IED ID | IndEnz0010001019 |
Enzyme Type ID | esterase001019 |
Protein Name |
Lysophospholipase NTE1 EC 3.1.1.5 Intracellular phospholipase B Neuropathy target esterase homolog |
Gene Name | NTE1 CNBD2140 |
Organism | Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) (Filobasidiella neoformans) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Basidiomycota Agaricomycotina Tremellomycetes Tremellales (jelly fungi) Cryptococcaceae Cryptococcus Cryptococcus neoformans species complex Cryptococcus neoformans (Filobasidiella neoformans) Cryptococcus neoformans var. neoformans Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) (Filobasidiella neoformans) |
Enzyme Sequence | MSSIPTPPDANGNPLIALAVAVIYAILYVLQGVKYGVSLLTIGIPSCIVRMLQYSLTISLGFPHLLALFAGALLALFFLIRYRYLTRYAQLKESALPPPSPPALASRLLPLDGDGLGLPDSRSQTSSFHNYLDDFLSAIRIFGYLEKPVFHELSRHLQTRRLAAGDTLEIGGGEFWCVVEGKVQVFAPDASSQGTPTPSSDTNSPTRPSFNGYHLLNEVSTGGTLSSLFSILSLFTEDIKLSWKSSADDEGEEEQIFEGAPEQSSAKLRVRRANSDVSQLGPDSIGVRAMDPTPLPESIDSHGDSSVPQRRRERSSSIDAAGETVREREGIFASASLPISSTEPPSPRRSQSLRSSPRLNSATNLLSSQSEHLRSSVPRKAGIEIGSKALKGTIARATEDTTLAVIPAAAFRKLTRKFPKASGTIVQVVLERFSRVTFMTAHKYLGLTREILQTESSLNLLVTHPLPRSFYTGGGMQALRARFQPEALAKESVHYDSLKSSPNARVSSKDYFNYVPASPTVKAPSLPAMTPKPLSPIIHKSSLGQTATTTVKNEPLNGGSSPLDETRDKVPSFGLSTAAATNPDASFRHASPFIRRTSAMRQQVAAGDLAMSVHNLPDESGQAYYRPTAITPGLSKMDTWQRRYSSSWNLNDSPHTDGQPVDPQRDDESLLNESFDLKEAVLNSIAKSIGLYQEAESNSDMIARSSMAPSVSALSTPNSPMFPPNAGTPLQGSTRSRPPHFGNVLDLINASSQNEGVIGGMLREAAFNSRPDDEASSISMSLHDSQGGASGVDRKIMKDLERHVEILFFKKGSVLVKEGERSPGMYYVIDGFLETSLPFRSTSSNQENPNSTPGSKHRQSSFGSSNERPFKTALGLDTSKGKELDDGSKKDEALFTVKPGGIAGYLSSLCCTDSYVDITAKTDCFVGFLPHHTLERIIERRPIVLLTLAKRLLSLLSPLVLHIDAALDWQQLNAGQVLYEKGDKSTDFYIVINGRLRAFTEKNDNMHVLREYGQNDSIGELDVITAVDRSETVHAIRDSELVRIPAALFDAISIKHPETTVQFMRLIAGRVRRALGDEMNGRVPGLPTTDMNLKTVCVLGSTRNVPVTQFAGKLKNALEEIGASTSYLDQGIVMRHLGRHAFARIGKLKVAGWLADQEQHYRTVLYVADSPPASQWTLTCIRQADLVLVVSMGDDPSLGEYEKLLLATKTTARKELILLHDERTVAPGSTRQWLSNRPWIQTHYHVELPGVVTPARPIPPVHDAAAIAAFKHLREQVETRIKKYRGLRPFTRPRRPPHMNDFARIARRLCGQQIGLVLGGGGARGISHIGMLQALEEFGIPIDAIGGCSIGSFVGGLYARETDLLETAGRTKQFSGRMGSMWRILSDVTYPFVSYTTGHEFNRGIYKAFYNTHIEDFWIPFFANSTNITHSRMEVHRTGYAWRYVRASMTLAGLLPPLSDNGNLLVDGGYMDNTPIQPLRENGIRDIIVVDVGSVDDTSPRDYGDSVSGWWIFFNRFNPFYERRVLSMTEISSRLTYVSSVKTLEGVKATPGCHYIAMPVQQFDTLGGFKRFSEVMEIGLKAGRETLKKWKEEGKLPTGLVDEAKGSKAVQRGNRLRRMSI |
Enzyme Length | 1621 |
Uniprot Accession Number | P0CP37 |
Absorption | |
Active Site | ACT_SITE 1349; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161; ACT_SITE 1467; /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 788..907; /note=cNMP 1; NP_BIND 951..1070; /note=cNMP 2 |
Features | Active site (2); Chain (1); Compositional bias (4); Domain (1); Motif (3); Nucleotide binding (2); Region (7); Topological domain (3); Transmembrane (2) |
Keywords | Endoplasmic reticulum;Hydrolase;Lipid degradation;Lipid metabolism;Membrane;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 1320..1325; /note=GXGXXG; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161; MOTIF 1347..1351; /note=GXSXG; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161; MOTIF 1467..1469; /note=DGA/G; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161 |
Gene Encoded By | |
Mass | 178,011 |
Kinetics | |
Metal Binding | |
Rhea ID | RHEA:15177 |
Cross Reference Brenda |