Aldehyde-alcohol dehydrogenase (P0A9Q7)

Identification
Name:Aldehyde-alcohol dehydrogenase
Synonyms:
  • Alcohol dehydrogenase
  • ADH
  • Acetaldehyde dehydrogenase [acetylating]
  • ACDH
  • Pyruvate-formate-lyase deactivase
  • PFL deactivase
Gene Name:adhE
Enzyme Class:
Biological Properties
General Function:Involved in oxidoreductase activity
Specific 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
Cellular Location:Not Available
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0Acetaldehyde + 1.0Coenzyme A + 1.0NAD ↔ 1.0Acetyl-CoA + 1.0Hydrogen ion + 1.0NADH
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0Ethanol + 1.0NAD ↔ 1.0Acetaldehyde + 1.0Hydrogen ion + 1.0NADH
ReactionCard
1.0Primary alcohol+1.0Thumb ↔ 1.0Aldehyde+1.0Thumb+1.0Thumb
1.0Primary alcohol + 1.0NAD ↔ 1.0Aldehyde + 1.0NADH + 1.0Hydrogen ion
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Butanoyl-CoA+1.0Thumb+1.0Thumb
1.0Butanal + 1.0Coenzyme A + 1.0NAD ↔ 1.0Butanoyl-CoA + 1.0NADH + 1.0Hydrogen ion
ReactionCard
1.0trans-3-Chloro-2-propene-1-ol+1.0Thumb ↔ 1.0trans-3-Chloroallyl aldehyde+1.0Thumb+1.0Thumb
1.0trans-3-Chloro-2-propene-1-ol + 1.0NAD ↔ 1.0trans-3-Chloroallyl aldehyde + 1.0NADH + 1.0Hydrogen ion
ReactionCard
1.0cis-3-Chloro-2-propene-1-ol+1.0Thumb ↔ 1.0cis-3-Chloroallyl aldehyde+1.0Thumb+1.0Thumb
1.0cis-3-Chloro-2-propene-1-ol + 1.0NAD ↔ 1.0cis-3-Chloroallyl aldehyde + 1.0NADH + 1.0Hydrogen ion
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0(2-Naphthyl)methanol + 1.0NAD ↔ 1.02-Naphthaldehyde + 1.0NADH + 1.0Hydrogen ion
ReactionCard
1.0Primary alcohol+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0Primary alcohol + 1.0NAD + 1.0Secondary alcohol ↔ 1.0Aldehyde + 1.0NADH + 1.0Hydrogen ion + 1.0Ketone
ReactionCard
SMPDB Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0(2-Naphthyl)methanol + 1.0NAD → 1.02-Naphthaldehyde + 1.0Hydrogen ion + 1.0NADH
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0Acetaldehyde + 1.0Coenzyme A + 1.0NAD ↔ 1.0Acetyl-CoA + 1.0Hydrogen ion + 1.0NADH
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0Ethanol + 1.0NAD ↔ 1.0Acetaldehyde + 1.0Hydrogen ion + 1.0NADH
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB20007(2-Naphthyl)methanolMetaboCard
ECMDB200211-HydroxymethylnaphthaleneMetaboCard
ECMDB200472-NaphthaldehydeMetaboCard
ECMDB003183,4-DihydroxyphenylglycolMetaboCard
ECMDB00990AcetaldehydeMetaboCard
ECMDB01206Acetyl-CoAMetaboCard
ECMDB21646AldehydeMetaboCard
ECMDB03543ButanalMetaboCard
ECMDB01088Butyryl-CoAMetaboCard
ECMDB01423Coenzyme AMetaboCard
ECMDB00108EthanolMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB00902NADMetaboCard
ECMDB01487NADHMetaboCard
GO Classification:
Function
acetaldehyde dehydrogenase (acetylating) activity
alcohol dehydrogenase (NAD) activity
binding
catalytic activity
cation binding
ion binding
metal ion binding
oxidoreductase activity
oxidoreductase activity, acting on CH-OH group of donors
oxidoreductase activity, acting on the aldehyde or oxo group of donors
oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
