DB code: D00018

CATH domain 3.90.180.10 : Quinone Oxidoreductase; Chain A, domain 1 Catalytic domain
3.40.50.720 : Rossmann fold Catalytic domain
E.C. 1.1.1.1 1.1.1.284 1.1.1.-
CSA 1teh
M-CSA 1teh
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 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 1 D00001 D00002 D00048 D00481 D00482 D00490 D00492 D00615

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq Pfam
P11766 Alcohol dehydrogenase class-3
EC 1.1.1.1
Alcohol dehydrogenase class-III
Alcohol dehydrogenase 5
Alcohol dehydrogenase class chi chain
S-(hydroxymethyl)glutathione dehydrogenase
EC 1.1.1.284
Glutathione-dependent formaldehyde dehydrogenase
GSH-FDH
FALDH
FDH
EC 1.1.1.-
NP_000662.3 (Protein)
NM_000671.3 (DNA/RNA sequence)
PF08240 (ADH_N)
PF00107 (ADH_zinc_N)
[Graphical View]

KEGG enzyme name
alcohol dehydrogenase
(EC 1.1.1.1 )
aldehyde reductase
(EC 1.1.1.1 )
ADH
(EC 1.1.1.1 )
alcohol dehydrogenase (NAD)
(EC 1.1.1.1 )
aliphatic alcohol dehydrogenase
(EC 1.1.1.1 )
ethanol dehydrogenase
(EC 1.1.1.1 )
NAD-dependent alcohol dehydrogenase
(EC 1.1.1.1 )
NAD-specific aromatic alcohol dehydrogenase
(EC 1.1.1.1 )
NADH-alcohol dehydrogenase
(EC 1.1.1.1 )
NADH-aldehyde dehydrogenase
(EC 1.1.1.1 )
primary alcohol dehydrogenase
(EC 1.1.1.1 )
yeast alcohol dehydrogenase
(EC 1.1.1.1 )
S-(hydroxymethyl)glutathione dehydrogenase
(EC 1.1.1.284 )
NAD-linked formaldehyde dehydrogenase (incorrect)
(EC 1.1.1.284 )
formaldehyde dehydrogenase (incorrect)
(EC 1.1.1.284 )
formic dehydrogenase (incorrect)
(EC 1.1.1.284 )
class III alcohol dehydrogenase
(EC 1.1.1.284 )
ADH3
(EC 1.1.1.284 )
&chi
(EC 1.1.1.284 )
-ADH
(EC 1.1.1.284 )
FDH (incorrect)
(EC 1.1.1.284 )
formaldehyde dehydrogenase (glutathione) (incorrect)
(EC 1.1.1.284 )
GS-FDH (incorrect)
(EC 1.1.1.284 )
glutathione-dependent formaldehyde dehydrogenase (incorrect)
(EC 1.1.1.284 )
NAD-dependent formaldehyde dehydrogenase
(EC 1.1.1.284 )
GD-FALDH
(EC 1.1.1.284 )
NAD- and glutathione-dependent formaldehyde dehydrogenase
(EC 1.1.1.284 )

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P11766 ADHX_HUMAN An alcohol + NAD(+) = an aldehyde or ketone + NADH. S-(hydroxymethyl)glutathione + NAD(P)(+) = S- formylglutathione + NAD(P)H. Homodimer. Cytoplasm. Binds 2 zinc ions per subunit.

