Detail Information for IndEnz0010000489
IED ID IndEnz0010000489
Enzyme Type ID esterase000489
Protein Name Lysophospholipase NTE1
EC 3.1.1.5
Intracellular phospholipase B
Neuropathy target esterase homolog
Gene Name NTE1 LELG_05397
Organism Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Debaryomycetaceae Candida/Lodderomyces clade Lodderomyces Lodderomyces elongisporus Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus)
Enzyme Sequence MEEELAIEDLPRLTGTVSLNNGLLHSIYNETTVFKILRWSLVEIPKYILKLMSKNLEINLNVSSILIITLLIAAGILVIVRYKFLTGYSEDIKKGGSNANTKALGQQSTNYPKSTSSGLFVEKSKDKKPSNYLDEFLMAIKVFGYLDKQVFHELTKSMTTQKLSRDEVMCLDEKIGFLIVVEGTAQVYTKVTKKSNRNKYDELGQNGRDEGEEADEDDEEEEKEVGDDGDDEMDVEAMRNRGNGTKNGKMHGLDTDNFEENDDFLKLGEQNYQLLNEVKSGAALSSLISTLDLFKPLKSESTLTPLDSMGSGVSLNLDYLDRAGARLKALENDSDADTRDSTYPDIIVRPKKKKHSDTITVAIIPQSAFERVQMKYPKSTSHIVTMVLTRLYKVTMTTIHNYLGLTGEIFKLEIELNKSCELGLPRYLVDGLIERLSQGGSNERKQQAKHFRRSPLERTQSRYVLLNSRVKSNNPGDLLSSVPISRDDPKLRVNKSSAPTLVDGSNRINFTDNIEETEENSLRIAIIENIFKIVGINEAQNLPHEQAPFRSLNSSANSSSIALNSPGYFSPNLPATTGRHHNVLKFSSNDSLMNTISLSQLKSQKTHSISRGSTTQKQLYKRRNPITEMNIKDAFAKVMELKYIEPNTTVVQQNSVFCGLYYVINGSLEVHYKQAETYSKSATSKHVYTVGAGGIAGYMSCVVGFRSLVSIKTPKKTGAVVAYIAKNDYNQLLDKFYFLQLPMATKLKSLLSKQVMTIDYALEWCHIPAGNVLCSQGDLANGFHVVLSGRFRVVRKEKRKGSNRDEVKVLGEYGHGESIGEVEVLTASRRSNSLIAVRDSETARIPRTLFEILSFQNPSIMVKVSRLVASKVLSSEKTLSQATHSFITSSSNESFISADYKTITILPTVSGLPVRDFADKLVHSLKAIGRNVIALDQALTLTHLGRHAFDESLVRLKLSGYFAYLEEEYETVVYICDTPVQSNWTSTCISQGDCVLLLADADDQYTASSVGEYEQLLIKMKTTARTDLCLIHQEKFVVSGSTSRWLKNRMWVQGHHHIQMYIERNNETIGPGKKSFINEMAAKFVQNKSLISKFEEARSKALSWRREEQLKDLTLGSHKSDFLRLARILSNEAVGLVLGGGGSRGISHVGVVTALERHGIPVDLIGGTSIGSFVGGLYAKDYNIVSIYGRAKKFSKRVSSVWRMIFDLTYPVTSYITGYEFNRGIWKVFGFTEIEDFWIKYFCNSTNITNSTMDIHESGYAWRFIRASMSLAGLLPPIAFKGCMLLDGGYLDNLPVMEMKRRGAKHIFAVDVGSVDDRTPMDYGDTLSGFWVVFNKWNPFSKHPNVPNMMDIQLRLAYVASVNALEEAKRTPGVYYLRPPIDNYATLDFGKFDEIYQVGLGYADKLFTEWENKKQLPEIAGFVKRDGMQNGGERIKMYRRNTM
Enzyme Length 1443
Uniprot Accession Number A5E708
Absorption
Active Site ACT_SITE 1169; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161; ACT_SITE 1287; /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 619..750; /note=cNMP 1; NP_BIND 746..871; /note=cNMP 2
Features Active site (2); Chain (1); Compositional bias (2); Domain (1); Motif (3); Nucleotide binding (2); Region (2); Topological domain (2); Transmembrane (1)
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:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif MOTIF 1140..1145; /note=GXGXXG; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161; MOTIF 1167..1171; /note=GXSXG; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161; MOTIF 1287..1289; /note=DGA/G; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161
Gene Encoded By
Mass 161,900
Kinetics
Metal Binding
Rhea ID RHEA:15177
Cross Reference Brenda