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PROSITE documentation PDOC00496

Pyridine nucleotide-disulphide oxidoreductases class-II active site

Description:

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.

Last update:

December 2004 / Pattern and text revised.

Technical section:

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:
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• 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]

References:

1 AuthorsKurlyan J., Krishna T.S.R., Wong L., Guenther B., Pahler A., Williams C.H. Jr., Model P.
SourceNature 352:172-174(1991).
2 AuthorsRussel M., Model P.
TitleSequence of thioredoxin reductase from Escherichia coli. Relationship to other flavoprotein disulfide oxidoreductases.
SourceJ. Biol. Chem. 263:9015-9019(1988).
PubMed ID3288628
3 AuthorsTartaglia L.A., Storz G., Brodsky M.H., Lai A., Ames B.N.
TitleAlkyl hydroperoxide reductase from Salmonella typhimurium. Sequence and homology to thioredoxin reductase and other flavoprotein disulfide oxidoreductases.
SourceJ. Biol. Chem. 265:10535-10540(1990).
PubMed ID2191951
4 AuthorsXu X.M., Koyama N., Cui M., Yamagishi A., Nosoh Y., Oshima T.
TitleNucleotide sequence of the gene encoding NADH dehydrogenase from an alkalophile, Bacillus sp. strain YN-1.
SourceJ. Biochem. 109:678-683(1991).
PubMed ID1917890
5 AuthorsMathieu I., Meyer J., Moulis J.M.
TitleCloning, sequencing and expression in Escherichia coli of the rubredoxin gene from Clostridium pasteurianum.
SourceBiochem. J. 285:255-262(1992).
PubMed ID1637309

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