A0A4Y9QK11 · A0A4Y9QK11_9BACT

  • 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

Lacks conserved residue(s) required for the propagation of feature annotation.
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 site13NADPH (UniProtKB | ChEBI)
Binding site14NADPH (UniProtKB | ChEBI)
Binding site15NADPH (UniProtKB | ChEBI)
Binding site16NADPH (UniProtKB | ChEBI)
Binding site41NADPH (UniProtKB | ChEBI)
Binding site125NADPH (UniProtKB | ChEBI)
Binding site1261-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI)
Binding site127NADPH (UniProtKB | ChEBI)
Binding site151Mn2+ (UniProtKB | ChEBI)
Binding site1521-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI)
Binding site1531-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI)
Binding site153Mn2+ (UniProtKB | ChEBI)
Binding site1771-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI)
Binding site2001-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI)
Binding site206NADPH (UniProtKB | ChEBI)
Binding site2131-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI)
Binding site2181-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI)
Binding site2191-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI)
Binding site2221-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI)
Binding site222Mn2+ (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
      E4S40_12310

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • XY-J91
  • Taxonomic lineage
    Bacteria > Bacteroidota > Cytophagia > Cytophagales > Cyclobacteriaceae > Algoriphagus

Accessions

  • Primary accession
    A0A4Y9QK11

Proteomes

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain7-1331-deoxy-D-xylulose 5-phosphate reductoisomerase N-terminal
Domain147-2301-deoxy-D-xylulose 5-phosphate reductoisomerase C-terminal
Domain262-378DXP reductoisomerase C-terminal

Sequence similarities

Belongs to the DXR family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    388
  • Mass (Da)
    43,205
  • Last updated
    2019-09-18 v1
  • Checksum
    2B7FC73A363E7492
MSELKRVAILGSTGSIGRQTLDVIRQHPEDFQVEVLTAQNNCDLLIQQALEFQPNAVVITNEAKYQVVKDALIPHDIKVFAGPKALAQVVEMETIDVVLTALVGYSGLIPTVQAIRAGKQIALANKETLVVAGEIITQLAKENAVNIYPVDSEHSAIFQCLVGEWHNPIEKIILTASGGPFRGKDRQFLESVTKEQALKHPNWDMGAKITIDSASLMNKGLEVIEAKWLFGLDTDQIEVVVHPQSIIHSLIQFEDGSIKAQLGLPDMRIPIQFALSYPHRLKSDFERFDFLNYPNLTFEQPDLKTFRNLQLAFDALEKGGNAPCMLNAANEIAVEAFLKDQIGFLQMSELIENAMNRADFISHPSLEDYVASDEQVRTISKELIKQYV

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
SPSB01000004
EMBL· GenBank· DDBJ
TFV93044.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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