaglandin E2 synthesis that stimulates Wnt signaling pathway in ICS cells and tissue regeneration (By similarity). May play a role in the biosynthesis of N-acyl ethanolamines that regulate energy metabolism and inflammation. Hydrolyzes N-acyl phosphatidylethanolamines to N-acyl lysophosphatidylethanolamines, which are further cleaved by a lysophospholipase D to release N-acyl ethanolamines . Independent of its catalytic activity, acts as a ligand for integrins . Binds to and activates integrins ITGAV:ITGB3, ITGA4:ITGB1 and ITGA5:ITGB1 . Binds to a site (site 2) which is distinct from the classical ligand-binding site (site 1) and induces integrin conformational changes and enhanced ligand binding to site 1 . Induces cell proliferation in an integrin-dependent manner .
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + H2O = a 1-acyl-sn-glycero-3-phosphoethanolamine + a fatty acid + H(+)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 16083
Sequence Length: 144
Subcellular Location: Secreted
EC: 3.1.1.4
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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 of phospholipids (phospholipase A2 activity) with preference for phosphatidylethanolamines and phosphatidylglycerols over phosphatidylcholines. Contributes to lipid remodeling of cellular membranes and generation of lipid mediators involved in pathogen clearance. Displays bactericidal activity against Gram-positive bacteria by directly hydrolyzing phospholipids of the bacterial membrane . Upon sterile inflammation, targets membrane phospholipids of extracellular mitochondria released from activated platelets, generating free unsaturated fatty acids such as arachidonate that is used by neighboring leukocytes to synthesize inflammatory eicosanoids such as leukotrienes. Simultaneously, by compromising mitochondrial membrane integrity, promotes the release in circulation of potent damage-associated molecular pattern molecules that activate the innate immune response (By similarity). Plays a stem cell regulator role in the intestinal crypt. Within intracellular compartment mediates Paneth cell differentiation and its stem cell supporting functions by inhibiting Wnt signaling pathway in intestinal stem cell (ICS). Secreted in the intestinal lumen upon inflammation, acts in an autocrine way and promotes prostaglandin E2 synthesis that stimulates Wnt signaling pathway in ICS cells and tissue regeneration . May play a role in the biosynthesis of N-acyl ethanolamines that regulate energy metabolism and inflammation. Hydrolyzes N-acyl phosphatidylethanolamines to N-acyl lysophosphatidylethanolamines, which are further cleaved by a lysophospholipase D to release N-acyl ethanolamines (By similarity). Independent of its catalytic activity, acts as a ligand for integrins. Binds to and activates integrins ITGAV:ITGB3, ITGA4:ITGB1 and ITGA5:ITGB1. Binds to a site (site 2) which is distinct from the classical ligand-binding site (site 1) and induces integrin conformational changes and enhanced ligand binding to site 1. Induces cell proliferation in an integrin-dependent manner (By similarity).
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + H2O = a 1-acyl-sn-glycero-3-phosphoethanolamine + a fatty acid + H(+)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 16145
Sequence Length: 146
Subcellular Location: Secreted
EC: 3.1.1.4
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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 at sn-2 position of phospholipids (phospholipase A2 activity) with preference for phosphatidylethanolamines and phosphatidylglycerols over phosphatidylcholines . Contributes to lipid remodeling of cellular membranes and generation of lipid mediators involved in pathogen clearance. Displays bactericidal activity against Gram-positive bacteria by directly hydrolyzing phospholipids of the bacterial membrane. Upon sterile inflammation, targets membrane phospholipids of extracellular mitochondria released from activated platelets, generating free unsaturated fatty acids such as arachidonate that is used by neighboring leukocytes to synthesize inflammatory eicosanoids such as leukotrienes. Simultaneously, by compromising mitochondrial membrane integrity, promotes the release in circulation of potent damage-associated molecular pattern molecules that activate the innate immune response (By similarity). Plays a stem cell regulator role in the intestinal crypt. Within intracellular compartment mediates Paneth cell differentiation and its stem cell supporting functions by inhibiting Wnt signaling pathway in intestinal stem cell (ICS). Secreted in the intestinal lumen upon inflammation, acts in an autocrine way and promotes prostaglandin E2 synthesis that stimulates Wnt signaling pathway in ICS cells and tissue regeneration (By similarity). May play a role in the biosynthesis of N-acyl ethanolamines that regulate energy metabolism and inflammation. Hydrolyzes N-acyl phosphatidylethanolamines to N-acyl lysophosphatidylethanolamines, which are further cleaved by a lysophospholipase D to release N-acyl ethanolamines. Independent of its catalytic activity, acts as a ligand for integrins. Binds to and activates integrins ITGAV:ITGB3, ITGA4:ITGB1 and ITGA5:ITGB1. Binds to a site (site 2) which is distinct from the classical ligand-binding site (site 1) and induces integrin conformational changes and enhanced ligand binding to site 1. Induces cell proliferation in an integrin-dependent manner (By similarity).
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + H2O = a 1-acyl-sn-glycero-3-phosphoethanolamine + a fatty acid + H(+)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 7592
Sequence Length: 68
Subcellular Location: Secreted
EC: 3.1.1.4
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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 tubules and the testicular capsule; they also seem to decrease sperm transit time through the male reproductive tract.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+)
Sequence Mass (Da): 16983
Sequence Length: 150
Subcellular Location: Secreted
EC: 3.1.1.4
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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 activity) with preference for phosphatidylethanolamines and phosphatidylglycerols over phosphatidylcholines (By similarity). In draining lymph nodes, selectively hydrolyzes diacyl and alkenyl forms of phosphatidylethanolamines, releasing omega-3 polyunsaturated fatty acids (PUFAs) such as eicosapentaenoate and docosahexaenoate that are precursors of the anti-inflammatory lipid mediators, resolvins . During the resolution phase of acute inflammation drives docosahexaenoate-derived resolvin D1 synthesis, which suppresses dendritic cell activation and T-helper 1 immune response . May act in an autocrine and paracrine manner. Via a mechanism independent of its catalytic activity, promotes differentiation of regulatory T cells (Tregs) and participates in the maintenance of immune tolerance . May contribute to lipid remodeling of cellular membranes and generation of lipid mediators involved in pathogen clearance. Displays bactericidal activity against Gram-positive bacteria by directly hydrolyzing phospholipids of the bacterial membrane .
