Protein Domain : Pyridine nucleotide-disulphide oxidoreductase, class I, active site IPR012999

Type  Active_site
Description  The pyridine nucleotide-disulphide oxidoreductases are FAD flavoproteins which contain 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 [ ] these enzymes can be classified into two categories. The first category groups together the following enzymes [, , , ]:Glutathione reductase ( ) (GR). Higher eukaryotes thioredoxin reductase ( ). Trypanothione reductase ( ). Lipoamide dehydrogenase ( ), the E3 component of alpha-ketoacid dehydrogenase complexes. Mercuric reductase ( ). The sequence around the two cysteines involved in the redox-active disulphide 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 [ ].
Short Name  Pyr_OxRdtase_I_AS

0 Child Features

0 Gene Families

493 Genes

1 Ontology Annotations

0 Parent Features

13 Publications

USDA
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