Q9AF95 · BDH_THABB
- Protein1-butanol dehydrogenase (cytochrome c)
- Genebdh
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids691 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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).
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
- butan-1-ol + 2 Fe(III)-[cytochrome c] = butanal + 2 Fe(II)-[cytochrome c] + 2 H+
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 PQQ group per subunit.
Note: Binds 1 Ca2+ ion per subunit.
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 μM | 1-butanol | |||||
535 μM | butyraldehyde |
pH Dependence
Optimum pH is 8.
Temperature Dependence
Optimum temperature is 60 degrees Celsius.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 84 | pyrroloquinoline quinone (UniProtKB | ChEBI) | |||
Binding site | 136 | pyrroloquinoline quinone (UniProtKB | ChEBI) | |||
Binding site | 181 | pyrroloquinoline quinone (UniProtKB | ChEBI) | |||
Binding site | 197-198 | pyrroloquinoline quinone (UniProtKB | ChEBI) | |||
Binding site | 199 | Ca2+ (UniProtKB | ChEBI) | |||
Active site | 322 | Proton acceptor | |||
Binding site | 322 | Ca2+ (UniProtKB | ChEBI) | |||
Binding site | 349 | pyrroloquinoline quinone (UniProtKB | ChEBI) | |||
Binding site | 408-409 | pyrroloquinoline quinone (UniProtKB | ChEBI) | |||
Binding site | 558 | pyrroloquinoline quinone (UniProtKB | ChEBI) | |||
Binding site | 618 | heme c (UniProtKB | ChEBI); covalent | |||
Binding site | 621 | heme c (UniProtKB | ChEBI); covalent | |||
Binding site | 622 | Fe (UniProtKB | ChEBI) of heme c (UniProtKB | ChEBI); axial binding residue | |||
Binding site | 661 | Fe (UniProtKB | ChEBI) of heme c (UniProtKB | ChEBI); axial binding residue | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | membrane | |
Cellular Component | periplasmic space | |
Molecular Function | calcium ion binding | |
Molecular Function | electron transfer activity | |
Molecular Function | heme binding | |
Molecular Function | oxidoreductase activity, acting on CH-OH group of donors |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name1-butanol dehydrogenase (cytochrome c)
- EC number
- Short namesBDH
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Betaproteobacteria > Rhodocyclales > Zoogloeaceae > Thauera
Accessions
- Primary accessionQ9AF95
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain, disulfide bond.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Signal | 1-38 | ||||
Chain | PRO_0000442915 | 39-691 | 1-butanol dehydrogenase (cytochrome c) | ||
Disulfide bond | 130↔131 | ||||
Keywords
- PTM
Expression
Induction
By butane and 1-butanol.
Interaction
Subunit
Monomer.
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length691
- Mass (Da)75,071
- Last updated2001-12-01 v2
- Checksum4FC7FD20CDA14E64
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF355798 EMBL· GenBank· DDBJ | AAK27220.2 EMBL· GenBank· DDBJ | Genomic DNA |