BGLH_ASPOR
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 25-MAY-2022, entry version 81.
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 EnsemblFungi; BAE61738; BAE61738; AO090166000090.
DR VEuPathDB; FungiDB:AO090166000090; -.
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; 2.60.40.10; -; 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; 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
