ID   TREZ_ARTSQ              Reviewed;         598 AA.
AC   Q44316;
DT   29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 114.
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   Arthrobacter sp. (strain Q36).
OC   Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Arthrobacter.
OX   NCBI_TaxID=104027;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8605217; DOI=10.1016/0304-4165(95)00139-5;
RA   Maruta K., Hattori K., Nakada T., Kubota M., Sugimoto T., Kurimoto M.;
RT   "Cloning and sequencing of trehalose biosynthesis genes from Arthrobacter
RT   sp. Q36.";
RL   Biochim. Biophys. Acta 1289:10-13(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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; D63343; BAA09668.1; -; Genomic_DNA.
DR   PIR; S65770; S65770.
DR   AlphaFoldDB; Q44316; -.
DR   SMR; Q44316; -.
DR   CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   KEGG; ag:BAA09668; -.
DR   BioCyc; MetaCyc:MON-6022; -.
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..598
FT                   /note="Malto-oligosyltrehalose trehalohydrolase"
FT                   /id="PRO_0000054321"
FT   ACT_SITE        267
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q55088"
FT   ACT_SITE        304
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q55088"
FT   BINDING         265..270
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q55088"
FT   BINDING         329..333
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q55088"
FT   BINDING         399..404
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q55088"
FT   SITE            400
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:Q55088"
SQ   SEQUENCE   598 AA;  65832 MW;  8B5C610AD3766947 CRC64;
     MTHTYPREAA KPVLGPARYD VWAPNAESVT LLAGGERYAM QRRAETGPED AGWWTAAGAP
     TDGNVDYGYL LDGDETPLPD PRTRRQPDGV HALSRTFDPS AYSWQDDAWQ GRELQGAVIY
     ELHLGTFTPE GTLEAAAGKL DYLAGLGVDF IELLPVNAFN GTHNWGYDGV QWFAVHEAYG
     GPEAYQRFVD AAHAAGLGVI QDVVYNHLGP SGNYLPRFGP YLKQGEGNTW GDSVNLDGPG
     SDHVRRYILD NLAMWLRDYR VDGLRLDAVH ALKDERAVHI LEDFGALADQ ISAEVGRPLT
     LIAESDLNNP RLLYPRDVNG YGLEGQWSDD FHHAVHVNVT GETTGYYSDF DSLAALAKVL
     RDGFFHDGSY SSFRERHHGR PINFSAVHPA ALVVCSQNHD QIGNRATGDR LSQTLPYGSL
     ALAAVLTLTG PFTPMLLMGE EYGASTPWQF FTSHPEPELG KATAEGRIKE FERMGWDPAV
     VPDPQDPETF RRSKLDWAEA AEGDHARLLE LYRSLTALRR STPDLTKLGF EDTQVAFDED
     ARWLRFRRGG VQVLLNFSEQ PVSLDGAGTA LLLATDDAVR LEGERAELGP LSAAVVSD