Detail Information for IndEnz0010000016
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