ID   BGLK_EMENI              Reviewed;         838 AA.
AC   Q5BA18; C8VKN4; Q1HFU3;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   25-MAY-2022, entry version 101.
DE   RecName: Full=Probable beta-glucosidase K;
DE            EC=3.2.1.21;
DE   AltName: Full=Beta-D-glucoside glucohydrolase K;
DE   AltName: Full=Cellobiase K;
DE   AltName: Full=Gentiobiase K;
GN   Name=bglK; ORFNames=AN2612;
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; DQ490481; ABF50857.1; -; mRNA.
DR   EMBL; AACD01000043; EAA64717.1; -; Genomic_DNA.
DR   EMBL; BN001307; CBF87201.1; -; Genomic_DNA.
DR   RefSeq; XP_660216.1; XM_655124.1.
DR   AlphaFoldDB; Q5BA18; -.
DR   SMR; Q5BA18; -.
DR   STRING; 162425.CADANIAP00009350; -.
DR   CAZy; GH3; Glycoside Hydrolase Family 3.
DR   EnsemblFungi; CBF87201; CBF87201; ANIA_02612.
DR   EnsemblFungi; EAA64717; EAA64717; AN2612.2.
DR   GeneID; 2874655; -.
DR   KEGG; ani:AN2612.2; -.
DR   VEuPathDB; FungiDB:AN2612; -.
DR   eggNOG; ENOG502SMPY; Eukaryota.
DR   HOGENOM; CLU_004542_4_0_1; -.
DR   InParanoid; Q5BA18; -.
DR   OMA; MEEEYHI; -.
DR   OrthoDB; 175854at2759; -.
DR   UniPathway; UPA00696; -.
DR   Proteomes; UP000000560; Chromosome VII.
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   2: Evidence at transcript level;
KW   Carbohydrate metabolism; Cellulose degradation; Glycoprotein; Glycosidase;
KW   Hydrolase; Polysaccharide degradation; Reference proteome; Secreted.
FT   CHAIN           1..838
FT                   /note="Probable beta-glucosidase K"
FT                   /id="PRO_0000394898"
FT   DOMAIN          405..564
FT                   /note="PA14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01164"
FT   ACT_SITE        232
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        19
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        324
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        489
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   838 AA;  91126 MW;  D69D1188267FB44C CRC64;
     MGEISPRGGD FDIDYILENA SSLEKISLLA GHDFWHTAPL PRFNVPSVRV SDGPNGVRGT
     KFFDGVRAAC LPCGTGLAAT WDQSLLFDAG VLIGQECLAK GAHCWLGPTV CIQRSPLGGR
     GFESFAEDPY ATGKLAAAYI RGAQSTGVIS TIKHFAANDQ EHERISVNAV MSERALREVH
     LLPFQIAIAD AAPGAVMTCY NKINGQHVSE SKEMLDGLLR KEWGWKGLIM SDWFGTYSTA
     EALNAGLDLE MPGPTRLRGP LLELAISSRK VSRSTLDERA RTVLEFVKRA NKAEVSTVES
     TRDFPEDRRL NRKLAADSIV LLKNESGLLP LNLKALKSAA LIGPNMKTAA FCGGGSASLQ
     PYYSISPYQG IMNQLPPGVE IIYETGASSY VFIPELEASE VRTPEGQPGL RMRFYREPPS
     VKERRVVEET ILQESSWQLM GFSNPQLDRL FYADIEAELI APATGPFEFG LAVYGSGSLF
     IDDQLIIDNT TVQRGGNFFF GKGTREEKAT VDLVKGQLYK IRVEFASGPS SKLMKPGVVN
     FGGGAGRLGM VQAIDPELAI ARAVEAAKRA DVTILGVGLT RDHESEGFDR SHMDLPPAVA
     SLVTAVLDVA PDAILMTQSG TPFNMLPWAD NVKTHLHAWF GGNELGNGIA DVLFGVVNPS
     GKLPLSFPRR IEDTPTYLNF GSERGQVTYG EGIYVGYRYY EKVLRDVLYP FGHGLSYTSF
     AYSDFAVDTA SATLNVRNSG DVAGAEVVQL YIAADATTSS IARPVKELKG FAKVTLQPGE
     TCSVSIPFDR FTTAFWDQEA HVWTCEKGQY RVMVGSSSQN ILLEGVLEIK ETTTWSGL