ID   TREZ_MYCTO              Reviewed;         580 AA.
AC   P9WQ22; 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=MT1613;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: Is involved in the biosynthesis of trehalose but not in that
CC       of capsular glucan and glycogen. {ECO:0000250|UniProtKB:P9WQ23}.
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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK45880.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE000516; AAK45880.1; ALT_INIT; Genomic_DNA.
DR   PIR; G70763; G70763.
DR   RefSeq; WP_003407788.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WQ22; -.
DR   SMR; P9WQ22; -.
DR   CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   EnsemblBacteria; AAK45880; AAK45880; MT1613.
DR   KEGG; mtc:MT1613; -.
DR   PATRIC; fig|83331.31.peg.1735; -.
DR   HOGENOM; CLU_020726_2_0_11; -.
DR   UniPathway; UPA00299; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0033942; F:4-alpha-D-(1->4)-alpha-D-glucanotrehalose trehalohydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005992; P:trehalose biosynthetic process; IEA:UniProtKB-UniPathway.
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   3: Inferred from homology;
KW   Carbohydrate metabolism; Cytoplasm; Glycosidase; Hydrolase.
FT   CHAIN           1..580
FT                   /note="Malto-oligosyltrehalose trehalohydrolase"
FT                   /id="PRO_0000426851"
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