IED ID | IndEnz0010001391 |
Enzyme Type ID | esterase001391 |
Protein Name |
Apo-salmochelin esterase EC 3.1.1.107 Enterobactin hydrolase IroE |
Gene Name | iroE c1251 |
Organism | Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) |
Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) |
Enzyme Sequence | MYAREYRSTRPHKAIFFHLSCLTLICSAQVYAKPDMRPLGPNIADKGSVFYHFSATSFDSVDGTRHYRVWTAVPNTTAPASGYPILYMLDGNAVMDRLDDELLKQLSEKTPPVIVAVGYQTNLPFDLNSRAYDYTPAAESRKTDLHSGRFSRKSGGSNNFRQLLETRIAPKVEQGLNIDRQRRGLWGHSYGGLFVLDSWLSSSYFRSYYSASPSLGRGYDALLSRVTAVEPLQFCTKHLAIMEGSATQGDNRETHAVGVLSKIHTTLTILKDKGVNAVFWDFPNLGHGPMFNASFRQALLDISGENANYTAGCHELSH |
Enzyme Length | 318 |
Uniprot Accession Number | A0A0H2V871 |
Absorption | |
Active Site | ACT_SITE 189; /evidence=ECO:0000305|PubMed:16922493; ACT_SITE 287; /evidence=ECO:0000305|PubMed:16922493 |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=enterobactin + H2O = N-(2,3-dihydroxybenzoyl)-L-serine trimer; Xref=Rhea:RHEA:60384, ChEBI:CHEBI:15377, ChEBI:CHEBI:77805, ChEBI:CHEBI:143020; EC=3.1.1.107; Evidence={ECO:0000269|PubMed:16076215};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60385; Evidence={ECO:0000269|PubMed:16076215}; CATALYTIC ACTIVITY: Reaction=H2O + monoglucosyl-enterobactin = [N-(2,3-dihydroxybenzoyl)-L-seryl]2-N-(C-5-[deoxy-beta-D-glucosyl]-2,3-dihydroxybenzoyl)-L-serine + H(+); Xref=Rhea:RHEA:60412, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:142958, ChEBI:CHEBI:143023; EC=3.1.1.107; Evidence={ECO:0000269|PubMed:16076215};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60413; Evidence={ECO:0000269|PubMed:16076215}; CATALYTIC ACTIVITY: Reaction=diglucosyl-enterobactin + H2O = H(+) + N-(2,3-dihydroxybenzoyl)-L-seryl-[N-(C-5-[deoxy-beta-D-glucosyl]-2,3-dihydroxybenzoyl)-L-serine]2; Xref=Rhea:RHEA:60416, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:142959, ChEBI:CHEBI:143022; EC=3.1.1.107; Evidence={ECO:0000269|PubMed:16076215};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60417; Evidence={ECO:0000269|PubMed:16076215}; CATALYTIC ACTIVITY: Reaction=H2O + triglucosyl-enterobactin = [N-(C-5-[deoxy-beta-D-glucosyl]-2,3-dihydroxybenzoyl)-L-serine]3 + H(+); Xref=Rhea:RHEA:60420, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:142960, ChEBI:CHEBI:143021; EC=3.1.1.107; Evidence={ECO:0000269|PubMed:16076215};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60421; Evidence={ECO:0000269|PubMed:16076215}; |
DNA Binding | |
EC Number | 3.1.1.107 |
Enzyme Function | FUNCTION: Catalyzes the hydrolysis of both the apo and Fe3(+)-bound forms of enterobactin (Ent), monoglucosyl-C-Ent (MGE), diglucosyl-C-Ent (DGE) and triglucosyl-C-Ent (TGE). It prefers apo siderophores as substrates and hydrolyzes the Fe3(+)-bound siderophores very inefficiently. Tends to hydrolyze the trilactone just once to produce linearized trimers. May hydrolyze and linearize some or all of apo enterobactins while they are being exported. {ECO:0000269|PubMed:16076215}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Chain (1); Mutagenesis (10); Transmembrane (1) |
Keywords | 3D-structure;Cell inner membrane;Cell membrane;Hydrolase;Membrane;Serine esterase;Transmembrane;Transmembrane helix |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305|PubMed:16076215}; Single-pass membrane protein {ECO:0000255}; Periplasmic side {ECO:0000305|PubMed:16076215}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | X-ray crystallography (2) |
Cross Reference PDB | 2GZR; 2GZS; |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 35,444 |
Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=16 uM for Ent {ECO:0000269|PubMed:16076215}; KM=3.4 uM for Fe-Ent {ECO:0000269|PubMed:16076215}; KM=29 uM for MGE {ECO:0000269|PubMed:16076215}; KM=4.8 uM for Fe-MGE {ECO:0000269|PubMed:16076215}; KM=39 uM for DGE {ECO:0000269|PubMed:16076215}; KM=4.6 uM for Fe-DGE {ECO:0000269|PubMed:16076215}; KM=155 uM for TGE {ECO:0000269|PubMed:16076215}; Note=kcat is 375 min(-1) with Ent as substrate. kcat is 3.0 min(-1) with Fe-Ent as substrate. kcat is 430 min(-1) with MGE as substrate. kcat is 3.2 min(-1) with Fe-MGE as substrate. kcat is 320 min(-1) with DGE as substrate. kcat is 2.5 min(-1) with Fe-DGE as substrate. kcat is 450 min(-1) with TGE as substrate. {ECO:0000269|PubMed:16076215}; |
Metal Binding | |
Rhea ID | RHEA:60384; RHEA:60385; RHEA:60412; RHEA:60413; RHEA:60416; RHEA:60417; RHEA:60420; RHEA:60421 |
Cross Reference Brenda | 3.1.1.107; |