| IED ID | IndEnz0010001009 |
| Enzyme Type ID | esterase001009 |
| Protein Name |
Lysophospholipase NTE1 EC 3.1.1.5 Intracellular phospholipase B Neuropathy target esterase homolog |
| Gene Name | NTE1 CAGL0L11154g |
| Organism | Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Saccharomycetaceae Nakaseomyces Nakaseomyces/Candida clade Candida glabrata (Yeast) (Torulopsis glabrata) Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata) |
| Enzyme Sequence | MDSSSIAHESDIVSTERNILPERFISNKQQGNYLEDGSGDGNGKAAEHWLLAAIFNFFWVISYFISGSTHIAFRSSWYIVSLLLLKFPKWIIVEANHIHLTIPFSVLVVTLAIIFYVSYEFLKGRLLSEYKNLTSDLNTDSLNSKNSKSSRLLHHDSKDSNTTRRRRYSSGKLLSSALHESHSGINGGDDGDDTFLSSYLDQFLSAIRIFGYLEKPVFHDLTKNMKTQKLDEGEILLLDNSVGFAIVVEGTLDIYHEVEEKGNMNDIDGDFMVDDNQSIYSILKRKKKKYSTSRHGQYNNNSDPGHYNGHNVNGDDEDDDDGILQMRSSSRNQNIPSFDAIESSSSDEESDINDGDSESQSESDDESTGFIRLKDGLGKFQLLNTVKAGNPVSSLVNILNLFTSANDNVTSPSRTGRMDSNYTNPVERPTSKLSTSIEESAMRLELGKYSLSPTEASYRSTSNPSNNFSKDNDPLSKSISGPDAVTTPSLPPLNNRAFVIPKVVARAATDCTIAIIPPQAFAKLKAKYPRSASHIIQMILTKLYHVTFQTAHKYLGLTQEIAYTELLLNRTVSYDLPNYLKEIVIDRFKDKGKDMNLQKGFQSPTSSRLTSNFNGNSNNQRTNSRNSQALMSTRDLRKTRPELSQQSSMIHSPTPITGSRHVVLESRDKYNPGDLLSNVPLSRINLASPSSRGFDYSSMKKESSPQSSVNSRKRSTTGERPRLLKRPSIYNNQSSSRSDALKGNNSNNKDINFTSFSAQEETEDSVVRMALVEAMLTYLGVNKTNMSILPGIYDGAPSEPHSHRASEISLVSSYTSSAAPQTTIRILPKEYAIVSTRKQKQSSKKRRKYKEEISPTLDYEYAKNEFAQAIELQYFKQGTVIVEQDTRGKGLYYVVSGKIDVTTSTVSDHEIFNSTRDKKKKKSKTLFTIESGGIAGYLSSLVSYKSFVTLIAKTDVYVGFLPYQTLEKLCDKYFLIYLRIAESLTSLLTPRMLKLDHALEWLHLNASDTLFNQGDPANGIYVILNGRLRQLRNPELEENSTDYPNDGEEKDSSRDSTIVMGELGQGESFGEVEVLTAMDRISSMVAVRDTELARIPRSLFELLAIEHPSIMIRVSRLVAKKILGQGQANMALPKIGSGSNLRHDLNLTIPPSSSSSIHTHSYGNDNSNQMNNANFRTITILPITSGLPVESFAMKLVHAFKQVGRTTIGLNQRTTLSHLGRHAFDKLAKLKESGYFAELEELYQTVVYIADTPVKSSWTKTCIAQADCVILLARADDSPEIGEYERLLLKSKTTSRTELVLLHNERSVEPGMTQRWLRSRSWVHNHYHIQFAMDSLVNSSNVKDTGGNIGALNLVDKFIQTELGRKTQYNISKLLPESIKMTVENFSSRFMKRKRQYYTPVHRHKDDFLRLARILSGQAIGLVLGGGGARGLSHLGILQALEERGIPIDMIGGTSIGSFVGGLYAKDYDLVPIFGRIKKFAGRISSIWRMLSDFTWPVTSYTTGHEFNRGIWKSFGDTRIEDFWVQYFCNSTNITESVQEIHSYGYAWRYVRASMSLAGLLPPIEDNGSMLLDGGYVDNLPVLEMKARGCNTIFAVDVGSVDDRTPMKYGDSLNGFWIILNRWNPFSKHPNIPTMAEIQVRLGYVSSVNALEKAKRTPGVIYVRPPIENYATLDFGKFEEIYKVGADFGKVFLQALAEEGKMPYIPGSNADLVGDVETGFFLHRRNSI |
| Enzyme Length | 1728 |
| Uniprot Accession Number | Q6FKJ1 |
| Absorption | |
| Active Site | ACT_SITE 1455; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161; ACT_SITE 1573; /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 854..987; /note=cNMP 1; NP_BIND 983..1121; /note=cNMP 2 |
| Features | Active site (2); Chain (1); Compositional bias (7); 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 1426..1431; /note=GXGXXG; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161; MOTIF 1453..1457; /note=GXSXG; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161; MOTIF 1573..1575; /note=DGA/G; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161 |
| Gene Encoded By | |
| Mass | 193,367 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:15177 |
| Cross Reference Brenda |