Protein Family Models for Protein (Select 499349791) - Protein Family Models

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Select item 4240321.

NAD(P)-binding protein

Date:: 2024-08-14

Family Accession:: NF024842.5
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:: 2024-10-16

Family Accession:: NF019604.5
Method:: HMM

Select item 4152854.

tryptophan 7-halogenase

Tryptophan halogenase catalyses the chlorination of tryptophan to form 7-chlorotryptophan. This is the first step in the biosynthesis of pyrrolnitrin, an antibiotic with broad-spectrum anti-fungal activity. Tryptophan halogenase is NADH-dependent [1]. [1]. 10547442. Conservation of the pyrrolnitrin biosynthetic gene cluster among six pyrrolnitrin-producing strains. Hammer PE, Burd W, Hill DS, Ligon JM, van Pee K;. FEMS Microbiol Lett 1999;180:39-44. (from Pfam)

GO Terms:

Molecular Function:: monooxygenase activity (GO:0004497)

Date:: 2024-10-16

Family Accession:: NF016693.5
Method:: HMM

Select item 4125315.

FAD-dependent oxidoreductase

This family includes various FAD dependent oxidoreductases: Glycerol-3-phosphate dehydrogenase EC:1.1.99.5, Sarcosine oxidase beta subunit EC:1.5.3.1, D-alanine oxidase EC:1.4.99.1, D-aspartate oxidase EC:1.4.3.1. [1]. 9153426. Active site plasticity in D-amino acid oxidase: a crystallographic analysis. Todone F, Vanoni MA, Mozzarelli A, Bolognesi M, Coda A, Curti B, Mattevi A;. Biochemistry 1997;36:5853-5860. (from Pfam)

GO Terms:

Molecular Function:: oxidoreductase activity (GO:0016491)

Date:: 2024-10-16

Family Accession:: NF013434.5
Method:: HMM

Select item 4120296.

FAD-dependent oxidoreductase

Date:: 2024-08-14

Family Accession:: NF013314.5
Method:: HMM

Select item 4115807.

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:: 2024-10-16

Family Accession:: NF013646.5
Method:: HMM

Select item 4111768.

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:: 2024-10-16

Family Accession:: NF013086.5
Method:: HMM

Select item 4001159.