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Protein

Trehalose-phosphatase

Gene

TPS2

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

Phosphatase 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.1 Publication

Catalytic activityi

Trehalose 6-phosphate + H2O = trehalose + phosphate.

Cofactori

Enzyme regulationi

Inhibited by EDTA.

Kineticsi

  1. KM=0.2 mM for trehalose 6-phosphate (at pH 6.0)1 Publication
  2. KM=0.5 mM for trehalose 6-phosphate (at pH 7.5)1 Publication
  1. Vmax=20 nmol/min/mg enzyme (at pH 6.0)1 Publication
  2. Vmax=10 nmol/min/mg enzyme (at pH 7.5)1 Publication

pH dependencei

Optimum pH is 6.0.1 Publication

GO - Molecular functioni

  • trehalose-phosphatase activity Source: SGD

GO - Biological processi

  • cellular response to heat Source: SGD
  • trehalose biosynthetic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Stress response

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-595.
YEAST:YDR074W-MONOMER.
BRENDAi2.4.1.15. 984.

Protein family/group databases

CAZyiGT20. Glycosyltransferase Family 20.

Names & Taxonomyi

Protein namesi
Recommended name:
Trehalose-phosphatase (EC:3.1.3.12)
Alternative name(s):
Trehalose synthase complex catalytic subunit TPS2
Trehalose-6-phosphate phosphatase
Short name:
TPP
Gene namesi
Name:TPS2
Synonyms:PFK3
Ordered Locus Names:YDR074W
ORF Names:YD8554.07
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR074W.
SGDiS000002481. TPS2.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 896896Trehalose-phosphatasePRO_0000122509Add
BLAST

Proteomic databases

MaxQBiP31688.

PTM databases

iPTMnetiP31688.

Expressioni

Inductioni

By heat shock. Repressed by glucose.

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
TPS1Q007648EBI-19440,EBI-19430
TPS3P384265EBI-19440,EBI-19448
TSL1P384273EBI-19440,EBI-19638

Protein-protein interaction databases

BioGridi32129. 286 interactions.
DIPiDIP-823N.
IntActiP31688. 9 interactions.
MINTiMINT-396338.

Structurei

3D structure databases

ProteinModelPortaliP31688.
SMRiP31688. Positions 101-541, 573-789.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 554554GlycosyltransferaseAdd
BLAST

Sequence similaritiesi

In the N-terminal section; belongs to the glycosyltransferase 20 family.Curated
In the C-terminal section; belongs to the trehalose phosphatase family.Curated

Phylogenomic databases

GeneTreeiENSGT00550000075394.
HOGENOMiHOG000191477.
InParanoidiP31688.
KOiK16055.
OMAiMRYSEEE.
OrthoDBiEOG76QFS6.

Family and domain databases

Gene3Di3.40.50.1000. 2 hits.
InterProiIPR001830. Glyco_trans_20.
IPR023214. HAD-like_dom.
IPR006379. HAD-SF_hydro_IIB.
IPR003337. Trehalose_PPase.
[Graphical view]
PfamiPF00982. Glyco_transf_20. 1 hit.
PF02358. Trehalose_PPase. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR01484. HAD-SF-IIB. 1 hit.
TIGR00685. T6PP. 1 hit.

Sequencei

Sequence statusi: Complete.

