P32397 · CGOX_BACSU
- ProteinCoproporphyrinogen III oxidase
- GenecgoX
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids470 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Involved in coproporphyrin-dependent heme b biosynthesis (PubMed:7928957, PubMed:9217019).
Catalyzes the oxidation of coproporphyrinogen III to coproporphyrin III (PubMed:7928957, PubMed:8288631, PubMed:9217019, PubMed:9784236).
Can also oxidize protoporphyrinogen IX to protoporphyrin-IX (PubMed:19944166, PubMed:7928957, PubMed:8288631, PubMed:9217019, PubMed:9784236).
The specific activity for the oxidation of coproporphyrinogen III is much higher than that for the oxidation of protoporphyrinogen IX (PubMed:7928957, PubMed:9217019).
Can also oxidize mesoporphyrinogen IX, but not uroporphyrinogen III (PubMed:7928957, PubMed:8288631, PubMed:9784236).
Catalyzes the oxidation of coproporphyrinogen III to coproporphyrin III (PubMed:7928957, PubMed:8288631, PubMed:9217019, PubMed:9784236).
Can also oxidize protoporphyrinogen IX to protoporphyrin-IX (PubMed:19944166, PubMed:7928957, PubMed:8288631, PubMed:9217019, PubMed:9784236).
The specific activity for the oxidation of coproporphyrinogen III is much higher than that for the oxidation of protoporphyrinogen IX (PubMed:7928957, PubMed:9217019).
Can also oxidize mesoporphyrinogen IX, but not uroporphyrinogen III (PubMed:7928957, PubMed:8288631, PubMed:9784236).
Catalytic activity
- coproporphyrinogen III + 3 O2 = coproporphyrin III + 3 H2O2This reaction proceeds in the forward direction.
Cofactor
Note: Binds 1 FAD per subunit.
Activity regulation
Only weakly inhibited by acifluorfen, in contrast to eukaryotic family members (PubMed:19944166, PubMed:8288631, PubMed:9784236).
Weakly inhibited by methylacifluorfen (PubMed:9784236).
Bilirubin, biliverdin and hemin are all competitive inhibitors (PubMed:9784236).
Weakly inhibited by methylacifluorfen (PubMed:9784236).
Bilirubin, biliverdin and hemin are all competitive inhibitors (PubMed:9784236).
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
0.56 μM | coproporphyrinogen III | |||||
5.29 μM | coproporphyrinogen III | |||||
0.95 μM | protoporphyrinogen IX | |||||
10.4 μM | protoporphyrinogen IX | |||||
1 μM | protoporphyrinogen IX | |||||
21.1 μM | mesoporphyrinogen IX | |||||
4.92 μM | mesoporphyrinogen IX |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
7 nmol/min/mg | with coproporphyrinogen III as substrate | ||||
0.98 nmol/min/mg | with coproporphyrinogen III as substrate | ||||
0.85 nmol/min/mg | with protoporphyrinogen IX as substrate | ||||
3.7 nmol/min/mg | with protoporphyrinogen IX as substrate | ||||
45 nmol/min/mg | with mesoporphyrinogen IX as substrate |
kcat is 0.05 min-1 with coproporphyrinogen III as substrate (PubMed:9784236).
kcat is 0.19 min-1 with protoporphyrinogen IX as substrate (PubMed:9784236).
kcat is 2.69 min-1 with mesoporphyrinogen IX as substrate (PubMed:9784236).
kcat is 0.19 min-1 with protoporphyrinogen IX as substrate (PubMed:9784236).
kcat is 2.69 min-1 with mesoporphyrinogen IX as substrate (PubMed:9784236).
pH Dependence
Optimum pH is 8.7 (for protoporphyrinogen oxidation).
Pathway
Porphyrin-containing compound metabolism; protoheme biosynthesis.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 12-17 | FAD (UniProtKB | ChEBI) | ||||
Sequence: GGGITG | ||||||
Binding site | 41-42 | FAD (UniProtKB | ChEBI) | ||||
Sequence: EA | ||||||
Binding site | 49 | FAD (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 63-66 | FAD (UniProtKB | ChEBI) | ||||
Sequence: GPDS | ||||||
Binding site | 256 | FAD (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 409 | FAD (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 448-450 | FAD (UniProtKB | ChEBI) | ||||
Sequence: VGI |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | plasma membrane | |
Molecular Function | oxidoreductase activity | |
Molecular Function | oxygen-dependent protoporphyrinogen oxidase activity | |
Biological Process | heme biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCoproporphyrinogen III oxidase
- EC number
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Bacillales > Bacillaceae > Bacillus
Accessions
- Primary accessionP32397
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Peripheral membrane protein
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Mutations cause the accumulation of coproporphyrinogen III or coproporphyrin III in the growth medium and the accumulation of trace amounts of other porphyrinogens or porphyrins intracellularly.
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 64 | Decreased affinity for protoporphyrinogen-IX. | ||||
Sequence: P → A | ||||||
Mutagenesis | 71 | Strongly decreased catalytic activity. | ||||
Sequence: K → A | ||||||
Mutagenesis | 176 | Strongly decreased catalytic activity. | ||||
Sequence: I → A | ||||||
Mutagenesis | 227 | Decreased affinity for protoporphyrinogen-IX. | ||||
Sequence: F → R | ||||||
Mutagenesis | 366 | Reduces protoporphyrinogen oxidation by 90%. | ||||
Sequence: Y → A or H | ||||||
Mutagenesis | 366 | Reduces protoporphyrinogen oxidation by 99%. | ||||
Sequence: Y → E |
Chemistry
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000135263 | 1-470 | Coproporphyrinogen III oxidase | |||
Sequence: MSDGKKHVVIIGGGITGLAAAFYMEKEIKEKNLPLELTLVEASPRVGGKIQTVKKDGYIIERGPDSFLERKKSAPQLVKDLGLEHLLVNNATGQSYVLVNRTLHPMPKGAVMGIPTKIAPFVSTGLFSLSGKARAAMDFILPASKTKDDQSLGEFFRRRVGDEVVENLIEPLLSGIYAGDIDKLSLMSTFPQFYQTEQKHRSLILGMKKTRPQGSGQQLTAKKQGQFQTLSTGLQTLVEEIEKQLKLTKVYKGTKVTKLSHSGSCYSLELDNGVTLDADSVIVTAPHKAAAGMLSELPAISHLKNMHSTSVANVALGFPEGSVQMEHEGTGFVISRNSDFAITACTWTNKKWPHAAPEGKTLLRAYVGKAGDESIVDLSDNDIINIVLEDLKKVMNINGEPEMTCVTRWHESMPQYHVGHKQRIKELREALASAYPGVYMTGASFEGVGIPDCIDQGKAAVSDALTYLFS |
Proteomic databases
Structure
Family & Domains
Sequence similarities
Belongs to the protoporphyrinogen/coproporphyrinogen oxidase family. Coproporphyrinogen III oxidase subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length470
- Mass (Da)51,203
- Last updated1993-10-01 v1
- Checksum95CC4E5847686D2E
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M97208 EMBL· GenBank· DDBJ | AAA22519.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Y14083 EMBL· GenBank· DDBJ | CAA74520.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL009126 EMBL· GenBank· DDBJ | CAB12854.1 EMBL· GenBank· DDBJ | Genomic DNA |