Process
alcohol metabolic process
carbon utilization
metabolic process
oxidation reduction
small molecule metabolic process
Gene Properties
Blattner:b1241
Gene OrientationCounterclockwise
Centisome Percentage:27.90
Left Sequence End1294669
Right Sequence End1297344
Gene Sequence:
>2676 bp
ATGGCTGTTACTAATGTCGCTGAACTTAACGCACTCGTAGAGCGTGTAAAAAAAGCCCAG
CGTGAATATGCCAGTTTCACTCAAGAGCAAGTAGACAAAATCTTCCGCGCCGCCGCTCTG
GCTGCTGCAGATGCTCGAATCCCACTCGCGAAAATGGCCGTTGCCGAATCCGGCATGGGT
ATCGTCGAAGATAAAGTGATCAAAAACCACTTTGCTTCTGAATATATCTACAACGCCTAT
AAAGATGAAAAAACCTGTGGTGTTCTGTCTGAAGACGACACTTTTGGTACCATCACTATC
GCTGAACCAATCGGTATTATTTGCGGTATCGTTCCGACCACTAACCCGACTTCAACTGCT
ATCTTCAAATCGCTGATCAGTCTGAAGACCCGTAACGCCATTATCTTCTCCCCGCACCCG
CGTGCAAAAGATGCCACCAACAAAGCGGCTGATATCGTTCTGCAGGCTGCTATCGCTGCC
GGTGCTCCGAAAGATCTGATCGGCTGGATCGATCAACCTTCTGTTGAACTGTCTAACGCA
CTGATGCACCACCCAGACATCAACCTGATCCTCGCGACTGGTGGTCCGGGCATGGTTAAA
GCCGCATACAGCTCCGGTAAACCAGCTATCGGTGTAGGCGCGGGCAACACTCCAGTTGTT
ATCGATGAAACTGCTGATATCAAACGTGCAGTTGCATCTGTACTGATGTCCAAAACCTTC
GACAACGGCGTAATCTGTGCTTCTGAACAGTCTGTTGTTGTTGTTGACTCTGTTTATGAC
GCTGTACGTGAACGTTTTGCAACCCACGGCGGCTATCTGTTGCAGGGTAAAGAGCTGAAA
GCTGTTCAGGATGTTATCCTGAAAAACGGTGCGCTGAACGCGGCTATCGTTGGTCAGCCA
GCCTATAAAATTGCTGAACTGGCAGGCTTCTCTGTACCAGAAAACACCAAGATTCTGATC
GGTGAAGTGACCGTTGTTGATGAAAGCGAACCGTTCGCACATGAAAAACTGTCCCCGACT
CTGGCAATGTACCGCGCTAAAGATTTCGAAGACGCGGTAGAAAAAGCAGAGAAACTGGTT
GCTATGGGCGGTATCGGTCATACCTCTTGCCTGTACACTGACCAGGATAACCAACCGGCT
CGCGTTTCTTACTTCGGTCAGAAAATGAAAACGGCGCGTATCCTGATTAACACCCCAGCG
TCTCAGGGTGGTATCGGTGACCTGTATAACTTCAAACTCGCACCTTCCCTGACTCTGGGT
TGTGGTTCTTGGGGTGGTAACTCCATCTCTGAAAACGTTGGTCCGAAACACCTGATCAAC
AAGAAAACCGTTGCTAAGCGAGCTGAAAACATGTTGTGGCACAAACTTCCGAAATCTATC
TACTTCCGCCGTGGCTCCCTGCCAATCGCGCTGGATGAAGTGATTACTGATGGCCACAAA
CGTGCGCTCATCGTGACTGACCGCTTCCTGTTCAACAATGGTTATGCTGATCAGATCACT
TCCGTACTGAAAGCAGCAGGCGTTGAAACTGAAGTCTTCTTCGAAGTAGAAGCGGACCCG
ACCCTGAGCATCGTTCGTAAAGGTGCAGAACTGGCAAACTCCTTCAAACCAGACGTGATT
ATCGCGCTGGGTGGTGGTTCCCCGATGGACGCCGCGAAGATCATGTGGGTTATGTACGAA
CATCCGGAAACTCACTTCGAAGAGCTGGCGCTGCGCTTTATGGATATCCGTAAACGTATC
TACAAGTTCCCGAAAATGGGCGTGAAAGCGAAAATGATCGCTGTCACCACCACTTCTGGT
ACAGGTTCTGAAGTCACTCCGTTTGCGGTTGTAACTGACGACGCTACTGGTCAGAAATAT
CCGCTGGCAGACTATGCGCTGACTCCGGATATGGCGATTGTCGACGCCAACCTGGTTATG
GACATGCCGAAGTCCCTGTGTGCTTTCGGTGGTCTGGACGCAGTAACTCACGCCATGGAA
GCTTATGTTTCTGTACTGGCATCTGAGTTCTCTGATGGTCAGGCTCTGCAGGCACTGAAA
CTGCTGAAAGAATATCTGCCAGCGTCCTACCACGAAGGGTCTAAAAATCCGGTAGCGCGT
GAACGTGTTCACAGTGCAGCGACTATCGCGGGTATCGCGTTTGCGAACGCCTTCCTGGGT
GTATGTCACTCAATGGCGCACAAACTGGGTTCCCAGTTCCATATTCCGCACGGTCTGGCA
AACGCCCTGCTGATTTGTAACGTTATTCGCTACAATGCGAACGACAACCCGACCAAGCAG
ACTGCATTCAGCCAGTATGACCGTCCGCAGGCTCGCCGTCGTTATGCTGAAATTGCCGAC
CACTTGGGTCTGAGCGCACCGGGCGACCGTACTGCTGCTAAGATCGAGAAACTGCTGGCA
TGGCTGGAAACGCTGAAAGCTGAACTGGGTATTCCGAAATCTATCCGTGAAGCTGGCGTT
CAGGAAGCAGACTTCCTGGCGAACGTGGATAAACTGTCTGAAGATGCATTCGATGACCAG
TGCACCGGCGCTAACCCGCGTTACCCGCTGATCTCCGAGCTGAAACAGATTCTGCTGGAT
ACCTACTACGGTCGTGATTATGTAGAAGGTGAAACTGCAGCGAAGAAAGAAGCTGCTCCG
GCTAAAGCTGAGAAAAAAGCGAAAAAATCCGCTTAA
