| Comment | The TenA protein of Bacillus subtilis and Staphylococcus aurues, and the C-terminal region of trifunctional protein Thi20p from Saccharomyces cerevisiae, perform cleavages on thiamine and related compounds to produce 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP), a substrate a salvage pathway for thiamine biosynthesis. The gene symbol tenA, for Transcription ENhancement A, reflects a misleading early characterization as a regulatory protein. This family is related to PqqC from the PQQ biosynthesis system (see TIGR02111), heme oxygenase (PF01126), and CADD (Chlamydia protein Associating with Death Domains), a putative folate metabolism enzyme (see TIGR04305). |
| References | RN [1]
RM PMID:18028398
RT Involvement of thiaminase II encoded by the THI20 gene in thiamin salvage of Saccharomyces cerevisiae.
RA Onozuka M, Konno H, Kawasaki Y, Akaji K, Nosaka K
RL FEMS Yeast Res. 2008 Mar;8(2):266-75.
RN [2]
RM PMID:21206023
RT Purification, crystallization and preliminary X-ray diffraction analysis of the thiaminase type II from Staphylococcus aureus.
RA Begum A, Drebes J, Perbandt M, Wrenger C, Betzel C
RL Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Jan 1;67(Pt 1):51-3.
RN [3]
RM PMID:15709744
RT Structural characterization of the regulatory proteins TenA and TenI from Bacillus subtilis and identification of TenA as a thiaminase II.
RA Toms AV, Haas AL, Park JH, Begley TP, Ealick SE
RL Biochemistry. 2005 Feb 22;44(7):2319-29. |
