EzCatDB: D00481
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DB codeD00481
CATH domainDomain 13.90.180.10 : Quinone Oxidoreductase; Chain A, domain 1Catalytic domain
Domain 23.40.50.720 : Rossmann fold
E.C.1.1.1.1

CATH domainRelated DB codes (homologues)
3.40.50.720 : Rossmann foldS00543,S00551,S00552,S00553,S00602,S00604,S00605,S00608,S00610,S00625,S00319,S00328,S00329,S00330,S00331,S00332,D00456,D00457,D00458,S00324,S00320,S00325,S00326,S00327,D00459,S00335,S00336,S00334,T00219,S00339,D00513,D00001,D00002,D00003,D00005,D00007,D00008,D00010,D00012,D00017,D00018,D00023,D00027,D00028,D00031,D00032,D00033,D00034,D00035,D00037,D00048,D00071,D00476,D00482,D00490,D00492,D00494,D00545,D00601,D00603,D00604,D00605,D00615,D00845,D00857,D00858,M00161,M00171,M00210,T00002,T00010,T00011,T00015,T00227,T00247,T00408,T00414,D00827,D00262,D00274,D00275,M00035,T00109
3.90.180.10 : Quinone Oxidoreductase; Chain A, domain 1D00001,D00002,D00018,D00048,D00482,D00490,D00492,D00615

Enzyme Name
UniProtKBKEGG

Q9QYY9
Protein nameAlcohol dehydrogenase 4alcohol dehydrogenase
aldehyde reductase
ADH
alcohol dehydrogenase (NAD)
aliphatic alcohol dehydrogenase
ethanol dehydrogenase
NAD-dependent alcohol dehydrogenase
NAD-specific aromatic alcohol dehydrogenase
NADH-alcohol dehydrogenase
NADH-aldehyde dehydrogenase
primary alcohol dehydrogenase
yeast alcohol dehydrogenase
SynonymsEC 1.1.1.1
ADH2
Alcohol dehydrogenase class II
Alcohol dehydrogenase II
RefSeqNP_036126.2 (Protein)
NM_011996.2 (DNA/RNA sequence)
PfamPF08240 (ADH_N)
PF00107 (ADH_zinc_N)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00010Glycolysis / Gluconeogenesis
MAP00071Fatty acid metabolism
MAP00120Bile acid biosynthesis
MAP00260Glycine, serine and threonine metabolism
MAP00350Tyrosine metabolism
MAP006241- and 2-Methylnaphthalene degradation
MAP006413-Chloroacrylic acid degradation
MAP00830Retinol metabolism
MAP00980Metabolism of xenobiotics by cytochrome P450
MAP00982Drug metabolism - cytochrome P450

UniProtKB:Accession NumberQ9QYY9
Entry nameADH4_MOUSE
ActivityAn alcohol + NAD(+) = an aldehyde or ketone + NADH.
SubunitDimer.
Subcellular locationCytoplasm (By similarity).
CofactorBinds 2 zinc ions per subunit.

Compound table: links to PDB-related databases & PoSSuM

CofactorsSubstratesProducts
KEGG-idC00038C00003C00069C00071C00709C00004C00080
CompoundZincNAD+AlcoholAldehydeKetoneNADHH+
Typeheavy metalamide group,amine group,nucleotidecarbohydratecarbohydratecarbohydrateamide group,amine group,nucleotideothers
ChEBI29105
15846



16908
15378
PubChem32051
5893



439153
1038
               
1e3eA01Bound:_ZN 378UnboundUnboundUnboundUnboundUnbound 
1e3eB01Bound:_ZN 378UnboundUnboundUnboundUnboundUnbound 
1e3iA01Bound:_ZN 380UnboundUnboundAnalogue:CXFUnboundUnbound 
1e3iB01Bound:_ZN 380UnboundUnboundAnalogue:CXFUnboundUnbound 
1e3lA01Bound:_ZN 380UnboundUnboundUnboundUnboundUnbound 
1e3lB01Bound:_ZN 380UnboundUnboundUnboundUnboundUnbound 
1e3eA02UnboundUnboundUnboundUnboundUnboundBound:NAD 
1e3eB02UnboundUnboundUnboundUnboundUnboundBound:NAD 
1e3iA02UnboundUnboundUnboundUnboundUnboundBound:NAD 
1e3iB02UnboundUnboundUnboundUnboundUnboundBound:NAD 
1e3lA02UnboundUnboundUnboundUnboundUnboundBound:NAD 
1e3lB02UnboundUnboundUnboundUnboundUnboundBound:NAD 

