BGLC_ASPOR
ID BGLC_ASPOR Reviewed; 638 AA.
AC Q2UFP8;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=Probable beta-glucosidase C;
DE EC=3.2.1.21;
DE AltName: Full=Beta-D-glucoside glucohydrolase C;
DE AltName: Full=Cellobiase C;
DE AltName: Full=Gentiobiase C;
DE Flags: Precursor;
GN Name=bglC; ORFNames=AO090026000123;
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=BAE59617.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AP007159; BAE59617.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q2UFP8; -.
DR SMR; Q2UFP8; -.
DR STRING; 510516.Q2UFP8; -.
DR CAZy; GH3; Glycoside Hydrolase Family 3.
DR EnsemblFungi; BAE59617; BAE59617; AO090026000123.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000006564; Chromosome 3.
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; 3.20.20.300; -; 1.
DR Gene3D; 3.40.50.1700; -; 1.
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 Pfam; PF00933; Glyco_hydro_3; 1.
DR Pfam; PF01915; Glyco_hydro_3_C; 1.
DR PRINTS; PR00133; GLHYDRLASE3.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF52279; SSF52279; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Cellulose degradation; Glycoprotein; Glycosidase;
KW Hydrolase; Polysaccharide degradation; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..638
FT /note="Probable beta-glucosidase C"
FT /id="PRO_0000394104"
FT ACT_SITE 341
FT /evidence="ECO:0000250"
FT CARBOHYD 40
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 223
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 274
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 364
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 480
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 488
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 528
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 638 AA; 70451 MW; F070472F086BA6F1 CRC64;
MKVLAPGYLA EASLTALASG CQALSTRPYV PRGYSLSRRN DSTPIYKDAS YCIDERVDDL
LARMTIEEKA GQLFHTRLMD GPLDDEGSGN NAHNSTSNMI GEKHMTHFNL ASDITNATET
AEFINRIQEL ALQTRLGIPV TVSTDPRHSF TENVGTGFKA GVFSQWPESI GLAALRDPYV
VRKFAEVAKE EYIAVGIRAA LHPQVDLSTE PRWARISNTW GENSTLTSEL LVEYIKGFQG
DKLGPQSVKT VTKHFPGGGP VENGEDSHFA YGKNQTYPGN NLEEHLKPFK AAIAAGATEI
MPYYSRPIGT EYEPVAFSFN KRIVTELLRN ELGFDGIVLT DWGLITDGYI AGQYMPARAW
GVENLTELQR AARILDAGCD QFGGEERPEL IVQLVQEGII SEDRIDVSVR RLLKEKFVLG
LFDNPFVDAE AAGRVVGNDY FVRLGREAQR RSYTLLSNNE DIVPLKKIEK STKFYIEGFN
ASFIESWNYT VVDSPEEAEY ALLRYNAPYE PRPGGFEANM HAGSLAFNDT EKARQAKIYS
AVPTIVDIVM DRPAVIPEII EQAKAVFASY GSDSNAFLDV VFGVSAPEGK LPFDLPSSME
AVEAQMEDVP FDTRNPVFKF GHGLSYANPC ASSSSKCS
