ID   BGLJ_EMENI              Reviewed;         850 AA.
AC   Q5AV15; C8V7D6;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   25-MAY-2022, entry version 92.
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=AN7865;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
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; AACD01000134; EAA58910.1; -; Genomic_DNA.
DR   EMBL; BN001302; CBF73413.1; -; Genomic_DNA.
DR   RefSeq; XP_681134.1; XM_676042.1.
DR   AlphaFoldDB; Q5AV15; -.
DR   SMR; Q5AV15; -.
DR   STRING; 162425.CADANIAP00003880; -.
DR   CAZy; GH3; Glycoside Hydrolase Family 3.
DR   EnsemblFungi; CBF73413; CBF73413; ANIA_07865.
DR   EnsemblFungi; EAA58910; EAA58910; AN7865.2.
DR   GeneID; 2869049; -.
DR   KEGG; ani:AN7865.2; -.
DR   eggNOG; ENOG502QR4D; Eukaryota.
DR   HOGENOM; CLU_004542_4_0_1; -.
DR   InParanoid; Q5AV15; -.
DR   OMA; WHTFAIP; -.
DR   OrthoDB; 175854at2759; -.
DR   UniPathway; UPA00696; -.
DR   Proteomes; UP000000560; Chromosome II.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
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; 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   InterPro; IPR037524; PA14/GLEYA.
DR   InterPro; IPR011658; PA14_dom.
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; SSF51445; 1.
DR   SUPFAM; SSF52279; SSF52279; 1.
DR   PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 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..850
FT                   /note="Probable beta-glucosidase J"
FT                   /id="PRO_0000394894"
FT   DOMAIN          423..583
FT                   /note="PA14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01164"
FT   ACT_SITE        254
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        43
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        52
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        508
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   850 AA;  92696 MW;  D960EA3EBBFA8555 CRC64;
     MYRQEATTVT ILAQAPPNWP APAFDISGFT SAFRPSRRAQ RSNTTMGSID TNSTDAWHTF
     AIPRLGIPAM RITDGPNGAR GTRYFNGVPS ACLPCGTALG ATFDTDLLFK LGRLLAAECK
     AKGAHVLLGP TINIQRGPLG GRGFESFSED PVLSGNSAAS YCAGVKDLGI VPTLKHLVCN
     DQEHERIAVS AMVTERALRE IYLMPFQLAI KNARPGALMT SYNKVNGLHA SEDPGLLNHI
     IRKEWGFEGL IMSDWFGTYS VASAVNAGLD LEMPGPTRFR GPALMHALTS NKVSEKTLDD
     RVRKVLELVQ LTSRAGIPEY APAQKLDRVE DRVLLRQAAA DSIVLLKNAN EVLPLDPRKK
     TLVIGPNADI AAYCGGGSAS LLAYYTVTPR QGIAEKCEEV VFSQGCYGHK ELPLLGDHLK
     TETGERGYTF RVYTEPATYE DRQPVDVLHM TNSCAFLMDY SHPKISGDTY YATLEGRFEP
     TESGVYELGL TVAGTGLLYI DGELVIDNKT KQRHGTSFFG IGTVEERGER YLEAGRQHHV
     FVEYSTAPTS NLKHHGVVSF GPGGVRLGGC RKLDAETAIK QAVQLAAETE QVVVCVGMNG
     NWESEGFDRP HMDLPPGTDN LVRAVIEAQP NAVIVVQSGT PVTMPWADQA KALVQAWYGG
     SEGGNGIADV LFGDVNPSAK LPLTFPRDIA HNPSYLSYRS ERGRVLYSED VYVGYRYYDK
     VKQAPLFHFG HGLSYTTFKL SGLNVQETDP QASDISAEVV QIYVRPPTTA SVGRPVRELK
     GYEKTMLHPG ETKEISVTVP MGVATSFWDE GRSAWLSEKG TYAIEVVGTG ERNMLSAPLC
     VQVSRYWNGL