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P23254

- TKT1_YEAST

UniProt

P23254 - TKT1_YEAST

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Protein

Transketolase 1

Gene

TKL1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - 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

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei30 – 301Substrate
Sitei30 – 301Important for catalytic activity
Binding sitei69 – 691Thiamine pyrophosphate3 Publications
Metal bindingi157 – 1571Magnesium
Binding sitei158 – 1581Thiamine pyrophosphate; via amide nitrogen3 Publications
Metal bindingi187 – 1871Magnesium
Binding sitei187 – 1871Thiamine pyrophosphate3 Publications
Metal bindingi189 – 1891Magnesium; via carbonyl oxygen
Binding sitei263 – 2631Substrate
Binding sitei263 – 2631Thiamine pyrophosphate3 Publications
Sitei263 – 2631Important for catalytic activity
Binding sitei359 – 3591Substrate
Binding sitei386 – 3861Substrate
Active sitei418 – 4181Proton donorCurated
Binding sitei418 – 4181Thiamine pyrophosphate3 Publications
Binding sitei445 – 4451Thiamine pyrophosphate3 Publications
Binding sitei469 – 4691Substrate
Binding sitei477 – 4771Substrate
Binding sitei528 – 5281Substrate

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi116 – 1183Thiamine pyrophosphate3 Publications

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. transketolase activity Source: SGD

GO - Biological processi

  1. 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.
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
ProteomesiUP000002311: Chromosome XVI

Organism-specific databases

SGDiS000006278. TKL1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: SGD
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi30 – 301H → A or Q: Strongly reduced catalytic activity. Decreases affinity for xylulose 5-phosphate about 15 times. 1 Publication
Mutagenesisi30 – 301H → N: Loss of activity. 1 Publication
Mutagenesisi69 – 691H → A: Reduces catalytic activity by about 98%. Decreased affinity for donor substrate. 1 Publication
Mutagenesisi103 – 1031H → A or N: Reduces activity by over 96% and decreases affinity for thiamine pyrophosphate and xylulose 5-phosphate. 2 Publications
Mutagenesisi103 – 1031H → F: Loss of activity. 2 Publications
Mutagenesisi162 – 1621E → A or Q: Most catalytic properties similar to wild-type. 1 Publication
Mutagenesisi263 – 2631H → A: Strongly reduced catalytic activity. 1 Publication
Mutagenesisi359 – 3591R → A: Slightly reduced affinity for xylulose 5-phosphate and strongly reduced affinity for ribose 5-phosphate. 1 Publication
Mutagenesisi382 – 3821D → A or R: Severe loss of activity. 1 Publication
Mutagenesisi469 – 4691H → A: Strongly reduced affinity for xylulose 5-phosphate and ribose 5-phosphate. 1 Publication
Mutagenesisi477 – 4771D → A: Strongly reduced catalytic activity. Strongly reduced affinity for xylulose 5-phosphate and ribose 5-phosphate. 1 Publication
Mutagenesisi481 – 4811H → A or Q: Reduces catalytic activity by about 95%. 1 Publication
Mutagenesisi528 – 5281R → A: Reduced affinity for xylulose 5-phosphate and strongly reduced affinity for ribose 5-phosphate. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 680679Transketolase 1PRO_0000191904Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei286 – 2861Phosphoserine1 Publication
Modified residuei335 – 3351Phosphoserine3 Publications
Modified residuei402 – 4021Phosphoserine1 Publication
Modified residuei492 – 4921Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP23254.
PaxDbiP23254.
PeptideAtlasiP23254.

2D gel databases

SWISS-2DPAGEP23254.

Expressioni

Gene expression databases

GenevestigatoriP23254.

Interactioni

Subunit structurei

Homodimer.5 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi36247. 103 interactions.
DIPiDIP-6765N.
IntActiP23254. 10 interactions.
MINTiMINT-629387.
STRINGi4932.YPR074C.

