Protein Family Models

This family includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. The structure of the domain is an alpha-antiparallel beta sandwich. (from Pfam)

Date:

2024-08-14

Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters. (from Pfam)

Date:

2024-08-14

The key element of this family is the CX31-38CCX33-34CXXC sequence motif normally found at the C-terminus in archaeal and bacterial Hdr-like proteins [2]. There may be one or two copies, and the motif is probably an iron-sulfur binding cluster. In some instances one of the cysteines is replaced by an aspartate, and aspartate can in principle also function as a ligand of an iron-sulfur cluster [2]. The family includes a subunit from heterodisulphide reductase and a subunit from glycolate oxidase [1] Swiss:P52074 and glycerol-3-phosphate dehydrogenase. [1]. 8606183. glc locus of Escherichia coli: characterization of genes encoding the subunits of glycolate oxidase and the glc regulator protein. Pellicer MT, Badia J, Aguilar J, Baldoma L;. J Bacteriol 1996;178:2051-2059. [2]. 11952791. Purification and characterization of a membrane-bound enzyme complex from the sulfate-reducing archaeon Archaeoglobus fulgidus related to heterodisulfide reductase from methanogenic archaea. Mander GJ, Duin EC, Linder D, Stetter KO, Hedderich R;. Eur J Biochem. 2002;269:1895-1904. (from Pfam)

Date:

2024-10-16

This domain has a ferredoxin-like fold. [1]. 9141139. Crystallization and preliminary X-ray analysis of the flavoenzyme vanillyl-alcohol oxidase from Penicillium simplicissimum. Mattevi A, Fraaije MW, Coda A, van Berkel WJ;. Proteins 1997;27:601-603. (from Pfam)

Date:

2024-10-16

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]. [1]. 9261083. 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 1997;5:907-920. [2]. 8805513. 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 1996;4:47-54. (from Pfam)

Date:

2024-10-16

FAD-binding and (Fe-S)-binding domain-containing protein, where the N-terminal FAD-binding and the C-terminal (Fe-S)-binding domains may function as oxidoreductases

Date:

2024-08-05