DB code: D00492

CATH domain 3.90.180.10 : Quinone Oxidoreductase; Chain A, domain 1 Catalytic domain
3.40.50.720 : Rossmann fold Catalytic domain
E.C. 1.1.1.2
CSA
M-CSA
MACiE

CATH domain Related DB codes (homologues)
3.90.180.10 : Quinone Oxidoreductase; Chain A, domain 1 D00001 D00002 D00018 D00048 D00481 D00482 D00490 D00615
3.40.50.720 : Rossmann fold S00543 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

Uniprot Enzyme Name
UniprotKB Protein name Synonyms Pfam
O57380 NADP-dependent alcohol dehydrogenase
EC 1.1.1.2
PF08240 (ADH_N)
PF00107 (ADH_zinc_N)
[Graphical View]

KEGG enzyme name
alcohol 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+)

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
O57380 ADH8_RANPE An alcohol + NADP(+) = an aldehyde + NADPH. Homodimer. Binds 2 zinc ions per subunit (By similarity).

KEGG Pathways
Map code Pathways E.C.
MAP00010 Glycolysis / Gluconeogenesis
MAP00561 Glycerolipid metabolism
MAP00930 Caprolactam degradation

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C00038 C00006 C00069 C00005 C00071 C00080
E.C.
Compound Zinc NADP+ Alcohol NADPH Aldehyde H+
Type heavy metal amide group,amine group,nucleotide carbohydrate amide group,amine group,nucleotide carbohydrate others
ChEBI 29105
18009
16474
15378
PubChem 32051
5886
5884
1038
1p0cA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:2x_ZN Unbound Unbound Unbound Unbound
1p0cB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:2x_ZN Unbound Unbound Unbound Unbound
1p0fA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:2x_ZN Unbound Bound:GOL Unbound Unbound
1p0fB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:2x_ZN Unbound Bound:GOL Unbound Unbound
1p0cA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1p0cB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1p0fA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:NAP Unbound Unbound Unbound
1p0fB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:NAP Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
Swiss-prot & literature [4], [7] & [10]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1p0cA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 1048;SER 1051 CYS 1046;HIS 1067;CYS 1173(Catalytic zinc);CYS 1097;CYS 1100;CYS 1103;CYS 1111(Zinc)
1p0cB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 2048;SER 2051 CYS 2046;HIS 2067;CYS 2173(Catalytic zinc);CYS 2097;CYS 2100;CYS 2103;CYS 2111(Zinc)
1p0fA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 1048;SER 1051 CYS 1046;HIS 1067;CYS 1173(Catalytic zinc);CYS 1097;CYS 1100;CYS 1103;CYS 1111(Zinc)
1p0fB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 2048;SER 2051 CYS 2046;HIS 2067;CYS 2173(Catalytic zinc);CYS 2097;CYS 2100;CYS 2103;CYS 2111(Zinc)
1p0cA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1p0cB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1p0fA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1p0fB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[4]
p.973-975
[7]
p.621-623
[10]
p.80-83

References
[1]
Resource
Comments
Medline ID
PubMed ID 8068002
Journal Biochem J
Year 1994
Volume 302
Pages 163-70
Authors Burdette D, Zeikus JG
Title Purification 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.
Related PDB
Related UniProtKB
[2]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID
Journal Acta Crystallogr D Biol Crystallogr
Year 1996
Volume 52
Pages 882-6
Authors Korkhin Y, Frolow F, Bogin O, Peretz M, Kalb(Gilboa) AJ, Burstein Y
Title Crystalline alcohol dehydrogenases from the mesophilic bacterium Clostridium beijerinckii and the thermophilic bacterium Thermoanaerobium brockii: Preparation, characterization and molecular symmetry.
Related PDB 1kev 1ped
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 8639709
Journal Biochim Biophys Acta
Year 1996
Volume 1294
Pages 15-24
Authors Dallet S, Legoy MD
Title Hydrostatic pressure induces conformational and catalytic changes on two alcohol dehydrogenases but no oligomeric dissociation.
Related PDB
Related UniProtKB
[4]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS)
Medline ID 98295421
PubMed ID 9836873
Journal J Mol Biol
Year 1998
Volume 278
Pages 967-81
Authors Korkhin Y, Kalb(Gilboa) AJ, Peretz M, Bogin O, Burstein Y, Frolow F
Title NADP-dependent bacterial alcohol dehydrogenases: crystal structure, cofactor-binding and cofactor specificity of the ADHs of Clostridium beijerinckii and Thermoanaerobacter brockii.
Related PDB 1ykf
Related UniProtKB P14941 P25984
[5]
Resource
Comments
Medline ID
PubMed ID 10473548
Journal J Biol Chem
Year 1999
Volume 274
Pages 26021-6
Authors Peralba JM, Cederlund E, Crosas B, Moreno A, Julia P, Martinez SE, Persson B, Farr s J, Pares X, Jornvall H
Title Structural and enzymatic properties of a gastric NADP(H)- dependent and retinal-active alcohol dehydrogenase.
Related PDB
Related UniProtKB O57380
[6]
Resource
Comments
Medline ID
PubMed ID 10417229
Journal Protein Sci
Year 1999
Volume 8
Pages 1241-9
Authors Korkhin Y, Kalb (Gilboa) AJ, Peretz M, Bogin O, Burstein Y, Frolow F
Title Oligomeric integrity--the structural key to thermal stability in bacterial alcohol dehydrogenases.
Related PDB
Related UniProtKB
[7]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 10651277
Journal Proteins
Year 1999
Volume 37
Pages 619-27
Authors Li C, Heatwole J, Soelaiman S, Shoham M
Title Crystal structure of a thermophilic alcohol dehydrogenase substrate complex suggests determinants of substrate specificity and thermostability.
Related PDB 1bxz
Related UniProtKB
[8]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 12381840
Journal Protein Sci
Year 2002
Volume 11
Pages 2561-74
Authors Bogin O, Levin I, Hacham Y, Tel-Or S, Peretz M, Frolow F, Burstein Y
Title Structural basis for the enhanced thermal stability of alcohol dehydrogenase mutants from the mesophilic bacterium Clostridium beijerinckii: contribution of salt bridging.
Related PDB 1jqb
Related UniProtKB
[9]
Resource
Comments
Medline ID
PubMed ID 12902331
Journal J Biol Chem
Year 2003
Volume 278
Pages 40573-80
Authors Rosell A, Valencia E, Ochoa WF, Fita I, Pares X, Farres J
Title Complete reversal of coenzyme specificity by concerted mutation of three consecutive residues in alcohol dehydrogenase.
Related PDB
Related UniProtKB
[10]
Resource
Comments
Medline ID
PubMed ID 12818203
Journal J Mol Biol
Year 2003
Volume 330
Pages 75-85
Authors Rosell A, Valencia E, Pares X, Fita I, Farres J, Ochoa WF
Title Crystal structure of the vertebrate NADP(H)-dependent alcohol dehydrogenase (ADH8).
Related PDB 1p0c 1p0f
Related UniProtKB

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.

Created Updated
2004-05-24 2009-02-26