EzCatDB: D00002
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DB codeD00002
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,D00003,D00005,D00007,D00008,D00010,D00012,D00017,D00018,D00023,D00027,D00028,D00031,D00032,D00033,D00034,D00035,D00037,D00048,D00071,D00476,D00481,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,D00018,D00048,D00481,D00482,D00490,D00492,D00615

Enzyme Name
UniProtKBKEGG

P14941P25984
Protein nameNADP-dependent alcohol dehydrogenaseNADP-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
EC 1.1.1.2
CbADH
PfamPF08240 (ADH_N)
PF00107 (ADH_zinc_N)
[Graphical view]
PF08240 (ADH_N)
PF00107 (ADH_zinc_N)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00010Glycolysis / Gluconeogenesis
MAP00561Glycerolipid metabolism
MAP00930Caprolactam degradation

UniProtKB:Accession NumberP14941P25984
Entry nameADH_THEBRADH_CLOBE
ActivityAn alcohol + NADP(+) = an aldehyde + NADPH.An alcohol + NADP(+) = an aldehyde + NADPH.
SubunitHomotetramer.Homotetramer.
Subcellular location

CofactorBinds 1 zinc ion per subunit.Binds 1 zinc ion per subunit.

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
              
1bxzA01Bound:_ZNUnboundBound:SBTUnboundUnbound 
1bxzB01Bound:_ZNUnboundBound:SBTUnboundUnbound 
1bxzC01Bound:_ZNUnboundBound:SBTUnboundUnbound 
1bxzD01Bound:_ZNUnboundBound:SBTUnboundUnbound 
1ykfA01Bound:_ZNUnboundUnboundUnboundUnbound 
1ykfB01Bound:_ZNUnboundUnboundUnboundUnbound 
1ykfC01Bound:_ZNUnboundUnboundUnboundUnbound 
1ykfD01Bound:_ZNUnboundUnboundUnboundUnbound 
1jqbA01Bound:_ZNUnboundUnboundUnboundUnbound 
1jqbB01Bound:_ZNUnboundUnboundUnboundUnbound 
1jqbC01Bound:_ZNUnboundUnboundUnboundUnbound 
1jqbD01Bound:_ZNUnboundUnboundUnboundUnbound 
1kevA01Bound:_ZNUnboundUnboundUnboundUnbound 
1kevB01Bound:_ZNUnboundUnboundUnboundUnbound 
1kevC01Bound:_ZNUnboundUnboundUnboundUnbound 
1kevD01Bound:_ZNUnboundUnboundUnboundUnbound 
1pedA01Bound:_ZNUnboundUnboundUnboundUnbound 
1pedB01Bound:_ZNUnboundUnboundUnboundUnbound 
1pedC01Bound:_ZNUnboundUnboundUnboundUnbound 
1pedD01Bound:_ZNUnboundUnboundUnboundUnbound 
1bxzA02UnboundUnboundUnboundUnboundUnbound 
1bxzB02UnboundUnboundUnboundUnboundUnbound 
1bxzC02UnboundUnboundUnboundUnboundUnbound 
1bxzD02UnboundUnboundUnboundUnboundUnbound 
1ykfA02UnboundBound:NAPUnboundUnboundUnbound 
1ykfB02UnboundBound:NAPUnboundUnboundUnbound 
1ykfC02UnboundBound:NAPUnboundUnboundUnbound 
1ykfD02UnboundBound:NAPUnboundUnboundUnbound 
1jqbA02UnboundUnboundUnboundUnboundUnbound 
1jqbB02UnboundUnboundUnboundUnboundUnbound 
1jqbC02UnboundUnboundUnboundUnboundUnbound 
1jqbD02UnboundUnboundUnboundUnboundUnbound 
1kevA02UnboundUnboundUnboundBound:NDPUnbound 
1kevB02UnboundUnboundUnboundBound:NDPUnbound 
1kevC02UnboundUnboundUnboundBound:NDPUnbound 
1kevD02UnboundUnboundUnboundBound:NDPUnbound 
1pedA02UnboundUnboundUnboundUnboundUnbound 
1pedB02UnboundUnboundUnboundUnboundUnbound 
1pedC02UnboundUnboundUnboundUnboundUnbound 
1pedD02UnboundUnboundUnboundUnboundUnbound 

Active-site residues
resource
Swiss-prot;P14941, P25984 & literature [4], [7] & [10]
pdbCatalytic residuesCofactor-binding residues
          
1bxzA01SER   39;HIS   42
CYS   37;HIS   59;ASP  150(Catalytic zinc)
1bxzB01SER   39;HIS   42
CYS   37;HIS   59;ASP  150(Catalytic zinc)
1bxzC01SER   39;HIS   42
CYS   37;HIS   59;ASP  150(Catalytic zinc)
1bxzD01SER   39;HIS   42
CYS   37;HIS   59;ASP  150(Catalytic zinc)
1ykfA01SER   39;HIS   42
CYS   37;HIS   59;ASP  150(Catalytic zinc)
1ykfB01SER   39;HIS   42
CYS   37;HIS   59;ASP  150(Catalytic zinc)
1ykfC01SER   39;HIS   42
CYS   37;HIS   59;ASP  150(Catalytic zinc)
1ykfD01SER   39;HIS   42
CYS   37;HIS   59;ASP  150(Catalytic zinc)
1jqbA01SER 1039;HIS 1042
CYS 1037;HIS 1059;ASP 1150(Catalytic zinc)
1jqbB01SER 2039;HIS 2042
CYS 2037;HIS 2059;ASP 2150(Catalytic zinc)
1jqbC01SER 3039;HIS 3042
CYS 3037;HIS 3059;ASP 3150(Catalytic zinc)
1jqbD01SER 4039;HIS 4042
CYS 4037;HIS 4059;ASP 4150(Catalytic zinc)
1kevA01SER   39;HIS   42
CYS   37;HIS   59;ASP  150(Catalytic zinc)
1kevB01SER   39;HIS   42
CYS   37;HIS   59;ASP  150(Catalytic zinc)
1kevC01SER   39;HIS   42
CYS   37;HIS   59;ASP  150(Catalytic zinc)
1kevD01SER   39;HIS   42
CYS   37;HIS   59;ASP  150(Catalytic zinc)
1pedA01SER   39;HIS   42
CYS   37;HIS   59;ASP  150(Catalytic zinc)
1pedB01SER   39;HIS   42
CYS   37;HIS   59;ASP  150(Catalytic zinc)
1pedC01SER   39;HIS   42
CYS   37;HIS   59;ASP  150(Catalytic zinc)
1pedD01SER   39;HIS   42
CYS   37;HIS   59;ASP  150(Catalytic zinc)
1bxzA02 
 
1bxzB02 
 
1bxzC02 
 
1bxzD02 
 
1ykfA02 
 
1ykfB02 
 
1ykfC02 
 
1ykfD02 
 
1jqbA02 
 
1jqbB02 
 
1jqbC02 
 
1jqbD02 
 
1kevA02 
 
1kevB02 
 
1kevC02 
 
1kevD02 
 
1pedA02 
 
1pedB02 
 
1pedC02 
 
1pedD02 
 

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 zinc-containing alcohol dehydrogenase family.

createdupdated
2004-05-242009-02-26


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Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
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