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]; ...
1-156
2.23e-96
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: 274.97 E-value: 2.23e-96
2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase; Members of this protein family are ...
2-156
1.09e-87
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: 252.98 E-value: 1.09e-87
MECDP_synthase (2-C-methyl-D-erythritol-2,4-cyclodiphosphate synthase), encoded by the ispF ...
2-154
7.25e-87
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: 250.82 E-value: 7.25e-87
2C-methyl-D-erythritol 2,4-cyclodiphosphate synthase [Lipid transport and metabolism]; ...
1-156
2.23e-96
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: 274.97 E-value: 2.23e-96
2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase; Members of this protein family are ...
2-156
1.09e-87
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: 252.98 E-value: 1.09e-87
MECDP_synthase (2-C-methyl-D-erythritol-2,4-cyclodiphosphate synthase), encoded by the ispF ...
2-154
7.25e-87
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: 250.82 E-value: 7.25e-87
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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if a domain or superfamily has been annotated with functional sites (conserved features),
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click on the bars or triangles to view your query sequence embedded in a multiple sequence alignment of the proteins used to develop the corresponding domain model.
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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Concise Display shows only the best scoring domain model, in each hit category listed below except non-specific hits, for each region on the query sequence.
(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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and represent a very high confidence that the query sequence belongs to the same protein family as the sequences use to create the domain model
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the domain superfamily to which the specific and non-specific hits belong
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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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