| P0A9Q7 |
| UniProt ID : |
P0A9Q7 |
| NCBI Taxonomy : |
83333 |
| Protein names : |
Aldehyde-alcohol dehydrogenase |
| Organism : |
Escherichia coli (strain K12) |
| Taxonomy : |
Bacteria |
| Length : |
891 |
| Gene Ontology : | | GO ID | Ontology | Definition | Evidence | | GO:0005829 | Cellular Component | cytosol | IDA | | GO:0016020 | Cellular Component | membrane | IDA | | GO:0008774 | Molecullar Function | acetaldehyde dehydrogenase (acetylating) activity | IMP | | GO:0004022 | Molecullar Function | alcohol dehydrogenase (NAD) activity | IMP | | GO:0046872 | Molecullar Function | metal ion binding | IEA | | GO:0015976 | Biological Process | carbon utilization | IEA | | GO:0006115 | Biological Process | ethanol biosynthetic process | IDA | |
| Catalytic activity : | An alcohol + NAD+ = an aldehyde or ketone + NADH.Acetaldehyde + CoA + NAD+ = acetyl-CoA + NADH.Iron. |
| SWISS-MODEL Repository : | P0A9Q7 |
| Sequences : |
MAVTNVAELNALVERVKKAQREYASFTQEQVDKIFRAAALAAADARIPLAKMAVAESGMGIVEDKVIKNHFASEYIYNAYKDEKTCGVLSEDDTFGTITIAEPIGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPRAKDATNKAADIVLQAAIAAGAPKDLIGWIDQPSVELSNALMHHPDINLILATGGPGMVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVASVLMSKTFDNGVICASEQSVVVVDSVYDAVRERFATHGGYLLQGKELKAVQDVILKNGALNAAIVGQPAYKIAELAGFSVPENTKILIGEVTVVDESEPFAHEKLSPTLAMYRAKDFEDAVEKAEKLVAMGGIGHTSCLYTDQDNQPARVSYFGQKMKTARILINTPASQGGIGDLYNFKLAPSLTLGCGSWGGNSISENVGPKHLINKKTVAKRAENMLWHKLPKSIYFRRGSLPIALDEVITDGHKRALIVTDRFLFNNGYADQITSVLKAAGVETEVFFEVEADPTLSIVRKGAELANSFKPDVIIALGGGSPMDAAKIMWVMYEHPETHFEELALRFMDIRKRIYKFPKMGVKAKMIAVTTTSGTGSEVTPFAVVTDDATGQKYPLADYALTPDMAIVDANLVMDMPKSLCAFGGLDAVTHAMEAYVSVLASEFSDGQALQALKLLKEYLPASYHEGSKNPVARERVHSAATIAGIAFANAFLGVCHSMAHKLGSQFHIPHGLANALLICNVIRYNANDNPTKQTAFSQYDRPQARRRYAEIADHLGLSAPGDRTAAKIEKLLAWLETLKAELGIPKSIREAGVQEADFLANVDKLSEDAFDDQCTGANPRYPLISELKQILLDTYYGRDYVEGETAAKKEAAPAKAEKKAKKSA |
| Function : | This enzyme has three activities: ADH, ACDH, and PFL-deactivase. In aerobic conditions it acts as a hydrogen peroxide scavenger. The PFL deactivase activity catalyzes the quenching of the pyruvate-formate-lyase catalyst in an iron, NAD, and CoA dependent reaction. |