| IED ID | IndEnz0018000253 |
| Enzyme Type ID | peroxidase000253 |
| Protein Name |
Coproheme decarboxylase EC 1.3.98.5 Coproheme III oxidative decarboxylase Hydrogen peroxide-dependent heme synthase |
| Gene Name | chdC TTHA1714 |
| Organism | Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Deinococcus-Thermus Deinococci Thermales Thermaceae Thermus Thermus thermophilus Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) |
| Enzyme Sequence | MERHVPEPTHTLEGWHVLHDFRLLDFARWFSAPLEAREDAWEELKGLVREWRELEEAGQGSYGIYQVVGHKADLLFLNLRPGLDPLLEAEARLSRSAFARYLGRSYSFYSVVELGSQEKPLDPESPYVKPRLTPRVPKSGYVCFYPMNKRRQGQDNWYMLPAKERASLMKAHGETGRKYQGKVMQVISGAQGLDDWEWGVDLFSEDPVQFKKIVYEMRFDEVSARYGEFGPFFVGKYLDEEALRAFLGL |
| Enzyme Length | 249 |
| Uniprot Accession Number | Q5SHL6 |
| Absorption | |
| Active Site | ACT_SITE 145; /evidence=ECO:0000255|HAMAP-Rule:MF_01442 |
| 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; BINDING 223; /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};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56517; Evidence={ECO:0000255|HAMAP-Rule:MF_01442}; 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};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57941; Evidence={ECO:0000255|HAMAP-Rule:MF_01442}; 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};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57945; Evidence={ECO:0000255|HAMAP-Rule:MF_01442}; |
| DNA Binding | |
| EC Number | 1.3.98.5 |
| Enzyme Function | FUNCTION: Involved in coproporphyrin-dependent heme b biosynthesis. Catalyzes the decarboxylation of Fe-coproporphyrin III (coproheme) to heme b (protoheme IX), the last step of the pathway. The reaction occurs in a stepwise manner with a three-propionate harderoheme intermediate (By similarity). When reconstituted with heme, can generate oxygen using chlorite or hydrogen peroxide as substrate (in vitro), but has very low affinity for hydrogen peroxide and chlorite and extremely low enzyme activity (PubMed:15965735). {ECO:0000255|HAMAP-Rule:MF_01442, ECO:0000269|PubMed:15965735}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Porphyrin-containing compound metabolism; protoheme biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01442}. |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (9); Binding site (3); Chain (1); Helix (10); Metal binding (1); Region (1); Turn (3) |
| 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 (1) |
| Cross Reference PDB | 1VDH; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 28,906 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=13 mM for chlorite {ECO:0000269|PubMed:15965735}; KM=25 mM for hydrogen peroxide {ECO:0000269|PubMed:15965735}; Note=kcat is 0.77 sec(-1) with chlorite and 0.52 sec(-1) with hydrogen peroxide. The kcat values are at least 1000 times lower than those observed for well-characterized chlorite dismutases, and the specific activity is even lower.; |
| 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 |