ID B9BQK5_9BURK Unreviewed; 473 AA.
AC B9BQK5;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 41.
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_2 {ECO:0000313|EMBL:EEE06900.1};
GN ORFNames=BURMUCGD2_1164 {ECO:0000313|EMBL:EEE06900.1};
OS Burkholderia multivorans CGD2.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=513052 {ECO:0000313|EMBL:EEE06900.1, ECO:0000313|Proteomes:UP000004535};
RN [1] {ECO:0000313|EMBL:EEE06900.1, ECO:0000313|Proteomes:UP000004535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGD2 {ECO:0000313|EMBL:EEE06900.1,
RC ECO:0000313|Proteomes:UP000004535};
RX PubMed=23105085; DOI=10.1128/JB.01306-12;
RA Varga J.J., Losada L., Zelazny A.M., Brinkac L., Harkins D., Radune D.,
RA Hostetler J., Sampaio E.P., Ronning C.M., Nierman W.C., Greenberg D.E.,
RA Holland S.M., Goldberg J.B.;
RT "Draft Genome Sequence Determination for Cystic Fibrosis and Chronic
RT Granulomatous Disease Burkholderia multivorans Isolates.";
RL J. Bacteriol. 194:6356-6357(2012).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EEE06900.1}.
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DR EMBL; ACFC01000005; EEE06900.1; -; Genomic_DNA.
DR RefSeq; WP_006405715.1; NZ_ACFC01000005.1.
DR AlphaFoldDB; B9BQK5; -.
DR UniPathway; UPA00299; -.
DR Proteomes; UP000004535; Unassembled WGS sequence.
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 473 AA; 52697 MW; 2C57374E60C2D067 CRC64;
MSRLIVVSNR VAIGEDTRPS AGGLAVGVMD ALRETGGVWF GWNGEIVGTP DAAPAIRRDG
NVTYATVGLT RRDYDQYYRG FSNATLWPVF HYRGDLARFD RQEYAGYLRV NAMLAKQLAA
LLRPDDLIWV HDYHLLPFAH ALRELGVKNP IGFFLHIPFP SPDVLRLVPP HDELVKFMCA
YDVTGFQTDA DKQAFTDYIE RRGIGTASED GMLHAHGRVV KVAAYPIGVY PDAIAQAAVQ
YGARKPVKML RDALGGRKLV MSVDRLDYSK GLVERFQAFE RMLANAPGWQ GRVSLVQIAP
PTRSDVQTYQ RIRETLEGEA GRINGRFSQL DWTPIQYLNR KYERNLLMAF FRMSQVGYVT
PLRDGMNLVA KEYVASQDPA DPGVLVLSEF AGAAAELTGA LLVNPYDLSQ MADALERALS
MPLAERQARH EENLARLRAN DLSVWRDTFV ADLRSVAAAA SVTQRAGRRI AHA
//
