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A0R6E0

- TRES_MYCS2

UniProt

A0R6E0 - TRES_MYCS2

Protein

Trehalose synthase/amylase TreS

Gene

treS

Organism
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 57 (01 Oct 2014)
      Sequence version 1 (09 Jan 2007)
      Previous versions | rss
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    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

    Pathwayi

    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

    1. alpha-amylase activity Source: UniProtKB
    2. calcium ion binding Source: UniProtKB
    3. maltose alpha-D-glucosyltransferase activity Source: UniProtKB

    GO - Biological processi

    1. glycogen biosynthetic process Source: UniProtKB-UniPathway
    2. glycogen metabolic process Source: UniProtKB
    3. maltose metabolic process Source: UniProtKB
    4. polysaccharide catabolic process Source: UniProtKB-KW
    5. trehalose metabolic process Source: UniProtKB

    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.
    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 lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium
    ProteomesiUP000000757: Chromosome, UP000006158: 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
    Helixi35 – 384
    Beta strandi41 – 433
    Helixi46 – 494
    Beta strandi52 – 576
    Helixi60 – 656
    Helixi67 – 737
    Beta strandi77 – 804
    Turni89 – 924
    Beta strandi96 – 1016
    Helixi103 – 1053
    Helixi108 – 12013
    Beta strandi124 – 1307
    Helixi139 – 1468
    Turni151 – 1544
    Beta strandi158 – 1625
    Turni171 – 1755
    Beta strandi179 – 1824
    Turni184 – 1863
    Beta strandi188 – 1914
    Helixi206 – 22217
    Beta strandi226 – 2316
    Helixi232 – 2343
    Beta strandi243 – 2453
    Helixi247 – 26317
    Beta strandi268 – 2725
    Helixi277 – 2804
    Helixi281 – 2844
    Helixi287 – 2893
    Beta strandi295 – 2984
    Helixi302 – 31211
    Helixi316 – 3238
    Beta strandi333 – 3364
    Turni343 – 3453
    Turni352 – 3543
    Turni356 – 3605
    Helixi361 – 3633
    Helixi365 – 3695
    Turni370 – 3723
    Helixi377 – 3804
    Turni381 – 3833
    Helixi385 – 39713
    Beta strandi398 – 4058
    Turni406 – 4116
    Helixi416 – 4183
    Helixi422 – 4243
    Helixi434 – 4374
    Helixi443 – 4453
    Beta strandi446 – 4483
    Turni454 – 4563
    Turni458 – 4603
    Helixi463 – 4675
    Helixi473 – 48513
    Helixi488 – 4925
    Beta strandi494 – 4974
    Beta strandi505 – 5128
    Beta strandi524 – 5318
    Beta strandi533 – 5353
    Beta strandi537 – 5415
    Helixi544 – 5463
    Beta strandi550 – 5534
    Turni554 – 5563
    Beta strandi568 – 5725
    Beta strandi577 – 5837

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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

    MEEHTQGSHV EAGIVEHPNA EDFGHARTLP TDTNWFKHAV FYEVLVRAFY    50
    DSNADGIGDL RGLTEKLDYI KWLGVDCLWL PPFYDSPLRD GGYDIRDFYK 100
    VLPEFGTVDD FVTLLDAAHR RGIRIITDLV MNHTSDQHEW FQESRHNPDG 150
    PYGDFYVWSD TSDRYPDARI IFVDTEESNW TFDPVRRQFY WHRFFSHQPD 200
    LNYDNPAVQE AMLDVLRFWL DLGIDGFRLD AVPYLFEREG TNCENLPETH 250
    AFLKRCRKAI DDEYPGRVLL AEANQWPADV VAYFGDPDTG GDECHMAFHF 300
    PLMPRIFMAV RRESRFPISE ILAQTPPIPD TAQWGIFLRN HDELTLEMVT 350
    DEERDYMYAE YAKDPRMKAN VGIRRRLAPL LENDRNQIEL FTALLLSLPG 400
    SPVLYYGDEI GMGDIIWLGD RDSVRTPMQW TPDRNAGFSK ATPGRLYLPP 450
    NQDAVYGYHS VNVEAQLDSS SSLLNWTRNM LAVRSRHDAF AVGTFRELGG 500
    SNPSVLAYIR EVTRQQGDGG AKTDAVLCVN NLSRFPQPIE LNLQQWAGYI 550
    PVEMTGYVEF PSIGQLPYLL TLPGHGFYWF QLREPDPEPG AQQ 593
    Length:593
    Mass (Da):68,201
    Last modified:January 9, 2007 - v1
    Checksum:iD63935658A86B6E4
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000480 Genomic DNA. Translation: ABK71531.1.
    CP001663 Genomic DNA. Translation: AFP42769.1.
    RefSeqiYP_006571064.1. NC_018289.1.
    YP_890728.1. NC_008596.1.

    Genome annotation databases

    EnsemblBacteriaiABK71531; ABK71531; MSMEG_6515.
    AFP42769; AFP42769; MSMEI_6343.
    GeneIDi4533171.
    KEGGimsg:MSMEI_6343.
    msm:MSMEG_6515.
    PATRICi18085253. VBIMycSme59918_6339.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000480 Genomic DNA. Translation: ABK71531.1 .
    CP001663 Genomic DNA. Translation: AFP42769.1 .
    RefSeqi YP_006571064.1. NC_018289.1.
    YP_890728.1. NC_008596.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3ZO9 X-ray 1.84 A/B 1-593 [» ]
    3ZOA X-ray 1.85 A/B 1-593 [» ]
    ProteinModelPortali A0R6E0.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 246196.MSMEG_6515.

    Protein family/group databases

    CAZyi GH13. Glycoside Hydrolase Family 13.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABK71531 ; ABK71531 ; MSMEG_6515 .
    AFP42769 ; AFP42769 ; MSMEI_6343 .
    GeneIDi 4533171.
    KEGGi msg:MSMEI_6343.
    msm:MSMEG_6515.
    PATRICi 18085253. VBIMycSme59918_6339.

    Phylogenomic databases

    eggNOGi COG0366.
    HOGENOMi HOG000220639.
    KOi K05343.
    OMAi RMKANIG.
    OrthoDBi EOG6RVFV2.

    Enzyme and pathway databases

    UniPathwayi UPA00164 .
    BioCyci MSME246196:GJ4Y-6514-MONOMER.

    Family and domain databases

    Gene3Di 2.60.40.1180. 1 hit.
    3.20.20.80. 3 hits.
    InterProi IPR015902. 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 ]
    PANTHERi PTHR10357. PTHR10357. 1 hit.
    Pfami PF00128. Alpha-amylase. 1 hit.
    [Graphical view ]
    SMARTi SM00642. Aamy. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 1 hit.
    TIGRFAMsi TIGR02456. treS_nterm. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 57 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