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P23254 (TKT1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 155. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transketolase 1

Short name=TK 1
EC=2.2.1.1
Gene names
Name:TKL1
Ordered Locus Names:YPR074C
ORF Names:YP9499.29C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length680 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.6

Catalytic activity

Sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-ribose 5-phosphate + D-xylulose 5-phosphate. Ref.6 Ref.16 Ref.19

Cofactor

Binds 1 magnesium ion per subunit. Can also utilize other divalent metal cations, such as Ca2+, Mn2+ and Co2+. Ref.11

Binds 1 thiamine pyrophosphate per subunit. Ref.11

Subunit structure

Homodimer.

Miscellaneous

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

Sequence similarities

Belongs to the transketolase family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

RSP5P399402EBI-19291,EBI-16219

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5
Chain2 – 680679Transketolase 1
PRO_0000191904

Regions

Nucleotide binding116 – 1183Thiamine pyrophosphate

Sites

Active site4181Proton donor Probable
Metal binding1571Magnesium
Metal binding1871Magnesium
Metal binding1891Magnesium; via carbonyl oxygen
Binding site301Substrate
Binding site691Thiamine pyrophosphate
Binding site1581Thiamine pyrophosphate; via amide nitrogen
Binding site1871Thiamine pyrophosphate
Binding site2631Substrate
Binding site2631Thiamine pyrophosphate
Binding site3591Substrate
Binding site3861Substrate
Binding site4181Thiamine pyrophosphate
Binding site4451Thiamine pyrophosphate
Binding site4691Substrate
Binding site4771Substrate
Binding site5281Substrate
Site301Important for catalytic activity
Site2631Important for catalytic activity

Amino acid modifications

Modified residue2861Phosphoserine Ref.12
Modified residue3351Phosphoserine Ref.9 Ref.10 Ref.12
Modified residue4021Phosphoserine Ref.10
Modified residue4921Phosphoserine Ref.10

Experimental info

Mutagenesis301H → A or Q: Strongly reduced catalytic activity. Decreases affinity for xylulose 5-phosphate about 15 times. Ref.18
Mutagenesis301H → N: Loss of activity. Ref.18
Mutagenesis691H → A: Reduces catalytic activity by about 98%. Decreased affinity for donor substrate. Ref.18
Mutagenesis1031H → A or N: Reduces activity by over 96% and decreases affinity for thiamine pyrophosphate and xylulose 5-phosphate. Ref.6 Ref.18
Mutagenesis1031H → F: Loss of activity. Ref.6 Ref.18
Mutagenesis1621E → A or Q: Most catalytic properties similar to wild-type. Ref.7
Mutagenesis2631H → A: Strongly reduced catalytic activity. Ref.18
Mutagenesis3591R → A: Slightly reduced affinity for xylulose 5-phosphate and strongly reduced affinity for ribose 5-phosphate. Ref.19
Mutagenesis3821D → A or R: Severe loss of activity. Ref.7
Mutagenesis4691H → A: Strongly reduced affinity for xylulose 5-phosphate and ribose 5-phosphate. Ref.19
Mutagenesis4771D → A: Strongly reduced catalytic activity. Strongly reduced affinity for xylulose 5-phosphate and ribose 5-phosphate. Ref.19
Mutagenesis4811H → A or Q: Reduces catalytic activity by about 95%. Ref.18
Mutagenesis5281R → A: Reduced affinity for xylulose 5-phosphate and strongly reduced affinity for ribose 5-phosphate. Ref.19
Sequence conflict37 – 382MA → RS in AAA35168. Ref.1
Sequence conflict45 – 7733WSQMR…LLYSM → GESNAHEPNQPKTGSTEIDL SCLTVTRSLCCIY in AAA35168. Ref.1
Sequence conflict136 – 1438AATYNKPG → DMPLTTSRA in AAA35168. Ref.1
Sequence conflict232 – 2343AQA → RQR in AAA35168. Ref.1
Sequence conflict243 – 25715LIKMT…GSLHA → FDQNDHNHWLRFLRS AA sequence Ref.1
Sequence conflict3831L → LVLPIL AA sequence Ref.1
Sequence conflict3961D → S in AAA35168. Ref.1
Sequence conflict528 – 53811RQNLPQLEGSS → PDKTCHNWKVAL in AAA35168. Ref.1
Sequence conflict639 – 68042SGKAP…LKKAF → PVRHQKSSSSSVSPQKVLLK ELKRPLHSIRVTS in AAA35168. Ref.1

