Arg_repressor_C

• PFAM accession number: PF02863
• Interpro abstract (IPR020899):

  The arginine dihydrolase (AD) pathway is found in many prokaryotes and some primitive eukaryotes, an example of the latter being Giardia lamblia (Giardia intestinalis) [ (PUBMED:9504342) ]. The three-enzyme anaerobic pathway breaks down L-arginine to form 1 mol of ATP, carbon dioxide and ammonia. In simpler bacteria, the first enzyme, arginine deiminase, can account for up to 10% of total cell protein [ (PUBMED:9504342) ].

  Most prokaryotic arginine deiminase pathways are under the control of a repressor gene, termed ArgR [ (PUBMED:1583685) ]. This is a negative regulator, and will only release the arginine deiminase operon for expression in the presence of arginine [ (PUBMED:9851988) ]. The crystal structure of apo-ArgR from Bacillus stearothermophilus has been determined to 2.5A by means of X-ray crystallography [ (PUBMED:10331868) ]. The protein exists as a hexamer of identical subunits, and is shown to have six DNA-binding domains, clustered around a central oligomeric core when bound to arginine. It predominantly interacts with A.T residues in ARG boxes. This hexameric protein binds DNA at its N terminus to repress arginine biosyntheis or activate arginine catabolism. Some species have several ArgR paralogs. In a neighbour-joining tree, some of these paralogous sequences show long branches and differ significantly from the well-conserved C-terminal region.

  The C-terminal domain of the arginine repressor is responsible for aginine binding and multimerisation [ (PUBMED:11856827) (PUBMED:9334747) ].

• GO process: protein complex oligomerization (GO:0051259)
• GO function: arginine binding (GO:0034618)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Arg_repressor_C