Protein Family Models

Family members were previously thought to be ArgK proteins acting as ATPase enzymes and kinases. They are now believed to be methylmalonyl Co-A mutase-associated GTPase MeaB. Structural studies of MeaB and the human ortholog (methylmalonyl associated protein A) MMAA, reveal alpha-helical domains at the N- and C-termini as well as a Ras-like GTPase domain. Mutational analysis of MeaB, show prohibited growth in Methylobacterium due to the inability to convert methylmalonyl-CoA to succinyl-CoA caused by an inactive form of methylmalonyl-CoA mutatase (mcm). In humans, mutations in (MMAA) are associated with the fatal disease methylmalonyl aciduria [1]. [1]. 25832174. Crystal structures of Mycobacterial MeaB and MMAA-like GTPases.. Edwards TE, Baugh L, Bullen J, Baydo RO, Witte P, Thompkins K,. Phan IQ, Abendroth J, Clifton MC, Sankaran B, Van Voorhis WC,. Myler PJ, Staker BL, Grundner C, Lorimer DD;. J Struct Funct Genomics. 2015;16:91-99. (from Pfam)

Date:

2024-08-14

ArgK/MeaB family GTPase such as human mitochondrial methylmalonic aciduria type A protein, mycobacterial methylmalonyl Co-A mutase-associated GTPase MeaB, and Escherichia coli GTPase ArgK

Date:

2018-03-02

In E. coli, mutation of this kinase blocks phosphorylation of two transporter system periplasmic binding proteins and consequently inhibits those transporters. This kinase is also found in Gram-positive bacteria, archaea, and the roundworm C. elegans. It may have a more general, but still unknown function. Mutations have also been found that do not phosphorylate the periplasmic binding proteins, yet still allow transport. The ATPase activity of this protein seems to be necessary, however.

Gene:

meaB

Date:

2024-05-30

Gene:

meaB

Date:

2021-07-30