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Protein

Trehalose synthase/amylase TreS

Gene

treS

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalyzes the reversible interconversion of maltose and trehalose by transglucosylation (PubMed:18505459). 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 (PubMed:18505459). TreS plays a key role in the utilization of trehalose for the production of glycogen and alpha-glucan via the TreS-Pep2 branch involved in the biosynthesis of maltose-1-phosphate (M1P) (PubMed:18505459, PubMed:27513637). Might also function as a sensor and/or regulator of trehalose levels within the cell (PubMed:18505459). Thus, when trehalose levels in the cell become dangerously low, TreS could expedite the conversion of glycogen to maltose via its amylase activity and then convert the maltose to trehalose; but this enzyme also could expedite or promote the conversion of trehalose to glycogen when cytoplasmic trehalose levels become too high (PubMed:18505459).2 Publications

Miscellaneous

Was identified as a high-confidence drug target.
Maltose-1-phosphate (M1P), the building block required for alpha-glucan production, is generated by two alternative routes: the TreS-Pep2 branch and the GlgC-GlgM branch, however it seems that TreS-Pep2 branch provides most of M1P for the GlgE pathway in M.tuberculosis.1 Publication

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

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.

Pathwayi: capsule polysaccharide biosynthesis

This protein is involved in the pathway capsule polysaccharide biosynthesis, which is part of Capsule biogenesis.1 Publication
View all proteins of this organism that are known to be involved in the pathway capsule polysaccharide biosynthesis and in Capsule biogenesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei98SubstrateBy similarity1
Metal bindingi140CalciumBy similarity1
Binding sitei141SubstrateBy similarity1
Binding sitei206SubstrateBy similarity1
Metal bindingi208CalciumBy similarity1
Binding sitei236SubstrateBy similarity1
Active sitei238NucleophileBy similarity1
Metal bindingi242Calcium; via carbonyl oxygenBy similarity1
Metal bindingi243Calcium; via carbonyl oxygenBy similarity1
Metal bindingi245CalciumBy similarity1
Active sitei280Proton donorBy similarity1
Binding sitei349SubstrateBy similarity1
Binding sitei350SubstrateBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionGlycosidase, Hydrolase, Isomerase
Biological processCapsule biogenesis/degradation, Carbohydrate metabolism, Glycogen biosynthesis, Glycogen metabolism, Polysaccharide degradation
LigandCalcium, Metal-binding

Enzyme and pathway databases

ReactomeiR-MTU-868688 Trehalose biosynthesis
UniPathwayi
UPA00164

UPA00934

Names & Taxonomyi

Protein namesi
Recommended name:
Trehalose synthase/amylase TreS1 Publication (EC:3.2.1.11 Publication, EC:5.4.99.161 Publication)
Alternative name(s):
Maltose alpha-D-glucosyltransferase1 Publication
Short name:
MTase1 Publication
Gene namesi
Name:treS1 Publication
Ordered Locus Names:Rv0126
OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Taxonomic identifieri83332 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
Proteomesi
  • UP000001584 Componenti: Chromosome

Organism-specific databases

TubercuListiRv0126

Subcellular locationi

GO - Cellular componenti

Pathology & Biotechi

Disruption phenotypei

Cells lacking this gene are as virulent as wild-type in mice, however also show a profound impact on intracellular and capsular glucan (PubMed:20305657, PubMed:27513637). It is not possible to inactivate Rv3032 in a mutant lacking treS, suggesting the joint essentiality of the different alpha-(1->4)-glucans biosynthesis pathways involving these two genes (PubMed:20305657). Combined inactivation of glgM and treS results in absence of alpha-glucan (PubMed:27513637). Combined inactivation of treS and glgC results in absence of alpha-glucan content and is significantly attenuated for growth in the lung and spleen of BALB/C mice during both the acute and chronic phase of infection (PubMed:27513637).2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004129061 – 601Trehalose synthase/amylase TreSAdd BLAST601

Proteomic databases

PaxDbiP9WQ19

Interactioni

Subunit structurei

Homohexamer.By similarity

Protein-protein interaction databases

STRINGi83332.Rv0126

Structurei

3D structure databases

ProteinModelPortaliP9WQ19
SMRiP9WQ19
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105CG3 Bacteria
COG0366 LUCA
KOiK05343
OMAiPNGEKWA
PhylomeDBiP9WQ19

Family and domain databases

Gene3Di2.60.40.1180, 1 hit
InterProiView protein in InterPro
IPR006047 Glyco_hydro_13_cat_dom
IPR013780 Glyco_hydro_b
IPR017853 Glycoside_hydrolase_SF
IPR032091 Malt_amylase_C
IPR012810 TreS/a-amylase_N
PfamiView protein in Pfam
PF00128 Alpha-amylase, 1 hit
PF16657 Malt_amylase_C, 1 hit
SMARTiView protein in SMART
SM00642 Aamy, 1 hit
SUPFAMiSSF51445 SSF51445, 1 hit
TIGRFAMsiTIGR02456 treS_nterm, 1 hit

Sequencei

Sequence statusi: Complete.

