| http://purl.uniprot.org/enzyme/1.1.5.5 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Enzyme |
| http://purl.uniprot.org/enzyme/1.1.5.5 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/1.1.-.- |
| http://purl.uniprot.org/enzyme/1.1.5.5 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/1.-.-.- |
| http://purl.uniprot.org/enzyme/1.1.5.5 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/1.1.5.- |
| http://purl.uniprot.org/enzyme/1.1.5.5 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/core/Enzyme |
| http://purl.uniprot.org/enzyme/1.1.5.5 | http://www.w3.org/2000/01/rdf-schema#comment | "Associated with membrane."xsd:string |
| http://purl.uniprot.org/enzyme/1.1.5.5 | http://www.w3.org/2000/01/rdf-schema#comment | "It is assayed with phenazine methosulfate or with ferricyanide."xsd:string |
| http://purl.uniprot.org/enzyme/1.1.5.5 | http://www.w3.org/2000/01/rdf-schema#comment | "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."xsd:string |
| http://purl.uniprot.org/enzyme/1.1.5.5 | http://www.w3.org/2000/01/rdf-schema#comment | "Electron acceptor is membrane ubiquinone."xsd:string |
| http://purl.uniprot.org/enzyme/1.1.5.5 | http://www.w3.org/2000/01/rdf-schema#comment | "It does not require amines for activation."xsd:string |
| http://purl.uniprot.org/enzyme/1.1.5.5 | http://www.w3.org/2000/01/rdf-schema#comment | "The enzyme has two additional subunits, one of which contains three molecules of heme c."xsd:string |
| http://purl.uniprot.org/enzyme/1.1.5.5 | http://www.w3.org/2000/01/rdf-schema#comment | "Only described in acetic acid bacteria where it is involved in acetic acid production."xsd:string |
| http://purl.uniprot.org/enzyme/1.1.5.5 | http://www.w3.org/2000/01/rdf-schema#comment | "It has a restricted substrate specificity, oxidizing a few primary alcohols (C2 to C6), but not methanol, secondary alcohols and some aldehydes."xsd:string |
| http://purl.uniprot.org/enzyme/1.1.5.5 | http://www.w3.org/2004/02/skos/core#prefLabel | "alcohol dehydrogenase (quinone)"xsd:string |
| http://purl.uniprot.org/enzyme/1.1.5.5 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/18838797 |
| http://purl.uniprot.org/enzyme/1.1.5.5 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/7772016 |
| http://purl.uniprot.org/enzyme/1.1.5.5 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/8617755 |
| http://purl.uniprot.org/enzyme/1.1.5.5 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/16233574 |
| http://purl.uniprot.org/enzyme/1.1.5.5 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/16636451 |
| http://purl.uniprot.org/enzyme/1.1.5.5 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/18321602 |
| http://purl.uniprot.org/enzyme/1.1.5.5 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/7942316 |
| http://purl.uniprot.org/enzyme/1.1.5.5 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/9526036 |
| http://purl.uniprot.org/enzyme/1.1.5.5 | http://www.w3.org/2004/02/skos/core#altLabel | "quinoprotein alcohol dehydrogenase"xsd:string |
| http://purl.uniprot.org/enzyme/1.1.5.5 | http://www.w3.org/2004/02/skos/core#altLabel | "pyrroloquinoline quinone-dependent alcohol dehydrogenase"xsd:string |
| http://purl.uniprot.org/enzyme/1.1.5.5 | http://www.w3.org/2004/02/skos/core#altLabel | "PQQ-dependent alcohol dehydrogenase"xsd:string |