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Database: UniProt
Entry: G8Y9J6_PICSO
LinkDB: G8Y9J6_PICSO
Original site: G8Y9J6_PICSO 
ID   G8Y9J6_PICSO            Unreviewed;       834 AA.
AC   G8Y9J6;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744, ECO:0000256|RuleBase:RU361161};
DE            EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744, ECO:0000256|RuleBase:RU361161};
GN   Name=Piso0_004713 {ECO:0000313|EMBL:CCE84110.1};
GN   ORFNames=GNLVRS01_PISO0K22934g {ECO:0000313|EMBL:CCE84110.1},
GN   GNLVRS01_PISO0L22935g {ECO:0000313|EMBL:CCE85141.1};
OS   Pichia sorbitophila (strain ATCC MYA-4447 / BCRC 22081 / CBS 7064 / NBRC
OS   10061 / NRRL Y-12695) (Hybrid yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Millerozyma.
OX   NCBI_TaxID=559304 {ECO:0000313|EMBL:CCE84110.1, ECO:0000313|Proteomes:UP000005222};
RN   [1] {ECO:0000313|EMBL:CCE84110.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Genoscope - CEA;
RL   Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000005222}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4447 / BCRC 22081 / CBS 7064 / NBRC 10061 / NRRL
RC   Y-12695 {ECO:0000313|Proteomes:UP000005222};
RX   DOI=10.1534/g3.111.000745;
RA   Leh Louis V., Despons L., Friedrich A., Martin T., Durrens P.,
RA   Casaregola S., Neuveglise C., Fairhead C., Marck C., Cruz J.A.,
RA   Straub M.L., Kugler V., Sacerdot C., Uzunov Z., Thierry A., Weiss S.,
RA   Bleykasten C., De Montigny J., Jacques N., Jung P., Lemaire M., Mallet S.,
RA   Morel G., Richard G.F., Sarkar A., Savel G., Schacherer J., Seret M.L.,
RA   Talla E., Samson G., Jubin C., Poulain J., Vacherie B., Barbe V.,
RA   Pelletier E., Sherman D.J., Westhof E., Weissenbach J., Baret P.V.,
RA   Wincker P., Gaillardin C., Dujon B., Souciet J.L.;
RT   "Pichia sorbitophila, an interspecies yeast hybrid reveals early steps of
RT   genome resolution following polyploidization.";
RL   G3 (Bethesda) 2:299-311(2012).
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         Evidence={ECO:0000256|ARBA:ARBA00000448,
CC         ECO:0000256|RuleBase:RU361161};
CC   -!- PATHWAY: Glycan metabolism; cellulose degradation.
CC       {ECO:0000256|RuleBase:RU361161}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC       {ECO:0000256|ARBA:ARBA00005336, ECO:0000256|RuleBase:RU361161}.
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DR   EMBL; FO082049; CCE84110.1; -; Genomic_DNA.
DR   EMBL; FO082048; CCE85141.1; -; Genomic_DNA.
DR   AlphaFoldDB; G8Y9J6; -.
DR   STRING; 559304.G8Y9J6; -.
DR   eggNOG; ENOG502QR4D; Eukaryota.
DR   HOGENOM; CLU_004542_4_0_1; -.
DR   InParanoid; G8Y9J6; -.
DR   OMA; YCSENSD; -.
DR   UniPathway; UPA00696; -.
DR   Proteomes; UP000005222; Chromosome K.
DR   Proteomes; UP000005222; Chromosome L.
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; 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; 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   Carbohydrate metabolism {ECO:0000256|RuleBase:RU361161};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361161};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361161};
KW   Polysaccharide degradation {ECO:0000256|RuleBase:RU361161};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005222}.
FT   DOMAIN          397..558
FT                   /note="PA14"
FT                   /evidence="ECO:0000259|PROSITE:PS51820"
SQ   SEQUENCE   834 AA;  92241 MW;  038EF115298D51BD CRC64;
     MGEFDIEQVL SQLTLHEKIS LLSGIDFWHT FPVHRLDIPS LRFSDGPNGV RGTKFFNGVP
     SACFPCGTAL ASTFDKQLLL DIGRLMGEEA IHKSVHVVLG PTTNMQRGPL GGRGFESFSE
     DPYLAGMASA SIINGIQDKK VAATIKHFVG NDLEDQRNSS NSIITERALR EIYLEPFRIA
     VKLSNPMAVM TGYNRLNGEH VSQSEKLLQD ILRDEWKWDG TIMSDWFGTY STKEALANGL
     DIEMPGPTRF RNPDPVAHSV NTKELHSKVI DERARNVLKL IKYTKMLNLP ENGPESDSNN
     TPQTQKLLKE VAADSIVLLK NEDVLPLNKN SSIAVIGPNA KYAAYCGGGS AALRSYYSVT
     PFEGIAKKMT SSPKYALGAM GVKSLQGLAE NLTNPFTGKR GYNMKFFKEP SSSSHRELVD
     ELNLDLSHVF LADYKNPKLD SNLYFIDFEG DLVVNESGEY AFGISVYGTA QLFVDGKLLV
     DNKTSQSRGD SFFNSGTSEK KGTIFLEKGK EYKIRVEFGS APSYTLVNAG VVEFGGGGGV
     NLGFSKVYEK DEEIKKAVEV AKSVDNVVLC IGLNQEWESE SFDRPDMNLP PNTDELVEAV
     INANPNTIVV NQSGTPVELP WVSKAKGLIQ AWFGGNELGN ALADVLFGDT NPSGKLSLSF
     PKVLEDNPTY LNFKTEMGRV LYGEDIYIGY RFYQKMRRDV AFPFGFGLSY TSFGYSDLNI
     ELSEDKLDVT IKVKNNGPYK GKDVPQLYIS ALNSAVSRPV RELKGFEKIE LESGESTLVH
     FDLPLKECIS YFDEYMNQWC AEAGAYTVEI GKSSEDIVLH SDFAVKETTY WLGA
//
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