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   27-MAR-2024, entry version 125.
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};
GN   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 /
RC   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 /
RC   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; 284590.Q07158; -.
DR   CAZy; GT20; Glycosyltransferase Family 20.
DR   PaxDb; 284590-Q07158; -.
DR   GeneID; 2896906; -.
DR   KEGG; kla:KLLA0_B08822g; -.
DR   eggNOG; KOG1050; Eukaryota.
DR   HOGENOM; CLU_002351_7_2_1; -.
DR   InParanoid; Q07158; -.
DR   OMA; RTIWPLF; -.
DR   Proteomes; UP000000598; Chromosome B.
DR   GO; GO:0003825; F:alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity; IEA:UniProtKB-EC.
DR   GO; GO:0005992; P:trehalose biosynthetic process; IEA:InterPro.
DR   CDD; cd03788; GT20_TPS; 1.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR   InterPro; IPR001830; Glyco_trans_20.
DR   InterPro; IPR012766; Trehalose_OtsA.
DR   NCBIfam; TIGR02400; trehalose_OtsA; 1.
DR   PANTHER; PTHR10788:SF106; BCDNA.GH08860; 1.
DR   PANTHER; PTHR10788; TREHALOSE-6-PHOSPHATE SYNTHASE; 1.
DR   Pfam; PF00982; Glyco_transf_20; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 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
//