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	PROSITE documentation PDOC00058

Zinc-containing alcohol dehydrogenases signatures

Alcohol dehydrogenase (EC 1.1.1.1) (ADH) catalyzes the reversible oxidation of ethanol to acetaldehyde with the concomitant reduction of NAD [1]. Currently three, structurally and catalytically, different types of alcohol dehydrogenases are known:

• Zinc-containing 'long-chain' alcohol dehydrogenases.
• Insect-type, or 'short-chain' alcohol dehydrogenases.
• Iron-containing alcohol dehydrogenases.

Zinc-containing ADH's [2,3] are dimeric or tetrameric enzymes that bind two atoms of zinc per subunit. One of the zinc atom is essential for catalytic activity while the other is not. Both zinc atoms are coordinated by either cysteine or histidine residues; the catalytic zinc is coordinated by two cysteines and one histidine. Zinc-containing ADH's are found in bacteria, mammals, plants, and in fungi. In most species there are more than one isozyme (for example, human have at least six isozymes, yeast have three, etc.). A number of other zinc-dependent dehydrogenases are closely related to zinc ADH [4], these are:

• Xylitol dehydrogenase (EC 1.1.1.9) (D-xylulose reductase).
• Sorbitol dehydrogenase (EC 1.1.1.14).
• Aryl-alcohol dehydrogenase (EC 1.1.1.90) (benzyl alcohol dehydrogenase).
• L-threonine 3-dehydrogenase (EC 1.1.1.103).
• Cinnamyl-alcohol dehydrogenase (EC 1.1.1.195) (CAD) [5]. CAD is a plant enzyme involved in the biosynthesis of lignin.
• Galactitol-1-phosphate 5-dehydrogenase (EC 1.1.1.251).
• Escherichia coli L-idonate 5-dehydrogenase (EC 1.1.1.264).
• Pseudomonas putida 5-exo-alcohol dehydrogenase (EC 1.1.1.-) [6].
• Escherichia coli starvation sensing protein rspB.
• Escherichia coli hypothetical protein yjgB.
• Escherichia coli hypothetical protein yjgV.
• Escherichia coli hypothetical protein yjjN.
• Yeast hypothetical protein YAL060w (FUN49).
• Yeast hypothetical protein YAL061w (FUN50).
• Yeast hypothetical protein YCR105w.

The pattern that we developed to detect this class of enzymes is based on a conserved region that includes a histidine residue which is the second ligand of the catalytic zinc atom.

This family also includes NADP-dependent quinone oxidoreductase (EC 1.6.5.5), an enzyme found in bacteria (gene qor), in yeast and in mammals where, in some species such as rodents, it has been recruited as an eye lens protein and is known as zeta-crystallin [7]. The sequence of quinone oxidoreductase is distantly related to that other zinc-containing alcohol dehydrogenases and it lacks the zinc-ligand residues. The torpedo fish and mammlian synaptic vesicle membrane protein vat-1 is realted to qor. We have developed a specific pattern for this subfamily.

Expert(s) to contact by email:

Joernvall H.
Persson B.

Last update:

April 2006 / Patterns revised.

PROSITE methods (with tools and information) covered by this documentation:

ADH_ZINC, PS00059; Zinc-containing alcohol dehydrogenases signature  (PATTERN)

• Consensus pattern:
  G-H-E-x-{EL}-G-{AP}-x(4)-[GA]-x(2)-[IVSAC]
  H is a zinc ligand
• Sequences in UniProtKB/Swiss-Prot known to belong to this class: 547
  • detected by PS00059: 491 (true positives)
  • undetected by PS00059: 56 (49 false negatives and 7 'partials')
• Other sequence(s) in UniProtKB/Swiss-Prot detected by PS00059:
  13 false positives.
• Retrieve an alignment of UniProtKB/Swiss-Prot true positive hits:
  Clustal format, color, condensed view  /  Clustal format, color  /  Clustal format, plain text  /  Fasta format
• Retrieve the sequence logo from the alignment
• Taxonomic distribution of all UniProtKB (Swiss-Prot + TrEMBL) entries matching PS00059
• Retrieve a list of all UniProtKB (Swiss-Prot + TrEMBL) entries matching PS00059
• Scan UniProtKB (Swiss-Prot and/or TrEMBL) entries against PS00059
• View ligand binding statistics of PS00059
• Matching PDB structures: 1A71 1A72 1ADB 1ADC ... [ALL]

QOR_ZETA_CRYSTAL, PS01162; Quinone oxidoreductase / zeta-crystallin signature  (PATTERN)

• Consensus pattern:
  [GSDN]-[DEQHKM]-x(2)-L-x(3)-[SAG](2)-G(2)-x-G-x(4)-Q-x(2)-[KRS]
• Sequences in UniProtKB/Swiss-Prot known to belong to this class: 50
  • detected by PS01162: 46 (true positives)
  • undetected by PS01162: 4 (4 false negatives and 0 'partial')
• Other sequence(s) in UniProtKB/Swiss-Prot detected by PS01162:
  NONE.
• Retrieve an alignment of UniProtKB/Swiss-Prot true positive hits:
  Clustal format, color, condensed view  /  Clustal format, color  /  Clustal format, plain text  /  Fasta format
• Retrieve the sequence logo from the alignment
• Taxonomic distribution of all UniProtKB (Swiss-Prot + TrEMBL) entries matching PS01162
• Retrieve a list of all UniProtKB (Swiss-Prot + TrEMBL) entries matching PS01162
• Scan UniProtKB (Swiss-Prot and/or TrEMBL) entries against PS01162
• View ligand binding statistics of PS01162
• Matching PDB structures: 1QOR 1YB5 2C0C 2VN8 ... [ALL]

1	Authors	Branden C.-I., Joernvall H., Eklund H., Furugren B.
	Source	(In) The Enzymes (3rd edition) 11:104-190(1975).

2	Authors	Joernvall H., Persson B., Jeffery J.
	Source	Eur. J. Biochem. 167:195-201(1987).

3	Authors	Sun H.-W., Plapp B.V.
	Title	Progressive sequence alignment and molecular evolution of the Zn-containing alcohol dehydrogenase family.
	Source	J. Mol. Evol. 34:522-535(1992).
	PubMed ID	1593644

4	Authors	Persson B., Hallborn J., Walfridsson M., Hahn-Hagerdal B., Keranen S., Penttila M., Jornvall H.
	Title	Dual relationships of xylitol and alcohol dehydrogenases in families of two protein types.
	Source	FEBS Lett. 324:9-14(1993).
	PubMed ID	8504864

5	Authors	Knight M.E., Halpin C., Schuch W.
	Title	Identification and characterisation of cDNA clones encoding cinnamyl alcohol dehydrogenase from tobacco.
	Source	Plant Mol. Biol. 19:793-801(1992).
	PubMed ID	1643282

6	Authors	Koga H., Aramaki H., Yamaguchi E., Takeuchi K., Horiuchi T., Gunsalus I.C.
	Title	camR, a negative regulator locus of the cytochrome P-450cam hydroxylase operon.
	Source	J. Bacteriol. 166:1089-1095(1986).
	PubMed ID	3011733

7	Authors	Joernvall H., Persson B., Du Bois G., Lavers G.C., Chen J.H., Gonzalez P., Rao P.V., Zigler J.S. Jr.
	Source	FEBS Lett. 322:240-244(1993).

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