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UniProtKB - P23254 (TKT1_YEAST)
Protein
Transketolase 1
Gene
TKL1
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Functioni
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.
1 PublicationMiscellaneous
Present with 40300 molecules/cell in log phase SD medium.1 Publication
Catalytic activityi
- D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate = aldehydo-D-ribose 5-phosphate + D-xylulose 5-phosphate3 PublicationsEC:2.2.1.13 Publications
Cofactori
Protein has several cofactor binding sites:- Mg2+1 Publication, Ca2+1 Publication, Mn2+1 Publication, Co2+1 PublicationNote: Binds 1 Mg2+ ion per subunit. Can also utilize other divalent metal cations, such as Ca2+, Mn2+ and Co2+.1 Publication
- thiamine diphosphate1 PublicationNote: Binds 1 thiamine pyrophosphate per subunit.1 Publication
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 30 | Substrate | 1 | |
Sitei | 30 | Important for catalytic activity | 1 | |
Binding sitei | 69 | Thiamine pyrophosphate3 Publications | 1 | |
Metal bindingi | 157 | Magnesium | 1 | |
Binding sitei | 158 | Thiamine pyrophosphate; via amide nitrogen3 Publications | 1 | |
Metal bindingi | 187 | Magnesium | 1 | |
Binding sitei | 187 | Thiamine pyrophosphate3 Publications | 1 | |
Metal bindingi | 189 | Magnesium; via carbonyl oxygen | 1 | |
Binding sitei | 263 | Substrate | 1 | |
Binding sitei | 263 | Thiamine pyrophosphate3 Publications | 1 | |
Sitei | 263 | Important for catalytic activity | 1 | |
Binding sitei | 359 | Substrate | 1 | |
Binding sitei | 386 | Substrate | 1 | |
Active sitei | 418 | Proton donorCurated | 1 | |
Binding sitei | 418 | Thiamine pyrophosphate3 Publications | 1 | |
Binding sitei | 445 | Thiamine pyrophosphate3 Publications | 1 | |
Binding sitei | 469 | Substrate | 1 | |
Binding sitei | 477 | Substrate | 1 | |
Binding sitei | 528 | Substrate | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 116 – 118 | Thiamine pyrophosphate3 Publications | 3 |
GO - Molecular functioni
- metal ion binding Source: UniProtKB-KW
- transketolase activity Source: SGD
GO - Biological processi
- pentose-phosphate shunt Source: SGD
Keywordsi
Molecular function | Transferase |
Ligand | Calcium, Magnesium, Metal-binding, Thiamine pyrophosphate |
Enzyme and pathway databases
BRENDAi | 2.2.1.1, 984 |
SABIO-RKi | P23254 |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:TKL1 Ordered Locus Names:YPR074C ORF Names:YP9499.29C |
Organismi | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
Taxonomic identifieri | 559292 [NCBI] |
Taxonomic lineagei | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › |
Proteomesi |
|
Organism-specific databases
SGDi | S000006278, TKL1 |
VEuPathDBi | FungiDB:YPR074C |
Subcellular locationi
Pathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 30 | H → A or Q: Strongly reduced catalytic activity. Decreases affinity for xylulose 5-phosphate about 15 times. 1 Publication | 1 | |
Mutagenesisi | 30 | H → N: Loss of activity. 1 Publication | 1 | |
