ID   BGLM_NEOFI              Reviewed;         769 AA.
AC   A1D122;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   24-JAN-2024, entry version 77.
DE   RecName: Full=Probable beta-glucosidase M;
DE            EC=3.2.1.21;
DE   AltName: Full=Beta-D-glucoside glucohydrolase M;
DE   AltName: Full=Cellobiase M;
DE   AltName: Full=Gentiobiase M;
DE   Flags: Precursor;
GN   Name=bglM; ORFNames=NFIA_007920;
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 /
RC   NRRL 181 / WB 181;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
CC   -!- FUNCTION: Beta-glucosidases are one of a number of cellulolytic enzymes
CC       involved in the degradation of cellulosic biomass. Catalyzes the last
CC       step releasing glucose from the inhibitory cellobiose (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal, non-reducing beta-D-glucosyl residues
CC         with release of beta-D-glucose.; EC=3.2.1.21;
CC   -!- PATHWAY: Glycan metabolism; cellulose degradation.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; DS027688; EAW22115.1; -; Genomic_DNA.
DR   RefSeq; XP_001264012.1; XM_001264011.1.
DR   AlphaFoldDB; A1D122; -.
DR   SMR; A1D122; -.
DR   STRING; 331117.A1D122; -.
DR   GlyCosmos; A1D122; 7 sites, No reported glycans.
DR   EnsemblFungi; EAW22115; EAW22115; NFIA_007920.
DR   GeneID; 4592105; -.
DR   KEGG; nfi:NFIA_007920; -.
DR   VEuPathDB; FungiDB:NFIA_007920; -.
DR   eggNOG; ENOG502SMNU; Eukaryota.
DR   HOGENOM; CLU_004542_2_1_1; -.
DR   OMA; NFPGLCV; -.
DR   OrthoDB; 5486783at2759; -.
DR   UniPathway; UPA00696; -.
DR   Proteomes; UP000006702; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008422; F:beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.1700; Glycoside hydrolase family 3 C-terminal domain; 1.
DR   Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR026891; Fn3-like.
DR   InterPro; IPR002772; Glyco_hydro_3_C.
DR   InterPro; IPR036881; Glyco_hydro_3_C_sf.
DR   InterPro; IPR001764; Glyco_hydro_3_N.
DR   InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   PANTHER; PTHR42715; BETA-GLUCOSIDASE; 1.
DR   PANTHER; PTHR42715:SF5; BETA-GLUCOSIDASE M-RELATED; 1.
DR   Pfam; PF14310; Fn3-like; 1.
DR   Pfam; PF00933; Glyco_hydro_3; 1.
DR   Pfam; PF01915; Glyco_hydro_3_C; 1.
DR   PRINTS; PR00133; GLHYDRLASE3.
DR   SMART; SM01217; Fn3_like; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cellulose degradation; Glycoprotein; Glycosidase;
KW   Hydrolase; Polysaccharide degradation; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..769
FT                   /note="Probable beta-glucosidase M"
FT                   /id="PRO_0000394910"
FT   ACT_SITE        290
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        28
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        75
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        262
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        318
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        325
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        437
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        546
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   769 AA;  82416 MW;  5E4C6555397E7FB9 CRC64;
     MHSNLGLAGL AGLLATASVC LSAPADQNIT SDTYCYGQSP PVYPSPEGSG TGSWAAAYAK
     AKNFVAQLTP EEKVNLTAGT DANNGCSGNI AAIPRLNFPG LCVSDAGNGL RGTDYVSSWP
     SGLHVGASWS KALAKQRAIH MAKEFRKKGV NVILGPVVGP LGRVAEAGRN WEGFSNDPYL
     SGALVYETVD GAQSVGVATC TKHYILNEQE TNRNPGTEDG VDIAAVSSNI DDKTMHELYL
     WPFQDAVLAG SASIMCSYNR VNNSYGCQNS KTLNGLLKTE LGFQGYVMTD WGAQHAGIAG
     ANAGLDMVMP STETWGANLT TAISNGTMDA SRLDDMAIRI IASWYQMNQN SDSPSPGVGM
     PTNMYAPHQR VIGREASSKQ TLLRGAIEGH VLVKNTNSAL PLKSPQLLSV FGYDAKGPDA
     LKQNFNWLSY SPAIQENHTL WVGGGSGANN AAYVDAPIDA IKRQAYEDGT SVLYDLSSED
     PDVDPTTDAC LVFINSYATE GWDRPGLADK SSDSLVKNVA GKCANTIVTI HNAGIRVIGD
     WIDHENVTAV IFAHLPGQDS GRALVELLYG RANPSGKLPY TVAKKAEDYG SLLHPSLPET
     PYGLFPQSDF DEGVYIDYRA FDKANITPQF EFGFGLSYTA FEYSGLRISN PKKSPQYPPS
     AAIQQGGNPH LWDKTVTVSA EVKNTGRVAG AEVAQLYIGI PNGPVRQLRG FEKVDVSAGE
     TTQVKFALNR RDLSTWDVEA QQWSLQRGTY RVYVGRSSRD LPLTGSFTL
//