Detail Information for IndEnz0010001068
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