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:

2024-08-14

This domain is found in NifU in combination with Pfam:PF01106. This domain is found on isolated in several bacterial species such as Swiss:O53156. The nif genes are responsible for nitrogen fixation. However this domain is found in bacteria that do not fix nitrogen, so it may have a broader significance in the cell than nitrogen fixation. These proteins appear to be scaffold proteins for iron-sulfur clusters [2]. [1]. 8875867. A modular domain of NifU, a nitrogen fixation cluster protein,. is highly conserved in evolution.. Hwang DM, Dempsey A, Tan KT, Liew CC;. J Mol Evol 1996;43:536-540.. [2]. 12970193. Components involved in assembly and dislocation of iron-sulfur. clusters on the scaffold protein Isu1p.. Muhlenhoff U, Gerber J, Richhardt N, Lill R;. EMBO J 2003;22:4815-4825. (from Pfam)

Date:

2024-08-14

This is an alignment of the carboxy-terminal domain. This is the only common region between the NifU protein from nitrogen-fixing bacteria and rhodobacterial species. The biochemical function of NifU is unknown [1]. [1]. 8048161. The modular structure of NifU proteins.. Ouzounis C, Bork P, Sander C;. Trends Biochem Sci 1994;19:199-200. (from Pfam)

Date:

2024-08-14

Three different but partially homologous Fe-S cluster assembly systems have been described: Isc, Suf, and Nif. The latter is associated with donation of an Fe-S cluster to nitrogenase in a number of nitrogen-fixing species. NifU, described here, consists of an N-terminal domain (PF01592) and a C-terminal domain (PF01106). Homologs with an equivalent domain archictecture from Helicobacter and Campylobacter, however, are excluded from this model by a high trusted cutoff. The model, therefore, is specific for NifU involved in nitrogenase maturation. The related model TIGR01999 homologous to the N-terminus of this model describes IscU from the Isc system as in E. coli, Saccharomyces cerevisiae, and Homo sapiens.

Gene:

nifU

Date:

2024-05-30

protein similar to nitrogen fixation protein NifU

Date:

2017-03-02