Detail Information for IndEnz0010001338
IED ID IndEnz0010001338
Enzyme Type ID esterase001338
Protein Name Proofreading thioesterase EntH
EC 3.1.2.-
Enterobactin synthase component H
p15
Gene Name entH ybdB b0597 JW0589
Organism Escherichia coli (strain K12)
Taxonomic Lineage cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12)
Enzyme Sequence MIWKRHLTLDELNATSDNTMVAHLGIVYTRLGDDVLEAEMPVDTRTHQPFGLLHGGASAALAETLGSMAGFMMTRDGQCVVGTELNATHHRPVSEGKVRGVCQPLHLGRQNQSWEIVVFDEQGRRCCTCRLGTAVLG
Enzyme Length 137
Uniprot Accession Number P0A8Y8
Absorption
Active Site ACT_SITE 63; /note="Nucleophile or proton acceptor"; /evidence="ECO:0000255|HAMAP-Rule:MF_00907, ECO:0000303|PubMed:25010423, ECO:0000305|PubMed:19193103"
Activity Regulation
Binding Site BINDING 48; /note=Substrate; /evidence=ECO:0000269|PubMed:25010423; BINDING 82; /note=Substrate; via carbonyl oxygen; /evidence=ECO:0000269|PubMed:25010423
Calcium Binding
catalytic Activity
DNA Binding
EC Number 3.1.2.-
Enzyme Function FUNCTION: Required for optimal enterobactin synthesis. Acts as a proofreading enzyme that prevents EntB misacylation by hydrolyzing the thioester bound existing between EntB and wrongly charged molecules. Displays esterase activity toward a wide range of substrates, including acyl-CoAs and aryl-CoAs. {ECO:0000269|PubMed:15808744, ECO:0000269|PubMed:17675380, ECO:0000269|PubMed:19119850, ECO:0000269|PubMed:19193103, ECO:0000269|PubMed:24992697}.
Temperature Dependency
PH Dependency
Pathway PATHWAY: Siderophore biosynthesis; enterobactin biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00907, ECO:0000269|PubMed:17675380}.
nucleotide Binding
Features Active site (1); Beta strand (7); Binding site (2); Chain (1); Helix (3); Mutagenesis (9); Region (2); Turn (2)
Keywords 3D-structure;Cytoplasm;Hydrolase;Reference proteome
Interact With P0ADI4
Induction INDUCTION: Induced by iron starvation. {ECO:0000269|PubMed:17675380}.
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00907, ECO:0000269|PubMed:17675380}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D X-ray crystallography (3)
Cross Reference PDB 1VH9; 4K4C; 4K4D;
Mapped Pubmed ID 16021622; 16606699;
Motif
Gene Encoded By
Mass 14,970
Kinetics BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=16 uM for 2,3-DHB-EntB {ECO:0000269|PubMed:19119850}; KM=116 uM for 2,3-DHB-EntB {ECO:0000269|PubMed:19193103}; KM=21 uM for 4-hydroxybenzoyl-CoA {ECO:0000269|PubMed:19119850}; KM=190 uM for 4-hydroxybenzoyl-CoA {ECO:0000269|PubMed:19193103}; KM=25 uM for 2,4-DHB-EntB {ECO:0000269|PubMed:19119850}; KM=32 uM for lauroyl-EntB {ECO:0000269|PubMed:19119850}; KM=35 uM for 3-hydroxybenzoyl-CoA {ECO:0000269|PubMed:19119850}; KM=265 uM for 3-hydroxybenzoyl-CoA {ECO:0000269|PubMed:19193103}; KM=37 uM for 3-HPA-CoA {ECO:0000269|PubMed:19119850}; KM=45 uM for lauroyl-CoA {ECO:0000269|PubMed:19119850}; KM=49 uM for decanoyl-CoA {ECO:0000269|PubMed:19119850}; KM=55 uM for palmitoyl-CoA {ECO:0000269|PubMed:19119850}; KM=4.25 uM for palmitoyl-CoA {ECO:0000269|PubMed:19193103}; KM=161 uM for 2,3-dihydroxybenzoyl-CoA {ECO:0000269|PubMed:19193103}; KM=176 uM for salicylyl-CoA {ECO:0000269|PubMed:19193103}; KM=212 uM for 3,4-dihydroxybenzoyl-CoA {ECO:0000269|PubMed:19193103}; KM=219 uM for 2,4-dihydroxybenzoyl-CoA {ECO:0000269|PubMed:19193103}; KM=256 uM for 3,5-dihydroxybenzoyl-CoA {ECO:0000269|PubMed:19193103}; KM=272 uM for salicylyl-EntB {ECO:0000269|PubMed:19193103}; KM=350 uM for hexanoyl-CoA {ECO:0000269|PubMed:19119850}; KM=400 uM for propionyl-CoA {ECO:0000269|PubMed:19119850}; KM=475 uM for benzoyl-CoA {ECO:0000269|PubMed:19193103}; KM=800 uM for acetyl-CoA {ECO:0000269|PubMed:19119850};
Metal Binding
Rhea ID
Cross Reference Brenda 3.1.2.2;3.1.2.28;