InterPro domain: IPR012675

This superfamily represents a domain with a beta-grasp fold and a core structure consisting of beta(2)-alpha-beta(2), which is similar to that found in ubiquitin [ 1 ]. Domains with this type of structure are found in the 2Fe-2S ferredoxin family (including putidaredoxin and adrenodoxin) [ 2 ], the 2Fe-2S ferredoxin-related family (including aldehyde reductase, and xanthine dehydrogenase) [ 3 ], the TGS family (including threonyl-tRNA synthetase) [ 4 ] and the MoaD/ThiS family (including molybdopterin, and thiamine biosynthesis sulphur carrier protein) [ 5 ].

1. The prokaryotic antecedents of the ubiquitin-signaling system and the early evolution of ubiquitin-like beta-grasp domains. Genome Biol. 7, R60
2. Redox-dependent structural reorganization in putidaredoxin, a vertebrate-type [2Fe-2S] ferredoxin from Pseudomonas putida. J. Mol. Biol. 347, 607-21
3. Structure refinement of the aldehyde oxidoreductase from Desulfovibrio gigas (MOP) at 1.28 A. J. Biol. Inorg. Chem. 6, 791-800
4. The structure of threonyl-tRNA synthetase-tRNA(Thr) complex enlightens its repressor activity and reveals an essential zinc ion in the active site. Cell 97, 371-81
5. Structure of the Escherichia coli ThiS-ThiF complex, a key component of the sulfur transfer system in thiamin biosynthesis. Biochemistry 45, 11-9