Protein Family Models

ThiS (thiaminS) is a 66 aa protein involved in sulphur transfer Swiss:O32583. ThiS is coded in the thiCEFSGH operon in E. coli. This family of proteins have two conserved Glycines at the COOH terminus. Thiocarboxylate is formed at the last G in the activation process. Sulphur is transferred from ThiI to ThiS in a reaction catalysed by IscS [1]. MoaD, Swiss:P30748 a protein involved sulphur transfer in molybdopterin synthesis, is about the same length and shows limited sequence similarity to ThiS. Both have the conserved GG at the COOH end. [1]. 10781607. The iscS gene in Escherichia coli is required for the biosynthesis of 4-thiouridine, thiamin, and NAD. Lauhon CT, Kambampati R;. J Biol Chem 2000;275:20096-20103. (from Pfam)

Date:

2024-10-16

This HMM describes MoaD. It excludes archaeal homologs, since many Archaea have two MoaD-like proteins, suggesting two different functions. The Pfam HMM PF02597 describes both the thiamine biosynthesis protein ThiS and this protein, MoaD, a subunit (together with MoaE, Pfam:PF02391) of the molybdopterin converting factor. Both ThiS and MoaD are involved in sulfur transfer reactions. Distribution of this family appears limited to species that also have a member of PF02391, but a number of Archaea have two different members, suggesting functionally distinct subtypes. The C-terminal Gly-Gly of this model is critical to function.

Gene:

moaD

Date:

2021-04-27

molybdopterin synthase sulfur carrier subunit, a ubiquitin-like protein similar to MoaD, the small subunit of molybdopterin synthase, which contains a C-terminal thiocarboxylated glycine residue that serves as a sulfur donor for molybdopterin synthesis

Date:

2016-05-13

Catalyzes the conversion of molybdopterin precursor Z into molybdopterin

Gene:

moaD

Date:

2021-10-04