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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

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

GO - Biological processi

  1. cellular carbohydrate metabolic process Source: SGD
  2. cellular response to desiccation Source: SGD
  3. cellular response to heat Source: SGD
  4. cellular response to oxidative stress Source: SGD
  5. 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.
SGDiS000000330. TPS1.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. 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.

Gene expression databases

ExpressionAtlasiQ00764. differential.
GenevestigatoriQ00764.

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. 222 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. 222 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.
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.

Gene expression databases

ExpressionAtlasiQ00764. differential.
GenevestigatoriQ00764.

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(1988) [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(1991) [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(1992) [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(1991) [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(1993) [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(1992) [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(1999) [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 (APR-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(1993) [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(1993) [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(1993) [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(1988) [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(1992) [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(1996) [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(1997) [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: April 1, 2015
This is version 151 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.