Secondary structure

.................................................................................................................... 680
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P23254 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 40225EAA23A63835

FASTA68073,806
        10         20         30         40         50         60 
MTQFTDIDKL AVSTIRILAV DTVSKANSGH PGAPLGMAPA AHVLWSQMRM NPTNPDWINR 

        70         80         90        100        110        120 
DRFVLSNGHA VALLYSMLHL TGYDLSIEDL KQFRQLGSRT PGHPEFELPG VEVTTGPLGQ 

       130        140        150        160        170        180 
GISNAVGMAM AQANLAATYN KPGFTLSDNY TYVFLGDGCL QEGISSEASS LAGHLKLGNL 

       190        200        210        220        230        240 
IAIYDDNKIT IDGATSISFD EDVAKRYEAY GWEVLYVENG NEDLAGIAKA IAQAKLSKDK 

       250        260        270        280        290        300 
PTLIKMTTTI GYGSLHAGSH SVHGAPLKAD DVKQLKSKFG FNPDKSFVVP QEVYDHYQKT 

       310        320        330        340        350        360 
ILKPGVEANN KWNKLFSEYQ KKFPELGAEL ARRLSGQLPA NWESKLPTYT AKDSAVATRK 

       370        380        390        400        410        420 
LSETVLEDVY NQLPELIGGS ADLTPSNLTR WKEALDFQPP SSGSGNYSGR YIRYGIREHA 

       430        440        450        460        470        480 
MGAIMNGISA FGANYKPYGG TFLNFVSYAA GAVRLSALSG HPVIWVATHD SIGVGEDGPT 

       490        500        510        520        530        540 
HQPIETLAHF RSLPNIQVWR PADGNEVSAA YKNSLESKHT PSIIALSRQN LPQLEGSSIE 

       550        560        570        580        590        600 
SASKGGYVLQ DVANPDIILV ATGSEVSLSV EAAKTLAAKN IKARVVSLPD FFTFDKQPLE 

       610        620        630        640        650        660 
YRLSVLPDNV PIMSVEVLAT TCWGKYAHQS FGIDRFGASG KAPEVFKFFG FTPEGVAERA 

