Protein Family Models

This is the C-terminal domain of NADH rubredoxin oxidoreductase present in Clostridium acetobutylicum. The majority of obligatory anaerobes detoxify micro-aerobic environments by consuming O2 via H2O-forming NADH oxidase. This enzyme offers an alternate reaction pathway for scavenging of O2 and reactive oxygen species, wherein the reducing equivalent is obtained from NADH [1]. [1]. 20017214. Crystal structure of NADH:rubredoxin oxidoreductase from Clostridium acetobutylicum: a key component of the dioxygen scavenging system in obligatory anaerobes. Nishikawa K, Shomura Y, Kawasaki S, Niimura Y, Higuchi Y;. Proteins. 2010;78:1066-1070. (from Pfam)

Date:

2024-10-16

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)

Date:

2024-10-16

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

Sulfite and Nitrite reductases are key to both biosynthetic assimilation of sulfur and nitrogen and dissimilation of oxidised anions for energy transduction [1]. Two copies of this repeat are found in Nitrite and Sulfite reductases and form a single structural domain. [1]. 7569952. Sulfite reductase structure at 1.6 A: evolution and catalysis for reduction of inorganic anions. Crane BR, Siegel LM, Getzoff ED;. Science 1995;270:59-67. (from Pfam)

Date:

2024-10-16

Sulphite and nitrite reductases are vital in the biosynthetic assimilation of sulphur and nitrogen, respectfully. They are also both important for the dissimilation of oxidised anions for energy transduction. [1]. 7569952. Sulfite reductase structure at 1.6 A: evolution and catalysis for reduction of inorganic anions. Crane BR, Siegel LM, Getzoff ED;. Science 1995;270:59-67. [2]. 9315849. Probing the catalytic mechanism of sulfite reductase by X-ray crystallography: structures of the Escherichia coli hemoprotein in complex with substrates, inhibitors, intermediates, and products. Crane BR, Siegel LM, Getzoff ED;. Biochemistry 1997;36:12120-12137. (from Pfam)

Date:

2024-10-16

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)

Date:

2024-10-16

nitrite reductase NAD(P)H large subunit similar to NirB, part of the NirBD complex that catalyzes the reduction of nitrite to ammonia

Date:

2017-11-17

Gene:

nirB

Date:

2020-10-26