ID OTSA_CROS8 Reviewed; 474 AA. AC A7MEE9; DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot. DT 02-OCT-2007, sequence version 1. DT 27-MAR-2024, entry version 88. 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=ESA_01335; OS Cronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Cronobacter. OX NCBI_TaxID=290339; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-894; RX PubMed=20221447; DOI=10.1371/journal.pone.0009556; RA Kucerova E., Clifton S.W., Xia X.Q., Long F., Porwollik S., Fulton L., RA Fronick C., Minx P., Kyung K., Warren W., Fulton R., Feng D., Wollam A., RA Shah N., Bhonagiri V., Nash W.E., Hallsworth-Pepin K., Wilson R.K., RA McClelland M., Forsythe S.J.; RT "Genome sequence of Cronobacter sakazakii BAA-894 and comparative genomic RT hybridization analysis with other Cronobacter species."; RL PLoS ONE 5:E9556-E9556(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}. 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; CP000783; ABU76595.1; -; Genomic_DNA. DR RefSeq; WP_012124438.1; NC_009778.1. DR AlphaFoldDB; A7MEE9; -. DR SMR; A7MEE9; -. DR CAZy; GT20; Glycosyltransferase Family 20. DR KEGG; esa:ESA_01335; -. DR PATRIC; fig|290339.8.peg.1180; -. DR HOGENOM; CLU_002351_7_1_6; -. DR UniPathway; UPA00299; -. DR Proteomes; UP000000260; 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_0000348891" 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; 53673 MW; F209D0DD7320D9C7 CRC64; MSRLVVVSNR IAPPDDKKSS AGGLAVGILG ALKAAGGLWF GWSGEIGNED APLKKVTRDN ITWASFNLSE QDHDQYYNQF SNGVLWPAFH YRLDLVNFQR EAWEGYLRVN SLLADKLKPL IEPDDNLWIH DYHLLPFASE LRKRGVNNRI GFFLHIPFPT PEIFNALPTN TELLEQLCDY DLLGFQTEND RTAFLDCLAM QTHLSTSSDG EYTAYGKTFR TEVYPIGIEP EEIAQASAGP LPPKLAQLKA ELASVKNIFS VERLDYSKGL PERFQAFETL LEKYPEHHGK IRYTQIAPTS RGDVQAYQDI RHQLETEAGR INGKYGQLGW TPLYYLNQHF DRKLLMKVFR YSDVGLVTPL RDGMNLVAKE YVAAQDPKNP GVLVLSQFAG AANELTAALL VNPYDRDDVA AALDRALKMP LAERIARHSE MLEIVRKNDI NHWQEAFIKD LKQVTPRSPE RELQNKVATF PKLA //