Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Trehalose synthase/amylase TreS

Gene

treS

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

Catalyzes the reversible interconversion of maltose and trehalose by transglucosylation. Maltose is the preferred substrate. 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. TreS plays a key role in the utilization of trehalose for the production of glycogen, and 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.4 Publications

Catalytic activityi

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

Enzyme 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

    Pathway: glycogen biosynthesis

    This protein is involved in the pathway glycogen biosynthesis, which is part of Glycan biosynthesis.1 Publication
    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)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi132 – 1321CalciumBy similarity
    Metal bindingi200 – 2001CalciumBy similarity
    Active sitei230 – 2301Nucleophile1 Publication
    Metal bindingi234 – 2341Calcium; via carbonyl oxygenBy similarity
    Active sitei272 – 2721Proton donorBy similarity

    GO - Molecular functioni

    • alpha-amylase activity Source: UniProtKB
    • calcium ion binding Source: UniProtKB
    • maltose alpha-D-glucosyltransferase activity Source: UniProtKB

    GO - Biological processi

    • glycogen biosynthetic process Source: UniProtKB-UniPathway
    • glycogen metabolic process Source: UniProtKB
    • maltose metabolic process Source: UniProtKB
    • polysaccharide catabolic process Source: UniProtKB-KW
    • trehalose metabolic process Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Glycosidase, Hydrolase, Isomerase

    Keywords - Biological processi

    Carbohydrate metabolism, Glycogen biosynthesis, Glycogen metabolism, Polysaccharide degradation

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    BioCyciMSME246196:GJ4Y-6514-MONOMER.
    BRENDAi5.4.99.16. 3512.
    UniPathwayiUPA00164.

    Protein family/group databases

    CAZyiGH13. Glycoside Hydrolase Family 13.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Trehalose synthase/amylase TreS (EC:3.2.1.1, EC:5.4.99.16)
    Alternative name(s):
    Maltose alpha-D-glucosyltransferase
    Short name:
    MTase
    Gene namesi
    Name:treS
    Ordered Locus Names:MSMEG_6515, MSMEI_6343
    OrganismiMycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
    Taxonomic identifieri246196 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacterium
    ProteomesiUP000006158 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.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 593593Trehalose synthase/amylase TreSPRO_0000412905Add
    BLAST

    Interactioni

    Subunit structurei

    Homohexamer.1 Publication

    Protein-protein interaction databases

    STRINGi246196.MSMEG_6515.

    Structurei

    Secondary structure

    1
    593
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi20 – 223Combined sources
    Helixi35 – 384Combined sources
    Beta strandi41 – 433Combined sources
    Helixi46 – 494Combined sources
    Beta strandi52 – 576Combined sources
    Helixi60 – 656Combined sources
    Helixi67 – 737Combined sources
    Beta strandi77 – 804Combined sources
    Turni89 – 924Combined sources
    Beta strandi96 – 1016Combined sources
    Helixi103 – 1053Combined sources
    Helixi108 – 12013Combined sources
    Beta strandi124 – 1307Combined sources
    Helixi139 – 1468Combined sources
    Turni151 – 1544Combined sources
    Beta strandi158 – 1625Combined sources
    Turni171 – 1755Combined sources
    Beta strandi179 – 1824Combined sources
    Turni184 – 1863Combined sources
    Beta strandi188 – 1914Combined sources
    Helixi206 – 22217Combined sources
    Beta strandi226 – 2316Combined sources
    Helixi232 – 2343Combined sources
    Beta strandi243 – 2453Combined sources
    Helixi247 – 26317Combined sources
    Beta strandi268 – 2725Combined sources
    Helixi277 – 2804Combined sources
    Helixi281 – 2844Combined sources
    Helixi287 – 2893Combined sources
    Beta strandi295 – 2984Combined sources
    Helixi302 – 31211Combined sources
    Helixi316 – 3238Combined sources
    Beta strandi333 – 3364Combined sources
    Turni343 – 3453Combined sources
    Turni352 – 3543Combined sources
    Turni356 – 3605Combined sources
    Helixi361 – 3633Combined sources
    Helixi365 – 3695Combined sources
    Turni370 – 3723Combined sources
    Helixi377 – 3804Combined sources
    Turni381 – 3833Combined sources
    Helixi385 – 39713Combined sources
    Beta strandi398 – 4058Combined sources
    Turni406 – 4116Combined sources
    Helixi416 – 4183Combined sources
    Helixi422 – 4243Combined sources
    Helixi434 – 4374Combined sources
    Helixi443 – 4453Combined sources
    Beta strandi446 – 4483Combined sources
    Turni454 – 4563Combined sources
    Turni458 – 4603Combined sources
    Helixi463 – 4675Combined sources
    Helixi473 – 48513Combined sources
    Helixi488 – 4925Combined sources
    Beta strandi494 – 4974Combined sources
    Beta strandi505 – 5128Combined sources
    Beta strandi524 – 5318Combined sources
    Beta strandi533 – 5353Combined sources
    Beta strandi537 – 5415Combined sources
    Helixi544 – 5463Combined sources
    Beta strandi550 – 5534Combined sources
    Turni554 – 5563Combined sources
    Beta strandi568 – 5725Combined sources
    Beta strandi577 – 5837Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3ZO9X-ray1.84A/B1-593[»]
    3ZOAX-ray1.85A/B1-593[»]
    ProteinModelPortaliA0R6E0.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0366.
    HOGENOMiHOG000220639.
    KOiK05343.
    OMAiRMKANIG.
    OrthoDBiEOG6RVFV2.

