FAD-binding, type PCMH, subdomain 2
IPR016169
Definition
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 PMID:11514662. 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 PMID:10623531. The two subdomains accommodate the FAD cofactor between them PMID:10694883. This superfamily represents the second (C-terminal) subdomain, which is found in: CO dehydrogenase flavoprotein (N-terminal domain; PMID:10966817) family, which includes xanthine oxidase (domain 3) ([ec:1.17.3.2]) PMID:15148401, subunit A of xanthine dehydrogenase (domain 3) ([ec:1.17.1.4]) PMID:11796116, and the beta-subunit of 4-hydroxybenzoyl-CoA reductase (HrcB) (N-terminal domain) ([ec:1.3.99.20]) PMID:15576037. Uridine diphospho-N-acetylenolpyruvylglucosamine reductase (MurB) (N-terminal domain) PMID:9020778. Magnesium and cobalt efflux protein CorC PMID:1779764. D-arabinono-1,4-lactone oxidase PMID:10094636. K(+)/H(+) antiporter NhaP2.
6 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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