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btuD vitamin B12 ABC transporter ATP binding subunit [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 945751, updated on 4-Feb-2026
Official Symbol
btuD
Official Full Name
vitamin B12 ABC transporter ATP binding subunit
Primary source
ECOCYC:EG10128
Locus tag
b1709
See related
ASAP:ABE-0005707
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
Lineage
Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia
Also known as
ECK1707
Summary
BtuD is the ATP-binding component of the BtuCD, an ABC-type vitamin B12 uptake system. [More information is available at EcoCyc: EG10128].
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Sequence:
NC_000913.3 (1792809..1793558, complement)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene anti-FlhDC factor RflP Neighboring gene NlpC/P60 family lipoprotein NlpC Neighboring gene thioredoxin/glutathione peroxidase BtuE Neighboring gene vitamin B12 ABC transporter membrane subunit

Genomic Sequence:
NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Related articles in PubMed

  1. ATP Hydrolysis Induced Conformational Changes in the Vitamin B12 Transporter BtuCD Revealed by MD Simulations. Pan C, et al. PLoS One, 2016. PMID 27870912, Free PMC Article
  2. Transport of vitamin B12 in Escherichia coli: cloning of the btuCD region. DeVeaux LC, et al. J Bacteriol, 1985 Jun. PMID 2987192, Free PMC Article
  3. Structural biology. Not just another ABC transporter. Davidson AL. Science, 2002 May 10. PMID 12004108
  4. The structure and function of drug pumps: an update. McKeegan KS, et al. Trends Microbiol, 2003 Jan. PMID 12526851
  5. Conformational transitions induced by the binding of MgATP to the vitamin B12 ATP-binding cassette (ABC) transporter BtuCD. Oloo EO, et al. J Biol Chem, 2004 Oct 22. PMID 15308647

See all (36) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. The periplasmic soluble binding protein BtuF binds the vitamin B12 and the transmembrane and ATPase domains BtuCD mediate the translocation.
    Title: Single-molecule visualization of conformational changes and substrate transport in the vitamin B(12) ABC importer BtuCD-F.
  2. study used molecular dynamics simulations to investigate the atomic-level mechanism of conformational coupling in the ABC transporter BtuCD-F
    Title: Release of Entropic Spring Reveals Conformational Coupling Mechanism in the ABC Transporter BtuCD-F.
  3. ATP Hydrolysis Induced Conformational Changes in the Vitamin B12 Transporter BtuCD Revealed by MD Simulations
    Title: ATP Hydrolysis Induced Conformational Changes in the Vitamin B12 Transporter BtuCD Revealed by MD Simulations.
  4. Data suggest that the asymmetric crystal structure of BtuCD-F is an intermediate state in the process of reverse inward-facing to outward-facing (I-->O) transition.
    Title: The conformational transition pathways of ATP-binding cassette transporter BtuCD revealed by targeted molecular dynamics simulation.
  5. Data suggest that BtuF does not discriminate between, or impose, asymmetric conformations of BtuC/BtuD complex. Data confirm conformational disorder observed in BtuC/BtuD/BtuF crystals.
    Title: Asymmetric states of vitamin B₁₂ transporter BtuCD are not discriminated by its cognate substrate binding protein BtuF.
  6. Data provide insights into the subunit interactions of an ABC transporter and lays the foundation for studies of the reassembly of BtuCD.
    Title: Unravelling the folding and stability of an ABC (ATP-binding cassette) transporter.
  7. ATP-binding cassette transporter BtuCD mediating vitamin B(12) uptake in Escherichia coli couples the energy of ATP hydrolysis to the translocation of vitamin B(12) across the membrane into the cell.
    Title: The conformational coupling and translocation mechanism of vitamin B12 ATP-binding cassette transporter BtuCD.
  8. The 2.6 angstrom crystal structure of a complex BtuCD-F reveals substantial conformational changes as compared with the previously reported structures of BtuCD and BtuF
    Title: Asymmetry in the structure of the ABC transporter-binding protein complex BtuCD-BtuF.
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Products Interactant Other Gene Complex Source Pubs Description

Homology

Gene Ontology Provided by EcoCyc

Function Evidence Code Pubs
enables ABC-type vitamin B12 transporter activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables ABC-type vitamin B12 transporter activity IEA
Inferred from Electronic Annotation
more info
  
enables ATP binding IEA
Inferred from Electronic Annotation
more info
  
enables ATP binding ISM
Inferred from Sequence Model
more info
 PubMed 
enables ATP binding RCA
inferred from Reviewed Computational Analysis
more info
 PubMed 
enables ATP hydrolysis activity IEA
Inferred from Electronic Annotation
more info
  
enables ATPase-coupled transmembrane transporter activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables nucleotide binding IEA
Inferred from Electronic Annotation
more info
  
enables protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
Process Evidence Code Pubs
acts_upstream_of_or_within cobalamin transport IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in cobalamin transport IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in cobalamin transport IEA
Inferred from Electronic Annotation
more info
  
involved_in transmembrane transport IEA
Inferred from Electronic Annotation
more info
  
Component Evidence Code Pubs
part_of ATP-binding cassette (ABC) transporter complex IBA
Inferred from Biological aspect of Ancestor
more info
  
part_of ATP-binding cassette (ABC) transporter complex IDA
Inferred from Direct Assay
more info
 PubMed 
located_in extrinsic component of membrane IDA
Inferred from Direct Assay
more info
 PubMed 
located_in membrane IDA
Inferred from Direct Assay
more info
 PubMed 
located_in plasma membrane IEA
Inferred from Electronic Annotation
more info
  
Preferred Names
vitamin B12 ABC transporter ATP binding subunit
NP_416224.1

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

  1. NC_000913.3 Reference assembly

    Range
    1792809..1793558 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_416224.1 vitamin B12 ABC transporter ATP binding subunit

    See identical proteins and their annotated locations for NP_416224.1

    Status: REVIEWED

    UniProtKB/TrEMBL
    A0A376KWZ5, A0A403CSX7
    Conserved Domains (1) summary
    COG4138
    Location:2 → 249
    BtuD; ABC-type cobalamin transport system, ATPase component [Coenzyme transport and metabolism]
Nucleotide Protein
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