ID   B2AGZ2_CUPTR            Unreviewed;       463 AA.
AC   B2AGZ2;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   04-NOV-2026, entry version 99.
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   Name=otsA {ECO:0000313|EMBL:CAP63041.1};
GN   OrderedLocusNames=RALTA_A0372 {ECO:0000313|EMBL:CAP63041.1};
OS   Cupriavidus taiwanensis (strain DSM 17343 / BCRC 17206 / CCUG 44338 / CIP
OS   107171 / LMG 19424 / R1) (Ralstonia taiwanensis (strain LMG 19424)).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC   Burkholderiales; Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=977880 {ECO:0000313|EMBL:CAP63041.1, ECO:0000313|Proteomes:UP000001692};
RN   [1] {ECO:0000313|EMBL:CAP63041.1, ECO:0000313|Proteomes:UP000001692}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17343 / BCRC 17206 / CCUG 44338 / CIP 107171 / LMG 19424 /
RC   R1 {ECO:0000313|Proteomes:UP000001692};
RX   PubMed=18490699; DOI=10.1101/gr.076448.108;
RA   Amadou C., Pascal G., Mangenot S., Glew M., Bontemps C., Capela D.,
RA   Carrere S., Cruveiller S., Dossat C., Lajus A., Marchetti M., Poinsot V.,
RA   Rouy Z., Servin B., Saad M., Schenowitz C., Barbe V., Batut J., Medigue C.,
RA   Masson-Boivin C.;
RT   "Genome sequence of the beta-rhizobium Cupriavidus taiwanensis and
RT   comparative genomics of rhizobia.";
RL   Genome Res. 18:1472-1483(2008).
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 + UDP + H(+); 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:ARBA00048039,
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; CU633749; CAP63041.1; -; Genomic_DNA.
DR   RefSeq; WP_012351706.1; NC_010528.1.
DR   AlphaFoldDB; B2AGZ2; -.
DR   GeneID; 29760538; -.
DR   KEGG; cti:RALTA_A0372; -.
DR   eggNOG; COG0380; Bacteria.
DR   HOGENOM; CLU_002351_7_1_4; -.
DR   OMA; AAIPQHE; -.
DR   BioCyc; CTAI977880:RALTA_RS01820-MONOMER; -.
DR   UniPathway; UPA00299; -.
DR   Proteomes; UP000001692; Chromosome 1.
DR   GO; GO:0003825; F:alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005992; P:trehalose biosynthetic process; IEA:UniProtKB-UniRule.
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   Reference proteome {ECO:0000313|Proteomes:UP000001692};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362045}.
SQ   SEQUENCE   463 AA;  52343 MW;  A2F1D51485F9A2C2 CRC64;
     MPRLVAVSNR VADPRNVAAG GLAVALSEAL RQTGGLWFGW SGKALQTAQG GTPGEGDLHL
     QQAGNVTLAT VDLSREDHDA YYLGYSNGVL WPVFHYRLDL ADFDSNFLNG YRRVNQLFAR
     KLAPLLQPDD IIWIHDYHLI PLASELRAIG CGQKIGFFLH VPLPPPLILA AIPQHEWLMR
     ALFAYDLLGF QSHADVEHFS RYVQAEAQAE PMGEHRYRAF HRTVRAQAFP IGIDVDEFME
     LGRGEEAQET YEMMCAQYAR RRLLLGIDRL DYSKGLPQRL KAFYRLLAEY PENRSSATLV
     QIAAPSRESV DAYADLRREM EQLSGSINGE FGELDWMPVR YIHRTTARKR LPGLCRASRV
     ALVTPLRDGM NLVAKEFIAA QDPEDPGVLV LSRFAGAAEQ LREALLVNPY DTRATAQAIQ
     QALHMPLAER HQRHQKLLER IRAQDVHWWS REYLRALSET EGA
//