| General Information |
| MoonProt ID | 302 |
| First appeared in release | 2.0 |
| Name(s) | aldehyde-alcohol dehydrogenase E, AdhE |
| UniProt ID | P0A9Q7 (ADHE_ECOLI) |
| GO terms | GO:0006066 alcohol metabolic process
GO:0006115 ethanol biosynthetic process
GO:0008152 metabolic process
GO:0015976 carbon utilization
GO:0055114 oxidation-reduction process
GO:0003824 catalytic activity
GO:0004022 alcohol dehydrogenase (NAD) activity
GO:0008774 acetaldehyde dehydrogenase (acetylating) activity
GO:0016491 oxidoreductase activity
GO:0016620 oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
GO:0042802 identical protein binding
GO:0046872 metal ion binding
GO:0005829 cytosol
GO:0016020 membrane |
| Organisms for which functions have been demonstrated | Escherichia coli (Gram negative bacterium) |
| Sequence length | 891 amino acids |
| FASTA sequence | >gi|26107972|gb|AAN80172.1|AE016760_31 Aldehyde-alcohol dehydrogenase [Escherichia coli CFT073]
MAVTNVAELNALVERVKKAQREYASFTQEQVDKIFRAAALAAADARIPLAKMAVAESGMGIVEDKVIKNHFASEYIYNAYKDEKTCGVLSEDDTFGTITIAEPIGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPRAKDATNKAADIVLQAAIAAGAPKDLIGWIDQPSVELSNALMHHPDINLILATGGPGMVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVASVLMSKTFDNGVICASEQSVVVVDSVYDAVRERFATHGGYLLQGKELKAVQDVILKNGALNAAIVGQPAYKIAELAGFSVPENTKILIGEVIVVDESEPFAHEKLSPTLAMYRAKDFEDAVEKAEKLVAMGGIGHTSCLYTDQDNQPARVSYFGQKMKTARILINTPASQGGIGDLYNFKLAPSLTLGCGSWGGNSISENVGPKHLINKKTVAKRAENMLWHKLPKSIYFRRGSLPIALDEVITDGHKRALIVTDRFLFNNGYADQITSVLKAAGVETEVFFEVEADPTLSIVRKGAELANSFKPDVIIALGGGSPMDAAKIMWVMYEHPETHFEELALRFMDIRKRIYKFPKMGVKAKMIAVTTTSGTGSEVTPFAVVTDDTTGQKYPLADYALTPDMAIVDANLVMDMPKSLCAFGGLDAVTHAMEAYVSVLASEFSDGQALQALKLLKEYLPASYHEGSKNPVARERVHSAATIAGIAFANAFLGVCHSMAHKLGSQFHIPHGLANALLICNVIRYNANDNPTKQTAFSQYDRPQ
ARRRYAEIADHLGLSAPGDRTAAKIEKLLAWLETLKAELGIPKSIREAGVQEADFLANVDKLSEDAFDDQCTGANPRYPLISELKQILLDTYYGRDYVEGETAAKKEAAPAKAEKKAKKSA |
| Structure Information |
| PDB ID | 6AHC |
| Quaternary structure | |
| SCOP | NA |
| CATH | 3.40.50.1970 |
| TM Helix Prediction | no TM helices |
| DisProt Annotation | Not in DisProt |
| Predicted Disorder Regions | 1-9, 870-891 |
| Connections to Disease |
| OMIM ID | |
| Function 1 |
| Function description | aldehyde alcohol dehydrogenase, alcohol dehydrogenase,
acetaldehyde-CoA dehydrogenase, and pyruvate formate-lyase (PFL) deactivase activities |
| References for function | Kessler D., Leibrecht I., Knappe J. Pyruvate-formate-lyase-deactivase and acetyl-CoA reductase activities of Escherichia coli reside on a polymeric protein particle encoded by adhE. FEBS Lett. 281:59-63(1991). PMID: 2015910 |
| E.C. number | |
| Location of functional site(s) | NAD binding region residues 422–427 |
| Cellular location of function | |
| Comments | |
| Function 2 |
| Function description | binds to ribosome and affects translation, RNA unwinding activity, RNA helicase |
| References for function | Shasmal M, Dey S, Shaikh TR, Bhakta S, Sengupta J. E. coli metabolic protein aldehyde-alcohol dehydrogenase-E binds to the ribosome: a unique moonlighting action revealed. Sci Rep. 2016 Jan 29;6:19936. doi: 10.1038/srep19936. PMID: 26822933 |
| E.C. number | |
| Location of functional site(s) | |
| Cellular location of function | cytoplasm, bound to ribosome proteins S3 and S10 |
| Comments | cryo-EM results suggest anchored at head of 30S subunit of ribosome, Shasmal and coworkers suggest: "ribosome-associated AdhE could be to promote local unwinding of some of the mRNAs with stable stem loop structure at the 3? end, ensuring its linear configuration at the entrance" |