Q98FW0 · LR3E_RHILO

Function

function

Catalyzes the epimerization of various ketoses at the C3 position. It is able to interconvert L-ribulose with high efficiency. The enzyme can also accept other ketopentoses such as D-psicose and D-tagatose with lower efficiency.

Catalytic activity

Cofactor

Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

Note: It can also use Fe2+.

Activity regulation

Strongly inhibited by Co2+ and Ni2+, and slightly inhibited by EDTA.

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
58 mMD-psicose
140 mMD-tagatose
230 mML-xylulose
291 mML-ribulose
Vmax pH TEMPERATURE[C] NOTES EVIDENCE
416 μmol/min/mgwith L-ribulose as substrate
290 μmol/min/mgwith L-xylulose as substrate
50 μmol/min/mgwith D-tagatose as substrate
10 μmol/min/mgwith D-psicose as substrate
kcat is 0.34 min-1 for epimerase activity with D-psicose as substrate. kcat is 3.4 min-1 for epimerase activity with D-tagatose as substrate. kcat is 8.5 min-1 for epimerase activity with L-xylulose as substrate. kcat is 13 min-1 for epimerase activity with L-ribulose as substrate.

pH Dependence

Optimum pH is 8. The enzyme is stable between 7 and 10.

Temperature Dependence

Optimum temperature is around 60 degrees Celsius. The enzyme is stable below 60 degrees Celsius.

Features

Showing features for active site, binding site.

TypeIDPosition(s)Description
Active site147Proton donor/acceptor
Binding site147Mn2+ (UniProtKB | ChEBI)
Binding site153substrate
Binding site180Mn2+ (UniProtKB | ChEBI)
Binding site180-183substrate
Binding site206Mn2+ (UniProtKB | ChEBI)
Binding site212substrate
Active site241Proton donor/acceptor
Binding site241Mn2+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular Functionisomerase activity
Molecular Functionmetal ion binding

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    L-ribulose 3-epimerase
  • Short names
    L-RE
  • Alternative names
    • D-tagatose 3-epimerase
      (DTE
      ) (EC:5.1.3.31
      ) . EC:5.1.3.31 (UniProtKB | ENZYME | Rhea)
    • Ketose 3-epimerase

Gene names

    • Ordered locus names
      mll3595

Organism names

Accessions

  • Primary accession
    Q98FW0

Proteomes

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004353071-297L-ribulose 3-epimerase

Interaction

Subunit

Homotetramer.

Structure

Family & Domains

Sequence similarities

Belongs to the hyi family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    297
  • Mass (Da)
    31,623
  • Last updated
    2001-10-01 v1
  • Checksum
    5D9E97AECC274DF8
MARIGIHSFVWSASSAQSELERTLANTREAGFDLIEFSYLDPADVDIGGLAKRIADLGLGVAISIGLPGDGDISSADKAVAARGVEILNETVALTRDLGGRKVAGILSAGHGLQLEAPTRDQWSRSTAALAKVAETAKAAGVTLNLEIVNRFESNLLNTAAQGLAFIEDTGSDNIFLHLDTFHMNIEEADVGLAIRHAAGKIGYVHIGESHRGFLGTGNIDFAAIFDALTAVGYADDLSFESFSSEIVDENLSKKTAIWRNLWADNMALAKHARAFIGLGLETARRKAELVSARHKP

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BA000012
EMBL· GenBank· DDBJ
BAB50456.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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