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HI0933-like protein barrel and H2TH domain
This entry represents two structural domains that are found inserted within a Rossmann domain. (from Pfam)
NAD(P)-binding protein
FAD-dependent oxidoreductase
This family of proteins contains FAD dependent oxidoreductases and related proteins. (from Pfam)
This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain. [1]. 8805537. Protein-protein interactions in the pyruvate dehydrogenase multienzyme complex: dihydrolipoamide dehydrogenase complexed with the binding domain of dihydrolipoamide acetyltransferase. Mande SS, Sarfaty S, Allen MD, Perham RN, Hol WG;. Structure 1996;4:277-286. (from Pfam)
NAD(P)/FAD-dependent oxidoreductase
This entry represents the Rossmann like domain in the HI0933 protein. (from Pfam)
FAD-binding protein
This family includes members that bind FAD. This family includes the flavoprotein subunits from succinate and fumarate dehydrogenase, aspartate oxidase and the alpha subunit of adenylylsulphate reductase. [1]. 8061609. Structure of glutathione reductase from Escherichia coli at 1.86 A resolution: comparison with the enzyme from human erythrocytes. Mittl PR, Schulz GE. Protein Sci 1994;3:799-809. (from Pfam)
NAD(P)/FAD-dependent oxidoreductase catalyzes the transfer of electrons from one molecule, the electron donor or reductant, to another molecule, the electron acceptor or oxidant
aminoacetone oxidase family FAD-binding enzyme
The model when searched with a partial length search brings in proteins with a dinucleotide-binding motif (Rossman fold) over the initial 40 residues of the model, including oxidoreductases and dehydrogenases. Partially characterized members include an FAD-binding protein from Bacillus cereus and flavoprotein HI0933 from Haemophilus influenzae.
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