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Protein

Transketolase 1

Gene

TKL1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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 Publication

Catalytic activityi

Sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-ribose 5-phosphate + D-xylulose 5-phosphate.3 Publications

Cofactori

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei30Substrate1
Sitei30Important for catalytic activity1
Binding sitei69Thiamine pyrophosphate3 Publications1
Metal bindingi157Magnesium1
Binding sitei158Thiamine pyrophosphate; via amide nitrogen3 Publications1
Metal bindingi187Magnesium1
Binding sitei187Thiamine pyrophosphate3 Publications1
Metal bindingi189Magnesium; via carbonyl oxygen1
Binding sitei263Substrate1
Binding sitei263Thiamine pyrophosphate3 Publications1
Sitei263Important for catalytic activity1
Binding sitei359Substrate1
Binding sitei386Substrate1
Active sitei418Proton donorCurated1
Binding sitei418Thiamine pyrophosphate3 Publications1
Binding sitei445Thiamine pyrophosphate3 Publications1
Binding sitei469Substrate1
Binding sitei477Substrate1
Binding sitei528Substrate1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi116 – 118Thiamine pyrophosphate3 Publications3

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • transketolase activity Source: SGD

GO - Biological processi

  • pentose-phosphate shunt Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Ligandi

Calcium, Magnesium, Metal-binding, Thiamine pyrophosphate

Enzyme and pathway databases

BioCyciYEAST:YPR074C-MONOMER.
BRENDAi2.2.1.1. 984.
ReactomeiR-SCE-163754. Insulin effects increased synthesis of Xylulose-5-Phosphate.
R-SCE-71336. Pentose phosphate pathway (hexose monophosphate shunt).
SABIO-RKP23254.

Names & Taxonomyi

Protein namesi
Recommended name:
Transketolase 1 (EC:2.2.1.1)
Short name:
TK 1
Gene namesi
Name:TKL1
Ordered Locus Names:YPR074C
ORF Names:YP9499.29C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XVI

Organism-specific databases

EuPathDBiFungiDB:YPR074C.
SGDiS000006278. TKL1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: SGD
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi30H → A or Q: Strongly reduced catalytic activity. Decreases affinity for xylulose 5-phosphate about 15 times. 1 Publication1
Mutagenesisi30H → N: Loss of activity. 1 Publication1
Mutagenesisi69H → A: Reduces catalytic activity by about 98%. Decreased affinity for donor substrate. 1 Publication1
Mutagenesisi103H → A or N: Reduces activity by over 96% and decreases affinity for thiamine pyrophosphate and xylulose 5-phosphate. 2 Publications1
Mutagenesisi103H → F: Loss of activity. 2 Publications1
Mutagenesisi162E → A or Q: Most catalytic properties similar to wild-type. 1 Publication1
Mutagenesisi263H → A: Strongly reduced catalytic activity. 1 Publication1
Mutagenesisi359R → A: Slightly reduced affinity for xylulose 5-phosphate and strongly reduced affinity for ribose 5-phosphate. 1 Publication1
Mutagenesisi382D → A or R: Severe loss of activity. 1 Publication1
Mutagenesisi469H → A: Strongly reduced affinity for xylulose 5-phosphate and ribose 5-phosphate. 1 Publication1
Mutagenesisi477D → A: Strongly reduced catalytic activity. Strongly reduced affinity for xylulose 5-phosphate and ribose 5-phosphate. 1 Publication1
Mutagenesisi481H → A or Q: Reduces catalytic activity by about 95%. 1 Publication1
Mutagenesisi528R → A: Reduced affinity for xylulose 5-phosphate and strongly reduced affinity for ribose 5-phosphate. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001919042 – 680Transketolase 1Add BLAST679

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei286PhosphoserineCombined sources1
Modified residuei335PhosphoserineCombined sources1
Modified residuei402PhosphoserineCombined sources1
Modified residuei492PhosphoserineCombined sources1
Cross-linki647Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP23254.
PRIDEiP23254.
TopDownProteomicsiP23254.

2D gel databases

SWISS-2DPAGEP23254.

PTM databases

iPTMnetiP23254.

Interactioni

Subunit structurei

Homodimer.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
RSP5P399402EBI-19291,EBI-16219

Protein-protein interaction databases

BioGridi36247. 106 interactors.
DIPiDIP-6765N.
IntActiP23254. 11 interactors.
MINTiMINT-629387.

