SMART: Pfam domain DeoC

The domain within your query sequence starts at position 2 and ends at position 97; the E-value for the DeoC domain shown below is 1e-6.

AAHCRGTELGSDFIKTSTGKETVNATFPVAIVMLRAIRDFFWKTGNKVGFKPAGGIRTAK
ESLAWLSLVKEELGDEWLTPDLFRIGASSLLSDIER

DeoC

PFAM accession number:	PF01791
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 4.1.2.13) 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)

PFAM accession number:

PF01791

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 4.1.2.13) 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)

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