ID   BGLG_NEOFI              Reviewed;         817 AA.
AC   A1DC16;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   24-JAN-2024, entry version 78.
DE   RecName: Full=Probable beta-glucosidase G;
DE            EC=3.2.1.21;
DE   AltName: Full=Beta-D-glucoside glucohydrolase G;
DE   AltName: Full=Cellobiase G;
DE   AltName: Full=Gentiobiase G;
DE   Flags: Precursor;
GN   Name=bglG; ORFNames=NFIA_100430;
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}.
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DR   EMBL; DS027694; EAW20406.1; -; Genomic_DNA.
DR   RefSeq; XP_001262303.1; XM_001262302.1.
DR   AlphaFoldDB; A1DC16; -.
DR   SMR; A1DC16; -.
DR   STRING; 331117.A1DC16; -.
DR   GlyCosmos; A1DC16; 14 sites, No reported glycans.
DR   EnsemblFungi; EAW20406; EAW20406; NFIA_100430.
DR   GeneID; 4588637; -.
DR   KEGG; nfi:NFIA_100430; -.
DR   VEuPathDB; FungiDB:NFIA_100430; -.
DR   eggNOG; ENOG502QR4D; Eukaryota.
DR   HOGENOM; CLU_004542_2_3_1; -.
DR   OMA; YERGYAM; -.
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:SF19; BETA-GLUCOSIDASE G-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..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..817
FT                   /note="Probable beta-glucosidase G"
FT                   /id="PRO_0000394120"
FT   ACT_SITE        304
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        40
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        58
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        229
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        276
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        343
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        350
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        402
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        507
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        563
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        584
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        623
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        662
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        679
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        715
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   817 AA;  88967 MW;  AEEE5B08E83E3B8D CRC64;
     MASIAHLIFS GLLAATVANS QQYEGSSRNE DAFNYVQPRN TTIFGQYGHS PAVLPSPNST
     GLGEWHAAYA KAREFVSLLT LEEKADMVTG QPGPCVGNIV AIPRLGFNGL CLQDGPMAIR
     VADYASVFSA GVTAASTWDR DILYERAFAM GQEFRAKGAH IALSPVAGPL GRSAYGGRNW
     EGFAADPYLT GIAMELSVQG YHDAGVQATP KHFIGNEQET QRNPTFDPNG TVTDVLQEAL
     SSNIDDRTMH ELYLWPFANA AHAKAASFMC SYQRLNGSYA CQNSKVLNGL LKEELGFQGY
     VMSDWGGTHS GVASIEAGLD MNMPGGLGPY GTIPEAGSFF GGNVTQAVKN GTVDEARVDD
     MIVRIMTPYY WLGQDQDFPS VDPSSADLNT FSPRSTWLRE FNLTGERSRD VRGDHAKLIR
     RHGAEATILL KNENNALPLK SPKALAIFGN DAGEPTMGAV NKANFEFGTL AAGGGSGTGR
     FTYVVSSLEA IKSRAKRANT LVQYWLNNTE VATTDVTTLW VPTPPDACLV FLKTWAEEGE
     DREHLSVDYD GNNVVFSVAR KCNNTIVITH SSGINELPFA DHPNVTAILA AHYPGQESGN
     SIVDVLYGDV NPSGRLPYTI ARNGSDYNAP PTTEIATTGK EDWQAWFDEK LEIDYRYFDA
     HNISVLYEFG FGLSYTTFNL SDINAEPLVK SISSVPEQLP IQPGGNPALW ENVYNVSVVV
     TNSGDVKGKA VPQLYVTFPD NTPAGTPPKQ LRGFDKVPLK PGESRAVSFQ LMRRDLSYWD
     VVSQQWLIPE GEFVIRVGFS SRDLREMIRI TPVTDST
//