TPS1_KLULA
ID TPS1_KLULA Reviewed; 488 AA.
AC Q07158;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Alpha,alpha-trehalose-phosphate synthase [UDP-forming] 56 kDa subunit;
DE EC=2.4.1.15 {ECO:0000305|PubMed:8223613};
DE AltName: Full=Trehalose-6-phosphate synthase;
DE AltName: Full=UDP-glucose-glucosephosphate glucosyltransferase;
GN Name=TPS1 {ECO:0000303|PubMed:8223613};
GN Synonyms=GGS1 {ECO:0000303|PubMed:8223613}; OrderedLocusNames=KLLA0B08822g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=8223613; DOI=10.1111/j.1432-1033.1993.tb18296.x;
RA Luyten K., de Koning W., Tesseur I., Ruiz M.C., Ramos J., Cobbaert P.,
RA Thevelein J.M., Hohmann S.;
RT "Disruption of the Kluyveromyces lactis GGS1 gene causes inability to grow
RT on glucose and fructose and is suppressed by mutations that reduce sugar
RT uptake.";
RL Eur. J. Biochem. 217:701-713(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Synthase catalytic subunit of the trehalose synthase complex
CC that catalyzes the production of trehalose from glucose-6-phosphate and
CC UDP-alpha-D-glucose in a two step process. Can function independently
CC of the complex. {ECO:0000269|PubMed:8223613}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucose 6-phosphate + UDP-alpha-D-glucose = alpha,alpha-
CC trehalose 6-phosphate + H(+) + UDP; Xref=Rhea:RHEA:18889,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:58429,
CC ChEBI:CHEBI:58885, ChEBI:CHEBI:61548; EC=2.4.1.15;
CC Evidence={ECO:0000305|PubMed:8223613};
CC -!- PATHWAY: Carbohydrate biosynthesis. {ECO:0000305}.
CC -!- SUBUNIT: Trehalose synthase/phosphatase complex contains three or four
CC polypeptides of 56 kDa (TPS1), 102 kDa (TPS2), 115 kDa (TPS3) and 123
CC kDa (TSL1).
CC -!- SIMILARITY: Belongs to the glycosyltransferase 20 family.
CC {ECO:0000305}.
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DR EMBL; X72499; CAA51164.1; -; Genomic_DNA.
DR EMBL; CR382122; CAH02314.1; -; Genomic_DNA.
DR PIR; S38987; S38987.
DR RefSeq; XP_451921.1; XM_451921.1.
DR AlphaFoldDB; Q07158; -.
DR SMR; Q07158; -.
DR STRING; 28985.XP_451921.1; -.
DR CAZy; GT20; Glycosyltransferase Family 20.
DR EnsemblFungi; CAH02314; CAH02314; KLLA0_B08822g.
DR GeneID; 2896906; -.
DR KEGG; kla:KLLA0_B08822g; -.
DR eggNOG; KOG1050; Eukaryota.
DR HOGENOM; CLU_002351_7_2_1; -.
DR InParanoid; Q07158; -.
DR OMA; YYGFSNR; -.
DR Proteomes; UP000000598; Chromosome B.
DR GO; GO:0005946; C:alpha,alpha-trehalose-phosphate synthase complex (UDP-forming); IEA:EnsemblFungi.
DR GO; GO:0003825; F:alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0004805; F:trehalose-phosphatase activity; IEA:EnsemblFungi.
DR GO; GO:0071465; P:cellular response to desiccation; IEA:EnsemblFungi.
DR GO; GO:0005992; P:trehalose biosynthetic process; IEA:EnsemblFungi.
DR CDD; cd03788; GT20_TPS; 1.
DR InterPro; IPR001830; Glyco_trans_20.
DR InterPro; IPR012766; Trehalose_OtsA.
DR PANTHER; PTHR10788; PTHR10788; 1.
DR Pfam; PF00982; Glyco_transf_20; 1.
DR TIGRFAMs; TIGR02400; trehalose_OtsA; 1.
PE 1: Evidence at protein level;
KW Glycosyltransferase; Reference proteome; Transferase.
FT CHAIN 1..488
FT /note="Alpha,alpha-trehalose-phosphate synthase [UDP-
FT forming] 56 kDa subunit"
FT /id="PRO_0000122498"
FT BINDING 102
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:Q92410"
FT BINDING 156
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:Q92410"
FT BINDING 293
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000250|UniProtKB:Q92410"
FT BINDING 293
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q92410"
FT BINDING 298
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000250|UniProtKB:Q92410"
FT BINDING 298
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q92410"
FT BINDING 331
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:Q92410"
FT BINDING 370
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000250|UniProtKB:Q92410"
FT BINDING 370
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q92410"
FT BINDING 392..400
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q92410"
FT BINDING 396..400
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000250|UniProtKB:Q92410"
SQ SEQUENCE 488 AA; 55356 MW; D616654C166B3C17 CRC64;
MVNQDISKLS LNECPGSVIV ISNRLPVTIK KDEKTGEYEY SMSSGGLVTA LQGLKKSTTF
QWYGWPGLEV PDEDKAKVKR ELLEKFNAIP IFLSDEVADL HYNGFSNSIL WPLFHYHPGE
ITFDDTAWLA YNEANMAFAD EIEGNINDND VVWVHDYHLM LLPEMIRQRV IAKKLKNIKI
GWFLHTPFPS SEIYRILPVR QEILKGVLSC DLIGFHTYDY ARHFLSAVQR ILNVNTLPNG
VEFDGRFVNV GAFPIGIDVE TFTEGLKQDA VIKRIKELKE SFKGCKIIIG VDRLDYIKGV
PQKLHALEVF LGAHPEWIGK VVLVQVAVPS RGDVEEYQYL RSVVNELVGR INGQFGTAEF
VPIHFMHRSI PFQELISLYA VSDVCLVSST RDGMNLVSYE YISCQEEKKG TLILSEFTGA
AQSLNGALIV NPWNTDDLAE SINEALTVPE EKRAANWEKL YKYISKYTSA FWGENFVHEL
YRLGSSNN
