Protein Family Models for Protein (Select 640552027) - Protein Family Models

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 4125953.

FAD-dependent oxidoreductase

This family consists of various amine oxidases, including maze polyamine oxidase (PAO) [1] and various flavin containing monoamine oxidases (MAO). The aligned region includes the flavin binding site of these enzymes. The family also contains phytoene dehydrogenases and related enzymes. In vertebrates MAO plays an important role regulating the intracellular levels of amines via there oxidation; these include various neurotransmitters, neurotoxins and trace amines [2]. In lower eukaryotes such as aspergillus and in bacteria the main role of amine oxidases is to provide a source of ammonium [3]. PAOs in plants, bacteria and protozoa oxidase spermidine and spermine to an aminobutyral, diaminopropane and hydrogen peroxide and are involved in the catabolism of polyamines [1]. Other members of this family include tryptophan 2-monooxygenase, putrescine oxidase, corticosteroid binding proteins and antibacterial glycoproteins. [1]. 9598979. Maize polyamine oxidase: primary structure from protein and cDNA. sequencing.. Tavladoraki P, Schinina ME, Cecconi F, Agostino SD, Manera F,. Rea G, Mariottini P, Federico R, Angelini R;. FEBS Lett 1998;426:62-66.. [2]. 9162023. A key amino acid responsible for substrate selectivity of. monoamine oxidase A and B.. Tsugeno Y, Ito A;. J Biol Chem 1997;272:14033-14036.. [3]. 7770050. Cloning, sequencing and heterologous expression of the monoamine. oxidase gene from Aspergillus niger.. Schilling B, Lerch K;. Mol Gen Genet 1995;247:430-438. (from Pfam)

GO Terms:

Molecular Function:: oxidoreductase activity (GO:0016491)

Date:: 2024-08-14

Family Accession:: NF013739.5
Method:: HMM

Select item 4125314.

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:: 2024-08-14

Family Accession:: NF013434.5
Method:: HMM

Select item 4115805.

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 4111766.

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 4001157.