| Description | According to structural similarities and conserved sequence motifs, FAD-binding domains have been grouped in three main families: (i) the ferredoxin reductase (FR)-type FAD-binding domain, (ii) the FAD-binding domains that adopt a Rossmann fold and (iii) the p-cresol methylhydroxylase (PCMH)-type FAD-binding domain [ ].The PCMH-type FAD-binding domain consists of two α-β subdomains: one is composed of three parallel β-strands (B1-B3) surrounded by α-helices, and is packed against the second subdomain containing five antiparallel β-strands (B4-B8) surrounded by α-helices [ ]. The two subdomains accommodate the FAD cofactor between them []. This superfamily represents the second (C-terminal) subdomain, which is found in:CO dehydrogenase flavoprotein (N-terminal domain; [ ]) family, which includes xanthine oxidase (domain 3) () [ ], subunit A of xanthine dehydrogenase (domain 3) () [ ], and the beta-subunit of 4-hydroxybenzoyl-CoA reductase (HrcB) (N-terminal domain) () [ ].Uridine diphospho-N-acetylenolpyruvylglucosamine reductase (MurB) (N-terminal domain) [ ].Magnesium and cobalt efflux protein CorC [ ].D-arabinono-1,4-lactone oxidase [ ].K(+)/H(+) antiporter NhaP2. | Name | FAD-binding, type PCMH, subdomain 2 |
| Short Name | FAD-bd_PCMH_sub2 | Type | Homologous_superfamily |
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