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + H2O = a 1-acyl-sn-glycero-3-phosphoethanolamine + a fatty acid + H(+)
Sequence Mass (Da): 16164
Sequence Length: 144
Subcellular Location: Secreted
EC: 3.1.1.4
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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 . Hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids (phospholipase A2 activity), releasing various unsaturated fatty acids including oleoate, linoleoate, arachidonate, docosahexaenoate and lysophosphatidylethanolamines in preference to lysophosphatidylcholines . In response to high-fat diet, hydrolyzes minor lipoprotein phospholipids including phosphatidylserines, phosphatidylinositols and phosphatidylglycerols, altering lipoprotein composition and fat storage in adipose tissue and liver (By similarity). May act in an autocrine and paracrine manner . Contributes to lipid remodeling of cellular membranes and generation of lipid mediators involved in pathogen clearance. Cleaves sn-2 fatty acyl chains of phosphatidylglycerols and phosphatidylethanolamines, which are major components of membrane phospholipids in bacteria . Acts as a hair follicle phospholipase A2. Selectively releases lysophosphatidylethanolamines (LPE) and various unsaturated fatty acids in skin to regulate hair follicle homeostasis (By similarity). May regulate the inflammatory response by releasing arachidonate, a precursor of prostaglandins and leukotrienes . Upon allergen exposure, may participate in allergic inflammatory response by enhancing leukotriene C4 synthesis and degranulation in mast cells (By similarity).
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + H2O = a 1-acyl-sn-glycero-3-phosphoethanolamine + a fatty acid + H(+)
Sequence Mass (Da): 15989
Sequence Length: 142
Subcellular Location: Secreted
EC: 3.1.1.4
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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 following order: phosphatidylglycerols > phosphatidylethanolamines > phosphatidylcholines > phosphatidylserines . May play a role in lipid mediator production in inflammatory conditions, by providing arachidonic acid to downstream cyclooxygenases and lipoxygenases .
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 18880
Sequence Length: 168
Subcellular Location: Secreted
EC: 3.1.1.4
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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 phosphatidylethanolamines. Preferentially releases sn-2 omega-6 and omega-3 polyunsaturated fatty acyl (PUFA) chains over saturated fatty acyls . Contributes to phospholipid remodeling of very low-density lipoprotein (VLDL), low-density lipoprotein (LDL) and high-density lipoprotein (HDL) particles . Hydrolyzes LDL phospholipids releasing unsaturated fatty acids that regulate macrophage differentiation toward foam cells . Efficiently hydrolyzes and inactivates platelet activating factor (PAF), a potent lipid mediator present in oxidized LDL . May act in an autocrine and paracrine manner. Secreted by lung epithelium, targets membrane phospholipids of infiltrating eosinophils, releasing arachidonate and boosting eicosanoid and cysteinyl leukotriene synthesis involved in airway inflammatory response (By similarity). Secreted by gut epithelium, hydrolyzes dietary and biliary phosphatidylcholines in the gastrointestinal lumen (By similarity). Plays a stem cell regulator role in colon epithelium. Within intracellular compartment, mediates Paneth-like cell differentiation and its stem cell supporting functions by inhibiting the Wnt signaling pathway in intestinal stem cell (ISC). Secreted in the intestinal lumen upon inflammation, acts in an autocrine way and promotes prostaglandin E2 synthesis that stimulates Wnt signaling pathway in ISCs and tissue regeneration (By similarity). May participate in hair follicle morphogenesis by regulating phosphatidylethanolamines metabolism at the outermost epithelial layer and facilitating melanin synthesis (By similarity). By releasing lysophosphatidylcholines (LPCs) at sperm acrosome, controls sperm cell capacitation, acrosome reaction and overall fertility (By similarity). May promote neurite outgrowth in neuron fibers involved in nociception (By similarity). Contributes to lipid remodeling of cellular membranes and generation of lipid mediators involved in pathogen clearance. Cleaves sn-2 fatty acyl chains of phosphatidylglycerols and phosphatidylethanolamines, which are major components of membrane phospholipids in bacteria . Displays bactericidal activity against Gram-positive bacteria by directly hydrolyzing phospholipids of the bacterial membrane . In pulmonary epithelium, may contribute to host defense response against adenoviral infection. Prevents adenovirus entry into host cells by hydrolyzing host cell plasma membrane, releasing C16:0 LPCs that inhibit virus-mediated membrane fusion and viral infection. Likely prevents adenoviral entry into the endosomes of host cells . May play a role in maturation and activation of innate immune cells including macrophages, group 2 innate lymphoid cells and mast cells (By similarity).
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+)
Sequence Mass (Da): 18153
Sequence Length: 165
Subcellular Location: Secreted
EC: 3.1.1.4
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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 phosphatidylethanolamines. Preferentially releases sn-2 omega-6 and omega-3 polyunsaturated fatty acyl (PUFA) chains over saturated fatty acyls. Contributes to phospholipid remodeling of very low-density lipoprotein (VLDL), low-density lipoprotein (LDL) and high-density lipoprotein (HDL) particles. Hydrolyzes LDL phospholipids releasing unsaturated fatty acids that regulate macrophage differentiation toward foam cells. Efficiently hydrolyzes and inactivates platelet activating factor (PAF), a potent lipid mediator present in oxidized LDL (By similarity). May act in an autocrine and paracrine manner. Secreted by lung epithelium, targets membrane phospholipids of infiltrating eosinophils, releasing arachidonate and boosting eicosanoid and cysteinyl leukotriene synthesis involved in airway inflammatory response. Secreted by gut epithelium, hydrolyzes dietary and biliary phosphatidylcholines in the gastrointestinal lumen. Plays a stem cell regulator role in colon epithelium. Within intracellular compartment, mediates Paneth-like cell differentiation and its stem cell supporting functions by inhibiting the Wnt signaling pathway in intestinal stem cell (ISC). Secreted in the intestinal lumen upon inflammation, acts in an autocrine way and promotes prostaglandin E2 synthesis that stimulates Wnt signaling pathway in ISCs and tissue regeneration. May participate in hair follicle morphogenesis by regulating phosphatidylethanolamines metabolism at the outermost epithelial layer and facilitating melanin synthesis. By releasing lysophosphatidylcholines (LPCs) at sperm acrosome, controls sperm cell capacitation, acrosome reaction and overall fertility. May promote neurite outgrowth in neuron fibers involved in nociception (By similarity). Contributes to lipid remodeling of cellular membranes and generation of lipid mediators involved in pathogen clearance. Cleaves sn-2 fatty acyl chains of phosphatidylglycerols and phosphatidylethanolamines, which are major components of membrane phospholipids in bacteria. Displays bactericidal activity against Gram-positive bacteria by directly hydrolyzing phospholipids of the bacterial membrane. In pulmonary epithelium, may contribute to host defense response against adenoviral infection. Prevents adenovirus entry into host cells by hydrolyzing host cell plasma membrane, releasing C16:0 LPCs that inhibit virus-mediated membrane fusion and viral infection. Likely prevents adenoviral entry into the endosomes of host cells (By similarity). May play a role in maturation and activation of innate immune cells including macrophages, group 2 innate lymphoid cells and mast cells (By similarity).