Mutagenesisi | 69 | H → A: Reduces catalytic activity by about 98%. Decreased affinity for donor substrate. 1 Publication | 1 | |
Mutagenesisi | 103 | H → A or N: Reduces activity by over 96% and decreases affinity for thiamine pyrophosphate and xylulose 5-phosphate. 2 Publications | 1 | |
Mutagenesisi | 103 | H → F: Loss of activity. 2 Publications | 1 | |
Mutagenesisi | 162 | E → A or Q: Most catalytic properties similar to wild-type. 1 Publication | 1 | |
Mutagenesisi | 263 | H → A: Strongly reduced catalytic activity. 1 Publication | 1 | |
Mutagenesisi | 359 | R → A: Slightly reduced affinity for xylulose 5-phosphate and strongly reduced affinity for ribose 5-phosphate. 1 Publication | 1 | |
Mutagenesisi | 382 | D → A or R: Severe loss of activity. 1 Publication | 1 | |
Mutagenesisi | 469 | H → A: Strongly reduced affinity for xylulose 5-phosphate and ribose 5-phosphate. 1 Publication | 1 | |
Mutagenesisi | 477 | D → A: Strongly reduced catalytic activity. Strongly reduced affinity for xylulose 5-phosphate and ribose 5-phosphate. 1 Publication | 1 | |
Mutagenesisi | 481 | H → A or Q: Reduces catalytic activity by about 95%. 1 Publication | 1 | |
Mutagenesisi | 528 | R → A: Reduced affinity for xylulose 5-phosphate and strongly reduced affinity for ribose 5-phosphate. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed1 Publication | |||
ChainiPRO_0000191904 | 2 – 680 | Transketolase 1Add BLAST | 679 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 286 | PhosphoserineCombined sources | 1 | |
Modified residuei | 335 | PhosphoserineCombined sources | 1 | |
Modified residuei | 402 | PhosphoserineCombined sources | 1 | |
Modified residuei | 492 | PhosphoserineCombined sources | 1 | |
Cross-linki | 647 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources |
Keywords - PTMi
Isopeptide bond, Phosphoprotein, Ubl conjugationProteomic databases
MaxQBi | P23254 |
PaxDbi | P23254 |
PRIDEi | P23254 |
TopDownProteomicsi | P23254 |
2D gel databases
SWISS-2DPAGEi | P23254 |
PTM databases
iPTMneti | P23254 |
Interactioni
Subunit structurei
Homodimer.
5 PublicationsBinary interactionsi
Protein-protein interaction databases
BioGRIDi | 36247, 219 interactors |
DIPi | DIP-6765N |
IntActi | P23254, 13 interactors |
MINTi | P23254 |
STRINGi | 4932.YPR074C |
Miscellaneous databases
RNActi | P23254, protein |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P23254 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P23254 |
Family & Domainsi
Sequence similaritiesi
Belongs to the transketolase family.Curated
Phylogenomic databases
eggNOGi | KOG0523, Eukaryota |
GeneTreei | ENSGT00940000176704 |
HOGENOMi | CLU_009227_0_0_1 |
InParanoidi | P23254 |
OMAi | GCAPMGY |
Family and domain databases
CDDi | cd02012, TPP_TK, 1 hit |
Gene3Di | 3.40.50.920, 1 hit |
InterProi | View protein in InterPro IPR029061, THDP-binding IPR009014, Transketo_C/PFOR_II IPR005475, Transketolase-like_Pyr-bd IPR005478, Transketolase_bac-like IPR020826, Transketolase_BS IPR033248, Transketolase_C IPR033247, Transketolase_fam IPR005474, Transketolase_N |
