ID   BGLJ_NEOFI              Reviewed;         864 AA.
AC   A1DNN8;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 89.
DE   RecName: Full=Probable beta-glucosidase J;
DE            EC=3.2.1.21;
DE   AltName: Full=Beta-D-glucoside glucohydrolase J;
DE   AltName: Full=Cellobiase J;
DE   AltName: Full=Gentiobiase J;
GN   Name=bglJ; ORFNames=NFIA_057590;
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 /
RC   NRRL 181 / 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; DS027698; EAW16409.1; -; Genomic_DNA.
DR   RefSeq; XP_001258306.1; XM_001258305.1.
DR   AlphaFoldDB; A1DNN8; -.
DR   SMR; A1DNN8; -.
DR   STRING; 331117.A1DNN8; -.
DR   GlyCosmos; A1DNN8; 3 sites, No reported glycans.
DR   EnsemblFungi; EAW16409; EAW16409; NFIA_057590.
DR   GeneID; 4584822; -.
DR   KEGG; nfi:NFIA_057590; -.
DR   VEuPathDB; FungiDB:NFIA_057590; -.
DR   eggNOG; ENOG502QR4D; Eukaryota.
DR   HOGENOM; CLU_004542_4_0_1; -.
DR   OMA; MHALTSN; -.
DR   OrthoDB; 5486783at2759; -.
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; 2.60.120.260; Galactose-binding domain-like; 1.
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   InterPro; IPR037524; PA14/GLEYA.
DR   InterPro; IPR011658; PA14_dom.
DR   PANTHER; PTHR42715; BETA-GLUCOSIDASE; 1.
DR   PANTHER; PTHR42715:SF16; BETA-GLUCOSIDASE J-RELATED; 1.
DR   Pfam; PF14310; Fn3-like; 1.
DR   Pfam; PF00933; Glyco_hydro_3; 1.
DR   Pfam; PF01915; Glyco_hydro_3_C; 1.
DR   Pfam; PF07691; PA14; 1.
DR   PRINTS; PR00133; GLHYDRLASE3.
DR   SMART; SM01217; Fn3_like; 1.
DR   SMART; SM00758; PA14; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF56988; Anthrax protective antigen; 1.
DR   SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
DR   PROSITE; PS51820; PA14; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cellulose degradation; Glycoprotein; Glycosidase;
KW   Hydrolase; Polysaccharide degradation; Reference proteome; Secreted.
FT   CHAIN           1..864
FT                   /note="Probable beta-glucosidase J"
FT                   /id="PRO_0000394895"
FT   DOMAIN          411..578
FT                   /note="PA14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01164"
FT   ACT_SITE        233
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        434
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        447
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        503
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   864 AA;  93160 MW;  B620FB8B941D14A6 CRC64;
     MGSLDTVDMG QRAIDQIISE LSLNEKVSLL SGVDAWHTFA IPRLGIPSIR TTDGPNGARG
     TRYFNGVPSA CLPCGTALGA TFDKDLIFSL GQLLAAECKA KGAHVLLGPT INIQRGPLGG
     RGFESFSEDP VLSGLAAASY CSGVQDGGVV PTLKHLVCND QEHERVAVSA LVTPRALREI
     YLLPFQLAIR GARPGAVMTS YNKVNGLHAS ESPGLIRDIL RGEWGYEGAV ISDWFGTYSV
     ADAVNAGLDL EMPGPTRFRG PALMHALTSN KVSEKTLNER VRKVLELVQL ASRSRVPEYA
     PERKLNRPED RALLRRAAGE SVVLLKNDKN DNNNSPILPL DREKKTLVIG PNADIAAYCG
     GGSASLLAYY TVTPRQGIAD KCGADQVVFS QGCYGHKELP LLGEHLRTIE TGEPGYTFRV
     YTEPPAASGS FKGNGSRKPV DELHMTNSSA FLMDYSHPQI SGDTYYATLE GTLEPPESGV
     YEFGLTVAGT GLLYIDGVLV VDNKTVQRAG TSFFGIGTVE ERGERYLEAG KKHHVFVEFG
     TAPTSNLQHH GVVSFGPGGL RLGGCRKLDT DAAIQQAVQS AAQTDQVVVC VGLSGDWESE
     GFDRPHMDLP PGTDELVNAV LEVQPNAVIV VQSGTPVTMP WADKAKALLQ AWYGGNEAGN
     GIADVLFGDV NPSAKLPLTF PRELSQNPSY LSYRSERGRV LYSEDIYVGY RYYDKARQPP
     LFRFGHGLSY TTFHLSDLAV RETAPYAANI KESSLRVSVT VSNTGARPGA EVVLVYVRPP
     PATCSVGRPV RELKGYEKVM LQPGETREVS IAIPVGYATS FWDEGCDAWL SEKGLYFVEA
     VGTGECNTLV APLSVQVSRM WNGL
//