Protein Family Models

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:

2024-10-16

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)

Date:

2024-10-16

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

Members of this protein family are the A subunit, product of the glpA gene, of a three-subunit, membrane-anchored, FAD-dependent anaerobic glycerol-3-phosphate dehydrogenase.

Gene:

glpA

Date:

2024-05-28

anaerobic glycerol-3-phosphate dehydrogenase subunit A (GlpA) is part of the enzyme complex, composed of a catalytic dimer GlpA/B and a membrane-bound GlpC, that catalyzes the conversion of glycerol 3-phosphate to dihydroxyacetone

Date:

2023-02-17

Catalyzes the conversion of glycerol 3-phosphate to dihydroxyacetone using fumarate or nitrate as electron acceptor

Gene:

glpA

Date:

2021-08-26