ID Q2T043_BURTA Unreviewed; 472 AA.
AC Q2T043;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE RecName: Full=Trehalose-6-phosphate synthase {ECO:0000256|ARBA:ARBA00018539, ECO:0000256|RuleBase:RU362045};
DE EC=2.4.1.15 {ECO:0000256|ARBA:ARBA00012538, ECO:0000256|RuleBase:RU362045};
DE AltName: Full=Osmoregulatory trehalose synthesis protein A {ECO:0000256|RuleBase:RU362045};
DE AltName: Full=UDP-glucose-glucosephosphate glucosyltransferase {ECO:0000256|RuleBase:RU362045};
GN OrderedLocusNames=BTH_I0900 {ECO:0000313|EMBL:ABC36336.1};
OS Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CCUG 48851 /
OS CIP 106301 / E264).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=271848 {ECO:0000313|EMBL:ABC36336.1, ECO:0000313|Proteomes:UP000001930};
RN [1] {ECO:0000313|EMBL:ABC36336.1, ECO:0000313|Proteomes:UP000001930}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264
RC {ECO:0000313|Proteomes:UP000001930};
RX PubMed=16336651; DOI=10.1186/1471-2164-6-174;
RA Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C.,
RA DeShazer D.;
RT "Bacterial genome adaptation to niches: divergence of the potential
RT virulence genes in three Burkholderia species of different survival
RT strategies.";
RL BMC Genomics 6:174-174(2005).
CC -!- FUNCTION: Probably involved in the osmoprotection via the biosynthesis
CC of trehalose. Catalyzes the transfer of glucose from UDP-alpha-D-
CC glucose (UDP-Glc) to D-glucose 6-phosphate (Glc-6-P) to form trehalose-
CC 6-phosphate. Acts with retention of the anomeric configuration of the
CC UDP-sugar donor. {ECO:0000256|RuleBase:RU362045}.
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:0000256|ARBA:ARBA00001516,
CC ECO:0000256|RuleBase:RU362045};
CC -!- PATHWAY: Glycan biosynthesis; trehalose biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005199, ECO:0000256|RuleBase:RU362045}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881,
CC ECO:0000256|RuleBase:RU362045}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 20 family.
CC {ECO:0000256|ARBA:ARBA00008799, ECO:0000256|RuleBase:RU362045}.
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DR EMBL; CP000086; ABC36336.1; -; Genomic_DNA.
DR RefSeq; WP_009892427.1; NZ_CP008785.1.
DR AlphaFoldDB; Q2T043; -.
DR CAZy; GT20; Glycosyltransferase Family 20.
DR KEGG; bte:BTH_I0900; -.
DR HOGENOM; CLU_002351_7_1_4; -.
DR UniPathway; UPA00299; -.
DR Proteomes; UP000001930; Chromosome I.
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:UniProtKB-UniPathway.
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 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000256|RuleBase:RU362045};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362045}.
SQ SEQUENCE 472 AA; 52713 MW; 7DF806C1D7C52715 CRC64;
MSRLIVVSNR VAAGQDARPT AGGLAVGVLD ALKETGGVWF GWNGEIAGAP EEPAIERDGN
VTYATVGLTR RDYDQYYRGF SNATLWPVFH YRGDLARFDR QEYAGYLRVN CALAKQLRAL
VQPDDIIWVH DYHLLPFAHC LRELGVKNPI GFFLHIPFPS PEVLRTVPPH EELMKFMCAY
DVVGLQTEGD KQAFVDYIER RGLGTSSEDG ILHAHGRVVK VAAYPIGIYP DAIGKAAVEY
GSRKAVKALR DTMRERKLVI SVDRLDYSKG LVERFQAFER MLANAPGWQG RVSLVQIAPP
TRSDVQTYQR IRQTLEGEAG RINGRFAQLD WTPIQYLNRK YERNLLMALF RLSQVGYVTP
LRDGMNLVAK EYVASQDPND PGVLVLSEFA GAAAELPGAL LVNPFDLSQM AESLERALAM
PLEERQARHA ENIARLRKND LSVWRDSFLA DLRSVATAAS VTQRAGRRVA NA
//
