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Q07158 (TPS1_KLULA) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
Gene names
Name:TPS1
Synonyms:GGS1
Ordered Locus Names:KLLA0B08822g
OrganismKluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica) [Complete proteome]
Taxonomic identifier284590 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeKluyveromyces

Protein attributes

Sequence length488 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Appears to play a role in controlling and restricting the influx of sugar into glycolysis, probably at the level of hexokinase. Necessary for trehalose-6-phosphate synthase and phosphatase activities.

Catalytic activity

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

Subunit structure

Trehalose synthase/phosphatase complex contains three or four polypeptides of 56 kDa (TPS1), 102 kDa (TPS2), 115 kDa (TPS3) and 123 kDa (TSL1).

Sequence similarities

Belongs to the glycosyltransferase 20 family.

Ontologies

Keywords
   Molecular functionGlycosyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processtrehalose biosynthetic process

Inferred from electronic annotation. Source: InterPro

   Molecular_functionalpha,alpha-trehalose-phosphate synthase (UDP-forming) activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 488488Alpha,alpha-trehalose-phosphate synthase [UDP-forming] 56 kDa subunit
PRO_0000122498

Sequences

Sequence LengthMass (Da)Tools
Q07158 [UniParc].

Last modified October 1, 1994. Version 1.
Checksum: D616654C166B3C17

FASTA48855,356
        10         20         30         40         50         60 
MVNQDISKLS LNECPGSVIV ISNRLPVTIK KDEKTGEYEY SMSSGGLVTA LQGLKKSTTF 

        70         80         90        100        110        120 
QWYGWPGLEV PDEDKAKVKR ELLEKFNAIP IFLSDEVADL HYNGFSNSIL WPLFHYHPGE 

       130        140        150        160        170        180 
ITFDDTAWLA YNEANMAFAD EIEGNINDND VVWVHDYHLM LLPEMIRQRV IAKKLKNIKI 

       190        200        210        220        230        240 
GWFLHTPFPS SEIYRILPVR QEILKGVLSC DLIGFHTYDY ARHFLSAVQR ILNVNTLPNG 

       250        260        270        280        290        300 
VEFDGRFVNV GAFPIGIDVE TFTEGLKQDA VIKRIKELKE SFKGCKIIIG VDRLDYIKGV 

       310        320        330        340        350        360 
PQKLHALEVF LGAHPEWIGK VVLVQVAVPS RGDVEEYQYL RSVVNELVGR INGQFGTAEF 

       370        380        390        400        410        420 
VPIHFMHRSI PFQELISLYA VSDVCLVSST RDGMNLVSYE YISCQEEKKG TLILSEFTGA 

       430        440        450        460        470        480 
AQSLNGALIV NPWNTDDLAE SINEALTVPE EKRAANWEKL YKYISKYTSA FWGENFVHEL 


YRLGSSNN 

« Hide

References

« Hide 'large scale' references
[1]"Disruption of the Kluyveromyces lactis GGS1 gene causes inability to grow on glucose and fructose and is suppressed by mutations that reduce sugar uptake."
Luyten K., de Koning W., Tesseur I., Ruiz M.C., Ramos J., Cobbaert P., Thevelein J.M., Hohmann S.
Eur. J. Biochem. 217:701-713(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37.
[2]"Genome evolution in yeasts."
Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S. expand/collapse author list , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L.
Nature 430:35-44(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X72499 Genomic DNA. Translation: CAA51164.1.
CR382122 Genomic DNA. Translation: CAH02314.1.
PIRS38987.
RefSeqXP_451921.1. XM_451921.1.

3D structure databases

ProteinModelPortalQ07158.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING28985.Q07158.

Protein family/group databases

CAZyGT20. Glycosyltransferase Family 20.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2896906.
KEGGkla:KLLA0B08822g.

Phylogenomic databases

eggNOGCOG0380.
HOGENOMHOG000191477.
KOK00697.
OMAIEFMPIH.
OrthoDBEOG76QFS6.

Family and domain databases

InterProIPR001830. Glyco_trans_20.
IPR012766. Trehalose_OtsA.
[Graphical view]
PfamPF00982. Glyco_transf_20. 1 hit.
[Graphical view]
TIGRFAMsTIGR02400. trehalose_OtsA. 1 hit.
ProtoNetSearch...

Entry information

Entry nameTPS1_KLULA
AccessionPrimary (citable) accession number: Q07158
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: November 13, 2013
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families