Function and Biology

Ferric camphor bound Cytochrome P450cam containing a selenocysteine as the 5th heme ligand, tetragonal crystal form

Source organism: Pseudomonas putida
Biochemical function: metal ion binding
Biological process: (+)-camphor catabolic process
Cellular component: cytoplasm

EC 1.14.15.1: Camphor 5-monooxygenase

Reaction catalysed:
(+)-camphor + reduced putidaredoxin + O(2) = (+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H(2)O
Systematic name:
(+)-camphor,reduced putidaredoxin:oxygen oxidoreductase (5-hydroxylating)
Alternative Name(s):
  • 2-bornanone 5-exo-hydroxylase
  • Bornanone 5-exo-hydroxylase
  • Camphor 5-exo-hydroxylase
  • Camphor 5-exo-methylene hydroxylase
  • Camphor 5-exohydroxylase
  • Camphor hydroxylase
  • Camphor methylene hydroxylase
  • Cytochrome p450-cam
  • D-camphor monooxygenase
  • D-camphor-exo-hydroxylase
  • Methylene hydroxylase
  • Methylene monooxygenase

Sequence family

Pfam Protein family (Pfam)
PF00067
Domain description: Cytochrome P450
Occurring in:
  1. Camphor 5-monooxygenase
The deposited structure of PDB entry 3fwi contains 1 copy of Pfam domain PF00067 (Cytochrome P450) in Camphor 5-monooxygenase. Showing 1 copy in chain A.

InterPro InterPro annotations
IPR002397
Domain description: Cytochrome P450, B-class
Occurring in:
  1. Camphor 5-monooxygenase
IPR036396
Domain description: Cytochrome P450 superfamily
Occurring in:
  1. Camphor 5-monooxygenase
IPR001128
Domain description: Cytochrome P450
Occurring in:
  1. Camphor 5-monooxygenase

Structure domain

CATH CATH domain
1.10.630.10
Class: Mainly Alpha
Architecture: Orthogonal Bundle
Topology: Cytochrome p450
Homology: Cytochrome P450
Occurring in:
  1. Camphor 5-monooxygenase
The deposited structure of PDB entry 3fwi contains 1 copy of CATH domain 1.10.630.10 (Cytochrome p450) in Camphor 5-monooxygenase. Showing 1 copy in chain A.