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+)
Sequence Mass (Da): 17088
Sequence Length: 151
Subcellular Location: Secreted
EC: 3.1.1.4
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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
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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.
EC: 5.3.3.18
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P76083 | MMINVQTVAVIGSGTMGAGIAEVAASHGHQVLLYDISAEALTRAIDGIHARLNSRVTRGKLTAETCERTLKRLIPVTDIHALAAADLVIEAASERLEVKKALFAQLAEVCPPQTLLTTNTSSISITAIAAEIKNPERVAGLHFFNPAPVMKLVEVVSGLATAAEVVEQLCELTLSWGKQPVRCHSTPGFIVNRVARPYYSEAWRALEEQVAAPEVIDAALRDGAGFPMGPLELTDLIGQDVNFAVTCSVFNAFWQERRFLPSLVQQELVIGGRLGKKSGLGVYDWRAEREAVVGLEAVSDSFSPMKVEKKSDGVTEIDDVLLIETQGETAQALAIRLARPVVVIDKMAGKVVTIAAAAVNPDSATRKAIYYLQQQGKTVLQIADYPGMLIWRTVAMIINEALDALQKGVASEQDIDTAMRLGVNYPYGPLAWGAQLGWQRILRLLENLQHHYGEERYRPCSLLRQRALLESGYES | 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 compound metabolism; phenylacetate degradation.
EC: 3.1.2.-
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P0C7L2 | MREAFICDGIRTPIGRYGGALSSVRADDLAAIPLRELLVRNPRLDAECIDDVILGCANQAGEDNRNVARMATLLAGLPQSVSGTTINRLCGSGLDALGFAARAIKAGDGDLLIAGGVESMSRAPFVMGKAASAFSRQAEMFDTTIGWRFVNPLMAQQFGTDSMPETAENVAELLKISREDQDSFALRSQQRTAKAQSSGILAEEIVPVVLKNKKGVVTEIQHDEHLRPETTLEQLRGLKAPFRANGVITAGNASGVNDGAAALIIASEQMAAAQGLTPRARIVAMATAGVEPRLMGLGPVPATRRVLERAGLSIHDMDVIELNEAFAAQALGVLRELGLPDDAPHVNPNGGAIALGHPLGMSGARLALAASHELHRRNGRYALCTMCIGVGQGIAMILERV | 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.
Catalytic Activity: acetyl-CoA + succinyl-CoA = 3-oxoadipyl-CoA + CoA
Sequence Mass (Da): 42277
Sequence Length: 401
Pathway: Aromatic compound metabolism; phenylacetate degradation.
EC: 2.3.1.174
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Q9L9C1 | MPVKTPSPGDLEPIEKASQDELRALQLERLKWSVRHAYENVPHYRKAFDAKGVHPDDLKSLADLAKFPFTAKGDLRDNYPFGMFAVPREKVARVHASSGTTGKPTVVGYTLKDIDTWATVVARSIRASGGRAGDMVHIAYGYGLFTGGLGAHYGAEKLGCTVVPMSGGQTEKQIQLIQDFKPDIIMVTPSYMLTVLDEMERMGIDPHQTSLKVGIFGAEPWTQAMRAAMEARAGIDAVDIYGLSEVMGPGVANECIEAKDGPVIWEDHFYPEIIDPHTGEVLPDGSEGELVFTTLTKEAMPVIRYRTRDLTRLLPPTARSMRRMAKITGRSDDMLIIRGVNLFPTQVEELICKNPKLAPQYLLEVDKDGHMDTLTVKVEINPEANVGRHPEQKEALAKELQHDIKTFIGVSAKVHVCEPFAIERVTIGKAKRVVDRRPKE | 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 degradation.
EC: 6.2.1.30
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P76085 | MITNTKLDPIETASVDELQALQTQRLKWTLKHAYENVPMYRRKFDAAGVHPDDFRELSDLRKFPCTTKQDLRDNYPFDTFAVPMEQVVRIHASSGTTGKPTVVGYTQNDIDNWANIVARSLRAAGGSPKDKIHVAYGYGLFTGGLGAHYGAERLGATVIPMSGGQTEKQAQLIRDFQPDMIMVTPSYCLNLIEELERQLGGDASGCSLRVGVFGAEPWTQAMRKEIERRLGITALDIYGLSEVMGPGVAMECLETTDGPTIWEDHFYPEIVNPHDGTPLADGEHGELLFTTLTKEALPVIRYRTRDLTRLLPGTARTMRRMDRISGRSDDMLIIRGVNVFPSQLEEEIVKFEHLSPHYQLEVNRRGHLDSLSVKVELKESSLTLTHEQRCQVCHQLRHRIKSMVGISTDVMIVNCGSIPRSEGKACRVFDLRNIVGA | 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
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O33469 | MNMYHDADRALLDPMETASVDALRQHQLERLRWSLKHAYDNVPLYRQRFAECGAHPDDLTCLEDLAKFPFTGKNDLRDNYPYGMFAVPQEEVVRLHASSGTTGKPTVVGYTQNDINTWANVVARSIRAAGGRKGDKVHVSYGYGLFTGGLGAHYGAERLGCTVIPMSGGQTEKQVQLIRDFQPDIIMVTPSYMLNLADEIERQGIDPHDLKLRLGIFGAEPWTDELRRSIEQRLGINALDIYGLSEIMGPGVAMECIETKDGPTIWEDHFYPEIIDPVTGEVLPDGQLGELVFTSLSKEALPMVRYRTRDLTRLLPGTARPMRRIGKITGRSDDMLIIRGVNVFPTQIEEQVLKIKQLSEMYEIHLYRNGNLDSVEVHVELRAECQHLDEGQRKLVIGELSKQIKTYIGISTQVHLQACGTLKRSEGKACHVYDKRLAS | 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: Aromatic compound metabolism; phenylacetate degradation.
