Detail Information for IndEnz0010000488
IED ID IndEnz0010000488
Enzyme Type ID esterase000488
Protein Name Lysophospholipase NTE1
EC 3.1.1.5
Intracellular phospholipase B
Neuropathy target esterase homolog
Gene Name NTE1 KLLA0B05225g
Organism Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Saccharomycetaceae Kluyveromyces Kluyveromyces lactis (Yeast) (Candida sphaerica) Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)
Enzyme Sequence MWLTSYVLPRLKNILLLQFHITLPLNYLVLLLLSTVIITYLFLRTRILSNYSQLKDDVSDENNINRKDYMDASSASFLLNREKHKGFTSYLDEFLSAIKIFGYLEKPVFHELTKSMKTEKLQEGEIVLLDDSVGFTIVVEGTLEILHKMDNRHSNPSGDAAANATAFEPPSNDDGYLINGEKFQLLNIVKTGNPLSSLVSIMKLFSNRSTHLNEGTHPSTTNNTPGPGSPNLTGEINSFLDSTLPAKFGSADSANGNHPISPMELESTFDNLSEASENDRSAKIPDIIARAASDCTIAIIPSSSFQRLLVKYPRSASHIIQMILTKLYRVTFKTAHTYLGLTNEIIFTEFQSINKDNLKLPEYFRRSIISYFTNRQDDTGSSASTIQKRPQLHRRDSNNSLNYGSRHVVLNSRDQYNPGDLLSNVPLPRLNPQQRNDLSNTNSSSTLSRADYRPIILNNFSSSQFEETEVSSWRLALVEIIFQQLGITKDTIEPPISDDFSLHDHSLDEKGLVRRSSYSSFTSLSSSIATHSSNHLVTFLPRESQQFSRLNRTGGKMASHSKRLNGSSRSNSRTDRSESFDHFRNENLGGDNQFSDFESVKEDFSKCIKILKFEEGETILCQNSNPQGIYYLVSGEVDVISETKDGNTDESYERTLYTATEGYILGYLSSILGCKSLVTLKVSKGPAYLGLIPYNDLERLCDKYFMIYLKLSEILTNSLSPNLLRLDYFLEWIQLDSSETLFNQGDPANGVYLVLNGRLRQLFYEDADSDIVTQMAELSKGESFGEVEVLTAIHRLNTVVAIRDTELARIPRTLFEFLAVEHPSIMIHVSRMVAKKAMLMNFKSGIGFSGSQPITKLIGDETAMQKRYDFNLNIKSNKSSKKNELISNTVNYKTLTLLPITEGLPVEEFAYKLINALRQCGKTTIGLNQRTTLSHLGRHAFNKLSKLKQSGYFAELEELYEIVVYIADTPVSSSWTQTCISQGDCILLLADATCDPKIGEFERLLLKSKTTARTDLILLHPERYVVPGSTSKWLKNRMWIQSHHHIQFTPMEKVAEPDPIPNIKPLSQLVEKFKENTKKTQENFVKFLPDSIKTTVETLSGKYIDPKPNPKFYTSVDPIKNDFLRLARTLSGQAVGLVLGGGGARGLSHLGIIKALEEQGIPIDIIGGTSIGSFVGGLYAMDYDLVPIYGRVKKFAGRVGSLWRMLSDLTWPVTSYTTGHEFNRGIWKSFRDYRIEDFWISYYCNSTNITESVQEIHSSGFAWRYIRASMSLAGLLPPIVDNGNMLLDGGYVDNLPVTEMTQRGCKIVFAVDVGSVDDRTPMSYGDSLNGFWIVLNRWNPFSKHPNIPNMAEIQMRLGYVASVNALERAKSTPGVVYIRPPIENYATLDFGKFEEIYQVGYAYGHDFLQHLQEKNELPPIAGTTTSAYADKENMLQRRNSI
Enzyme Length 1441
Uniprot Accession Number Q6CWC2
Absorption
Active Site ACT_SITE 1170; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161; ACT_SITE 1288; /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 592..718; /note=cNMP 1; NP_BIND 707..836; /note=cNMP 2
Features Active site (2); Chain (1); Compositional bias (3); Domain (1); Motif (3); Nucleotide binding (2); Region (4); 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 1141..1146; /note=GXGXXG; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161; MOTIF 1168..1172; /note=GXSXG; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161; MOTIF 1288..1290; /note=DGA/G; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161
Gene Encoded By
Mass 162,157
Kinetics
Metal Binding
Rhea ID RHEA:15177
Cross Reference Brenda