ID   BGLH_ASPOR              Reviewed;         827 AA.
AC   Q2U9M7;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 2.
DT   22-FEB-2023, entry version 83.
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=AO090166000090;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE61738.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AP007163; BAE61738.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_001822871.2; XM_001822819.2.
DR   AlphaFoldDB; Q2U9M7; -.
DR   SMR; Q2U9M7; -.
DR   STRING; 510516.Q2U9M7; -.
DR   CAZy; GH3; Glycoside Hydrolase Family 3.
DR   GlyCosmos; Q2U9M7; 4 sites, No reported glycans.
DR   EnsemblFungi; BAE61738; BAE61738; AO090166000090.
DR   VEuPathDB; FungiDB:AO090166000090; -.
DR   OrthoDB; 5486783at2759; -.
DR   UniPathway; UPA00696; -.
DR   Proteomes; UP000006564; Chromosome 4.
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..827
FT                   /note="Probable beta-glucosidase H"
FT                   /id="PRO_0000394880"
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;  90680 MW;  7D495C5BD7FBF59C CRC64;
     MALEIDYVLS 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 QPMSKTAFQL
     MDFNAPELNR GLFYATLTGD FTPDVSGVWD FGLTVFGTGL LYVDDELVVD NTTHQTRGTA
     FFGKGTVQEL GSKTLNAGQT 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
//