       670        680 
QKTIAFYKGD KLISPLKKAF 

« Hide

References

« Hide 'large scale' references
[1]"DNA sequence of the yeast transketolase gene."
Fletcher T.S., Kwee I.L., Nakada T., Largman C., Martin B.M.
Biochemistry 31:1892-1896(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
[2]"Yeast TKL1 gene encodes a transketolase that is required for efficient glycolysis and biosynthesis of aromatic amino acids."
Sundstroem M., Lindqvist Y., Schneider G., Hellman U., Ronne H.
J. Biol. Chem. 268:24346-24352(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 208353 / W303-1A.
[3]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M. expand/collapse author list , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
Nature 387:103-105(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]"The N-terminal amino acid sequence of yeast transketolase."
Nixon P.F., Duggleby R.G.
Protein Seq. Data Anal. 4:325-326(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-36.
[6]"His103 in yeast transketolase is required for substrate recognition and catalysis."
Wikner C., Meshalnika L., Nilsson U., Baeckstroem S., Lindqvist Y., Schneider G.
Eur. J. Biochem. 233:750-755(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF HIS-103, FUNCTION, CATALYTIC ACTIVITY.
[7]"Examination of the thiamin diphosphate binding site in yeast transketolase by site-directed mutagenesis."
Meshalkina L., Nilsson U., Wikner C., Kostikowa T., Schneider G.
Eur. J. Biochem. 244:646-652(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF GLU-162 AND ASP-382.
[8]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[9]"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[10]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335; SER-402 AND SER-492, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Effect of bivalent cations on the interaction of transketolase with its donor substrate."
Sevostyanova I.A., Yurshev V.A., Solovjeva O.N., Zabrodskaya S.V., Kochetov G.A.
Proteins 71:541-545(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: COFACTOR.
[12]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-286 AND SER-335, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Sites of ubiquitin attachment in Saccharomyces cerevisiae."
Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Three-dimensional structure of transketolase, a thiamine diphosphate dependent enzyme, at 2.5-A resolution."
Lindqvist Y., Schneider G., Ermler U., Sundstroem M.
EMBO J. 11:2373-2379(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[16]"Specificity of coenzyme binding in thiamin diphosphate-dependent enzymes. Crystal structures of yeast transketolase in complex with analogs of thiamin diphosphate."
Konig S., Schellenberger A., Neef H., Schneider G.
J. Biol. Chem. 269:10879-10882(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 3-679 IN COMPLEX WITH CALCIUM AND THIAMINE PYROPHOSPHATE ANALOGS, CATALYTIC ACTIVITY.
[17]"Refined structure of transketolase from Saccharomyces cerevisiae at 2.0-A resolution."
Nikkola M., Lindqvist Y., Schneider G.
J. Mol. Biol. 238:387-404(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH CALCIUM AND THIAMINE PYROPHOSPHATE.
[18]"Identification of catalytically important residues in yeast transketolase."
Wikner C., Nilsson U., Meshalkina L., Udekwu C., Lindqvist Y., Schneider G.
Biochemistry 36:15643-15649(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH CALCIUM AND THIAMINE PYROPHOSPHATE, MUTAGENESIS OF HIS-30; HIS-69; HIS-103; HIS-263 AND HIS-481.
[19]"Examination of substrate binding in thiamin diphosphate-dependent transketolase by protein crystallography and site-directed mutagenesis."
Nilsson U., Meshalkina L., Lindqvist Y., Schneider G.
J. Biol. Chem. 272:1864-1869(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 2-679 IN COMPLEX WITH CALCIUM; D-ERYTHROSE 4-PHOSPHATE AND THIAMINE PYROPHOSPHATE, CATALYTIC ACTIVITY, MUTAGENESIS OF ARG-359; HIS-469; ASP-477 AND ARG-528.
[20]"Snapshot of a key intermediate in enzymatic thiamin catalysis: crystal structure of the alpha-carbanion of (alpha,beta-dihydroxyethyl)-thiamin diphosphate in the active site of transketolase from Saccharomyces cerevisiae."
Fiedler E., Thorell S., Sandalova T., Golbik R., Konig S., Schneider G.
Proc. Natl. Acad. Sci. U.S.A. 99:591-595(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) OF 2-679 IN COMPLEX WITH REACTION INTERMEDIATE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRXJBYTK. A49510.
RefSeqNP_015399.1. NM_001184171.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP23254.
SMRP23254. Positions 3-680.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid36247. 103 interactions.
DIPDIP-6765N.
IntActP23254. 10 interactions.
MINTMINT-629387.
STRING4932.YPR074C.

2D gel databases

SWISS-2DPAGEP23254.

Proteomic databases

MaxQBP23254.
PaxDbP23254.
PeptideAtlasP23254.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYPR074C; YPR074C; YPR074C.
GeneID856188.
KEGGsce:YPR074C.

Organism-specific databases

SGDS000006278. TKL1.

Phylogenomic databases

eggNOGCOG0021.
GeneTreeENSGT00390000005240.
HOGENOMHOG000225953.
KOK00615.
OMAMETVECW.
OrthoDBEOG78H42J.

Enzyme and pathway databases

BioCycYEAST:YPR074C-MONOMER.
SABIO-RKP23254.

Gene expression databases

GenevestigatorP23254.

Family and domain databases

Gene3D3.40.50.920. 1 hit.
3.40.50.970. 2 hits.
InterProIPR029061. THDP-binding.
IPR009014. Transketo_C/Pyr-ferredox_oxred.
IPR005475. Transketolase-like_Pyr-bd.
IPR005478. Transketolase_bac-like.
IPR020826. Transketolase_BS.
IPR005476. Transketolase_C.
IPR005474. Transketolase_N.
[Graphical view]
PfamPF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
PF00456. Transketolase_N. 1 hit.
[Graphical view]
SMARTSM00861. Transket_pyr. 1 hit.
[Graphical view]
SUPFAMSSF52518. SSF52518. 2 hits.
SSF52922. SSF52922. 1 hit.
TIGRFAMsTIGR00232. tktlase_bact. 1 hit.
PROSITEPS00801. TRANSKETOLASE_1. 1 hit.
PS00802. TRANSKETOLASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP23254.
NextBio981372.

Entry information

Entry nameTKT1_YEAST
AccessionPrimary (citable) accession number: P23254
Secondary accession number(s): D6W478
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 155 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XVI

Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references