ID OTSA_ECOL6 Reviewed; 474 AA. AC Q8FGN6; DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot. DT 02-SEP-2008, sequence version 2. DT 24-JAN-2024, entry version 89. 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=c2310; OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=199310; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CFT073 / ATCC 700928 / UPEC; RX PubMed=12471157; DOI=10.1073/pnas.252529799; RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., RA Donnenberg M.S., Blattner F.R.; RT "Extensive mosaic structure revealed by the complete genome sequence of RT uropathogenic Escherichia coli."; RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002). 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=AAN80769.1; Type=Erroneous initiation; Evidence={ECO:0000305}; 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; AE014075; AAN80769.1; ALT_INIT; Genomic_DNA. DR RefSeq; WP_001296148.1; NZ_CP051263.1. DR AlphaFoldDB; Q8FGN6; -. DR SMR; Q8FGN6; -. DR STRING; 199310.c2310; -. DR CAZy; GT20; Glycosyltransferase Family 20. DR KEGG; ecc:c2310; -. DR eggNOG; COG0380; Bacteria. DR HOGENOM; CLU_002351_7_1_6; -. DR UniPathway; UPA00299; -. DR Proteomes; UP000001410; 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..474 FT /note="Trehalose-6-phosphate synthase" FT /id="PRO_0000348899" 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; 53528 MW; C81B480CF458A7FE CRC64; MSRLVVVSNR IAPPDEHAAS AGGLAVGILG ALKAAGGLWF GWSGETGNED QPLKKVKKGN ITWASFNLSE QDLDEYYNKF SNAVLWPAFH YRLDLVQFQR PAWDGYLRVN ALLADKLLPL LQDDDIIWIH DYHLLPFAHE LRKRGVNNRI GFFLHIPFPT PEIFNALPTY DTLLEQLCDY DLLGFQTEND RLAFLDCLSN LTRVTTRSAK SHTACGKAFR TEVYPIGIEP KEIAKQAAGP LPPKLAQLKA ELKNVQNIFS VERLDYSKGL PERFLAYEAL LEKYPQHHGK IRYTQIAPTS RGDVQAYQDI RHQLENEAGR INGKYGQLGW TPLYYLNQHF DRKLLMKIFR YSDVGLVTPL RDGMNLVAKE YVAAQDPANP GVLVLSQFAG AANELTSALI VNPYDRDEVA AALDRALTMS LAERISRHAE MLDVIVKNDI NHWQECFISD LKQIVPRSAE SQQRDKVATF PKLA //