A0A210GPL8 · A0A210GPL8_ECOLX
- ProteindTDP-4-dehydrorhamnose 3,5-epimerase
- GenerfbC
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids181 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the epimerization of the C3' and C5'positions of dTDP-6-deoxy-D-xylo-4-hexulose, forming dTDP-6-deoxy-L-lyxo-4-hexulose.
Catalytic activity
- dTDP-4-dehydro-6-deoxy-alpha-D-glucose = dTDP-4-dehydro-beta-L-rhamnose
Pathway
Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
Features
Showing features for active site, site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Active site | 62 | Proton acceptor | |||
Active site | 132 | Proton donor | |||
Site | 138 | Participates in a stacking interaction with the thymidine ring of dTDP-4-oxo-6-deoxyglucose | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | dTDP-4-dehydrorhamnose 3,5-epimerase activity | |
Biological Process | dTDP-rhamnose biosynthetic process | |
Biological Process | extracellular polysaccharide biosynthetic process |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namedTDP-4-dehydrorhamnose 3,5-epimerase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionA0A210GPL8
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Interaction
Subunit
Homodimer.
Structure
Sequence
- Sequence statusComplete
- Length181
- Mass (Da)21,133
- Last updated2017-10-25 v1
- MD5 Checksum4F3CE92392191F1E9FF3BDDB3AEDFBE0
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AATJYL010000008 EMBL· GenBank· DDBJ | EFM1444940.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP042615 EMBL· GenBank· DDBJ | QED73333.1 EMBL· GenBank· DDBJ | Genomic DNA |