PbH1 Parallel beta-helix repeats
SMART ACC:	SM000710
Description:	The tertiary structures of pectate lyases and rhamnogalacturonase A show a stack of parallel beta strands that are coiled into a large helix. Each coil of the helix represents a structural repeat that, in some homologues, can be recognised from sequence information alone. Conservation of asparagines might be connected with asparagine-ladders that contribute to the stability of the fold. Proteins containing these repeats most often are enzymes with polysaccharide substrates.
InterPro ACC:	IPR006626
InterPro abstract:	The tertiary structures of pectate lyases and rhamnogalacturonase A show a stack of parallel β-strands that are coiled into a large helix. Each coil of the helix represents a structural repeat that, in some homologues, can be recognised from sequence information alone. Conservation of asparagines might be connected with asparagine-ladders that contribute to the stability of the fold. Proteins … expand The tertiary structures of pectate lyases and rhamnogalacturonase A show a stack of parallel β-strands that are coiled into a large helix. Each coil of the helix represents a structural repeat that, in some homologues, can be recognised from sequence information alone. Conservation of asparagines might be connected with asparagine-ladders that contribute to the stability of the fold. Proteins containing these repeats most often are enzymes with polysaccharide substrates [ PUBMED:9724625 ]. collapse
Family alignment:	View the Family alignment or the Alignment consensus sequence
There are 585 506 PbH1 domains in 92 548 proteins in SMART's NRDB database.

Taxonomic distribution of proteins containing PbH1 domains

The tree below includes only several representative species and genera. The complete taxonomic breakdown of all proteins containing PbH1 domains can be accessed here. Click the counts or percentage values to display the corresponding proteins.

Predicted cellular role

Binding / catalysis:	Polysaccharide hydrolysis

Relevant references for this domain

Primary literature for the PbH1 domain is listed below. Automatically-derived, secondary literature is also available.

KEGG pathways involving proteins which contain this domain

This information is based on the mapping of SMART genomic protein database to KEGG orthologous groups. Percentages are related to the number of proteins containing a PbH1 domain which could be assigned to a KEGG orthologous group, and not all proteins containing PbH1 domains. Please note that proteins can be included in multiple pathways, ie. the numbers below will not add to 100%.

KEGG pathways

Some of these pathways are included in the interactive Pathways Explorer overview maps. Select an overview map and click the button below to highlight them in iPath.

KEGG orthologous groups

Some of these KOs are included in the interactive Pathways Explorer overview maps. Select an overview map and click the button below to highlight them in iPath.

3D structures in PDB containing this domain

Links to other resources describing this domain

InterPro	IPR006626