KEGG Pathways
Map code Pathways E.C.
MAP00010 Glycolysis / Gluconeogenesis 1.1.1.1
MAP00071 Fatty acid metabolism 1.1.1.1
MAP00120 Bile acid biosynthesis 1.1.1.1
MAP00260 Glycine, serine and threonine metabolism 1.1.1.1
MAP00350 Tyrosine metabolism 1.1.1.1
MAP00624 1- and 2-Methylnaphthalene degradation 1.1.1.1
MAP00641 3-Chloroacrylic acid degradation 1.1.1.1
MAP00680 Methane metabolism 1.1.1.284
MAP00830 Retinol metabolism 1.1.1.1
MAP00980 Metabolism of xenobiotics by cytochrome P450 1.1.1.1
MAP00982 Drug metabolism - cytochrome P450 1.1.1.1

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C00038 C00003 C00069 C14180 C00004 C00071 C00709 C01031 C00080
E.C. 1.1.1.1
1.1.1.284
1.1.1.1
1.1.1.284
1.1.1.1
1.1.1.284
1.1.1.1
1.1.1.1
1.1.1.284
1.1.1.1
1.1.1.284
Compound Zinc NAD+ Alcohol S-(Hydroxymethyl)glutathione NADH Aldehyde Ketone S-Formylglutathione H+
Type heavy metal amide group,amine group,nucleotide carbohydrate amino acids,carbohydrate,carboxyl group,peptide/protein,sulfide group amide group,amine group,nucleotide carbohydrate carbohydrate amino acids,carbohydrate,carboxyl group,peptide/protein,sulfide group others
ChEBI 29105
 29105
 		15846
 15846
 		48926
 48926
 		16908
 16908
 		16225
 16225
 		15378
 15378
PubChem 32051
 32051
 		5893
 5893
 		447123
 447123
 		439153
 439153
 		189122
 189122
 		1038
 1038
1m6hA01 Bound:2x_ZN Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1m6hB01 Bound:2x_ZN Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1m6wA01 Bound:2x_ZN Unbound Bound:12H Unbound Unbound Unbound Unbound Unbound
1m6wB01 Bound:2x_ZN Unbound Bound:12H Unbound Unbound Unbound Unbound Unbound
1ma0A01 Bound:2x_ZN Unbound Analogue:DAO Unbound Unbound Unbound Unbound Unbound
1ma0B01 Bound:2x_ZN Unbound Analogue:DAO Unbound Unbound Unbound Unbound Unbound
1mc5A01 Bound:2x_ZN Unbound Unbound Bound:AHE Unbound Unbound Unbound Unbound
1mc5B01 Bound:2x_ZN Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1mp0A01 Bound:2x_ZN Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1mp0B01 Bound:2x_ZN Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1tehA01 Bound:2x_ZN Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1tehB01 Bound:3x_ZN Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1m6hA02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1m6hB02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1m6wA02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1m6wB02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1ma0A02 Unbound Bound:NAD Unbound Unbound Unbound Unbound Unbound Unbound
