EzCatDB: D00492
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DB codeD00492
CATH domainDomain 13.90.180.10 : Quinone Oxidoreductase; Chain A, domain 1Catalytic domain
Domain 23.40.50.720 : Rossmann foldCatalytic domain
E.C.1.1.1.2

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,D00481,D00482,D00490,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,D00481,D00482,D00490,D00615

Enzyme Name
UniProtKBKEGG

O57380
Protein nameNADP-dependent alcohol dehydrogenasealcohol dehydrogenase (NADP+)
aldehyde reductase (NADPH2)
NADP-alcohol dehydrogenase
NADP+-aldehyde reductase
NADP+-dependent aldehyde reductase
NADPH-aldehyde reductase
NADPH-dependent aldehyde reductase
nonspecific succinic semialdehyde reductase
ALR 1
low-Km aldehyde reductase
high-Km aldehyde reductase
alcohol dehydrogenase (NADP+)
SynonymsEC 1.1.1.2
PfamPF08240 (ADH_N)
PF00107 (ADH_zinc_N)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00010Glycolysis / Gluconeogenesis
MAP00561Glycerolipid metabolism
MAP00930Caprolactam degradation

UniProtKB:Accession NumberO57380
Entry nameADH8_RANPE
ActivityAn alcohol + NADP(+) = an aldehyde + NADPH.
SubunitHomodimer.
Subcellular location
CofactorBinds 2 zinc ions per subunit (By similarity).

Compound table: links to PDB-related databases & PoSSuM

CofactorsSubstratesProducts
KEGG-idC00038C00006C00069C00005C00071C00080
CompoundZincNADP+AlcoholNADPHAldehydeH+
Typeheavy metalamide group,amine group,nucleotidecarbohydrateamide group,amine group,nucleotidecarbohydrateothers
ChEBI29105
18009

16474

15378
PubChem32051
5886

5884

1038
              
1p0cA01Bound:2x_ZNUnboundUnboundUnboundUnbound 
1p0cB01Bound:2x_ZNUnboundUnboundUnboundUnbound 
1p0fA01Bound:2x_ZNUnboundBound:GOLUnboundUnbound 
1p0fB01Bound:2x_ZNUnboundBound:GOLUnboundUnbound 
1p0cA02UnboundUnboundUnboundUnboundUnbound 
1p0cB02UnboundUnboundUnboundUnboundUnbound 
1p0fA02UnboundBound:NAPUnboundUnboundUnbound 
1p0fB02UnboundBound:NAPUnboundUnboundUnbound 

Active-site residues
resource
Swiss-prot & literature [4], [7] & [10]
pdbCatalytic residuesCofactor-binding residues
          
1p0cA01SER 1048;SER 1051
CYS 1046;HIS 1067;CYS 1173(Catalytic zinc);CYS 1097;CYS 1100;CYS 1103;CYS 1111(Zinc)
1p0cB01SER 2048;SER 2051
CYS 2046;HIS 2067;CYS 2173(Catalytic zinc);CYS 2097;CYS 2100;CYS 2103;CYS 2111(Zinc)
1p0fA01SER 1048;SER 1051
CYS 1046;HIS 1067;CYS 1173(Catalytic zinc);CYS 1097;CYS 1100;CYS 1103;CYS 1111(Zinc)
1p0fB01SER 2048;SER 2051
CYS 2046;HIS 2067;CYS 2173(Catalytic zinc);CYS 2097;CYS 2100;CYS 2103;CYS 2111(Zinc)
1p0cA02 
 
