TenA_C proteins similar to Staphylococcus aureus TenA (SaTenA)
This family of TenA proteins belongs to the TenA_C class as it has a conserved active site Cys residue; the double Glu residues identified in the active site of TenA_E from the archaeon Pyrococcus furiosus is conserved in this family. TenA_C proteins (EC 3.5.99.2) catalyze the hydrolysis of the thiamin breakdown product 4-amino-5-amino-methyl-2-methylpyrimidine (amino-HMP) to 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP) in a thiamin salvage pathway. This family includes Staphylococcus aureus TenA (SaTenA) which plays two essential roles in thiamin metabolism: in the deamination of aminopyrimidine to HMP, and in hydrolyzing thiamin into HMP and 5-(2-hydroxyethyl)4-methylthiazole (THZ). It has also been suggested that TenA proteins act as transcriptional regulators based on changes in gene-expression patterns when TenA is overexpressed in Bacillus subtilis, however this effect may be indirect. SaTenA is then also a putative transcriptional regulator controlling the secretion of extracellular proteases such as subtilisin-type proteases in bacteria. This family includes mostly uncharacterized TenA like proteins.
Feature 1: conserved active site residues [active site], 3 residue positions
Conserved feature residue pattern:E C E
Evidence:
Comment:these proteins have a conserved active site Cys residue, and 2 conserved Glu residues in the active site; the Cys is thought to act as a nucleophile in the thiaminase reaction, Glu are thought to interact with the substituent at the 5-position of the pyrimidine ring
Jiyao W et al.(2023). "The conserved domain database in 2023.",