ID   OTSA_CITK8              Reviewed;         473 AA.
AC   A8AFD4;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 2.
DT   24-JAN-2024, entry version 72.
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}; OrderedLocusNames=CKO_01054;
OS   Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Citrobacter.
OX   NCBI_TaxID=290338;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-895 / CDC 4225-83 / SGSC4696;
RG   The Citrobacter koseri Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Latreille P., Courtney L., Wang C., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (AUG-2007) 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: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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABV12197.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000822; ABV12197.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_024130244.1; NC_009792.1.
DR   AlphaFoldDB; A8AFD4; -.
DR   SMR; A8AFD4; -.
DR   STRING; 290338.CKO_01054; -.
DR   CAZy; GT20; Glycosyltransferase Family 20.
DR   GeneID; 45135211; -.
DR   KEGG; cko:CKO_01054; -.
DR   HOGENOM; CLU_002351_7_1_6; -.
DR   OrthoDB; 9815690at2; -.
DR   UniPathway; UPA00299; -.
DR   Proteomes; UP000008148; 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; Reference proteome; Transferase.
FT   CHAIN           1..473
FT                   /note="Trehalose-6-phosphate synthase"
FT                   /id="PRO_0000348890"
FT   BINDING         10
FT                   /ligand="D-glucose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61548"
FT                   /evidence="ECO:0000250|UniProtKB:P31677"
FT   BINDING         21..22
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:P31677"
FT   BINDING         76
FT                   /ligand="D-glucose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61548"
FT                   /evidence="ECO:0000250|UniProtKB:P31677"
FT   BINDING         130
FT                   /ligand="D-glucose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61548"
FT                   /evidence="ECO:0000250|UniProtKB:P31677"
FT   BINDING         262
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:P31677"
FT   BINDING         267
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:P31677"
FT   BINDING         300
FT                   /ligand="D-glucose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61548"
FT                   /evidence="ECO:0000250|UniProtKB:P31677"
FT   BINDING         339
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:P31677"
FT   BINDING         365..369
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:P31677"
FT   SITE            85
FT                   /note="Involved in alpha anomer selectivity"
FT                   /evidence="ECO:0000250|UniProtKB:P31677"
FT   SITE            155
FT                   /note="Involved in alpha anomer selectivity"
FT                   /evidence="ECO:0000250|UniProtKB:P31677"
SQ   SEQUENCE   473 AA;  53476 MW;  0A46A76686A24EC6 CRC64;
     MGRLVVVSNR IAPPDNKGGA GGLAVGVLGA LKAAGGLWFG WSGETGNEDK PLKKVTRGNM
     TWASFNLSEQ DYEEYYCQFS NAVLWPAFHY RLDLVQFQRP AWEGYSRVNA LLADKLLPLL
     KDDDIIWVHD YHLLPFASEL RKRGVNNRIG FFLHIPFPTP EIFNALPPHD TLLEQLCDFD
     LLGFQTENDR LAFLDSLSSQ TRVTTRGSKS HSAWGKSFRT EVYPIGIEPD EIAQQASGPL
     PPKLAQLKAE LKNVQNIFSV ERLDYSKGLP ERFQAYEALL EKYPQHHGKI RYTQIAPTSR
     GEVQAYQDIR HQLETEAGRI NGKYGQLGWT PLYYLNQHFD RKLLMKVFRY SDVGLVTPLR
     DGMNLVAKEF VAAQDPANPG VLVLSQFAGA ANELTSALIV NPYDRDDVAV ALHRALTMPL
     AERISRHAEM LETIIKNDIN HWQQRFIRDL KDVAPRSAET LHRNKVATFP KLA
//