EC: 6.2.1.30
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Q8RY79 | MENGSGKVLKPMDSEQLREYGHLMVDFIADYYKTIEDFPVLSQVQPGYLHKLLPDSAPDHPETLDQVLDDVRAKILPGVTHWQSPSFFAYYPSNSSVAGFLGEMLSAGLGIVGFSWVTSPAATELEMIVLDWVAKLLNLPEQFMSKGNGGGVIQGSASEAVLVVLIAARDKVLRSVGKNALEKLVVYSSDQTHSALQKACQIAGIHPENCRVLTTDSSTNYALRPESLQEAVSRDLEAGLIPFFLCANVGTTSSTAVDPLAALGKIANSNGIWFHVDAAYAGSACICPEYRQYIDGVETADSFNMNAHKWFLTNFDCSLLWVKDQDSLTLALSTNPEFLKNKASQANLVVDYKDWQIPLGRRFRSLKLWMVLRLYGSETLKSYIRNHIKLAKEFEQLVSQDPNFEIVTPRIFALVCFRLVPVKDEEKKCNNRNRELLDAVNSSGKLFMSHTALSGKIVLRCAIGAPLTEEKHVKEAWKIIQEEASYLLHK | 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 and deamination of L-dopa to 3,4-dihydroxylphenylacetaldehyde (DHPAA) .
Catalytic Activity: H(+) + H2O + L-phenylalanine + O2 = 2-phenylacetaldehyde + CO2 + H2O2 + NH4(+)
Sequence Mass (Da): 54423
Sequence Length: 490
EC: 4.1.1.109
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Q9H8K7 | METRTEDGGLTRRPTLASSWDVAGGALTHSLLLTRAGLGPGDFDWEELLAPPAPGQDLVILKRNHNNKDENPCFLYLRCGPDGGEEIASIGILSSARNMEVYLGEEYCGTSRGKNVCTVLDDSEHEKIILYKKNLKLESSTHACKIKLLSFGERQCVFISKVVVHMRSVFANSSTSSPALGSRIDLDKVQTIMESMGSKLSPGAQQLMDMVRCQQRNCIPIGEQLQSVLGNSGYKHMIGLQSSSTLGTLNKSSSTPFPFRTGLTSGNVTENLQTYIDKSTQLPGGENSTKLDECKVMPQNHSFLENDLKNAMASFLPKKVSDNSNIPNSELLPFLQNLCSQVNHLHVGNKTECQENITKHGERILGVGMEEQSICSYLEKILSKNMELMEKKLMDYIDQRIHELQEHIDDKIALLLDLLQNPNSPPTGIPLRHYDSGERLSNGER | 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 (Da): 49249
Sequence Length: 445
Subcellular Location: Cytoplasm
EC: 3.6.1.-
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B6HIC2 | MEAPRSDQAHTDATTPMEAIRTTSLGTNNYGPVPDDYLDLPVREVNDGADLREYITETRTGEIIKPIKSNVTGKTEDWKMVTFTIDDPENPKNWSKAFKWYCTMVVAFTCFVVAFCSSVITADVEGPIEEFGIGREASLVVITVFVIGFGLGPMVFAPMSEIVGRRPVYALTLALAVIFVIPCAVSKNIGTLIVCRLIDGIAFSAPMTLVGGTLADLWKSEERGVPMAAFSAAPFIGPAIGPLVGGYLADNCGWRWLYWIQLILAFVAWVMITFTVPETFAPILLKKRAQKLRKAEDDPKYTTETELDARPMGEKLRIFLFRPFQLLFLEPIVLFISLYMSVIYGLLYMFFVAYPIVYMGGKGWSASNTGLMFIPLAIGVIFSACCAPFVNNHYLKVSVAYGGKPPAEKRLIPMMWACWCIPSGLFVFAWTSYPDLHWMGPAMGGFLIGVGVILLYNSANNYLVDTYQHQAASALAAKTFIRSIWGACTVLFTEQMYERLGDQWASTLLAFIGLACCAIPYVFYFKGESIRRFSKFAFSDDEEKAIKA | 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
Sequence Length: 548
Domain: The peroxisomal targeting signal allows recruitment to the peroxisomal membrane by pex19.
Subcellular Location: Peroxisome membrane
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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 bypass of replication-fork-blocking lesions. Also acts as a regulator of centrosome number (By similarity).
PTM: Monoubiquitinated at Lys-15 and Lys-24 during normal S phase, promoting its association with PCNA. Also diubiquitinated at these 2 sites. Following DNA damage, monoubiquitin chains at Lys-15 and Lys-24 are probably extended, leading to disrupt the interaction with PCNA. Polyubiquitinated by the APC/C complex at the mitotic exit, leading to its degradation by the proteasome (By similarity).
Sequence Mass (Da): 11993
Sequence Length: 110
Domain: The PIP-box mediates the interaction with PCNA.
Subcellular Location: Nucleus
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P79106 | MGVNQSVSFPPVTGPHLVGCGDVMEGQSLQGSFFRLFYPCQEAEETSEQPLWIPRYEYCAGLAEYLKFNKRWGGLLFNLGVGSCRLPVSWNGPFKTKDSGYPLIIFSHGMGAFRTVYSAFCMELASRGFVVAVPEHRDGSAAATCFCKQTPEENQPDNEALKEEWIPHRQIEEGEKEFYVRNYQVHQRVSECVRVLKILQEVTAGQAVLNILPGGLDLMTLKGGIDVSRVAVMGHSFGGATAILALAKEMQFRCAVALDAWMFPLEHDFYPTARGPIFFINAEKFQTVETVNLMKKICDQHHQSRIITVLGSVHRSLTDFVFVAGNWISKFFSSHTRGSLDPYEGQETVVRAMLAFLQKHLDLKEDYDQWNNFIEGIGPSLTPGAPHHLSSL | 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-activating factor (PAF) to lysoplasmalogen and to sphingosine, producing plasmalogen analogs of PAF and N-acetylsphingosine (C2-ceramide) respectively. Has a marked selectivity for phospholipids with short acyl chains at the sn-2 position (By similarity).
