Q2G0J1 · CHDC_STAA8
- ProteinCoproheme decarboxylase
- GenechdC
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids250 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Involved in coproporphyrin-dependent heme b biosynthesis (PubMed:25908396).
Catalyzes the decarboxylation of Fe-coproporphyrin III (coproheme) to heme b (protoheme IX), the last step of the pathway (By similarity).
The reaction occurs in a stepwise manner with a three-propionate harderoheme intermediate (By similarity).
Can stimulate the generation of protoporphyrin IX, but not coproporphyrin III, by HemY (PubMed:27597779).
Catalyzes the decarboxylation of Fe-coproporphyrin III (coproheme) to heme b (protoheme IX), the last step of the pathway (By similarity).
The reaction occurs in a stepwise manner with a three-propionate harderoheme intermediate (By similarity).
Can stimulate the generation of protoporphyrin IX, but not coproporphyrin III, by HemY (PubMed:27597779).
Catalytic activity
- Fe-coproporphyrin III + 2 H+ + 2 H2O2 = 2 CO2 + 4 H2O + heme bThis reaction proceeds in the forward direction.
- Fe-coproporphyrin III + H+ + H2O2 = CO2 + 2 H2O + harderoheme IIIThis reaction proceeds in the forward direction.
- H+ + H2O2 + harderoheme III = CO2 + 2 H2O + heme bThis reaction proceeds in the forward direction.
Cofactor
Note: Fe-coproporphyrin III acts both as a substrate and a redox cofactor (By similarity).
Was originally thought to use heme as a cofactor (PubMed:25908396).
Was originally thought to use heme as a cofactor (PubMed:25908396).
Pathway
Porphyrin-containing compound metabolism; protoheme biosynthesis.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 131 | Fe-coproporphyrin III (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Active site | 145 | |||||
Sequence: Y | ||||||
Binding site | 145-149 | Fe-coproporphyrin III (UniProtKB | ChEBI) | ||||
Sequence: YPMNK | ||||||
Binding site | 172 | Fe (UniProtKB | ChEBI) of Fe-coproporphyrin III (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 185 | Fe-coproporphyrin III (UniProtKB | ChEBI) | ||||
Sequence: Q |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | heme binding | |
Molecular Function | metal ion binding | |
Molecular Function | peroxidase activity | |
Biological Process | heme biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCoproheme decarboxylase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Bacillales > Staphylococcaceae > Staphylococcus
Accessions
- Primary accessionQ2G0J1
Proteomes
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000294046 | 1-250 | Coproheme decarboxylase | |||
Sequence: MSQAAETLDGWYSLHLFYAVDWASLRIVPKDERDALVTEFQSFLENTATVRSSKSGDQAIYNITGQKADLLLWFLRPEMKSLNHIENEFNKLRIADFLIPTYSYVSVIELSNYLAGKSDEDPYENPHIKARLYPELPHSDYICFYPMNKRRNETYNWYMLTMEERQKLMYDHGMIGRKYAGKIKQFITGSVGFDDFEWGVTLFSDDVLQFKKIVYEMRFDETTARYGEFGSFFVGHIINTNEFDQFFAIS |
Proteomic databases
Interaction
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length250
- Mass (Da)29,390
- Last updated2006-03-21 v1
- ChecksumB991C3DB917160E0
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000253 EMBL· GenBank· DDBJ | ABD29716.1 EMBL· GenBank· DDBJ | Genomic DNA |