ID   TREA_TENMO              Reviewed;         555 AA.
AC   P32359;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Trehalase;
DE            EC=3.2.1.28;
DE   AltName: Full=Alpha,alpha-trehalase;
DE   AltName: Full=Alpha,alpha-trehalose glucohydrolase;
DE   Flags: Precursor;
OS   Tenebrio molitor (Yellow mealworm beetle).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC   Tenebrionidae; Tenebrio.
OX   NCBI_TaxID=7067;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Male accessory gland;
RX   PubMed=1445264; DOI=10.1042/bj2880019;
RA   Takiguchi M., Niimi T., Su Z.-H., Yaginuma T.;
RT   "Trehalase from male accessory gland of an insect, Tenebrio molitor. cDNA
RT   sequencing and developmental profile of the gene expression.";
RL   Biochem. J. 288:19-22(1992).
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   -!- SUBCELLULAR LOCATION: Secreted. Note=It is incorporated into the wall
CC       of the spermatophore.
CC   -!- TISSUE SPECIFICITY: Bean-shaped accessory glands (bags).
CC   -!- INDUCTION: It is increased from 1 to 2 days after adult ecdysis, but
CC       decreased after 4 days. It is dependent on ecdysteroid hormone during
CC       pupal stage.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 37 family. {ECO:0000305}.
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DR   EMBL; D11338; BAA01951.1; -; mRNA.
DR   PIR; S27163; S27163.
DR   AlphaFoldDB; P32359; -.
DR   SMR; P32359; -.
DR   CAZy; GH37; Glycoside Hydrolase Family 37.
DR   BRENDA; 3.2.1.28; 6230.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; PTHR23403; 1.
DR   Pfam; PF01204; Trehalase; 1.
DR   PRINTS; PR00744; GLHYDRLASE37.
DR   SUPFAM; SSF48208; SSF48208; 1.
DR   PROSITE; PS00927; TREHALASE_1; 1.
DR   PROSITE; PS00928; TREHALASE_2; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Glycosidase; Hydrolase; Secreted; Signal.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..555
FT                   /note="Trehalase"
FT                   /id="PRO_0000012059"
FT   ACT_SITE        318
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        516
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         164
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         171..172
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         208
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         217..219
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         282..284
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         316
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         531
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        46
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        216
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        334
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        371
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   555 AA;  64464 MW;  E7B7C9117A4F074A CRC64;
     MIPFLLMVAF ADTVLQVSAQ SQPSCDSKVY CQGKLLHVVE MSRIFNDSKT FVELKMINDE
     QTTLENFDNF LRDTNHKRTR ADLMKFVSDN FKQENEFESW TPTDFTDNPT LLSRIEDKTI
     RQFAQDLVKI WPTLARKVKK EVLDYPEHYS LLPVDNGFII PGGRFTEFYY WDSYWIVEGL
     LLSDMHETVR GMLDNFLSIV EKYGFIPNGA RVFYLNRSQP PLLTLMVSLY VSATNDMEWL
     AKNIRTIDTE LRFWLNNRLV DVVKDGIVYK LAQYNSNSGS PRPESYYEDV TTASVFSDER
     DKAELYMDLK SAAESGWDFS SRWIVDEYGG TRGNLSALHT RRIIPVDLNA FLCQAFQKLS
     EFYQTLGDYP NATFWSKLVK IWQHSIEMVH YNRDDGIWYD WDNELSQHRR MFFPSNFAPL
     WSETFDSRNA EILGEMAAEY FITQNMMDYH GGIPTSLSHT GEQWDYPNAW PPMQSIIVMG
     LDKSGSYRAK QLARELARRW VKANLIGFRQ TGEMFEKYNV EVPGQNGGGG EYVVQSGFGW
     TNGVVLEFIN QFFTT