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O07176 (TRES_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 102. 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:Rv0126, MT0134
OrganismMycobacterium tuberculosis [Reference proteome] [HAMAP]
Taxonomic identifier1773 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex

Protein attributes

Sequence length601 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the reversible interconversion of maltose and trehalose by transglucosylation. 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 probably 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 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. Ref.4

Catalytic activity

Maltose = alpha,alpha-trehalose. Ref.4

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

Pathway

Glycan biosynthesis; glycogen biosynthesis.

Subunit structure

Homohexamer By similarity.

Disruption phenotype

Cells lacking this gene are as virulent as wild-type in mice. 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. Ref.5

Miscellaneous

Was identified as a high-confidence drug target.

Sequence similarities

Belongs to the glycosyl hydrolase 13 family. TreS subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 601601Trehalose synthase/amylase TreS
PRO_0000412906

Sites

Active site2381Nucleophile By similarity
Active site2801Proton donor By similarity
Metal binding1401Calcium By similarity
Metal binding2081Calcium By similarity
Metal binding2421Calcium; via carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
O07176 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: FE52E5258F38116E

FASTA60168,593
        10         20         30         40         50         60 
MNEAEHSVEH PPVQGSHVEG GVVEHPDAKD FGSAAALPAD PTWFKHAVFY EVLVRAFFDA 

        70         80         90        100        110        120 
SADGSGDLRG LIDRLDYLQW LGIDCIWLPP FYDSPLRDGG YDIRDFYKVL PEFGTVDDFV 

       130        140        150        160        170        180 
ALVDAAHRRG IRIITDLVMN HTSESHPWFQ ESRRDPDGPY GDYYVWSDTS ERYTDARIIF 

       190        200        210        220        230        240 
VDTEESNWSF DPVRRQFYWH RFFSHQPDLN YDNPAVQEAM IDVIRFWLGL GIDGFRLDAV 

       250        260        270        280        290        300 
PYLFEREGTN CENLPETHAF LKRVRKVVDD EFPGRVLLAE ANQWPGDVVE YFGDPNTGGD 

       310        320        330        340        350        360 
ECHMAFHFPL MPRIFMAVRR ESRFPISEII AQTPPIPDMA QWGIFLRNHD ELTLEMVTDE 

       370        380        390        400        410        420 
ERDYMYAEYA KDPRMKANVG IRRRLAPLLD NDRNQIELFT ALLLSLPGSP VLYYGDEIGM 

       430        440        450        460        470        480 
GDVIWLGDRD GVRIPMQWTP DRNAGFSTAN PGRLYLPPSQ DPVYGYQAVN VEAQRDTSTS 

       490        500        510        520        530        540 
LLNFTRTMLA VRRRHPAFAV GAFQELGGSN PSVLAYVRQV AGDDGDTVLC VNNLSRFPQP 

       550        560        570        580        590        600 
IELDLQQWTN YTPVELTGHV EFPRIGQVPY LLTLPGHGFY WFQLTTHEVG APPTCGGERR 


L 

« Hide

References

« Hide 'large scale' references
[1]"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence."
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. expand/collapse author list , Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., Barrell B.G.
Nature 393:537-544(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25618 / H37Rv.
[2]"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains."
Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. expand/collapse author list , Weidman J.F., Khouri H.M., Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.
J. Bacteriol. 184:5479-5490(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CDC 1551 / Oshkosh.
[3]"targetTB: a target identification pipeline for Mycobacterium tuberculosis through an interactome, reactome and genome-scale structural analysis."
Raman K., Yeturu K., Chandra N.
BMC Syst. Biol. 2:109-109(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
[4]"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, CATALYTIC ACTIVITY.
[5]"Self-poisoning of Mycobacterium tuberculosis by targeting GlgE in an alpha-glucan pathway."
Kalscheuer R., Syson K., Veeraraghavan U., Weinrick B., Biermann K.E., Liu Z., Sacchettini J.C., Besra G., Bornemann S., Jacobs W.R. Jr.
Nat. Chem. Biol. 6:376-384(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, SYNTHETIC LETHALITY.
Strain: ATCC 25618 / H37Rv.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000516 Genomic DNA. Translation: AAK44358.1.
AL123456 Genomic DNA. Translation: CCP42851.1.
PIRG70983.
RefSeqNP_214640.1. NC_000962.3.
NP_334544.1. NC_002755.2.
YP_006513445.1. NC_018143.2.

3D structure databases

ProteinModelPortalO07176.
SMRO07176. Positions 12-586.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING83332.Rv0126.

Protein family/group databases

CAZyGH13. Glycoside Hydrolase Family 13.

Proteomic databases

PRIDEO07176.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK44358; AAK44358; MT0134.
CCP42851; CCP42851; Rv0126.
GeneID13316109.
886881.
922997.
KEGGmtc:MT0134.
mtu:Rv0126.
mtv:RVBD_0126.
PATRIC18122020. VBIMycTub22151_0145.

Organism-specific databases

TubercuListRv0126.

Phylogenomic databases

HOGENOMHOG000220639.
KOK05343.
OMARMKANIG.
OrthoDBEOG6RVFV2.
ProtClustDBCLSK871760.

Enzyme and pathway databases

BioCycMTBCDC:MT0134-MONOMER.
MTBRV:RV0126-MONOMER.
ReactomeREACT_27295. Mycobacterium tuberculosis biological processes.
UniPathwayUPA00164.

Family and domain databases

Gene3D2.60.40.1180. 1 hit.
3.20.20.80. 3 hits.
InterProIPR022567. DUF3459.
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]
PANTHERPTHR10357. PTHR10357. 1 hit.
PfamPF00128. Alpha-amylase. 1 hit.
PF11941. DUF3459. 1 hit.
[Graphical view]
SMARTSM00642. Aamy. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
TIGRFAMsTIGR02456. treS_nterm. 1 hit.
ProtoNetSearch...

Entry information

Entry nameTRES_MYCTU
AccessionPrimary (citable) accession number: O07176
Secondary accession number(s): L0T5R2, Q7DAF7
Entry history
Integrated into UniProtKB/Swiss-Prot: September 21, 2011
Last sequence update: July 1, 1997
Last modified: March 19, 2014
This is version 102 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh

Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries