BGLG_NEOFI
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 03-AUG-2022, entry version 75.
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 / NRRL 181
RC / 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; 36630.CADNFIAP00008542; -.
DR PRIDE; A1DC16; -.
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; 201102at2759; -.
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; 2.60.40.10; -; 1.
DR Gene3D; 3.20.20.300; -; 1.
DR Gene3D; 3.40.50.1700; -; 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 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; SSF51445; 1.
DR SUPFAM; SSF52279; SSF52279; 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
