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Protein

Trehalose synthase/amylase TreS

Gene

treS

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

Functioni

Catalyzes the reversible interconversion of maltose and trehalose by transglucosylation (PubMed:15511231, PubMed:18505459, PubMed:20118231, PubMed:21840994). Maltose is the preferred substrate (PubMed:15511231, PubMed:18505459). To a lesser extent, also displays amylase activity, catalyzing the endohydrolysis of (1->4)-alpha-D-glucosidic linkages in glycogen and maltooligosaccharides such as maltoheptaose, to produce maltose which then can be converted to trehalose (PubMed:18505459). TreS plays a key role in the utilization of trehalose for the production of glycogen and alpha-glucan via the TreS-Pep2 branch involved in the biosynthesis of maltose-1-phosphate (M1P) (PubMed:20118231, PubMed:27513637). Might also function as a sensor and/or regulator of trehalose levels within the cell. Thus, when trehalose levels in the cell become dangerously low, TreS can expedite the conversion of glycogen to maltose via its amylase activity and then convert the maltose to trehalose; but this enzyme also can expedite or promote the conversion of trehalose to glycogen when cytoplasmic trehalose levels become too high. Is also able to catalyze the hydrolytic cleavage of alpha-aryl glucosides, as well as alpha-glucosyl fluoride in vitro.5 Publications

Miscellaneous

Maltose-1-phosphate (M1P), the building block required for alpha-glucan production, is generated by two alternative routes: the TreS-Pep2 branch and the GlgC-GlgM branch, however it seems that the GlgC-GlgM branch provides most of M1P for the GlgE pathway in M.smegmatis.1 Publication

Catalytic activityi

Maltose = alpha,alpha-trehalose.3 Publications
Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.1 Publication

Activity regulationi

The amylase activity is stimulated by addition of Ca2+, but this cation and other divalent cations inhibit the trehalose synthase activity. In addition, trehalose synthase activity, but not amylase activity, is strongly inhibited, and in a competitive manner, by validoxylamine. On the other hand, amylase, but not trehalose synthase activity, is inhibited by the known transition-state amylase inhibitor, acarbose, suggesting the possibility of two different active sites. Other metal ions such as Mg2+, Mn2+, and Co2+ are also somewhat effective in the stimulation of amylase activity, but Hg2+, Cu2+, Ni2+ and Zn2+ are inhibitory.3 Publications

Kineticsi

  1. KM=8.0 mM for maltose (at pH 6.8 and 37 degrees Celsius)3 Publications
  2. KM=87 mM for trehalose (at pH 6.8 and at 37 degrees Celsius)3 Publications
  3. KM=2.9 mM for 2,4-dinitrophenyl alpha-D-glucoside (at pH 6.8 and 37 degrees Celsius)3 Publications
  4. KM=2.5 mM for 3,4-dinitrophenyl alpha-D-glucoside (at pH 6.8 and 37 degrees Celsius)3 Publications
  5. KM=2.2 mM for 4-chloro-2-nitrophenyl alpha-D-glucoside (at pH 6.8 and 37 degrees Celsius)3 Publications
  6. KM=5.8 mM for 4-nitrophenyl alpha-D-glucoside (at pH 6.8 and 37 degrees Celsius)3 Publications
  7. KM=0.7 mM for 2-nitrophenyl alpha-D-glucoside (at pH 6.8 and 37 degrees Celsius)3 Publications
  8. KM=0.15 mM for alpha-glucosyl fluoride (at pH 6.8 and 37 degrees Celsius)3 Publications

    pH dependencei

    Optimum pH is between 6.0-6.2 for the amylase activity and 7.0 for the trehalose synthase activity.2 Publications

    Pathwayi: glycogen biosynthesis

    This protein is involved in the pathway glycogen biosynthesis, which is part of Glycan biosynthesis.2 Publications
    View all proteins of this organism that are known to be involved in the pathway glycogen biosynthesis and in Glycan biosynthesis.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei90SubstrateBy similarity1
    Metal bindingi132CalciumCombined sources1 Publication1
    Binding sitei133SubstrateBy similarity1
    Binding sitei198SubstrateBy similarity1
    Metal bindingi200CalciumCombined sources1 Publication1
    Binding sitei228SubstrateBy similarity1
    Active sitei230Nucleophile1 Publication1
    Metal bindingi234Calcium; via carbonyl oxygenCombined sources1 Publication1
    Metal bindingi235Calcium; via carbonyl oxygenCombined sources1 Publication1
    Metal bindingi237CalciumCombined sources1 Publication1
    Active sitei272Proton donorBy similarity1
    Binding sitei341SubstrateBy similarity1
    Binding sitei342SubstrateBy similarity1

    GO - Molecular functioni

    GO - Biological processi

    Keywordsi

    Molecular functionGlycosidase, Hydrolase, Isomerase
    Biological processCarbohydrate metabolism, Glycogen biosynthesis, Glycogen metabolism, Polysaccharide degradation
    LigandCalcium, Metal-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-6023
    BRENDAi5.4.99.16 3512
    UniPathwayi
    UPA00164

