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Database: UniProt
Entry: F8Q0S5_SERL3
LinkDB: F8Q0S5_SERL3
Original site: F8Q0S5_SERL3 
ID   F8Q0S5_SERL3            Unreviewed;       750 AA.
AC   F8Q0S5;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 33.
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   ORFNames=SERLA73DRAFT_182692 {ECO:0000313|EMBL:EGN97904.1};
OS   Serpula lacrymans var. lacrymans (strain S7.3) (Dry rot fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Boletales; Coniophorineae; Serpulaceae; Serpula.
OX   NCBI_TaxID=936435 {ECO:0000313|Proteomes:UP000008063};
RN   [1] {ECO:0000313|Proteomes:UP000008063}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=strain S7.3 {ECO:0000313|Proteomes:UP000008063};
RX   PubMed=21764756; DOI=10.1126/science.1205411;
RA   Eastwood D.C., Floudas D., Binder M., Majcherczyk A., Schneider P.,
RA   Aerts A., Asiegbu F.O., Baker S.E., Barry K., Bendiksby M., Blumentritt M.,
RA   Coutinho P.M., Cullen D., de Vries R.P., Gathman A., Goodell B.,
RA   Henrissat B., Ihrmark K., Kauserud H., Kohler A., LaButti K., Lapidus A.,
RA   Lavin J.L., Lee Y.-H., Lindquist E., Lilly W., Lucas S., Morin E.,
RA   Murat C., Oguiza J.A., Park J., Pisabarro A.G., Riley R., Rosling A.,
RA   Salamov A., Schmidt O., Schmutz J., Skrede I., Stenlid J., Wiebenga A.,
RA   Xie X., Kuees U., Hibbett D.S., Hoffmeister D., Hoegberg N., Martin F.,
RA   Grigoriev I.V., Watkinson S.C.;
RT   "The plant cell wall-decomposing machinery underlies the functional
RT   diversity of forest fungi.";
RL   Science 333:762-765(2011).
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; GL945481; EGN97904.1; -; Genomic_DNA.
DR   AlphaFoldDB; F8Q0S5; -.
DR   STRING; 936435.F8Q0S5; -.
DR   eggNOG; KOG0602; Eukaryota.
DR   HOGENOM; CLU_006451_4_0_1; -.
DR   InParanoid; F8Q0S5; -.
DR   OMA; NRYWDAS; -.
DR   OrthoDB; 1329212at2759; -.
DR   Proteomes; UP000008063; Unassembled WGS sequence.
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; 2.
DR   PRINTS; PR00744; GLHYDRLASE37.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR   PROSITE; PS00927; TREHALASE_1; 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:UP000008063};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..750
FT                   /note="Trehalase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003382493"
SQ   SEQUENCE   750 AA;  81220 MW;  F2E4C65BAA17517F CRC64;
     MLTKRLHLAA LAGLAHWHGV LAAPSGTATA PFTVQTGVPT LTFSTSVPSP SASLGATLPS
     QVALPPSQWW CIGQIFCAGS LLQTVNVAQL YPDPKTFVDK PTKKSSQQVL SDFGAFNVST
     VTEGDLVNFV DNDFSGEGLE LEGIALQGFN ANPPFLNNVS DPLLRSFAQI VNSYWTQLAR
     STNYSSTCDD YPGGQCEGSF IPLNHSFVIP GGRFREQYYW DSYWIIQGLI QSQLYESING
     TLQNFMDEIE TFGFIPNGGR IYYLNRSQPP LFIHMLYDYV TATNDSSILE RALPLAEVEL
     TWWQNNRTSE VTSPFTGQTY AMARYAVTNT APRPESYLTD YLTANDPTLT TPLTEEQRAD
     LYGELASGAE TGWDYTARFE SIPALGNPGL RSLNVSNNIP VCLNSILYKA HILLADLYGS
     SNASAAATHL QVAAGIRAGI LDLFWNSTKL AFYDFNLTSN ARNDIFTAAT FYPLWNGIIP
     DEVLSSQENA FGFFASLNMV FNRYNGTFPT TFIDYTGLQW DAPNTWPPHQ YIALQALRAL
     PSNLTSNPLP TPPSNESAYS LVPVGQLALT EAQLPGQPLR GPQANQNVTQ TGPGADLNAL
     NGTVVNGGNA TAGEGWNHVL QRELANRFFT SALCSWHATG GSIPGYLPQL SPAELNVTNS
     IGNTGNMFEK FSNLNVDSSG FGGEYTVQAG FGWTNGAVLW VAATYGDLLV APECPPLLYT
     STNAATGLRS SSAAVLLAVV VSLLFHSLLS
//
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