BGLM_ASPNC
ID BGLM_ASPNC Reviewed; 765 AA.
AC A5ABF5;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 25-MAY-2022, entry version 68.
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=An11g00200;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
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; AM270218; CAK48253.1; -; Genomic_DNA.
DR RefSeq; XP_001394024.1; XM_001393987.1.
DR AlphaFoldDB; A5ABF5; -.
DR SMR; A5ABF5; -.
DR CAZy; GH3; Glycoside Hydrolase Family 3.
DR PaxDb; A5ABF5; -.
DR EnsemblFungi; CAK48253; CAK48253; An11g00200.
DR GeneID; 4984238; -.
DR KEGG; ang:ANI_1_24094; -.
DR VEuPathDB; FungiDB:An11g00200; -.
DR HOGENOM; CLU_004542_2_1_1; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000006706; Chromosome 7R.
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 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; 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..19
FT /evidence="ECO:0000255"
FT CHAIN 20..765
FT /note="Probable beta-glucosidase M"
FT /id="PRO_5000242398"
FT ACT_SITE 286
FT /evidence="ECO:0000250"
FT CARBOHYD 24
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 258
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 314
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 321
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 432
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 519
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 541
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 647
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 765 AA; 82116 MW; 4D423F77A47A34A1 CRC64;
MHSISALLSL LGGLALSSAA PTQNITSDAY FYGQSPAVYP SPEGTGTGSW ASAYEKAKAF
VAQLTDDEKV NLTAGVSSKT GCSGFIAEIP RLNFTGLCVS DASNGLRGTD YVNGWSSGIH
VGASWNRTLA RDRAKYMGQE FHRKGVNLLL GPVVGPLGRV AEGGRNWEGF SNDPYLTGAL
VYETVQGVQS SGVGVSTKHY IGNEQETNRN PETVNGVDVA SVSSNIDDKT IHELYLWPFQ
DAVLAGSVAI MCSYERINNS YACQNSKTLN GLLKTELGFQ GYVITDWGAQ HGGIASANAG
LDMVMPETTL WGSNLTTAIA NGTMEASRLD DMATRIIATW YQLNQDTDFP TPGVGMPASA
QSEHQVVVGT APDEKSTLLE SAIEGHVLVK NTNNALPLQT PQLVSVFGYD AKVTDSFDLA
STVLGTSPLF QNYTLWVGGG SGSNSPAYVI APLNAIQQQA YEDGTSVLWD VSAQDPEVDP
TSEACLVFIN SFATEGYDRS ALTDDYSDTL VTNVASKCNN TIVVVHNAGI RLVYNWIDHE
NVTAVVLAHL PGQDTGHALV DILYGRANPS GKLPYTIAKQ ASDYGSLLHP SEPQTPYGLF
PQSDFSEGVY IDYRAFDKDN ITPQFEFGFG LSYTTFAYSG LSIEKTNETT SEYPPSAAIQ
EGGNPRLWDD LVTVTAEVQN SGSVDGAEVA QLYVGIPNGP VRQLRGFDKV LLSAGETAQV
SFSLNRRDLS TWNVEAQQWQ LQSGTYQVYV GRSSRDLPLT GEFSI