1p0cB02 
 
1p0fA02 
 
1p0fB02 
 

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[4]p.973-975
[7]p.621-623
[10]p.80-83

references
[1]
PubMed ID8068002
JournalBiochem J
Year1994
Volume302
Pages163-70
AuthorsBurdette D, Zeikus JG
TitlePurification of acetaldehyde dehydrogenase and alcohol dehydrogenases from Thermoanaerobacter ethanolicus 39E and characterization of the secondary-alcohol dehydrogenase (2 degrees Adh) as a bifunctional alcohol dehydrogenase--acetyl-CoA reductive thioesterase.
[2]
CommentsX-ray crystallography
JournalActa Crystallogr D Biol Crystallogr
Year1996
Volume52
Pages882-6
AuthorsKorkhin Y, Frolow F, Bogin O, Peretz M, Kalb(Gilboa) AJ, Burstein Y
TitleCrystalline alcohol dehydrogenases from the mesophilic bacterium Clostridium beijerinckii and the thermophilic bacterium Thermoanaerobium brockii: Preparation, characterization and molecular symmetry.
Related PDB1kev,1ped
[3]
PubMed ID8639709
JournalBiochim Biophys Acta
Year1996
Volume1294
Pages15-24
AuthorsDallet S, Legoy MD
TitleHydrostatic pressure induces conformational and catalytic changes on two alcohol dehydrogenases but no oligomeric dissociation.
[4]
CommentsX-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS)
Medline ID98295421
PubMed ID9836873
JournalJ Mol Biol
Year1998
Volume278
Pages967-81
AuthorsKorkhin Y, Kalb(Gilboa) AJ, Peretz M, Bogin O, Burstein Y, Frolow F
TitleNADP-dependent bacterial alcohol dehydrogenases: crystal structure, cofactor-binding and cofactor specificity of the ADHs of Clostridium beijerinckii and Thermoanaerobacter brockii.
Related PDB1ykf
Related UniProtKBP14941,P25984
[5]
PubMed ID10473548
JournalJ Biol Chem
Year1999
Volume274
Pages26021-6
AuthorsPeralba JM, Cederlund E, Crosas B, Moreno A, Julia P, Martinez SE, Persson B, Farr s J, Pares X, Jornvall H
TitleStructural and enzymatic properties of a gastric NADP(H)- dependent and retinal-active alcohol dehydrogenase.
Related UniProtKBO57380
[6]
PubMed ID10417229
JournalProtein Sci
Year1999
Volume8
Pages1241-9
AuthorsKorkhin Y, Kalb (Gilboa) AJ, Peretz M, Bogin O, Burstein Y, Frolow F
TitleOligomeric integrity--the structural key to thermal stability in bacterial alcohol dehydrogenases.
[7]
CommentsX-ray crystallography
PubMed ID10651277
JournalProteins
Year1999
Volume37
Pages619-27
AuthorsLi C, Heatwole J, Soelaiman S, Shoham M
TitleCrystal structure of a thermophilic alcohol dehydrogenase substrate complex suggests determinants of substrate specificity and thermostability.
Related PDB1bxz
[8]
CommentsX-ray crystallography
PubMed ID12381840
JournalProtein Sci
Year2002
Volume11
Pages2561-74
AuthorsBogin O, Levin I, Hacham Y, Tel-Or S, Peretz M, Frolow F, Burstein Y
TitleStructural basis for the enhanced thermal stability of alcohol dehydrogenase mutants from the mesophilic bacterium Clostridium beijerinckii: contribution of salt bridging.
Related PDB1jqb
[9]
PubMed ID12902331
JournalJ Biol Chem
Year2003
Volume278
Pages40573-80
AuthorsRosell A, Valencia E, Ochoa WF, Fita I, Pares X, Farres J
TitleComplete reversal of coenzyme specificity by concerted mutation of three consecutive residues in alcohol dehydrogenase.
[10]
PubMed ID12818203
JournalJ Mol Biol
Year2003
Volume330
Pages75-85
AuthorsRosell A, Valencia E, Pares X, Fita I, Farres J, Ochoa WF
TitleCrystal structure of the vertebrate NADP(H)-dependent alcohol dehydrogenase (ADH8).
Related PDB1p0c,1p0f

comments
This enzyme belongs to class-IV subfamily of zinc-containing alcohol dehydrogenase family.
Although this enzyme binds two zinc ions per subunit, only one zinc ion is involved in catalysis.

createdupdated
2004-05-242009-02-26
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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