PANTHERi | PTHR43522, PTHR43522, 1 hit |
Pfami | View protein in Pfam PF02779, Transket_pyr, 1 hit PF02780, Transketolase_C, 1 hit PF00456, Transketolase_N, 1 hit |
SMARTi | View protein in SMART SM00861, Transket_pyr, 1 hit |
SUPFAMi | SSF52518, SSF52518, 2 hits SSF52922, SSF52922, 1 hit |
TIGRFAMsi | TIGR00232, tktlase_bact, 1 hit |
PROSITEi | View protein in PROSITE PS00801, TRANSKETOLASE_1, 1 hit PS00802, TRANSKETOLASE_2, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P23254-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MTQFTDIDKL AVSTIRILAV DTVSKANSGH PGAPLGMAPA AHVLWSQMRM
60 70 80 90 100
NPTNPDWINR DRFVLSNGHA VALLYSMLHL TGYDLSIEDL KQFRQLGSRT
110 120 130 140 150
PGHPEFELPG VEVTTGPLGQ GISNAVGMAM AQANLAATYN KPGFTLSDNY
160 170 180 190 200
TYVFLGDGCL QEGISSEASS LAGHLKLGNL IAIYDDNKIT IDGATSISFD
210 220 230 240 250
EDVAKRYEAY GWEVLYVENG NEDLAGIAKA IAQAKLSKDK PTLIKMTTTI
260 270 280 290 300
GYGSLHAGSH SVHGAPLKAD DVKQLKSKFG FNPDKSFVVP QEVYDHYQKT
310 320 330 340 350
ILKPGVEANN KWNKLFSEYQ KKFPELGAEL ARRLSGQLPA NWESKLPTYT
360 370 380 390 400
AKDSAVATRK LSETVLEDVY NQLPELIGGS ADLTPSNLTR WKEALDFQPP
410 420 430 440 450
SSGSGNYSGR YIRYGIREHA MGAIMNGISA FGANYKPYGG TFLNFVSYAA
460 470 480 490 500
GAVRLSALSG HPVIWVATHD SIGVGEDGPT HQPIETLAHF RSLPNIQVWR
510 520 530 540 550
PADGNEVSAA YKNSLESKHT PSIIALSRQN LPQLEGSSIE SASKGGYVLQ
560 570 580 590 600
DVANPDIILV ATGSEVSLSV EAAKTLAAKN IKARVVSLPD FFTFDKQPLE
610 620 630 640 650
YRLSVLPDNV PIMSVEVLAT TCWGKYAHQS FGIDRFGASG KAPEVFKFFG
660 670 680
FTPEGVAERA QKTIAFYKGD KLISPLKKAF
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 37 – 38 | MA → RS in AAA35168 (PubMed:1737042).Curated | 2 | |
Sequence conflicti | 45 – 77 | WSQMR…LLYSM → GESNAHEPNQPKTGSTEIDL SCLTVTRSLCCIY in AAA35168 (PubMed:1737042).CuratedAdd BLAST | 33 | |
Sequence conflicti | 136 – 143 | AATYNKPG → DMPLTTSRA in AAA35168 (PubMed:1737042).Curated | 8 | |
Sequence conflicti | 232 – 234 | AQA → RQR in AAA35168 (PubMed:1737042).Curated | 3 | |
Sequence conflicti | 243 – 257 | LIKMT…GSLHA → FDQNDHNHWLRFLRS AA sequence (PubMed:1737042).CuratedAdd BLAST | 15 | |
Sequence conflicti | 383 | L → LVLPIL AA sequence (PubMed:1737042).Curated | 1 | |
Sequence conflicti | 396 | D → S in AAA35168 (PubMed:1737042).Curated | 1 | |
Sequence conflicti | 528 – 538 | RQNLPQLEGSS → PDKTCHNWKVAL in AAA35168 (PubMed:1737042).CuratedAdd BLAST | 11 | |
Sequence conflicti | 639 – 680 | SGKAP…LKKAF → PVRHQKSSSSSVSPQKVLLK ELKRPLHSIRVTS in AAA35168 (PubMed:1737042).CuratedAdd BLAST | 42 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M63302 Genomic DNA Translation: AAA35168.1 X73224 Genomic DNA Translation: CAA51693.1 Z49219 Genomic DNA Translation: CAA89191.1 Z71255 Genomic DNA Translation: CAA94982.1 U51033 Genomic DNA Translation: AAB68125.1 BK006949 Genomic DNA Translation: DAA11494.1 |
PIRi | A49510, XJBYTK |
RefSeqi | NP_015399.1, NM_001184171.1 |
Genome annotation databases
EnsemblFungii | YPR074C_mRNA; YPR074C; YPR074C |
GeneIDi | 856188 |
