IED ID | IndEnz0010000016 |
Enzyme Type ID | esterase000016 |
Protein Name |
Iron III enterobactin esterase EC 3.1.1.108 Enterochelin esterase Ferric enterobactin esterase |
Gene Name | fes b0585 JW0576 |
Organism | Escherichia coli (strain K12) |
Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12) |
Enzyme Sequence | MTALKVGSESWWQSKHGPEWQRLNDEMFEVTFWWRDPQGSEEYSTIKRVWVYITGVTDHHQNSQPQSMQRIAGTNVWQWTTQLNANWRGSYCFIPTERDDIFSVPSPDRLELREGWRKLLPQAIADPLNLQSWKGGRGHAVSALEMPQAPLQPGWDCPQAPEIPAKEIIWKSERLKKSRRVWIFTTGDATAEERPLAVLLDGEFWAQSMPVWPVLTSLTHRQQLPPAVYVLIDAIDTTHRAHELPCNADFWLAVQQELLPLVKAIAPFSDRADRTVVAGQSFGGLSALYAGLHWPERFGCVLSQSGSYWWPHRGGQQEGVLLEKLKAGEVSAEGLRIVLEAGIREPMIMRANQALYAQLHPIKESIFWRQVDGGHDALCWRGGLMQGLIDLWQPLFHDRS |
Enzyme Length | 400 |
Uniprot Accession Number | P13039 |
Absorption | |
Active Site | |
Activity Regulation | ACTIVITY REGULATION: Inhibited by N-ethylmaleimide. {ECO:0000269|PubMed:150859}. |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=Fe(III)-enterobactin + H(+) + 3 H2O = Fe(III)-[N-(2,3-dihydroxybenzoyl)-L-serine] + 2 N-(2,3-dihydroxybenzoyl)-L-serine; Xref=Rhea:RHEA:30111, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28199, ChEBI:CHEBI:58154, ChEBI:CHEBI:143010; EC=3.1.1.108; Evidence={ECO:0000269|PubMed:150859, ECO:0000269|PubMed:1534808, ECO:0000269|PubMed:8148617};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30112; Evidence={ECO:0000269|PubMed:150859, ECO:0000269|PubMed:1534808, ECO:0000269|PubMed:8148617}; CATALYTIC ACTIVITY: Reaction=Fe(III)-enterobactin + H2O = Fe(III)-[N-(2,3-dihydroxybenzoyl)-L-serine]3 + H(+); Xref=Rhea:RHEA:59256, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28199, ChEBI:CHEBI:143011; Evidence={ECO:0000269|PubMed:8148617};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59257; Evidence={ECO:0000269|PubMed:8148617}; CATALYTIC ACTIVITY: Reaction=Fe(III)-[N-(2,3-dihydroxybenzoyl)-L-serine]3 + H(+) + H2O = Fe(III)-[N-(2,3-dihydroxybenzoyl)-L-serine]2 + N-(2,3-dihydroxybenzoyl)-L-serine; Xref=Rhea:RHEA:59260, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58154, ChEBI:CHEBI:143011, ChEBI:CHEBI:143012; Evidence={ECO:0000269|PubMed:8148617};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59261; Evidence={ECO:0000269|PubMed:8148617}; CATALYTIC ACTIVITY: Reaction=Fe(III)-[N-(2,3-dihydroxybenzoyl)-L-serine]2 + H(+) + H2O = Fe(III)-[N-(2,3-dihydroxybenzoyl)-L-serine] + N-(2,3-dihydroxybenzoyl)-L-serine; Xref=Rhea:RHEA:59264, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58154, ChEBI:CHEBI:143010, ChEBI:CHEBI:143012; Evidence={ECO:0000269|PubMed:8148617};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59265; Evidence={ECO:0000269|PubMed:8148617}; |
DNA Binding | |
EC Number | 3.1.1.108 |
Enzyme Function | FUNCTION: Catalyzes the hydrolysis of ferric enterobactin (Fe-Ent) (PubMed:150859, PubMed:1534808, PubMed:8148617). Is responsible for the release of iron from ferric enterobactin (PubMed:1534808). Also catalyzes the hydrolysis of iron-free enterobactin (Ent) (PubMed:150859, PubMed:1534808, PubMed:8148617). Cleavage of ferric enterobactin results in a mixture of three hydrolysis products, 2,3-dihydroxybenzoylserine (DHBS), the linear dimer (DHBS)2 and the linear trimer (DHBS)3, while cleavage of iron-free enterobactin yields only the monomer (PubMed:8148617). Hydrolysis of ferric enterobactin is less efficient than hydrolysis of unliganded enterobactin (PubMed:150859, PubMed:1534808). It also cleaves the aluminum (III) complex at a rate similar to the ferric complex (PubMed:1534808). {ECO:0000269|PubMed:150859, ECO:0000269|PubMed:1534808, ECO:0000269|PubMed:8148617}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Chain (1); Erroneous initiation (2) |
Keywords | Cytoplasm;Direct protein sequencing;Hydrolase;Reference proteome |
Interact With | |
Induction | INDUCTION: Expression is increased under iron stress (PubMed:3040679). Repressed by Fur under iron-rich conditions (PubMed:9573216). {ECO:0000269|PubMed:3040679, ECO:0000269|PubMed:9573216}. |
Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:1534808}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | 131121; 132428; 16606699; 2958600; 4568262; 6260579; |
Motif | |
Gene Encoded By | |
Mass | 45,652 |
Kinetics | |
Metal Binding | |
Rhea ID | RHEA:30111; RHEA:30112; RHEA:59256; RHEA:59257; RHEA:59260; RHEA:59261; RHEA:59264; RHEA:59265 |
Cross Reference Brenda |