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The pyridine nucleotide-disulphide oxidoreductases are FAD flavoproteins which contains a pair of redox-active cysteines involved in the transfer of reducing equivalents from the FAD cofactor to the substrate. On the basis of sequence and structural similarities [1] these enzymes can be classified into two categories. The second category groups together the following enzymes:

• Bacterial and fungal thioredoxin reductase (EC 1.8.1.9) (gene trxB) [2].
• Salmonella typhimurium alkyl hydroperoxide reductase protein F52a (gene aphF) [3], an enzyme that serves to protect the cell against damage to DNA by alkyl hydroperoxides.
• NADH dehydrogenase (EC 1.6.99.3) from Bacillus strain YN-1 (gene ndh) [4].
• A probable oxidoreductase which is encoded in the Clostridium pasteurianum rubredoxin operon [5].
• Yeast hypothetical protein YHR106w.

The sequence around the two cysteines involved in the redox-active disulfide bond is conserved and can be used as a signature pattern.

December 2004 / Pattern and text revised.

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

PYRIDINE_REDOX_2, PS00573; Pyridine nucleotide-disulphide oxidoreductases class-II active site  (PATTERN)

Consensus pattern: C-x(2)-C-D-[GAS]-x(2,4)-[FYA]-x(4)-[LIVMAT]-x(0,1)-[LIVM](2)-[GI]-[GDS]-[GRD]-[DN] The two C's form the active site disulfide bond Sequences known to belong to this class detected by the pattern: ALL Other sequence(s) detected in Swiss-Prot: NONE

• Retrieve an alignment of 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 tree view of all Swiss-Prot/TrEMBL entries matching PS00573 • Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS00573 • Scan Swiss-Prot/TrEMBL entries against PS00573 • view ligand binding statistics

Matching PDB structures: 1CL0 1FL2 1HYU 1TDE ... [ALL]

1	Authors	Kurlyan J., Krishna T.S.R., Wong L., Guenther B., Pahler A., Williams C.H. Jr., Model P.
	Source	Nature 352:172-174(1991).

2	Authors	Russel M., Model P.
	Title	Sequence of thioredoxin reductase from Escherichia coli. Relationship to other flavoprotein disulfide oxidoreductases.
	Source	J. Biol. Chem. 263:9015-9019(1988).
	PubMed ID	3288628

3	Authors	Tartaglia L.A., Storz G., Brodsky M.H., Lai A., Ames B.N.
	Title	Alkyl hydroperoxide reductase from Salmonella typhimurium. Sequence and homology to thioredoxin reductase and other flavoprotein disulfide oxidoreductases.
	Source	J. Biol. Chem. 265:10535-10540(1990).
	PubMed ID	2191951

4	Authors	Xu X.M., Koyama N., Cui M., Yamagishi A., Nosoh Y., Oshima T.
	Title	Nucleotide sequence of the gene encoding NADH dehydrogenase from an alkalophile, Bacillus sp. strain YN-1.
	Source	J. Biochem. 109:678-683(1991).
	PubMed ID	1917890

5	Authors	Mathieu I., Meyer J., Moulis J.M.
	Title	Cloning, sequencing and expression in Escherichia coli of the rubredoxin gene from Clostridium pasteurianum.
	Source	Biochem. J. 285:255-262(1992).
	PubMed ID	1637309

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