BGLM_NEOFI
ID BGLM_NEOFI Reviewed; 769 AA.
AC A1D122;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 74.
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=NFIA_007920;
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC / WB 181;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027688; EAW22115.1; -; Genomic_DNA.
DR RefSeq; XP_001264012.1; XM_001264011.1.
DR AlphaFoldDB; A1D122; -.
DR SMR; A1D122; -.
DR STRING; 36630.CADNFIAP00001080; -.
DR EnsemblFungi; EAW22115; EAW22115; NFIA_007920.
DR GeneID; 4592105; -.
DR KEGG; nfi:NFIA_007920; -.
DR VEuPathDB; FungiDB:NFIA_007920; -.
DR eggNOG; ENOG502SMNU; Eukaryota.
DR HOGENOM; CLU_004542_2_1_1; -.
DR OMA; NFPGLCV; -.
DR OrthoDB; 321444at2759; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000006702; 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..22
FT /evidence="ECO:0000255"
FT CHAIN 23..769
FT /note="Probable beta-glucosidase M"
FT /id="PRO_0000394910"
FT ACT_SITE 290
FT /evidence="ECO:0000250"
FT CARBOHYD 28
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 262
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 318
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 325
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 437
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 546
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 769 AA; 82416 MW; 5E4C6555397E7FB9 CRC64;
MHSNLGLAGL AGLLATASVC LSAPADQNIT SDTYCYGQSP PVYPSPEGSG TGSWAAAYAK
AKNFVAQLTP EEKVNLTAGT DANNGCSGNI AAIPRLNFPG LCVSDAGNGL RGTDYVSSWP
SGLHVGASWS KALAKQRAIH MAKEFRKKGV NVILGPVVGP LGRVAEAGRN WEGFSNDPYL
SGALVYETVD GAQSVGVATC TKHYILNEQE TNRNPGTEDG VDIAAVSSNI DDKTMHELYL
WPFQDAVLAG SASIMCSYNR VNNSYGCQNS KTLNGLLKTE LGFQGYVMTD WGAQHAGIAG
ANAGLDMVMP STETWGANLT TAISNGTMDA SRLDDMAIRI IASWYQMNQN SDSPSPGVGM
PTNMYAPHQR VIGREASSKQ TLLRGAIEGH VLVKNTNSAL PLKSPQLLSV FGYDAKGPDA
LKQNFNWLSY SPAIQENHTL WVGGGSGANN AAYVDAPIDA IKRQAYEDGT SVLYDLSSED
PDVDPTTDAC LVFINSYATE GWDRPGLADK SSDSLVKNVA GKCANTIVTI HNAGIRVIGD
WIDHENVTAV IFAHLPGQDS GRALVELLYG RANPSGKLPY TVAKKAEDYG SLLHPSLPET
PYGLFPQSDF DEGVYIDYRA FDKANITPQF EFGFGLSYTA FEYSGLRISN PKKSPQYPPS
AAIQQGGNPH LWDKTVTVSA EVKNTGRVAG AEVAQLYIGI PNGPVRQLRG FEKVDVSAGE
TTQVKFALNR RDLSTWDVEA QQWSLQRGTY RVYVGRSSRD LPLTGSFTL
