ID D8QIA1_SCHCM Unreviewed; 718 AA.
AC D8QIA1;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 44.
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=SCHCODRAFT_61255 {ECO:0000313|EMBL:EFI92193.1};
OS Schizophyllum commune (strain H4-8 / FGSC 9210) (Split gill fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Schizophyllaceae; Schizophyllum.
OX NCBI_TaxID=578458 {ECO:0000313|Proteomes:UP000007431};
RN [1] {ECO:0000313|EMBL:EFI92193.1, ECO:0000313|Proteomes:UP000007431}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H4-8 / FGSC 9210 {ECO:0000313|Proteomes:UP000007431};
RX PubMed=20622885; DOI=10.1038/nbt.1643;
RA Ohm R.A., de Jong J.F., Lugones L.G., Aerts A., Kothe E., Stajich J.E.,
RA de Vries R.P., Record E., Levasseur A., Baker S.E., Bartholomew K.A.,
RA Coutinho P.M., Erdmann S., Fowler T.J., Gathman A.C., Lombard V.,
RA Henrissat B., Knabe N., Kuees U., Lilly W.W., Lindquist E., Lucas S.,
RA Magnuson J.K., Piumi F., Raudaskoski M., Salamov A., Schmutz J.,
RA Schwarze F.W.M.R., vanKuyk P.A., Horton J.S., Grigoriev I.V.,
RA Woesten H.A.B.;
RT "Genome sequence of the model mushroom Schizophyllum commune.";
RL Nat. Biotechnol. 28:957-963(2010).
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; GL377313; EFI92193.1; -; Genomic_DNA.
DR RefSeq; XP_003027096.1; XM_003027050.1.
DR AlphaFoldDB; D8QIA1; -.
DR STRING; 578458.D8QIA1; -.
DR GeneID; 9593586; -.
DR KEGG; scm:SCHCO_02642810; -.
DR VEuPathDB; FungiDB:SCHCODRAFT_02642810; -.
DR eggNOG; KOG0602; Eukaryota.
DR HOGENOM; CLU_006451_1_3_1; -.
DR InParanoid; D8QIA1; -.
DR OMA; WLFMMTK; -.
DR OrthoDB; 1329212at2759; -.
DR Proteomes; UP000007431; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0004555; F:alpha,alpha-trehalase activity; IEA:UniProtKB-EC.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005993; P:trehalose catabolic 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 InterPro; IPR011120; Trehalase_Ca-bd.
DR PANTHER; PTHR23403:SF6; CYTOSOLIC NEUTRAL TREHALASE-RELATED; 1.
DR PANTHER; PTHR23403; TREHALASE; 1.
DR Pfam; PF01204; Trehalase; 1.
DR Pfam; PF07492; Trehalase_Ca-bi; 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:UP000007431}.
FT DOMAIN 32..60
FT /note="Neutral trehalase Ca2+ binding"
FT /evidence="ECO:0000259|Pfam:PF07492"
SQ SEQUENCE 718 AA; 82685 MW; 0EF20BC6E4098D36 CRC64;
MFGDPTKSRR LSHDEKPSAP RRFLIDVEET IRVILEQEDT DGDFQISVTD AGPKLMPLGT
ATSNGFKTFD IRGTYMLSNL LQELALARDH NRKRIVLDEA RLTENPVDRL SRMIKNSFWH
SLTRRIDGEG LEIITADPKN RTGRMNPRIY VPYGEPEMAE YYRKVAREKP HMRLDVQVLP
PKPDDPAFVK SLNDKPGLLA LAMQEVLDAK GEKTLKGIPF IVPGARFNEL YNWDSYFISL
GLLVDGHVQM AKNMVDHFIF EIKHYNKILN GSRSYYLCRA QPPFLTDMAL QIYNQLDRTD
EDANRDWLKR AIQAAIKEYH TVWMSAPRID PKTGLTRYRP EGLGIPPETE ASHFTHILEP
YANKHGISIL EFTEKYNDGV LKEPELDEYF QHDRGVRESG HDTTYRLEKR CANLATIDLQ
ALLYKYEIDI GTAIREVFDD ELELEEDFAL SPFPPTEESY ANPKRESSKS RLQNSEEWFQ
RAEFRKAQID KYLWNESKSL YFDYDTVTEQ QSLYETVTAF WALWAGCASE EQGWKLVSNS
LKKFEVLGGV VPGTEESRGQ ISLDRPNRQW DYPYAWPPHQ IMAWVGLERY GYLEDAQRLA
YRFLYMMTTA FVDFNGVVPE KFDAVKLSHL VDAEYGNQGI DFKLVPREGF GWMNAAFQVG
LSFMTTHMRR AVAACTSPEV FFRQPNTDAN TLAGHAQPSN DPLAMAMDQL RLPHEDGN
//