Function and Biology Details
Reaction catalysed:
Trans,octacis-decaprenylphospho-beta-D-ribofuranose + FAD = trans,octacis-decaprenylphospho-beta-D-erythro-pentofuranosid-2-ulose + FADH(2)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Vanillyl-alcohol oxidase, C-terminal subdomain 2
- D-arabinono-1,4-lactone oxidase, C-terminal domain
- FAD-binding, type PCMH, subdomain 2
- FAD linked oxidase, N-terminal
- FAD-binding domain, PCMH-type
- FAD-binding, type PCMH-like superfamily
- L-gulonolactone/D-arabinono-1,4-lactone oxidase-like
- FAD-binding, type PCMH, subdomain 1
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
Decaprenylphosphoryl-beta-D-ribose oxidase (preferred)
PDBe Complex ID:
PDB-CPX-106479 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Decaprenylphosphoryl-beta-D-ribose oxidase
Molecule details ›
Chain: A
Length: 468 amino acids
Theoretical weight: 51.19 KDa
Source organism: Mycolicibacterium smegmatis
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains:
Length: 468 amino acids
Theoretical weight: 51.19 KDa
Source organism: Mycolicibacterium smegmatis
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
A0R607 (Residues: 1-460; Coverage: 100%)
Sequence domains:
