| IED ID | IndEnz0018000231 |
| Enzyme Type ID | peroxidase000231 |
| Protein Name |
Coproheme decarboxylase EC 1.3.98.5 Coproheme III oxidative decarboxylase Hydrogen peroxide-dependent heme synthase LmCld |
| Gene Name | chdC hemQ lmo2113 |
| Organism | Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Listeriaceae Listeria Listeria monocytogenes Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e) |
| Enzyme Sequence | MNEAVKTLDGWFCLHDFRSIDWAAWRELNPGNQELMLNELSHFLSDMEITKNIGEGEHTIYSILGQKADLVFFTLRDSLEALNEVENRFNKLAIADYLLPTYSYISVVELSNYLASHMAGGDDPYQNKGVRARLYPALPPKKHICFYPMSKKRDGADNWYMLPMEERQQLIRDHGLIGRSYAGKVQQIIGGSIGFDDYEWGVTLFSDDALEFKRIVTEMRFDEASARYAEFGSFFIGNLLLSEQLSKLFTI |
| Enzyme Length | 251 |
| Uniprot Accession Number | Q8Y5F1 |
| Absorption | |
| Active Site | ACT_SITE 147; /evidence="ECO:0000255|HAMAP-Rule:MF_01442, ECO:0000305|PubMed:31423350" |
| Activity Regulation | |
| Binding Site | BINDING 133; /note="Fe-coproporphyrin III"; /evidence="ECO:0000255|HAMAP-Rule:MF_01442, ECO:0000269|PubMed:27758026, ECO:0007744|PDB:5LOQ"; BINDING 187; /note="Fe-coproporphyrin III"; /evidence="ECO:0000255|HAMAP-Rule:MF_01442, ECO:0000269|PubMed:27758026, ECO:0007744|PDB:5LOQ"; BINDING 225; /note="Fe-coproporphyrin III"; /evidence="ECO:0000255|HAMAP-Rule:MF_01442, ECO:0000269|PubMed:27758026, ECO:0007744|PDB:5LOQ" |
| 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:27758026, ECO:0000269|PubMed:29536725, ECO:0000269|PubMed:31423350};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56517; Evidence={ECO:0000255|HAMAP-Rule:MF_01442, ECO:0000269|PubMed:27758026, ECO:0000269|PubMed:31423350}; 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:31423350};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57941; Evidence={ECO:0000255|HAMAP-Rule:MF_01442, ECO:0000269|PubMed:27758026, ECO:0000269|PubMed:31423350}; 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:31423350};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57945; Evidence={ECO:0000255|HAMAP-Rule:MF_01442, ECO:0000269|PubMed:27758026, ECO:0000269|PubMed:31423350}; |
| DNA Binding | |
| EC Number | 1.3.98.5 |
| Enzyme Function | FUNCTION: Involved in coproporphyrin-dependent heme b biosynthesis (PubMed:27758026, PubMed:31423350). Catalyzes the decarboxylation of Fe-coproporphyrin III (coproheme) to heme b (protoheme IX), the last step of the pathway (PubMed:27758026, PubMed:31423350, PubMed:29536725). The reaction occurs in a stepwise manner with a three-propionate intermediate (PubMed:27758026, PubMed:31423350). {ECO:0000269|PubMed:27758026, ECO:0000269|PubMed:29536725, ECO:0000269|PubMed:31423350}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Porphyrin-containing compound metabolism; protoheme biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01442, ECO:0000305|PubMed:27758026}. |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (11); Binding site (3); Chain (1); Helix (11); Metal binding (1); Mutagenesis (3); Region (1); Turn (2) |
| Keywords | 3D-structure;Heme;Heme biosynthesis;Iron;Metal-binding;Oxidoreductase;Reference proteome |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (4) |
| Cross Reference PDB | 4WWS; 5LOQ; 6FXJ; 6FXQ; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 28,852 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=37.1 uM for H(2)O(2) {ECO:0000269|PubMed:27758026}; |
| Metal Binding | METAL 174; /note="Iron (Fe-coproporphyrin III axial ligand)"; /evidence="ECO:0000255|HAMAP-Rule:MF_01442, ECO:0000269|PubMed:27758026, ECO:0007744|PDB:5LOQ" |
| Rhea ID | RHEA:56516; RHEA:56517; RHEA:57940; RHEA:57941; RHEA:57944; RHEA:57945 |
| Cross Reference Brenda | 1.3.98.5; |