A0A454A689 · A0A454A689_ECOL5
- ProteinTransketolase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids667 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate.
Catalytic activity
- D-sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = aldehydo-D-ribose 5-phosphate + D-xylulose 5-phosphate
Cofactor
Protein has several cofactor binding sites:
Ca2+ (UniProtKB | Rhea| CHEBI:29108 )
Mn2+ (UniProtKB | Rhea| CHEBI:29035 )
Co2+ (UniProtKB | Rhea| CHEBI:48828 )
Note: Binds 1 Mg2+ ion per subunit. Can also utilize other divalent metal cations, such as Ca2+, Mn2+ and Co2+.
Note: Binds 1 thiamine pyrophosphate per subunit.
Features
Showing features for binding site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 25 | substrate | ||||
Sequence: H | ||||||
Site | 25 | Important for catalytic activity | ||||
Sequence: H | ||||||
Binding site | 260 | substrate | ||||
Sequence: H | ||||||
Site | 260 | Important for catalytic activity | ||||
Sequence: H | ||||||
Binding site | 357 | substrate | ||||
Sequence: R | ||||||
Binding site | 384 | substrate | ||||
Sequence: S | ||||||
Binding site | 460 | substrate | ||||
Sequence: H | ||||||
Binding site | 468 | substrate | ||||
Sequence: D | ||||||
Binding site | 472 | substrate | ||||
Sequence: H | ||||||
Binding site | 519 | substrate | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | metal ion binding | |
Molecular Function | transketolase activity | |
Biological Process | pentose-phosphate shunt |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameTransketolase
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionA0A454A689
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 354-524 | Transketolase-like pyrimidine-binding | ||||
Sequence: IATRKASQNTLNAYGPMLPELLGGSADLAPSNLTIWKGSVSLKEDPAGNYIHYGVREFGMTAIANGIAHHGGFVPYTATFLMFVEYARNAARMAALMKARQIMVYTHDSIGLGEDGPTHQAVEQLASLRLTPNFSTWRPCDQVEAAVGWKLAVERHNGPTALILSRQNLAQ |
Sequence similarities
Belongs to the transketolase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length667
- Mass (Da)73,099
- Last updated2019-05-08 v1
- Checksum11AE5F286F1CC9A2
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000247 EMBL· GenBank· DDBJ | ABG70466.1 EMBL· GenBank· DDBJ | Genomic DNA |