Active-site residues
resource
Swiss-prot;P40394, P00325, P00327, P00326, P00328,P26325
pdbCatalytic residuesCofactor-binding residuescomment
           
1e3eA01THR 48
CYS 46;HIS 67;CYS 178(Catalytic Zinc binding)
 
1e3eB01THR 48
CYS 46;HIS 67;CYS 178(Catalytic Zinc binding)
 
1e3iA01THR 48
CYS 46;HIS 67;CYS 178(Catalytic Zinc binding)
 
1e3iB01THR 48
CYS 46;HIS 67;CYS 178(Catalytic Zinc binding)
 
1e3lA01THR 48
CYS 46;HIS 67;CYS 178(Catalytic Zinc binding)
mutant P47H
1e3lB01THR 48
CYS 46;HIS 67;CYS 178(Catalytic Zinc binding)
mutant P47H
1e3eA02 
 
 
1e3eB02 
 
 
1e3iA02 
 
 
1e3iB02 
 
 
1e3lA02 
 
 
1e3lB02 
 
 

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[7]p.450-451
[8]p.346-348
[11]Figure 3 p.3859

references
[1]
PubMed ID7484389
JournalAdv Exp Med Biol
Year1995
Volume372
Pages281-94
AuthorsJornvall H, Danielsson O, Hjelmqvist L, Persson B, Shafqat J
TitleThe alcohol dehydrogenase system.
[2]
PubMed ID7479907
JournalProc Natl Acad Sci U S A
Year1995
Volume92
Pages10904-8
AuthorsHjelmqvist L, Estonius M, Jornvall H
TitleThe vertebrate alcohol dehydrogenase system: variable class II type form elucidates separate stages of enzymogenesis.
[3]
PubMed ID9059633
JournalAdv Exp Med Biol
Year1997
Volume414
Pages291-302
AuthorsHurley TD, Steinmetz CG, Xie P, Yang ZN
TitleThree-dimensional structures of human alcohol dehydrogenase isoenzymes reveal the molecular basis for their functional diversity.
[4]
PubMed ID9059632
JournalAdv Exp Med Biol
Year1997
Volume414
Pages281-9
AuthorsJornvall H, Shafqat J, el-Ahmad M, Hjelmqvist L, Persson B, Danielsson O
TitleAlcohol dehydrogenase variability. Evolutionary and functional conclusions from characterization of further variants.
[5]
PubMed ID9572895
JournalJ Med Chem
Year1998
Volume41
Pages1696-701
AuthorsSchindler JF, Berst KB, Plapp BV
TitleInhibition of human alcohol dehydrogenases by formamides.
[6]
PubMed ID10352708
JournalAdv Exp Med Biol
Year1999
Volume463
Pages373-7
AuthorsPersson B, Nordling E, Kallberg Y, Lundh D, Oppermann UC, Marschall HU, Jornvall H
TitleBioinformatics in studies of SDR and MDR enzymes.
[7]
CommentsX-ray crystallography
PubMed ID10970744
JournalJ Mol Biol
Year2000
Volume302
Pages441-53
AuthorsSvensson S, Hoog JO, Schneider G, Sandalova T
TitleCrystal structures of mouse class II alcohol dehydrogenase reveal determinants of substrate specificity and catalytic efficiency.
Related PDB1e3e,1e3i,1e3l
[8]
PubMed ID11306056
JournalChem Biol Interact
Year2001
Volume130-132
Pages339-50
AuthorsSvensson S, Stromberg P, Sandalova T, Hoog J
TitleClass II alcohol dehydrogenase (ADH2)--adding the structure.
[9]
PubMed ID11173978
JournalJ Biomed Sci
Year2001
Volume8
Pages71-6
AuthorsHoog JO, Hedberg JJ, Stromberg P, Svensson S
TitleMammalian alcohol dehydrogenase - functional and structural implications.
[10]
PubMed ID11964133
JournalCell Mol Life Sci
Year2002
Volume59
Pages552-9
AuthorsStromberg P, Svensson S, Hedberg JJ, Nordling E, Hoog JO
TitleIdentification and characterisation of two allelic forms of human alcohol dehydrogenase 2.
[11]
PubMed ID11942822
JournalJ Am Chem Soc
Year2002
Volume124
Pages3858-64
AuthorsKohen A, Jensen JH
TitleBoundary conditions for the Swain-Schaad relationship as a criterion for hydrogen tunneling.

comments
This enzyme belongs to the zinc-containing alcohol dehydrogenase class II.
According to the literature [7] & [8], this enzyme is inefficient, probably due to Pro47, whose mutation to His restores the activity.

createdupdated
2005-01-112009-02-26
Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )
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