ID   BGLM_ASPFN              Reviewed;         768 AA.
AC   B8N5S6;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 74.
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=AFLA_014190;
OS   Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS   / JCM 12722 / SRRC 167).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=332952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 /
RC   SRRC 167;
RX   PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA   Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA   Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT   "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT   aflatoxin contamination of food and feed.";
RL   Genome Announc. 3:E0016815-E0016815(2015).
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; EQ963474; EED54167.1; -; Genomic_DNA.
DR   RefSeq; XP_002375439.1; XM_002375398.1.
DR   AlphaFoldDB; B8N5S6; -.
DR   SMR; B8N5S6; -.
DR   STRING; 332952.B8N5S6; -.
DR   GlyCosmos; B8N5S6; 10 sites, No reported glycans.
DR   EnsemblFungi; EED54167; EED54167; AFLA_014190.
DR   VEuPathDB; FungiDB:AFLA_001849; -.
DR   eggNOG; ENOG502SMNU; Eukaryota.
DR   HOGENOM; CLU_004542_2_1_1; -.
DR   OMA; NFPGLCV; -.
DR   OrthoDB; 5486783at2759; -.
DR   UniPathway; UPA00696; -.
DR   Proteomes; UP000001875; 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; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..768
FT                   /note="Probable beta-glucosidase M"
FT                   /id="PRO_0000394905"
FT   ACT_SITE        287
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        25
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        72
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        259
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        315
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        322
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        394
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        434
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        472
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        543
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        651
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   768 AA;  82429 MW;  1881AC77816F1F05 CRC64;
     MHAIAGLTGF LAGVSLSYAA PTQENITSDA YFYGQSPAVY PSPEGTGSGA WASAYEKAKA
     FVANLTPEEK VNLTAGTDAD NGCSGNIPAI PRLNFPGLCV SDAGNGLRST DHVNAWSSGI
     HTGASWNKDL AQKRGLHMGS EYHKKGVNVL LGPVVGPLGR IAEGGRNWEG FSVDPYHSGL
     LVYETIRGIQ AAGVGTSTKH YIANEQETNR NPESTDGIDV AAVSSNIDDK TMHELYLWPF
     QDVVRAGSVS IMCSYQRINN SYGCQNSKTL NGLLKTELGF QGYVMTDWGA QHGGIASSNA
     GLDMVMPSST LWNSNLTDAI ANGTMEASRL DDMATRIIAS WYQMNQDAGF PSPGIGMPAD
     VYAPHQAIIG KSSDSRKVLL QSAIEGHVLV KNKNNTLPLK SPEMISVFGY DAKGPDSLGF
     ALEWLSYSPA IQPNHTLIVG GGSGGNSPAY ISAPLDALQQ QVIEDGSSIL WNISAQDPEV
     DPNTDACLVF INSYATEGYD RAGLVDEGSD ELVTNVASKC SNTIVTIHNA GIRLVNNWID
     HENVTAVIFA HLPGQDSGRA LVELLYGRSN PSGKLPYTVA KNADDYGALL HPKLPEGQYG
     LFPQDDFSEG VYIDYRAFDK QGIEPQFEFG FGLSYTTFDY SGLNIGQVSD NSTSRYPPSA
     AIQEGGNPHL WDVILRVSVD ITNSGPVAGD EVAQLYVGIP NGPVRQLRGF EKVNIPVGQT
     VTVEFALGRR DLSTWDVVAQ EWLLQSGTYQ VYVGRSSRDL PLQGEFTI
//