1-deoxy-D-xylulose-5-phosphate reductoisomerase catalyzes the NADP-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP)
1-deoxy-D-xylulose 5-phosphate reductoisomerase [Lipid transport and metabolism]; ...
13-419
1.60e-179
1-deoxy-D-xylulose 5-phosphate reductoisomerase [Lipid transport and metabolism]; 1-deoxy-D-xylulose 5-phosphate reductoisomerase is part of the Pathway/BioSystem: Isoprenoid biosynthesis
Pssm-ID: 440506 Cd Length: 385 Bit Score: 505.31 E-value: 1.60e-179
1-deoxy-D-xylulose 5-phosphate reductoisomerase; 1-deoxy-D-xylulose 5-phosphate is converted ...
13-412
1.13e-135
1-deoxy-D-xylulose 5-phosphate reductoisomerase; 1-deoxy-D-xylulose 5-phosphate is converted to 2-C-methyl-D-erythritol 4-phosphate in the presence of NADPH. It is involved in the synthesis of isopentenyl diphosphate (IPP), a basic building block in isoprenoid, thiamin, and pyridoxal biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 161787 [Multi-domain] Cd Length: 389 Bit Score: 394.19 E-value: 1.13e-135
1-deoxy-D-xylulose 5-phosphate reductoisomerase; This is a family of 1-deoxy-D-xylulose ...
14-146
5.16e-51
1-deoxy-D-xylulose 5-phosphate reductoisomerase; This is a family of 1-deoxy-D-xylulose 5-phosphate reductoisomerases. This enzyme catalyzes the formation of 2-C-methyl-D-erythritol 4-phosphate from 1-deoxy-D-xylulose-5-phosphate in the presence of NADPH. This reaction is part of the terpenoid biosynthesis pathway.
Pssm-ID: 460644 [Multi-domain] Cd Length: 127 Bit Score: 168.04 E-value: 5.16e-51
1-deoxy-D-xylulose 5-phosphate reductoisomerase [Lipid transport and metabolism]; ...
13-419
1.60e-179
1-deoxy-D-xylulose 5-phosphate reductoisomerase [Lipid transport and metabolism]; 1-deoxy-D-xylulose 5-phosphate reductoisomerase is part of the Pathway/BioSystem: Isoprenoid biosynthesis
Pssm-ID: 440506 Cd Length: 385 Bit Score: 505.31 E-value: 1.60e-179
1-deoxy-D-xylulose 5-phosphate reductoisomerase; 1-deoxy-D-xylulose 5-phosphate is converted ...
13-412
1.13e-135
1-deoxy-D-xylulose 5-phosphate reductoisomerase; 1-deoxy-D-xylulose 5-phosphate is converted to 2-C-methyl-D-erythritol 4-phosphate in the presence of NADPH. It is involved in the synthesis of isopentenyl diphosphate (IPP), a basic building block in isoprenoid, thiamin, and pyridoxal biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 161787 [Multi-domain] Cd Length: 389 Bit Score: 394.19 E-value: 1.13e-135
1-deoxy-D-xylulose 5-phosphate reductoisomerase; This is a family of 1-deoxy-D-xylulose ...
14-146
5.16e-51
1-deoxy-D-xylulose 5-phosphate reductoisomerase; This is a family of 1-deoxy-D-xylulose 5-phosphate reductoisomerases. This enzyme catalyzes the formation of 2-C-methyl-D-erythritol 4-phosphate from 1-deoxy-D-xylulose-5-phosphate in the presence of NADPH. This reaction is part of the terpenoid biosynthesis pathway.
Pssm-ID: 460644 [Multi-domain] Cd Length: 127 Bit Score: 168.04 E-value: 5.16e-51
1-deoxy-D-xylulose 5-phosphate reductoisomerase C-terminal domain; This domain is found to the ...
161-257
1.58e-50
1-deoxy-D-xylulose 5-phosphate reductoisomerase C-terminal domain; This domain is found to the C-terminus of pfam02670 domains in bacterial and plant 1-deoxy-D-xylulose 5-phosphate reductoisomerases which catalyze the formation of 2-C-methyl-D-erythritol 4-phosphate from 1-deoxy-D-xylulose-5-phosphate in the presence of NADPH.
Pssm-ID: 462477 [Multi-domain] Cd Length: 84 Bit Score: 165.26 E-value: 1.58e-50
DXP reductoisomerase C-terminal domain; This is the C-terminal domain of the ...
292-411
2.06e-47
DXP reductoisomerase C-terminal domain; This is the C-terminal domain of the 1-deoxy-D-xylulose-5-phosphate reductoisomerase enzyme. This domain forms a left handed super-helix.
Pssm-ID: 463830 [Multi-domain] Cd Length: 116 Bit Score: 157.97 E-value: 2.06e-47
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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(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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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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