P32397 · CGOX_BACSU

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).

Catalytic activity

Cofactor

FAD (UniProtKB | Rhea| CHEBI:57692 )

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).

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
0.56 μMcoproporphyrinogen III
5.29 μMcoproporphyrinogen III
0.95 μMprotoporphyrinogen IX
10.4 μMprotoporphyrinogen IX
1 μMprotoporphyrinogen IX
21.1 μMmesoporphyrinogen IX
4.92 μMmesoporphyrinogen IX
Vmax pH TEMPERATURE[C] NOTES EVIDENCE
7 nmol/min/mgwith coproporphyrinogen III as substrate
0.98 nmol/min/mgwith coproporphyrinogen III as substrate
0.85 nmol/min/mgwith protoporphyrinogen IX as substrate
3.7 nmol/min/mgwith protoporphyrinogen IX as substrate
45 nmol/min/mgwith 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).

pH Dependence

Optimum pH is 8.7 (for protoporphyrinogen oxidation).

Pathway

Porphyrin-containing compound metabolism; protoheme biosynthesis.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site12-17FAD (UniProtKB | ChEBI)
Binding site41-42FAD (UniProtKB | ChEBI)
Binding site49FAD (UniProtKB | ChEBI)
Binding site63-66FAD (UniProtKB | ChEBI)
Binding site256FAD (UniProtKB | ChEBI)
Binding site409FAD (UniProtKB | ChEBI)
Binding site448-450FAD (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentplasma membrane
Molecular Functionoxidoreductase activity
Molecular Functionoxygen-dependent protoporphyrinogen oxidase activity
Biological Processheme biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Coproporphyrinogen III oxidase
  • EC number

Gene names

    • Name
      cgoX
    • Synonyms
      hemG
      , hemY
    • Ordered locus names
      BSU10140

Organism names

Accessions

  • Primary accession
    P32397

Proteomes

Subcellular Location

Cytoplasm
Cell membrane
; Peripheral membrane protein

Keywords

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.

TypeIDPosition(s)Description
Mutagenesis64Decreased affinity for protoporphyrinogen-IX.
Mutagenesis71Strongly decreased catalytic activity.
Mutagenesis176Strongly decreased catalytic activity.
Mutagenesis227Decreased affinity for protoporphyrinogen-IX.
Mutagenesis366Reduces protoporphyrinogen oxidation by 90%.
Mutagenesis366Reduces protoporphyrinogen oxidation by 99%.

Chemistry

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001352631-470Coproporphyrinogen III oxidase

Proteomic databases

Interaction

Subunit

Monomer.

Protein-protein interaction databases

Chemistry

Family & Domains

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    470
  • Mass (Da)
    51,203
  • Last updated
    1993-10-01 v1
  • Checksum
    95CC4E5847686D2E
MSDGKKHVVIIGGGITGLAAAFYMEKEIKEKNLPLELTLVEASPRVGGKIQTVKKDGYIIERGPDSFLERKKSAPQLVKDLGLEHLLVNNATGQSYVLVNRTLHPMPKGAVMGIPTKIAPFVSTGLFSLSGKARAAMDFILPASKTKDDQSLGEFFRRRVGDEVVENLIEPLLSGIYAGDIDKLSLMSTFPQFYQTEQKHRSLILGMKKTRPQGSGQQLTAKKQGQFQTLSTGLQTLVEEIEKQLKLTKVYKGTKVTKLSHSGSCYSLELDNGVTLDADSVIVTAPHKAAAGMLSELPAISHLKNMHSTSVANVALGFPEGSVQMEHEGTGFVISRNSDFAITACTWTNKKWPHAAPEGKTLLRAYVGKAGDESIVDLSDNDIINIVLEDLKKVMNINGEPEMTCVTRWHESMPQYHVGHKQRIKELREALASAYPGVYMTGASFEGVGIPDCIDQGKAAVSDALTYLFS

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

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