P31688-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTTAQDNSP KKRQRIINCV TQLPYKIQLG ESNDDWKISA TTGNSALFSS
60 70 80 90 100
LEYLQFDSTE YEQHVVGWTG EITRTERNLF TREAKEKPQD LDDDPLYLTK
110 120 130 140 150
EQINGLTTTL QDHMKSDKEA KTDTTQTAPV TNNVHPVWLL RKNQSRWRNY
160 170 180 190 200
AEKVIWPTFH YILNPSNEGE QEKNWWYDYV KFNEAYAQKI GEVYRKGDII
210 220 230 240 250
WIHDYYLLLL PQLLRMKFND ESIIIGYFHH APWPSNEYFR CLPRRKQILD
260 270 280 290 300
GLVGANRICF QNESFSRHFV SSCKRLLDAT AKKSKNSSNS DQYQVSVYGG
310 320 330 340 350
DVLVDSLPIG VNTTQILKDA FTKDIDSKVL SIKQAYQNKK IIIGRDRLDS
360 370 380 390 400
VRGVVQKLRA FETFLAMYPE WRDQVVLIQV SSPTANRNSP QTIRLEQQVN
410 420 430 440 450
ELVNSINSEY GNLNFSPVQH YYMRIPKDVY LSLLRVADLC LITSVRDGMN
460 470 480 490 500
TTALEYVTVK SHMSNFLCYG NPLILSEFSG SSNVLKDAIV VNPWDSVAVA
510 520 530 540 550
KSINMALKLD KEEKSNLESK LWKEVPTIQD WTNKFLSSLK EQASSNDDME
560 570 580 590 600
RKMTPALNRP VLLENYKQAK RRLFLFDYDG TLTPIVKDPA AAIPSARLYT
610 620 630 640 650
ILQKLCADPH NQIWIISGRD QKFLNKWLGG KLPQLGLSAE HGCFMKDVSC
660 670 680 690 700
QDWVNLTEKV DMSWQVRVNE VMEEFTTRTP GSFIERKKVA LTWHYRRTVP
710 720 730 740 750
ELGEFHAKEL KEKLLSFTDD FDLEVMDGKA NIEVRPRFVN KGEIVKRLVW
760 770 780 790 800
HQHGKPQDML KGISEKLPKD EMPDFVLCLG DDFTDEDMFR QLNTIETCWK
810 820 830 840 850
EKYPDQKNQW GNYGFYPVTV GSASKKTVAK AHLTDPQQVL ETLGLLVGDV
860 870 880 890
SLFQSAGTVD LDSRGHVKNS ESSLKSKLAS KAYVMKRSAS YTGAKV
Length:896
Mass (Da):102,976
Last modified:October 1, 1996 - v3
Checksum:iE349672CCCDA9349
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti48 – 481F → Y in CAA50025 (PubMed:8444170).Curated
Sequence conflicti289 – 2891N → D in CAA50025 (PubMed:8444170).Curated
Sequence conflicti542 – 5421Q → K in CAA50025 (PubMed:8444170).Curated
Sequence conflicti546 – 5461N → D in CAA50025 (PubMed:8444170).Curated
Sequence conflicti549 – 5491M → V in CAA50025 (PubMed:8444170).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X70694 Genomic DNA. Translation: CAA50025.1.
Z46796 Genomic DNA. Translation: CAA86796.1.
Z74370 Genomic DNA. Translation: CAA98893.1.
X58858 Genomic DNA. Translation: CAA41661.1.
BK006938 Genomic DNA. Translation: DAA11920.1.
PIRiS48761.
RefSeqiNP_010359.1. NM_001180382.1.

Genome annotation databases

EnsemblFungiiYDR074W; YDR074W; YDR074W.
GeneIDi851646.
KEGGisce:YDR074W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X70694 Genomic DNA. Translation: CAA50025.1.
Z46796 Genomic DNA. Translation: CAA86796.1.
Z74370 Genomic DNA. Translation: CAA98893.1.
X58858 Genomic DNA. Translation: CAA41661.1.
BK006938 Genomic DNA. Translation: DAA11920.1.
PIRiS48761.
RefSeqiNP_010359.1. NM_001180382.1.

3D structure databases

ProteinModelPortaliP31688.
SMRiP31688. Positions 101-541, 573-789.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32129. 286 interactions.
DIPiDIP-823N.
IntActiP31688. 9 interactions.
MINTiMINT-396338.

Protein family/group databases

CAZyiGT20. Glycosyltransferase Family 20.

PTM databases

iPTMnetiP31688.

Proteomic databases

MaxQBiP31688.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR074W; YDR074W; YDR074W.
GeneIDi851646.
KEGGisce:YDR074W.

Organism-specific databases

EuPathDBiFungiDB:YDR074W.
SGDiS000002481. TPS2.

Phylogenomic databases

GeneTreeiENSGT00550000075394.
HOGENOMiHOG000191477.
InParanoidiP31688.
KOiK16055.
OMAiMRYSEEE.
OrthoDBiEOG76QFS6.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-595.
YEAST:YDR074W-MONOMER.
BRENDAi2.4.1.15. 984.

Miscellaneous databases

PROiP31688.

Family and domain databases

Gene3Di3.40.50.1000. 2 hits.
InterProiIPR001830. Glyco_trans_20.
IPR023214. HAD-like_dom.
IPR006379. HAD-SF_hydro_IIB.
IPR003337. Trehalose_PPase.
[Graphical view]
PfamiPF00982. Glyco_transf_20. 1 hit.
PF02358. Trehalose_PPase. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR01484. HAD-SF-IIB. 1 hit.
TIGR00685. T6PP. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Disruption of TPS2, the gene encoding the 100-kDa subunit of the trehalose-6-phosphate synthase/phosphatase complex in Saccharomyces cerevisiae, causes accumulation of trehalose-6-phosphate and loss of trehalose-6-phosphate phosphatase activity."
    de Virgilio C., Buerckert N., Bell W., Jenoe P., Boller T., Wiemken A.
    Eur. J. Biochem. 212:315-323(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
    Strain: C13-ABYS86.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "Protein phosphatase 2A in Saccharomyces cerevisiae: effects on cell growth and bud morphogenesis."
    Ronne H., Carlberg M., Hu G.-Z., Nehlin J.O.
    Mol. Cell. Biol. 11:4876-4884(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 608-896.
    Strain: ATCC 208353 / W303-1A.
  5. "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.
  6. "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 TPS1; TPS3 AND TSL1.
  7. "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.
  8. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  9. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  10. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  11. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiTPS2_YEAST
AccessioniPrimary (citable) accession number: P31688
Secondary accession number(s): D6VS60
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: October 1, 1996
Last modified: July 6, 2016
This is version 161 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 22700 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 IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

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 one 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.