ID   TREZ_RHIS1              Reviewed;         596 AA.
AC   Q53238;
DT   29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 117.
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   Rhizobium sp. (strain M-11).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=269089;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8829547; DOI=10.1271/bbb.60.717;
RA   Maruta K., Hattori K., Nakada T., Kubota M., Sugimoto T., Kurimoto M.;
RT   "Cloning and sequencing of trehalose biosynthesis genes from Rhizobium sp.
RT   M-11.";
RL   Biosci. Biotechnol. Biochem. 60:717-720(1996).
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; D78001; BAA11187.1; -; Genomic_DNA.
DR   PIR; JC4697; JC4697.
DR   AlphaFoldDB; Q53238; -.
DR   SMR; Q53238; -.
DR   CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
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..596
FT                   /note="Malto-oligosyltrehalose trehalohydrolase"
FT                   /id="PRO_0000054325"
FT   ACT_SITE        265
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q55088"
FT   ACT_SITE        302
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q55088"
FT   BINDING         263..268
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q55088"
FT   BINDING         327..331
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q55088"
FT   BINDING         397..402
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q55088"
FT   SITE            398
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:Q55088"
SQ   SEQUENCE   596 AA;  65263 MW;  73EA80AE0534DDCD CRC64;
     MTQPNDAAKP VQGAGRFDIW APEAGTVTLL AGGERYEMGR RPGNGPADEG WWTAADAPTG
     ADVDYGYLLD GDEIPLPDPR TRRQPEGVHA LSRTFDPGAH RWQDAGWQGR ELQGSVIYEL
     HIGTFTPEGT LDAAAGKLDY LAGLGIDFIE LLPVNAFNGT HNWGYDGVQW FAVHEGYGGP
     AAYQRFVDAA HAAGLGVIQD VVYNHLGPSG NYLPRYGPYL KHGEGNTWGD SVNLDGPGSD
     HVRQYILDNV AMWLRDYRVD GLRLDAVHAL KDERAVHILE EFGALADALS SEGGRPLTLI
     AESDLNNPRL LYPRDVNGYG LAGQWSDDFH HAVHVNVSGE TTGYYSDFDS LGALAKVLRD
     GFFHDGSYSS FRGRCHGRPI NFSAVHPAAL VVCSQNHDQI GNRATGDRLS QSLPYGSLAL
     AAVLTLTGPF TPMLFMGEEY GATTPWQFFT SHPEPELGKA TAEGRIREFE RMGWDPAVVP
     DPQDPETFTR SKLDWAEASA GDHARLLELY RSLITLRRST PELARLGFAD TAVEFDDDAR
     WLRYWRGGVQ VVLNFADRPI SLDRPGTALL LATDDAVRMD GVQVELPPLS AAVLRD