OTSA_MYCUA
ID OTSA_MYCUA Reviewed; 500 AA.
AC A0PUT6;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Trehalose-6-phosphate synthase {ECO:0000250|UniProtKB:P9WN11};
DE Short=TPS {ECO:0000250|UniProtKB:P9WN11};
DE EC=2.4.1.15 {ECO:0000250|UniProtKB:P9WN11};
DE EC=2.4.1.347 {ECO:0000250|UniProtKB:P9WN11};
DE AltName: Full=Alpha,alpha-trehalose-phosphate synthase [UDP-forming] {ECO:0000250|UniProtKB:P9WN11};
DE AltName: Full=Osmoregulatory trehalose synthesis protein A {ECO:0000250|UniProtKB:P31677};
DE Short=OtsA {ECO:0000250|UniProtKB:P31677};
GN Name=otsA {ECO:0000250|UniProtKB:P9WN11}; OrderedLocusNames=MUL_4052;
OS Mycobacterium ulcerans (strain Agy99).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=362242;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Agy99;
RX PubMed=17210928; DOI=10.1101/gr.5942807;
RA Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T.,
RA Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., Ryan J.,
RA Johnson P.D.R., Davies J.K., Jenkin G.A., Small P.L.C., Jones L.M.,
RA Tekaia F., Laval F., Daffe M., Parkhill J., Cole S.T.;
RT "Reductive evolution and niche adaptation inferred from the genome of
RT Mycobacterium ulcerans, the causative agent of Buruli ulcer.";
RL Genome Res. 17:192-200(2007).
CC -!- FUNCTION: Probably involved in the osmoprotection via the biosynthesis
CC of trehalose and in the production of glycogen and alpha-glucan via the
CC TreS-Pep2 branch involved in the biosynthesis of maltose-1-phosphate
CC (M1P). Catalyzes the transfer of glucose from UDP-glucose (UDP-Glc) to
CC D-glucose 6-phosphate (Glc-6-P) to form trehalose-6-phosphate. Probably
CC also able to use ADP-Glc, CDP-Glc, GDP-Glc and TDP-Glc as glucosyl
CC donors. {ECO:0000250|UniProtKB:P9WN11}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ADP-alpha-D-glucose + D-glucose 6-phosphate = ADP +
CC alpha,alpha-trehalose 6-phosphate + H(+); Xref=Rhea:RHEA:53880,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57498, ChEBI:CHEBI:58429,
CC ChEBI:CHEBI:61548, ChEBI:CHEBI:456216; EC=2.4.1.347;
CC Evidence={ECO:0000250|UniProtKB:P9WN11};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CDP-alpha-D-glucose + D-glucose 6-phosphate = alpha,alpha-
CC trehalose 6-phosphate + CDP + H(+); Xref=Rhea:RHEA:53884,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58069, ChEBI:CHEBI:58429,
CC ChEBI:CHEBI:61548, ChEBI:CHEBI:137927;
CC Evidence={ECO:0000250|UniProtKB:P9WN11};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucose 6-phosphate + GDP-alpha-D-glucose = alpha,alpha-
CC trehalose 6-phosphate + GDP + H(+); Xref=Rhea:RHEA:14605,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58189, ChEBI:CHEBI:58429,
CC ChEBI:CHEBI:61548, ChEBI:CHEBI:62230;
CC Evidence={ECO:0000250|UniProtKB:P9WN11};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucose 6-phosphate + TDP-alpha-D-glucose = alpha,alpha-
CC trehalose 6-phosphate + H(+) + TDP; Xref=Rhea:RHEA:53888,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58429, ChEBI:CHEBI:61417,
CC ChEBI:CHEBI:61548, ChEBI:CHEBI:137931;
CC Evidence={ECO:0000250|UniProtKB:P9WN11};
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:P9WN11};
CC -!- PATHWAY: Glycan biosynthesis; trehalose biosynthesis.
CC {ECO:0000250|UniProtKB:P9WN11}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P9WN11}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 20 family.
CC {ECO:0000250|UniProtKB:P9WN11}.
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; CP000325; ABL06105.1; -; Genomic_DNA.
DR RefSeq; WP_011741709.1; NC_008611.1.
DR AlphaFoldDB; A0PUT6; -.
DR SMR; A0PUT6; -.
DR STRING; 362242.MUL_4052; -.
DR CAZy; GT20; Glycosyltransferase Family 20.
DR PRIDE; A0PUT6; -.
DR EnsemblBacteria; ABL06105; ABL06105; MUL_4052.
DR KEGG; mul:MUL_4052; -.
DR eggNOG; COG0380; Bacteria.
DR HOGENOM; CLU_002351_7_1_11; -.
DR OMA; YYGFSNR; -.
DR UniPathway; UPA00299; -.
DR Proteomes; UP000000765; Chromosome.
DR GO; GO:0047260; F:alpha,alpha-trehalose-phosphate synthase (GDP-forming) activity; IEA:RHEA.
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 PANTHER; PTHR10788; PTHR10788; 1.
DR Pfam; PF00982; Glyco_transf_20; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase; Transferase.
FT CHAIN 1..500
FT /note="Trehalose-6-phosphate synthase"
FT /id="PRO_0000348924"
FT BINDING 28
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:P31677"
FT BINDING 48..49
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:P31677"
FT BINDING 104
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:P31677"
FT BINDING 158
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:P31677"
FT BINDING 300
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:P31677"
FT BINDING 305
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:P31677"
FT BINDING 338
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:P31677"
FT BINDING 403..407
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:P31677"
FT SITE 113
FT /note="Involved in alpha anomer selectivity"
FT /evidence="ECO:0000250|UniProtKB:P31677"
FT SITE 183
FT /note="Involved in alpha anomer selectivity"
FT /evidence="ECO:0000250|UniProtKB:P31677"
SQ SEQUENCE 500 AA; 56100 MW; 8F9B71DBA741915C CRC64;
MGPGGRQSAE PASTEVFGDS DFVVVANRLP VDQERLPDGT IAWKRSPGGL VTALEPLLRR
RRGAWVGWAG VVENDVDVQD EPIVQDELQL QPVRLSADDV AQYYEGFSNA TLWPLYHDVI
VRPIYHREWW DRYVDVNRRF AEATARAAAR GGTVWVQDYQ LQLVPKMLRA MRPDLTIGFF
LHIPFPPVEL FMQLPWRTEI IQGLLGADLV GFHLPGGAQN FLILSRRLVG ADTSRGTVGV
RSRFGEVILG SRTIRVGAFP ISIDSGALDQ TARDRNIRRR SREIRAELGN PRKILLGVDR
LDYTKGIDVR LKAFSELLAE GRVKRDDTVL VQLATPSRER VESYQTLRND IERQVGHING
EYAEVGHPVV HYLHRPVPRN ELIAFFVASD VMLVTPLRDG MNLVAKEYVA CRSDLGGALV
LSEFTGAAAE LRHAYLVNPH DLEGVNDGIE EALNQTEEAG RRRMRSMRRQ VLAHDVDRWA
RSFLDALADS RPNDSADAAD
