| IED ID | IndEnz0010000775 |
| Enzyme Type ID | esterase000775 |
| Protein Name |
Iron III salmochelin esterase EC 3.1.1.109 |
| Gene Name | iroD c1252 |
| 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 | MLNMQQHPSAIASLRNQLAAGHIANLTDFWREAESLNVPLVTPVEGAEDEREVTFLWRARHPLQGVYLRLNRVTDKEHVEKGMMSALPETDIWTLTLRLPASYCGSYSLLEIPPGTTAETIALSGGRFATLAGKADPLNKMPEINVRGNAKESVLTLDKAPALSEWNGGFHTGQLLTSMRIIAGKSRQVRLYIPDIDISQPLGLVVLPDGETWFDHLGVCAAIDAAINNRRIVPVAVLGIDNINEHERTEILGGRSKLIKDIAGHLLPMIRAEQPQRQWADRSRTVLAGQSLGGISALMGARYAPETFGLVLSHSPSMWWTPERTSRPGLFSETDTSWVSEHLLSAPPQGVRISLCVGSLEGSTVPHVQQLHQRLITAGVESHCAIYTGGHDYAWWRGALIDGIGLLQG |
| Enzyme Length | 409 |
| Uniprot Accession Number | A0A0H2V660 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Fe(III)-C-5-deoxy-beta-D-glucosyl-enterobactin + H2O = Fe(III)-{di[N-(2,3-dihydroxybenzoyl)-L-seryl]-N-(C-5-[deoxy-beta-D-glucosyl]-2,3-dihydroxybenzoyl)-L-serine} + H(+); Xref=Rhea:RHEA:60392, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:143772, ChEBI:CHEBI:143774; EC=3.1.1.109; Evidence={ECO:0000269|PubMed:16076215}; CATALYTIC ACTIVITY: Reaction=Fe(III)-{di[N-(2,3-dihydroxybenzoyl)-L-seryl]-N-(C-5-[deoxy-beta-D-glucosyl]-2,3-dihydroxybenzoyl)-L-serine} + H(+) + H2O = Fe(III)-{N-(2,3-dihydroxybenzoyl)-L-seryl-N-(C-5-[deoxy-beta-D-glucosyl]-2,3-dihydroxybenzoyl)-L-serine} + N-(2,3-dihydroxybenzoyl)-L-serine; Xref=Rhea:RHEA:60404, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58154, ChEBI:CHEBI:143774, ChEBI:CHEBI:143775; EC=3.1.1.109; Evidence={ECO:0000269|PubMed:16076215}; CATALYTIC ACTIVITY: Reaction=Fe(III)-{N-(2,3-dihydroxybenzoyl)-L-seryl-[N-(C-5-[deoxy-beta-D-glucosyl]-2,3-dihydroxybenzoyl)-L-serine]2} + H(+) + H2O = Fe(III)-{N-(2,3-dihydroxybenzoyl)-L-seryl-N-(C-5-[deoxy-beta-D-glucosyl]-2,3-dihydroxybenzoyl)-L-serine} + N-(C-5-[deoxy-beta-D-glucosyl]-2,3-dihydroxybenzoyl)-L-serine; Xref=Rhea:RHEA:60400, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:143773, ChEBI:CHEBI:143775, ChEBI:CHEBI:143778; EC=3.1.1.109; Evidence={ECO:0000269|PubMed:16076215}; CATALYTIC ACTIVITY: Reaction=Fe(III)-di(C-5-deoxy-beta-D-glucosyl)-enterobactin + H2O = Fe(III)-{N-(2,3-dihydroxybenzoyl)-L-seryl-[N-(C-5-[deoxy-beta-D-glucosyl]-2,3-dihydroxybenzoyl)-L-serine]2} + H(+); Xref=Rhea:RHEA:60388, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:143771, ChEBI:CHEBI:143773; EC=3.1.1.109; Evidence={ECO:0000269|PubMed:16076215}; CATALYTIC ACTIVITY: Reaction=Fe(III)-{N-(2,3-dihydroxybenzoyl)-L-seryl-[N-(C-5-[deoxy-beta-D-glucosyl]-2,3-dihydroxybenzoyl)-L-serine]2} + H(+) + H2O = Fe(III)-[N-(C-5-[deoxy-beta-D-glucosyl]-2,3-dihydroxybenzoyl)-L-serine]2 + N-(2,3-dihydroxybenzoyl)-L-serine; Xref=Rhea:RHEA:60396, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58154, ChEBI:CHEBI:143773, ChEBI:CHEBI:143776; EC=3.1.1.109; Evidence={ECO:0000269|PubMed:16076215}; CATALYTIC ACTIVITY: Reaction=Fe(III)-[N-(C-5-[deoxy-beta-D-glucosyl]-2,3-dihydroxybenzoyl)-L-serine]2 + H(+) + H2O = Fe(III)-[N-(C-5-[deoxy-beta-D-glucosyl]-2,3-dihydroxybenzoyl)-L-serine] + N-(C-5-[deoxy-beta-D-glucosyl]-2,3-dihydroxybenzoyl)-L-serine; Xref=Rhea:RHEA:60408, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:143776, ChEBI:CHEBI:143777, ChEBI:CHEBI:143778; EC=3.1.1.109; Evidence={ECO:0000269|PubMed:16076215}; |
| DNA Binding | |
| EC Number | 3.1.1.109 |
| 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). Shows higher catalytic efficiencies on Fe3(+)-bound forms. The initial linear trimer products are, in turn, very good substrates for further hydrolytic cleavage by IroD, leading to complete degradation of the trilactone to DHB-Ser and/or Glc-DHB-Ser monomers. Hydrolyzes MGE and DGE regioselectively. May be the ferric MGE/DGE esterase responsible for cytoplasmic iron release. {ECO:0000269|PubMed:16076215}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1) |
| Keywords | Cytoplasm;Hydrolase |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:16076215}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 44,760 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=40 uM for Ent {ECO:0000269|PubMed:16076215}; KM=0.12 uM for Fe-Ent {ECO:0000269|PubMed:16076215}; KM=60 uM for MGE {ECO:0000269|PubMed:16076215}; KM=0.08 uM for Fe-MGE {ECO:0000269|PubMed:16076215}; KM=120 uM for DGE {ECO:0000269|PubMed:16076215}; KM=0.12 uM for Fe-DGE {ECO:0000269|PubMed:16076215}; KM=160 uM for TGE {ECO:0000269|PubMed:16076215}; KM=0.43 uM for Fe-TGE {ECO:0000269|PubMed:16076215}; Note=kcat is 1060 min(-1) with Ent as substrate. kcat is 74 min(-1) with Fe-Ent as substrate. kcat is 3720 min(-1) with MGE as substrate. kcat is 46 min(-1) with Fe-MGE as substrate. kcat is 6500 min(-1) with DGE as substrate. kcat is 32 min(-1) with Fe-DGE as substrate. kcat is 4460 min(-1) with TGE as substrate. kcat is 84 min(-1) with Fe-TGE as substrate. {ECO:0000269|PubMed:16076215}; |
| Metal Binding | |
| Rhea ID | RHEA:60392; RHEA:60404; RHEA:60400; RHEA:60388; RHEA:60396; RHEA:60408 |
| Cross Reference Brenda | 3.1.1.109; |