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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.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

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: 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)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

    • 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

    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:3.2.1.11 Publication, EC:5.4.99.163 Publications)
    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
    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.1 Publication

    PTM / Processingi

    Molecule processing

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

    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
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi20 – 22Combined sources3
    Helixi35 – 38Combined sources4
    Beta strandi41 – 43Combined sources3
    Helixi46 – 49Combined sources4
    Beta strandi52 – 57Combined sources6
    Helixi60 – 65Combined sources6
    Helixi67 – 73Combined sources7
    Beta strandi77 – 80Combined sources4
    Turni89 – 92Combined sources4
    Beta strandi96 – 101Combined sources6
    Helixi103 – 105Combined sources3
    Helixi108 – 120Combined sources13
    Beta strandi124 – 130Combined sources7
    Helixi139 – 146Combined sources8
    Turni151 – 154Combined sources4
    Beta strandi158 – 162Combined sources5
    Turni171 – 175Combined sources5
    Beta strandi179 – 182Combined sources4
    Turni184 – 186Combined sources3
    Beta strandi188 – 191Combined sources4
    Helixi206 – 222Combined sources17
    Beta strandi226 – 231Combined sources6
    Helixi232 – 234Combined sources3
    Beta strandi243 – 245Combined sources3
    Helixi247 – 263Combined sources17
    Beta strandi268 – 272Combined sources5
    Helixi277 – 280Combined sources4
    Helixi281 – 284Combined sources4
    Helixi287 – 289Combined sources3
    Beta strandi295 – 298Combined sources4
    Helixi302 – 312Combined sources11
    Helixi316 – 323Combined sources8
    Beta strandi333 – 336Combined sources4
    Turni343 – 345Combined sources3
    Turni352 – 354Combined sources3
    Turni356 – 360Combined sources5
    Helixi361 – 363Combined sources3
    Helixi365 – 369Combined sources5
    Turni370 – 372Combined sources3
    Helixi377 – 380Combined sources4
    Turni381 – 383Combined sources3
    Helixi385 – 397Combined sources13
    Beta strandi398 – 405Combined sources8
    Turni406 – 411Combined sources6
    Helixi416 – 418Combined sources3
    Helixi422 – 424Combined sources3
    Helixi434 – 437Combined sources4
    Helixi443 – 445Combined sources3
    Beta strandi446 – 448Combined sources3
    Turni454 – 456Combined sources3
    Turni458 – 460Combined sources3
    Helixi463 – 467Combined sources5
    Helixi473 – 485Combined sources13
    Helixi488 – 492Combined sources5
    Beta strandi494 – 497Combined sources4
    Beta strandi505 – 512Combined sources8
    Beta strandi524 – 531Combined sources8
    Beta strandi533 – 535Combined sources3
    Beta strandi537 – 541Combined sources5
    Helixi544 – 546Combined sources3
    Beta strandi550 – 553Combined sources4
    Turni554 – 556Combined sources3
    Beta strandi568 – 572Combined sources5
    Beta strandi577 – 583Combined sources7

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3ZO9X-ray1.84A/B1-593[»]
    3ZOAX-ray1.85A/B1-593[»]
    ProteinModelPortaliA0R6E0.
    SMRiA0R6E0.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG4105CG3. Bacteria.
    COG0366. LUCA.
    HOGENOMiHOG000220639.
    KOiK05343.
    OMAiLLNWTER.
    OrthoDBiPOG091H07NZ.

    Family and domain databases

    Gene3Di2.60.40.1180. 1 hit.
    3.20.20.80. 3 hits.
    InterProiIPR015902. Glyco_hydro_13.
    IPR006047. Glyco_hydro_13_cat_dom.
    IPR013780. Glyco_hydro_b.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    IPR032091. Malt_amylase_C.
    IPR012810. TreS/a-amylase_N.
    [Graphical view]
    PANTHERiPTHR10357. PTHR10357. 2 hits.
    PfamiPF00128. Alpha-amylase. 1 hit.
    PF16657. Malt_amylase_C. 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. 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.
    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. NZ_CP009494.1.
    YP_890728.1. NC_008596.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3ZO9X-ray1.84A/B1-593[»]
    3ZOAX-ray1.85A/B1-593[»]
    ProteinModelPortaliA0R6E0.
    SMRiA0R6E0.
    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.
    KEGGimsb:LJ00_32205.
    msg:MSMEI_6343.
    msm:MSMEG_6515.
    PATRICi18085253. VBIMycSme59918_6339.

    Phylogenomic databases

    eggNOGiENOG4105CG3. Bacteria.
    COG0366. LUCA.
    HOGENOMiHOG000220639.
    KOiK05343.
    OMAiLLNWTER.
    OrthoDBiPOG091H07NZ.

    Enzyme and pathway databases

    UniPathwayiUPA00164.
    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.
    IPR006047. Glyco_hydro_13_cat_dom.
    IPR013780. Glyco_hydro_b.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    IPR032091. Malt_amylase_C.
    IPR012810. TreS/a-amylase_N.
    [Graphical view]
    PANTHERiPTHR10357. PTHR10357. 2 hits.
    PfamiPF00128. Alpha-amylase. 1 hit.
    PF16657. Malt_amylase_C. 1 hit.
    [Graphical view]
    SMARTiSM00642. Aamy. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.
    TIGRFAMsiTIGR02456. treS_nterm. 1 hit.
    ProtoNetiSearch...

    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: November 2, 2016
    This is version 70 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

    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 one 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.