BGLA_ASPCL
ID BGLA_ASPCL Reviewed; 867 AA.
AC A1CR85;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 68.
DE RecName: Full=Probable beta-glucosidase A;
DE EC=3.2.1.21;
DE AltName: Full=Beta-D-glucoside glucohydrolase A;
DE AltName: Full=Cellobiase A;
DE AltName: Full=Gentiobiase A;
DE Flags: Precursor;
GN Name=bglA; Synonyms=bgl1; ORFNames=ACLA_028810;
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
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; DS027059; EAW08156.1; -; Genomic_DNA.
DR RefSeq; XP_001269582.1; XM_001269581.1.
DR AlphaFoldDB; A1CR85; -.
DR SMR; A1CR85; -.
DR STRING; 5057.CADACLAP00002846; -.
DR EnsemblFungi; EAW08156; EAW08156; ACLA_028810.
DR GeneID; 4701004; -.
DR KEGG; act:ACLA_028810; -.
DR VEuPathDB; FungiDB:ACLA_028810; -.
DR eggNOG; ENOG502QR4D; Eukaryota.
DR HOGENOM; CLU_004542_2_0_1; -.
DR OMA; EAQGYGF; -.
DR OrthoDB; 559385at2759; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000006701; 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; IPR019800; Glyco_hydro_3_AS.
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.
DR PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 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..18
FT /evidence="ECO:0000255"
FT CHAIN 19..867
FT /note="Probable beta-glucosidase A"
FT /id="PRO_0000394092"
FT ACT_SITE 287
FT /evidence="ECO:0000250"
FT CARBOHYD 67
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 218
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 322
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 329
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 361
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 530
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 549
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 571
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 675
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 719
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 867 AA; 94053 MW; 6E9D96C46B830BA5 CRC64;
MRFSWLEVAV TAASLANANV CIPLFPWYVS SPPFYPSPWA NGQGEWAEAH QRAVEIVSQM
TLTEKVNLTT GTGWMMEECV GQTGSVPRLG INWGLCGQDS PLGIRFSDLN SAFPAGINVA
ATWDKTLAYL RGKAMGEEFN DKGIDIQLGP AAGPLGKYPD GGRIWEGFSP DPALTGVLFA
ETIKGIQDAG VIATAKHYIL NEQEQFRQVA EAQGYGYNIT ETLSSNVDDK TMHELYLWPF
ADAVRAGVGA IMCSYNQINN SYGCQNSQTL NKLLKAELGF QGFVMSDWSA HHSGVGAALA
GLDMSMPGDI SFDDGLSFWG ANMTVGVLNG TIPAWRVDDM AVRIMTAYYK VGRDRLRVPP
NFSSWTRDEY GYEHAAVSEG AWKKVNDFVN VQRDHAQLIR EVGSASTVLL KNVGALPLTG
KERKVGIFGE DAGSNPWGPN GCENRGCDNG TLAMAWGSGT AEFPYLVTPE QAIQSEVIKN
GGNVFPVTHN GALTQMANIA SQSSVSLVFV NADAGEGFIS VDGNIGDRKN LTLWKNGEEV
IKTVASHSNN TVVVIHSVGP ILVDEWHDNP NITAILWAGL PGQESGNSIA DVLYGRVNPS
AKTPFTWGKT RESYGAPLVT KPNNGNGAPQ DDFSEGVFID YRYFDKRNET PVYEFGFGLS
YTSFGYSHLR VQPLNGSTYV PATGTTGPAP AYGSIGSAAD YLFPEGLKRI TKFIYPWLNS
TDLKASSADP NYGWEDSEYI PEAATDGSPQ PILKAGGAPG GNPTLYHDLV KVSATITNTG
NVAGYEVPQL YVSLGGPNEP RVVLRKFDRI HLAPGEQKVW TTTLTRRDLA NWDVEAQDWV
ITKYPKRVYV GSSSRKLPLR APLPRVQ