Structurei

Secondary structure

1680
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi6 – 26Combined sources21
Helixi32 – 46Combined sources15
Beta strandi62 – 67Combined sources6
Helixi68 – 70Combined sources3
Helixi71 – 80Combined sources10
Helixi87 – 90Combined sources4
Turni91 – 94Combined sources4
Helixi120 – 139Combined sources20
Beta strandi151 – 155Combined sources5
Helixi157 – 161Combined sources5
Helixi163 – 174Combined sources12
Beta strandi180 – 186Combined sources7
Beta strandi188 – 190Combined sources3
Beta strandi191 – 194Combined sources4
Helixi195 – 197Combined sources3
Helixi203 – 210Combined sources8
Beta strandi213 – 218Combined sources6
Turni220 – 222Combined sources3
Helixi224 – 236Combined sources13
Beta strandi242 – 247Combined sources6
Turni250 – 253Combined sources4
Turni255 – 258Combined sources4
Helixi260 – 262Combined sources3
Beta strandi263 – 265Combined sources3
Helixi269 – 278Combined sources10
Helixi291 – 300Combined sources10
Helixi302 – 322Combined sources21
Helixi324 – 334Combined sources11
Helixi342 – 345Combined sources4
Helixi358 – 369Combined sources12
Turni370 – 372Combined sources3
Beta strandi376 – 382Combined sources7
Helixi384 – 387Combined sources4
Beta strandi402 – 406Combined sources5
Beta strandi411 – 413Combined sources3
Helixi418 – 431Combined sources14
Beta strandi436 – 442Combined sources7
Helixi443 – 446Combined sources4
Helixi447 – 449Combined sources3
Helixi450 – 459Combined sources10
Beta strandi464 – 468Combined sources5
Helixi472 – 474Combined sources3
Turni479 – 481Combined sources3
Helixi486 – 491Combined sources6
Beta strandi493 – 495Combined sources3
Beta strandi497 – 499Combined sources3
Helixi504 – 516Combined sources13
Beta strandi522 – 525Combined sources4
Beta strandi528 – 531Combined sources4
Helixi539 – 542Combined sources4
Beta strandi547 – 550Combined sources4
Beta strandi556 – 561Combined sources6
Helixi565 – 577Combined sources13
Turni578 – 580Combined sources3
Beta strandi583 – 587Combined sources5
Helixi591 – 596Combined sources6
Helixi599 – 605Combined sources7
Beta strandi608 – 610Combined sources3
Beta strandi612 – 615Combined sources4
Helixi623 – 625Combined sources3
Beta strandi628 – 631Combined sources4
Helixi642 – 648Combined sources7
Helixi653 – 667Combined sources15

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AY0X-ray2.60A/B1-680[»]
1GPUX-ray1.86A/B1-680[»]
1NGSX-ray2.40A/B1-680[»]
1TKAX-ray2.70A/B3-680[»]
1TKBX-ray2.30A/B3-680[»]
1TKCX-ray2.70A/B3-680[»]
1TRKX-ray2.00A/B1-680[»]
ProteinModelPortaliP23254.
SMRiP23254.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP23254.

Family & Domainsi

Sequence similaritiesi

Belongs to the transketolase family.Curated

Phylogenomic databases

GeneTreeiENSGT00390000005240.
HOGENOMiHOG000225953.
InParanoidiP23254.
KOiK00615.
OMAiWEVLYVE.
OrthoDBiEOG092C0ZWN.

Family and domain databases

Gene3Di3.40.50.920. 1 hit.
3.40.50.970. 2 hits.
InterProiIPR029061. 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.
[Graphical view]
PANTHERiPTHR11624. PTHR11624. 2 hits.
PfamiPF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
PF00456. Transketolase_N. 1 hit.
[Graphical view]
SMARTiSM00861. Transket_pyr. 1 hit.
[Graphical view]
SUPFAMiSSF52518. SSF52518. 2 hits.
SSF52922. SSF52922. 1 hit.
TIGRFAMsiTIGR00232. tktlase_bact. 1 hit.
PROSITEiPS00801. TRANSKETOLASE_1. 1 hit.
PS00802. TRANSKETOLASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P23254-1 [UniParc]FASTAAdd to basket

