BGLG_ASPTN
ID BGLG_ASPTN Reviewed; 817 AA.
AC Q0CUC1;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 25-MAY-2022, entry version 62.
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=ATEG_02713;
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CH476596; EAU37675.1; -; Genomic_DNA.
DR RefSeq; XP_001211891.1; XM_001211891.1.
DR AlphaFoldDB; Q0CUC1; -.
DR SMR; Q0CUC1; -.
DR STRING; 341663.Q0CUC1; -.
DR EnsemblFungi; EAU37675; EAU37675; ATEG_02713.
DR GeneID; 4317206; -.
DR VEuPathDB; FungiDB:ATEG_02713; -.
DR eggNOG; ENOG502QR4D; Eukaryota.
DR HOGENOM; CLU_004542_2_3_1; -.
DR OMA; YERGYAM; -.
DR OrthoDB; 201102at2759; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000007963; 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_0000394118"
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; 88407 MW; C3D3219F884364C1 CRC64;
MANIAHLIVS GLLAATVAHG QQYEGSSRSE DAFSYVQPRN TTILGQYGHS PAVLPSPNST
GSGGWQAAHT KARHFVSQLT LEEKADMVTG QPGPCVGNIV AIPRLGFNGL CLQDGPLAIR
VADYASVFSA GVTAASTWDR DVLYERAFAM GQEFRAKGAH IALGPVAGPL GRSAYGGRNW
EGFAADPYLT GVAMELSVKG YHDAGVQATP KHFIGNEQET QRNPIYNPNG TITDVLQEAV
SSNIDDRTMH ELYLWPFANA AHAKAAAFMC SYQRLNGSYA CQNSKALNGL LKEELGFQGY
VMSDWGGTHS GVASIESGLD MNMPGGLGPY GTIPQAGSFY GGNVTQGVKN GTIDEARVDD
MIIRIMTPYY WLGQDKDFPS VDPSSADLNT FSPRSTWLRQ FNLTGERNRD VRGDHAKIIR
RQAAEATVLL KNEKNALPLK SPKSLAIFGN DAGEPTMGAV NQANFEFGTL AAGGGSGTGR
FTYVVSPLEA IQSRAKQANT LVQYWMNNTD IATTDVTTLW VPAPPDACLV FLKTWAEEGE
DREYLHVDYD GNDVVSSVAS KCNNTIVVTH SSGINELPFA DHPNVTAILA AHYPGQESGN
SIVDVLYGDV NPSGRLPYTI ARNGSEYNAP PTTEVTTTGA EDWQAWFNEK LEIDYRYFDA
HNISVLYEFG FGLSYTTFNL SEINAEPLVE SISSVPEQRP IQPGGNPALW ENVYNVSVVV
TNTGDVEGKA VPQLYVTFPD STPAGTPPKQ LRGFDKVALK PGQSQAASFQ LMRRDLSYWD
VVSQQWLIPE GEFVISVGFS SRDLREVVRV TPVSGST
