Protein Family Models

This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate (TPP) synthesis pathway, TPP is an essential cofactor for many enzymes [1]. [1]. 9244280. Identification and characterization of an operon in Salmonella typhimurium involved in thiamine biosynthesis. Petersen LA, Downs DM;. J Bacteriol 1997;179:4894-4900. (from Pfam)

Date:

2024-10-16

Members of this family are found in all the three major phyla of life: archaebacteria, eubacteria, and eukaryotes. In Bacillus subtilis, TENA is one of a number of proteins that enhance the expression of extracellular enzymes, such as alkaline protease, neutral protease and levansucrase [1]. The THI-4 protein, which is involved in thiamine biosynthesis, is also a member of this family. The C-terminal part of these proteins consistently show significant sequence similarity to TENA proteins. This similarity was first noted with the Neurospora crassa THI-4 [2]. This family includes bacterial coenzyme PQQ synthesis protein C or PQQC proteins. Pyrroloquinoline quinone (PQQ) is the prosthetic group of several bacterial enzymes,including methanol dehydrogenase of methylotrophs and the glucose dehydrogenase of a number of bacteria [3]. PQQC has been found to be required in the synthesis of PQQ but its function is unclear. The exact molecular function of members of this family is uncertain. [1]. 1898926. Cloning and characterization of a pair of novel genes that regulate production of extracellular enzymes in Bacillus subtilis. Pang AS, Nathoo S, Wong SL;. J Bacteriol 1991;173:46-54. [2]. 8662211. Molecular cloning of thi-4, a gene necessary for the biosynthesis of thiamine in Neurospora crassa. Akiyama M, Nakashima H;. Curr Genet 1996;30:62-67. [3]. 12437981. PqqC/D, which converts a biosynthetic intermediate to pyrroloquinoline quinone. Toyama H, Fukumoto H, Saeki M, Matsushita K, Adachi O, Lidstrom ME;. Biochem Biophys Res Commun 2002;299:268-272. (from Pfam)

Date:

2024-10-16

This family is related to Pfam:PF02110 and Pfam:PF00294 implying that it also is a carbohydrate kinase. (personal obs Yeats C). (from Pfam)

Date:

2024-08-14

Date:

2021-03-12

This HMM represents a bifunctional enzyme, phosphomethylpyrimidine kinase (EC 2.7.4.7)/Hydroxymethylpyrimidine kinase (EC 2.7.1.49), the ThiD/J protein of thiamine biosynthesis. The protein is commonly observed within operons containing other thiamine biosynthesis genes. Numerous examples are fusion proteins with other thiamine-biosynthetic domains. Saccaromyces has three recent paralogs, two of which are isofunctional and score above the trusted cutoff. The third shows a longer branch length in a phylogenetic tree and scores below the trusted cutoff, as do putative second copies in a number of species.

Gene:

thiD

Date:

2021-04-27