Cloned (Comment) | Organism |
---|---|
sequence comparisons, phylogenetic tree | Gluconobacter oxydans |
sequence comparisons, phylogenetic tree | Acetobacter pasteurianus |
sequence comparisons, phylogenetic tree | Acidomonas methanolica |
sequence comparisons, phylogenetic tree | Gluconacetobacter polyoxogenes |
sequence comparisons, phylogenetic tree | Acetobacter aceti |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
membrane | - |
Gluconobacter oxydans | 16020 | - |
membrane | - |
Acetobacter pasteurianus | 16020 | - |
membrane | - |
Acidomonas methanolica | 16020 | - |
membrane | - |
Gluconacetobacter polyoxogenes | 16020 | - |
membrane | - |
Acetobacter aceti | 16020 | - |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Acetobacter pasteurianus | by the defect of type III ADH in Acetobacter pasteurianus SKU1108, the strain turns out to grow even better than the wild strain in ethanol containing medium, where two NAD-dependent ADHs, present in only a small amount in the wild-type strain, are dramatically increased in the cytoplasm, concomitant to the increase of the key enzyme activities in TCA and glyoxylate cycles | ? | - |
? | |
additional information | Acetobacter pasteurianus SKU1108 | by the defect of type III ADH in Acetobacter pasteurianus SKU1108, the strain turns out to grow even better than the wild strain in ethanol containing medium, where two NAD-dependent ADHs, present in only a small amount in the wild-type strain, are dramatically increased in the cytoplasm, concomitant to the increase of the key enzyme activities in TCA and glyoxylate cycles | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Acetobacter aceti | P18278 | - |
- |
Acetobacter pasteurianus | - |
- |
- |
Acetobacter pasteurianus SKU1108 | - |
- |
- |
Acidomonas methanolica | - |
- |
- |
Gluconacetobacter polyoxogenes | - |
- |
- |
Gluconobacter oxydans | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | the quinohemoprotein is able to oxidize alcohols, structure-function relationship, overview | Gluconobacter oxydans | ? | - |
? | |
additional information | the quinohemoprotein is able to oxidize alcohols, structure-function relationship, overview | Acetobacter pasteurianus | ? | - |
? | |
additional information | the quinohemoprotein is able to oxidize alcohols, structure-function relationship, overview | Acidomonas methanolica | ? | - |
? | |
additional information | the quinohemoprotein is able to oxidize alcohols, structure-function relationship, overview | Gluconacetobacter polyoxogenes | ? | - |
? | |
additional information | the quinohemoprotein is able to oxidize alcohols, structure-function relationship, overview | Acetobacter aceti | ? | - |
? | |
additional information | by the defect of type III ADH in Acetobacter pasteurianus SKU1108, the strain turns out to grow even better than the wild strain in ethanol containing medium, where two NAD-dependent ADHs, present in only a small amount in the wild-type strain, are dramatically increased in the cytoplasm, concomitant to the increase of the key enzyme activities in TCA and glyoxylate cycles | Acetobacter pasteurianus | ? | - |
? | |
additional information | the quinohemoprotein is able to oxidize alcohols, structure-function relationship, overview | Acetobacter pasteurianus SKU1108 | ? | - |
? | |
additional information | by the defect of type III ADH in Acetobacter pasteurianus SKU1108, the strain turns out to grow even better than the wild strain in ethanol containing medium, where two NAD-dependent ADHs, present in only a small amount in the wild-type strain, are dramatically increased in the cytoplasm, concomitant to the increase of the key enzyme activities in TCA and glyoxylate cycles | Acetobacter pasteurianus SKU1108 | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | structure-function relationship, overview | Gluconobacter oxydans |
More | structure-function relationship, overview | Acetobacter pasteurianus |
More | structure-function relationship, overview | Acidomonas methanolica |
More | structure-function relationship, overview | Gluconacetobacter polyoxogenes |
More | structure-function relationship, overview | Acetobacter aceti |
Synonyms | Comment | Organism |
---|---|---|
ADHIIB | - |
- |
ADHIIG | - |
- |
alcohol dehydrogenase | - |
- |
BOH | - |
- |
GLDH | - |
- |
glycerol dehydrogenase | - |
- |
lupanine hydroxylase (PQQ/heme c) | - |
- |
PEGDH | - |
- |
polyethyleneglycol dehydrogenase | - |
- |
polypropyleneglycol dehydrogenase | - |
- |
polyvinylalcohol dehydrogenase | - |
- |
PPGDH | - |
- |
PVADH | - |
- |
quinohemoprotein alcohol dehydrogenase | - |
Gluconobacter oxydans |
quinohemoprotein alcohol dehydrogenase | - |
Acetobacter pasteurianus |
quinohemoprotein alcohol dehydrogenase | - |
Acidomonas methanolica |
quinohemoprotein alcohol dehydrogenase | - |
Gluconacetobacter polyoxogenes |
quinohemoprotein alcohol dehydrogenase | - |
Acetobacter aceti |
quinoprotein ethanol dehydrogenase | - |
- |
tetrahydrofurfuryl alcohol dehydrogenase | - |
- |
THFADH | - |
- |
type I ADH (PQQ) | - |
- |
type II ADH | - |
- |
type II ADH (PQQ/heme c) | - |
- |
type III ADH (PQQ/heme c /3 hemes c) | - |
- |
vanillyl alcohol dehydrogenase | - |
- |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
heme c | type III ADH is a quinohemoprotein able to oxidize alcohols | Gluconobacter oxydans | |
heme c | type III ADH is a quinohemoprotein able to oxidize alcohols | Acetobacter pasteurianus | |
heme c | type III ADH is a quinohemoprotein able to oxidize alcohols | Acidomonas methanolica | |
heme c | type III ADH is a quinohemoprotein able to oxidize alcohols | Gluconacetobacter polyoxogenes | |
heme c | type III ADH is a quinohemoprotein able to oxidize alcohols | Acetobacter aceti | |
pyrroloquinoline quinone | PQQ, type III ADH is a quinohemoprotein able to oxidize alcohols, PQQ binding structure and electron transfer reaction, overview | Gluconobacter oxydans | |
pyrroloquinoline quinone | PQQ, type III ADH is a quinohemoprotein able to oxidize alcohols, PQQ binding structure and electron transfer reaction, overview | Acetobacter pasteurianus | |
pyrroloquinoline quinone | PQQ, type III ADH is a quinohemoprotein able to oxidize alcohols, PQQ binding structure and electron transfer reaction, overview | Acidomonas methanolica | |
pyrroloquinoline quinone | PQQ, type III ADH is a quinohemoprotein able to oxidize alcohols, PQQ binding structure and electron transfer reaction, overview | Gluconacetobacter polyoxogenes | |
pyrroloquinoline quinone | PQQ, type III ADH is a quinohemoprotein able to oxidize alcohols, PQQ binding structure and electron transfer reaction, overview | Acetobacter aceti |