The domain within your query sequence starts at position 6 and ends at position 49; the E-value for the Ribul_P_3_epim domain shown below is 3.6e-8.

KIGPSILNSDLANLGAECLRMLDSGADYLHLDVMDGHPALQGGQ

Ribul_P_3_epim

Ribul_P_3_epim
PFAM accession number:PF00834
Interpro abstract (IPR000056):

Ribulose-phosphate 3-epimerase ( EC 5.1.3.1 ) (also known as RPE, pentose-5-phosphate 3-epimerase or PPE) is the enzyme that converts D-ribulose 5-phosphate (Ru5P) into D-xylulose 5-phosphate in Calvin's reductive pentose phosphate cycle. In Ralstonia eutropha (Alcaligenes eutrophus) two copies of the gene coding for PPE are known [ (PUBMED:1429456) ], one is chromosomally encoded P40117 the other one is on a plasmid Q04539 . PPE has been found in a wide range of bacteria, archaebacteria, fungi and plants. All the proteins have from 209 to 241 amino acid residues. The enzyme has a TIM barrel structure.

This family also includes other enzymes from the ribulose-phosphate 3-epimerase family, like D-allulose-6-phosphate 3-epimerase and other putative pentose-5-phosphate 3-epimerases. D-allulose-6-phosphate 3-epimerase catalyses the reversible epimerization of D-allulose 6-phosphate to D-fructose 6-phosphate, but it can also catalyse with lower efficiency the reversible epimerization of D-ribulose 5-phosphate to D-xylulose 5-phosphate [ (PUBMED:18700786) ].

GO process:carbohydrate metabolic process (GO:0005975)
GO function:racemase and epimerase activity, acting on carbohydrates and derivatives (GO:0016857)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Ribul_P_3_epim