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TREA_PIMHY
ID   TREA_PIMHY              Reviewed;         585 AA.
AC   Q8MMG9;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 55.
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;
GN   Name=tre1;
OS   Pimpla hypochondriaca (Parasitoid wasp).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Parasitoida;
OC   Ichneumonoidea; Ichneumonidae; Pimplinae; Pimplini; Pimpla.
OX   NCBI_TaxID=135724;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 33-38.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=12727301; DOI=10.1016/s1532-0456(03)00041-3;
RA   Parkinson N.M., Conyers C.M., Keen J.N., MacNicoll A.D., Smith I.,
RA   Weaver R.J.;
RT   "cDNAs encoding large venom proteins from the parasitoid wasp Pimpla
RT   hypochondriaca identified by random sequence analysis.";
RL   Comp. Biochem. Physiol. 134C:513-520(2003).
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.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 37 family. {ECO:0000305}.
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DR   EMBL; AJ459958; CAD31109.1; -; mRNA.
DR   AlphaFoldDB; Q8MMG9; -.
DR   SMR; Q8MMG9; -.
DR   CAZy; GH37; Glycoside Hydrolase Family 37.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Glycoprotein; Glycosidase; Hydrolase; Secreted;
KW   Signal.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000269|PubMed:12727301"
FT   CHAIN           33..585
FT                   /note="Trehalase"
FT                   /id="PRO_0000230800"
FT   ACT_SITE        338
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        535
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         184
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         191..192
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         228
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         237..239
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         302..304
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         336
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         550
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        207
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        348
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   585 AA;  66458 MW;  B991F2D9C94A2579 CRC64;
     MAKTTPMAKP SVGLLTLQVL VFCALTGSLA SAGSIGHVTP RSDLCDSEVY CQGELLKTIQ
     LGEVFKDGKT FVDHYQVNDP SVTVANFRKL MAETGGKPNK DQLTQYVKEN FAQENEVIDW
     SPPDWQENPE FLQRVQDPVF RKWAKDLNDV WKIISRKVAP SVAEHPERHS IISVDNGFIV
     PGGRFQEFYY WDSYWVMEGL LLTGMKNTSR GILENFLSMV TRFGFIPNGG RVYYLMRSQP
     PLLIPMVDLY LTHTGDMQFL RDNIGTLEKE LGYFLSQKTV DVTKNGKTYK MARYIVSSNG
     PRPESYREDY ELAKNINDEA EKRRFYEDLK AAAESGWDFS SRWYISENGT RGSLSNIATR
     NIIPVELNAF LQRNARMLAQ FHTTLGNPTK AKYYKDIATS YQQAIDDVLW SESEGVWLDF
     DLRNSQHRNY FFPTNVAPLY TQSFDSSKAQ IYGQRAAAYL TRNGILDYMG GTPASLFPTG
     EQWDLPNAWP PLQSIIVQAL RNSNEESAEK LAKELAIRWL RANHKGYSQS GQMFEKYDAL
     NPGKFGGGGE YVVQEGFGWT NGVVYEFLNS YPNATPDDNV HMNNN
 
 
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