1ma0B02 Unbound Bound:NAD Unbound Unbound Unbound Unbound Unbound Unbound
1mc5A02 Unbound Unbound Unbound Unbound Bound:NAD Unbound Unbound Unbound
1mc5B02 Unbound Unbound Unbound Unbound Bound:NAD Unbound Unbound Unbound
1mp0A02 Unbound Unbound Unbound Unbound Bound:NAD Unbound Unbound Unbound
1mp0B02 Unbound Unbound Unbound Unbound Bound:NAD Unbound Unbound Unbound
1tehA02 Unbound Bound:NAD Unbound Unbound Unbound Unbound Unbound Unbound
1tehB02 Unbound Bound:NAD Unbound Unbound Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
PDB;1teh & Swiss-prot;P11766 & literature [10]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1m6hA01 THR 46 CYS 44;HIS 66;GLU 67;CYS 173(Catalytic zinc binding);CYS 96;CYS 99;CYS 102;CYS 110(Zinc binding)
1m6hB01 THR 46 CYS 44;HIS 66;GLU 67;CYS 173(Catalytic zinc binding);CYS 96;CYS 99;CYS 102;CYS 110(Zinc binding)
1m6wA01 THR 46 CYS 44;HIS 66;GLU 67;CYS 173(Catalytic zinc binding);CYS 96;CYS 99;CYS 102;CYS 110(Zinc binding)
1m6wB01 THR 46 CYS 44;HIS 66;GLU 67;CYS 173(Catalytic zinc binding);CYS 96;CYS 99;CYS 102;CYS 110(Zinc binding)
1ma0A01 THR 46 CYS 44;HIS 66;GLU 67;CYS 173(Catalytic zinc binding);CYS 96;CYS 99;CYS 102;CYS 110(Zinc binding)
1ma0B01 THR 46 CYS 44;HIS 66;GLU 67;CYS 173(Catalytic zinc binding);CYS 96;CYS 99;CYS 102;CYS 110(Zinc binding)
1mc5A01 THR 46 CYS 44;HIS 66;GLU 67;CYS 173(Catalytic zinc binding);CYS 96;CYS 99;CYS 102;CYS 110(Zinc binding)
1mc5B01 THR 46 CYS 44;HIS 66;GLU 67;CYS 173(Catalytic zinc binding);CYS 96;CYS 99;CYS 102;CYS 110(Zinc binding)
1mp0A01 THR 46 CYS 44;HIS 66;GLU 67;CYS 173(Catalytic zinc binding);CYS 96;CYS 99;CYS 102;CYS 110(Zinc binding)
1mp0B01 THR 46 CYS 44;HIS 66;GLU 67;CYS 173(Catalytic zinc binding);CYS 96;CYS 99;CYS 102;CYS 110(Zinc binding)
1tehA01 THR 48 CYS 46;HIS 67;GLU 68;CYS 174(Catalytic zinc binding);CYS 97;CYS 100;CYS 103;CYS 111(Zinc binding)
1tehB01 THR 48 CYS 46;HIS 67;GLU 68;CYS 174(Catalytic zinc binding);CYS 97;CYS 100;CYS 103;CYS 111(Zinc binding)
1m6hA02
1m6hB02
1m6wA02
1m6wB02
1ma0A02
1ma0B02
1mc5A02
1mc5B02
1mp0A02
1mp0B02
1tehA02
1tehB02