Catalytic Activity: a 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-O-alkyl-sn-glycero-3-phosphocholine + acetate + H(+)
Location Topology: Lipid-anchor
Sequence Mass (Da): 43865
Sequence Length: 392
Subcellular Location: Cytoplasm
EC: 3.1.1.47
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Q99487 | MGVNQSVGFPPVTGPHLVGCGDVMEGQNLQGSFFRLFYPCQKAEETMEQPLWIPRYEYCTGLAEYLQFNKRCGGLLFNLAVGSCRLPVSWNGPFKTKDSGYPLIIFSHGLGAFRTLYSAFCMELASRGFVVAVPEHRDRSAATTYFCKQAPEENQPTNESLQEEWIPFRRVEEGEKEFHVRNPQVHQRVSECLRVLKILQEVTAGQTVFNILPGGLDLMTLKGNIDMSRVAVMGHSFGGATAILALAKETQFRCAVALDAWMFPLERDFYPKARGPVFFINTEKFQTMESVNLMKKICAQHEQSRIITVLGSVHRSQTDFAFVTGNLIGKFFSTETRGSLDPYEGQEVMVRAMLAFLQKHLDLKEDYNQWNNLIEGIGPSLTPGAPHHLSSL | 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 platelet-activating factor (PAF) to lysoplasmalogen and to sphingosine, producing plasmalogen analogs of PAF and N-acetylsphingosine (C2-ceramide) respectively. Has a marked selectivity for phospholipids with short acyl chains at the sn-2 position (By similarity).
Catalytic Activity: a 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-O-alkyl-sn-glycero-3-phosphocholine + acetate + H(+)
Location Topology: Lipid-anchor
Sequence Mass (Da): 44036
Sequence Length: 392
Subcellular Location: Cytoplasm
EC: 3.1.1.47
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Q13177 | MSDNGELEDKPPAPPVRMSSTIFSTGGKDPLSANHSLKPLPSVPEEKKPRHKIISIFSGTEKGSKKKEKERPEISPPSDFEHTIHVGFDAVTGEFTGMPEQWARLLQTSNITKLEQKKNPQAVLDVLKFYDSNTVKQKYLSFTPPEKDGFPSGTPALNAKGTEAPAVVTEEEDDDEETAPPVIAPRPDHTKSIYTRSVIDPVPAPVGDSHVDGAAKSLDKQKKKTKMTDEEIMEKLRTIVSIGDPKKKYTRYEKIGQGASGTVFTATDVALGQEVAIKQINLQKQPKKELIINEILVMKELKNPNIVNFLDSYLVGDELFVVMEYLAGGSLTDVVTETCMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMEGSVKLTDFGFCAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPEKLSPIFRDFLNRCLEMDVEKRGSAKELLQHPFLKLAKPLSSLTPLIMAAKEAMKSNR | 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 RAC1 results in a conformational change and a subsequent autophosphorylation on several serine and/or threonine residues . Full-length PAK2 stimulates cell survival and cell growth . Phosphorylates MAPK4 and MAPK6 and activates the downstream target MAPKAPK5, a regulator of F-actin polymerization and cell migration . Phosphorylates JUN and plays an important role in EGF-induced cell proliferation . Phosphorylates many other substrates including histone H4 to promote assembly of H3.3 and H4 into nucleosomes, BAD, ribosomal protein S6, or MBP . Phosphorylates CASP7, thereby preventing its activity . Additionally, associates with ARHGEF7 and GIT1 to perform kinase-independent functions such as spindle orientation control during mitosis . On the other hand, apoptotic stimuli such as DNA damage lead to caspase-mediated cleavage of PAK2, generating PAK-2p34, an active p34 fragment that translocates to the nucleus and promotes cellular apoptosis involving the JNK signaling pathway . Caspase-activated PAK2 phosphorylates MKNK1 and reduces cellular translation .
PTM: Full-length PAK2 is autophosphorylated when activated by CDC42/p21. Following cleavage, both peptides, PAK-2p27 and PAK-2p34, become highly autophosphorylated, with PAK-2p27 being phosphorylated on serine and PAK-2p34 on threonine residues, respectively. Autophosphorylation of PAK-2p27 can occur in the absence of any effectors and is dependent on phosphorylation of Thr-402, because PAK-2p27 is acting as an exogenous substrate.
Location Topology: Lipid-anchor
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 58043
Sequence Length: 524
Subcellular Location: Cytoplasm
EC: 2.7.11.1
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Q61036 | MSDSLDNEEKPPAPPLRMNSNNRDSSALNHSSKPLPMAPEEKNKKARLRSIFPGGGDKTNKKKEKERPEISLPSDFEHTIHVGFDAVTGEFTPDLYGSQMCPGKLPEGIPEQWARLLQTSNITKLEQKKNPQAVLDVLKFYDSKETVNNQKYMSFTSGDKSAHGYIAAHQSNTKTASEPPLAPPVSEEEDEEEEEEEDDNEPPPVIAPRPEHTKSIYTRSVVESIASPAAPNKEDIPPSAENANSTTLYRNTDRQRKKSKMTDEEILEKLRSIVSVGDPKKKYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPERLSAVFRDFLNRCLEMDVDRRGSAKELLQHPFLKLAKPLSSLTPLIIAAKEAIKNSSR | 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 GTPases CDC42 and RAC1. Activation by the binding of active CDC42 and RAC1 results in a conformational change and a subsequent autophosphorylation on several serine and/or threonine residues. Phosphorylates MAPK4 and MAPK6 and activates the downstream target MAPKAPK5, a regulator of F-actin polymerization and cell migration. Additionally, phosphorylates TNNI3/troponin I to modulate calcium sensitivity and relaxation kinetics of thin myofilaments. May also be involved in early neuronal development. In hippocampal neurons, necessary for the formation of dendritic spines and excitatory synapses; this function is dependent on kinase activity and may be exerted by the regulation of actomyosin contractility through the phosphorylation of myosin II regulatory light chain (MLC) .
