Function and Biology Details
Biochemical function:
Biological process:
- not assigned
Cellular component:
- not assigned
Sequence domains:
- B12-dependent dehydratases, beta subunit
- Diol dehydratase-reactivating factor, alpha subunit, swiveling domain superfamily
- ATPase, nucleotide binding domain
- Diol dehydratase-reactivating factor large subunit
- Diol/glycerol dehydratase/dehydratase reactivating factor
- Diol/glycerol dehydratase reactivating factor, small subunit
- Nucleic acid-binding, OB-fold
- Diol dehydratase reactivase ATPase-like domain
1 more domain
Structure analysis Details
Assembly composition:
hetero tetramer (preferred)
Assembly name:
Diol dehydratase-reactivating factor (preferred)
PDBe Complex ID:
PDB-CPX-130605 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Diol dehydratase-reactivating factor large subunit
Molecule details ›
Chains: A, C
Length: 610 amino acids
Theoretical weight: 64.33 KDa
Source organism: Klebsiella oxytoca
Expression system: Escherichia coli
UniProt:
Sequence domains:
Structure domains:
Length: 610 amino acids
Theoretical weight: 64.33 KDa
Source organism: Klebsiella oxytoca
Expression system: Escherichia coli
UniProt:
- Canonical:
O68195 (Residues: 1-610; Coverage: 100%)
Sequence domains:
Structure domains:
Diol dehydratase-reactivating factor small subunit
Molecule details ›
Chains: B, D
Length: 125 amino acids
Theoretical weight: 13.64 KDa
Source organism: Klebsiella oxytoca
Expression system: Escherichia coli
UniProt:
Sequence domains: Dehydratase medium subunit
Structure domains: B12-dependent dehydatase associated subunit
Length: 125 amino acids
Theoretical weight: 13.64 KDa
Source organism: Klebsiella oxytoca
Expression system: Escherichia coli
UniProt:
- Canonical: O68196 (Residues: 1-125; Coverage: 100%)
Sequence domains: Dehydratase medium subunit
Structure domains: B12-dependent dehydatase associated subunit
