DB code: D00492

CATH domain	3.90.180.10 : Quinone Oxidoreductase; Chain A, domain 1	Catalytic domain
CATH 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)
3.40.50.720 : 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
3.90.180.10 : Quinone Oxidoreductase; Chain A, domain 1	D00001 D00002 D00018 D00048 D00481 D00482 D00490 D00615

CATH domain

Related DB codes (homologues)

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

3.90.180.10 : Quinone Oxidoreductase; Chain A, domain 1

D00001 D00002 D00018 D00048 D00481 D00482 D00490 D00615

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 29105	18009 18009		16474 16474		15378 15378
PubChem	32051 32051	5886 5886		5884 5884		1038 1038

1p0cA01	Bound:2x_ZN	Unbound	Unbound	Unbound	Unbound
1p0cB01	Bound:2x_ZN	Unbound	Unbound	Unbound	Unbound
1p0fA01	Bound:2x_ZN	Unbound	Bound:GOL	Unbound	Unbound
1p0fB01	Bound:2x_ZN	Unbound	Bound:GOL	Unbound	Unbound
1p0cA02	Unbound	Unbound	Unbound	Unbound	Unbound
1p0cB02	Unbound	Unbound	Unbound	Unbound	Unbound
1p0fA02	Unbound	Bound:NAP	Unbound	Unbound	Unbound
1p0fB02	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	SER 1048;SER 1051	CYS 1046;HIS 1067;CYS 1173(Catalytic zinc);CYS 1097;CYS 1100;CYS 1103;CYS 1111(Zinc)
1p0cB01	SER 2048;SER 2051	CYS 2046;HIS 2067;CYS 2173(Catalytic zinc);CYS 2097;CYS 2100;CYS 2103;CYS 2111(Zinc)
1p0fA01	SER 1048;SER 1051	CYS 1046;HIS 1067;CYS 1173(Catalytic zinc);CYS 1097;CYS 1100;CYS 1103;CYS 1111(Zinc)
1p0fB01	SER 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
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