Q9AF95 · BDH_THABB

Function

function

Involved in the metabolism of butane (PubMed:11889098).
Could be important in the detoxification of 1-butanol (PubMed:12142403).
Catalyzes the oxidation of 1-butanol to butyraldehyde (PubMed:11238982, PubMed:12142403).
Also able to use 1-propanol, 2-pentanol, propionaldehyde and butyraldehyde as substrates (PubMed:11238982).

Catalytic activity

Cofactor

Protein has several cofactor binding sites:
pyrroloquinoline quinone (UniProtKB | Rhea| CHEBI:58442 )

Note: Binds 1 PQQ group per subunit.
Ca2+ (UniProtKB | Rhea| CHEBI:29108 )

Note: Binds 1 Ca2+ ion per subunit.
heme c (UniProtKB | Rhea| CHEBI:61717 )

Note: Binds 1 heme c group per subunit.

Activity regulation

Dehydrogenase activity is increased by ammonium ions.

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
7 μM1-butanol
535 μMbutyraldehyde

pH Dependence

Optimum pH is 8.

Temperature Dependence

Optimum temperature is 60 degrees Celsius.

Features

Showing features for binding site, active site.

Type
IDPosition(s)Description
Binding site84pyrroloquinoline quinone (UniProtKB | ChEBI)
Binding site136pyrroloquinoline quinone (UniProtKB | ChEBI)
Binding site181pyrroloquinoline quinone (UniProtKB | ChEBI)
Binding site197-198pyrroloquinoline quinone (UniProtKB | ChEBI)
Binding site199Ca2+ (UniProtKB | ChEBI)
Active site322Proton acceptor
Binding site322Ca2+ (UniProtKB | ChEBI)
Binding site349pyrroloquinoline quinone (UniProtKB | ChEBI)
Binding site408-409pyrroloquinoline quinone (UniProtKB | ChEBI)
Binding site558pyrroloquinoline quinone (UniProtKB | ChEBI)
Binding site618heme c (UniProtKB | ChEBI); covalent
Binding site621heme c (UniProtKB | ChEBI); covalent
Binding site622Fe (UniProtKB | ChEBI) of heme c (UniProtKB | ChEBI); axial binding residue
Binding site661Fe (UniProtKB | ChEBI) of heme c (UniProtKB | ChEBI); axial binding residue

GO annotations

AspectTerm
Cellular Componentmembrane
Cellular Componentperiplasmic space
Molecular Functioncalcium ion binding
Molecular Functionelectron transfer activity
Molecular Functionheme binding
Molecular Functionoxidoreductase activity, acting on CH-OH group of donors

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    1-butanol dehydrogenase (cytochrome c)
  • EC number
  • Short names
    BDH
  • Alternative names
    • NAD-independent 1-butanol dehydrogenase
    • PQQ-containing alcohol dehydrogenase
    • Quinohemoprotein

Gene names

    • Name
      bdh

Organism names

Accessions

  • Primary accession
    Q9AF95

Subcellular Location

Keywords

Phenotypes & Variants

Disruption phenotype

Cells lacking this gene show a delayed growth on butane and are unable to tolerate high level of 1-butanol (PubMed:11889098, PubMed:12142403).
When both bdh and boh genes are inactivated, growth on butane and 1-butanol is eliminated (PubMed:11889098).

PTM/Processing

Features

Showing features for signal, chain, disulfide bond.

Type
IDPosition(s)Description
Signal1-38
ChainPRO_000044291539-6911-butanol dehydrogenase (cytochrome c)
Disulfide bond130↔131

Keywords

Expression

Induction

By butane and 1-butanol.

Interaction

Subunit

Monomer.

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain605-684Cytochrome c

Sequence similarities

Belongs to the bacterial PQQ dehydrogenase family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    691
  • Mass (Da)
    75,071
  • Last updated
    2001-12-01 v2
  • Checksum
    4FC7FD20CDA14E64
MLTTTFARKREESVPLRKGIQRALLGLSCLVLSTTSFAAGGEWRTHGYDDAGTRYSPLAQITPDNAKELGLVWSYDLESSRGVEATPIVVDGVMYVTAPWSVVHALDVRSGKRLWTYDPEVPREKGKNACCDVVNRGVAVHEGKVFVGSLDGRLVAIDARTGKRVWERNTLIDDDKPYTITGAPRVIKGKVVIGNGGAEFGVRGYITAYDPTAASRPGVVPGPGDPSLPFEDASMEAAAKTWDPAGQVLGSGRRRHGVELDGLYRKAGFCCTSAPATPSPWSHRKRSPAGGDNLYTASIVALRPDTGEYVWHYQQTPADNWDYTSTQDLILADIELGGKPRKVILHAPKNGFFFVIDRTDGKFISAQNFVPVNWATGYDENGRPIENPEGAWPGHLSMRFPAPSARTNWHSMSYSPQTGLAYFPAQNIPLVLQEDKNWSYNQAQPGQAMAGIGWNLGMLVNPRPPASQPFGRLIAWDPVQQKEVWRKEHVSPWNGGTLVTAGNVVFQGTADARLLAFDARDGKELWSAPMGTGVIAAPVTYEVDGKQYVSIAVGWGGVYGNFTRASERRTPGTVYTFALGGKAEMPAFTEYQLNNLVSGVDYNPDDVAEGTGLYVTNCVFCHGVPGVDKGGGIPNLGYSTAETIAHLDQFVFKGPFMPRGMPDFTGKLTPEQVEKIKAFILGTADAVRPKK

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF355798
EMBL· GenBank· DDBJ
AAK27220.2
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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