| IED ID | IndEnz0018000233 |
| Enzyme Type ID | peroxidase000233 |
| Protein Name |
Deferrochelatase EC 4.99.1.1 Peroxidase EfeB EC 1.11.1.- |
| Gene Name | efeB ycdB Z1521 ECs1265 |
| Organism | Escherichia coli O157:H7 |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli O157:H7 |
| Enzyme Sequence | MQYEDKNGVNEPSRRRLLKGIGALALAGSCPVAHAQKTQSAPGTLSPVARNEKQPFYGEHQAGILTPQQAAMMLVAFDVLASDKADLERLFRLLTQRFAFLTQGGAAPETPNPRLPPLDSGILGGYIAPDNLTITLSVGHSLFDERFGLAPQMPKKLQKMTRFPNDSLDAALCHGDVLLQICANTQDTVIHALRDIIKHTPDLLSVRWKREGFISDHAARSKGKETPINLLGFKDGTANPDSQNDKLMQKVVWVTADQQEPAWTIGGSYQAVRLIQFRVEFWDRTPLKEQQTIFGRDKQTGAPLGMQHEHDVPDYASDPEGKGIALDSHIRLANPRTAESESSLMLRRGYSYSLGVTNSGQLDMGLLFVCYQHDLEKGFLTVQKRLNGEALEEYVKPIGGGYFFALPGVKDANDYLGSALLRV |
| Enzyme Length | 423 |
| Uniprot Accession Number | Q8XAS4 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 347; /note="Heme b"; /evidence="ECO:0000269|PubMed:21324904, ECO:0007744|PDB:3O72" |
| 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:0000269|PubMed:21324904};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22585; Evidence={ECO:0000269|PubMed:21324904}; |
| 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. Also displays peroxidase activity on guaiacol and catechol in vitro. The deferrochelatase activity appears to be closely related to the peroxidation activity, but the link is unclear. {ECO:0000269|PubMed:21324904}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (13); Binding site (1); Chain (1); Helix (16); Metal binding (1); Mutagenesis (16); Region (2); Signal peptide (1); Turn (5) |
| Keywords | 3D-structure;Heme;Iron;Lyase;Metal-binding;Oxidoreductase;Periplasm;Peroxidase;Reference proteome;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 | X-ray crystallography (1) |
| Cross Reference PDB | 3O72; |
| 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:0000269|PubMed:21324904, ECO:0007744|PDB:3O72" |
| Rhea ID | RHEA:22584; RHEA:22585 |
| Cross Reference Brenda |