IED ID | IndEnz0010001068 |
Enzyme Type ID | esterase001068 |
Protein Name |
Lysophospholipase NTE1 EC 3.1.1.5 Intracellular phospholipase B Neuropathy target esterase homolog |
Gene Name | NTE1 UMAG_01230 |
Organism | Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Basidiomycota Ustilaginomycotina Ustilaginomycetes Ustilaginales Ustilaginaceae Ustilago Ustilago maydis (Corn smut fungus) Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus) |
Enzyme Sequence | MSQVPVASPASWSSVASAAAAAVSAATSASSSLAASVDEPAATTATAATASYADERNPLIALFDGLLRVVLASLNLIRILATFSTITVPSLVYAILHYSLTLQLNFPSLALLFLTSLISAFIWLRYRHLNKYERLREVPITRDEGFNLNPDVASPGGDNDRGSFHNYLDDFLQAIRIFGFLEKPVFHELARHLQTRRLVAGDSLSLDTDFSFYIVIDGHVQVYAPLPSATASAVGQDSVEDEDDSGYQLLNEVESGGTLSSLFTILSLFTEDVKLSFDDHDDPHLAPPHPAYPAMDRLNNSSAANHLGRGNNATAPTSPYSSAFNPPSQTAAQLQLNAAALRNVPAAISTEGAVERLGGSAAVRSTSKSSHARTASSGTASATVQDGDTSTIMDPLEQNDDGVTSSLYHAPDLQMPPAQAAAPFSHFAPSYHPSPAGTPISSLPGSTHSPYFRGRATSIHALHEAAGGPNTPGSILSAMSSSAHGHYHPQADYLPRQGAGTVARATVDTTLAVIPAEAFKRLTKKFPNAAAHIVQVILARLSRVTFHTAHKYLGLTKEVMRTEKSINDLACFPLPSEFYEKGGMDKLRHRFLPQPNSKRETTVDDDYFRDFQEWTSISQRSSTPVPGSKDDTKDAATSSPPKVRIASDLPSLTTSSKQSNQKPTSSRISAARTPWGHPDPPLKTPTARNMVGPGDLLSMASLSQDGWYTTGFDMHSAQPTPRAKPRSVSKLEPFHGPLPHPVDDSTDGTSPLSGASPIPIRKGSSTMYHQGEAIGTDRPFANIGLPHFDIKNEVMDCIAKSIGLAQAAHSPLAPSYQASPHINAQDSLLQRSVFKSAFGSLSMLDAAMAEEESSITGTNSSMAGHGHSGFHPSDFENEVEIKFFPAGSTLVKAGESRAGLFYVIDGFLDVLLPAEANELEEEDRLKPNMNHKSAKTDASSGSSRQNRPGSHRKDSSSASLRAGLLDERNLREADVSLPQRRGTEADRISSNGDGNSGSVHRPAMREGSSSSTSYGTPAGLRKKPTESAKVGNALDGTGGAGSSSRRKPSHVSSGSGATTMPRHPDATNSNMAFTAKQPVLHPSLHQQQPLRGKPSQQSSQRSKDGKRSIFTVGRGGIAGYLSSLLGTASYVDITAKTDVYVGFLPAHALERIMERRPIVLLTLCKRLLSLLPPLILHIDSSLDWQQVNAGQVIYREDDPSDSFFIVINGRLRAITEKTNGIEVHNEYGQGDSVGELDVITNSRRRTTLHAIRDSELAKMPSTLFNAISVRHPAITIQISRIIARRVRTELVRSKQEGAALGAPIPGLPDLGRNNLNLKTVAIVPVTRQVPVIDFAAKLQTAFDDTIGGRAIFLDQSSVMGVLGRHAFSRMGKLKLAGWLADLEQKYRLVVYVVDTPVSSAWSQTSIRQADCVLMVGFGDEPAMGEYERLLMSVKTTARKELVLLHPERSVPPGSTREWLKNRPWVHAHHHVEMPGLTGSHAGAAISTGGDPKAVKALRNLKQKLETSLQRYRKTMTPLSASGRPHHASDFARLARRLCGMSIGLVLGGGGARGCAHLGVIRALEERGIPIDMVGGTSIGSLVGGLYAREAEMVSTFGRAKRFAGRMASLWRFASDLTYPVVSYTTGHEFNRGVFKAIQETHIEDMWIPFFCNTTNITWSRMEVHTSGYAWRYIRGSMTLAGLIPPLVDEGNMLVDGGYVDNLPVTVMLAMGARSVFAVDVGSIDDTSPRAYGDTLSGWWVLLNRWNPWSDASKIPSIPDIQGRLTYVSSVKTLEEAKKVKGCFYMRMPVEEFGTLAFGRFDMIYEKGYKAAVELLDGWDAEGKLPSGTEREDFEDDWEDGDEYEEYEVYTDDESGVGGGVRKIRKKRRRTRRKAGISARRNSI |
Enzyme Length | 1883 |
Uniprot Accession Number | Q4PF83 |
Absorption | |
Active Site | ACT_SITE 1577; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161; ACT_SITE 1695; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161 |
Activity Regulation | ACTIVITY REGULATION: Inhibited by organophosphorus esters. {ECO:0000250}. |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid + H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5; |
DNA Binding | |
EC Number | 3.1.1.5 |
Enzyme Function | FUNCTION: Intracellular phospholipase B that catalyzes the double deacylation of phosphatidylcholine (PC) to glycerophosphocholine (GroPCho). Plays an important role in membrane lipid homeostasis. Responsible for the rapid PC turnover in response to inositol, elevated temperatures, or when choline is present in the growth medium (By similarity). {ECO:0000250}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | NP_BIND 863..1158; /note=cNMP 1; NP_BIND 1166..1285; /note=cNMP 2 |
Features | Active site (2); Chain (1); Compositional bias (10); Domain (1); Motif (3); Nucleotide binding (2); Region (7); Topological domain (3); Transmembrane (2) |
Keywords | Endoplasmic reticulum;Hydrolase;Lipid degradation;Lipid metabolism;Membrane;Reference proteome;Repeat;Transmembrane;Transmembrane helix |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | MOTIF 1548..1553; /note=GXGXXG; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161; MOTIF 1575..1579; /note=GXSXG; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161; MOTIF 1695..1697; /note=DGA/G; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161 |
Gene Encoded By | |
Mass | 203,826 |
Kinetics | |
Metal Binding | |
Rhea ID | RHEA:15177 |
Cross Reference Brenda |