ID F6DEF2_THETG Unreviewed; 449 AA.
AC F6DEF2;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
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=Ththe16_0478 {ECO:0000313|EMBL:AEG32907.1};
OS Thermus thermophilus (strain SG0.5JP17-16).
OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=762633 {ECO:0000313|EMBL:AEG32907.1, ECO:0000313|Proteomes:UP000009233};
RN [1] {ECO:0000313|EMBL:AEG32907.1, ECO:0000313|Proteomes:UP000009233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG0.5JP17-16 {ECO:0000313|EMBL:AEG32907.1,
RC ECO:0000313|Proteomes:UP000009233};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Teshima H., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Pagani I., Allgaier M., Hugenholtz P., Singer S.,
RA Gladden J., Woyke T.;
RT "Complete sequence of chromosome of Thermus thermophilus SG0.5JP17-16.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000009233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG0.5JP17-16 {ECO:0000313|Proteomes:UP000009233};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Teshima H., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Pagani I., Allgaier M., Hugenholtz P., Singer S.,
RA Gladden J., Woyke T.;
RT "Complete sequence of chromosome of Thermus thermophilus SG0.5JP17-16.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
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|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; CP002777; AEG32907.1; -; Genomic_DNA.
DR RefSeq; WP_008631750.1; NC_017272.1.
DR AlphaFoldDB; F6DEF2; -.
DR KEGG; tts:Ththe16_0478; -.
DR PATRIC; fig|762633.3.peg.479; -.
DR HOGENOM; CLU_002351_7_1_0; -.
DR UniPathway; UPA00299; -.
DR Proteomes; UP000009233; Chromosome.
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 449 AA; 51628 MW; 27C58A465392EBDD CRC64;
MGLIIVANRA PFRLTPEGLV PAVGGLATAL LPVLERRHGV WVAAGEWREK GQAATPRESQ
VRLEQVFLPE KEWQGYYGGF SNRVLWPLCH YFLERVELRR DFYQDYQRAN RRFAERVAQV
FREGDTVFVQ DYHLLLLPRL LRERIPAKIG FFFHIPWPSS GVFRILPWGR ALVEGVLGAD
LIGFHTPEYV ENFLRTAAYY GYQVEENRVR VGERWVRVEA HPLGIDTGRF GELAQDPHIG
LHARALKRLA GAERLILGVD RLDYTKGILE RLLAYERLLQ SYPQWRGRVA FFQIATPSRT
SVHAYRELKR RVDEVVGRIM GSFLREDWVP LRYFYQTYTQ EELAAFYRAA DVALITPLRD
GMNLVAMEYA YTTEDGVLVL SNLAGAAEYL KEALLVNPYD LDGMAQALDR ALRMPGGERW
ERLSALKARI EALDVQGWAE RFLASLEEG
//
