ID M5FYA3_DACPD Unreviewed; 683 AA.
AC M5FYA3;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
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=DACRYDRAFT_88103 {ECO:0000313|EMBL:EJU03036.1};
OS Dacryopinax primogenitus (strain DJM 731) (Brown rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC Dacrymycetales; Dacrymycetaceae; Dacryopinax.
OX NCBI_TaxID=1858805 {ECO:0000313|EMBL:EJU03036.1, ECO:0000313|Proteomes:UP000030653};
RN [1] {ECO:0000313|EMBL:EJU03036.1, ECO:0000313|Proteomes:UP000030653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DJM-731 SS1 {ECO:0000313|EMBL:EJU03036.1,
RC ECO:0000313|Proteomes:UP000030653};
RX PubMed=22745431; DOI=10.1126/science.1221748;
RA Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT 31 fungal genomes.";
RL Science 336:1715-1719(2012).
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; JH795860; EJU03036.1; -; Genomic_DNA.
DR AlphaFoldDB; M5FYA3; -.
DR STRING; 1858805.M5FYA3; -.
DR HOGENOM; CLU_006451_4_0_1; -.
DR OMA; NRYWDAS; -.
DR OrthoDB; 1329212at2759; -.
DR Proteomes; UP000030653; 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 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.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|RuleBase:RU361180};
KW Hydrolase {ECO:0000256|RuleBase:RU361180, ECO:0000313|EMBL:EJU03036.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030653};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..683
FT /note="Trehalase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004067421"
FT REGION 28..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..60
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 683 AA; 74595 MW; 936C34467C7C736A CRC64;
MALSSFRLSG ALALFVLAGH SLLVYAQPSG SGNTPSAAQP TSPPPPPEAP SPNHPPLSKA
YPPPDIFCPG ALLQTVDLAQ LYSDSKTFVD KPTVFSPNTT LADFARIGGA NATIGNLEAY
VEQDFSGEGL ELVPVQLENF TSTPGFLQGV RTRLSTNTSA LCDGLHCASS LIPLNNTFVI
PGGRFREQYY WDSFWILEGL LQSELYYVAR STLENFMDEL ERFGFIPNGG RIYYLNRSQP
PLFVHMVYTY LQTTNDSSIL TRALPLAEVE LAWWQTNRST TVLSPNTNTT HTVYQYRVTN
SAPRPESYLE DYQTANANAA GLQAPLSPEE AEELYAELAS GAETGWDYSS RWCKQPFLGN
LSENDPALRT LDVRGVVPVD LNSMLPNAHW MLARMYDAAR QENDGNVDVD GSGSGRKKWE
HERKGDDLRE AVLDLMWDEE RVAFYDWNLT AGERGTVFSS AHYYPFWNNI IPPSLLGNAT
RLRQAFGSLN LMLDMYNGSV PVTFLNTGLQ WDFPNATSMY LLWVDIILRA LQNLPGNLTF
LPLLTDSTPE LENAFALLPA NQTGLSSPSL LPLQPGTNIS LSTKVNVNAG QGWLALGLGT
NGTSGWKDAL MLEVAQRYID AAFCSWYSTG GSIPGSLAQL SPQDLSVTGS TPQSTGVMFE
KFNATDLDAA GGGGEYTVQA GLG
//
