The domain within your query sequence starts at position 49 and ends at position 299; the E-value for the DeoC domain shown below is 1.16e-79.



DeoC/LacD family aldolase
SMART accession number:SM01133
Description: This family includes diverse aldolase enzymes. This family includes the enzyme deoxyribose-phosphate aldolase EC:, which is involved in nucleotide metabolism. The family also includes a group of related bacterial proteins of unknown function, see examples Q57843 and P76143. The family also includes tagatose 1,6-diphosphate aldolase ( EC: is part of the tagatose-6-phosphate pathway of galactose-6-phosphate degradation ((PUBMED:1655695)).
Interpro abstract (IPR002915):

This entry represents diverse aldolases, such as deoxyribose-phosphate aldolase, tagatose 1,6-diphosphate aldolase, fructose-bisphosphate aldolase class 1, 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate synthase, 2-amino-4,5-dihydroxy-6-one-heptanoic acid-7-phosphate synthase, phospho-2-dehydro-3-deoxyheptonate aldolase, and 6-deoxy-5-ketofructose 1-phosphate synthase, etc.

Aldolases play important roles in essential metabolic pathways, such as gluconeogenesis and glycolysis. They are classified with respect to their catalytic mechanism into two classes: class I adolases are are characterised by formation of covalent Schiff base intermediates, while class II aldolases are metallodependent enzymes and use a divalent transition metal ion to polarize the substrate ketose [ (PUBMED:16843441) (PUBMED:13950007) (PUBMED:5972827) (PUBMED:5793710) (PUBMED:5816380) ].

Fructose-1,6-bisphosphate (FBP) aldolase (EC catalyzes the reversible aldol condensation of glyceraldehyde 3-phosphate (GAP) and dihydroxyacetone phosphate (DHAP) yielding FBP. Two distinct classes of FBP aldolases occur in nature,Class I FBP aldolases form a Schiff-base intermediate between the carbonyl substrate (FBP and DHAP), whereas Class II FBP aldolases depend on divalent metal ions to stabilise the carbanion intermediate [ (PUBMED:11387336) (PUBMED:15766250) ].

Tagatose 1,6-diphosphate aldolase is a class I aldolase. It catalyses the reversible cleavage of four diastereoisomers (fructose 1,6-bisphosphate (FBP), psicose 1,6-bisphosphate, sorbose 1,6-bisphosphate, and tagatose 1,6-bisphosphate) to dihydroxyacetone phosphate (DHAP) and d-glyceraldehyde 3-phosphate with high catalytic efficiency [ (PUBMED:20427286) ].

GO function:lyase activity (GO:0016829)
Family alignment:
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There are 24839 DeoC domains in 24838 proteins in SMART's nrdb database.

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