ID   A0A094FTC2_9PEZI        Unreviewed;       830 AA.
AC   A0A094FTC2;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   22-FEB-2023, entry version 28.
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=V498_05218 {ECO:0000313|EMBL:KFY91953.1};
OS   Pseudogymnoascus sp. VKM F-4517 (FW-2822).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420911 {ECO:0000313|EMBL:KFY91953.1, ECO:0000313|Proteomes:UP000029270};
RN   [1] {ECO:0000313|EMBL:KFY91953.1, ECO:0000313|Proteomes:UP000029270}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4517 (FW-2822) {ECO:0000313|Proteomes:UP000029270};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KFY91953.1}.
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DR   EMBL; JPKA01001153; KFY91953.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094FTC2; -.
DR   HOGENOM; CLU_006451_1_3_1; -.
DR   Proteomes; UP000029270; 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; PS00927; TREHALASE_1; 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}.
FT   DOMAIN          96..125
FT                   /note="Neutral trehalase Ca2+ binding"
FT                   /evidence="ECO:0000259|Pfam:PF07492"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          765..793
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   830 AA;  94817 MW;  C312F5498E2AB75E CRC64;
     MSTTDGNKPK ESNGNGTPNE PRRISIEIDQ FAPAETYYGL KNTAHQNPRR QSTFSTNYAA
     SRVREDTLSE LPARRGSHDE STLGQLKFLI NVDSTLENLQ KQEDTDNNFQ ITIEDNGPKV
     ISLGTVTSNG FRRHDIRGTY MLSNLLQELS LAKEAGRHMI VLDESRLNEN PVSRLSRLIK
     DTFWDRLTRR IDGHVIEIAG KDPKDWTDDP RPRVYIPRGA PEQFEYYTQV AKDRPEVRLD
     VQWLPEKITP ESVRDMNAKP GLLALAMEEY RDPSTQKMTL RGVPFVVPGG RFNELYGWDS
     YMESLGLIVN GRVDLAKAMV TNFCFCIKHY GKILNANRSY YLCRSQPPFL TDMASRVYDK
     IQHEKGAREF LRLATLAAIK EYRSVWIAEP RLDSITGLSR YRPEGLGVPP ETEASHFIHI
     LEPYAKKHNL SFDAFVEAFN NRVILEPELD DYFMHDRAVR ESGHDTSYRL ERTCADLATI
     DLNSLLYKYE VDIARIIRVH FDDKLAVPAE FCTGNMVPGQ LETSALWDRA SRARKKAINK
     YLWNEEKGMF FDYNTVSQQQ QTYESATTFW AMWAGLATPK QGEQMVAQAI PILEAAGGLL
     SGTRHSRGEI GIERPNRQWD YPYGWAPQQM LAWTGLQRYG HQDVAERLAY KWLYMITKAF
     VDYNGVVVEK YDVTRPVDPH RVDAEYGNQG SDFKGVAKEG FGWVNASYVY GMQICNVHMR
     RALGTCTPYE TYRKMTEHGQ ISLRSRWTYG SRWLHYYSAN GSGGEWMGDG GEREESAQEQ
     AHPQSQAIDP ASPIQTSTME DRAAAFAFRG FRMLIVFVPA DSVATCIIYF
//