TREZ_ARTRM
ID TREZ_ARTRM Reviewed; 575 AA.
AC Q9AJN6;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 101.
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 ramosus.
OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Arthrobacter.
OX NCBI_TaxID=1672;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=S34;
RX PubMed=11471747; DOI=10.1271/bbb.65.1419;
RA Yamamoto T., Maruta K., Watanabe H., Yamashita H., Kubota M., Fukuda S.,
RA Kurimoto M.;
RT "Trehalose-producing operon treYZ from Arthrobacter ramosus S34.";
RL Biosci. Biotechnol. Biochem. 65:1419-1423(2001).
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; AB045141; BAB40766.1; -; Genomic_DNA.
DR PIR; JC7727; JC7727.
DR AlphaFoldDB; Q9AJN6; -.
DR SMR; Q9AJN6; -.
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; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR004193; Glyco_hydro_13_N.
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; PF02922; CBM_48; 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..575
FT /note="Malto-oligosyltrehalose trehalohydrolase"
FT /id="PRO_0000054322"
FT ACT_SITE 250
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q55088"
FT ACT_SITE 287
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q55088"
FT BINDING 248..253
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q55088"
FT BINDING 312..316
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q55088"
FT BINDING 381..386
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q55088"
FT SITE 382
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:Q55088"
SQ SEQUENCE 575 AA; 63080 MW; 284A3F20207E228B CRC64;
MNRRFPVWAP QAAQVTLVVG QGRAELPLTR DENGWWALQQ PWDGGPDLVD YGYLVDGKGP
FADPRSLRQP RGVHELGREF DPARYAWGDD GWRGRDLTGA VIYELHVGTF TPEGTLDSAI
RRLDHLVRLG VDAVELLPVN AFNGTHGWGY DGVLWYAVHE PYGGPEAYQR FVDACHARGL
AVVQDVVYNH LGPSGNHLPD FGPYLGSGAA NTWGDALNLD GPLSDEVRRY IIDNAVYWLR
DMHADGLRLD AVHALRDARA LHLLEELAAR VDELAGELGR PLTLIAESDL NDPKLIRSRA
AHGYGLDAQW DDDVHHAVHA NVTGETVGYY ADFGGLGALV KVFQRGWFHD GTWSSFRERH
HGRPLDPDIP FRRLVAFAQD HDQVGNRAVG DRMSAQVGEG SLAAAAALVL LGPFTPMLFM
GEEWGARTPW QFFTSHPEPE LGEATARGRI AEFARMGWDP AVVPDPQDPA TFARSHLDWS
EPEREPHAGL LAFYTDLIAL RRELPVDAPA REVDADEARG VFAFSRGPLR VTVALRPGPV
GVPEHGGLVL AYGEVRAGAA GLHLDGPGAA IVRLE