ID   BGLM_ASPFU              Reviewed;         769 AA.
AC   Q4WR62;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   24-JAN-2024, entry version 90.
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=AFUA_1G17410;
OS   Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 /
OS   Af293) (Neosartorya fumigata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(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; AAHF01000004; EAL91070.1; -; Genomic_DNA.
DR   RefSeq; XP_753108.1; XM_748015.1.
DR   AlphaFoldDB; Q4WR62; -.
DR   SMR; Q4WR62; -.
DR   STRING; 330879.Q4WR62; -.
DR   CAZy; GH3; Glycoside Hydrolase Family 3.
DR   GlyCosmos; Q4WR62; 10 sites, No reported glycans.
DR   EnsemblFungi; EAL91070; EAL91070; AFUA_1G17410.
DR   GeneID; 3510140; -.
DR   KEGG; afm:AFUA_1G17410; -.
DR   VEuPathDB; FungiDB:Afu1g17410; -.
DR   eggNOG; ENOG502SMNU; Eukaryota.
DR   HOGENOM; CLU_004542_2_1_1; -.
DR   InParanoid; Q4WR62; -.
DR   OMA; NFPGLCV; -.
DR   OrthoDB; 5486783at2759; -.
DR   UniPathway; UPA00696; -.
DR   Proteomes; UP000002530; Chromosome 1.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004565; F:beta-galactosidase activity; IDA:AspGD.
DR   GO; GO:0008422; F:beta-glucosidase activity; IBA:GO_Central.
DR   GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009251; P:glucan catabolic process; IBA:GO_Central.
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..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..769
FT                   /note="Probable beta-glucosidase M"
FT                   /id="PRO_0000394906"
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        396
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        510
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        546
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        625
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   769 AA;  82681 MW;  79C92A56D4325D19 CRC64;
     MHSNVGLAGL AGLLATASVC LSAPADQNIT SDTYFYGQSP PVYPSPEGTG TGSWAAAYAK
     AKKFVAQLTP EEKVNLTAGT DANNGCSGNI AAIPRLNFPG LCVSDAGNGL RGTDYVSSWP
     SGLHVGASWN KALARQRAVQ MATEFRKKGV NVLLGPVVGP LGRVAEAGRN WEGFSNDPYL
     SGALVYETVD GAQSVGVATC TKHYILNEQE TNRNPGMEDG VEVAAVSSNI DDKTMHELYL
     WPFQDAVLAG SASIMCSYNR VNNSYGCQNS KTLNGLLKTE LGFQGYVMTD WGAQHAGIAG
     ANAGLDMVMP STETWGANLT TAISNGTMDA SRLDDMATRI IASWYQMNQD SDFPSPGAGM
     PSDMYAPHQR VIGRDASSKQ TLLRGAIEGH VLVKNNHSAL PLKSPQLLSV FGYDAKGPNA
     LKQNFNWLSY SPAIQENHTL WVGGGSGANN AAYIDAPIDA IQRQAYEDGT SVLYDISSED
     PEVDPTTDAC LVFINSYATE GWDRPGLADN SSDTLVKNVA RKCANTIVTI HNAGIRVVGE
     WIDHENVTAV IFAHLPGQDS GRALVELLYG RANPSGKLPY TVAKKVEDYG SLLHPSLPET
     PYGLFPQSDF DEGVYIDYRA FDRANITAQF EFGFGLSYTS FDYSGLQISN PKQSPQYPPS
     AAIQQGGNPH LWDNIVTVSA EIKNTGRVAG AEVAQLYIGI PNGPVRQLRG FEKVDVSAGE
     TTQVQFALNR RDLSTWDVEA QQWSLQRGTY RVYVGRSSRD LPLTGSFTL
//