O32434 · CGOX_PROFF

Function

function

Involved in coproporphyrin-dependent heme b biosynthesis. Catalyzes the oxidation of coproporphyrinogen III to coproporphyrin III.

Catalytic activity

Cofactor

FAD (UniProtKB | Rhea| CHEBI:57692 )

Note: Binds 1 FAD per subunit.

Pathway

Porphyrin-containing compound metabolism; protoheme biosynthesis.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site33-38FAD (UniProtKB | ChEBI)
Binding site56-57FAD (UniProtKB | ChEBI)
Binding site64FAD (UniProtKB | ChEBI)
Binding site78-81FAD (UniProtKB | ChEBI)
Binding site300FAD (UniProtKB | ChEBI)
Binding site448FAD (UniProtKB | ChEBI)
Binding site487-489FAD (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
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
      hemY

Organism names

Accessions

  • Primary accession
    O32434

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001352681-527Coproporphyrinogen III oxidase

Structure

Family & Domains

Features

Showing features for compositional bias, region.

TypeIDPosition(s)Description
Compositional bias1-18Polar residues
Region1-23Disordered
Region231-267Disordered
Compositional bias235-264Polar residues

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    527
  • Mass (Da)
    55,268
  • Last updated
    1998-01-01 v1
  • Checksum
    579CB0A3318BF938
MSTTDRVTTPTPTVSGTDAPGPDASHCHLVVVGGGITGLAAAWQGMARGARVSVVESDDHFGGKVVTDRRDGFLVEQGPDSFVAYRPAALKLIEELGLSDQVIAPGGGRRVSLLSRGKLRPMPAGMGMVLPTRMWPFVTTTVLSWPDKIRAGLDLVIPRRLPDHDVAIGAFLRQRLGDGIVRRFADPMVGGIYGAGIDELSLDAVLPSLRDNERDHRSLMVASLAGGRASRRAARQRAAQNNAQQNSSHQNSTGQNNSAGTRGPAASPFRTLRGGLGQLIDALVDQLRAGGVELLVNTSVDLLGRDGVHLSDGRVLPADAVVLAGGVASSARLLRPQLPAAARALAQIPLASTTIVSLAWPVSAFDVAPDSQGWLEADAGPVSGLTASSIKFAGRAPDGSVLMRVFVPDKRGPLTDAPDDELLSAVIDHVRPLLGVHGEPGLTQITRWHKVMPKYTVGHLERAAVVDSTLAEQRPTWAVAGSALHGVGLPDCISDARHSADEVIDAALAATPSAPNRNAATDRTETR

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias1-18Polar residues
Compositional bias235-264Polar residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
D85417
EMBL· GenBank· DDBJ
BAA21909.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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