ID   BGLH_ASPFC              Reviewed;         829 AA.
AC   B0XM94;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-MAY-2023, entry version 69.
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=AFUB_000280;
OS   Aspergillus fumigatus (strain CBS 144.89 / FGSC A1163 / CEA10) (Neosartorya
OS   fumigata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=451804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 144.89 / FGSC A1163 / CEA10;
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; DS499594; EDP55338.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0XM94; -.
DR   SMR; B0XM94; -.
DR   GlyCosmos; B0XM94; 7 sites, No reported glycans.
DR   EnsemblFungi; EDP55338; EDP55338; AFUB_000280.
DR   VEuPathDB; FungiDB:AFUB_000280; -.
DR   HOGENOM; CLU_004542_4_0_1; -.
DR   PhylomeDB; B0XM94; -.
DR   UniPathway; UPA00696; -.
DR   Proteomes; UP000001699; 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; 2.60.120.260; Galactose-binding domain-like; 1.
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   InterPro; IPR037524; PA14/GLEYA.
DR   InterPro; IPR011658; PA14_dom.
DR   PANTHER; PTHR42715; BETA-GLUCOSIDASE; 1.
DR   PANTHER; PTHR42715:SF17; BETA-GLUCOSIDASE H-RELATED; 1.
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; (Trans)glycosidases; 1.
DR   SUPFAM; SSF56988; Anthrax protective antigen; 1.
DR   SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 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..829
FT                   /note="Probable beta-glucosidase H"
FT                   /id="PRO_0000394877"
FT   DOMAIN          389..548
FT                   /note="PA14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01164"
FT   ACT_SITE        225
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        13
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        304
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        473
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        602
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        627
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        664
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        749
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   829 AA;  91020 MW;  9E62CDC1659A8EC8 CRC64;
     MTPKFDIDYV LANITEDDKI ALLSGSDFWH THAIPKFNVP PIRTTDGPNG IRGTKFFAGV
     PAACLPCGTA LGATWDRDLL HQAGVLLGKE CLAKGAHCWL GPTINMQRSP LGGRGFESFA
     EDPHLSGIMA KSIILGCEST GVISTVKHYV GNDQEHERRA VDVLVTPRAL REIYLRPFQI
     VARDAHPGAL MTSYNKINGK HVVENPAMLD IVRKDWHWDP LIMSDWLGTY TTIDSLNAGL
     DLEMPGPTRY RGKYIESAMQ ARLIKQSTIS KRARKVLEFV ERASRAPVSA DETGRDFPED
     RALNRTLCAN SIVLLKNDGN LLPIPKTVKK IALIGSHVKT PAISGGGSAS LEPYYAVSLY
     DAVVEALPDA EILYEAGAYA HRMLPVIDRM LSNAVIHFYN EPPEKERTLL ATEPVVNTAF
     QLMDYNAPGL NRALFWATLI GEFTPDVSGL WDFGLTVFGT ATLFIDDEMV IDNATRQTRG
     TAFFGKGTVQ EVGQKQLTAG QTYKIRIEFG SANTSPMKAI GVVHFGGGAA HLGACLHMDP
     EQMVANAVRV AAEADYTIVC TGLNRDWESE GFDRPDMDLP PGIDALISSV LDVAADRTVI
     VNQSGTPVTM PWAHRARGIV QAWYGGNETG HGIADVLFGD VNPSGKLPLS WPADVRHNPT
     YLNNMSVGGR MLYGEDVYIG YRFYEKVGRE VLFPFGHGLS YTTFHVSPEA TVSPIVFSSD
     SPPTATVLVK NTGPMAGAQT LQLYIAAPNS TTPRPVKELH GFTKVFLQSG EERSVSIHID
     RYATSFWDEI EDMWKSEEGV YQVLIGTSSQ EIVSRGEFRV EQTRYWRGV
//