| IED ID | IndEnz0010001043 |
| Enzyme Type ID | esterase001043 |
| Protein Name |
Lysophospholipase NTE1 EC 3.1.1.5 Intracellular phospholipase B Neuropathy target esterase homolog |
| Gene Name | NTE1 DEHA2E04400g |
| Organism | Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Debaryomycetaceae Debaryomyces Debaryomyces hansenii (Yeast) (Torulaspora hansenii) Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii) |
| Enzyme Sequence | MSTIEIVSTVAEYTEIHSPVSSKFLLPSARDSSSSISLFSAIFWFWSWLFFKIMNIFLYYIPNIIVNLFSVNFQITLSLSSIVITLTGIISFCFLIVRYKYLTRYSKTTKSTDKPKSSNKNIDLVGSIKKNKRGDSKSTSNYLDEFLSAIKVFGYLERPVFHELTRNMTTQKLSSEEILYLDEKLGFSIVVEGTIQVYTKVNSVNSSTTSNSDDNELNFEKDDLLTIGDQCYQLLNEVKSGSPLSSLMSTLDLFKPVDPDTMSNRLFSPFELDSNPASNPLSPDNTGSKSFDPLSSGNFNDTSLSSSDRNYPNIVARPKPIEDSNNLNTATIAIIPYSAFQKVQSKYPKATSHIVTMVITRLYKITMNTIHSYLGLTREIIRSEIQLNESEGAKDSLPSYLYDGVIEKFYGDKNNETLLNKTAESPSVSINKTSSSSSSLPKKSTTSLRPLNRNQSSRYVVLDSRSKSTHPGDLLSSVPLSRRSDYYQTHTTIQPDPEEVRSQSRTKMTSPVLPKRQISSNGGPTLKGHSSSTTKFENIRDRTFSDEREETEETSLRIAIIENIFKILGINEVSNMIGSMSDLNSRSSSVNSSVVGLPSLMNNGNESKYPNGIFDFNTGKVRYDSISSFPTSLNKGANNNLKFYDTVNQSQLKDMDHENDKSSQVDINNLMFKRKSIPIQSFESNFYDVKNEFSKHLNIKYFGPNTTLVEQESFNSGLYYVIDGTLDVFYKPASKESENLTPMNKKKLYTVKSGGLAGYLSSIIGVRSLVSISTPGDKGVIVAHIPKNEFSKLLDKFYFLQLPVASKLKSLLSSQILTIDYALEWCHIPAGDVLCSQGDLANGFHIVLSGRFRVVRYNNNKSSEVNPDDNTDIHDYNNNLIDESLSYKSRKKKDDITILGEYGHGETIGEVEVLTASRRTNSLIAVRDSETARIPRTLFEMLSLRNPSIMVKVSRIVANKMAKKDNIGIPSTISSNVPLIVTNTDSHISNDYKTITILPTVSGLPVRDFADKLVSALKNIGRNVIALDQASTLTHLGRHAFDERLAQLKLSGYFAYLEEEYQTIVYVCDTPLKSNWTSTCISQGDCILLLADADDDDVATNIGEYERLLMKLKTTARTDLCLIHADKYVEPGSTSVWLKNRIWVQGHHHIQMEIARDNSVQQGQKTSIIKNIAAKISSRTNTNIKSRLENVKTKAILSLNKFNNRLSRRTHSYKTVQAHKNDFLRLARILSNESVGLVLGGGGSRGISHVGVVMALEKHGIPIDLIGGTSIGSFVGGLYAKDYNIVSIYGRAKRFAKRVSSWWRMVLDLTYPVTSYITGYEFNRGIWKIFGSSEIEDFWIRYFCNSTNITNSTMDIHESGFSWRFIRASMSLAGLLPPITYGGSMLLDGGYLDNLPVMEMKKKGAKYIIAVDVGSVDDRTPMNYGDTLSGFWVLFNRWNPFSRHPNVPNMMDIQLRLAYVASVNALELAKKTPGVIYLRPPIDDYATLDFAKFDEIYHVGMAYADNLLTRWEQTGKIPPIAGMIDRSRIRNGEERKSLYRRSSI |
| Enzyme Length | 1544 |
| Uniprot Accession Number | Q6BQK9 |
| Absorption | |
| Active Site | ACT_SITE 1270; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161; ACT_SITE 1388; /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 681..811; /note=cNMP 1; NP_BIND 807..960; /note=cNMP 2 |
| Features | Active site (2); Chain (1); Compositional bias (3); Domain (1); Motif (3); Nucleotide binding (2); Region (2); 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 1241..1246; /note=GXGXXG; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161; MOTIF 1268..1272; /note=GXSXG; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161; MOTIF 1388..1390; /note=DGA/G; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161 |
| Gene Encoded By | |
| Mass | 173,122 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:15177 |
| Cross Reference Brenda |