aldolase/citrate lyase/malate synthase family protein; similar to 4-hydroxy-2-ketoheptane-1,7-dioate (HKHD) aldolase (HpcH/HpaI) that catalyzes the reversible retro-aldol cleavage of HKHD to pyruvate and succinic semialdehyde, and to malate synthase that catalyzes the Claisen condensation of glyoxylate and acetyl-CoA to malyl-CoA, which hydrolyzes to malate and CoA, in the glyoxylate cycle
Malate synthase catalyzes the Claisen condensation of glyoxylate and acetyl-CoA to malyl-CoA , ...
18-282
5.59e-163
Malate synthase catalyzes the Claisen condensation of glyoxylate and acetyl-CoA to malyl-CoA , which hydrolyzes to malate and CoA. This reaction is part of the glyoxylate cycle, which allows certain organisms, like plants and fungi, to derive their carbon requirements from two-carbon compounds, by bypassing the two carboxylation steps of the citric acid cycle.
The actual alignment was detected with superfamily member pfam01274:
Pssm-ID: 451263 Cd Length: 523 Bit Score: 462.63 E-value: 5.59e-163
Malate synthase A (MSA), present in some bacteria, plants and fungi. Prokaryotic MSAs tend to ...
31-282
4.42e-162
Malate synthase A (MSA), present in some bacteria, plants and fungi. Prokaryotic MSAs tend to be monomeric, whereas eukaryotic enzymes are homomultimers. In general, malate synthase catalyzes the Claisen condensation of glyoxylate and acetyl-CoA to malyl-CoA, which hydrolyzes to malate and CoA. This reaction is part of the glyoxylate cycle, which allows certain organisms, like plants and fungi, to derive their carbon requirements from two-carbon compounds, by bypassing the two carboxylation steps of the citric acid cycle.
Pssm-ID: 238369 Cd Length: 511 Bit Score: 460.18 E-value: 4.42e-162
malate synthase A; This model represents plant malate synthase and one of two bacterial forms, ...
31-282
5.06e-157
malate synthase A; This model represents plant malate synthase and one of two bacterial forms, designated malate synthase A. The distantly related malate synthase G is described by a separate model. This enzyme and isocitrate lyase are the two characteristic enzymes of the glyoxylate shunt. The shunt enables the cell to use acetyl-CoA to generate increased levels of TCA cycle intermediates for biosynthetic pathways such as gluconeogenesis. [Energy metabolism, TCA cycle]
Pssm-ID: 188132 Cd Length: 511 Bit Score: 447.33 E-value: 5.06e-157
Malate synthase A (MSA), present in some bacteria, plants and fungi. Prokaryotic MSAs tend to ...
31-282
4.42e-162
Malate synthase A (MSA), present in some bacteria, plants and fungi. Prokaryotic MSAs tend to be monomeric, whereas eukaryotic enzymes are homomultimers. In general, malate synthase catalyzes the Claisen condensation of glyoxylate and acetyl-CoA to malyl-CoA, which hydrolyzes to malate and CoA. This reaction is part of the glyoxylate cycle, which allows certain organisms, like plants and fungi, to derive their carbon requirements from two-carbon compounds, by bypassing the two carboxylation steps of the citric acid cycle.
Pssm-ID: 238369 Cd Length: 511 Bit Score: 460.18 E-value: 4.42e-162
malate synthase A; This model represents plant malate synthase and one of two bacterial forms, ...
31-282
5.06e-157
malate synthase A; This model represents plant malate synthase and one of two bacterial forms, designated malate synthase A. The distantly related malate synthase G is described by a separate model. This enzyme and isocitrate lyase are the two characteristic enzymes of the glyoxylate shunt. The shunt enables the cell to use acetyl-CoA to generate increased levels of TCA cycle intermediates for biosynthetic pathways such as gluconeogenesis. [Energy metabolism, TCA cycle]
Pssm-ID: 188132 Cd Length: 511 Bit Score: 447.33 E-value: 5.06e-157
Malate synthase catalyzes the Claisen condensation of glyoxylate and acetyl-CoA to malyl-CoA , ...
36-282
8.08e-143
Malate synthase catalyzes the Claisen condensation of glyoxylate and acetyl-CoA to malyl-CoA , which hydrolyzes to malate and CoA. This reaction is part of the glyoxylate cycle, which allows certain organisms, like plants and fungi, to derive their carbon requirements from two-carbon compounds, by bypassing the two carboxylation steps of the citric acid cycle.
Pssm-ID: 238267 Cd Length: 511 Bit Score: 411.24 E-value: 8.08e-143
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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