Protein Family Models for Protein (Select 525765818) - Protein Family Models

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Select item 4214941.

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 4160812.

(2Fe-2S)-binding protein

The two Fe ions are each coordinated by two conserved cysteine residues. This domain occurs alone in small proteins such as Bacterioferritin-associated ferredoxin (BFD, Swiss:P13655). The function of BFD is not known, but it may may be a general redox and/or regulatory component involved in the iron storage or mobilisation functions of bacterioferritin in bacteria [1]. This domain is also found in nitrate reductase proteins in association with Nitrite and sulphite reductase 4Fe-4S domain [2] (Pfam:PF01077), Nitrite/Sulfite reductase ferredoxin-like half domain (Pfam:PF03460) and Pyridine nucleotide-disulphide oxidoreductase (Pfam:PF00070). It is also found in NifU nitrogen fixation proteins, in association with NifU-like N terminal domain (Pfam:PF01592) and NifU-like domain [3] (Pfam:PF01106). [1]. 8639572. A [2Fe-2S] protein encoded by an open reading frame upstream of. the Escherichia coli bacterioferritin gene.. Garg RP, Vargo CJ, Cui X, Kurtz DM Jr;. Biochemistry 1996;35:6297-6301.. [2]. 8954950. Spectroscopic and voltammetric characterisation of the. bacterioferritin-associated ferredoxin of Escherichia coli.. Quail MA, Jordan P, Grogan JM, Butt JN, Lutz M, Thomson AJ,. Andrews SC, Guest JR;. Biochem Biophys Res Commun 1996;229:635-642.. [3]. 9889981. Iron storage in bacteria.. Andrews SC;. Adv Microb Physiol 1998;40:281-351. (from Pfam)

Date:: 2024-08-14

Family Accession:: NF016230.5
Method:: HMM

Select item 4125313.

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 4115804.

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 4111765.

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 4001156.