| IED ID | IndEnz0018001468 |
| Enzyme Type ID | peroxidase001468 |
| Protein Name |
Coproheme decarboxylase EC 1.3.98.5 Coproheme III oxidative decarboxylase Hydrogen peroxide-dependent heme synthase |
| Gene Name | chdC hemQ NWMN_0550 |
| Organism | Staphylococcus aureus (strain Newman) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Staphylococcaceae Staphylococcus Staphylococcus aureus Staphylococcus aureus (strain Newman) |
| Enzyme Sequence | MSQAAETLDGWYSLHLFYAVDWASLRIVPKDERDALVTEFQSFLENTATVRSSKSGDQAIYNITGQKADLLLWFLRPEMKSLNHIENEFNKLRIADFLIPTYSYVSVIELSNYLAGKSDEDPYENPHIKARLYPELPHSDYICFYPMNKRRNETYNWYMLTMEERQKLMYDHGMIGRKYAGKIKQFITGSVGFDDFEWGVTLFSDDVLQFKKIVYEMRFDETTARYGEFGSFFVGHIINTNEFDQFFAIS |
| Enzyme Length | 250 |
| Uniprot Accession Number | A6QEP0 |
| Absorption | |
| Active Site | ACT_SITE 145; /evidence="ECO:0000255|HAMAP-Rule:MF_01442, ECO:0000305|PubMed:27936663" |
| Activity Regulation | |
| Binding Site | BINDING 131; /note=Fe-coproporphyrin III; /evidence=ECO:0000255|HAMAP-Rule:MF_01442; BINDING 185; /note=Fe-coproporphyrin III; /evidence=ECO:0000255|HAMAP-Rule:MF_01442 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Fe-coproporphyrin III + 2 H(+) + 2 H2O2 = 2 CO2 + 4 H2O + heme b; Xref=Rhea:RHEA:56516, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16240, ChEBI:CHEBI:16526, ChEBI:CHEBI:60344, ChEBI:CHEBI:68438; EC=1.3.98.5; Evidence={ECO:0000255|HAMAP-Rule:MF_01442, ECO:0000269|PubMed:26083961, ECO:0000269|PubMed:27936663, ECO:0000269|PubMed:27982566};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56517; Evidence={ECO:0000255|HAMAP-Rule:MF_01442, ECO:0000269|PubMed:26083961, ECO:0000269|PubMed:27936663}; CATALYTIC ACTIVITY: Reaction=Fe-coproporphyrin III + H(+) + H2O2 = CO2 + 2 H2O + harderoheme III; Xref=Rhea:RHEA:57940, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16240, ChEBI:CHEBI:16526, ChEBI:CHEBI:68438, ChEBI:CHEBI:142463; Evidence={ECO:0000255|HAMAP-Rule:MF_01442, ECO:0000269|PubMed:26083961, ECO:0000269|PubMed:27936663};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57941; Evidence={ECO:0000255|HAMAP-Rule:MF_01442, ECO:0000269|PubMed:26083961, ECO:0000269|PubMed:27936663}; CATALYTIC ACTIVITY: Reaction=H(+) + H2O2 + harderoheme III = CO2 + 2 H2O + heme b; Xref=Rhea:RHEA:57944, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16240, ChEBI:CHEBI:16526, ChEBI:CHEBI:60344, ChEBI:CHEBI:142463; Evidence={ECO:0000255|HAMAP-Rule:MF_01442, ECO:0000269|PubMed:26083961, ECO:0000269|PubMed:27936663};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57945; Evidence={ECO:0000255|HAMAP-Rule:MF_01442, ECO:0000269|PubMed:26083961, ECO:0000269|PubMed:27936663}; |
| DNA Binding | |
| EC Number | 1.3.98.5 |
| Enzyme Function | FUNCTION: Involved in coproporphyrin-dependent heme b biosynthesis (PubMed:26083961). Catalyzes the decarboxylation of Fe-coproporphyrin III (coproheme) to heme b (protoheme IX), the last step of the pathway (PubMed:26083961, PubMed:27936663, PubMed:27982566). The reaction occurs in a stepwise manner with a three-propionate harderoheme intermediate (PubMed:26083961, PubMed:27936663, PubMed:27982566). The first decarboxylation step is fast and yields the three-propionate harderoheme isomer III intermediate, while the slower second decarboxylation appears to control the overall rate. H(2)O(2) is the assumed biological oxidant, but either H(2)O(2) or peracetic acid yields the same intermediates and products (PubMed:26083961). Has weak peroxidase and catalase activities in vitro (PubMed:23737523). {ECO:0000269|PubMed:23737523, ECO:0000269|PubMed:26083961, ECO:0000269|PubMed:27936663, ECO:0000269|PubMed:27982566}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Porphyrin-containing compound metabolism; protoheme biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01442, ECO:0000305|PubMed:23737523, ECO:0000305|PubMed:26083961}. |
| nucleotide Binding | |
| Features | Active site (1); Binding site (2); Chain (1); Metal binding (1); Mutagenesis (8); Region (1) |
| Keywords | Heme;Heme biosynthesis;Iron;Metal-binding;Oxidoreductase |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 29,390 |
| Kinetics | |
| Metal Binding | METAL 172; /note=Iron (Fe-coproporphyrin III axial ligand); /evidence=ECO:0000255|HAMAP-Rule:MF_01442 |
| Rhea ID | RHEA:56516; RHEA:56517; RHEA:57940; RHEA:57941; RHEA:57944; RHEA:57945 |
| Cross Reference Brenda |