PTM: Autophosphorylated when activated by CDC42/p21.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 62398
Sequence Length: 559
Subcellular Location: Cytoplasm
EC: 2.7.11.1
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Q8AXB4 | MSDSVDIEEKPPAPPLRMNSNNRDSSALNHCSKPLPMAPEEKNKKARLRSIFPGGGDKTNKKKEKERPEISLPSDFEHTIHVGFDAVTGEFTPDLCGSQMGTGKLPEGIPEQWARLLQTSNITKLEQKKNPQAVLDVLKFYDSKETVNNQKYMSFTSGDKSAHGYIAAHSLNAKTASEPPLAPPVSEEEDEEEEEEEDDNEPPPVIAPRPEHTKSIYTRSVIEPVALTAPAKEASTSPVTPQPENSNSSTSTLYRNTDRQRKKSKMTDEEILEKLRSIVSVGDPKKKYTRFEKIGQGASGTVYTAIDIATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPERLSAIFRDFLNRCLEMDVDRRGSAKELLQHPFLKIAKPLSSLTPLIIAAKEAIKNSSR | 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 synergistically with mturn to promote primary neural differentiation within the neural plate. Involved in the cement gland formation.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 62767
Sequence Length: 564
Subcellular Location: Cytoplasm
EC: 2.7.11.1
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O96013 | MFGKRKKRVEISAPSNFEHRVHTGFDQHEQKFTGLPRQWQSLIEESARRPKPLVDPACITSIQPGAPKTIVRGSKGAKDGALTLLLDEFENMSVTRSNSLRRDSPPPPARARQENGMPEEPATTARGGPGKAGSRGRFAGHSEAGGGSGDRRRAGPEKRPKSSREGSGGPQESSRDKRPLSGPDVGTPQPAGLASGAKLAAGRPFNTYPRADTDHPSRGAQGEPHDVAPNGPSAGGLAIPQSSSSSSRPPTRARGAPSPGVLGPHASEPQLAPPACTPAAPAVPGPPGPRSPQREPQRVSHEQFRAALQLVVDPGDPRSYLDNFIKIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTDIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPRLKNLHKVSPSLKGFLDRLLVRDPAQRATAAELLKHPFLAKAGPPASIVPLMRQNRTR | 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 change and a subsequent autophosphorylation on several serine and/or threonine residues. Phosphorylates and inactivates the protein phosphatase SSH1, leading to increased inhibitory phosphorylation of the actin binding/depolymerizing factor cofilin. Decreased cofilin activity may lead to stabilization of actin filaments. Phosphorylates LIMK1, a kinase that also inhibits the activity of cofilin. Phosphorylates integrin beta5/ITGB5 and thus regulates cell motility. Phosphorylates ARHGEF2 and activates the downstream target RHOA that plays a role in the regulation of assembly of focal adhesions and actin stress fibers. Stimulates cell survival by phosphorylating the BCL2 antagonist of cell death BAD. Alternatively, inhibits apoptosis by preventing caspase-8 binding to death domain receptors in a kinase independent manner. Plays a role in cell-cycle progression by controlling levels of the cell-cycle regulatory protein CDKN1A and by phosphorylating RAN.
PTM: Autophosphorylated on serine residues when activated by CDC42/p21 (Ref.32). Phosphorylated on tyrosine residues upon stimulation of FGFR2 (By similarity). Methylated by SETD6.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 64072
Sequence Length: 591
Subcellular Location: Cytoplasm
EC: 2.7.11.1
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Q9P286 | MFGKKKKKIEISGPSNFEHRVHTGFDPQEQKFTGLPQQWHSLLADTANRPKPMVDPSCITPIQLAPMKTIVRGNKPCKETSINGLLEDFDNISVTRSNSLRKESPPTPDQGASSHGPGHAEENGFITFSQYSSESDTTADYTTEKYREKSLYGDDLDPYYRGSHAAKQNGHVMKMKHGEAYYSEVKPLKSDFARFSADYHSHLDSLSKPSEYSDLKWEYQRASSSSPLDYSFQFTPSRTAGTSGCSKESLAYSESEWGPSLDDYDRRPKSSYLNQTSPQPTMRQRSRSGSGLQEPMMPFGASAFKTHPQGHSYNSYTYPRLSEPTMCIPKVDYDRAQMVLSPPLSGSDTYPRGPAKLPQSQSKSGYSSSSHQYPSGYHKATLYHHPSLQSSSQYISTASYLSSLSLSSSTYPPPSWGSSSDQQPSRVSHEQFRAALQLVVSPGDPREYLANFIKIGEGSTGIVCIATEKHTGKQVAVKKMDLRKQQRRELLFNEVVIMRDYHHDNVVDMYSSYLVGDELWVVMEFLEGGALTDIVTHTRMNEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILLTSDGRIKLSDFGFCAQVSKEVPKRKSLVGTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMIDGEPPYFNEPPLQAMRRIRDSLPPRVKDLHKVSSVLRGFLDLMLVREPSQRATAQELLGHPFLKLAGPPSCIVPLMRQYRHH | 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 subsequent autophosphorylation on several serine and/or threonine residues. Phosphorylates the proto-oncogene RAF1 and stimulates its kinase activity. Promotes cell survival by phosphorylating the BCL2 antagonist of cell death BAD. Phosphorylates CTNND1, probably to regulate cytoskeletal organization and cell morphology. Keeps microtubules stable through MARK2 inhibition and destabilizes the F-actin network leading to the disappearance of stress fibers and focal adhesions.
PTM: Autophosphorylated when activated by CDC42/p21.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 80745
Sequence Length: 719
Domain: An autoinhibitory domain is present in the N-terminal region of the protein.
Subcellular Location: Mitochondrion
EC: 2.7.11.1
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Q9NQU5 | MFRKKKKKRPEISAPQNFQHRVHTSFDPKEGKFVGLPPQWQNILDTLRRPKPVVDPSRITRVQLQPMKTVVRGSAMPVDGYISGLLNDIQKLSVISSNTLRGRSPTSRRRAQSLGLLGDEHWATDPDMYLQSPQSERTDPHGLYLSCNGGTPAGHKQMPWPEPQSPRVLPNGLAAKAQSLGPAEFQGASQRCLQLGACLQSSPPGASPPTGTNRHGMKAAKHGSEEARPQSCLVGSATGRPGGEGSPSPKTRESSLKRRLFRSMFLSTAATAPPSSSKPGPPPQSKPNSSFRPPQKDNPPSLVAKAQSLPSDQPVGTFSPLTTSDTSSPQKSLRTAPATGQLPGRSSPAGSPRTWHAQISTSNLYLPQDPTVAKGALAGEDTGVVTHEQFKAALRMVVDQGDPRLLLDSYVKIGEGSTGIVCLAREKHSGRQVAVKMMDLRKQQRRELLFNEVVIMRDYQHFNVVEMYKSYLVGEELWVLMEFLQGGALTDIVSQVRLNEEQIATVCEAVLQALAYLHAQGVIHRDIKSDSILLTLDGRVKLSDFGFCAQISKDVPKRKSLVGTPYWMAPEVISRSLYATEVDIWSLGIMVIEMVDGEPPYFSDSPVQAMKRLRDSPPPKLKNSHKVSPVLRDFLERMLVRDPQERATAQELLDHPFLLQTGLPECLVPLIQLYRKQTSTC | 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-mediated transcription. May play a role in cytoskeleton regulation by interacting with IQGAP1. May protect cells from apoptosis through phosphorylation of BAD.