Protein Properties
Pfam Domain Function:
Protein Residues:891
Protein Molecular Weight:96126
Protein Theoretical pI:7
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Aldehyde-alcohol dehydrogenase
MAVTNVAELNALVERVKKAQREYASFTQEQVDKIFRAAALAAADARIPLAKMAVAESGMG
IVEDKVIKNHFASEYIYNAYKDEKTCGVLSEDDTFGTITIAEPIGIICGIVPTTNPTSTA
IFKSLISLKTRNAIIFSPHPRAKDATNKAADIVLQAAIAAGAPKDLIGWIDQPSVELSNA
LMHHPDINLILATGGPGMVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVASVLMSKTF
DNGVICASEQSVVVVDSVYDAVRERFATHGGYLLQGKELKAVQDVILKNGALNAAIVGQP
AYKIAELAGFSVPENTKILIGEVTVVDESEPFAHEKLSPTLAMYRAKDFEDAVEKAEKLV
AMGGIGHTSCLYTDQDNQPARVSYFGQKMKTARILINTPASQGGIGDLYNFKLAPSLTLG
CGSWGGNSISENVGPKHLINKKTVAKRAENMLWHKLPKSIYFRRGSLPIALDEVITDGHK
RALIVTDRFLFNNGYADQITSVLKAAGVETEVFFEVEADPTLSIVRKGAELANSFKPDVI
IALGGGSPMDAAKIMWVMYEHPETHFEELALRFMDIRKRIYKFPKMGVKAKMIAVTTTSG
TGSEVTPFAVVTDDATGQKYPLADYALTPDMAIVDANLVMDMPKSLCAFGGLDAVTHAME
AYVSVLASEFSDGQALQALKLLKEYLPASYHEGSKNPVARERVHSAATIAGIAFANAFLG
VCHSMAHKLGSQFHIPHGLANALLICNVIRYNANDNPTKQTAFSQYDRPQARRRYAEIAD
HLGLSAPGDRTAAKIEKLLAWLETLKAELGIPKSIREAGVQEADFLANVDKLSEDAFDDQ
CTGANPRYPLISELKQILLDTYYGRDYVEGETAAKKEAAPAKAEKKAKKSA
References
External Links:
ResourceLink
Uniprot ID:P0A9Q7
Uniprot Name:ADHE_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:1651639
Ecogene ID:EG10031
Ecocyc:EG10031
ColiBase:b1241
Kegg Gene:b1241
EchoBASE ID:EB0030
CCDB:ADHE_ECOLI
BacMap:16129202
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Danchin, A., Krin, E. (1995). "Filling the gap between hns and adhE in Escherichia coli K12." Microbiology 141 ( Pt 4):959-960. Pubmed: 7773397
  • Echave, P., Tamarit, J., Cabiscol, E., Ros, J. (2003). "Novel antioxidant role of alcohol dehydrogenase E from Escherichia coli." J Biol Chem 278:30193-30198. Pubmed: 12783863
  • Goodlove, P. E., Cunningham, P. R., Parker, J., Clark, D. P. (1989). "Cloning and sequence analysis of the fermentative alcohol-dehydrogenase-encoding gene of Escherichia coli." Gene 85:209-214. Pubmed: 2695398
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Kessler, D., Leibrecht, I., Knappe, J. (1991). "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. Pubmed: 2015910
  • Oshima, T., Aiba, H., Baba, T., Fujita, K., Hayashi, K., Honjo, A., Ikemoto, K., Inada, T., Itoh, T., Kajihara, M., Kanai, K., Kashimoto, K., Kimura, S., Kitagawa, M., Makino, K., Masuda, S., Miki, T., Mizobuchi, K., Mori, H., Motomura, K., Nakamura, Y., Nashimoto, H., Nishio, Y., Saito, N., Horiuchi, T., et, a. l. .. (1996). "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." DNA Res 3:137-155. Pubmed: 8905232
  • Yamato, M., Takahashi, Y., Tomotake, H., Ota, F., Hirota, K., Yamaguchi, K. (1994). "Monoclonal antibodies to spirosin of Yersinia enterocolitica and analysis of the localization of spirosome by use of them." Microbiol Immunol 38:177-182. Pubmed: 7521508
  • Zhang, J., Sprung, R., Pei, J., Tan, X., Kim, S., Zhu, H., Liu, C. F., Grishin, N. V., Zhao, Y. (2009). "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli." Mol Cell Proteomics 8:215-225. Pubmed: 18723842