Protein Family Models for Protein (Select 916698701) - Protein Family Models

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Select item 4304621.

HI0933-like protein barrel and H2TH domain

Date:: 2024-08-14

Family Accession:: NF046916.1
Method:: HMM

Select item 4214942.

FAD-dependent oxidoreductase

This family of proteins contains FAD dependent oxidoreductases and related proteins. (from Pfam)

Date:: 2024-08-14

Family Accession:: NF024240.5
Method:: HMM

Select item 4169533.

FAD-dependent oxidoreductase

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)

GO Terms:

Molecular Function:: oxidoreductase activity (GO:0016491)

Date:: 2024-08-14

Family Accession:: NF019604.5
Method:: HMM

Select item 4145874.

NAD(P)/FAD-dependent oxidoreductase

Date:: 2024-08-14

Family Accession:: NF015451.5
Method:: HMM

Select item 4120295.

FAD-dependent oxidoreductase

Date:: 2024-08-14

Family Accession:: NF013314.5
Method:: HMM

Select item 4115806.

FAD-dependent monooxygenase

This domain is involved in FAD binding in a number of enzymes. [1]. 1409567. Crystal structure of the reduced form of p-hydroxybenzoate. hydroxylase refined at 2.3A resolution.. Schreuder HA, van der Laan JM, Swarte MB, Kalk KH, Hol WG,. Drenth J;. Proteins 1992;14:178-190. (from Pfam)

GO Terms:

Molecular Function:: FAD binding (GO:0071949)

Date:: 2024-08-14

Family Accession:: NF013646.5
Method:: HMM

Select item 4111767.

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)

Date:: 2024-08-14

Family Accession:: NF013086.5
Method:: HMM

Select item 3996598.