PTM: Autophosphorylated. Phosphorylated by MAP2K6//MAPKK6, leading to PAK6 activation.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 74869
Sequence Length: 681
Subcellular Location: Cytoplasm
EC: 2.7.11.1
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Q3ULB5 | MFRKKKKKRPEISAPQNFQHRVHTSFDPKEGKFVGLPPQWQNILDTLRRPKPVVDPSRITRVQLQPMKTVVRGSSVPTEGYISGLLNDIQKLSVISSNTLRGRSPTSRRRAQSLGLLGDDQWAADPDMYLQSPQSEHTDPHGLYLSCNGGTPAGHRQVPWPEPQSPQALPNGMAAKAQSLGPAEFQGASQRCLQQLGACLQSSPPGTSPPMATGRRGVKVAKHSSEEARPQSCLVGSAIGRPGGEGSPSPKNQESSLKHRLFRSMFLSTPATGAASSSKPVPLPQNKPNSAFRPPQKDSSSNLVAKAQSLPSEQPMGTFSPLTTSDTSSPQKSLRTAPAAGPLPGRSSPAGSPRTRHAQISTSNLYLPQDPTVAKGALGGEDTGIVTHEQFKAALRMVVDQGDPRLLLDSYVKIGEGSTGIVCLAREKHSGRQVAVKMMDLRKQQRRELLFNEVVIMRDYQHLNVVEMYKSYLVGEELWVLMEFLQGGALTDIISQVRLNEEQIATVCEAVLQALAYLHAQGVIHRDIKSDSILLTLDGRVKLSDFGFCAQISKDVPKRKSLVGTPYWMAPEVISRSLYATEVDIWSLGIMVIEMVDGEPPYFSDSPVQAMKRLRDSAPPKLKNSYKVSPVLRDFLDRMLVREPQERATAQELLDHPFLLQTGLPECLVPLIQLYRKQTSTC | 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-mediated transcription. May play a role in cytoskeleton regulation by interacting with IQGAP1. May protect cells from apoptosis through phosphorylation of BAD (By similarity).
PTM: Autophosphorylated. Phosphorylated by MAP2K6/MAPKK6, leading to PAK6 activation (By similarity).
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 74867
Sequence Length: 682
Subcellular Location: Cytoplasm
EC: 2.7.11.1
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Q869N2 | MEQSKRVSMMREKFEAQSNEAESSPPPNRKPPPPNKRVQTNGTSSLNSSGSSFVSPSPSPSPSPQQPVKRPLPSPGVNKQAPPALPTQPRPQQQQPEIPVRPTTPTRTPPNLINSNGTSGGSGFSSSSGNSGYSSSNNNNSNSNSSINMNGNHSNGLNGGSSNPVPMRKVSSPINIANGTTPPPPPQPTPSQQPQQSPSSASHNNTQHNIPSPPPLPNNKPKKLAPTAVPAGLGSIIGGPKTPAISPGSTSPSLGSSNGNIPISTTSTPITPTPPISVPLATSPNNSHKDSISNSNSNNNNNNNNNNNNNSSNATTSPPSPPVSNVGNKQDEEKKGFLSIFTNKKKNKDKKKEFSVGSPFNVKHNIHVNYHSVTGFEGLPKEWEVILQSSGITREDVVEHSEVVIDVLDFHMQQQQQQAQQEQQALMQKQMQQSGIPAHMLNNPKPPTIPIRDANKQPHNQLQPTPHQPPQHHHQQQPPQQHHHQQQQQQHNNNNNNNNNNNNNNNNQQSAQQQSAGILSQQQEQQLEEMMCGGAYDDEQYDLNNQPLPDETNVSLYDLVSQEDPTKLFGEGSTKIGEGAAGEVFVVTQLKTNNKVAIKKMPLNQQNMKLIVTEIGIMKSCRHQNIIDYIDSYLVGDSLWVAMEFMGGGCLTEILEQFNSVKLVEAQIAYVCAETLKGLAYIHSQHRIHRDIKSDNILLGSDGSVKLADFGYAAQLTKSKQKRVTIVGTPYWMAPELIRGQNYDRKVDIWSLGIMAMEMAESEPPYMSFPPLRALFLITTKGIPDLKDQNKWSDDFKDFVKKCLDKDVENRPEAKVLLNHPFLKTACNSNGLVPAIMEAKKAKEAHSKFSIH | 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 Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 93123
Sequence Length: 852
Subcellular Location: Membrane
EC: 2.7.11.1
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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)-5,6,7,8-tetrahydrofolate + 2-dehydropantoate
Sequence Mass (Da): 29352
Sequence Length: 263
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.1.2.11
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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)-5,6,7,8-tetrahydrofolate + 2-dehydropantoate
Sequence Mass (Da): 28726
Sequence Length: 271
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.1.2.11
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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)-5,6,7,8-tetrahydrofolate + 2-dehydropantoate
Sequence Mass (Da): 30258
Sequence Length: 289
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.1.2.11
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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)-5,6,7,8-tetrahydrofolate + 2-dehydropantoate
Sequence Mass (Da): 28913
Sequence Length: 265
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.1.2.11
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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)-5,6,7,8-tetrahydrofolate + 2-dehydropantoate
Sequence Mass (Da): 29855
Sequence Length: 277
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.1.2.11
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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)-5,6,7,8-tetrahydrofolate + 2-dehydropantoate
Sequence Mass (Da): 28434
Sequence Length: 268
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.1.2.11
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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)-5,6,7,8-tetrahydrofolate + 2-dehydropantoate
Sequence Mass (Da): 29258
Sequence Length: 272
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.1.2.11
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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)-5,6,7,8-tetrahydrofolate + 2-dehydropantoate
Sequence Mass (Da): 28927
Sequence Length: 268
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.1.2.11
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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)-5,6,7,8-tetrahydrofolate + 2-dehydropantoate
Sequence Mass (Da): 27996
Sequence Length: 261
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.1.2.11
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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)-5,6,7,8-tetrahydrofolate + 2-dehydropantoate
Sequence Mass (Da): 29063
Sequence Length: 272
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.1.2.11
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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)-5,6,7,8-tetrahydrofolate + 2-dehydropantoate
Sequence Mass (Da): 30234
Sequence Length: 276
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.1.2.11
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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)-5,6,7,8-tetrahydrofolate + 2-dehydropantoate
Sequence Mass (Da): 31743
Sequence Length: 284
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.1.2.11
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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)-5,6,7,8-tetrahydrofolate + 2-dehydropantoate
Sequence Mass (Da): 29691
Sequence Length: 270
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.1.2.11
|
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)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1.
