Protein Domain : IPR020900

Type:  Domain Name:  Arginine repressor, DNA-binding domain
Description:  The arginine dihydrolase (AD) pathway is found in many prokaryotes and some primitive eukaryotes, an example of the latter being Giardia lamblia(Giardia intestinalis) []. 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 [].Most prokaryotic arginine deiminase pathways are under the control of a repressor gene, termed ArgR []. This is a negative regulator, and will only release the arginine deiminase operon for expression in the presence of arginine []. The crystal structure of apo-ArgR from Bacillus stearothermophilushas been determined to 2.5A by means of X-ray crystallography []. 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. Short Name:  Arg_repress_DNA-bd

0 Child Features

0 Contains

1 Cross References

Identifier
PF01316

1 Found In

DB identifier Type Name
IPR001669 Family Arginine repressor

3 GO Annotations

GO Term Gene Name
GO:0003700 IPR020900
GO:0006355 IPR020900
GO:0006525 IPR020900

3 Ontology Annotations

GO Term Gene Name
GO:0003700 IPR020900
GO:0006355 IPR020900
GO:0006525 IPR020900

1 Parent Features

DB identifier Type Name
IPR011991 Domain Winged helix-turn-helix DNA-binding domain

0 Proteins

4 Publications

First Author Title Year Journal Volume Pages PubMed ID
            9504342
            9851988
            1583685
            10331868