PF01565

FAD binding domain

Pfam entry
Member databasePfam
Pfam typedomain
Short nameFAD_binding_4
ClanFAD_PCMH
Author Bashton M;0000-0002-6847-1525 Bateman A;0000-0002-6982-4660
Sequence Ontology0000417

Description

This family consists of various enzymes that use FAD as a co-factor, most of the enzymes are similar to oxygen oxidoreductase. One of the enzymes Vanillyl-alcohol oxidase (VAO) has a solved structure, the alignment includes the FAD binding site, called the PP-loop, between residues 99-110
[1]
. The FAD molecule is covalently bound in the known structure, however the residue that links to the FAD is not in the alignment. VAO catalyses the oxidation of a wide variety of substrates, ranging form aromatic amines to 4-alkylphenols. Other members of this family include D-lactate dehydrogenase, this enzyme catalyses the conversion of D-lactate to pyruvate using FAD as a co-factor; mitomycin radical oxidase, this enzyme oxidises the reduced form of mitomycins and is involved in mitomycin resistance. This family includes MurB an UDP-N-acetylenolpyruvoylglucosamine reductase enzyme EC:1.1.1.158. This enzyme is involved in the biosynthesis of peptidoglycan
[2]
.

References

1.Crystal structures and inhibitor binding in the octameric flavoenzyme vanillyl-alcohol oxidase: the shape of the active-site cavity controls substrate specificity. Mattevi A, Fraaije MW, Mozzarelli A, Olivi L, Coda A, van Berkel WJ. Structure 5, 907-20, (1997). View articlePMID: 9261083

2.The structure of the substrate-free form of MurB, an essential enzyme for the synthesis of bacterial cell walls. Benson TE, Walsh CT, Hogle JM. Structure 4, 47-54, (1996). View articlePMID: 8805513

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