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	PROSITE documentation PDOC00073

Pyridine nucleotide-disulphide oxidoreductases class-I active site

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 first category groups together the following enzymes [2,3,4,5,6]:

• Glutathione reductase (EC 1.8.1.7) (GR).
• Higher eukaryotes thioredoxin reductase (EC 1.8.1.9).
• Trypanothione reductase (EC 1.8.1.12).
• Lipoamide dehydrogenase (EC 1.8.1.4), the E3 component of α-ketoacid dehydrogenase complexes.
• Mercuric reductase (EC 1.16.1.1).

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

Note:

In positions 6 and 7 of the pattern all known sequences have Asn-(Val/ Ile) with the exception of GR from plant chloroplasts and from cyanobacteria which have Ile-Arg [7].

Last update:

May 2004 / Text revised.

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

PYRIDINE_REDOX_1, PS00076; Pyridine nucleotide-disulphide oxidoreductases class-I active site  (PATTERN)

• Consensus pattern:
  G-G-x-C-[LIVA]-x(2)-G-C-[LIVM]-P
  The 2 C's form the active site disulfide bond
• Sequences in UniProtKB/Swiss-Prot known to belong to this class: 151
  • detected by PS00076: 147 (true positives)
  • undetected by PS00076: 4 (1 false negative and 3 'partials')
• Other sequence(s) in UniProtKB/Swiss-Prot detected by PS00076:
  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 PS00076
• Retrieve a list of all UniProtKB (Swiss-Prot + TrEMBL) entries matching PS00076
• Scan UniProtKB (Swiss-Prot and/or TrEMBL) entries against PS00076
• View ligand binding statistics of PS00076
• Matching PDB structures: 1AOG 1BWC 1BZL 1DXL ... [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	Rice D.W., Schulz G.E., Guest J.R.
	Title	Structural relationship between glutathione reductase and lipoamide dehydrogenase.
	Source	J. Mol. Biol. 174:483-496(1984).
	PubMed ID	6546954

3	Authors	Brown N.L.
	Source	Trends Biochem. Sci. 10:400-402(1985).

4	Authors	Carothers D.J., Pons G., Patel M.S.
	Title	Dihydrolipoamide dehydrogenase: functional similarities and divergent evolution of the pyridine nucleotide-disulfide oxidoreductases.
	Source	Arch. Biochem. Biophys. 268:409-425(1989).
	PubMed ID	2643922

5	Authors	Walsh C.T., Bradley M., Nadeau K.
	Title	Molecular studies on trypanothione reductase, a target for antiparasitic drugs.
	Source	Trends Biochem. Sci. 16:305-309(1991).
	PubMed ID	1957352

6	Authors	Gasdaska P.Y., Gasdaska J.R., Cochran S., Powis G.
	Title	Cloning and sequencing of a human thioredoxin reductase.
	Source	FEBS Lett. 373:5-9(1995).
	PubMed ID	7589432

7	Authors	Creissen G., Edwards E.A., Enard C., Wellburn A., Mullineaux P.
	Title	Molecular characterization of glutathione reductase cDNAs from pea (Pisum sativum L.).
	Source	Plant J. 2:129-131(1992).
	PubMed ID	1303792

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