Pathways & interactions
FAD-binding, type PCMH, subdomain 2 (IPR016169)
Short name: FAD-bd_PCMH_sub2
- Molybdopterin dehydrogenase, FAD-binding (IPR002346)
- UDP-N-acetylenolpyruvoylglucosamine reductase (IPR003170)
- Transporter-associated domain (IPR005170)
- 4-hydroxybenzoyl-CoA reductase, beta subunit (IPR017608)
- Xanthine dehydrogenase C subunit (IPR017612)
- Probable selenate reductase, FAD-binding subunit (IPR017698)
- FAD-binding, type PCMH-like superfamily (IPR036318)
According to structural similarities and conserved sequence motifs,FAD-binding domains have been grouped in three main families: (i) theferredoxin 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 alpha-beta subdomains: one is composed of three parallel beta-strands (B1-B3) surrounded by alpha-helices, and is packed against the second subdomain containing five antiparallel beta-strands (B4-B8) surrounded by alpha-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:18.104.22.168) [PMID: 15148401], subunit A of xanthine dehydrogenase (domain 3) (EC:22.214.171.124) [PMID: 11796116], medium subunit of quinoline 2-oxidoreductase (QorM) (EC:126.96.36.199) [PMID: 15296736], and the beta-subunit of 4-hydroxybenzoyl-CoA reductase (HrcB) (N-terminal domain) (EC:188.8.131.52) [PMID: 15576037].
- Uridine diphospho-N-acetylenolpyruvylglucosamine reductase (MurB) (N-terminal domain) [PMID: 9020778].
- G3DSA:3.30.465.10 (G3DSA:3.30.465.10)