TPS1_YARLI
ID TPS1_YARLI Reviewed; 469 AA.
AC O74932;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Alpha,alpha-trehalose-phosphate synthase [UDP-forming];
DE EC=2.4.1.15 {ECO:0000305|PubMed:21931609};
DE AltName: Full=Trehalose-6-phosphate synthase;
DE AltName: Full=UDP-glucose-glucosephosphate glucosyltransferase;
GN Name=TPS1 {ECO:0000303|PubMed:21931609};
GN Synonyms=YITPS1 {ECO:0000303|PubMed:21931609};
GN OrderedLocusNames=YALI0E14685g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=PO1a;
RX PubMed=21931609; DOI=10.1371/journal.pone.0023695;
RA Flores C.L., Gancedo C., Petit T.;
RT "Disruption of Yarrowia lipolytica TPS1 gene encoding trehalose-6-P
RT synthase does not affect growth in glucose but impairs growth at high
RT temperature.";
RL PLoS ONE 6:e23695-e23695(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
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 (PubMed:21931609). The
CC disaccharide trehalose serves as a storage carbohydrate that is
CC mobilized during spore germination (PubMed:21931609).
CC {ECO:0000269|PubMed:21931609}.
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:21931609};
CC -!- PATHWAY: Carbohydrate biosynthesis. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 20 family.
CC {ECO:0000305}.
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DR EMBL; AJ011032; CAA09463.1; -; mRNA.
DR EMBL; CR382131; CAG79544.1; -; Genomic_DNA.
DR RefSeq; XP_503951.1; XM_503951.1.
DR AlphaFoldDB; O74932; -.
DR SMR; O74932; -.
DR STRING; 4952.CAG79544; -.
DR CAZy; GT20; Glycosyltransferase Family 20.
DR PRIDE; O74932; -.
DR EnsemblFungi; CAG79544; CAG79544; YALI0_E14685g.
DR GeneID; 2912305; -.
DR KEGG; yli:YALI0E14685g; -.
DR VEuPathDB; FungiDB:YALI0_E14685g; -.
DR HOGENOM; CLU_002351_7_2_1; -.
DR InParanoid; O74932; -.
DR OMA; YYGFSNR; -.
DR Proteomes; UP000001300; Chromosome E.
DR GO; GO:0005946; C:alpha,alpha-trehalose-phosphate synthase complex (UDP-forming); IBA:GO_Central.
DR GO; GO:0003825; F:alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity; IBA:GO_Central.
DR GO; GO:0102986; F:trehalose synthase activity; IGI:UniProtKB.
DR GO; GO:0004805; F:trehalose-phosphatase activity; IEA:EnsemblFungi.
DR GO; GO:0071465; P:cellular response to desiccation; IEA:EnsemblFungi.
DR GO; GO:0034605; P:cellular response to heat; IBA:GO_Central.
DR GO; GO:0005992; P:trehalose biosynthetic process; IGI:UniProtKB.
DR GO; GO:0070413; P:trehalose metabolism in response to stress; IBA:GO_Central.
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..469
FT /note="Alpha,alpha-trehalose-phosphate synthase [UDP-
FT forming]"
FT /id="PRO_0000122501"
FT BINDING 87
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:Q92410"
FT BINDING 141
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:Q92410"
FT BINDING 279
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000250|UniProtKB:Q92410"
FT BINDING 279
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q92410"
FT BINDING 284
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000250|UniProtKB:Q92410"
FT BINDING 284
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q92410"
FT BINDING 317
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:Q92410"
FT BINDING 378..386
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q92410"
FT BINDING 382..386
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000250|UniProtKB:Q92410"
SQ SEQUENCE 469 AA; 53259 MW; BCA5A82B98B0F23E CRC64;
MPNVLVISNR LPVTISREED GTYKYTMSSG GLVTALSGLK QSTTFQWFGW PGLEIPEKDK
PRLINDLETM FSCVPVFMDD DLADLHYNGF SNSILWPLFH YHPGEMNFDQ VAWEAYTQAN
RLFAKKVASI VKPGDIVWVH DYHLMLLPEM LREECENNSA LDGLKIGFFL HTPFPSSEIY
RILPVRKEVL TGVLSCNLIG FHTYDYARHF LSSVSRILDL ETMPNGTYYK GRHVVVGAFP
IGIDVNKFLE GCKRPAVQER IAQLQDKFKG IKVVVGVDRL DYIKGVPQKL HAFEVFLSEH
PEWIGKVVLV QVAVPSRGLV EEYQNLRAVV NELVGRINGM FGTVEFTPIH FMHRSVDFNE
LIALYSISDV CFVSSTRDGM NLVSYEYVAC QTEKHGSLIL SEFTGAAQSL NGALIVNPWN
TEDMAEALYD SLTFSPEKKA ENHRKLFKYV SKYTSQHWGE AFVSELKRC
