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P23254

- TKT1_YEAST

UniProt

P23254 - TKT1_YEAST

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
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    • History
      Entry version 156 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    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. protein binding Source: IntAct
    3. transketolase activity Source: SGD

    GO - Biological processi

    1. pentose-phosphate shunt Source: SGD

    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

    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.
    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

    MTQFTDIDKL AVSTIRILAV DTVSKANSGH PGAPLGMAPA AHVLWSQMRM    50
    NPTNPDWINR DRFVLSNGHA VALLYSMLHL TGYDLSIEDL KQFRQLGSRT 100
    PGHPEFELPG VEVTTGPLGQ GISNAVGMAM AQANLAATYN KPGFTLSDNY 150
    TYVFLGDGCL QEGISSEASS LAGHLKLGNL IAIYDDNKIT IDGATSISFD 200
    EDVAKRYEAY GWEVLYVENG NEDLAGIAKA IAQAKLSKDK PTLIKMTTTI 250
    GYGSLHAGSH SVHGAPLKAD DVKQLKSKFG FNPDKSFVVP QEVYDHYQKT 300
    ILKPGVEANN KWNKLFSEYQ KKFPELGAEL ARRLSGQLPA NWESKLPTYT 350
    AKDSAVATRK LSETVLEDVY NQLPELIGGS ADLTPSNLTR WKEALDFQPP 400
    SSGSGNYSGR YIRYGIREHA MGAIMNGISA FGANYKPYGG TFLNFVSYAA 450
    GAVRLSALSG HPVIWVATHD SIGVGEDGPT HQPIETLAHF RSLPNIQVWR 500
    PADGNEVSAA YKNSLESKHT PSIIALSRQN LPQLEGSSIE SASKGGYVLQ 550
    DVANPDIILV ATGSEVSLSV EAAKTLAAKN IKARVVSLPD FFTFDKQPLE 600
    YRLSVLPDNV PIMSVEVLAT TCWGKYAHQS FGIDRFGASG KAPEVFKFFG 650
    FTPEGVAERA QKTIAFYKGD KLISPLKKAF 680
    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.
    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

    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 1, 2014
    This is version 156 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