Pathways & interactions
FAD-binding, type PCMH, subdomain 1 (IPR016167)
Short name: FAD-bd_PCMH_sub1
- UDP-N-acetylenolpyruvoylglucosamine reductase (IPR003170)
- Oxygen oxidoreductase covalent FAD-binding site (IPR006093)
- FAD linked oxidase, N-terminal (IPR006094)
- Galactonolactone dehydrogenase (IPR010029)
- L-gulonolactone/D-arabinono-1,4-lactone oxidase (IPR010031)
- D-lactate dehydrogenase (IPR012256)
- FAD-binding domain, PCMH-type (IPR016166)
- Alkyldihydroxyacetonephosphate synthase (IPR025650)
- Sugar 1,4-lactone oxidase (IPR030654)
- 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 first (N-terminal) subdomain, which is found in:
- FAD-linked oxidases (N-terminal domain), such as vanillyl-alochol oxidase (EC:220.127.116.11) [PMID: 10585424], flavoprotein subunit of p-cresol methylhydroxylase (EC:18.104.22.168) [PMID: 15723539], D-lactate dehydrogenases (EC:22.214.171.124, EC:126.96.36.199 -cytochrome) [PMID: 10944213], Cholesterol oxidases (EC:188.8.131.52) [PMID: 11397813], Cytokinin dehydrogenase 1 (EC:184.108.40.206) [PMID: 15321719].
- Uridine diphospho-N-acetylenolpyruvylglucosamine reductase (MurB) (N-terminal domain) [PMID: 9020778].
- CO dehydrogenase flavoprotein (N-terminal domain; [PMID: 10966817]) family.
- G3DSA:220.127.116.11 (G3DSA:18.104.22.168)