A0A0M9AFS7 · A0A0M9AFS7_THEAQ

  • Protein
    1-deoxy-D-xylulose 5-phosphate reductoisomerase
  • Gene
    dxr
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

Function

function

Catalyzes the NADPH-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP).

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

Pathway

Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 1/6.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site10NADPH (UniProtKB | ChEBI)
Binding site11NADPH (UniProtKB | ChEBI)
Binding site12NADPH (UniProtKB | ChEBI)
Binding site13NADPH (UniProtKB | ChEBI)
Binding site34NADPH (UniProtKB | ChEBI)
Binding site35NADPH (UniProtKB | ChEBI)
Binding site36NADPH (UniProtKB | ChEBI)
Binding site112NADPH (UniProtKB | ChEBI)
Binding site1131-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI)
Binding site114NADPH (UniProtKB | ChEBI)
Binding site138Mn2+ (UniProtKB | ChEBI)
Binding site1391-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI)
Binding site1401-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI)
Binding site140Mn2+ (UniProtKB | ChEBI)
Binding site1641-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI)
Binding site1861-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI)
Binding site192NADPH (UniProtKB | ChEBI)
Binding site1991-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI)
Binding site2041-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI)
Binding site2051-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI)
Binding site2081-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI)
Binding site208Mn2+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular Function1-deoxy-D-xylulose-5-phosphate reductoisomerase activity
Molecular Functionisomerase activity
Molecular Functionmetal ion binding
Molecular FunctionNADPH binding
Biological Processisopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    1-deoxy-D-xylulose 5-phosphate reductoisomerase
  • EC number
  • Short names
    DXP reductoisomerase
  • Alternative names
    • 1-deoxyxylulose-5-phosphate reductoisomerase
    • 2-C-methyl-D-erythritol 4-phosphate synthase

Gene names

    • Name
      dxr
    • ORF names
      BVI061214_02246

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • ATCC 25104 / DSM 625 / JCM 10724 / NBRC 103206 / NCIMB 11243 / YT-1
  • Taxonomic lineage
    Bacteria > Deinococcota > Deinococci > Thermales > Thermaceae > Thermus

Accessions

  • Primary accession
    A0A0M9AFS7

Proteomes

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain4-1201-deoxy-D-xylulose 5-phosphate reductoisomerase N-terminal
Domain134-2161-deoxy-D-xylulose 5-phosphate reductoisomerase C-terminal
Domain248-361DXP reductoisomerase C-terminal

Sequence similarities

Belongs to the DXR family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    367
  • Mass (Da)
    39,910
  • Last updated
    2015-12-09 v1
  • Checksum
    84B7AE89E2231309
MKRLVILGSTGSIGRQALEVALWRGYRVVGLAAGKNLEVLAEQIARFRPLLVAAEEGLHRELKARFPWLKLASAEEVAAMEAEVAVAAIPGLAGLPPTRVAVRTGKRVALANKEAMVAAGPLLWQEVEKGGAEILPVDSEHSALFQALLGESKEEVAELILTASGGPFLRGPEDLSQVTPEMALNHPRWRMGPKVTVDSATLFNKGLEVLEAKELFRLPLEKIRVLVHPQAYVHGLVRFVDGSLKAQLGPTDMRLPIQYALTYPHRAETPLKDLPIPGVLEFLEPDLKRFPALAVAYEAGKRGGVAQVAVSAADEVAVEAFLAGRIPFTRIPEVLAKVLENTPSVPLTWENLFAVDAWAREEAKRWA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LHCI01000106
EMBL· GenBank· DDBJ
KOX91042.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp