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Protein

Trehalose-6-phosphate synthase

Gene

otsA

Organism
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the production of glycogen and alpha-glucan via the TreS-Pep2 branch involved in the biosynthesis of maltose-1-phosphate (M1P), and probably in the osmoprotection via the biosynthesis of trehalose (Ref. 4, PubMed:27513637). Catalyzes the transfer of glucose from UDP-glucose (UDP-Glc) to glucose-6-phosphate (Glc-6-P) to form trehalose-6-phosphate (Ref. 4). ADP-Glc, CDP-Glc, GDP-Glc and TDP-Glc are also glucosyl donors, however, when the pyrimidine sugar nucleotides (CDP-Glc, TDP-Glc and UDP-Glc) are used as substrates, there is an absolute requirement for a high molecular weight polyanion for activity (Ref. 4).2 Publications

Catalytic activityi

ADP-glucose + D-glucose 6-phosphate = ADP + alpha,alpha-trehalose 6-phosphate.1 Publication
CDP-glucose + D-glucose 6-phosphate = CDP + alpha,alpha-trehalose 6-phosphate.1 Publication
GDP-glucose + D-glucose 6-phosphate = GDP + alpha,alpha-trehalose 6-phosphate.1 Publication
TDP-glucose + D-glucose 6-phosphate = TDP + alpha,alpha-trehalose 6-phosphate.1 Publication
UDP-glucose + D-glucose 6-phosphate = UDP + alpha,alpha-trehalose 6-phosphate.1 Publication

Enzyme regulationi

Stimulated by the polynucleotide FII (physiological activator), and by chondroitin sulfate (CS) and heparin. Activation by the polyanion is inhibited by high salt concentration as well as by high concentrations of mononucleoside phosphates.1 Publication

Kineticsi

  1. KM=40 µM for UDP-Glc (in the presence of polyanion)1 Publication
  2. KM=1 mM for Glc-6-P (with UDP-Glc in the presence of polyanion)1 Publication
  3. KM=2 mM for Glc-6-P (with GDP-Glc in the presence of polyanion)1 Publication

    pH dependencei

    Optimum pH is 7.1 Publication

    Temperature dependencei

    About 60% of the activity is lost in the absence of FII after 10 minutes at 40 degrees Celsius, but only 35% in the presence of FII.1 Publication

    Pathwayi: trehalose biosynthesis

    This protein is involved in the pathway trehalose biosynthesis, which is part of Glycan biosynthesis.Curated
    View all proteins of this organism that are known to be involved in the pathway trehalose biosynthesis and in Glycan biosynthesis.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei22D-glucose 6-phosphateBy similarity1
    Binding sitei94D-glucose 6-phosphateBy similarity1
    Sitei103Involved in alpha anomer selectivityBy similarity1
    Binding sitei148D-glucose 6-phosphateBy similarity1
    Sitei173Involved in alpha anomer selectivityBy similarity1
    Binding sitei290UDP-glucoseBy similarity1
    Binding sitei295UDP-glucoseBy similarity1
    Binding sitei328D-glucose 6-phosphateBy similarity1

    GO - Molecular functioni

    GO - Biological processi

    Keywordsi

    Molecular functionGlycosyltransferase, Transferase

    Enzyme and pathway databases

    UniPathwayiUPA00299.

    Protein family/group databases

    CAZyiGT20. Glycosyltransferase Family 20.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Trehalose-6-phosphate synthase1 Publication (EC:2.4.1.-1 Publication, EC:2.4.1.151 Publication)
    Short name:
    TPS1 Publication
    Alternative name(s):
    Alpha,alpha-trehalose-phosphate synthase [UDP-forming]Curated
    Osmoregulatory trehalose synthesis protein ABy similarity
    Short name:
    OtsABy similarity
    Gene namesi
    Name:otsA1 Publication
    Ordered Locus Names:MSMEG_5892, MSMEI_5731
    OrganismiMycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
    Taxonomic identifieri246196 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacterium
    Proteomesi
    • UP000006158 Componenti: Chromosome
    • UP000000757 Componenti: Chromosome

    Pathology & Biotechi

    Disruption phenotypei

    Cells lacking this gene do not accumulate ADP-glucose, however combined inactivation of both glgM and ostA accumulates ADP-glucose.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00003489101 – 503Trehalose-6-phosphate synthaseAdd BLAST503

    Proteomic databases

    PRIDEiA0R4M9.

