FAD/NAD-linked reductase, dimerisation domain superfamily

Definition

This superfamily represents a dimerisation domain that is usually found at the C-terminal of FAD and NAD-linked reductases. This domain has a core α+β sandwich structure consisting of beta(3,4)-alpha(3). The first two domains are of the same β/β/α fold. This domain can be found in the following proteins: Glutathione reductase PMID:9546215. Trypanothione reductase PMID:8771196. Mammalian thioredoxin reductase PMID:11481439. Apoptosis-inducing factor (AIF), which contains a large loop insertion in this domain PMID:12198487. NADH peroxidase PMID:7766608. Biphenyl 2,3-dioxygenase, ferredoxin reductase (also known as NADH-dependent ferredoxin reductase, BphA4) PMID:11090282. Putidaredoxin reductase PMID:15095867. Dihydrolipoyl dehydrogenase (also known as dihydrolipoamide dehydrogenase) PMID:8805537. 2-oxopropyl-CoM reductase, carboxylating (also known as NADH-dependent 2-ketopropyl coenzyme M oxidoreductase/carboxylase) PMID:12390015. The flavin-binding subunit of flavocytochrome c sulphide dehydrogenase (FCSD) PMID:7939681. NADH oxidase /nitrite reductase.

8 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.

Download CSV (8 proteins: gene, accession, name)

• AIFM1
• AIFM3
• DLD
• GSR
• PYROXD1
• TXNRD1
• TXNRD2
• TXNRD3