    Family and domain databases

    Gene3Di2.60.40.1180. 1 hit.
    3.20.20.80. 3 hits.
    InterProiIPR015902. Glyco_hydro_13.
    IPR013780. Glyco_hydro_13_b.
    IPR006047. Glyco_hydro_13_cat_dom.
    IPR006589. Glyco_hydro_13_sub_cat_dom.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    IPR012810. TreS/a-amylase_N.
    [Graphical view]
    PANTHERiPTHR10357. PTHR10357. 1 hit.
    PfamiPF00128. Alpha-amylase. 1 hit.
    [Graphical view]
    SMARTiSM00642. Aamy. 1 hit.
    [Graphical view]
    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. NC_018289.1.
    YP_006571064.1. NC_018289.1.
    YP_890728.1. NC_008596.1.

    Genome annotation databases

    EnsemblBacteriaiABK71531; ABK71531; MSMEG_6515.
    AFP42769; AFP42769; MSMEI_6343.
    GeneIDi4533171.
    KEGGimsm:MSMEG_6515.
    PATRICi18085253. VBIMycSme59918_6339.

    Cross-referencesi

    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. NC_018289.1.
    YP_006571064.1. NC_018289.1.
    YP_890728.1. NC_008596.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3ZO9X-ray1.84A/B1-593[»]
    3ZOAX-ray1.85A/B1-593[»]
    ProteinModelPortaliA0R6E0.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi246196.MSMEG_6515.

    Protein family/group databases

    CAZyiGH13. Glycoside Hydrolase Family 13.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiABK71531; ABK71531; MSMEG_6515.
    AFP42769; AFP42769; MSMEI_6343.
    GeneIDi4533171.
    KEGGimsm:MSMEG_6515.
    PATRICi18085253. VBIMycSme59918_6339.

    Phylogenomic databases

    eggNOGiCOG0366.
    HOGENOMiHOG000220639.
    KOiK05343.
    OMAiRMKANIG.
    OrthoDBiEOG6RVFV2.

    Enzyme and pathway databases

    UniPathwayiUPA00164.
    BioCyciMSME246196:GJ4Y-6514-MONOMER.
    BRENDAi5.4.99.16. 3512.

    Family and domain databases

    Gene3Di2.60.40.1180. 1 hit.
    3.20.20.80. 3 hits.
    InterProiIPR015902. Glyco_hydro_13.
    IPR013780. Glyco_hydro_13_b.
    IPR006047. Glyco_hydro_13_cat_dom.
    IPR006589. Glyco_hydro_13_sub_cat_dom.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    IPR012810. TreS/a-amylase_N.
    [Graphical view]
    PANTHERiPTHR10357. PTHR10357. 1 hit.
    PfamiPF00128. Alpha-amylase. 1 hit.
    [Graphical view]
    SMARTiSM00642. Aamy. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.
    TIGRFAMsiTIGR02456. treS_nterm. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C., Fraser C.M.
      Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 700084 / mc(2)155.
    2. "Interrupted coding sequences in Mycobacterium smegmatis: authentic mutations or sequencing errors?"
      Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C., Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.
      Genome Biol. 8:R20.1-R20.9(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 700084 / mc(2)155.
    3. "Ortho-proteogenomics: multiple proteomes investigation through orthology and a new MS-based protocol."
      Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M., Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.
      Genome Res. 19:128-135(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 700084 / mc(2)155.
    4. "Validoxylamines as trehalase inhibitors."
      Kameda Y., Asano N., Yamaguchi T., Matsui K.
      J. Antibiot. 40:563-565(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    5. "Trehalose synthase of Mycobacterium smegmatis: purification, cloning, expression, and properties of the enzyme."
      Pan Y.T., Koroth Edavana V., Jourdian W.J., Edmondson R., Carroll J.D., Pastuszak I., Elbein A.D.
      Eur. J. Biochem. 271:4259-4269(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS A TREHALOSE SYNTHASE, CATALYTIC ACTIVITY, SUBUNIT, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: ATCC 14468 / DSM 43277 / NCIB 9953 / NCTC 10265 / W-113 and ATCC 700084 / mc(2)155.
    6. Cited for: FUNCTION AS A TREHALOSE SYNTHASE AND AMYLASE, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, ENZYME REGULATION.
    7. "Last step in the conversion of trehalose to glycogen: a mycobacterial enzyme that transfers maltose from maltose 1-phosphate to glycogen."
      Elbein A.D., Pastuszak I., Tackett A.J., Wilson T., Pan Y.T.
      J. Biol. Chem. 285:9803-9812(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ROLE IN CONVERSION OF TREHALOSE TO GLYCOGEN, DISRUPTION PHENOTYPE, PATHWAY.
      Strain: ATCC 14468 / DSM 43277 / NCIB 9953 / NCTC 10265 / W-113.
    8. "Mechanistic analysis of trehalose synthase from mycobacterium smegmatis."
      Zhang R., Pan Y.T., He S., Lam M., Brayer G.D., Elbein A.D., Withers S.G.
      J. Biol. Chem. 286:35601-35609(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, KINETIC PARAMETERS, CATALYTIC MECHANISM, ACTIVE SITE.

    Entry informationi

    Entry nameiTRES_MYCS2
    AccessioniPrimary (citable) accession number: A0R6E0
    Secondary accession number(s): I7GGI2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 21, 2011
    Last sequence update: January 9, 2007
    Last modified: June 24, 2015
    This is version 63 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.