Function and Biology Details
Reaction catalysed:
ATP + H(2)O + vitamin B12-[cobalamin-binding protein](Side 1) = ADP + phosphate + vitamin B12(Side 2) + [cobalamin-binding protein](Side 1)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- P-loop containing nucleoside triphosphate hydrolase
- ABC transporter-like, ATP-binding domain
- ABC transporter, permease protein, BtuC-like
- ABC transporter, BtuC-like
- ABC transporter-like, conserved site
- AAA+ ATPase domain
- ABC transporter, vitamin B12, BtuD
- ABC transporter, vitamin B12 import, permease protein BtuC
Structure analysis Details
Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139092 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Vitamin B12 import system permease protein BtuC
Molecule details ›
Chains: A, B
Length: 326 amino acids
Theoretical weight: 35.49 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
Sequence domains: FecCD transport family
Structure domains: ABC transporter involved in vitamin B12 uptake, BtuC
Length: 326 amino acids
Theoretical weight: 35.49 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
- Canonical:
P06609 (Residues: 1-326; Coverage: 100%)
Sequence domains: FecCD transport family
Structure domains: ABC transporter involved in vitamin B12 uptake, BtuC
Vitamin B12 import ATP-binding protein BtuD
Molecule details ›
Chains: C, D
Length: 249 amino acids
Theoretical weight: 27.54 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
Sequence domains: ABC transporter
Structure domains: P-loop containing nucleotide triphosphate hydrolases
Length: 249 amino acids
Theoretical weight: 27.54 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
- Canonical: P06611 (Residues: 1-249; Coverage: 100%)
Sequence domains: ABC transporter
Structure domains: P-loop containing nucleotide triphosphate hydrolases
