| IED ID | IndEnz0018001214 |
| Enzyme Type ID | peroxidase001214 |
| Protein Name |
Deferrochelatase EC 4.99.1.1 Peroxidase EfeB EC 1.11.1.- |
| Gene Name | efeB ycdB b1019 JW1004 |
| Organism | Escherichia coli (strain K12) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12) |
| Enzyme Sequence | MQYKDENGVNEPSRRRLLKVIGALALAGSCPVAHAQKTQSAPGTLSPDARNEKQPFYGEHQAGILTPQQAAMMLVAFDVLASDKADLERLFRLLTQRFAFLTQGGAAPETPNPRLPPLDSGILGGYIAPDNLTITLSVGHSLFDERFGLAPQMPKKLQKMTRFPNDSLDAALCHGDVLLQICANTQDTVIHALRDIIKHTPDLLSVRWKREGFISDHAARSKGKETPINLLGFKDGTANPDSQNDKLMQKVVWVTADQQEPAWTIGGSYQAVRLIQFRVEFWDRTPLKEQQTIFGRDKQTGAPLGMQHEHDVPDYASDPEGKVIALDSHIRLANPRTAESESSLMLRRGYSYSLGVTNSGQLDMGLLFVCYQHDLEKGFLTVQKRLNGEALEEYVKPIGGGYFFALPGVKDANDYFGSALLRV |
| Enzyme Length | 423 |
| Uniprot Accession Number | P31545 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 296; /note="Protoporphyrin IX"; /evidence="ECO:0000269|Ref.11, ECO:0007744|PDB:2Y4E"; BINDING 347; /note="Heme b"; /evidence="ECO:0000269|Ref.11, ECO:0007744|PDB:2Y4F" |
| 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:19564607};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22585; Evidence={ECO:0000269|PubMed:19564607}; |
| 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 in vitro. {ECO:0000269|PubMed:16551627, ECO:0000269|PubMed:19564607}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (13); Binding site (2); Chain (1); Helix (17); Metal binding (1); Region (3); Signal peptide (1); Turn (5) |
| Keywords | 3D-structure;Heme;Iron;Lyase;Metal-binding;Oxidoreductase;Periplasm;Peroxidase;Reference proteome;Signal |
| Interact With | |
| Induction | INDUCTION: Repressed by Fur in the presence of iron. Repressed at high pH by the two-component regulatory system CpxA/CpxR. {ECO:0000269|PubMed:12746439, ECO:0000269|PubMed:17627767}. |
| Subcellular Location | SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:16551627}. |
| Modified Residue | |
| Post Translational Modification | PTM: Exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven. Can also be exported by the Sec system. |
| Signal Peptide | SIGNAL 1..35; /note=Tat-type signal |
| Structure 3D | X-ray crystallography (3) |
| Cross Reference PDB | 2Y4D; 2Y4E; 2Y4F; |
| Mapped Pubmed ID | 16606699; |
| Motif | |
| Gene Encoded By | |
| Mass | 46,754 |
| Kinetics | |
| Metal Binding | METAL 329; /note="Iron (heme b proximal ligand); via tele nitrogen"; /evidence="ECO:0000269|Ref.11, ECO:0007744|PDB:2Y4F" |
| Rhea ID | RHEA:22584; RHEA:22585 |
| Cross Reference Brenda |