ID BGLM_ASPOR Reviewed; 768 AA.
AC Q2UDK7;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 22-FEB-2023, entry version 84.
DE RecName: Full=Probable beta-glucosidase M;
DE EC=3.2.1.21;
DE AltName: Full=Beta-D-glucoside glucohydrolase M;
DE AltName: Full=Cellobiase M;
DE AltName: Full=Gentiobiase M;
DE Flags: Precursor;
GN Name=bglM; ORFNames=AO090012000135;
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}.
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DR EMBL; AP007161; BAE60358.1; -; Genomic_DNA.
DR RefSeq; XP_001727197.1; XM_001727145.1.
DR AlphaFoldDB; Q2UDK7; -.
DR SMR; Q2UDK7; -.
DR STRING; 510516.Q2UDK7; -.
DR CAZy; GH3; Glycoside Hydrolase Family 3.
DR GlyCosmos; Q2UDK7; 10 sites, No reported glycans.
DR EnsemblFungi; BAE60358; BAE60358; AO090012000135.
DR GeneID; 5987671; -.
DR KEGG; aor:AO090012000135; -.
DR VEuPathDB; FungiDB:AO090012000135; -.
DR HOGENOM; CLU_004542_2_1_1; -.
DR OMA; NFPGLCV; -.
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; 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 PANTHER; PTHR42715; BETA-GLUCOSIDASE; 1.
DR PANTHER; PTHR42715:SF5; BETA-GLUCOSIDASE M-RELATED; 1.
DR Pfam; PF14310; Fn3-like; 1.
DR Pfam; PF00933; Glyco_hydro_3; 1.
DR Pfam; PF01915; Glyco_hydro_3_C; 1.
DR PRINTS; PR00133; GLHYDRLASE3.
DR SMART; SM01217; Fn3_like; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 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..19
FT /evidence="ECO:0000255"
FT CHAIN 20..768
FT /note="Probable beta-glucosidase M"
FT /id="PRO_0000394907"
FT ACT_SITE 287
FT /evidence="ECO:0000250"
FT CARBOHYD 25
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 259
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 315
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 322
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 394
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 434
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 472
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 543
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 651
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 768 AA; 82363 MW; C0177EC254F455ED CRC64;
MHAIAGLTGL LAGVSLSYAA PTHENITSDA YFYGQSPAVY PSPEGTGSGA WASAYEKAKA
FVANLTPEEK VNLTAGTDAD NGCSGNIPAI PRLNFPGLCV SDAGNGLRST DHVNAWSSGI
HTGASWNKDL AQKRGLHMGS EYHKKGVNVL LGPVVGPLGR IAEGGRNWEG FSVDPYHSGL
LVYETIRGIQ AAGVGTSTKH YIANEQETNR NPESTDGIDV AAVSSNIDDK TMHELYLWPF
QDVVRAGSVS IMCSYQRINN SYGCQNSKTL NGLLKTELGF QGYVMTDWGA QHGGIASSNA
GLDMVMPSST LWNSNLTDAI ANGTMEASRL DDMATRIIAS WYQMNQDAGF PSPGVGMPAD
VYAPHQAIIG KSSDSRKVLL QSAIEGHVLV KNKNNTLPLK SPEMISVFGY DAKGPDSLGF
ALEWLSYSPA IQPNHTLIVG GGSGGNSPAY ISAPLDALQQ QVIEDGSSIL WNISAQDPEV
DPNTDACLVF INSYATEGYD RAGLVDEGSD ELVTNVASKC SNTIVTIHNA GIRLVNNWID
HENVTAVIFA HLPGQDSGRA LVELLYGRSN PSGKLPYTVA KSADDYGALL HPKLPEGQYG
LFPQDDFSEG VYIDYRAFDK QGIEPQFEFG FGLSYTTFDY SGLNIGQVSD NSTSRYPPSA
AIQEGGNPHL WDVILRVSVD ITNSGPVAGD EVAQLYVGIP NGPVRQLRGF EKVNIPVGQT
VTVEFALGRR DLSTWDVVAQ EWLLQSGTYQ VYVGRSSRDL PLQGEFTI
//
