UniProt functional annotation for Q9U2D9

UniProt code: Q9U2D9.

Organism: Caenorhabditis elegans.
Taxonomy: Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
 
Function: Transfers the glycosyl residue from UDP-Glc to the non- reducing end of alpha-1,4-glucan. {ECO:0000269|PubMed:24982189}.
 
Catalytic activity: Reaction=[(1->4)-alpha-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->4)- alpha-D-glucosyl](n+1) + H(+) + UDP; Xref=Rhea:RHEA:18549, Rhea:RHEA- COMP:9584, Rhea:RHEA-COMP:9587, ChEBI:CHEBI:15378, ChEBI:CHEBI:15444, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.11; Evidence={ECO:0000269|PubMed:24982189};
Biophysicochemical properties: Kinetic parameters: KM=3.9 mM for UDP-glucose (at 30 degrees Celsius) {ECO:0000269|PubMed:24982189}; Vmax=126 pmol/min/ug enzyme {ECO:0000269|PubMed:24982189};
Pathway: Glycan biosynthesis; glycogen biosynthesis. {ECO:0000269|PubMed:24982189}.
Subunit: Forms a hetero-octamer with each protomer of the gsy-1 homotetramer bound to one molecule of gyg-1. The N-terminus is involved in interprotomer contacts with gyg-1. The interaction with gyg-1 is required for glycogen production but is not required for gsy-1 intrinsic activity. {ECO:0000269|PubMed:24982189}.
Disruption phenotype: RNAi-mediated knockdown results in reduced survival. {ECO:0000269|PubMed:26439621}.
Similarity: Belongs to the glycosyltransferase 3 family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.