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Protein

Alpha,alpha-trehalose-phosphate synthase [UDP-forming] 56 kDa subunit

Gene

TPS1

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

Synthase catalytic subunit of the trehalose synthase complex that catalyzes the production of trehalose from glucose-6-phosphate and UDP-glucose in a two step process. Can function independently of the complex.1 Publication

Catalytic activityi

UDP-glucose + D-glucose 6-phosphate = UDP + alpha,alpha-trehalose 6-phosphate.

Enzyme regulationi

Activated by fructose 6-phosphate. Inorganic phosphate inhibits the synthase activity in the complex, but activates the synthase activity in the free monomeric form.1 Publication

Kineticsi

  1. KM=3.5 mM for D-glucose 6-phosphate1 Publication
  2. KM=0.5 mM for UDP-glucose1 Publication

    GO - Molecular functioni

    • alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity Source: SGD
    • identical protein binding Source: IntAct

    GO - Biological processi

    • cellular carbohydrate metabolic process Source: SGD
    • cellular response to desiccation Source: SGD
    • cellular response to heat Source: SGD
    • cellular response to oxidative stress Source: SGD
    • trehalose biosynthetic process Source: SGD
    Complete GO annotation...

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Biological processi

    Stress response

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-563.
    YEAST:YBR126C-MONOMER.
    BRENDAi2.4.1.15. 984.

    Protein family/group databases

    CAZyiGT20. Glycosyltransferase Family 20.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alpha,alpha-trehalose-phosphate synthase [UDP-forming] 56 kDa subunit (EC:2.4.1.15)
    Alternative name(s):
    General glucose sensor subunit 1
    Glycogen metabolism control protein GLC6
    Trehalose synthase complex catalytic subunit TPS1
    Trehalose-6-phosphate synthase
    UDP-glucose-glucosephosphate glucosyltransferase
    Gene namesi
    Name:TPS1
    Synonyms:BYP1, CIF1, FDP1, GGS1, GLC6, TSS1
    Ordered Locus Names:YBR126C
    ORF Names:YBR0922
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311 Componenti: Chromosome II

    Organism-specific databases

    CYGDiYBR126c.
    EuPathDBiFungiDB:YBR126C.
    SGDiS000000330. TPS1.

    Subcellular locationi

    GO - Cellular componenti

    • alpha,alpha-trehalose-phosphate synthase complex (UDP-forming) Source: SGD
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi223 – 2231H → Y in GLC6-1; low glycogen accumulation. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 495495Alpha,alpha-trehalose-phosphate synthase [UDP-forming] 56 kDa subunitPRO_0000122502Add
    BLAST

    Proteomic databases

    MaxQBiQ00764.
    PaxDbiQ00764.
    PeptideAtlasiQ00764.
    PRIDEiQ00764.

    Expressioni

    Inductioni

    Either partial repression by glucose or induction by galactose. Induced by heat shock.

    Interactioni

    Subunit structurei

    The trehalose synthase complex is composed of the two catalytic subunits TPS1 and TPS2 and at least one of the two regulatory subunits TPS3 or TSL1.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself3EBI-19430,EBI-19430
    TPS2P316888EBI-19430,EBI-19440
    TPS3P384266EBI-19430,EBI-19448
    TSL1P384277EBI-19430,EBI-19638

    Protein-protein interaction databases

    BioGridi32827. 223 interactions.
    DIPiDIP-744N.
    IntActiQ00764. 26 interactions.
    MINTiMINT-618278.
    STRINGi4932.YBR126C.

    Structurei

    3D structure databases

    ProteinModelPortaliQ00764.
    SMRiQ00764. Positions 15-480.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyltransferase 20 family.Curated

    Phylogenomic databases

    eggNOGiCOG0380.
    GeneTreeiENSGT00550000075557.
    HOGENOMiHOG000191477.
    InParanoidiQ00764.
    KOiK00697.
    OMAiWLAYNEA.
    OrthoDBiEOG76QFS6.

    Family and domain databases

    InterProiIPR001830. Glyco_trans_20.
    IPR012766. Trehalose_OtsA.
    [Graphical view]
    PfamiPF00982. Glyco_transf_20. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR02400. trehalose_OtsA. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q00764-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MTTDNAKAQL TSSSGGNIIV VSNRLPVTIT KNSSTGQYEY AMSSGGLVTA
    60 70 80 90 100
    LEGLKKTYTF KWFGWPGLEI PDDEKDQVRK DLLEKFNAVP IFLSDEIADL
    110 120 130 140 150
    HYNGFSNSIL WPLFHYHPGE INFDENAWLA YNEANQTFTN EIAKTMNHND
    160 170 180 190 200
    LIWVHDYHLM LVPEMLRVKI HEKQLQNVKV GWFLHTPFPS SEIYRILPVR
    210 220 230 240 250
    QEILKGVLSC DLVGFHTYDY ARHFLSSVQR VLNVNTLPNG VEYQGRFVNV
    260 270 280 290 300
    GAFPIGIDVD KFTDGLKKES VQKRIQQLKE TFKGCKIIVG VDRLDYIKGV
    310 320 330 340 350
    PQKLHAMEVF LNEHPEWRGK VVLVQVAVPS RGDVEEYQYL RSVVNELVGR
    360 370 380 390 400
    INGQFGTVEF VPIHFMHKSI PFEELISLYA VSDVCLVSST RDGMNLVSYE
    410 420 430 440 450
    YIACQEEKKG SLILSEFTGA AQSLNGAIIV NPWNTDDLSD AINEALTLPD
    460 470 480 490
    VKKEVNWEKL YKYISKYTSA FWGENFVHEL YSTSSSSTSS SATKN
    Length:495
    Mass (Da):56,148
    Last modified:July 1, 1993 - v2
    Checksum:i47325A0FA3554E3D
    GO

