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Information on EC 1.1.5.5 - alcohol dehydrogenase (quinone) and Organism(s) Acetobacter aceti and UniProt Accession P18278

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EC Tree
IUBMB Comments
Only described in acetic acid bacteria where it is involved in acetic acid production. Associated with membrane. Electron acceptor is membrane ubiquinone. A model structure suggests that, like all other quinoprotein alcohol dehydrogenases, the catalytic subunit has an 8-bladed 'propeller' structure, a calcium ion bound to the PQQ in the active site and an unusual disulfide ring structure in close proximity to the PQQ; the catalytic subunit also has a heme c in the C-terminal domain. The enzyme has two additional subunits, one of which contains three molecules of heme c. It does not require amines for activation. It has a restricted substrate specificity, oxidizing a few primary alcohols (C2 to C6), but not methanol, secondary alcohols and some aldehydes. It is assayed with phenazine methosulfate or with ferricyanide.
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Acetobacter aceti
UNIPROT: P18278
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The taxonomic range for the selected organisms is: Acetobacter aceti
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
membrane-bound alcohol dehydrogenase, pqq-adh, quinoprotein ethanol dehydrogenase, quinoprotein alcohol dehydrogenase, quinoprotein methanol dehydrogenase, quinohemoprotein alcohol dehydrogenase, qh-adh, adh-iig, adh-iib, ppg-dh, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PQQ–alcohol dehydrogenase
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pyrroloquinoline quinone–alcohol dehydrogenase
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quinohaemoprotein alcohol dehydrogenase
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quinohemoprotein alcohol dehydrogenase
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PQQ alcohol dehydrogenase
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-
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quinohemoprotein ethanol dehydrogenase
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-
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quinone dependent alcohol dehydrogenase
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-
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quinoprotein ADH
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-
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quinoprotein ethanol dehydrogenase
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quinoprotein methanol dehydrogenase
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SYSTEMATIC NAME
IUBMB Comments
alcohol:quinone oxidoreductase
Only described in acetic acid bacteria where it is involved in acetic acid production. Associated with membrane. Electron acceptor is membrane ubiquinone. A model structure suggests that, like all other quinoprotein alcohol dehydrogenases, the catalytic subunit has an 8-bladed 'propeller' structure, a calcium ion bound to the PQQ in the active site and an unusual disulfide ring structure in close proximity to the PQQ; the catalytic subunit also has a heme c in the C-terminal domain. The enzyme has two additional subunits, one of which contains three molecules of heme c. It does not require amines for activation. It has a restricted substrate specificity, oxidizing a few primary alcohols (C2 to C6), but not methanol, secondary alcohols and some aldehydes. It is assayed with phenazine methosulfate or with ferricyanide.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
heme c
pyrroloquinoline quinone
additional information
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
a heme protein
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ADHA_ACEAC
742
1
81521
Swiss-Prot
-
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
structure-function relationship, overview
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
sequence comparisons, phylogenetic tree
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
adhA expression is related to the ability to oxidize and grow on ethanol. Differential expression of pyrroloquinoline quinone–alcohol dehydrogenase could be a marker to analyse both growth and oxidation ability in some acetic acid bacteria, especially those of the genus Acetobacter
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Toyama, H.; Mathews, F.S.; Adachi, O.; Matsushita, K.
Quinohemoprotein alcohol dehydrogenases: structure, function, and physiology
Arch. Biochem. Biophys.
428
10-21
2004
Acetobacter aceti (P18278), Acetobacter pasteurianus, Acetobacter pasteurianus SKU1108, Acidomonas methanolica, Gluconacetobacter polyoxogenes, Gluconobacter oxydans
Manually annotated by BRENDA team
Cozier, G.E.; Giles, I.G.; Anthony, C.
The structure of the quinoprotein alcohol dehydrogenase of Acetobacter aceti modelled on that of methanol dehydrogenase from Methylobacterium extorquens
Biochem. J.
308
375-379
1995
Acetobacter aceti (P18278), Acetobacter aceti
Manually annotated by BRENDA team
Quintero, Y.; Poblet, M.; Guillamon, J.M.; Mas, A.
Quantification of the expression of reference and alcohol dehydrogenase genes of some acetic acid bacteria in different growth conditions
J. Appl. Microbiol.
106
666-674
2009
Acetobacter aceti (P18278), Acetobacter pasteurianus
Manually annotated by BRENDA team