ID OTSA_MYCS2 Reviewed; 503 AA.
AC A0R4M9; I7FLH5;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 101.
DE RecName: Full=Trehalose-6-phosphate synthase {ECO:0000303|Ref.4};
DE Short=TPS {ECO:0000303|Ref.4};
DE EC=2.4.1.15 {ECO:0000269|Ref.4};
DE EC=2.4.1.347 {ECO:0000269|Ref.4};
DE AltName: Full=Alpha,alpha-trehalose-phosphate synthase [UDP-forming] {ECO:0000305};
DE AltName: Full=Osmoregulatory trehalose synthesis protein A {ECO:0000250|UniProtKB:P31677};
DE Short=OtsA {ECO:0000250|UniProtKB:P31677};
GN Name=otsA {ECO:0000303|Ref.4}; OrderedLocusNames=MSMEG_5892, MSMEI_5731;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, AND SUBSTRATE SPECIFICITY.
RA Lapp D., Patterson B.W., Elbein A.D.;
RT "Properties of a trehalose phosphate synthetase from Mycobacterium
RT smegmatis. Activation of the enzyme by polynucleotides and other
RT polyanions.";
RL J. Biol. Chem. 246:4567-4579(1971).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=27513637; DOI=10.1371/journal.ppat.1005768;
RA Koliwer-Brandl H., Syson K., van de Weerd R., Chandra G., Appelmelk B.,
RA Alber M., Ioerger T.R., Jacobs W.R. Jr., Geurtsen J., Bornemann S.,
RA Kalscheuer R.;
RT "Metabolic network for the biosynthesis of intra- and extracellular alpha-
RT glucans required for virulence of Mycobacterium tuberculosis.";
RL PLoS Pathog. 12:E1005768-E1005768(2016).
CC -!- FUNCTION: Involved in the production of glycogen and alpha-glucan via
CC the TreS-Pep2 branch involved in the biosynthesis of maltose-1-
CC phosphate (M1P), and probably in the osmoprotection via the
CC biosynthesis of trehalose (Ref.4, PubMed:27513637). Catalyzes the
CC transfer of glucose from UDP-glucose (UDP-Glc) to glucose-6-phosphate
CC (Glc-6-P) to form trehalose-6-phosphate (Ref.4). ADP-Glc, CDP-Glc, GDP-
CC Glc and TDP-Glc are also glucosyl donors, however, when the pyrimidine
CC sugar nucleotides (CDP-Glc, TDP-Glc and UDP-Glc) are used as
CC substrates, there is an absolute requirement for a high molecular
CC weight polyanion for activity (Ref.4). {ECO:0000269|PubMed:27513637,
CC ECO:0000269|Ref.4}.
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:0000269|Ref.4};
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; Evidence={ECO:0000269|Ref.4};
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; Evidence={ECO:0000269|Ref.4};
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; Evidence={ECO:0000269|Ref.4};
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:0000269|Ref.4};
CC -!- ACTIVITY REGULATION: Stimulated by the polynucleotide FII
CC (physiological activator), and by chondroitin sulfate (CS) and heparin.
CC Activation by the polyanion is inhibited by high salt concentration as
CC well as by high concentrations of mononucleoside phosphates.
CC {ECO:0000269|Ref.4}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=40 uM for UDP-Glc (in the presence of polyanion)
CC {ECO:0000269|Ref.4};
CC KM=1 mM for Glc-6-P (with UDP-Glc in the presence of polyanion)
CC {ECO:0000269|Ref.4};
CC KM=2 mM for Glc-6-P (with GDP-Glc in the presence of polyanion)
CC {ECO:0000269|Ref.4};
CC pH dependence:
CC Optimum pH is 7. {ECO:0000269|Ref.4};
CC Temperature dependence:
CC About 60% of the activity is lost in the absence of FII after 10
CC minutes at 40 degrees Celsius, but only 35% in the presence of FII.
CC {ECO:0000269|Ref.4};
CC -!- PATHWAY: Glycan biosynthesis; trehalose biosynthesis. {ECO:0000305}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P9WN11}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene do not accumulate ADP-
CC glucose, however combined inactivation of both glgM and ostA
CC accumulates ADP-glucose. {ECO:0000269|PubMed:27513637}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 20 family.
CC {ECO:0000305}.
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DR EMBL; CP000480; ABK71484.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP42165.1; -; Genomic_DNA.
DR RefSeq; WP_011730872.1; NZ_SIJM01000007.1.
DR RefSeq; YP_890117.1; NC_008596.1.
DR AlphaFoldDB; A0R4M9; -.
DR SMR; A0R4M9; -.
DR STRING; 246196.MSMEG_5892; -.
DR CAZy; GT20; Glycosyltransferase Family 20.
DR PaxDb; 246196-MSMEI_5731; -.
DR GeneID; 66737179; -.
DR KEGG; msg:MSMEI_5731; -.
DR KEGG; msm:MSMEG_5892; -.
DR PATRIC; fig|246196.19.peg.5733; -.
DR eggNOG; COG0380; Bacteria.
DR OrthoDB; 9761633at2; -.
DR UniPathway; UPA00299; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; 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 Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR InterPro; IPR001830; Glyco_trans_20.
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 1: Evidence at protein level;
KW Glycosyltransferase; Reference proteome; Transferase.
FT CHAIN 1..503
FT /note="Trehalose-6-phosphate synthase"
FT /id="PRO_0000348910"
FT REGION 481..503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..503
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 22
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:P31677"
FT BINDING 42..43
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:P31677"
FT BINDING 94
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:P31677"
FT BINDING 148
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:P31677"
FT BINDING 290
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:P31677"
FT BINDING 295
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:P31677"
FT BINDING 328
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:P31677"
FT BINDING 393..397
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:P31677"
FT SITE 103
FT /note="Involved in alpha anomer selectivity"
FT /evidence="ECO:0000250|UniProtKB:P31677"
FT SITE 173
FT /note="Involved in alpha anomer selectivity"
FT /evidence="ECO:0000250|UniProtKB:P31677"
SQ SEQUENCE 503 AA; 56280 MW; 3D4B5CE2E6DA5ACF CRC64;
MSPESGHETI SGTSDFVVVA NRLPVDLERL PDGTTRWKRS PGGLVTALEP LLRKRRGSWI
GWAGVADSDE EPIVQDGLQL HPVRLSADDV AKYYEGFSNA TLWPLYHDLI VKPEYHREWW
DRYVEVNRRF AEATARAAAE GATVWIQDYQ LQLVPKMLRM LRPDVTIGFF LHIPFPPVEL
FMQMPWRTEI VEGLLGADLV GFHLPGGAQN FLVLSRRLVG ANTSRASIGV RSRFGEVQVG
FRTVKVGAFP ISIDSAELDG KARNRAIRQR ARQIRAELGN PRKIMLGVDR LDYTKGIDVR
LRALSELLEE KRIKRDDTVL VQLATPSRER VESYIAMRED IERQVGHING EYGEVGHPIV
HYLHRPIPRD ELIAFFVAAD VMLVTPLRDG MNLVAKEYVA CRSDLGGALV LSEFTGAAAE
LRQAYLVNPH DLEGVKDKIE AAVNQNPEEG KRRMRALRRQ VLAHDVDRWA RSFLDALAAT
GETGDSGVTG ESTPAPESDS GSF
//
