BGLL_ASPFU
ID BGLL_ASPFU Reviewed; 739 AA.
AC Q4WGT3;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=Probable beta-glucosidase L;
DE EC=3.2.1.21;
DE AltName: Full=Beta-D-glucoside glucohydrolase L;
DE AltName: Full=Cellobiase L;
DE AltName: Full=Gentiobiase L;
DE Flags: Precursor;
GN Name=bglL; ORFNames=AFUA_7G06140;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
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 / Af293 / CBS 101355 / FGSC A1100;
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; AAHF01000009; EAL86858.1; -; Genomic_DNA.
DR RefSeq; XP_748896.1; XM_743803.1.
DR AlphaFoldDB; Q4WGT3; -.
DR SMR; Q4WGT3; -.
DR STRING; 746128.CADAFUBP00008919; -.
DR EnsemblFungi; EAL86858; EAL86858; AFUA_7G06140.
DR GeneID; 3506305; -.
DR KEGG; afm:AFUA_7G06140; -.
DR VEuPathDB; FungiDB:Afu7g06140; -.
DR eggNOG; ENOG502QR4D; Eukaryota.
DR HOGENOM; CLU_004542_2_3_1; -.
DR InParanoid; Q4WGT3; -.
DR OMA; GYPPVAF; -.
DR OrthoDB; 321444at2759; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000002530; Chromosome 7.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; 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..17
FT /evidence="ECO:0000255"
FT CHAIN 18..739
FT /note="Probable beta-glucosidase L"
FT /id="PRO_0000394900"
FT ACT_SITE 252
FT /evidence="ECO:0000250"
FT CARBOHYD 40
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 224
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 398
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 739 AA; 78381 MW; DCDFA27EB664D341 CRC64;
MQTLFLSLLA AAVTVHAYGS GGSNWDQAYS RAKDALQKLN QTEKVGLVTG VKWMGGPCVG
NTYKPESIDY PSLCLQDSPL GIRFANPVTA FPAGINAGAT WDTQLLYARG AAMGAEAKGL
GIHVQLGPVA GPLGKNPNGG RNWEGFSVDP YLSGVAMEKT IRGMQDSGVQ ACAKHWLGNE
QEHYRDTISS NIGDRAAHEL YVWPFMDAVK AGVASVMCSY NKVNGTWACE SDALNNKLMK
EELGFPGYIM SDWNAQHSTV NSAVSGLDMT MPGSDFSNPP GSIFWGSNLE AAVADGSVPQ
SRLDDMVTRI LAAWYLVGQD QGYPPVAFSS WNGGKANVDV TADHGTVARA VARDSIVLLK
NGHGTLPLRK PKSLAIVGSD AIVNPAGPNA CSDRGCNNGT LAMGWGSGTA EFPYLVGPLD
AIQKRAAADG TKIVPSATDD PTAGASAAAA AETAIVFINS DSGEGYITVE GNLGDRNNLD
PWHNGNELVK AVAAASKNVI VVIHSVGPII LETILAQPSV KAIVWAGLPG QESGNALVDV
IYGDTTPSGK LPYTIAKQAA DYGASWINAE TDDFPEGLYV DYRHFDAKGI APRYEFGYGL
SYTTFKYSGL WVNMDASAGA ANGQVVPGGP ADLFEVVGQV SVSVRNNGRV AGAEVAQLYL
GLPDSAPATP PKQLRGFQKL MLQPGQTGRA TFKLTRRDLS YWDVQQQKWV VPSGTFKVYV
GSSSRDIREE GSFRVRRGW