Subcellular Location: Cytoplasm
EC: 6.3.2.1
|
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)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1.
Subcellular Location: Cytoplasm
EC: 6.3.2.1
|
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)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1.
Subcellular Location: Cytoplasm
EC: 6.3.2.1
|
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)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1.
Subcellular Location: Cytoplasm
EC: 6.3.2.1
|
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)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1.
Subcellular Location: Cytoplasm
EC: 6.3.2.1
|
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)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1.
Subcellular Location: Cytoplasm
EC: 6.3.2.1
|
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)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1.
Subcellular Location: Cytoplasm
EC: 6.3.2.1
|
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; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1.
Subcellular Location: Cytoplasm
EC: 6.3.2.1
|
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)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1.
Subcellular Location: Cytoplasm
EC: 6.3.2.1
|
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)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1.
Subcellular Location: Cytoplasm
EC: 6.3.2.1
|
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 at its C-terminus and an alpha-subunit with a pyruvoyl group at its N-terminus.
Catalytic Activity: H(+) + L-aspartate = beta-alanine + CO2
Sequence Mass (Da): 14315
Sequence Length: 131
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; beta-alanine from L-aspartate: step 1/1.
Subcellular Location: Cytoplasm
EC: 4.1.1.11
|
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 at its C-terminus and an alpha-subunit with a pyruvoyl group at its N-terminus.
Catalytic Activity: H(+) + L-aspartate = beta-alanine + CO2
Sequence Mass (Da): 14144
Sequence Length: 126
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; beta-alanine from L-aspartate: step 1/1.
Subcellular Location: Cytoplasm
EC: 4.1.1.11
|
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 at its C-terminus and an alpha-subunit with a pyruvoyl group at its N-terminus.
Catalytic Activity: H(+) + L-aspartate = beta-alanine + CO2
Sequence Mass (Da): 13779
Sequence Length: 126
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; beta-alanine from L-aspartate: step 1/1.
Subcellular Location: Cytoplasm
EC: 4.1.1.11
|
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 at its C-terminus and an alpha-subunit with a pyruvoyl group at its N-terminus.
Catalytic Activity: H(+) + L-aspartate = beta-alanine + CO2
Sequence Mass (Da): 14100
Sequence Length: 127
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; beta-alanine from L-aspartate: step 1/1.
Subcellular Location: Cytoplasm
EC: 4.1.1.11
|
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 at its C-terminus and an alpha-subunit with a pyruvoyl group at its N-terminus.
Catalytic Activity: H(+) + L-aspartate = beta-alanine + CO2
Sequence Mass (Da): 14546
Sequence Length: 129
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; beta-alanine from L-aspartate: step 1/1.
Subcellular Location: Cytoplasm
EC: 4.1.1.11
|
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 at its C-terminus and an alpha-subunit with a pyruvoyl group at its N-terminus.
Catalytic Activity: H(+) + L-aspartate = beta-alanine + CO2
Sequence Mass (Da): 13102
Sequence Length: 115
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; beta-alanine from L-aspartate: step 1/1.
Subcellular Location: Cytoplasm
EC: 4.1.1.11
|
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 at its C-terminus and an alpha-subunit with a pyruvoyl group at its N-terminus.
Catalytic Activity: H(+) + L-aspartate = beta-alanine + CO2
Sequence Mass (Da): 14641
Sequence Length: 131
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; beta-alanine from L-aspartate: step 1/1.
Subcellular Location: Cytoplasm
EC: 4.1.1.11
|
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 at its C-terminus and an alpha-subunit with a pyruvoyl group at its N-terminus.
Catalytic Activity: H(+) + L-aspartate = beta-alanine + CO2
Sequence Mass (Da): 12834
Sequence Length: 116
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; beta-alanine from L-aspartate: step 1/1.
Subcellular Location: Cytoplasm
EC: 4.1.1.11
|
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 2/2.
Subcellular Location: Cytoplasm
EC: 1.1.1.169
|
F4KIN4 | MESRCKKGYFRLAVIGLSKAKDCWEKNACAVTFIGDGGTSEGDFHAGLNFAAVMEAPVVFICRNNGWAISTHISEQFRSDGIVVKGQAYGIRSIRVDGNDALAVYSAVCSAREMAVTEQRPVLIEMMIYRVGHHSTSDDSTKYRAADEIQYWKMSRNSVNRFRKSVEDNGWWSEEDESKLRSNARKQLLQAIQAAEKWEKQPLTELFNDVYDVKPKNLEEEELGLKELIEKQPQDYMMLKELIPNWILGIGTLALRYDFQETLFNGWHAIAELQQLKLKIKLNSLLNDQADTESLKAARNSALNVIQAMIIHLVLTLKGRFSLPLTEETVRFNEPIQLNQNMVKDGGYTAELFPIRKEEQGEVRR | 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 2/2.
EC: 1.1.1.169
|
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 2/2.
Subcellular Location: Cytoplasm
EC: 1.1.1.169
|
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 2/2.
Subcellular Location: Cytoplasm
EC: 1.1.1.169
|
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 2/2.
Subcellular Location: Cytoplasm
EC: 1.1.1.169
|
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 2/2.
Subcellular Location: Cytoplasm
EC: 1.1.1.169
|
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 2/2.
Subcellular Location: Cytoplasm
EC: 1.1.1.169
|
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 2/2.
Subcellular Location: Cytoplasm
EC: 1.1.1.169
|
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 2/2.
Subcellular Location: Cytoplasm
EC: 1.1.1.169
|
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