ID   TREZ_BREHE              Reviewed;         589 AA.
AC   O52520;
DT   29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 109.
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;
OS   Brevibacterium helvolum.
OC   Bacteria; Actinobacteria; Micrococcales; Brevibacteriaceae; Brevibacterium.
OX   NCBI_TaxID=1704;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 11822 / CA3 / IAM 1637;
RX   PubMed=11055902; DOI=10.1128/aem.66.11.4620-4624.2000;
RA   Kim Y.H., Kwon T.K., Park S., Seo H.S., Cheong J.J., Kim C.H., Kim J.K.,
RA   Lee J.S., Choi Y.D.;
RT   "Trehalose synthesis by sequential reactions of recombinant
RT   maltooligosyltrehalose synthase and maltooligosyltrehalose trehalohydrolase
RT   from Brevibacterium helvolum.";
RL   Appl. Environ. Microbiol. 66:4620-4624(2000).
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}.
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DR   EMBL; AF039919; AAB95369.1; -; Genomic_DNA.
DR   AlphaFoldDB; O52520; -.
DR   SMR; O52520; -.
DR   CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   BRENDA; 3.2.1.141; 964.
DR   UniPathway; UPA00299; -.
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..589
FT                   /note="Malto-oligosyltrehalose trehalohydrolase"
FT                   /id="PRO_0000054323"
FT   ACT_SITE        258
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q55088"
FT   ACT_SITE        295
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q55088"
FT   BINDING         256..261
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q55088"
FT   BINDING         320..324
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q55088"
FT   BINDING         390..395
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q55088"
FT   SITE            391
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:Q55088"
SQ   SEQUENCE   589 AA;  64217 MW;  C282314B6E9BA029 CRC64;
     MTLVNVGPER FDVWAPDVSS VVLVADGRQY PMQKKETAPG SEGWWTASDA PPNGDVDYGY
     LLDGNTTPVP EPRSRRLPAG VHNHSRTYNP PPYRWQDSRW RGKELQGTLI YQLHVGTSTP
     DGTLDAAGEK LSYLVDLGID FIELLPVNGF NGTHNWGYDG VQWYTVHEGY GGPAAYQRFV
     DAAHAAGLGV IQDVVYNHLG LRGNYFPKLG PNLKQGDANT LGDSVNLDGA GSDVFREYIL
     DNAALWVGDY HVDGVGFDAV HAVRDERAVH ILEDLGALGD AISGETGLPK TLIAESDFNN
     PRLIYPRDVN GYGLAGQWSD DFHTAVHVSV SGETTGYYSD FESLAVLAKV LKDGFLHDGS
     YSSFRGRHHG RPINPSLANP AALVVCNQNH DQIGNRATGD RLSQSLSYGQ LAVAAVLTLT
     SPFTPMLFMG EEYGASTPWQ FFTSHPEPEL GKATAEGRIK EFERMGWDPA VVPDPQDPET
     FNRSKLDWSE ASTGDHARLL ELYKSLTALR REHPDLADLG FGQTEVSFDD DAGWLRFRPV
     SVEVLVNLSD AKVRLDDAAG DLLLATDEGN PLDGGSLALV PWSAAVLKS