| IED ID | IndEnz0010000991 |
| Enzyme Type ID | esterase000991 |
| Protein Name |
Lysophospholipase NTE1 EC 3.1.1.5 Intracellular phospholipase B Neuropathy target esterase homolog |
| Gene Name | NTE1 ECU05_0070 |
| Organism | Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Fungi incertae sedis Microsporidia Apansporoblastina Unikaryonidae Encephalitozoon Encephalitozoon cuniculi (Microsporidian parasite) Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite) |
| Enzyme Sequence | MVSLSLLIAIIVVTGLLAGFRHYGSSRCRTVPFKIKSRSIEKTASTRLLGMSLEDAMKRYPLFNFYPGQSIREILSSWERVTYGNGETIAAPGFILQGLVEIWYREHLVCVKEKGSFLNGSMELLGYSTRGTKKARGSVEVLLIDASLVRDNIWYILFSMLRKSCIEIACRYFELESKLVEKETMKIKDDGQGHLDLFLSFLNEKLLLNLDDGKEILRRDIEARLIGRGETIKDSEESMDYIMYVVSGEILVLAGESAFVFGKGSVFGYFSLFFDLYSSIKIQAREDSSVLLCSSSVLLKFGLDEKKFDHSMLLDIDESLHIIDESAEWMRLLPGDMIAQKGDASKEIFYIGAGSVKSASRESSSGTVIGGKECIFGESWNESSIATRITDVVRIPSLLVDYFLERDKSFFKKYTKRLFESGNKANGKIVSIIPVGQYKDIESFSRKLKSAIGASSLLLSRRDVVEILARRAFDTTEEVRFMDYLTKMSRRYEIILIYVENEYSRLLRYLLNFSDVLLAVGTTFADIPEYNVYCRIEFVKIYEERRASDERSVKKSKKINHGPRYLESRKESFGQYDRVHHVLFPSKTMLFCSKDFQRLARSLLGKRIGLVLGGGGARGLAHIGVIQALEEEGIPIDCVGGTSMGAFIGALYAKECNNYHVFKQAKRFSRKMSNIWILLLDLTYPICSMFSGHAFNRSLHSIFGDGLIQDLWLEYFCITTNIVSYEEEVHRNGMVWRYVRASMGLCGYLPPICDNKKLLVDGGYLNNVPADVMMGMQVEKIITVDVGTVLENDHFDYGDTLSGFTILFNKFFGNKKFVTMEEIQYRLAYISTERKMKELEANGNIIMLRPDLGKYRTMDFKKFDEIVACGYQSTKNAIAKWKQEGTYDVLFFSLKKQTPKRRYSV |
| Enzyme Length | 905 |
| Uniprot Accession Number | Q8SVN8 |
| Absorption | |
| Active Site | ACT_SITE 643; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161; ACT_SITE 761; /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 198..319; /note=cNMP 1; NP_BIND 310..428; /note=cNMP 2 |
| Features | Active site (2); Chain (1); Domain (1); Motif (3); Nucleotide binding (2); Topological domain (1); Transmembrane (1) |
| 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:0000305}; Single-pass type I membrane protein {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 614..619; /note=GXGXXG; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161; MOTIF 641..645; /note=GXSXG; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161; MOTIF 761..763; /note=DGA/G; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161 |
| Gene Encoded By | |
| Mass | 103,088 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:15177 |
| Cross Reference Brenda |