Protein Family Models

A member of the nucleic acid/nucleotide deaminase superfamily prototyped by Neisseria MafB19 [1]. Members of this family are present in a wide phyletic range of bacteria and are predicted to function as toxins in bacterial polymorphic toxin systems [1]. [1]. 21890906. Evolution of the deaminase fold and multiple origins of. eukaryotic editing and mutagenic nucleic acid deaminases from. bacterial toxin systems.. Iyer LM, Zhang D, Rogozin IB, Aravind L;. Nucleic Acids Res. 2011; [Epub ahead of print] (from Pfam)

Date:

2024-08-14

The function of this domain is not known, but it is thought to be involved in riboflavin biosynthesis. This domain is found in the C terminus of RibD/RibG Swiss:P25539, in combination with Pfam:PF00383, as well as in isolation in some archaebacterial proteins Swiss:P95872. This family appears to be related to Pfam:PF00186. (from Pfam)

Date:

2024-08-14

Date:

2024-08-14

bifunctional diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6-(5-phosphoribosylamino)uracil reductase catalyzes steps in the riboflavin biosynthesis pathway

Date:

2017-02-03

Riboflavin biosynthesis protein which catalyzes the deamination and reduction steps in the riboflavin biosynthesis pathway; catalyzes the formation of 5-amino-6-(5-phosphoribosylamino)uracil from 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine and the formation of 5-amino-6-(5-phosphoribosylamino)uracil from 5-amino-6-(5-phosphoribitylamino)uracil

Gene:

ribD

Date:

2021-08-26

This HMM describes the ribD protein as found in Escherichia coli. The N-terminal domain includes the conserved zinc-binding site region captured in the HMM dCMP_cyt_deam and shared by proteins such as cytosine deaminase, mammalian apolipoprotein B mRNA editing protein, blasticidin-S deaminase, and Bacillus subtilis competence protein comEB. The C-terminal domain is homologous to the full length of yeast HTP reductase, a protein required for riboflavin biosynthesis. A number of archaeal proteins believed related to riboflavin biosynthesis contain only this C-terminal domain and are not found as full-length matches to this model.

Gene:

ribD

Date:

2021-04-27

Eubacterial riboflavin-specific deaminases have a zinc-binding domain recognized by the dCMP_cyt_deam HMM toward the N-terminus and this domain toward the C-terminus. Yeast HTP reductase, a riboflavin-biosynthetic enzyme, and several archaeal proteins believed related to riboflavin biosynthesis consist only of this domain and lack the dCMP_cyt_deam domain.

Date:

2024-05-30