Detail Information for IndEnz0010001529
IED ID IndEnz0010001529
Enzyme Type ID esterase001529
Protein Name Lysophospholipase NTE1
EC 3.1.1.5
Intracellular phospholipase B
Neuropathy target esterase homolog
Gene Name NTE1 CHGG_04763
Organism Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970) (Soil fungus)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Sordariomycetes Sordariomycetidae Sordariales Chaetomiaceae Chaetomium Chaetomium globosum (Soil fungus) Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970) (Soil fungus)
Enzyme Sequence MDVVNSTARAAVTSATAVTAVTGTGDRHPNPLSSAVAAASDVANAHGSSSWLGLFARVVLWLLQFVSMVLYYAIKLATISVPTLLYTLFSTSLTVTMNATTLMLIVAAMIGAISWVVRYRYLNMYSRLPPEPQRKEPDVDLFPDTHEEGIKSGLSNYFDEFLSAIKIFGYLERPVFHELTRSMQTRKLIAGESFNLEEEKGFCLVVDGLVEIFVKSSSYNRRYPHGPYFSPNSEAPSSDDEHPAPGQQRYQLLTEVRNGAPMSSLFSIMSLFTEDVPLRHADEDNSEPGTTTHSGLFPNYPASADFRKSRVRMDSVPNTPQMDASASSSANNLPGQLDRGLPHVPPISLDGTGFSKPQRPVPKRSNTTSAHPDIIARATVDTTVAIIPASAFRRLIKIYPKATAHIVHVILSRFQRVTLATAYNYLGLTNEVLQIERQMLKYTTQQLPNHLRGDALDRLKEKFKREVERMGEEDDVSKGIALHNARAGRRRRSTATLRKEAALQAFSKQRNISSMSGSSLAIPNAGDLVTHLQQSRGGGNRAQSVAFTDGPSPHLDVEREAVSPLAQRTFDPFVTPRSIHVALEKRETLDEDNLFRESILECMFRSIGLTGSGGSNKDADSNQASPRLISFDQRRQKALYTNHAFGFMDGLDGSADGDTESITSAGLSLPASPNPQFLAQEMRDEMEIVFFPKGSVLVEQGERNPGLYYVVDGFLDICTQEDAAASDVVHPTSRTSLHAMDSAQSIRSPQRSPQPFAESMRSGNKVDDAEIKSKPNRRSVALIKPGGLAGYVGTISSYRSFIEVVAKTDVYVGFLPLTSIERIVDRYPIVLLTMAKRLTNLLPRLILHIDFALEWLQVNAGQVIFHEGDESEAIYIVLNGRLRLVEDRKDGGMNVKAEYGQGESIGELEVLTETSRSGTLHAIRDTELVKFPRTLFNSLAQEHPNITIKISKIIASRMRALIDDPSTMLGIKDSSGRSSINKSSTTLNLRTVAVLPVSAGVPVVEFSNRLLSALTEVGAPNGATSLNSAAVLNHLGKHAFNRMGKLKLSQYLADLEEKYGLVIYVADTNVNAPWTQTCVAQADCVLMVGLADGSPEIGEYERFMLGMKSTARKILVLLHQERYSNSGLTRKWLKNRVWINGGHFHVQMTYSPNAVPIHPPAKPSGPTLRERVQILQAEIQKYTSRKVRHSPFYSPDAPFKGDFHRLARRLCGKSVGLVLGGGGARGIAQIGIIRAMQEAGIPIDIVGGTSIGAFIGALYARHADFVPIVNAAKKFSGRMASMWRFALDLTYPSASYTTGHEFNRGIFKAFGNTQIEDFWLDYYCNTTNISKSRAEFHTSGYAWWYVRASMSLAGLLLPLCDEGSMLLDGGYVDNLTVSHMKSLGSDVIFAVDVGALDDNTPQAFGDSLSGMWAFFNRWNPFSSVANPPTLAEIQARLAYVSSVDALERAKTLPGCIYMRPPIEEYGTLDFGKFMEIYGVGYKYGQEFLAKLRERGGVLPIGEEMGGKKGLRRTMAPRRASI
Enzyme Length 1521
Uniprot Accession Number Q2H0D3
Absorption
Active Site ACT_SITE 1250; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161; ACT_SITE 1368; /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 670..789; /note=cNMP 1; NP_BIND 837..957; /note=cNMP 2
Features Active site (2); Chain (1); Compositional bias (2); Domain (1); Frameshift (1); Motif (3); Nucleotide binding (2); Region (3); 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 1221..1226; /note=GXGXXG; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161; MOTIF 1248..1252; /note=GXSXG; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161; MOTIF 1368..1370; /note=DGA/G; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161
Gene Encoded By
Mass 167,339
Kinetics
Metal Binding
Rhea ID RHEA:15177
Cross Reference Brenda