| IED ID | IndEnz0010001021 |
| Enzyme Type ID | esterase001021 |
| Protein Name |
Lysophospholipase nte1 EC 3.1.1.5 Intracellular phospholipase B Neuropathy target esterase homolog |
| Gene Name | nte1 NFIA_030460 |
| Organism | Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Fumigati Aspergillus fischeri Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus) |
| Enzyme Sequence | MADGVTLVDSTGLHSFSSSPSLSTSSSSLTAVALSLATSASAVTASYSISHLPPPPLPPVPTTMAGWIGWVFSFFFQVIPSVLYWVITFSTITLPTWLFTLFSMSLTFTMNFTTLLLIVLAMVSTISWFIRYRFLNMYSRLPPEPQRKEPQVDLFPDVQEGDSKPGLANYLDEFLSAIKVFGYLERPVFHELTRTMQTRKLIAGETLMLEEEKGFCLVVDGLVQIFVKSMRDGKSDTDEELHHLGAESSDEEHHIDGKQGYQLLTEVKNGASMSSLFSILSLFTEDIQLRENESSGSSSSSIALRAARVPNSIPTSPRGVMDSPSLGFQDHSDDTSNMITNGDLPSVPPLHLGESHTPPSGDQHHQQHHESRKHSSRKRRKSVHPDIVARAMVDTTIAIIPASAFRRLTRVYPRATAHIVQVILTRLQRVTFATAHSYLGLSNEVLGIEKQMTKFTTYDLPNNMRGAALDRLKDKFIKERDRLGSEEVTKGIALHNPSAGRRRRSSSFLRKDAALQVKMMTPRRAATVVTPESAPAEHDTYGVSPGDLLSTIQSSRFGPRYEQPPAKLQSPLAEKENTHFRLPAMQARHTFRRQDTMDEDALFRECILDCIMKGIGLTSSTRDALRKSSHSGDASPKLLSYDSRRQKAIFTNNAFGFIDPYEGSGDGETESLMSMSVTSAGGTSPVINLREELRNDIEIVYFPKGSVLVEQGERHPGLYYVIDGFLDVGVPIVEKGEDLVGVSKPAASKESFPTLKRTTTANSIGAGGTAANDSRRRKQSRKSLYLIKPGGIQGYVGAVASYRSYTDVVAKTDVYVGFLPRASLERIAERYPIALLTLAKRLTSILPRLLLHIDFALEWLQVNAGQVIYHQGDESDAIYLVLNGRLRSVLESPGNKLAVIGEYGQGESVGELEVMTESTRPATLHAIRDTELAKFPRSLFNSLAQEHPGITIQVSKLIAQRMRDLVERPVTEKGVERSNAGGVQTATSTVNLRTVGILPVTAGVPVVEFGNRLLHALHQVGVTNGVTSLNQAAILNHLGRHAFSKMGKLKLSQYLADLEEKYGMVLYIADTNVSSPWTQTCITQADCILLVGLAESSPSIGEYERFLLGMKTTARKELVLLHSERYCPPGLTRRWLKNRVWINGGHHHIQMAFRLTAEPSHPETKRFGTVLKQRVQVLQAEIQKYTSRRIRQTPLYSAQSPFKGDFHRLARRLCGRAVGLVLGGGGARGIAHVGVIKALEEAGIPVDIIGGTSIGSFIGALYARDADVVPMYGRAKKFAGRMGSMWRFALDLTYPTVSYTTGHEFNRGIFKTFGDSQIEDFWLEFYCNTTNISKSRPEYHSSGYVWRYVRASMSLAGLIPPICDEGSMLLDGGYIDNLTVDHMKGLGADVIFAVDVGSIDDNTPQVYGDSLSGFWSVFNRWNPFSSCPNPPTLSEIQARLAYVSSIDNLERAKNIPGCLYMRPPIDGYGTLEFGKFDEIYQVGYAFGKQFLEKLKTEGSLPLPEETEEKKKLQRTMAPRRASI |
| Enzyme Length | 1523 |
| Uniprot Accession Number | A1D9Y2 |
| Absorption | |
| Active Site | ACT_SITE 1253; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161; ACT_SITE 1371; /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..800; /note=cNMP 1; NP_BIND 841..961; /note=cNMP 2 |
| Features | Active site (2); Chain (1); Compositional bias (2); Domain (1); Erroneous initiation (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 1224..1229; /note=GXGXXG; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161; MOTIF 1251..1255; /note=GXSXG; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161; MOTIF 1371..1373; /note=DGA/G; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161 |
| Gene Encoded By | |
| Mass | 168,447 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:15177 |
| Cross Reference Brenda |