OTSA_SINFN
ID OTSA_SINFN Reviewed; 464 AA.
AC P55612;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 113.
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=NGR_a02090;
GN ORFNames=y4pC;
OS Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OG Plasmid sym pNGR234a.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=394;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 101917 / NGR234;
RX PubMed=9163424; DOI=10.1038/387394a0;
RA Freiberg C.A., Fellay R., Bairoch A., Broughton W.J., Rosenthal A.,
RA Perret X.;
RT "Molecular basis of symbiosis between Rhizobium and legumes.";
RL Nature 387:394-401(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 101917 / NGR234;
RX PubMed=19376903; DOI=10.1128/aem.00515-09;
RA Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT "Rhizobium sp. strain NGR234 possesses a remarkable number of secretion
RT systems.";
RL Appl. Environ. Microbiol. 75:4035-4045(2009).
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}.
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DR EMBL; U00090; AAB91813.1; -; Genomic_DNA.
DR RefSeq; NP_444016.1; NC_000914.2.
DR RefSeq; WP_010875236.1; NC_000914.2.
DR AlphaFoldDB; P55612; -.
DR SMR; P55612; -.
DR STRING; 394.NGR_a02090; -.
DR CAZy; GT20; Glycosyltransferase Family 20.
DR EnsemblBacteria; AAB91813; AAB91813; NGR_a02090.
DR KEGG; rhi:NGR_a02090; -.
DR PATRIC; fig|394.7.peg.220; -.
DR eggNOG; COG0380; Bacteria.
DR HOGENOM; CLU_002351_7_1_5; -.
DR OMA; YYGFSNR; -.
DR OrthoDB; 556566at2; -.
DR UniPathway; UPA00299; -.
DR Proteomes; UP000001054; Plasmid sym pNGR234a.
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; Plasmid; Reference proteome; Transferase.
FT CHAIN 1..464
FT /note="Trehalose-6-phosphate synthase"
FT /id="PRO_0000122491"
FT BINDING 10
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:P31677"
FT BINDING 23..24
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:P31677"
FT BINDING 81
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:P31677"
FT BINDING 135
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
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 273
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:P31677"
FT BINDING 306
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:P31677"
FT BINDING 371..375
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:P31677"
FT SITE 90
FT /note="Involved in alpha anomer selectivity"
FT /evidence="ECO:0000250|UniProtKB:P31677"
FT SITE 160
FT /note="Involved in alpha anomer selectivity"
FT /evidence="ECO:0000250|UniProtKB:P31677"
SQ SEQUENCE 464 AA; 51627 MW; 96DC610DD739FA73 CRC64;
MSRLVIVSNR VPVPDKGGIA PAGGLAVALK VALEEQGGGI WMGWSGKSSG EDEPAPLAQL
QQGNITYALT DLTDTDVEEY YHGFANRVLW PICHYRLDLA EYGRKEMAGY FRVNRFFAHR
LAPLVKPDDV IWVHDYPLIP LAAELRQMGL ENRIGFFLHI PWPPADVLFT MPVHEEIMRG
LSHYDVVGFQ TDHDLENFAS CLRREGIGDA LGGGRLSAYG RIFKGGVYAI GIETAAFAEF
AKKASTNSTV KKARESIERR SLIIGVDRLD YSKGLTQRIE AFERFILANP AQRGRVTYLQ
ITPKSRSEVP EYEAMQRTVA EQAGRVNGAL GAVDWVPMRY INRSVGRRVL AGLYRLGKVG
LVTPLRDGKN LVAKEYVAAQ DPDDPGVLVL SRFAGAAREL QGALLVNPYD IEGTANAMAR
SLSMPLEERQ ERWTTMMDQL LEHDVSRWCR DFLNDLTASS DRCG
