BGLM_ASPTN
ID BGLM_ASPTN Reviewed; 782 AA.
AC Q0C7L4;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 25-MAY-2022, entry version 62.
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=ATEG_10320;
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CH476610; EAU29317.1; -; Genomic_DNA.
DR RefSeq; XP_001218668.1; XM_001218667.1.
DR AlphaFoldDB; Q0C7L4; -.
DR SMR; Q0C7L4; -.
DR STRING; 341663.Q0C7L4; -.
DR EnsemblFungi; EAU29317; EAU29317; ATEG_10320.
DR GeneID; 4354713; -.
DR VEuPathDB; FungiDB:ATEG_10320; -.
DR eggNOG; ENOG502SMNU; Eukaryota.
DR HOGENOM; CLU_004542_2_1_1; -.
DR OMA; NFPGLCV; -.
DR OrthoDB; 321444at2759; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000007963; 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; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..782
FT /note="Probable beta-glucosidase M"
FT /id="PRO_0000394908"
FT ACT_SITE 303
FT /evidence="ECO:0000250"
FT CARBOHYD 25
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 46
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 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 331
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 338
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 443
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 449
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 536
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 558
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 654
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 664
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 782 AA; 84156 MW; 9A643E8C0562AB5E CRC64;
MHSFLGLVGL LAGVSVSSAA PSVQNITSDT YFYGQSPPVY PSPEGNGTGS WAVAYQKAKA
FVAQLTSEEK VNLTAGVTSD TGCSGMIPAI PRLNFPGLCV SDAGDGLRGT DYVNSWPSGI
HAGASWNKNL ARQRAYHMGT EFHKKGVNVL LGPVVAPLGR VVEGGRNWEG FSNDPYLSGA
LVYETVKGIQ SAGVGACTKV RFPQRLQSSG SNLVQHFTGY EQETNRNPET VDGVDIASVS
SNIDDKAMHE LYLWPFQDAV HAGSVSVMCS YQRINNSYAC QNSKTLNGLL KTELGFQGYV
MTDWYGQHGG IAAANAGLDM VMPYTELWGS NLTDAISNGT MEASRLDDMA TRIIASWYQV
NQNKNFPAPG IGMPADVNEP HQAVIGKSPD SRTTLLQGAI EGHVLVKNTK QALPLQSPRL
LSVFGYDAKA GDSLIVNDVS FVNASVQKNH TLYVGGGSGT NSAAYVLAPL DAVQQQAYED
GTSVLWDVVS EDPDVDATTD ACLVFINAYA TEGYDRPGLV NKESDTLITN VAGKCNNTIV
TIHNAGIRLV GDWINHENVT AVIFAHLPGQ DTGKALVELL YGRANPSGRL PYTVAKRAGD
YGSLLHPSQP EGKYGLFPQS DFSEGVFIDY RAFDKQGIEP QFEFGFGLSY TSFNYSGLAV
KKVNRTTEPY PASAPVQEGG NPNLWDEILT VSAKVQNSGS MDGDEVAQLY LGIPNAPVRQ
LRGFEKVGIP AGQAVNVKFS LTRRDLSVWD TEAQQWKLQS GDYQVYVGRS SRDLPLKGQF
SI
