Q2FXA5 · CGOX_STAA8
- ProteinCoproporphyrinogen III oxidase
- GenecgoX
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids466 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Involved in coproporphyrin-dependent heme b biosynthesis (PubMed:25908396).
Catalyzes the oxidation of coproporphyrinogen III to coproporphyrin III (PubMed:25908396, PubMed:27597779).
Can also oxidize protoporphyrinogen IX (PubMed:27597779).
Catalyzes the oxidation of coproporphyrinogen III to coproporphyrin III (PubMed:25908396, PubMed:27597779).
Can also oxidize protoporphyrinogen IX (PubMed:27597779).
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
The generation of protoporphyrin IX, but not coproporphyrin III, is stimulated by heme-bound HemQ. This stimulatory effect is mediated by superoxide (PubMed:27597779).
Inhibited by acifluorfen analogs (PubMed:25908396).
Inhibited by acifluorfen analogs (PubMed:25908396).
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
0.31 μM | coproporphyrinogen III | |||||
6.7 μM | coproporphyrinogen III |
kcat is 1.33 min-1 with coproporphyrinogen III as substrate (PubMed:25908396).
kcat is 0.46 min-1 with coproporphyrinogen III as substrate (PubMed:27597779).
kcat is 0.44 min-1 with protoporphyrinogen IX as substrate (PubMed:27597779).
kcat is 0.46 min-1 with coproporphyrinogen III as substrate (PubMed:27597779).
kcat is 0.44 min-1 with protoporphyrinogen IX as substrate (PubMed:27597779).
Pathway
Porphyrin-containing compound metabolism; protoheme biosynthesis.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 9-14 | FAD (UniProtKB | ChEBI) | ||||
Sequence: GAGITG | ||||||
Binding site | 34-35 | FAD (UniProtKB | ChEBI) | ||||
Sequence: EA | ||||||
Binding site | 42 | FAD (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 56-59 | FAD (UniProtKB | ChEBI) | ||||
Sequence: GPES | ||||||
Binding site | 254 | FAD (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 446-448 | FAD (UniProtKB | ChEBI) | ||||
Sequence: VGL |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
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
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Bacillales > Staphylococcaceae > Staphylococcus
Accessions
- Primary accessionQ2FXA5
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000450281 | 1-466 | Coproporphyrinogen III oxidase | |||
Sequence: MTKSVAIIGAGITGLSSAYFLKQQDPNIDVTIFEASNRPGGKIQSYRKDGYMIELGPESYLGRKTIMTELAKDIGLEQDIVTNTTGQSYIFAKNKLYPIPGGSIMGIPTDIKPFVTTKLISPLGKLRAGFDLLKKPTQMQDGDISVGAFFRARLGNEVLENLIEPLMGGIYGTDIDKLSLMSTFPNFKEKEEAFGSLIKGMKDEKNKRLKQRQLYPGAPKGQFKQFKHGLSSFIEALEQDVKNKGVTIRYNTSVDDIITSQKQYKIVYNDQLEEVYDGVLVTTPHQVFLNWFGQDPAFDYFKTMDSTTVATVVLAFDEKDIENTHDGTGFVIARTSDTDITACTWTSKKWPFTTPEGKVLIRAYVGKPGDTVVDDHTDNELVSIVRRDLSQMMTFKGDPEFTIVNRLPKSMPQYHVGHIQQIRQIQAHIKQTYPRLRVTGASFEAVGLPDCITQGKVAAEEVIAEL |
Proteomic databases
Interaction
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length466
- Mass (Da)51,983
- Last updated2006-03-21 v1
- ChecksumF732B045F34C4B79
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000253 EMBL· GenBank· DDBJ | ABD31021.1 EMBL· GenBank· DDBJ | Genomic DNA |