| 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; |