Detail Information for IndEnz0010000534
IED ID IndEnz0010000534
Enzyme Type ID esterase000534
Protein Name Lysophospholipase NTE1
EC 3.1.1.5
Intracellular phospholipase B
Neuropathy target esterase homolog
Gene Name NTE1 CIMG_08886
Organism Coccidioides immitis (strain RS) (Valley fever fungus)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Onygenales Onygenaceae Coccidioides Coccidioides immitis (Valley fever fungus) Coccidioides immitis (strain RS) (Valley fever fungus)
Enzyme Sequence MNLTTTMPAAVAPDPPAQLAVSSRSLSDSSDAAGASRTSSSCRASSPSHCPTHAWNPDPPPSSLQPVFSFSPSLPPPCPSPAISSCPPNTLSPPNLLQGIVSQLAMASYIGRLLLYLFQVVPSLLYWAITFTTITVPTALFTLFSMSLTFTMNFTTLLIIVLLLVSTVSWFIRYRFLNIYSRLPPEPQRKEPEIDLFPDSQDGDSKPGLSNYLDEFLSAIKVFGYLERPVFHELTRTMQTRKLIAGETLLLEEEKGFCLVVDGLVQIFVKSIQERDDDRDGWQLDEAVEDSVDEDDEIRRRGHQGYQLLTEVKNGASMSSLFSILSLFSEDIKLRHNEDMESSSSSFNNVPAPDSNPMSPALLLESPTRVSFPDQRDIPTQPSADTLPKVSPLALEGSPGPFEHDPKPRGHRRKRPSRPKRAKSVHPDILARAMVDTTIAIIPASAFRRLTRVYPKATAHIIQVILTRLQRVTFATAHSYLGLTTEVLSIEQQMTKYTSFDLPNHLRGAALDKLKSKFTKEKERLGPEDGTKGIALHNPALNRRRRSSSSLRKDAALHAKLTAVRGKGSASNPIRYGDHESTGVSPGDLLSTIQLSRFGPRYGSERLNGRSVFYDAASGMKTPAGGPPSPLATPGQPLFRFPAQNVTFQRQDSLDQDAIFRESILDCMMKALGLTGSTQDALRKTHNSGDASPHLVSYDSRRQKAVFNNAFGFIDPYDGFGDGDSESLMSMSVTSAGGTSPVHNLRTELQDEIEIVYFPKGSVLIEQGEHNPGLYYVIDGFLDVGIPVNEKGEDLIGSSRRPTAEDILLPITGNASRVSSTLGTAHNQRKKASRRSLYMVKPGGVEGYIGSITSYRSFTDVTAKTDVYVGFLPRAVLERIADRYPLVMLTMAKRLTTVLPRLILHIDFALEWVQVNAGQVIHHQGDESDAIYIVLNGRLRAVLDKGDGKVSVLGEYGQGDSVGELEVMTESTRPGTLHAIRDTELAKFPRTLFNSLAQEHPGITIQISKLIAQRMRHIIDNPLEKGSDKGSPDSAKPTTSTLNLRTVAVLPVTAGIPVVEFGNRLLNAFNQVGVTNGVTSLHQADILNHLGRHAFSKMGKLKLAQYLADLEERYGMVLYVGDTSVNAPWTQTCIAQADCILLVALAEGSPAIGEYERFLLGMKTTARKELVLLHAERYSQPGLTRQWLKNRMWINGGHHHIQMAFRLTAEPVHPETKRLGAVLKQRVQVIQAEIQKYTSRRIRQTPVYSTSTPVKGDFHRLARRLCGKSVGLVLGGGGARGIAHIGVIKALEEAGIPIDIIGGTSIGSFIGALYARDADVVPAYGRAKKFSGRMASMWRFALDLTYPSASYTTGHEFNRGIFKAFGNSHIEDFWLEFYCNTTNISKSRLEFHSSGYAWRYVRASMSLAGLIPPLCDEGNMLLDGGYVDNLTVARMKSLGADVIFAVDVGAIDDNTPQGYGDSLSGFWALVNRWNPFSSLPNPPTLSEIQARLAYVSSVDALERAKSTPGCLYMRPPIDAFGTLDFAKFDEIYQVGYKFGKEFLDRLKNEGGLPIQEETEEKKKLRRTMAPRRASI
Enzyme Length 1575
Uniprot Accession Number Q1DLC7
Absorption
Active Site ACT_SITE 1305; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161; ACT_SITE 1423; /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 737..856; /note=cNMP 1; NP_BIND 894..1014; /note=cNMP 2
Features Active site (2); Chain (1); Compositional bias (3); Domain (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 1276..1281; /note=GXGXXG; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161; MOTIF 1303..1307; /note=GXSXG; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161; MOTIF 1423..1425; /note=DGA/G; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161
Gene Encoded By
Mass 173,384
Kinetics
Metal Binding
Rhea ID RHEA:15177
Cross Reference Brenda