ID   BGLH_ASPCL              Reviewed;         829 AA.
AC   A1CUR8;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 76.
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=ACLA_087610;
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS   NRRL 1 / QM 1276 / 107).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=344612;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
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; DS027060; EAW07055.1; -; Genomic_DNA.
DR   RefSeq; XP_001268481.1; XM_001268480.1.
DR   AlphaFoldDB; A1CUR8; -.
DR   SMR; A1CUR8; -.
DR   STRING; 344612.A1CUR8; -.
DR   GlyCosmos; A1CUR8; 5 sites, No reported glycans.
DR   EnsemblFungi; EAW07055; EAW07055; ACLA_087610.
DR   GeneID; 4699856; -.
DR   KEGG; act:ACLA_087610; -.
DR   VEuPathDB; FungiDB:ACLA_087610; -.
DR   eggNOG; ENOG502SMPY; Eukaryota.
DR   HOGENOM; CLU_004542_4_0_1; -.
DR   OMA; DVKHNPA; -.
DR   OrthoDB; 5486783at2759; -.
DR   UniPathway; UPA00696; -.
DR   Proteomes; UP000006701; 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; Reference proteome; Secreted.
FT   CHAIN           1..829
FT                   /note="Probable beta-glucosidase H"
FT                   /id="PRO_0000394876"
FT   DOMAIN          389..548
FT                   /note="PA14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01164"
FT   ACT_SITE        225
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        416
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        431
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"
SQ   SEQUENCE   829 AA;  90774 MW;  F6CD19443ADAD23C CRC64;
     MTAKFDVDHV LNSISEDDKI ALLSGTDFWH TYSIPEHNVP PIRTTDGPNG VRGTKFFAGV
     PAACLPCGTA LGATWDRDLL HKAGVLLGQE CLAKGAHCWL GPTINMQRSP LGGRGFESFA
     EDPHLSGTMA KSIILGCEST GVISAVKHYV GNDQEHERRA VDVMVTPRAL REIYLRPFQI
     VARDAHSGAL MTSYNKINGK HVVENPAMYD IIRKEWKWDP LIMSDWLGTY TTIDSLNAGL
     DLEMPGPSRY RGKYIESAVQ ARLVKQSTID QRARKVLEFA ARASQAPASA VESGRDYPED
     RALNREICGN SIVLLKNEDT LLPLPKKIKK IALIGSHVKT PAISGGGSAS LQPYYAVSLY
     DAIIEVLPDT EIIYETGAYA HKMLPVIDRM LSNAVIRFYN EPADKERTLL STEPVNNTAF
     QLMDYNTPGL NRTLFWATLD GEFTPDVSGL WDFGLTVFGT ATLYIDDEMV IDNTTQQTRG
     TAFFGKGTIQ EVGAKELTAG RTYKIRIEFG SANTSPIKAI GVVHFGGGAA HLGAFLHMDP
     EQMVRDAVKA ASEADYTILC TGLNRDWESE GFDRPDMDLP PRIDALISAV LDVAGDKTII
     VNQSGTPVMM PWSDRARAII QAWYGGNETG HGIADVLFGD VNPCAKLPLS WPADVRHNPA
     YLNSLSVGGR MLYGEDIYVG YRFYEKIGQV TLFPFGHGLS YTLFEVSPKV TVSPTAFTVE
     TPLSATVRIK NTGPVAGAQI LQLYVAAPTS ATPRPVKELQ GFSKVFLQSG EEKTVVISVD
     KYATSFWDGI EDMWKSEAGV YQVLIGTSSQ DIVARGEFTV DETTFWTGV
//