ID   BGLS_SCHPO              Reviewed;         832 AA.
AC   Q9P6J6;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 124.
DE   RecName: Full=Putative beta-glucosidase;
DE            EC=3.2.1.21;
DE   AltName: Full=Beta-D-glucoside glucohydrolase;
DE   AltName: Full=Cellobiase;
DE   AltName: Full=Gentiobiase;
GN   ORFNames=SPBC1683.04;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family. {ECO:0000305}.
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DR   EMBL; CU329671; CAB91166.1; -; Genomic_DNA.
DR   RefSeq; NP_595060.1; NM_001020966.2.
DR   AlphaFoldDB; Q9P6J6; -.
DR   SMR; Q9P6J6; -.
DR   BioGRID; 276702; 11.
DR   STRING; 4896.SPBC1683.04.1; -.
DR   CAZy; GH3; Glycoside Hydrolase Family 3.
DR   MaxQB; Q9P6J6; -.
DR   PaxDb; Q9P6J6; -.
DR   EnsemblFungi; SPBC1683.04.1; SPBC1683.04.1:pep; SPBC1683.04.
DR   GeneID; 2540167; -.
DR   KEGG; spo:SPBC1683.04; -.
DR   PomBase; SPBC1683.04; -.
DR   VEuPathDB; FungiDB:SPBC1683.04; -.
DR   eggNOG; ENOG502QR4D; Eukaryota.
DR   HOGENOM; CLU_004542_4_0_1; -.
DR   InParanoid; Q9P6J6; -.
DR   OMA; GPTINTQ; -.
DR   PhylomeDB; Q9P6J6; -.
DR   PRO; PR:Q9P6J6; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
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:0044275; P:cellular carbohydrate catabolic process; IC:PomBase.
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   Cytoplasm; Glycosidase; Hydrolase; Reference proteome.
FT   CHAIN           1..832
FT                   /note="Putative beta-glucosidase"
FT                   /id="PRO_0000363374"
FT   DOMAIN          397..556
FT                   /note="PA14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01164"
FT   ACT_SITE        225
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   832 AA;  93169 MW;  24C8EF2B248BB02F CRC64;
     MMEHDVEDLI NQLDISEKAM LLSGTDLWHT AAIPRLNIPS IRLSDGPNGI RGTSFFNSSP
     SACFPCGTAL GATFDKKLLF EVGEYLAEEA KAKGVSVVLG PTVNIHRGPL NGRGFESFSE
     DSTLSGLAAS YVILGLQSKN VQACIKHFVC NDMEDERNSV SIDVSQRALR EVYLMPFQLA
     CKYSNFKSLM TSYNKVNGEH VSQSRILLDN ILRKEWEWKG TIISDWFGTY SLKKAIDAGL
     DLEMPGKPRF RNVNTIQHLV GSKELSESIL DERAKNVLKL VKHSWQNTEA ENHCELNNDS
     SCLREALKKF ASQSIVLLKN KKKLLPLSRK GTFAVIGPNA KVCNYSGGGS ANLKPYYTVS
     MYDGIAAKID GVPEYALGCH NYLNLPNIAN LLVNPRTGKH GYVAKFYLEP ATSENRTLID
     DYDLEDGVVR FYDYCNDKMK DGYFYIDIEG YLIPDEDAVY EFGISVFGTA LLFIDDVLLI
     DNKTKQTPTN HTFEFGTIEE RNSIYLKKGR KYNVRVEYGS AATYTLSTNL SPSTGGRYSI
     GCVKVIDPET EIDYAVRVAK SVDCVILCVG LTAEWETEGE DRKTMTLPSL SDKLVYSILQ
     SNPNTVVVTQ SGTPIEMPWI SEAHTLLHIW YNGNELGNAL ANIIFGEQNP CGKLPITFPK
     KLKDNPAYLS FRSSRGHCVY GEDVFVGYKY YEAVEREVLF PFGYGLSYTT FELSNLYLKN
     CGERLRIDLE ISNTGPMSGA EIIQVYISQI VRSVNRPVKE LKEFSKVVLC PKETKLIRIE
     LDIKYATSFY DELNEKWCSE EGEYNVLVGT SSKDIALTGK FTLPKTIHWT GL