P37351 · RPIB_ECOLI
- ProteinRibose-5-phosphate isomerase B
- GenerpiB
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids149 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the interconversion of ribulose-5-P and ribose-5-P. It probably also has activity on D-allose 6-phosphate.
Catalytic activity
- aldehydo-D-ribose 5-phosphate = D-ribulose 5-phosphate
- D-allose 6-phosphate = D-allulose 6-phosphate
Activity regulation
Inhibited by iodoacetate and glucose 6-phosphate.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
0.83 mM | D-ribose 5-phosphate | 37 | ||||
1.23 mM | D-ribose 5-phosphate | |||||
0.5 mM | D-allose 6-phosphate |
Temperature Dependence
After incubation at 45 degrees Celsius for 30 minutes RpiB retains 65% of its original activities. At 60 degrees Celsius RpiB is rapidly inactivated.
Pathway
Carbohydrate degradation; pentose phosphate pathway; D-ribose 5-phosphate from D-ribulose 5-phosphate (non-oxidative stage): step 1/1.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 9-10 | D-ribulose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: DH | ||||||
Active site | 66 | Proton acceptor | ||||
Sequence: C | ||||||
Binding site | 67-71 | D-ribulose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: GTGVG | ||||||
Active site | 99 | Proton donor | ||||
Sequence: H | ||||||
Binding site | 100 | D-ribulose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 110 | D-ribulose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 133 | D-ribulose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 137 | D-ribulose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | D-allose 6-phosphate isomerase activity | |
Molecular Function | ribose-5-phosphate isomerase activity | |
Biological Process | D-allose catabolic process | |
Biological Process | pentose-phosphate shunt, non-oxidative branch |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameRibose-5-phosphate isomerase B
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionP37351
- Secondary accessions
Proteomes
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 99 | Strongly reduced enzyme activity. | ||||
Sequence: H → N |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000208163 | 1-149 | Ribose-5-phosphate isomerase B | |||
Sequence: MKKIAFGCDHVGFILKHEIVAHLVERGVEVIDKGTWSSERTDYPHYASQVALAVAGGEVDGGILICGTGVGISIAANKFAGIRAVVCSEPYSAQLSRQHNDTNVLAFGSRVVGLELAKMIVDAWLGAQYEGGRHQQRVEAITAIEQRRN |
Proteomic databases
Expression
Induction
Induced by ribose and repressed by RpiR.
Interaction
Subunit
Homodimer, and homotetramer.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P37351 | rplJ P0A7J3 | 2 | EBI-557460, EBI-546827 |
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length149
- Mass (Da)16,073
- Last updated1995-02-01 v2
- ChecksumBE610B5F995CEEB6
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X82203 EMBL· GenBank· DDBJ | CAA57688.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U14003 EMBL· GenBank· DDBJ | AAA96989.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U00096 EMBL· GenBank· DDBJ | AAC77051.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP009048 EMBL· GenBank· DDBJ | BAE78093.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
D90227 EMBL· GenBank· DDBJ | BAA21501.1 EMBL· GenBank· DDBJ | Genomic DNA |