Detail Information for IndEnz0010000990
IED ID IndEnz0010000990
Enzyme Type ID esterase000990
Protein Name Lysophospholipase NTE1
EC 3.1.1.5
Intracellular phospholipase B
Neuropathy target esterase homolog
Gene Name NTE1 CND04180
Organism Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC MYA-565) (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 JEC21 / ATCC MYA-565) (Filobasidiella neoformans)
Enzyme Sequence MSSIPTPPDANGNPLIALAVAVIYAILYVLQGVKYGVSLLTIGIPSCIVRMLQYSLTISLGFPHLLALFAGALLALFFLIRYRYLTRYAQLKESALPPPSPPALASRLLPLDGDGLGLPDSRSQTSSFHNYLDDFLSAIRIFGYLEKPVFHELSRHLQTRRLAAGDTLEIGGGEFWCVVEGKVQVFAPDASSQGTPTPSSDTNSPTRPSFNGYHLLNEVSTGGTLSSLFSILSLFTEDIKLSWKSSADDEGEEEQIFEGAPEQSSAKLRVRRANSDVSQLGPDSIGVRAMDPTPLPESIDSHGDSSVPQRRRERSSSIDAAGETVREREGIFASASLPISSTEPPSPRRSQSLRSSPRLNSATNLLSSQSEHLRSSVPRKAGIEIGSKALKGTIARATEDTTLAVIPAAAFRKLTRKFPKASGTIVQVVLERFSRVTFMTAHKYLGLTREILQTESSLNLLVTHPLPRSFYTGGGMQALRARFQPEALAKESVHYDSLKSSPNARVSSKDYFNYVPASPTVKAPSLPAMTPKPLSPIIHKSSLGQTATTTVKNEPLNGGSSPLDETRDKVPSFGLSTAAATNPDASFRHASPFIRRTSAMRQQVAAGDLAMSVHNLPDESGQAYYRPTAITPGLSKMDTWQRRYSSSWNLNDSPHTDGQPVDPQRDDESLLNESFDLKEAVLNSIAKSIGLYQEAESNSDMIARSSMAPSVSALSTPNSPMFPPNAGTPLQGSTRSRPPHFGNVLDLINASSQNEGVIGGMLREAAFNSRPDDEASSISMSLHDSQGGASGVDRKIMKDLERHVEILFFKKGSVLVKEGERSPGMYYVIDGFLETSLPFRSTSSNQENPNSTPGSKHRQSSFGSSNERPFKTALGLDTSKGKELDDGSKKDEALFTVKPGGIAGYLSSLCCTDSYVDITAKTDCFVGFLPHHTLERIIERRPIVLLTLAKRLLSLLSPLVLHIDAALDWQQLNAGQVLYEKGDKSTDFYIVINGRLRAFTEKNDNMHVLREYGQNDSIGELDVITAVDRSETVHAIRDSELVRIPAALFDAISIKHPETTVQFMRLIAGRVRRALGDEMNGRVPGLPTTDMNLKTVCVLGSTRNVPVTQFAGKLKNALEEIGASTSYLDQGIVMRHLGRHAFARIGKLKVAGWLADQEQHYRTVLYVADSPPASQWTLTCIRQADLVLVVSMGDDPSLGEYEKLLLATKTTARKELILLHDERTVAPGSTRQWLSNRPWIQTHYHVELPGVVTPARPIPPVHDAAAIAAFKHLREQVETRIKKYRGLRPFTRPRRPPHMNDFARIARRLCGQQIGLVLGGGGARGISHIGMLQALEEFGIPIDAIGGCSIGSFVGGLYARETDLLETAGRTKQFSGRMGSMWRILSDVTYPFVSYTTGHEFNRGIYKAFYNTHIEDFWIPFFANSTNITHSRMEVHRTGYAWRYVRASMTLAGLLPPLSDNGNLLVDGGYMDNTPIQPLRENGIRDIIVVDVGSVDDTSPRDYGDSVSGWWIFFNRFNPFYERRVLSMTEISSRLTYVSSVKTLEGVKATPGCHYIAMPVQQFDTLGGFKRFSEVMEIGLKAGRETLKKWKEEGKLPTGLVDEAKGSKAVQRGNRLRRMSI
Enzyme Length 1621
Uniprot Accession Number P0CP36
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); Erroneous gene model prediction (1); Motif (3); Nucleotide binding (2); Region (7); 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 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