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144  structures 6040  species 0  interactions 6843  sequences 21  architectures

Family: DXP_redisom_C (PF08436)

Summary: 1-deoxy-D-xylulose 5-phosphate reductoisomerase C-terminal domain

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This is the Wikipedia entry entitled "DXP reductoisomerase". More...

DXP reductoisomerase Edit Wikipedia article

1-deoxy-D-xylulose-5-phosphate reductoisomerase
PDB 1q0q EBI.jpg
crystal structure of DXR in complex with the substrate 1-deoxy-D-xylulose 5-phosphate
Pfam clanCL0063
DXP reductoisomerase
EC number1.1.1.267
CAS number210756-42-6
IntEnzIntEnz view
ExPASyNiceZyme view
MetaCycmetabolic pathway
PDB structuresRCSB PDB PDBe PDBsum

DXP reductoisomerase (1-deoxy-D-xylulose 5-phosphate reductoisomerase or DXR) is an enzyme that interconverts 1-deoxy-D-xylulose 5-phosphate (DXP) and 2-C-methyl-D-erythritol 4-phosphate (MEP).[1]

It is classified under EC It is normally abbreviated DXR, but it is sometimes named IspC, as the product of the ispC gene.

DXR is part of the MEP pathway (nonmevalonate pathway) of isoprenoid precursor biosynthesis. DXR is inhibited by fosmidomycin.

This enzyme is required for terpenoid biosynthesis in some organisms, since it is a key enzyme on the MEP pathway for the production of the isoprenoid precursors IPP and DMAPP.[1] In Arabidopsis thaliana 1-deoxy-D-xylulose 5-phosphate reductoisomerase is the first committed enzyme of the MEP pathway for isoprenoid precursor biosynthesis. The enzyme requires Mn2+, Co2+ or Mg2+ for activity, with Mn2+ being most effective.


External links

This article incorporates text from the public domain Pfam and InterPro: IPR013512
This article incorporates text from the public domain Pfam and InterPro: IPR013644

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

1-deoxy-D-xylulose 5-phosphate reductoisomerase C-terminal domain Provide feedback

This domain is found to the C-terminus of PF02670 domains in bacterial and plant 1-deoxy-D-xylulose 5-phosphate reductoisomerases which catalyse the formation of 2-C-methyl-D-erythritol 4-phosphate from 1-deoxy-D-xylulose-5-phosphate in the presence of NADPH [1].

Literature references

  1. Takahashi S, Kuzuyama T, Watanabe H, Seto H; , Proc Natl Acad Sci U S A 1998;95:9879-9884.: A 1-deoxy-D-xylulose 5-phosphate reductoisomerase catalyzing the formation of 2-C-methyl-D-erythritol 4-phosphate in an alternative nonmevalonate pathway for terpenoid biosynthesis. PUBMED:9707569 EPMC:9707569

This tab holds annotation information from the InterPro database.

InterPro entry IPR013644

1-deoxy-D-xylulose 5-phosphate reductoisomerase synthesises 2-C-methyl-D-erythritol 4-phosphate from 1-deoxy-D-xylulose 5-phosphate in a single step by intramolecular rearrangement and reduction and is responsible for terpenoid biosynthesis in some organisms [ PUBMED:9707569 ]. In Arabidopsis thaliana 1-deoxy-D-xylulose 5-phosphate reductoisomerase is the first committed enzyme of the non-mevalonate pathway for isoprenoid biosynthesis. The enzyme requires Mn2+, Co2+ or Mg2+ for activity, with the first being most effective.

This domain is found to the C terminus of INTERPRO domains in bacterial and plant 1-deoxy-D-xylulose 5-phosphate reductoisomerases.

Gene Ontology

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Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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Pfam Clan

This family is a member of clan GADPH_aa-bio_dh (CL0139), which has the following description:

This clan contains the C terminal domains of dehydrogenase enzymes involved in the biosynthesis of arginine, aspartate and aspartate derived amino acids. It also contains the C terminal domain of GAPDH, a dehydrogenase involved in glycolysis and gluconeogenesis.

The clan contains the following 17 members:

AcetDehyd-dimer Biliv-reduc_cat DapB_C DAPDH_C DUF108 DXP_redisom_C G6PD_C GFO_IDH_MocA_C GFO_IDH_MocA_C2 Gp_dh_C Homoserine_dh Inos-1-P_synth ox_reductase_C Oxidoreduct_C OxRdtase_C Sacchrp_dh_C Semialdhyde_dhC


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Curation and family details

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Seed source: Pfam-B_445 (release 18.0)
Previous IDs: none
Type: Domain
Sequence Ontology: SO:0000417
Author: Wuster A
Number in seed: 458
Number in full: 6843
Average length of the domain: 85.10 aa
Average identity of full alignment: 58 %
Average coverage of the sequence by the domain: 21.63 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 57096847 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 26.0 26.0
Trusted cut-off 26.2 30.1
Noise cut-off 24.7 25.9
Model length: 84
Family (HMM) version: 14
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Species distribution

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Archea Archea Eukaryota Eukaryota
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the DXP_redisom_C domain has been found. There are 144 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.

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