ID   BGLH_ASPFN              Reviewed;         827 AA.
AC   B8NPL7;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Probable beta-glucosidase H;
DE            EC=3.2.1.21;
DE   AltName: Full=Beta-D-glucoside glucohydrolase H;
DE   AltName: Full=Cellobiase H;
DE   AltName: Full=Gentiobiase H;
GN   Name=bglH; ORFNames=AFLA_000810;
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 / SRRC
RC   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}.
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DR   EMBL; EQ963482; EED47440.1; -; Genomic_DNA.
DR   RefSeq; XP_002382282.1; XM_002382241.1.
DR   AlphaFoldDB; B8NPL7; -.
DR   SMR; B8NPL7; -.
DR   STRING; 5059.CADAFLAP00010147; -.
DR   EnsemblFungi; EED47440; EED47440; AFLA_000810.
DR   VEuPathDB; FungiDB:AFLA_000810; -.
DR   eggNOG; ENOG502SMPY; Eukaryota.
DR   HOGENOM; CLU_004542_4_0_1; -.
DR   OMA; CESTGVI; -.
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; 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   InterPro; IPR037524; PA14/GLEYA.
DR   InterPro; IPR011658; PA14_dom.
DR   Pfam; PF14310; Fn3-like; 1.
DR   Pfam; PF00933; Glyco_hydro_3; 1.
DR   Pfam; PF01915; Glyco_hydro_3_C; 1.
DR   Pfam; PF07691; PA14; 1.
DR   PRINTS; PR00133; GLHYDRLASE3.
DR   SMART; SM01217; Fn3_like; 1.
DR   SMART; SM00758; PA14; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   SUPFAM; SSF52279; SSF52279; 1.
DR   PROSITE; PS51820; PA14; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cellulose degradation; Glycoprotein; Glycosidase;
KW   Hydrolase; Polysaccharide degradation; Secreted.
FT   CHAIN           1..827
FT                   /note="Probable beta-glucosidase H"
FT                   /id="PRO_0000394878"
FT   DOMAIN          387..546
FT                   /note="PA14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01164"
FT   ACT_SITE        223
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        471
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        594
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        600
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        625
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   827 AA;  90797 MW;  7E5438F60066A83B CRC64;
     MALDIDYVLS HISQEDKIAL LAGIDFWHTH PIPELNVPSI RSTDGPNGIR GTKFFAGVPA
     ACLPCGTALA STWDQNLLRE VGVLIGKECL AKGAHCWLGP TINMPRSPLG GRGFESFAED
     PHLAGAMAAS MITGCESTGV ISAVKHFVGN DQEHERRAVD VLVTQRALRE IYLRPFQIVA
     RDAGPGALMT SYNKINGKHV VESKEMLDMV RQEWKWNPLI MSDWLGTYTT IDSMNAGLDL
     EMPGPSRYRG RYVESALQAR LIKESTIDSR ARKVLEFVQQ ASRAPVSAVE TGRDYPEDRA
     LNRNLCANSI VLLKNQNDIL PLPKTIKKIA LVGSHVRTPA ISGGGSASLE PYYTVSLYDA
     VSEALPHTEI LYEVGAYAHK MLPVIDRLLT NAVMHFYNEP VGTERILRAT QRMSKTAFQL
     MDFNAPELNR GLFYATLTGD FTPDVSGVWD FGLTVFGTGL LYVDDELVVD NTTHQTRGTA
     FFGKGTVQEL GSKTLNAEQT YKIRIEYGSA NTSPMKAIGV VHFGGGAAHL GACLHVDSAE
     MVRSAVKAAA EADYTILCTG LNHEWESEGF DRSHMDLPPG IDALITSVLD VAANKTVIVN
     QSGTPVTMPW ADRARGIVQA WYGGNETGHG IADVIFGDVN PSGKLPLSWP VDVKHNPAYL
     NYASVGGRVL YGEDVYVGYR YYEKVGREVL FPFGHGLSYT TFTVSPDVVF SQEVFRPEEP
     PTAAVKIKNT GKVAGAQVLQ LYISAPHSPT PRPTKELHGF TKVLLQPGEE RVAHIRMDKY
     ATNFWDEIEG MWKSEEGIYE ALIGTSSQNI LAKGTFRVDR TRYWLGL