InterPro domain: IPR027574

The TenA protein of Bacillus subtilis and Staphylococcus aureus [ 1 , 2 ], and the C-terminal region of trifunctional protein Thi20p from Saccharomyces cerevisiae [ 3 ], perform cleavages on thiamine and related compounds to produce 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP), a substrate of a salvage pathway for thiamine biosynthesis. The gene symbol tenA, for Transcription ENhancement A, reflects a misleading early characterisation as a regulatory protein. This family is related to PqqC from the PQQ biosynthesis system IPR011845 , heme oxygenase IPR016053 , and CADD (Chlamydia protein Associating with Death Domains), a putative folate metabolism enzyme IPR027572 .

1. Structural characterization of the regulatory proteins TenA and TenI from Bacillus subtilis and identification of TenA as a thiaminase II. Biochemistry 44, 2319-29
2. Purification, crystallization and preliminary X-ray diffraction analysis of the thiaminase type II from Staphylococcus aureus. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 67, 51-3
3. Involvement of thiaminase II encoded by the THI20 gene in thiamin salvage of Saccharomyces cerevisiae. FEMS Yeast Res. 8, 266-75