P9WQ19-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MNEAEHSVEH PPVQGSHVEG GVVEHPDAKD FGSAAALPAD PTWFKHAVFY
60 70 80 90 100
EVLVRAFFDA SADGSGDLRG LIDRLDYLQW LGIDCIWLPP FYDSPLRDGG
110 120 130 140 150
YDIRDFYKVL PEFGTVDDFV ALVDAAHRRG IRIITDLVMN HTSESHPWFQ
160 170 180 190 200
ESRRDPDGPY GDYYVWSDTS ERYTDARIIF VDTEESNWSF DPVRRQFYWH
210 220 230 240 250
RFFSHQPDLN YDNPAVQEAM IDVIRFWLGL GIDGFRLDAV PYLFEREGTN
260 270 280 290 300
CENLPETHAF LKRVRKVVDD EFPGRVLLAE ANQWPGDVVE YFGDPNTGGD
310 320 330 340 350
ECHMAFHFPL MPRIFMAVRR ESRFPISEII AQTPPIPDMA QWGIFLRNHD
360 370 380 390 400
ELTLEMVTDE ERDYMYAEYA KDPRMKANVG IRRRLAPLLD NDRNQIELFT
410 420 430 440 450
ALLLSLPGSP VLYYGDEIGM GDVIWLGDRD GVRIPMQWTP DRNAGFSTAN
460 470 480 490 500
PGRLYLPPSQ DPVYGYQAVN VEAQRDTSTS LLNFTRTMLA VRRRHPAFAV
510 520 530 540 550
GAFQELGGSN PSVLAYVRQV AGDDGDTVLC VNNLSRFPQP IELDLQQWTN
560 570 580 590 600
YTPVELTGHV EFPRIGQVPY LLTLPGHGFY WFQLTTHEVG APPTCGGERR

L
Length:601
Mass (Da):68,593
Last modified:April 16, 2014 - v1
Checksum:iFE52E5258F38116E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA Translation: CCP42851.1
PIRiG70983
RefSeqiNP_214640.1, NC_000962.3
WP_003400893.1, NZ_NVQJ01000001.1

Genome annotation databases

EnsemblBacteriaiCCP42851; CCP42851; Rv0126
GeneIDi886881
KEGGimtu:Rv0126

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA Translation: CCP42851.1
PIRiG70983
RefSeqiNP_214640.1, NC_000962.3
WP_003400893.1, NZ_NVQJ01000001.1

3D structure databases

ProteinModelPortaliP9WQ19
SMRiP9WQ19
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi83332.Rv0126

Proteomic databases

PaxDbiP9WQ19

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCCP42851; CCP42851; Rv0126
GeneIDi886881
KEGGimtu:Rv0126

Organism-specific databases

TubercuListiRv0126

Phylogenomic databases

eggNOGiENOG4105CG3 Bacteria
COG0366 LUCA
KOiK05343
OMAiPNGEKWA
PhylomeDBiP9WQ19

Enzyme and pathway databases

UniPathwayi
UPA00164

UPA00934

ReactomeiR-MTU-868688 Trehalose biosynthesis

Family and domain databases

Gene3Di2.60.40.1180, 1 hit
InterProiView protein in InterPro
IPR006047 Glyco_hydro_13_cat_dom
IPR013780 Glyco_hydro_b
IPR017853 Glycoside_hydrolase_SF
IPR032091 Malt_amylase_C
IPR012810 TreS/a-amylase_N
PfamiView protein in Pfam
PF00128 Alpha-amylase, 1 hit
PF16657 Malt_amylase_C, 1 hit
SMARTiView protein in SMART
SM00642 Aamy, 1 hit
SUPFAMiSSF51445 SSF51445, 1 hit
TIGRFAMsiTIGR02456 treS_nterm, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiTRES_MYCTU
AccessioniPrimary (citable) accession number: P9WQ19
Secondary accession number(s): L0T5R2, O07176, Q7DAF7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 16, 2014
Last sequence update: April 16, 2014
Last modified: November 7, 2018
This is version 30 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  4. Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
    Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names
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Main funding by: National Institutes of Health

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