| IED ID | IndEnz0018000289 |
| Enzyme Type ID | peroxidase000289 |
| Protein Name |
Deferrochelatase EC 4.99.1.1 Peroxidase EfeB EC 1.11.1.- |
| Gene Name | efeB ECP_1018 |
| Organism | Escherichia coli O6:K15:H31 (strain 536 / UPEC) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli O6:K15:H31 (strain 536 / UPEC) |
| Enzyme Sequence | MQYEDENGVNEPSRRRLLKGIGALALAGSCPVAHAQKTQSAPGTLSPDARNEKQPFYGEHQAGILTPQQAAMMLVAFDVLASDKADLERLFRLLTQRFAFLTQGGAAPETPNPRLPPLDSGILGGYIAPDNLTITLSVGHSLFDERFGLAPQMPKKLQKMTRFPNDSLDAALCHGDVLLQICANTQDTVIHALRDIIKHTPDLLSVRWKREGFISDHAARSKGKETPINLLGFKDGTANPDSQNAKLMQKVVWVTADQQEPAWTIGGSYQAVRLIQFRVEFWDRTPLKEQQTIFGRDKQTGAPLGMLHEHDVPDYASDPEGKVIALDSHIRLANPRTAESESSLMLRRGYSYSLGVTNSGQLDMGLLFVCYQHDLEKGFLTVQKRLNGEALEEYVKPIGGGYFFALPGVKDANDYLGSALLRV |
| Enzyme Length | 423 |
| Uniprot Accession Number | Q0TJ48 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 347; /note=Heme b; /evidence=ECO:0000250|UniProtKB:P31545 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=2 H(+) + heme b = Fe(2+) + protoporphyrin IX; Xref=Rhea:RHEA:22584, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:57306, ChEBI:CHEBI:60344; EC=4.99.1.1; Evidence={ECO:0000250|UniProtKB:P31545};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22585; Evidence={ECO:0000250|UniProtKB:P31545}; |
| DNA Binding | |
| EC Number | 4.99.1.1; 1.11.1.- |
| Enzyme Function | FUNCTION: Involved in the recovery of exogenous heme iron. Extracts iron from heme while preserving the protoporphyrin ring intact. {ECO:0000250|UniProtKB:P31545}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Binding site (1); Chain (1); Metal binding (1); Region (2); Signal peptide (1) |
| Keywords | Heme;Iron;Lyase;Metal-binding;Oxidoreductase;Periplasm;Peroxidase;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Periplasm {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven. |
| Signal Peptide | SIGNAL 1..35; /note=Tat-type signal; /evidence=ECO:0000255|PROSITE-ProRule:PRU00648 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 46,620 |
| Kinetics | |
| Metal Binding | METAL 329; /note=Iron (heme b proximal ligand); via tele nitrogen; /evidence=ECO:0000250|UniProtKB:P31545 |
| Rhea ID | RHEA:22584; RHEA:22585 |
| Cross Reference Brenda |