ID Q8SQJ2_ENCCU Unreviewed; 659 AA.
AC Q8SQJ2;
DT 01-JUN-2002, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 3.
DT 22-FEB-2023, entry version 94.
DE RecName: Full=Trehalase {ECO:0000256|RuleBase:RU361180};
DE EC=3.2.1.28 {ECO:0000256|RuleBase:RU361180};
DE AltName: Full=Alpha-trehalose glucohydrolase {ECO:0000256|RuleBase:RU361180};
GN OrderedLocusNames=ECU02_1370 {ECO:0000313|EMBL:CAD25166.3};
OS Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC Encephalitozoon.
OX NCBI_TaxID=284813 {ECO:0000313|EMBL:CAD25166.3, ECO:0000313|Proteomes:UP000000819};
RN [1] {ECO:0000313|EMBL:CAD25166.3, ECO:0000313|Proteomes:UP000000819}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-M1 {ECO:0000313|EMBL:CAD25166.3,
RC ECO:0000313|Proteomes:UP000000819};
RX PubMed=11719806; DOI=10.1038/35106579;
RA Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA Vivares C.P.;
RT "Genome sequence and gene compaction of the eukaryote parasite
RT Encephalitozoon cuniculi.";
RL Nature 414:450-453(2001).
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; AL590442; CAD25166.3; -; Genomic_DNA.
DR RefSeq; NP_584662.1; NM_001040851.1.
DR AlphaFoldDB; Q8SQJ2; -.
DR STRING; 284813.Q8SQJ2; -.
DR CAZy; GH37; Glycoside Hydrolase Family 37.
DR GeneID; 858652; -.
DR KEGG; ecu:ECU02_1370; -.
DR HOGENOM; CLU_006451_4_0_1; -.
DR InParanoid; Q8SQJ2; -.
DR OMA; DAPFGWA; -.
DR OrthoDB; 1329212at2759; -.
DR Proteomes; UP000000819; Chromosome II.
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; PS00928; TREHALASE_2; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361180};
KW Reference proteome {ECO:0000313|Proteomes:UP000000819};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..659
FT /note="Trehalase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010546989"
FT REGION 639..659
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 640..659
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 659 AA; 76692 MW; 7BFD686091CAA0C4 CRC64;
MNFTWWMRWT LVPLTIHAAK RPSKMPRMDT NPCVSRKLLE AAFENKITKD SKYLVDKLFL
KPPEEIDEML RSMESEGKFF RSEEDFWNFV GMHSIEPGSE FIFAKDNEEL EASMFSGVPE
YVSRLEERLL EPNPQRESEG FKQSLETLVR VSKELNDAWK NLYVKQRDLD KGYYSTMIKV
KNPFVIPGDR FKECYYWDTY WIIEGLVKSG MHKIAVGMVE NFILLIEKYG FIPNGTRTYY
LNRTQPPYFC MMLFTVYRHV PWTEEVEEII KRGLKAAVME YNFFMNYRKE EIEKDGKSYV
LNVYRVSDCT PRAESYSEDR KVAENNKSKD EVYRRREEDI YSNLKAGAES GWDYSSRWLG
VRGELDSIRT SKRVPADLNA IMYANELIIM KLFEVVEGKR SKNAEDFKKK SEERYRAINA
VLWSDEEGVW NDYDIEKKKH TSPGFYFSNL APMCYGISPP PDKNITVYDI LNAFAEEIFG
HPGGMPASGS KNKNSPEQWD YPNVWPPLVH IMTFFLERIG ERQMALHLAR SLLENISVST
SISDVTRRGI FEKYNCERVG DSGYKGEYAP QVGFGWTNGS AIHFLEHFSF ELASTKSHAV
SYQEIKDLME KKVASREVPR KHTPENCLLL EDKLWDIESH SEGPNSSSGR PHPVVPTTV
//