| IED ID | IndEnz0010000847 |
| Enzyme Type ID | esterase000847 |
| Protein Name |
Lysophospholipase nte1 EC 3.1.1.5 Intracellular phospholipase B Neuropathy target esterase homolog |
| Gene Name | nte1 AFUA_4G03000 |
| Organism | Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Fumigati Neosartorya fumigata (Aspergillus fumigatus) Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) |
| Enzyme Sequence | MADGVTQVDSTGLHSFSPSPSLSSSSSLPAVALSLAVSASAVTASYSISHLPPPPLPPVPTTMAGWIGWVFSFFFQVIPSVLYWIITFSTITLPTWLFTLFSMSLTFTMNFTTLLLIVLAVVSTISWFIRYRFLNMYSRLPPEPQRKEPQVDLFPDVQEGDSKPGLANYLDEFLSAIKVFGYLERPVFHELTRTMQTRKLIAGETLMLEEEKGFCLVVDGLVQIFVKSMRDGKSDTDEELHHLGAESSDEEHHIDGKQGYQLLTEVKNGASMSSLFSILSLFTEDIQLRENESSGSSSSSIALRAARVPNSIPTSPRGVMDSPSLGFQDHSDDTSNMITNGELPSVPPLHLGESRTPPSGDQHHQQHHESRKHSSRKRRKSVHPDIVARAMVDTTIAIIPASAFRRLTRVYPRATAHIVQVILTRLQRVTFATAHSYLGLSNEVLGIEKQMTKFTTYDLPNNMRGAALDRLKDKFIKERDRLGSEEVTKGIALHNPSAGRRRRSSSFLRKDAALQAKLMTPRRAATVVTPESAPAEHDTYGVSPGDLLSTIQSSRFGPRYEQPPAKLQTPLAEKENTHFRLPAMQARHTFRRQDTMDEDGLFRECILDCIMKGIGLTSSTRDALRKSNHSGEASPKLLSYDSRRQKAIFTNNAFGFIDPYEGSGDGETESLMSMSVTSAGGTSPVINLREELRNDIEIVYFPKGSVLVEQGERHPGLYYVIDGFLDVGVPIVDKGEDLVGVSKPAASKGSFPTLKRTTTANSVGAGGTAANDSRRRKQSRKSLYLIKPGGIQGYVGAVASYRSYTDVVAKTDVYVGFLPRASLERIAERYPIALLTLAKRLTSILPRLLLHIDFALEWVQVNAGQVIYRQGDESDAIYLVLNGRLRSVLESPGNKLAVVGEYGQGESVGELEVMTESTRPATLHAIRDTELAKFPRSLFNSLAQEHPGITIQVSKLIAQRMRDLVERPVTEKGVERSNAGSVQTATSTVNLRTVGILPVTAGVPVVEFGNRLLHALHQVGVTNGVTSLNQAAILNHLGRHAFSKMGKLKLSQYLADLEEKYGMVLYIADTNVSSPWTQTCITQADCILLVGLAESSPSIGEYERFLLGMKTTARKELVLLHAERYCPPGLTRRWLKNRVWINGGHHHIQMAFRLTAEPTHPETKRFGTVLKQRVQVLQAEIQKYTSRRIRQTPLYSAQSPFKGDFHRLARRLCGRAVGLVLGGGGARGIAHVGVIKALEEAGIPVDIIGGTSIGSFIGALYARDADVVPMYGRAKKFAGRMGSMWRFALDLTYPTVSYTTGHEFNRGIFKTFGDSQIEDFWLEFYCNTTNISKSRPEYHSSGYVWRYVRASMSLAGLIPPICDEGSMLLDGGYIDNLTVDHMKGLGADVIFAVDVGSIDDNTPQVYGDSLSGFWSVFNRWNPFSSCPNPPTLSEIQARLAYVSSIDNLERAKNIPGCLYMRPPIDGYGTLEFGKFDEIYQVGYAFGKQFLEKLKSEGSLPLPEETEEKKKLQRTLAPRRASI |
| Enzyme Length | 1522 |
| Uniprot Accession Number | Q4WA15 |
| Absorption | |
| Active Site | ACT_SITE 1252; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161; ACT_SITE 1370; /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 680..800; /note=cNMP 1; NP_BIND 840..960; /note=cNMP 2 |
| Features | Active site (2); Chain (1); Compositional bias (3); Domain (1); Motif (3); Nucleotide binding (2); Region (5); 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 1223..1228; /note=GXGXXG; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161; MOTIF 1250..1254; /note=GXSXG; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161; MOTIF 1370..1372; /note=DGA/G; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161 |
| Gene Encoded By | |
| Mass | 168,262 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:15177 |
| Cross Reference Brenda |