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A0R6E0 (TRES_MYCS2) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:treS
Ordered Locus Names:MSMEG_6515, MSMEI_6343
OrganismMycobacterium smegmatis (strain ATCC 700084 / mc(2)155) [Reference proteome] [HAMAP]
Taxonomic identifier246196 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

Protein attributes

Sequence length593 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.5 Ref.6 Ref.7 Ref.8

Catalytic activity

Maltose = alpha,alpha-trehalose. Ref.5

Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units. Ref.5

Enzyme regulation

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. Ref.4 Ref.5 Ref.6

Pathway

Glycan biosynthesis; glycogen biosynthesis. Ref.7

Subunit structure

Homohexamer. Ref.5

Disruption phenotype

Cells lacking this gene do not accumulate increased amounts of glycogen in the presence of trehalose. Ref.7

Sequence similarities

Belongs to the glycosyl hydrolase 13 family. TreS subfamily.

Biophysicochemical properties

Kinetic parameters:

KM=8.0 mM for maltose (at pH 6.8 and 37 degrees Celsius) Ref.5 Ref.6 Ref.8

KM=87 mM for trehalose (at pH 6.8 and at 37 degrees Celsius)

KM=2.9 mM for 2,4-dinitrophenyl alpha-D-glucoside (at pH 6.8 and 37 degrees Celsius)

KM=2.5 mM for 3,4-dinitrophenyl alpha-D-glucoside (at pH 6.8 and 37 degrees Celsius)

KM=2.2 mM for 4-chloro-2-nitrophenyl alpha-D-glucoside (at pH 6.8 and 37 degrees Celsius)

KM=5.8 mM for 4-nitrophenyl alpha-D-glucoside (at pH 6.8 and 37 degrees Celsius)

KM=0.7 mM for 2-nitrophenyl alpha-D-glucoside (at pH 6.8 and 37 degrees Celsius)

KM=0.15 mM for alpha-glucosyl fluoride (at pH 6.8 and 37 degrees Celsius)

pH dependence:

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 593593Trehalose synthase/amylase TreS
PRO_0000412905

Sites

Active site2301Nucleophile Ref.8
Active site2721Proton donor By similarity
Metal binding1321Calcium By similarity
Metal binding2001Calcium By similarity
Metal binding2341Calcium; via carbonyl oxygen By similarity

Secondary structure

...................................................................................................................... 593
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
A0R6E0 [UniParc].

Last modified January 9, 2007. Version 1.
Checksum: D63935658A86B6E4

FASTA59368,201
        10         20         30         40         50         60 
MEEHTQGSHV EAGIVEHPNA EDFGHARTLP TDTNWFKHAV FYEVLVRAFY DSNADGIGDL 

        70         80         90        100        110        120 
RGLTEKLDYI KWLGVDCLWL PPFYDSPLRD GGYDIRDFYK VLPEFGTVDD FVTLLDAAHR 

       130        140        150        160        170        180 
RGIRIITDLV MNHTSDQHEW FQESRHNPDG PYGDFYVWSD TSDRYPDARI IFVDTEESNW 

       190        200        210        220        230        240 
TFDPVRRQFY WHRFFSHQPD LNYDNPAVQE AMLDVLRFWL DLGIDGFRLD AVPYLFEREG 

       250        260        270        280        290        300 
TNCENLPETH AFLKRCRKAI DDEYPGRVLL AEANQWPADV VAYFGDPDTG GDECHMAFHF 

       310        320        330        340        350        360 
PLMPRIFMAV RRESRFPISE ILAQTPPIPD TAQWGIFLRN HDELTLEMVT DEERDYMYAE 

       370        380        390        400        410        420 
YAKDPRMKAN VGIRRRLAPL LENDRNQIEL FTALLLSLPG SPVLYYGDEI GMGDIIWLGD 

       430        440        450        460        470        480 
RDSVRTPMQW TPDRNAGFSK ATPGRLYLPP NQDAVYGYHS VNVEAQLDSS SSLLNWTRNM 

       490        500        510        520        530        540 
LAVRSRHDAF AVGTFRELGG SNPSVLAYIR EVTRQQGDGG AKTDAVLCVN NLSRFPQPIE 

       550        560        570        580        590 
LNLQQWAGYI PVEMTGYVEF PSIGQLPYLL TLPGHGFYWF QLREPDPEPG AQQ 

« Hide

References

« Hide 'large scale' references
[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]"Trehalose synthase converts glycogen to trehalose."
Pan Y.T., Carroll J.D., Asano N., Pastuszak I., Edavana V.K., Elbein A.D.
FEBS J. 275:3408-3420(2008) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000480 Genomic DNA. Translation: ABK71531.1.
CP001663 Genomic DNA. Translation: AFP42769.1.
RefSeqYP_006571064.1. NC_018289.1.
YP_890728.1. NC_008596.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3ZO9X-ray1.84A/B1-593[»]
3ZOAX-ray1.85A/B1-593[»]
ProteinModelPortalA0R6E0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING246196.MSMEG_6515.

Protein family/group databases

CAZyGH13. Glycoside Hydrolase Family 13.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABK71531; ABK71531; MSMEG_6515.
AFP42769; AFP42769; MSMEI_6343.
GeneID4533171.
KEGGmsg:MSMEI_6343.
msm:MSMEG_6515.
PATRIC18085253. VBIMycSme59918_6339.

Phylogenomic databases

eggNOGCOG0366.
HOGENOMHOG000220639.
KOK05343.
OMARMKANIG.
OrthoDBEOG6RVFV2.

Enzyme and pathway databases

BioCycMSME246196:GJ4Y-6514-MONOMER.
UniPathwayUPA00164.

Family and domain databases

Gene3D2.60.40.1180. 1 hit.
3.20.20.80. 3 hits.
InterProIPR015902. 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]
PANTHERPTHR10357. PTHR10357. 1 hit.
PfamPF00128. Alpha-amylase. 1 hit.
[Graphical view]
SMARTSM00642. Aamy. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
TIGRFAMsTIGR02456. treS_nterm. 1 hit.
ProtoNetSearch...

Entry information

Entry nameTRES_MYCS2
AccessionPrimary (citable) accession number: A0R6E0
Secondary accession number(s): I7GGI2
Entry history
Integrated into UniProtKB/Swiss-Prot: September 21, 2011
Last sequence update: January 9, 2007
Last modified: July 9, 2014
This is version 56 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries