FAD-binding, type PCMH, subdomain 1

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 first (N-terminal) subdomain, which is found in: FAD-linked oxidases (N-terminal domain), such as vanillyl-alochol oxidase ([ec:1.1.3.38]) PMID:10585424, flavoprotein subunit of p-cresol methylhydroxylase ([ec:1.17.99.1]) PMID:15723539, D-lactate dehydrogenases ([ec:1.1.1.28], [ec:1.1.2.4] -cytochrome) PMID:10944213, Cholesterol oxidases ([ec:1.1.3.6]) PMID:11397813, Cytokinin dehydrogenase 1 ([ec:1.5.99.12]) PMID:15321719. Uridine diphospho-N-acetylenolpyruvylglucosamine reductase (MurB) (N-terminal domain) PMID:9020778. CO dehydrogenase flavoprotein (N-terminal domain; PMID:10966817) family.

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.

Download CSV (5 proteins: gene, accession, name)

• AGPS
• AOX1
• D2HGDH
• LDHD
• XDH