Detail Information for IndEnz0005000277
IED ID IndEnz0005000277
Enzyme Type ID lipase000277
Protein Name Thermolabile hemolysin
TL
Atypical phospholipase
Lecithin-dependent hemolysin
LDH
Lysophospholipase
Phospholipase A2
Gene Name VPA0226
Organism Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633)
Taxonomic Lineage cellular organisms Bacteria Proteobacteria Gammaproteobacteria Vibrionales Vibrionaceae Vibrio Vibrio harveyi group Vibrio parahaemolyticus Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633)
Enzyme Sequence MMKKTITLLTALLPLASAVAEEPTLSPEMVSASEVISTQENQTYTYVRCWYRTSYSKDDPATDWEWAKNEDGSYFTIDGYWWSSVSFKNMFYTNTSQNVIRQRCEATLDLANENADITFFAADNRFSYNHTIWSNDAAMQPDQINKVVALGDSLSDTGNIFNASQWRFPNPNSWFLGHFSNGFVWTEYIAKAKNLPLYNWAVGGAAGENQYIALTGVGEQVSSYLTYAKLAKNYKPANTLFTLEFGLNDFMNYNRGVPEVKADYAEALIRLTDAGAKNFMLMTLPDATKAPQFKYSTQEEIDKIRAKVLEMNEFIKAQAMYYKAQGYNITLFDTHALFETLTSAPEEHGFVNASDPCLDINRSSSVDYMYTHALRSECAASGAEKFVFWDVTHPTTATHRYVAEKMLESSNNLAEYRF
Enzyme Length 418
Uniprot Accession Number Q99289
Absorption
Active Site ACT_SITE 153; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 390; /evidence=ECO:0000250; ACT_SITE 393; /evidence=ECO:0000250
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: Phospholipase hydrolyzing both fatty acid esters of phospholipid, i.e. it hydrolyzes phosphatidylcholine (PC) to lysophosphatidylcholine (LPC) and then LPC to glycerophosphorylcholine (GPC).
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Chain (1); Natural variant (1); Sequence conflict (3); Signal peptide (1)
Keywords Cytolysis;Direct protein sequencing;Hemolysis;Hydrolase;Lipid degradation;Lipid metabolism;Reference proteome;Secreted;Signal;Toxin;Virulence
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted.
Modified Residue
Post Translational Modification PTM: There are two forms of LDH. The LDH(S) may be a protein in which 13 residues of the N-terminal of LDH(L) are deleted.
Signal Peptide SIGNAL 1..19; /evidence=ECO:0000269|PubMed:1791426
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 47,392
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda