Q10769 (TREZ_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Malto-oligosyltrehalose trehalohydrolase
Short name=MTHase
EC=3.2.1.141

Alternative name(s):
4-alpha-D-((1->4)-alpha-D-glucano)trehalose trehalohydrolase
Maltooligosyl trehalose trehalohydrolase

Gene names

Name:	treZ
Ordered Locus Names:	Rv1562c, MT1613
ORF Names:	MTCY48.03

Organism

Mycobacterium tuberculosis

Taxonomic identifier

1773 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length	580 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Is involved in the biosynthesis of trehalose but not in that of capsular glucan and glycogen. Ref.3
Catalytic activity	Hydrolysis of (1->4)-alpha-D-glucosidic linkage in 4-alpha-D-((1->4)-alpha-D-glucanosyl)(n) trehalose to yield trehalose and (1->4)-alpha-D-glucan.
Pathway	Glycan biosynthesis; trehalose biosynthesis.
Subcellular location	Cytoplasm By similarity.
Disruption phenotype	Inactivation of treZ does not affect the production of both capsular alpha-D-glucan and glycogen. Cells lacking this gene are not affected in their multiplication or persistence in the BALB/c mouse infection model. Ref.4
Sequence similarities	Belongs to the glycosyl hydrolase 13 family.
Sequence caution	The sequence AAK45880.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Carbohydrate metabolism
Cellular component	Cytoplasm
Molecular function	Glycosidase Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	alpha-glucan catabolic process Inferred from direct assay Ref.3. Source: MTBBASE trehalose biosynthetic process Inferred from direct assay Ref.3. Source: MTBBASE
Cellular component	cytosol Traceable author statement. Source: Reactome
Molecular function	4-alpha-D-{(1->4)-alpha-D-glucano}trehalose trehalohydrolase activity Inferred from direct assay Ref.3. Source: MTBBASE cation binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 580	580	Malto-oligosyltrehalose trehalohydrolase		PRO_0000054324
Regions
	Region	309 – 313	5	Substrate binding By similarity
Sites
	Active site	247	1	Nucleophile By similarity
	Active site	284	1	Proton donor By similarity
	Site	380	1	Transition state stabilizer By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q10769 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 506190468F44B862	FASTA	580	64,077
	10 20 30 40 50 60 MPEFRVWAPK PALVRLDVNG AVHAMTRSAD GWWHTTVAAP ADARYGYLLD DDPTVLPDPR 70 80 90 100 110 120 SARQPDGVHA RSQRWEPPGQ FGAARTDTGW PGRSVEGAVI YELHIGTFTT AGTFDAAIEK 130 140 150 160 170 180 LDYLVDLGID FVELMPVNSF AGTRGWGYDG VLWYSVHEPY GGPDGLVRFI DACHARRLGV 190 200 210 220 230 240 LIDAVFNHLG PSGNYLPRFG PYLSSASNPW GDGINIAGAD SDEVRHYIID CALRWMRDFH 250 260 270 280 290 300 ADGLRLDAVH ALVDTTAVHV LEELANATRW LSGQLGRPLS LIAETDRNDP RLITRPSHGG 310 320 330 340 350 360 YGITAQWNDD IHHAIHTAVS GERQGYYADF GSLATLAYTL RNGYFHAGTY SSFRRRRHGR 370 380 390 400 410 420 ALDTSAIPAT RLLAYTCTHD QVGNRALGDR PSQYLTGGQL AIKAALTLGS PYTAMLFMGE 430 440 450 460 470 480 EWGASSPFQF FCSHPEPELA HSTVAGRKEE FAEHGWAADD IPDPQDPQTF QRCKLNWAEA 490 500 510 520 530 540 GSGEHARLHR FYRDLIALRH NEADLADPWL DHLMVDYDEQ QRWVVMRRGQ LMIACNLGAE 550 560 570 580 PTCVPVSGEL VLAWESPIIG DNSTELAAYS LAILRAAEPA

References

	« Hide 'large scale' referencesShow '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. , 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: 9634230] [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. , 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: 12218036] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CDC 1551 / Oshkosh.
[3]	"Three pathways for trehalose biosynthesis in mycobacteria." De Smet K.A., Weston A., Brown I.N., Young D.B., Robertson B.D. Microbiology 146:199-208(2000) [PubMed: 10658666] [Abstract] Cited for: FUNCTION IN TREHALOSE BIOSYNTHESIS.
[4]	"Capsular glucan and intracellular glycogen of Mycobacterium tuberculosis: biosynthesis and impact on the persistence in mice." Sambou T., Dinadayala P., Stadthagen G., Barilone N., Bordat Y., Constant P., Levillain F., Neyrolles O., Gicquel B., Lemassu A., Daffe M., Jackson M. Mol. Microbiol. 70:762-774(2008) [PubMed: 18808383] [Abstract] Cited for: DISRUPTION PHENOTYPE. Strain: ATCC 25618 / H37Rv.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX842577 Genomic DNA. Translation: CAE55403.1. AE000516 Genomic DNA. Translation: AAK45880.1. Different initiation.
PIR	G70763.
RefSeq	NP_336066.1. NC_002755.2. YP_177819.1. NC_000962.2.
3D structure databases
ProteinModelPortal	Q10769.
ModBase	Search...
Protein family/group databases
CAZy	CBM48. Carbohydrate-Binding Module Family 48. GH13. Glycoside Hydrolase Family 13.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBMYCT00000002030; EBMYCP00000002030; EBMYCG00000002028. EBMYCT00000072604; EBMYCP00000070663; EBMYCG00000072599.
GeneID	886355. 924321.
GenomeReviews	Gene locus MT1613 in contig AE000516_GR. Gene locus Rv1562c in contig AL123456_GR.
KEGG	mtc:MT1613. mtu:Rv1562c.
PATRIC	18125314. VBIMycTub22151_1771.
TIGR	MT1613.
Organism-specific databases
TubercuList	Rv1562c.
Phylogenomic databases
GeneTree	EBGT00050000016657.
HOGENOM	HBG367595.
OMA	EGFVYQG.
PhylomeDB	Q10769.
ProtClustDB	CLSK799816.
Enzyme and pathway databases
Reactome	REACT_27295. Mycobacterium tuberculosis biological processes.
Family and domain databases
InterPro	IPR015902. Alpha_amylase. IPR006047. Glyco_hydro_13_cat_dom. IPR013781. Glyco_hydro_subgr_catalytic. IPR017853. Glycoside_hydrolase_SF. IPR013783. Ig-like_fold. IPR014756. Ig_E-set. IPR022567. Maltooligo_trehalose_bac_C. IPR012768. Trehalose_TreZ. [Graphical view]
Gene3D	G3DSA:3.20.20.80. Glyco_hydro_cat. 2 hits. G3DSA:2.60.40.10. Ig-like_fold. 1 hit.
KO	K01236.
PANTHER	PTHR10357. Alpha_amylase. 1 hit. PTHR10357:SF21. PTHR10357:SF21. 1 hit.
Pfam	PF00128. Alpha-amylase. 1 hit. PF11941. DUF3459. 1 hit. [Graphical view]
PIRSF	PIRSF006337. Trehalose_TreZ. 1 hit.
SUPFAM	SSF51445. Glyco_hydro_cat. 1 hit. SSF81296. Ig_E-set. 1 hit.
TIGRFAMs	TIGR02402. Trehalose_TreZ. 1 hit.
ProtoNet	Search...

Entry information

Entry name

TREZ_MYCTU

Accession

Primary (citable) accession number: Q10769

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	January 25, 2012
This is version 92 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program