    Sequence cautioni

    The sequence AAA66891.1 differs from that shown. Reason: Frameshift at position 32. Curated

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti75 – 751K → M in CAA48296 (PubMed:1425702).Curated
    Sequence conflicti101 – 1011H → L in CAA48296 (PubMed:1425702).Curated
    Sequence conflicti104 – 1041G → W in CAA48296 (PubMed:1425702).Curated
    Sequence conflicti129 – 1302LA → FG in CAA43580 (PubMed:1315471).Curated
    Sequence conflicti217 – 2171T → S in CAA48296 (PubMed:1425702).Curated
    Sequence conflicti288 – 2881I → L in CAA48296 (PubMed:1425702).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    J04450 Genomic DNA. Translation: AAA66891.1. Frameshift.
    X68214 mRNA. Translation: CAA48296.1.
    X68496 Genomic DNA. Translation: CAA48510.1.
    X67499 Genomic DNA. Translation: CAA47834.1.
    X61275 Genomic DNA. Translation: CAA43580.1.
    L21999 Genomic DNA. Translation: AAA53672.1.
    X78993 Genomic DNA. Translation: CAA55627.1. Sequence problems.
    X75891 Genomic DNA. Translation: CAA53485.1.
    AF061037 mRNA. Translation: AAC16974.1.
    AY598966 Genomic DNA. Translation: AAT27376.1.
    AY598964 Genomic DNA. Translation: AAT27374.1.
    Z35995 Genomic DNA. Translation: CAA85083.1.
    AY693147 Genomic DNA. Translation: AAT93166.1.
    BK006936 Genomic DNA. Translation: DAA07243.1.
    PIRiS34979.
    RefSeqiNP_009684.1. NM_001178474.1.

    Genome annotation databases

    EnsemblFungiiYBR126C; YBR126C; YBR126C.
    GeneIDi852423.
    KEGGisce:YBR126C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    J04450 Genomic DNA. Translation: AAA66891.1. Frameshift.
    X68214 mRNA. Translation: CAA48296.1.
    X68496 Genomic DNA. Translation: CAA48510.1.
    X67499 Genomic DNA. Translation: CAA47834.1.
    X61275 Genomic DNA. Translation: CAA43580.1.
    L21999 Genomic DNA. Translation: AAA53672.1.
    X78993 Genomic DNA. Translation: CAA55627.1. Sequence problems.
    X75891 Genomic DNA. Translation: CAA53485.1.
    AF061037 mRNA. Translation: AAC16974.1.
    AY598966 Genomic DNA. Translation: AAT27376.1.
    AY598964 Genomic DNA. Translation: AAT27374.1.
    Z35995 Genomic DNA. Translation: CAA85083.1.
    AY693147 Genomic DNA. Translation: AAT93166.1.
    BK006936 Genomic DNA. Translation: DAA07243.1.
    PIRiS34979.
    RefSeqiNP_009684.1. NM_001178474.1.

    3D structure databases

    ProteinModelPortaliQ00764.
    SMRiQ00764. Positions 15-480.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi32827. 223 interactions.
    DIPiDIP-744N.
    IntActiQ00764. 26 interactions.
    MINTiMINT-618278.
    STRINGi4932.YBR126C.

    Protein family/group databases

    CAZyiGT20. Glycosyltransferase Family 20.

    Proteomic databases

    MaxQBiQ00764.
    PaxDbiQ00764.
    PeptideAtlasiQ00764.
    PRIDEiQ00764.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiYBR126C; YBR126C; YBR126C.
    GeneIDi852423.
    KEGGisce:YBR126C.

    Organism-specific databases

    CYGDiYBR126c.
    EuPathDBiFungiDB:YBR126C.
    SGDiS000000330. TPS1.

    Phylogenomic databases

    eggNOGiCOG0380.
    GeneTreeiENSGT00550000075557.
    HOGENOMiHOG000191477.
    InParanoidiQ00764.
    KOiK00697.
    OMAiWLAYNEA.
    OrthoDBiEOG76QFS6.