    Interactioni

    Subunit structurei

    Homotetramer.By similarity

    Protein-protein interaction databases

    STRINGi246196.MSMEG_5892.

    Structurei

    3D structure databases

    ProteinModelPortaliA0R4M9.
    SMRiA0R4M9.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni42 – 43UDP-glucose bindingBy similarity2
    Regioni393 – 397UDP-glucose bindingBy similarity5

    Sequence similaritiesi

    Belongs to the glycosyltransferase 20 family.Curated

    Phylogenomic databases

    eggNOGiENOG4105C1K. Bacteria.
    COG0380. LUCA.
    HOGENOMiHOG000191477.
    KOiK00697.
    OMAiIEFMPIH.
    OrthoDBiPOG091H0ASR.

    Family and domain databases

    CDDicd03788. GT1_TPS. 1 hit.
    InterProiView protein in InterPro
    IPR001830. Glyco_trans_20.
    PfamiView protein in Pfam
    PF00982. Glyco_transf_20. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    A0R4M9-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSPESGHETI SGTSDFVVVA NRLPVDLERL PDGTTRWKRS PGGLVTALEP
    60 70 80 90 100
    LLRKRRGSWI GWAGVADSDE EPIVQDGLQL HPVRLSADDV AKYYEGFSNA
    110 120 130 140 150
    TLWPLYHDLI VKPEYHREWW DRYVEVNRRF AEATARAAAE GATVWIQDYQ
    160 170 180 190 200
    LQLVPKMLRM LRPDVTIGFF LHIPFPPVEL FMQMPWRTEI VEGLLGADLV
    210 220 230 240 250
    GFHLPGGAQN FLVLSRRLVG ANTSRASIGV RSRFGEVQVG FRTVKVGAFP
    260 270 280 290 300
    ISIDSAELDG KARNRAIRQR ARQIRAELGN PRKIMLGVDR LDYTKGIDVR
    310 320 330 340 350
    LRALSELLEE KRIKRDDTVL VQLATPSRER VESYIAMRED IERQVGHING
    360 370 380 390 400
    EYGEVGHPIV HYLHRPIPRD ELIAFFVAAD VMLVTPLRDG MNLVAKEYVA
    410 420 430 440 450
    CRSDLGGALV LSEFTGAAAE LRQAYLVNPH DLEGVKDKIE AAVNQNPEEG
    460 470 480 490 500
    KRRMRALRRQ VLAHDVDRWA RSFLDALAAT GETGDSGVTG ESTPAPESDS

    GSF
    Length:503
    Mass (Da):56,280
    Last modified:January 9, 2007 - v1
    Checksum:i3D4B5CE2E6DA5ACF
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    CP000480 Genomic DNA. Translation: ABK71484.1.
    CP001663 Genomic DNA. Translation: AFP42165.1.
    RefSeqiWP_011730872.1. NZ_CP009494.1.
    YP_890117.1. NC_008596.1.

    Genome annotation databases

    EnsemblBacteriaiABK71484; ABK71484; MSMEG_5892.
    AFP42165; AFP42165; MSMEI_5731.
    GeneIDi4532640.
    KEGGimsb:LJ00_29135.
    msg:MSMEI_5731.
    msm:MSMEG_5892.
    PATRICifig|246196.19.peg.5733.

    Similar proteinsi

    Entry informationi

    Entry nameiOTSA_MYCS2
    AccessioniPrimary (citable) accession number: A0R4M9
    Secondary accession number(s): I7FLH5
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 2, 2008
    Last sequence update: January 9, 2007
    Last modified: August 30, 2017
    This is version 68 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families