« Hide

        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
Length:680
Mass (Da):73,806
Last modified:January 23, 2007 - v4
Checksum:i40225EAA23A63835
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti37 – 38MA → RS in AAA35168 (PubMed:1737042).Curated2
Sequence conflicti45 – 77WSQMR…LLYSM → GESNAHEPNQPKTGSTEIDL SCLTVTRSLCCIY in AAA35168 (PubMed:1737042).CuratedAdd BLAST33
Sequence conflicti136 – 143AATYNKPG → DMPLTTSRA in AAA35168 (PubMed:1737042).Curated8
Sequence conflicti232 – 234AQA → RQR in AAA35168 (PubMed:1737042).Curated3
Sequence conflicti243 – 257LIKMT…GSLHA → FDQNDHNHWLRFLRS AA sequence (PubMed:1737042).CuratedAdd BLAST15
Sequence conflicti383L → LVLPIL AA sequence (PubMed:1737042).Curated1
Sequence conflicti396D → S in AAA35168 (PubMed:1737042).Curated1
Sequence conflicti528 – 538RQNLPQLEGSS → PDKTCHNWKVAL in AAA35168 (PubMed:1737042).CuratedAdd BLAST11
Sequence conflicti639 – 680SGKAP…LKKAF → PVRHQKSSSSSVSPQKVLLK ELKRPLHSIRVTS in AAA35168 (PubMed:1737042).CuratedAdd BLAST42

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.
PIRiA49510. XJBYTK.
RefSeqiNP_015399.1. NM_001184171.1.

Genome annotation databases

EnsemblFungiiYPR074C; YPR074C; YPR074C.
GeneIDi856188.
KEGGisce:YPR074C.

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.
PIRiA49510. XJBYTK.
RefSeqiNP_015399.1. NM_001184171.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AY0X-ray2.60A/B1-680[»]
1GPUX-ray1.86A/B1-680[»]
1NGSX-ray2.40A/B1-680[»]
1TKAX-ray2.70A/B3-680[»]
1TKBX-ray2.30A/B3-680[»]
1TKCX-ray2.70A/B3-680[»]
1TRKX-ray2.00A/B1-680[»]
ProteinModelPortaliP23254.
SMRiP23254.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36247. 106 interactors.
DIPiDIP-6765N.
IntActiP23254. 11 interactors.
MINTiMINT-629387.

PTM databases

iPTMnetiP23254.

2D gel databases

SWISS-2DPAGEP23254.

Proteomic databases

MaxQBiP23254.
PRIDEiP23254.
TopDownProteomicsiP23254.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYPR074C; YPR074C; YPR074C.
GeneIDi856188.
KEGGisce:YPR074C.

Organism-specific databases

EuPathDBiFungiDB:YPR074C.
SGDiS000006278. TKL1.

Phylogenomic databases

GeneTreeiENSGT00390000005240.
HOGENOMiHOG000225953.
InParanoidiP23254.
KOiK00615.
OMAiWEVLYVE.
OrthoDBiEOG092C0ZWN.

Enzyme and pathway databases

BioCyciYEAST:YPR074C-MONOMER.
BRENDAi2.2.1.1. 984.
ReactomeiR-SCE-163754. Insulin effects increased synthesis of Xylulose-5-Phosphate.
R-SCE-71336. Pentose phosphate pathway (hexose monophosphate shunt).
SABIO-RKP23254.

Miscellaneous databases

EvolutionaryTraceiP23254.
PROiP23254.

Family and domain databases

Gene3Di3.40.50.920. 1 hit.
3.40.50.970. 2 hits.
InterProiIPR029061. 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.
[Graphical view]
PANTHERiPTHR11624. PTHR11624. 2 hits.
PfamiPF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
PF00456. Transketolase_N. 1 hit.
[Graphical view]
SMARTiSM00861. Transket_pyr. 1 hit.
[Graphical view]
SUPFAMiSSF52518. SSF52518. 2 hits.
SSF52922. SSF52922. 1 hit.
TIGRFAMsiTIGR00232. tktlase_bact. 1 hit.
PROSITEiPS00801. TRANSKETOLASE_1. 1 hit.
PS00802. TRANSKETOLASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTKT1_YEAST
AccessioniPrimary (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: November 2, 2016
This is version 176 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 40300 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XVI
    Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.