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 27-MAR-2024, entry version 132.
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; 284812.Q9P6J6; -.
DR CAZy; GH3; Glycoside Hydrolase Family 3.
DR MaxQB; Q9P6J6; -.
DR PaxDb; 4896-SPBC1683-04-1; -.
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; TYYVDME; -.
DR PhylomeDB; Q9P6J6; -.
DR PRO; PR:Q9P6J6; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0043227; C:membrane-bounded organelle; IEA:UniProt.
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:0044248; P:cellular catabolic process; NAS:PomBase.
DR GO; GO:0009251; P:glucan catabolic process; IBA:GO_Central.
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; 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 PANTHER; PTHR42715; BETA-GLUCOSIDASE; 1.
DR PANTHER; PTHR42715:SF28; BETA-GLUCOSIDASE-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; 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
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