ID   O70282_RAT              Unreviewed;       557 AA.
AC   O70282;
DT   01-AUG-1998, integrated into UniProtKB/TrEMBL.
DT   01-AUG-1998, sequence version 1.
DT   27-MAR-2024, entry version 108.
DE   RecName: Full=Trehalase {ECO:0000256|ARBA:ARBA00019905, ECO:0000256|RuleBase:RU361180};
DE            EC=3.2.1.28 {ECO:0000256|ARBA:ARBA00012757, ECO:0000256|RuleBase:RU361180};
DE   AltName: Full=Alpha-trehalose glucohydrolase {ECO:0000256|RuleBase:RU361180};
DE   Flags: Fragment;
GN   Name=Treh {ECO:0000313|RGD:61831};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116 {ECO:0000313|EMBL:AAC25985.1};
RN   [1] {ECO:0000313|EMBL:AAC25985.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Sprague-Dawley {ECO:0000313|EMBL:AAC25985.1};
RC   TISSUE=Jejunum {ECO:0000313|EMBL:AAC25985.1};
RX   PubMed=9644033;
RA   Oesterreicher T.J., Nanthakumar N.N., Winston J.H., Henning S.J.;
RT   "Rat trehalase: cDNA cloning and mRNA expression in adult rat tissues and
RT   during intestinal ontogeny.";
RL   Am. J. Physiol. 274:R1220-R1227(1998).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha,alpha-trehalose + H2O = alpha-D-glucose + beta-D-
CC         glucose; Xref=Rhea:RHEA:32675, ChEBI:CHEBI:15377, ChEBI:CHEBI:15903,
CC         ChEBI:CHEBI:16551, ChEBI:CHEBI:17925; EC=3.2.1.28;
CC         Evidence={ECO:0000256|ARBA:ARBA00001576,
CC         ECO:0000256|RuleBase:RU361180};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 37 family.
CC       {ECO:0000256|ARBA:ARBA00005615, ECO:0000256|RuleBase:RU361180}.
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DR   EMBL; AF038043; AAC25985.1; -; mRNA.
DR   AlphaFoldDB; O70282; -.
DR   IntAct; O70282; 1.
DR   BindingDB; O70282; -.
DR   ChEMBL; CHEMBL3248; -.
DR   DrugCentral; O70282; -.
DR   CAZy; GH37; Glycoside Hydrolase Family 37.
DR   UCSC; RGD:61831; rat.
DR   RGD; 61831; Treh.
DR   PhylomeDB; O70282; -.
DR   BRENDA; 3.2.1.28; 5301.
DR   GO; GO:0004555; F:alpha,alpha-trehalase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005991; P:trehalose metabolic process; IEA:InterPro.
DR   Gene3D; 1.50.10.10; -; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR001661; Glyco_hydro_37.
DR   InterPro; IPR018232; Glyco_hydro_37_CS.
DR   PANTHER; PTHR23403; TREHALASE; 1.
DR   PANTHER; PTHR23403:SF1; TREHALASE; 1.
DR   Pfam; PF01204; Trehalase; 1.
DR   PRINTS; PR00744; GLHYDRLASE37.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR   PROSITE; PS00927; TREHALASE_1; 1.
DR   PROSITE; PS00928; TREHALASE_2; 1.
PE   2: Evidence at transcript level;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361180};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361180}.
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAC25985.1"
SQ   SEQUENCE   557 AA;  63489 MW;  D99B8CF400836C49 CRC64;
     ALSPLCESQI YCHGELLHQV QMAQLYQDDK QFVDMSLATS PDEVLQKFSE LAVAHNHSIP
     REELQNFVQS YFQPVGQELQ PWTPEDWKDS PQFLQKISDS RLRVWAEELH KIWKKLGKKM
     KAEVLSHPER SSLIYSEHPF IVPGGRFVEF YYWDSYWVME GLLLSEMAST VKGMLQNFLD
     LVKTYGHIPN GGRVYYLQRS HPPLLTLMME RYVAHTNDVA FLRENIGTLA LELEFWTVNR
     TVSVGSGGQS YILNRYYVPY GGPRPESYSK DEELAKTVPE GDRETLWAEL KAGAESGWDF
     SSRWLVGGPD PDLLSSIRTS KMVPADLNAF LCQAEELMSN FYSRLGNDTE AKRYRNLRAQ
     RLAAMEAILW DEQKGAWFDY DLEKGKKNLE FYPSNLTPLW AGCFSDPNVA DRALKYLEDN
     KILTYQYGIP TSLRNTGQQW DFPNAWAPLQ DLVIRGLAKS ASPRTQEVAF QLAQNRIKTN
     FKVYSQKSAM YEKYDISNGG HPGGGGEYEV QEGFGWTNGL ALMLLDRYGD QLTSGTQLAS
     LGPHCLVTAL LLSLLLQ
//