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InterPro: IPR014183 Alcohol dehydrogenase class III/S-(hydroxymethyl)glutathione dehydrogenase

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UniProtKB

Matches:

796 proteins

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Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR014183 ADH_3

Type

Family

Signatures Help

Database	ID	Name	Proteins
TIGRFAMs	TIGR02818	adh_III_F_hyde	796
Signatures in BioMart

InterPro Relationships Help

Parent

IPR002085 Alcohol dehydrogenase superfamily, zinc-containing

Contains

IPR002328 Alcohol dehydrogenase, zinc-containing, conserved site
IPR013149 Alcohol dehydrogenase, zinc-binding
IPR013154 Alcohol dehydrogenase GroES-like

GO Term annotation Help

Process

GO:0006069 ethanol oxidation
GO:0055114 oxidation reduction

Function

GO:0008270 zinc ion binding
GO:0051903 S-(hydroxymethyl)glutathione dehydrogenase activity

InterPro annotation

Entry Details in BioMart

Abstract

The members of this protein family show dual function. First, they remove formaldehyde, a toxic metabolite, by acting as S-(hydroxymethyl)glutathione dehydrogenase (EC:1.1.1.284). S-(hydroxymethyl)glutathione can form spontaneously from formaldehyde and glutathione, and so this enzyme previously was designated glutathione-dependent formaldehyde dehydrogenase. These same proteins are also designated as class III alcohol dehydrogenases (EC:1.1.1.1), i.e. alcohol dehydrogenases that do not require glutathione and they tend to show poor activity for ethanol among their various substrate alcohols.

Structural links Help

PDB - click here

SCOP: b.35.1.2 , c.2.1.1

CATH: 3.40.50.720 , 3.90.180.10

Database links Help

Enzyme: EC:1.1.1.1 , EC:1.1.1.284

CluSTr: ALLvsALL:3558:146.1

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR014183

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P11766 Alcohol dehydrogenase class-3

P28474 Alcohol dehydrogenase class-3

P32771 S-(hydroxymethyl)glutathione dehydrogenase

P46415 Alcohol dehydrogenase class-3

Q17335 Alcohol dehydrogenase class-3

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR002328	Alcohol dehydrogenase, zinc-containing, conserved site
IPR013149	Alcohol dehydrogenase, zinc-binding
IPR013154	Alcohol dehydrogenase GroES-like
IPR011032	GroES-like
IPR016040	NAD(P)-binding domain
IPR002085	Alcohol dehydrogenase superfamily, zinc-containing
IPR014183	Alcohol dehydrogenase class III/S-(hydroxymethyl)glutathione dehydrogenase
	SWISS-MODEL
	PDB Chain
	ModBase
	SCOP Domain
	CATH Domain

Publications Help

Additional Reading Open in usermanual
	Yang ZN, Bosron WF, Hurley TD. Structure of human chi chi alcohol dehydrogenase: a glutathione-dependent formaldehyde dehydrogenase. J. Mol. Biol. 265 1997 330-43 [PubMed: 9018047] http://dx.doi.org/10.1006/jmbi.1996.0731
	Sanghani PC, Bosron WF, Hurley TD. Human glutathione-dependent formaldehyde dehydrogenase. Structural changes associated with ternary complex formation. Biochemistry 41 2002 15189-94 [PubMed: 12484756] http://dx.doi.org/10.1021/bi026705q
	Sanghani PC, Davis WI, Zhai L, Robinson H. Structure-function relationships in human glutathione-dependent formaldehyde dehydrogenase. Role of Glu-67 and Arg-368 in the catalytic mechanism. Biochemistry 45 2006 4819-30 [PubMed: 16605250] http://dx.doi.org/10.1021/bi052554q
	Sanghani PC, Robinson H, Bennett-Lovsey R, Hurley TD, Bosron WF. Structure-function relationships in human Class III alcohol dehydrogenase (formaldehyde dehydrogenase). Chem. Biol. Interact. 143-144 2003 195-200 [PubMed: 12604204] http://dx.doi.org/10.1016/S0009-2797(02)00203-X
	Sanghani PC, Robinson H, Bosron WF, Hurley TD. Human glutathione-dependent formaldehyde dehydrogenase. Structures of apo, binary, and inhibitory ternary complexes. Biochemistry 41 2002 10778-86 [PubMed: 12196016] http://dx.doi.org/10.1021/bi0257639

InterPro 23.1