BGLM_ASPFN
ID BGLM_ASPFN Reviewed; 768 AA.
AC B8N5S6;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 70.
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=AFLA_014190;
OS Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS / JCM 12722 / SRRC 167).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=332952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC 167;
RX PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT aflatoxin contamination of food and feed.";
RL Genome Announc. 3:E0016815-E0016815(2015).
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; EQ963474; EED54167.1; -; Genomic_DNA.
DR RefSeq; XP_002375439.1; XM_002375398.1.
DR AlphaFoldDB; B8N5S6; -.
DR SMR; B8N5S6; -.
DR STRING; 5059.CADAFLAP00003304; -.
DR EnsemblFungi; EED54167; EED54167; AFLA_014190.
DR VEuPathDB; FungiDB:AFLA_014190; -.
DR eggNOG; ENOG502SMNU; Eukaryota.
DR HOGENOM; CLU_004542_2_1_1; -.
DR OMA; NFPGLCV; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000001875; Unassembled WGS sequence.
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; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..768
FT /note="Probable beta-glucosidase M"
FT /id="PRO_0000394905"
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; 82429 MW; 1881AC77816F1F05 CRC64;
MHAIAGLTGF LAGVSLSYAA PTQENITSDA 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 PSPGIGMPAD
VYAPHQAIIG KSSDSRKVLL QSAIEGHVLV KNKNNTLPLK SPEMISVFGY DAKGPDSLGF
ALEWLSYSPA IQPNHTLIVG GGSGGNSPAY ISAPLDALQQ QVIEDGSSIL WNISAQDPEV
DPNTDACLVF INSYATEGYD RAGLVDEGSD ELVTNVASKC SNTIVTIHNA GIRLVNNWID
HENVTAVIFA HLPGQDSGRA LVELLYGRSN PSGKLPYTVA KNADDYGALL HPKLPEGQYG
LFPQDDFSEG VYIDYRAFDK QGIEPQFEFG FGLSYTTFDY SGLNIGQVSD NSTSRYPPSA
AIQEGGNPHL WDVILRVSVD ITNSGPVAGD EVAQLYVGIP NGPVRQLRGF EKVNIPVGQT
VTVEFALGRR DLSTWDVVAQ EWLLQSGTYQ VYVGRSSRDL PLQGEFTI
