Q98FW0 · LR3E_RHILO
- ProteinL-ribulose 3-epimerase
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids297 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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
- L-ribulose = L-xylulose
Cofactor
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 mM | D-psicose | |||||
140 mM | D-tagatose | |||||
230 mM | L-xylulose | |||||
291 mM | L-ribulose |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
416 μmol/min/mg | with L-ribulose as substrate | ||||
290 μmol/min/mg | with L-xylulose as substrate | ||||
50 μmol/min/mg | with D-tagatose as substrate | ||||
10 μmol/min/mg | with 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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 147 | Proton donor/acceptor | ||||
Sequence: E | ||||||
Binding site | 147 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 153 | substrate | ||||
Sequence: E | ||||||
Binding site | 180 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 180-183 | substrate | ||||
Sequence: DTFH | ||||||
Binding site | 206 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 212 | substrate | ||||
Sequence: R | ||||||
Active site | 241 | Proton donor/acceptor | ||||
Sequence: E | ||||||
Binding site | 241 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | isomerase activity | |
Molecular Function | metal ion binding |
Keywords
- Molecular function
- Ligand
Names & Taxonomy
Protein names
- Recommended nameL-ribulose 3-epimerase
- Short namesL-RE
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Alphaproteobacteria > Hyphomicrobiales > Phyllobacteriaceae > Mesorhizobium
Accessions
- Primary accessionQ98FW0
Proteomes
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000435307 | 1-297 | L-ribulose 3-epimerase | |||
Sequence: MARIGIHSFVWSASSAQSELERTLANTREAGFDLIEFSYLDPADVDIGGLAKRIADLGLGVAISIGLPGDGDISSADKAVAARGVEILNETVALTRDLGGRKVAGILSAGHGLQLEAPTRDQWSRSTAALAKVAETAKAAGVTLNLEIVNRFESNLLNTAAQGLAFIEDTGSDNIFLHLDTFHMNIEEADVGLAIRHAAGKIGYVHIGESHRGFLGTGNIDFAAIFDALTAVGYADDLSFESFSSEIVDENLSKKTAIWRNLWADNMALAKHARAFIGLGLETARRKAELVSARHKP |
Interaction
Subunit
Homotetramer.
Structure
Sequence
- Sequence statusComplete
- Length297
- Mass (Da)31,623
- Last updated2001-10-01 v1
- Checksum5D9E97AECC274DF8
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
BA000012 EMBL· GenBank· DDBJ | BAB50456.1 EMBL· GenBank· DDBJ | Genomic DNA |