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[9]
p.337-340
[11]
p.15194
[12]

References
[1]
Resource
Comments
Medline ID
PubMed ID 6385855
Journal Arch Biochem Biophys
Year 1984
Volume 233
Pages 447-56
Authors Langston-Unkefer PJ, Gander JE
Title Occurrence of multiple forms of alcohol dehydrogenase in Penicillium supplemented with 2,3-butanediol.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 2688201
Journal Trends Biochem Sci
Year 1989
Volume 14
Pages 368-73
Authors Klinman JP
Title Quantum mechanical effects in enzyme-catalysed hydrogen transfer reactions.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 1985938
Journal J Biol Chem
Year 1991
Volume 266
Pages 1128-33
Authors Moreno A, Pares X
Title Purification and characterization of a new alcohol dehydrogenase from human stomach.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 8493900
Journal Adv Exp Med Biol
Year 1993
Volume 328
Pages 245-50
Authors Hurley TD, Yang Z, Bosron WF, Weiner H
Title Crystallization and preliminary X-ray analysis of bovine mitochondrial aldehyde dehydrogenase and human glutathione-dependent formaldehyde dehydrogenase.
Related PDB
Related UniProtKB
[5]
Resource
Comments MUTAGENESIS OF ARG-114
Medline ID 93211987
PubMed ID 8460164
Journal Proc Natl Acad Sci U S A
Year 1993
Volume 90
Pages 2491-4
Authors Engeland K, Hoog JO, Holmquist B, Estonius M, Jornvall H, Vallee BL
Title Mutation of Arg-115 of human class III alcohol dehydrogenase: a binding site required for formaldehyde dehydrogenase activity and fatty acid activation.
Related PDB
Related UniProtKB P11766
[6]
Resource
Comments
Medline ID
PubMed ID 7957198
Journal Eur J Biochem
Year 1994
Volume 225
Pages 1081-8
Authors Danielsson O, Shafqat J, Estonius M, Jornvall H
Title Alcohol dehydrogenase class III contrasted to class I. Characterization of the cyclostome enzyme, the existence of multiple forms as for the human enzyme, and distant cross-species hybridization.
Related PDB
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 8931553
Journal Biochemistry
Year 1996
Volume 35
Pages 14561-8
Authors Danielsson O, Shafqat J, Estonius M, el-Ahmad M, Jornvall H
Title Isozyme multiplicity with anomalous dimer patterns in a class III alcohol dehydrogenase. Effects on the activity and quaternary structure of residue exchanges at "nonfunctional" sites in a native protein.
Related PDB
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 8944774
Journal Eur J Biochem
Year 1996
Volume 241
Pages 849-57
Authors Martinez MC, Achkor H, Persson B, Fernandez MR, Shafqat J, Farres J, Jornvall H, Pares X
Title Arabidopsis formaldehyde dehydrogenase. Molecular properties of plant class III alcohol dehydrogenase provide further insights into the origins, structure and function of plant class p and liver class I alcohol dehydrogenases.
Related PDB
Related UniProtKB
[9]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS)
Medline ID 97170743
PubMed ID 9018047
Journal J Mol Biol
Year 1997
Volume 265
Pages 330-43
Authors Yang ZN, Bosron WF, Hurley TD
Title Structure of human chi chi alcohol dehydrogenase: a glutathione-dependent formaldehyde dehydrogenase.
Related PDB 1teh
Related UniProtKB P11766
[10]
Resource
Comments
Medline ID
PubMed ID 9613842
Journal Protein Eng
Year 1998
Volume 11
Pages 185-98
Authors Jongejan A, Jongejan JA, Duine JA
Title Homology model of the quinohaemoprotein alcohol dehydrogenase from Comamonas testosteroni.
Related PDB
Related UniProtKB
[11]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 12484756
Journal Biochemistry
Year 2002
Volume 41
Pages 15189-94
Authors Sanghani PC, Bosron WF, Hurley TD
Title Human glutathione-dependent formaldehyde dehydrogenase. Structural changes associated with ternary complex formation.
Related PDB 1mc5
Related UniProtKB
[12]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 12196016
Journal Biochemistry
Year 2002
Volume 41
Pages 10778-86
Authors Sanghani PC, Robinson H, Bosron WF, Hurley TD
Title Human glutathione-dependent formaldehyde dehydrogenase. Structures of apo, binary, and inhibitory ternary complexes.
Related PDB 1m6h 1m6w 1ma0
Related UniProtKB
[13]
Resource
Comments
Medline ID
PubMed ID 14523561
Journal Cell Mol Life Sci
Year 2003
Volume 60
Pages 2009-16
Authors Hjelmqvist L, Norin A, El-Ahmad M, Griffiths W, Jornvall H
Title Distinct but parallel evolutionary patterns between alcohol and aldehyde dehydrogenases: addition of fish/human betaine aldehyde dehydrogenase divergence.
Related PDB
Related UniProtKB
[14]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 12604204
Journal Chem Biol Interact
Year 2003
Volume 143-144
Pages 195-200
Authors Sanghani PC, Robinson H, Bennett-Lovsey R, Hurley TD, Bosron WF
Title Structure-function relationships in human Class III alcohol dehydrogenase (formaldehyde dehydrogenase).
Related PDB 1mp0
Related UniProtKB
[15]
Resource
Comments
Medline ID
PubMed ID 14960302
Journal FEBS Lett
Year 2004
Volume 559
Pages 27-32
Authors Norin A, Shafqat J, El-Ahmad M, Alvelius G, Cederlund E, Hjelmqvist L, Jornvall H
Title Class III alcohol dehydrogenase: consistent pattern complemented with the mushroom enzyme.
Related PDB
Related UniProtKB

Comments
The E.C. was transferred from 1.2.1.1 to 1.1.1.284.
There are several isozymes of alcohol dehydrogenase in human; class-I, class-II, class-III, class-IV, & class-V. This enzyme belongs to the class-III isozyme.

Created Updated
2004-03-24 2009-03-16