ID OTSA_SALCH Reviewed; 473 AA. AC Q57N70; DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot. DT 10-MAY-2005, sequence version 1. DT 27-MAR-2024, entry version 84. 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=SCH_1935; OS Salmonella choleraesuis (strain SC-B67). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=321314; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SC-B67; RX PubMed=15781495; DOI=10.1093/nar/gki297; RA Chiu C.-H., Tang P., Chu C., Hu S., Bao Q., Yu J., Chou Y.-Y., Wang H.-S., RA Lee Y.-S.; RT "The genome sequence of Salmonella enterica serovar Choleraesuis, a highly RT invasive and resistant zoonotic pathogen."; RL Nucleic Acids Res. 33:1690-1698(2005). 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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE017220; AAX65841.1; -; Genomic_DNA. DR RefSeq; WP_000089037.1; NC_006905.1. DR AlphaFoldDB; Q57N70; -. DR SMR; Q57N70; -. DR CAZy; GT20; Glycosyltransferase Family 20. DR KEGG; sec:SCH_1935; -. DR HOGENOM; CLU_002351_7_1_6; -. DR UniPathway; UPA00299; -. DR Proteomes; UP000000538; 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..473 FT /note="Trehalose-6-phosphate synthase" FT /id="PRO_0000348916" FT REGION 454..473 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 457..473 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" 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; 53607 MW; 218FAF0F31658442 CRC64; MSRLVVVSNR IAPPDNKGGA GGLAVGVLGA LKAAGGLWFG WSGETGNEDE PLKKVTKGNI TWASFNLSEQ DYEDYYCQFS NAVLWPAFHY RLDLVQFQRP AWEGYMRVNA LLADKLLPLI KENDIIWVHD YHLLPFASEL RKRGVNNRIG FFLHIPFPTP EIFNALPPHD ELLEQLCDFD LLGFQTENDR LAFLDSLLSQ TRVTTRSGKQ HIAWGKDFQT EVYPIGIEPD EIALQAAGPL PPKLAQLKAE LKNVKNIFSV ERLDYSKGLP ERFLAYEALL ENYPQHRGKI RYTQIAPTSR GEVQAYQDIR HQLETEAGRI NGKYGQLGWT PLYYLNQHFD RKLLMKIFRY SDVGLVTPLR DGMNLVAKEF VAAQDPANPG VLVLSQFAGA ANELTSALIV NPYDRDDVAA ALNRALTMPL AERISRHAEM LDVIVKNDIN RWQERFIHDL KEVTPRSPER QQQNNVATFP KLA //