|PROSITE documentation PDOC51464 [for PROSITE entry PS51464]|
The sugar isomerase (SIS) domain is a phosphosugar-binding module that is found in a variety of eubacterial, archaebacterial and eukaryotic proteins that have a role in phosphosugar isomerization or regulation . In enzymes, the SIS domain can have a catalytic function as an isomerase and bind to phosphorylated sugars. In bacterial transcriptional regulators of the rpiR family, the domain seems to bind substrates implicated in the genes for sugar metabolism that are controlled by the regulator. The SIS domain is found in one or two copies and can be linked to additional domains, such as helix-turn-helix (HTH) (see <PDOC51071>), CBS (see <PDOC51371>), glutamine amidotransferases type 2 (see <PDOC00406>), or phosphopantetheine-attachment (see <PDOC00012>) [1,2].
The SIS domain has an α-β structure and is dominated by a five-stranded parallel β sheet flanked on either side by α helices forming a three-layer α-β-α sandwich (see <PDB:1MOQ>) . The fold shows similarities to that of glucose-6-phosphate isomerase (see <PDOC00157>).
Some proteins known to contain a SIS domain are listed below:
The profile we developed covers the entire SIS domain.Last update:
September 2009 / First entry.
PROSITE method (with tools and information) covered by this documentation:
|Title||The SIS domain: a phosphosugar-binding domain.|
|Source||Trends Biochem. Sci. 24:94-95(1999).|
|2||Authors||Jaeger T., Mayer C.|
|Title||N-acetylmuramic acid 6-phosphate lyases (MurNAc etherases): role in cell wall metabolism, distribution, structure, and mechanism.|
|Source||Cell. Mol. Life Sci. 65:928-939(2008).|
|3||Authors||Teplyakov A., Obmolova G., Badet-Denisot M.A., Badet B., Polikarpov I.|
|Title||Involvement of the C terminus in intramolecular nitrogen channeling in glucosamine 6-phosphate synthase: evidence from a 1.6 A crystal structure of the isomerase domain.|