| IED ID | IndEnz0018001126 |
| Enzyme Type ID | peroxidase001126 |
| Protein Name |
Deferrochelatase EC 4.99.1.1 Peroxidase EfeN EC 1.11.1.- |
| Gene Name | efeN ywbN BSU38260 ipa-29d |
| Organism | Bacillus subtilis (strain 168) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Bacillus Bacillus subtilis group Bacillus subtilis Bacillus subtilis subsp. subtilis Bacillus subtilis (strain 168) |
| Enzyme Sequence | MSDEQKKPEQIHRRDILKWGAMAGAAVAIGASGLGGLAPLVQTAAKPSKKDEKEEEQIVPFYGKHQAGITTAHQTYVYFAALDVTAKDKSDIITLFRNWTSLTQMLTSGKKMSAEQRNQYLPPQDTGESADLSPSNLTVTFGFGPGFFEKDGKDRFGLKSKKPKHLAALPAMPNDNLDEKQGGGDICIQVCADDEQVAFHALRNLLNQAVGTCEVRFVNKGFLSGGKNGETPRNLFGFKDGTGNQSTKDDTLMNSIVWIQSGEPDWMTGGTYMAFRKIKMFLEVWDRSSLKDQEDTFGRRKSSGAPFGQKKETDPVKLNQIPSNSHVSLAKSTGKQILRRAFSYTEGLDPKTGYMDAGLLFISFQKNPDNQFIPMLKALSAKDALNEYTQTIGSALYACPGGCKKGEYIAQRLLES |
| Enzyme Length | 416 |
| Uniprot Accession Number | P39597 |
| Absorption | |
| Active Site | ACT_SITE 240; /note=Proton acceptor; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | BINDING 339; /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 (By similarity). {ECO:0000250, ECO:0000269|PubMed:16672620}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (13); Binding site (1); Chain (1); Helix (15); Metal binding (1); Region (2); Signal peptide (1); Turn (3) |
| Keywords | 3D-structure;Heme;Iron;Lyase;Metal-binding;Oxidoreductase;Peroxidase;Reference proteome;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | |
| Post Translational Modification | PTM: Exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven. |
| Signal Peptide | SIGNAL 1..28; /note=Tat-type signal; /evidence=ECO:0000255|PROSITE-ProRule:PRU00648 |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 6KMM; 6KMN; |
| Mapped Pubmed ID | 32971035; |
| Motif | |
| Gene Encoded By | |
| Mass | 45,693 |
| Kinetics | |
| Metal Binding | METAL 326; /note=Iron (heme b proximal ligand); /evidence=ECO:0000250|UniProtKB:P31545 |
| Rhea ID | RHEA:22584; RHEA:22585 |
| Cross Reference Brenda |