TREZ_MYCTU
ID TREZ_MYCTU Reviewed; 580 AA.
AC P9WQ23; L0T712; Q10769;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 47.
DE RecName: Full=Malto-oligosyltrehalose trehalohydrolase;
DE Short=MTHase;
DE EC=3.2.1.141 {ECO:0000250|UniProtKB:Q55088};
DE AltName: Full=4-alpha-D-((1->4)-alpha-D-glucano)trehalose trehalohydrolase;
DE AltName: Full=Maltooligosyl trehalose trehalohydrolase;
GN Name=treZ; OrderedLocusNames=Rv1562c; ORFNames=MTCY48.03;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP FUNCTION IN TREHALOSE BIOSYNTHESIS.
RX PubMed=10658666; DOI=10.1099/00221287-146-1-199;
RA De Smet K.A., Weston A., Brown I.N., Young D.B., Robertson B.D.;
RT "Three pathways for trehalose biosynthesis in mycobacteria.";
RL Microbiology 146:199-208(2000).
RN [3]
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=18808383; DOI=10.1111/j.1365-2958.2008.06445.x;
RA Sambou T., Dinadayala P., Stadthagen G., Barilone N., Bordat Y.,
RA Constant P., Levillain F., Neyrolles O., Gicquel B., Lemassu A., Daffe M.,
RA Jackson M.;
RT "Capsular glucan and intracellular glycogen of Mycobacterium tuberculosis:
RT biosynthesis and impact on the persistence in mice.";
RL Mol. Microbiol. 70:762-774(2008).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC -!- FUNCTION: Is involved in the biosynthesis of trehalose but not in that
CC of capsular glucan and glycogen. {ECO:0000269|PubMed:10658666}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hydrolysis of (1->4)-alpha-D-glucosidic linkage in 4-alpha-D-
CC [(1->4)-alpha-D-glucanosyl]n trehalose to yield trehalose and (1->4)-
CC alpha-D-glucan.; EC=3.2.1.141;
CC Evidence={ECO:0000250|UniProtKB:Q55088};
CC -!- PATHWAY: Glycan biosynthesis; trehalose biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Inactivation of treZ does not affect the
CC production of both capsular alpha-D-glucan and glycogen. Cells lacking
CC this gene are not affected in their multiplication or persistence in
CC the BALB/c mouse infection model. {ECO:0000269|PubMed:18808383}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR EMBL; AL123456; CCP44326.1; -; Genomic_DNA.
DR PIR; G70763; G70763.
DR RefSeq; WP_003407788.1; NZ_NVQJ01000004.1.
DR RefSeq; YP_177819.1; NC_000962.3.
DR AlphaFoldDB; P9WQ23; -.
DR SMR; P9WQ23; -.
DR STRING; 83332.Rv1562c; -.
DR PaxDb; P9WQ23; -.
DR DNASU; 886355; -.
DR GeneID; 886355; -.
DR KEGG; mtu:Rv1562c; -.
DR TubercuList; Rv1562c; -.
DR eggNOG; COG0296; Bacteria.
DR OMA; FTPMLFM; -.
DR PhylomeDB; P9WQ23; -.
DR Reactome; R-MTU-868688; Trehalose biosynthesis.
DR UniPathway; UPA00299; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0033942; F:4-alpha-D-(1->4)-alpha-D-glucanotrehalose trehalohydrolase activity; IDA:MTBBASE.
DR GO; GO:0030980; P:alpha-glucan catabolic process; IDA:MTBBASE.
DR GO; GO:0005992; P:trehalose biosynthetic process; IDA:MTBBASE.
DR Gene3D; 1.10.10.760; -; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR022567; DUF3459.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR012768; Trehalose_TreZ.
DR InterPro; IPR044901; Trehalose_TreZ_E-set_sf.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF11941; DUF3459; 1.
DR PIRSF; PIRSF006337; Trehalose_TreZ; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR TIGRFAMs; TIGR02402; trehalose_TreZ; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cytoplasm; Glycosidase; Hydrolase;
KW Reference proteome.
FT CHAIN 1..580
FT /note="Malto-oligosyltrehalose trehalohydrolase"
FT /id="PRO_0000054324"
FT REGION 56..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 247
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q55088"
FT ACT_SITE 284
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q55088"
FT BINDING 245..250
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q55088"
FT BINDING 309..313
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q55088"
FT BINDING 379..384
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q55088"
FT SITE 380
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:Q55088"
SQ SEQUENCE 580 AA; 64077 MW; 506190468F44B862 CRC64;
MPEFRVWAPK PALVRLDVNG AVHAMTRSAD GWWHTTVAAP ADARYGYLLD DDPTVLPDPR
SARQPDGVHA RSQRWEPPGQ FGAARTDTGW PGRSVEGAVI YELHIGTFTT AGTFDAAIEK
LDYLVDLGID FVELMPVNSF AGTRGWGYDG VLWYSVHEPY GGPDGLVRFI DACHARRLGV
LIDAVFNHLG PSGNYLPRFG PYLSSASNPW GDGINIAGAD SDEVRHYIID CALRWMRDFH
ADGLRLDAVH ALVDTTAVHV LEELANATRW LSGQLGRPLS LIAETDRNDP RLITRPSHGG
YGITAQWNDD IHHAIHTAVS GERQGYYADF GSLATLAYTL RNGYFHAGTY SSFRRRRHGR
ALDTSAIPAT RLLAYTCTHD QVGNRALGDR PSQYLTGGQL AIKAALTLGS PYTAMLFMGE
EWGASSPFQF FCSHPEPELA HSTVAGRKEE FAEHGWAADD IPDPQDPQTF QRCKLNWAEA
GSGEHARLHR FYRDLIALRH NEADLADPWL DHLMVDYDEQ QRWVVMRRGQ LMIACNLGAE
PTCVPVSGEL VLAWESPIIG DNSTELAAYS LAILRAAEPA