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-563.
    YEAST:YBR126C-MONOMER.
    BRENDAi2.4.1.15. 984.

    Miscellaneous databases

    NextBioi971291.
    PROiQ00764.

    Family and domain databases

    InterProiIPR001830. Glyco_trans_20.
    IPR012766. Trehalose_OtsA.
    [Graphical view]
    PfamiPF00982. Glyco_transf_20. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR02400. trehalose_OtsA. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "A conserved gene encoding the 57-kDa subunit of the yeast vacuolar H+-ATPase."
      Nelson H., Mandiyan S., Nelson N.
      J. Biol. Chem. 264:1775-1778(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Characterization of the 56-kDa subunit of yeast trehalose-6-phosphate synthase and cloning of its gene reveal its identity with the product of CIF1, a regulator of carbon catabolite inactivation."
      Bell W., Klaassen P., Ohnacker M., Boller T., Herweijer M., Schoppink P., van der Zee P., Wiemken A.
      Eur. J. Biochem. 209:951-959(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: C13-ABYS86.
    3. "A yeast gene for trehalose-6-phosphate synthase and its complementation of an Escherichia coli otsA mutant."
      McDougall J., Kaasen I., Stroem A.R.
      FEMS Microbiol. Lett. 107:25-30(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "Molecular cloning of CIF1, a yeast gene necessary for growth on glucose."
      Gonzales M.I., Stucka R., Blazquez M.A., Feldmann H., Gancedo C.
      Yeast 8:183-192(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: C836.
    5. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    6. "Characterization of glycogen-deficient glc mutants of Saccharomyces cerevisiae."
      Cannon J.F., Pringle J.R., Fiechter A., Khalil M.
      Genetics 136:485-503(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF HIS-223.
    7. "Cloning of two related genes encoding the 56-kDa and 123-kDa subunits of trehalose synthase from the yeast Saccharomyces cerevisiae."
      Vuorio O.E., Kalkkinen N., Londesborough J.
      Eur. J. Biochem. 216:849-861(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
      Strain: ATCC 204508 / S288c.
    8. "cDNA cloning, sequence analysis of trehalose-6-phosphate synthase gene from Saccharomyces cerevisiae AS2.1416."
      Dong Z.Y., Duan Y.K., Chen H.M., Jin C., Zhang S.Z.
      Sheng Wu Gong Cheng Xue Bao 16:408-410(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: AS2.1416.
    9. "Research on the mechanism of osmotolerance and thermotolerance of yeast."
      Ma X., Guo Y., Zhang F., Yu H., Kuang J., Yao J., Li Z., He G.
      Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: FHS and WFB.
    10. "The sequence of 29.7 kb from the right arm of chromosome II reveals 13 complete open reading frames, of which ten correspond to new genes."
      Becam A.-M., Cullin C., Grzybowska E., Lacroute F., Nasr F., Ozier-Kalogeropoulos O., Palucha A., Slonimski P.P., Zagulski M., Herbert C.J.
      Yeast 10:S1-S11(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    11. "Complete DNA sequence of yeast chromosome II."
      Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C.
      , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
      EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    12. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    13. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    14. "Analysis of a 70 kb region on the right arm of yeast chromosome II."
      Mannhaupt G., Stucka R., Ehnle S., Vetter I., Feldmann H.
      Yeast 10:1363-1381(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 291-495.
      Strain: ATCC 204508 / S288c.
    15. "Characterization of trehalose-6-phosphate synthase and trehalose-6-phosphate phosphatase of Saccharomyces cerevisiae."
      Vandercammen A., Francois J., Hers H.-G.
      Eur. J. Biochem. 182:613-620(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
    16. "Purification of trehalose synthase from baker's yeast. Its temperature-dependent activation by fructose 6-phosphate and inhibition by phosphate."
      Londesborough J., Vuorio O.E.
      Eur. J. Biochem. 216:841-848(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    17. "Structural analysis of the subunits of the trehalose-6-phosphate synthase/phosphatase complex in Saccharomyces cerevisiae and their function during heat shock."
      Reinders A., Buerckert N., Hohmann S., Thevelein J.M., Boller T., Wiemken A., De Virgilio C.
      Mol. Microbiol. 24:687-695(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH TPS2; TPS3 AND TSL1.
    18. "Composition and functional analysis of the Saccharomyces cerevisiae trehalose synthase complex."
      Bell W., Sun W., Hohmann S., Wera S., Reinders A., De Virgilio C., Wiemken A., Thevelein J.M.
      J. Biol. Chem. 273:33311-33319(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
    19. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    20. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiTPS1_YEAST
    AccessioniPrimary (citable) accession number: Q00764
    Secondary accession number(s): D6VQC3
    , Q01801, Q05168, Q6J5J4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: July 1, 1993
    Last modified: June 24, 2015
    This is version 154 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 10900 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

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

    External Data

    Dasty 3

    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 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.