| 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 first (N-terminal) subdomain, which is found in:FAD-linked oxidases (N-terminal domain), such as vanillyl-alochol oxidase ( ) [ ], flavoprotein subunit of p-cresol methylhydroxylase () [ ], D-lactate dehydrogenases (, -cytochrome) [ ], Cholesterol oxidases () [ ], Cytokinin dehydrogenase 1 () [ ].Uridine diphospho-N-acetylenolpyruvylglucosamine reductase (MurB) (N-terminal domain) [ ].CO dehydrogenase flavoprotein (N-terminal domain; [ ]) family. | Name | FAD-binding, type PCMH, subdomain 1 |
| Short Name | FAD-bd_PCMH_sub1 | Type | Homologous_superfamily |
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