The domain within your query sequence starts at position 15 and ends at position 363; the E-value for the Glycolytic domain shown below is 5.5e-179.

ELSDIALRIVTPGKGILAADESVGSMAKRLSQIGVENTEENRRLYRQVLFSADDRVKKCI
GGVIFFHETLYQKDDNGVPFVRTIQDKGILVGIKVDKGVVPLAGTDGETTTQGLDGLLER
CAQYKKDGADFAKWRCVLKISDRTPSALAILENANVLARYASICQQNGIVPIVEPEILPD
GDHDLKRCQYVTEKVLAAVYKALSDHHVYLEGTLLKPNMVTPGHACPIKYSPEEIAMATV
TALRRTVPPAVPGVTFLSGGQSEEEASLNLNAINRCPLPRPWALTFSYGRALQASALNAW
RGQRDNAGAATEEFIKRAEMNGLAAQGRYEGSGDGGAAAQSLYIANHAY

Glycolytic

Glycolytic
PFAM accession number:PF00274
Interpro abstract (IPR000741):

Fructose-bisphosphate aldolase (EC 4.1.2.13) [(PUBMED:2199259), (PUBMED:1412694)] is a glycolytic enzyme that catalyses the reversible aldol cleavage or condensation of fructose-1,6-bisphosphate into dihydroxyacetone-phosphate and glyceraldehyde 3-phosphate. There are two classes of fructose-bisphosphate aldolases with different catalytic mechanisms: class I enzymes [(PUBMED:3355497)] do not require a metal ion, and are characterised by the formation of a Schiff base intermediate between a highly conserved active site lysine and a substrate carbonyl group, while the class II enzymes require an active-site divalent metal ion. This entry represents the class I enzymes.

In vertebrates, three forms of this enzyme are found: aldolase A is expressed in muscle, aldolase B in liver, kidney, stomach and intestine, and aldolase C in brain, heart and ovary. The different isozymes have different catalytic functions: aldolases A and C are mainly involved in glycolysis, while aldolase B is involved in both glycolysis and gluconeogenesis. Defects in aldolase A cause Glycogen storage disease 12 (GSD12) [(PUBMED:14766013)], while defects in aldolase B result in hereditary fructose intolerance [(PUBMED:15880727)].

GO process:glycolytic process (GO:0006096)
GO function:fructose-bisphosphate aldolase activity (GO:0004332)

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