OTSA_SALAR
ID OTSA_SALAR Reviewed; 473 AA.
AC A9MMQ2;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 2.
DT 03-AUG-2022, entry version 62.
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; OrderedLocusNames=SARI_01013;
OS Salmonella arizonae (strain ATCC BAA-731 / CDC346-86 / RSK2980).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=41514;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-731 / CDC346-86 / RSK2980;
RG The Salmonella enterica serovar Arizonae Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA Fulton R., Chunyan W., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA Johnson M., Thiruvilangam P., Wilson R.;
RL Submitted (NOV-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=ABX20921.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000880; ABX20921.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_000089039.1; NC_010067.1.
DR AlphaFoldDB; A9MMQ2; -.
DR SMR; A9MMQ2; -.
DR STRING; 41514.SARI_01013; -.
DR CAZy; GT20; Glycosyltransferase Family 20.
DR EnsemblBacteria; ABX20921; ABX20921; SARI_01013.
DR KEGG; ses:SARI_01013; -.
DR HOGENOM; CLU_002351_7_1_6; -.
DR OrthoDB; 556566at2; -.
DR UniPathway; UPA00299; -.
DR Proteomes; UP000002084; 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 InterPro; IPR001830; Glyco_trans_20.
DR InterPro; IPR012766; Trehalose_OtsA.
DR PANTHER; PTHR10788; PTHR10788; 1.
DR Pfam; PF00982; Glyco_transf_20; 1.
DR TIGRFAMs; TIGR02400; trehalose_OtsA; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase; Reference proteome; Transferase.
FT CHAIN 1..473
FT /note="Trehalose-6-phosphate synthase"
FT /id="PRO_0000348915"
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; 53648 MW; DDC0BA37B0F625E8 CRC64;
MSRLVVVSNR IAPPDNKGGA GGLAVGVLGA LKAAGGLWFG WSGETGNEDE PLKKVTKGNI
TWASFNLSEQ DYEDYYCQFS NAVLWPAFHY RLDLVQFQRP AWEGYMRVNA LLADKLLPLI
KENDIIWVHD YHLLPFASEL RKRGVNNRIG FFLHIPFPTP EIFNALPPHD ELLEQLCDFD
LLGFQTENDR LAFLDSLSSQ TRVTTRSGKH HIAWGKDFQT EVYPIGIEPD EIALQAAGPL
PPKLVQLKAE LKNVKNIFSV ERLDYSKGLP ERFLAYEALL ENYPQHRGKI RYTQIAPTSR
GEVQAYQDIR HQLETEAGRI NGRYGQLGWT PLYYLNQHFD RKLLMKIFRY SDVGLVTPLR
DGMNLVAKEF VAAQDPANPG VLVLSQFAGA ANELTSALIV NPYDRDDVAA ALNRALTMPL
AERISRHAEM LDVIVKNDIN RWQERFIHDL KEVTPRSAER RQQNNVATFP KLA
