Q5R1W6 · TKT_PANTR
- ProteinTransketolase
- GeneTKT
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids623 (go to sequence)
- Protein existenceEvidence at transcript level
- 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, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 37 | substrate | ||||
Sequence: H | ||||||
Site | 37 | Important for catalytic activity | ||||
Sequence: H | ||||||
Binding site | 40 | thiamine diphosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 77 | thiamine diphosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 123-125 | thiamine diphosphate (UniProtKB | ChEBI) | ||||
Sequence: GSL | ||||||
Binding site | 155 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 156 | thiamine diphosphate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 185 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 185 | thiamine diphosphate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 187 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 244 | thiamine diphosphate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 258 | substrate | ||||
Sequence: H | ||||||
Binding site | 258 | thiamine diphosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Site | 258 | Important for catalytic activity | ||||
Sequence: H | ||||||
Binding site | 318 | substrate | ||||
Sequence: R | ||||||
Binding site | 345 | substrate | ||||
Sequence: S | ||||||
Active site | 366 | Proton donor | ||||
Sequence: E | ||||||
Binding site | 392 | thiamine diphosphate (UniProtKB | ChEBI) | ||||
Sequence: F | ||||||
Binding site | 416 | substrate | ||||
Sequence: H | ||||||
Binding site | 424 | substrate | ||||
Sequence: D | ||||||
Binding site | 428 | thiamine diphosphate (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 474 | substrate | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | endoplasmic reticulum membrane | |
Molecular Function | metal ion binding | |
Molecular Function | thiamine pyrophosphate binding | |
Molecular Function | transketolase activity | |
Biological Process | pentose-phosphate shunt, non-oxidative branch |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameTransketolase
- EC number
- Short namesTK
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Pan
Accessions
- Primary accessionQ5R1W6
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for modified residue, chain, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 1 | N-acetylmethionine | ||||
Sequence: M | ||||||
Chain | PRO_0000191897 | 1-623 | Transketolase | |||
Sequence: MESYHKPDQQKLQALKDTANRLRISSIQATTAAGSGHPTSCCSAAEIMAVLFFHTMRYKSQDPRNPHNDRFVLSKGHAAPILYAVWAEAGFLAEAELLNLRKISSDLDGHPVPKQAFTDVATGSLGQGLGAACGMAYTGKYFDKASYRVYCLLGDGELSEGSVWEAMAFASIYKLDNLVAILDINRLGQSDPAPLQHQMDIYQKRCEAFGWHAIIVDGHSVEELCKAFGQAKHQPTAIIAKTFKGRGITGVEGKESWHGKPFPKNMAEQIIQEIYSQIQSKKKILATPPQEDAPSVDIANIRMPSLPSYKVGDKIATRKAYGQALAKLGHASDRIIALDGDTKNSTFSEIFKKEHPDRFIECYIAEQNMVSIAVGCATRNRTVPFCSTFAAFFTRAFDQIRMAAISESNINLCGSHCGVSIGEDGPSQMALEDLAMFRSVPTSTVFYPSDGVATEKAVELAANTKGICFIRTSRPENAIIYNNNEDFQVGQAKVILKSKDDQVTVIGAGVTLHEALAAAELLKKEKINIRVLDPFTIKPLDRKLILDSARATKGRILTVEDHYYEGGIGEAVSSAVVGEPGITVTHLAVNRVPRSGKPAELLKMFGIDKDAIAQAVRGLITKA | ||||||
Modified residue | 6 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 11 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 104 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 144 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 204 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 232 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 241 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 260 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 275 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 287 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 295 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 345 | Phosphoserine | ||||
Sequence: S | ||||||
Cross-link | 352 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Modified residue | 538 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 603 | N6-acetyllysine | ||||
Sequence: K |
Keywords
- PTM
Proteomic databases
Interaction
Structure
Sequence
- Sequence statusComplete
- Length623
- Mass (Da)67,840
- Last updated2005-01-04 v1
- ChecksumCC41ED5AF9C40DDF
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB188281 EMBL· GenBank· DDBJ | BAD74032.1 EMBL· GenBank· DDBJ | mRNA |