Pyridine nucleotide-disulphide oxidoreductase, class I, active site
IPR012999
Definition
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 PMID:2067578 these enzymes can be classified into two categories. The first category groups together the following enzymes [[cite:PMID:6546954], [cite:PMID:2643922], [cite:PMID:1957352], [cite:PMID:7589432]]: 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 alpha-ketoacid dehydrogenase complexes. Mercuric reductase ([ec:1.16.1.1]). 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 PMID:1303792.
5 human proteins with this domain
Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.
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