Structurei

Secondary structure

1
680
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 2621
Helixi32 – 4615
Beta strandi62 – 676
Helixi68 – 703
Helixi71 – 8010
Helixi87 – 904
Turni91 – 944
Helixi120 – 13920
Beta strandi151 – 1555
Helixi157 – 1615
Helixi163 – 17412
Beta strandi180 – 1867
Beta strandi188 – 1903
Beta strandi191 – 1944
Helixi195 – 1973
Helixi203 – 2108
Beta strandi213 – 2186
Turni220 – 2223
Helixi224 – 23613
Beta strandi242 – 2476
Turni250 – 2534
Turni255 – 2584
Helixi260 – 2623
Beta strandi263 – 2653
Helixi269 – 27810
Helixi291 – 30010
Helixi302 – 32221
Helixi324 – 33411
Helixi342 – 3454
Helixi358 – 36912
Turni370 – 3723
Beta strandi376 – 3827
Helixi384 – 3874
Beta strandi402 – 4065
Beta strandi411 – 4133
Helixi418 – 43114
Beta strandi436 – 4427
Helixi443 – 4464
Helixi447 – 4493
Helixi450 – 45910
Beta strandi464 – 4685
Helixi472 – 4743
Turni479 – 4813
Helixi486 – 4916
Beta strandi493 – 4953
Beta strandi497 – 4993
Helixi504 – 51613
Beta strandi522 – 5254
Beta strandi528 – 5314
Helixi539 – 5424
Beta strandi547 – 5504
Beta strandi556 – 5616
Helixi565 – 57713
Turni578 – 5803
Beta strandi583 – 5875
Helixi591 – 5966
Helixi599 – 6057
Beta strandi608 – 6103
Beta strandi612 – 6154
Helixi623 – 6253
Beta strandi628 – 6314
Helixi642 – 6487
Helixi653 – 66715

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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. Positions 3-680.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP23254.

Family & Domainsi

Sequence similaritiesi

Belongs to the transketolase family.Curated

Phylogenomic databases

eggNOGiCOG0021.
GeneTreeiENSGT00390000005240.
HOGENOMiHOG000225953.
InParanoidiP23254.
KOiK00615.
OMAiMETVECW.
OrthoDBiEOG78H42J.

Family and domain databases

Gene3Di3.40.50.920. 1 hit.
3.40.50.970. 2 hits.
InterProiIPR029061. 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]
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti37 – 382MA → RS in AAA35168. (PubMed:1737042)Curated
Sequence conflicti45 – 7733WSQMR…LLYSM → GESNAHEPNQPKTGSTEIDL SCLTVTRSLCCIY in AAA35168. (PubMed:1737042)CuratedAdd
BLAST
Sequence conflicti136 – 1438AATYNKPG → DMPLTTSRA in AAA35168. (PubMed:1737042)Curated
Sequence conflicti232 – 2343AQA → RQR in AAA35168. (PubMed:1737042)Curated
Sequence conflicti243 – 25715LIKMT…GSLHA → FDQNDHNHWLRFLRS AA sequence (PubMed:1737042)CuratedAdd
BLAST
Sequence conflicti383 – 3831L → LVLPIL AA sequence (PubMed:1737042)Curated
Sequence conflicti396 – 3961D → S in AAA35168. (PubMed:1737042)Curated
Sequence conflicti528 – 53811RQNLPQLEGSS → PDKTCHNWKVAL in AAA35168. (PubMed:1737042)CuratedAdd
BLAST
Sequence conflicti639 – 68042SGKAP…LKKAF → PVRHQKSSSSSVSPQKVLLK ELKRPLHSIRVTS in AAA35168. (PubMed:1737042)CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali P23254.
SMRi P23254. Positions 3-680.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 36247. 103 interactions.
DIPi DIP-6765N.
IntActi P23254. 10 interactions.
MINTi MINT-629387.
STRINGi 4932.YPR074C.

2D gel databases

SWISS-2DPAGE P23254.

Proteomic databases

MaxQBi P23254.
PaxDbi P23254.
PeptideAtlasi P23254.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YPR074C ; YPR074C ; YPR074C .
GeneIDi 856188.
KEGGi sce:YPR074C.

Organism-specific databases

SGDi S000006278. TKL1.

Phylogenomic databases

eggNOGi COG0021.
GeneTreei ENSGT00390000005240.
HOGENOMi HOG000225953.
InParanoidi P23254.
KOi K00615.
OMAi METVECW.
OrthoDBi EOG78H42J.

Enzyme and pathway databases

BioCyci YEAST:YPR074C-MONOMER.
SABIO-RK P23254.

Miscellaneous databases

EvolutionaryTracei P23254.
NextBioi 981372.

Gene expression databases

Genevestigatori P23254.

Family and domain databases

Gene3Di 3.40.50.920. 1 hit.
3.40.50.970. 2 hits.
InterProi IPR029061. 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 ]
Pfami PF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
PF00456. Transketolase_N. 1 hit.
[Graphical view ]
SMARTi SM00861. Transket_pyr. 1 hit.
[Graphical view ]
SUPFAMi SSF52518. SSF52518. 2 hits.
SSF52922. SSF52922. 1 hit.
TIGRFAMsi TIGR00232. tktlase_bact. 1 hit.
PROSITEi PS00801. TRANSKETOLASE_1. 1 hit.
PS00802. TRANSKETOLASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. 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.
    , 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. 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. 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. 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.

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: October 29, 2014
This is version 157 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

External Data

Dasty 3