ID   OTSA_ENT38              Reviewed;         474 AA.
AC   A4WBR1;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 91.
DE   RecName: Full=Trehalose-6-phosphate synthase {ECO:0000250|UniProtKB:P31677};
DE            Short=TPS {ECO:0000250|UniProtKB:P31677};
DE            EC=2.4.1.15 {ECO:0000250|UniProtKB:P31677};
DE   AltName: Full=Alpha,alpha-trehalose-phosphate synthase [UDP-forming] {ECO:0000250|UniProtKB:P31677};
DE   AltName: Full=Osmoregulatory trehalose synthesis protein A {ECO:0000250|UniProtKB:P31677};
DE            Short=OtsA {ECO:0000250|UniProtKB:P31677};
DE   AltName: Full=UDP-glucose-glucosephosphate glucosyltransferase {ECO:0000250|UniProtKB:P31677};
GN   Name=otsA {ECO:0000250|UniProtKB:P31677};
GN   OrderedLocusNames=Ent638_2472;
OS   Enterobacter sp. (strain 638).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Enterobacter.
OX   NCBI_TaxID=399742;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=638;
RX   PubMed=20485560; DOI=10.1371/journal.pgen.1000943;
RA   Taghavi S., van der Lelie D., Hoffman A., Zhang Y.B., Walla M.D.,
RA   Vangronsveld J., Newman L., Monchy S.;
RT   "Genome sequence of the plant growth promoting endophytic bacterium
RT   Enterobacter sp. 638.";
RL   PLoS Genet. 6:E1000943-E1000943(2010).
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:0000250|UniProtKB:P31677}.
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:0000250|UniProtKB:P31677};
CC   -!- PATHWAY: Glycan biosynthesis; trehalose biosynthesis.
CC       {ECO:0000250|UniProtKB:P31677}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P31677}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 20 family.
CC       {ECO:0000250|UniProtKB:P31677}.
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DR   EMBL; CP000653; ABP61141.1; -; Genomic_DNA.
DR   RefSeq; WP_015959474.1; NC_009436.1.
DR   AlphaFoldDB; A4WBR1; -.
DR   SMR; A4WBR1; -.
DR   STRING; 399742.Ent638_2472; -.
DR   CAZy; GT20; Glycosyltransferase Family 20.
DR   KEGG; ent:Ent638_2472; -.
DR   eggNOG; COG0380; Bacteria.
DR   HOGENOM; CLU_002351_7_1_6; -.
DR   OrthoDB; 9815690at2; -.
DR   UniPathway; UPA00299; -.
DR   Proteomes; UP000000230; 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; Transferase.
FT   CHAIN           1..474
FT                   /note="Trehalose-6-phosphate synthase"
FT                   /id="PRO_0000348892"
FT   BINDING         10
FT                   /ligand="D-glucose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61548"
FT                   /evidence="ECO:0000250|UniProtKB:P31677"
FT   BINDING         22..23
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:P31677"
FT   BINDING         77
FT                   /ligand="D-glucose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61548"
FT                   /evidence="ECO:0000250|UniProtKB:P31677"
FT   BINDING         131
FT                   /ligand="D-glucose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61548"
FT                   /evidence="ECO:0000250|UniProtKB:P31677"
FT   BINDING         263
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:P31677"
FT   BINDING         268
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:P31677"
FT   BINDING         301
FT                   /ligand="D-glucose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61548"
FT                   /evidence="ECO:0000250|UniProtKB:P31677"
FT   BINDING         340
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:P31677"
FT   BINDING         366..370
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:P31677"
FT   SITE            86
FT                   /note="Involved in alpha anomer selectivity"
FT                   /evidence="ECO:0000250|UniProtKB:P31677"
FT   SITE            156
FT                   /note="Involved in alpha anomer selectivity"
FT                   /evidence="ECO:0000250|UniProtKB:P31677"
SQ   SEQUENCE   474 AA;  53911 MW;  58A0FA8BED879316 CRC64;
     MGRLVVVSNR IAPPDDKKSS AGGLAVGILG ALKTAGGLWF GWSGEVGNED KPLQKVTRGN
     ITWASFNLSE QDHEEYYSQF SNAVLWPAFH YRLDLVKFQR DSWEGYTRVN ALLADKLLPL
     IEEDDILWIH DYHLLPFASE LRKRGVNNRI GFFLHIPFPT PEIFTAIPPH EELLEGLCDY
     DLLGFQTEND RQAFLESVAG KTRLTTHNGK SHQAWGKTFD TEVYPIGIEP DEIAADASGP
     LPPKLAQLKN ELKNVKNIFS VERLDYSKGL PERFQAYERL LEKYPQHHGK IRYTQIAPTS
     RGEVQAYQDI RHQLETEAGR INGRYGQLGW TPLYYLNQHF ERKVLMKVFR YAEVGLVTPL
     RDGMNLVAKE YVAAQDPKDP GVLVLSQFAG AANELTSALL VNPYDSDDVA NALDRALKMP
     LTERISRHAE MMKVIRENDI NHWQETFIRD LKRTTPRSVE SNLQKKIATF PKLA
//