Reviewed, UniProtKB/Swiss-Prot Q00764 (TPS1_YEAST)

Names and origin

Protein names

Recommended name:
    Alpha,alpha-trehalose-phosphate synthase [UDP-forming] 56 kDa subunit
    EC=2.4.1.15
Alternative name(s):
    Trehalose-6-phosphate synthase
    UDP-glucose-glucosephosphate glucosyltransferase
    Trehalose synthase complex catalytic subunit TPS1
    General glucose sensor subunit 1
    Glycogen metabolism control protein GLC6

Gene names

Name:	TPS1
Synonyms:	BYP1, CIF1, FDP1, GGS1, GLC6, TSS1
Ordered Locus Names:	YBR126C
ORF Names:	YBR0922

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	495 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	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. Ref.16
Catalytic activity	UDP-glucose + D-glucose 6-phosphate = UDP + alpha,alpha-trehalose 6-phosphate.
Enzyme regulation	Activated by fructose 6-phosphate. Inorganic phosphate inhibits the synthase activity in the complex, but activates the syntase acivity in the free monomeric form. Ref.15
Subunit structure	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. Ref.17
Subcellular location	Cytoplasm Ref.18.
Induction	Either partial repression by glucose or induction by galactose. Induced by heat shock.
Miscellaneous	Present with 10900 molecules/cell in log phase SD medium. Ref.19
Sequence similarities	Belongs to the glycosyltransferase 20 family.
Biophysicochemical properties	Kinetic parameters: KM=3.5 mM for D-glucose 6-phosphate KM=0.5 mM for UDP-glucose
Sequence caution	The sequence AAA66891.1 differs from that shown. Reason: Frameshift at position 32.

Ontologies

Keywords
Biological process	Stress response
Cellular component	Cytoplasm
Molecular function	Glycosyltransferase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	response to drug Inferred from mutant phenotype. Source: SGD trehalose biosynthetic process Ref.2 Inferred from direct assay. Source: SGD
Cellular component	alpha,alpha-trehalose-phosphate synthase complex (UDP-forming) Ref.2 Ref.17 Inferred from direct assay. Source: SGD
Molecular function	alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity Ref.2 Inferred from direct assay. Source: SGD protein binding Ref.16 Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
TPS3	P38426	2	EBI-19430,EBI-19448
TSL1	P38427	2	EBI-19430,EBI-19638

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 495	495	Alpha,alpha-trehalose-phosphate synthase [UDP-forming] 56 kDa subunit		PRO_0000122502
Amino acid modifications
	Modified residue	13	1	Phosphoserine Ref.20
Experimental info
	Mutagenesis	223	1	H → Y in GLC6-1; low glycogen accumulation. Ref.6
	Sequence conflict	75	1	K → M in CAA48296. Ref.2
	Sequence conflict	101	1	H → L in CAA48296. Ref.2
	Sequence conflict	104	1	G → W in CAA48296. Ref.2
	Sequence conflict	129 – 130	2	LA → FG in CAA43580. Ref.4
	Sequence conflict	217	1	T → S in CAA48296. Ref.2
	Sequence conflict	288	1	I → L in CAA48296. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q00764-1 [UniParc]. Last modified July 1, 1993. Version 2. Checksum: 47325A0FA3554E3D	FASTA	495	56,148
	10 20 30 40 50 60 MTTDNAKAQL TSSSGGNIIV VSNRLPVTIT KNSSTGQYEY AMSSGGLVTA LEGLKKTYTF 70 80 90 100 110 120 KWFGWPGLEI PDDEKDQVRK DLLEKFNAVP IFLSDEIADL HYNGFSNSIL WPLFHYHPGE 130 140 150 160 170 180 INFDENAWLA YNEANQTFTN EIAKTMNHND LIWVHDYHLM LVPEMLRVKI HEKQLQNVKV 190 200 210 220 230 240 GWFLHTPFPS SEIYRILPVR QEILKGVLSC DLVGFHTYDY ARHFLSSVQR VLNVNTLPNG 250 260 270 280 290 300 VEYQGRFVNV GAFPIGIDVD KFTDGLKKES VQKRIQQLKE TFKGCKIIVG VDRLDYIKGV 310 320 330 340 350 360 PQKLHAMEVF LNEHPEWRGK VVLVQVAVPS RGDVEEYQYL RSVVNELVGR INGQFGTVEF 370 380 390 400 410 420 VPIHFMHKSI PFEELISLYA VSDVCLVSST RDGMNLVSYE YIACQEEKKG SLILSEFTGA 430 440 450 460 470 480 AQSLNGAIIV NPWNTDDLSD AINEALTLPD VKKEVNWEKL YKYISKYTSA FWGENFVHEL 490 YSTSSSSTSS SATKN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 2521486] [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: 1425702] [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: 8467996] [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: 1315471] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: C836.
[5]	"Molecular cloning of a gene involved in glucose sensing in the yeast Saccharomyces cerevisiae." van Aelst L., Hohmann S., Bulaya B., de Koning W., Sierkstra L., Neves M.J., Luyten K., Alijo R., Ramos J., Coccetti P., Martegani E., de Magalhaes-Rocha N.M., Brandao R.L., van Dijck P., Vanhalewyn M., Durnez P., Jans A.W.H., Thevelein J.M. Mol. Microbiol. 8:927-943(1993) [PubMed: 8355617] [Abstract] 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: 8150278] [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: 8404905] [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: 11059292] [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: 8091856] [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: 7813418] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[12]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J. Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[13]	"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: 7900426] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 291-495. Strain: ATCC 204508 / S288c.
[14]	"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: 2546763] [Abstract] Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
[15]	"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: 8404904] [Abstract] Cited for: ENZYME REGULATION.
[16]	"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: 9194697] [Abstract] Cited for: FUNCTION, INTERACTION WITH TPS2; TPS3 AND TSL1.
[17]	"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: 9837904] [Abstract] Cited for: SUBUNIT.
[18]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[19]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[20]	"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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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.
PIR	S34979.
RefSeq	NP_009684.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-744N.
IntAct	Q00764. 40 interactions.
STRING	Q00764.
Protein family/group databases
CAZy	GT20. Glycosyltransferase Family 20.
Proteomic databases
PeptideAtlas	Q00764.
PRIDE	Q00764.
Genome annotation databases
Ensembl	YBR126C; YBR126C; YBR126C; Saccharomyces cerevisiae. [Genome view]
GeneID	852423.
KEGG	sce:YBR126C.
NMPDR	fig|4932.3.peg.386.
Organism-specific databases
CYGD	YBR126c.
SGD	S000000330. TPS1.
Phylogenomic databases
HOGENOM	HBG559076.
OMA	HEINMAA.
OrthoDB	EOG900321.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-563.
BRENDA	2.4.1.15. 250.
Gene expression databases
ArrayExpress	Q00764.
Genevestigator	Q00764.
GermOnline	YBR126C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR001830. Glyco_trans_20. IPR012766. Trehalose_OtsA. [Graphical view]
Pfam	PF00982. Glyco_transf_20. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	971291.

Entry information

Entry name

TPS1_YEAST

Accession

Primary (citable) accession number: Q00764
Secondary accession number(s): Q01801, Q05168, Q6J5J4

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	July 1, 1993
Last modified:	December 15, 2009
This is version 100 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)