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A0R6E0

- TRES_MYCS2

UniProt

A0R6E0 - TRES_MYCS2

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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

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
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.
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 – 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.
RefSeqiYP_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 .
RefSeqi 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
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 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

« 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: November 26, 2014
This is version 59 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