    Protein family/group databases

    CAZyiGH13 Glycoside Hydrolase Family 13

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Trehalose synthase/amylase TreS1 Publication (EC:3.2.1.11 Publication, EC:5.4.99.163 Publications)
    Alternative name(s):
    Maltose alpha-D-glucosyltransferase1 Publication
    Short name:
    MTase1 Publication
    Gene namesi
    Name:treS1 Publication
    Ordered Locus Names:MSMEG_6515, MSMEI_6343
    OrganismiMycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
    Taxonomic identifieri246196 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycolicibacterium
    Proteomesi
    • UP000006158 Componenti: Chromosome
    • UP000000757 Componenti: Chromosome

    Pathology & Biotechi

    Disruption phenotypei

    Cells lacking this gene do not accumulate increased amounts of glycogen in the presence of trehalose and show only a small effect in alpha-glucan (PubMed:20118231, PubMed:27513637). Combined inactivation of treS with glgB or glgC completely blocks alpha-glucan production (PubMed:27513637).2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00004129051 – 593Trehalose synthase/amylase TreSAdd BLAST593

    Proteomic databases

    PRIDEiA0R6E0

    Interactioni

    Subunit structurei

    Homohexamer.1 Publication

    Protein-protein interaction databases

    STRINGi246196.MSMEG_6515

    Structurei

    Secondary structure

    1593
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    ProteinModelPortaliA0R6E0
    SMRiA0R6E0
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG4105CG3 Bacteria
    COG0366 LUCA
    HOGENOMiHOG000220639
    KOiK05343
    OMAiVDVQKTQ
    OrthoDBiPOG091H07NZ

    Family and domain databases

    Gene3Di2.60.40.1180, 1 hit
    InterProiView protein in InterPro
    IPR006047 Glyco_hydro_13_cat_dom
    IPR013780 Glyco_hydro_b
    IPR017853 Glycoside_hydrolase_SF
    IPR032091 Malt_amylase_C
    IPR012810 TreS/a-amylase_N
    PfamiView protein in Pfam
    PF00128 Alpha-amylase, 1 hit
    PF16657 Malt_amylase_C, 1 hit
    SMARTiView protein in SMART
    SM00642 Aamy, 1 hit
    SUPFAMiSSF51445 SSF51445, 1 hit
    TIGRFAMsiTIGR02456 treS_nterm, 1 hit

    Sequencei

    Sequence statusi: Complete.

    A0R6E0-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MEEHTQGSHV EAGIVEHPNA EDFGHARTLP TDTNWFKHAV FYEVLVRAFY
    60 70 80 90 100
    DSNADGIGDL RGLTEKLDYI KWLGVDCLWL PPFYDSPLRD GGYDIRDFYK
    110 120 130 140 150
    VLPEFGTVDD FVTLLDAAHR RGIRIITDLV MNHTSDQHEW FQESRHNPDG
    160 170 180 190 200
    PYGDFYVWSD TSDRYPDARI IFVDTEESNW TFDPVRRQFY WHRFFSHQPD
    210 220 230 240 250
    LNYDNPAVQE AMLDVLRFWL DLGIDGFRLD AVPYLFEREG TNCENLPETH
    260 270 280 290 300
    AFLKRCRKAI DDEYPGRVLL AEANQWPADV VAYFGDPDTG GDECHMAFHF
    310 320 330 340 350
    PLMPRIFMAV RRESRFPISE ILAQTPPIPD TAQWGIFLRN HDELTLEMVT
    360 370 380 390 400
    DEERDYMYAE YAKDPRMKAN VGIRRRLAPL LENDRNQIEL FTALLLSLPG
    410 420 430 440 450
    SPVLYYGDEI GMGDIIWLGD RDSVRTPMQW TPDRNAGFSK ATPGRLYLPP
    460 470 480 490 500
    NQDAVYGYHS VNVEAQLDSS SSLLNWTRNM LAVRSRHDAF AVGTFRELGG
    510 520 530 540 550
    SNPSVLAYIR EVTRQQGDGG AKTDAVLCVN NLSRFPQPIE LNLQQWAGYI
    560 570 580 590
    PVEMTGYVEF PSIGQLPYLL TLPGHGFYWF QLREPDPEPG AQQ
    Length:593
    Mass (Da):68,201
    Last modified:January 9, 2007 - v1
    Checksum:iD63935658A86B6E4
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    CP000480 Genomic DNA Translation: ABK71531.1
    CP001663 Genomic DNA Translation: AFP42769.1
    RefSeqiWP_003897929.1, NZ_CP009494.1
    YP_890728.1, NC_008596.1

    Genome annotation databases

    EnsemblBacteriaiABK71531; ABK71531; MSMEG_6515
    AFP42769; AFP42769; MSMEI_6343
    GeneIDi4533171
    KEGGimsb:LJ00_32205
    msg:MSMEI_6343
    msm:MSMEG_6515
    PATRICifig|246196.19.peg.6339

    Similar proteinsi

    Entry informationi

    Entry nameiTRES_MYCS2
    AccessioniPrimary (citable) accession number: A0R6E0
    Secondary accession number(s): I7GGI2
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 21, 2011
    Last sequence update: January 9, 2007
    Last modified: September 12, 2018
    This is version 81 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

    3D-structure, Complete proteome, Reference proteome
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health

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