Protein Information

General Information
MoonProt ID302
First appeared in release2.0
Name(s)aldehyde-alcohol dehydrogenase E, AdhE
UniProt IDP0A9Q7 (ADHE_ECOLI)
GO termsGO: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 GO:0006412 translation GO:0003724 RNA helicase
Organisms for which functions have been demonstratedE. coli
Sequence length891 amino acids
FASTA sequence>gi|26107972|gb|AAN80172.1|AE016760_31 Aldehyde-alcohol dehydrogenase [Escherichia coli CFT073] MAVTNVAELNALVERVKKAQREYASFTQEQVDKIFRAAALAAADARIPLAKMAVAESGMGIVEDKVIKNHFASEYIYNAYKDEKTCGVLSEDDTFGTITIAEPIGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPRAKDATNKAADIVLQAAIAAGAPKDLIGWIDQPSVELSNALMHHPDINLILATGGPGMVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVASVLMSKTFDNGVICASEQSVVVVDSVYDAVRERFATHGGYLLQGKELKAVQDVILKNGALNAAIVGQPAYKIAELAGFSVPENTKILIGEVIVVDESEPFAHEKLSPTLAMYRAKDFEDAVEKAEKLVAMGGIGHTSCLYTDQDNQPARVSYFGQKMKTARILINTPASQGGIGDLYNFKLAPSLTLGCGSWGGNSISENVGPKHLINKKTVAKRAENMLWHKLPKSIYFRRGSLPIALDEVITDGHKRALIVTDRFLFNNGYADQITSVLKAAGVETEVFFEVEADPTLSIVRKGAELANSFKPDVIIALGGGSPMDAAKIMWVMYEHPETHFEELALRFMDIRKRIYKFPKMGVKAKMIAVTTTSGTGSEVTPFAVVTDDTTGQKYPLADYALTPDMAIVDANLVMDMPKSLCAFGGLDAVTHAMEAYVSVLASEFSDGQALQALKLLKEYLPASYHEGSKNPVARERVHSAATIAGIAFANAFLGVCHSMAHKLGSQFHIPHGLANALLICNVIRYNANDNPTKQTAFSQYDRPQ ARRRYAEIADHLGLSAPGDRTAAKIEKLLAWLETLKAELGIPKSIREAGVQEADFLANVDKLSEDAFDDQCTGANPRYPLISELKQILLDTYYGRDYVEGETAAKKEAAPAKAEKKAKKSA
Structure Information
PDB ID
Quaternary structure
Function 1
Function descriptionaldehyde alcohol dehydrogenase, alcohol dehydrogenase, acetaldehyde-CoA dehydrogenase, and pyruvate formate-lyase (PFL) deactivase activities
References for functionKessler 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)active site: 246; nucleotide binding: 422-427
Cellular location of function
Comments
Function 2
Function descriptionbinds to ribosome and affects translation, RNA unwinding activity, RNA helicase
References for functionShasmal 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 functioncytoplasm, bound to ribosome proteins S3 and S10
Commentscryo-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"