Dxr protein complex

GO:1990065 · Other · Multiprotein complex · Proposed

A protein complex that is involved in the MEP pathway of IPP biosynthesis. It catalyzes the NADP-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP). [GO:1990065]

Synonyms: 1-deoxy-D-xylulose 5-phosphate reductoisomerase complex

UniProt location names: UniProt Consortium, CC BY 4.0. Reference label and route sources.

Components

Component	Type	Part of / acts on	Grounding	Genes	Stoichiometry	Essential	Role
1-deoxy-D-xylulose 5-phosphate reductoisomerase	Protein	part of	`InterPro:IPR003821`	dxr, ispC	2 copies per E. coli Dxr homodimer in PDB:1Q0Q	UNKNOWN	Homodimeric reductoisomerase subunit that catalyzes the NADPH-dependent DXP-to-MEP step of the methylerythritol phosphate pathway. `GO:1990065` GO:1990065 defines the Dxr protein complex by its role in the MEP pathway and DXP-to-MEP reductoisomerase reaction. `InterPro:IPR003821` InterPro IPR003821 is the 1-deoxy-D-xylulose 5-phosphate reductoisomerase family entry. `PDB:1Q0Q` RCSB describes PDB:1Q0Q as a homomeric E. coli Dxr protein structure with two deposited polymer instances.

Organism-specific protein examples

Named proteins in which each component's role was established, with the organism the evidence comes from. The component above is the taxon-agnostic family; these are the specific entries behind it.

1-deoxy-D-xylulose 5-phosphate reductoisomerase

Accession	Protein	Gene	Organism	Entry
`UniProtKB:P45568`	1-deoxy-D-xylulose 5-phosphate reductoisomerase	dxr	Escherichia coli K-12 (`NCBITaxon:83333`)	REVIEWED
Role and evidence (2 references) Reviewed E. coli K-12 Dxr accession mapped by RCSB to the two protein chains in PDB:1Q0Q. `UniProtKB:P45568` UniProtKB P45568 is the reviewed Escherichia coli K-12 entry for Dxr, also named IspC. `PDB:1Q0Q` RCSB SIFTS maps PDB:1Q0Q polymer entity 1 to UniProtKB:P45568 with two E. coli Dxr chains.

Canonical examples

NCBITaxon:562 Escherichia coli — E. coli source of the two-chain Dxr structure in complex with NADPH and 1-deoxy-D-xylulose 5-phosphate deposited as PDB:1Q0Q. [PDB:1Q0Q]

Functions

1-deoxy-D-xylulose-5-phosphate reductoisomerase activity GO:0030604 — The Dxr homodimer catalyzes the NADPH-dependent rearrangement and reduction of 1-deoxy-D-xylulose 5-phosphate to 2-C-methyl-D-erythritol 4-phosphate in the MEP pathway.
- GO:1990065 GO:1990065 defines the Dxr protein complex by the NADP-dependent DXP-to-MEP rearrangement and reduction.
- GO:0030604 GO:0030604 is the Gene Ontology molecular-function term for 1-deoxy-D-xylulose-5-phosphate reductoisomerase activity.

Physical properties

SUBUNIT_COUNT: 2 (E. coli Dxr homodimer in PDB:1Q0Q) [PDB:1Q0Q]

Evidence

GO:1990065 Gene Ontology cellular-component term for the Dxr protein complex and source of its exact 1-deoxy-D-xylulose 5-phosphate reductoisomerase complex synonym.
GO:0032991 QuickGO reports GO:1990065 Dxr protein complex as an is-a child of GO:0032991 protein-containing complex.
GO:0030604 Gene Ontology molecular-function term for 1-deoxy-D-xylulose-5-phosphate reductoisomerase activity.
InterPro:IPR003821 InterPro family entry for 1-deoxy-D-xylulose 5-phosphate reductoisomerases.
UniProtKB:P45568 UniProtKB reviewed E. coli K-12 Dxr entry.
PDB:1Q0Q RCSB Protein Data Bank entry for the E. coli Dxr homodimeric structure with 1-deoxy-D-xylulose 5-phosphate and NADPH.
PMID:15567415 PubMed identifier for Mac Sweeney et al. 2005, the Journal of Molecular Biology E. coli Dxr structural paper cited by PDB:1Q0Q.
DOI:10.1016/j.jmb.2004.10.030 DOI for Mac Sweeney et al. 2005, 'The crystal structure of E.coli 1-deoxy-D-xylulose-5-phosphate reductoisomerase in a ternary complex with the antimalarial compound fosmidomycin and NADPH reveals a tight-binding closed enzyme conformation', as reported by PubMed.

Curation history

2026-10-01T18:16:50Z codex · CREATED_RECORD — Scaffolded by scripts/new_record.py
2026-10-01T18:17:52Z codex · EXPANDED_RECORD — Added the GO exact synonym and protein-containing-complex parent, grounded the Dxr constituent to exact InterPro family IPR003821, added the E. coli PDB:1Q0Q homodimeric structure with a reviewed UniProt example, and cited DOI/PMID/PDB evidence.

Source: data/structures/other/dxr_protein_complex.yaml