KEGGi | sce:YPR074C |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M63302 Genomic DNA Translation: AAA35168.1 X73224 Genomic DNA Translation: CAA51693.1 Z49219 Genomic DNA Translation: CAA89191.1 Z71255 Genomic DNA Translation: CAA94982.1 U51033 Genomic DNA Translation: AAB68125.1 BK006949 Genomic DNA Translation: DAA11494.1 |
PIRi | A49510, XJBYTK |
RefSeqi | NP_015399.1, NM_001184171.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1AY0 | X-ray | 2.60 | A/B | 1-680 | [»] | |
1GPU | X-ray | 1.86 | A/B | 1-680 | [»] | |
1NGS | X-ray | 2.40 | A/B | 1-680 | [»] | |
1TKA | X-ray | 2.70 | A/B | 3-680 | [»] | |
1TKB | X-ray | 2.30 | A/B | 3-680 | [»] | |
1TKC | X-ray | 2.70 | A/B | 3-680 | [»] | |
1TRK | X-ray | 2.00 | A/B | 1-680 | [»] | |
SMRi | P23254 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 36247, 219 interactors |
DIPi | DIP-6765N |
IntActi | P23254, 13 interactors |
MINTi | P23254 |
STRINGi | 4932.YPR074C |
PTM databases
iPTMneti | P23254 |
2D gel databases
SWISS-2DPAGEi | P23254 |
Proteomic databases
MaxQBi | P23254 |
PaxDbi | P23254 |
PRIDEi | P23254 |
TopDownProteomicsi | P23254 |
Genome annotation databases
EnsemblFungii | YPR074C_mRNA; YPR074C; YPR074C |
GeneIDi | 856188 |
KEGGi | sce:YPR074C |
Organism-specific databases
SGDi | S000006278, TKL1 |
VEuPathDBi | FungiDB:YPR074C |
Phylogenomic databases
eggNOGi | KOG0523, Eukaryota |
GeneTreei | ENSGT00940000176704 |
HOGENOMi | CLU_009227_0_0_1 |
InParanoidi | P23254 |
OMAi | GCAPMGY |
Enzyme and pathway databases
BRENDAi | 2.2.1.1, 984 |
SABIO-RKi | P23254 |
Miscellaneous databases
EvolutionaryTracei | P23254 |
PROi | PR:P23254 |
RNActi | P23254, protein |
Family and domain databases
CDDi | cd02012, TPP_TK, 1 hit |
Gene3Di | 3.40.50.920, 1 hit |
InterProi | View protein in InterPro IPR029061, THDP-binding IPR009014, Transketo_C/PFOR_II IPR005475, Transketolase-like_Pyr-bd IPR005478, Transketolase_bac-like IPR020826, Transketolase_BS IPR033248, Transketolase_C IPR033247, Transketolase_fam IPR005474, Transketolase_N |
PANTHERi | PTHR43522, PTHR43522, 1 hit |
Pfami | View protein in Pfam PF02779, Transket_pyr, 1 hit PF02780, Transketolase_C, 1 hit PF00456, Transketolase_N, 1 hit |
SMARTi | View protein in SMART SM00861, Transket_pyr, 1 hit |
SUPFAMi | SSF52518, SSF52518, 2 hits SSF52922, SSF52922, 1 hit |
TIGRFAMsi | TIGR00232, tktlase_bact, 1 hit |
PROSITEi | View protein in PROSITE PS00801, TRANSKETOLASE_1, 1 hit PS00802, TRANSKETOLASE_2, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | TKT1_YEAST | |
Accessioni | P23254Primary (citable) accession number: P23254 Secondary accession number(s): D6W478 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 1, 1991 |
Last sequence update: | January 23, 2007 | |
Last modified: | June 2, 2021 | |
This is version 210 of the entry and version 4 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Fungal Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- Yeast
Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD - Yeast chromosome XVI
Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families