2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with the corresponding release of cytidine 5-monophosphate (CMP)
2C-methyl-D-erythritol 2,4-cyclodiphosphate synthase [Lipid transport and metabolism]; ...
1-157
2.62e-100
2C-methyl-D-erythritol 2,4-cyclodiphosphate synthase [Lipid transport and metabolism]; 2C-methyl-D-erythritol 2,4-cyclodiphosphate synthase is part of the Pathway/BioSystem: Isoprenoid biosynthesis
:
Pssm-ID: 440015 Cd Length: 157 Bit Score: 284.60 E-value: 2.62e-100
2C-methyl-D-erythritol 2,4-cyclodiphosphate synthase [Lipid transport and metabolism]; ...
1-157
2.62e-100
2C-methyl-D-erythritol 2,4-cyclodiphosphate synthase [Lipid transport and metabolism]; 2C-methyl-D-erythritol 2,4-cyclodiphosphate synthase is part of the Pathway/BioSystem: Isoprenoid biosynthesis
Pssm-ID: 440015 Cd Length: 157 Bit Score: 284.60 E-value: 2.62e-100
MECDP_synthase (2-C-methyl-D-erythritol-2,4-cyclodiphosphate synthase), encoded by the ispF ...
3-155
6.01e-89
MECDP_synthase (2-C-methyl-D-erythritol-2,4-cyclodiphosphate synthase), encoded by the ispF gene, catalyzes the formation of 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (MEC) in the non-mevalonate deoxyxylulose (DOXP) pathway for isoprenoid biosynthesis. This pathway is present in bacteria, plants and some protozoa but is distinct from that used by mammals and Archaea. MECDP_synthase forms a homotrimer, carrying three active sites, each of which is formed in a cleft between pairs of subunits.
Pssm-ID: 100025 Cd Length: 153 Bit Score: 255.83 E-value: 6.01e-89
2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase; Members of this protein family are ...
3-157
4.97e-83
2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase; Members of this protein family are 2C-methyl-D-erythritol 2,4-cyclodiphosphate synthase, the IspF protein of the deoxyxylulose (non-mevalonate) pathway of IPP biosynthesis. This protein occurs as an IspDF bifunctional fusion protein in about 20 percent of bacterial genomes. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 129255 Cd Length: 155 Bit Score: 241.04 E-value: 4.97e-83
2C-methyl-D-erythritol 2,4-cyclodiphosphate synthase [Lipid transport and metabolism]; ...
1-157
2.62e-100
2C-methyl-D-erythritol 2,4-cyclodiphosphate synthase [Lipid transport and metabolism]; 2C-methyl-D-erythritol 2,4-cyclodiphosphate synthase is part of the Pathway/BioSystem: Isoprenoid biosynthesis
Pssm-ID: 440015 Cd Length: 157 Bit Score: 284.60 E-value: 2.62e-100
MECDP_synthase (2-C-methyl-D-erythritol-2,4-cyclodiphosphate synthase), encoded by the ispF ...
3-155
6.01e-89
MECDP_synthase (2-C-methyl-D-erythritol-2,4-cyclodiphosphate synthase), encoded by the ispF gene, catalyzes the formation of 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (MEC) in the non-mevalonate deoxyxylulose (DOXP) pathway for isoprenoid biosynthesis. This pathway is present in bacteria, plants and some protozoa but is distinct from that used by mammals and Archaea. MECDP_synthase forms a homotrimer, carrying three active sites, each of which is formed in a cleft between pairs of subunits.
Pssm-ID: 100025 Cd Length: 153 Bit Score: 255.83 E-value: 6.01e-89
2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase; Members of this protein family are ...
3-157
4.97e-83
2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase; Members of this protein family are 2C-methyl-D-erythritol 2,4-cyclodiphosphate synthase, the IspF protein of the deoxyxylulose (non-mevalonate) pathway of IPP biosynthesis. This protein occurs as an IspDF bifunctional fusion protein in about 20 percent of bacterial genomes. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 129255 Cd Length: 155 Bit Score: 241.04 E-value: 4.97e-83
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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Functional characterization of the conserved domain architecture found on the query.
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This image shows a graphical summary of conserved domains identified on the query sequence.
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The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
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(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
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specific hits meet or exceed a domain-specific e-value threshold
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Retrieve proteins that contain one or more of the domains present in the query sequence, using the Conserved Domain Architecture Retrieval Tool
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