| IED ID | IndEnz0010001057 |
| Enzyme Type ID | esterase001057 |
| Protein Name |
Lysophospholipase NTE1 EC 3.1.1.5 Intracellular phospholipase B Neuropathy target esterase homolog |
| Gene Name | NTE1 SNOG_08222 |
| Organism | Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume blotch fungus) (Parastagonospora nodorum) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta dothideomyceta Dothideomycetes Pleosporomycetidae Pleosporales Pleosporineae Phaeosphaeriaceae Parastagonospora Phaeosphaeria nodorum (Glume blotch fungus) (Parastagonospora nodorum) Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume blotch fungus) (Parastagonospora nodorum) |
| Enzyme Sequence | MAAPDAMTSLVKSSVALLSSAHESLPTSLAAMKTAETAPSSTFGILGRVILSILSVLPTLLFWVSYTLPTWLFTLFSMSLTFTMNFTTLMLVLVFVVSTISYFVRYRYLTMYARLPPEPQREEPQVEVFPESQEGDSKRGLSNYLDEFLSAIKVFGYLERPVFHELTRTMQTRRLAAGETILLEEEKGFCLVVDGLVQIFVKSNREESDSDEDDGELQGESGGGSAQAHRQGYQLLTEVKNGAPMSSLFSILSLFTEDVKLRHDEDSGPSSSTPMSPQHRPSMTRNSSFNMDDSRPETPIEAQEATIRRRRTSALASPTAGGRLSNVPPLSLDTDGFNDNFKHSKQRRSPSRSTKPKSAHPDIVARATVDTTIAIIPATAFRRLTRIYPKATAHIVQVILTRLQRVTLATSHAYLSLTNEVLRTEKLMNKYTTYDLPGFLRDAPLERLKEKFTKETERLGSDEGMKGIALHNPGAGRRRRTSVSIRSSTAAQARLAAARGTSIGSNVEAISRLTSPEQGMRNDRISAGDLLTNTQMSRGTGRSGRSSFSQPYQHDVRRDARTPLDASGFNPFASPSMRPNLHRQESIDEATVFRESVLGCMFKAIGLTSPENPVPRPAASVEQSPRLVSFDAKRQKAIFTSAFGFMDPYEASRDGDADSVASASNLSTLSASGNGNLLEEVVNDVEIVFFPKDAVLVEQGERNPGLYYVIDGFLDVSVAVEEDSSESNVLGTLPTGPAVTEDDLFGPPLQPTATNTSLRNGENSKKKRSRKSLFMTRPGGLAGYLGTVSSNRSFVDVTAKTDVYVGFLPRASIERIVERYPVVLLTMAKRLTTLLPRLIQHIDFALEWVQVNAGQVIYNQGEESDAIYIVLNGRLRAIKDAENGKVTVIGEYGQGDSVGELEVLTETARPGSLHAIRDTELAKFPKTLFNSLALEHPGITIKISKIIASRMRALVDDPLHEQSKERSNKATRTNVSSTVNLRTVAILPVTAGIPVVDFASRLMNALNQIGVPRGVVSLNQAAILNHLGRHAFNRMGKLKLSQYLADLEEKYGMVLYVADTPVKSPWTQTCISQADCILLVGLAESSPNIGEYERFLLTTKTTARKELVLLHAERYCPSGLTRKWLRNWPWINGSHHHMQMSFRATAEPVHQTGRRLGNAIKQRVQVIQAEIQKYTSKRVRQTPLYSADTPFKGDFHRLARRLCGKSVGLVLGGGGARGISQIGIIRALEEAGIPIDIVGGTSIGSFIGALYAWDADVVPMYGRAKKFSGRMGSMWRFALDLTYPSASYTTGHEFNRGIFKTFGNSQIEDFWLEFYCNTTNISKSRSEIHTSGYVWRYVRASMSLAGLLPPLCDNGSMLLDGGYIDNLTVAHMKSLGADVIFAIDVGSLDEDTPQAFGDSLSGFWATFNRWNPFSTHANPPTLSEIQSRLAYVSSIDALERAKNTPGCRYMRPPIDPYGTLDFAKFEEIYEVGYKYGKGFLAQLREQGVLPVTEETEKEKNLRRTMAPRRASI |
| Enzyme Length | 1512 |
| Uniprot Accession Number | Q0UJ42 |
| Absorption | |
| Active Site | ACT_SITE 1242; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161; ACT_SITE 1360; /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 669..793; /note=cNMP 1; NP_BIND 830..950; /note=cNMP 2 |
| Features | Active site (2); Chain (1); Compositional bias (2); Domain (1); Erroneous gene model prediction (1); Motif (3); Nucleotide binding (2); Region (4); 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 1213..1218; /note=GXGXXG; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161; MOTIF 1240..1244; /note=GXSXG; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161; MOTIF 1360..1362; /note=DGA/G; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161 |
| Gene Encoded By | |
| Mass | 166,935 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:15177 |
| Cross Reference Brenda |