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Database: UniProt
Entry: G3AZH6_CANTC
LinkDB: G3AZH6_CANTC
Original site: G3AZH6_CANTC 
ID   G3AZH6_CANTC            Unreviewed;       838 AA.
AC   G3AZH6;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 48.
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   ORFNames=CANTEDRAFT_101864 {ECO:0000313|EMBL:EGV65580.1};
OS   Candida tenuis (strain ATCC 10573 / BCRC 21748 / CBS 615 / JCM 9827 / NBRC
OS   10315 / NRRL Y-1498 / VKM Y-70) (Yeast) (Yamadazyma tenuis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Yamadazyma.
OX   NCBI_TaxID=590646 {ECO:0000313|Proteomes:UP000000707};
RN   [1] {ECO:0000313|EMBL:EGV65580.1, ECO:0000313|Proteomes:UP000000707}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10573 / BCRC 21748 / CBS 615 / JCM 9827 / NBRC 10315 /
RC   NRRL Y-1498 / VKM Y-70 {ECO:0000313|Proteomes:UP000000707};
RX   PubMed=21788494; DOI=10.1073/pnas.1103039108;
RA   Wohlbach D.J., Kuo A., Sato T.K., Potts K.M., Salamov A.A., LaButti K.M.,
RA   Sun H., Clum A., Pangilinan J.L., Lindquist E.A., Lucas S., Lapidus A.,
RA   Jin M., Gunawan C., Balan V., Dale B.E., Jeffries T.W., Zinkel R.,
RA   Barry K.W., Grigoriev I.V., Gasch A.P.;
RT   "Comparative genomics of xylose-fermenting fungi for enhanced biofuel
RT   production.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:13212-13217(2011).
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; GL996512; EGV65580.1; -; Genomic_DNA.
DR   RefSeq; XP_006684154.1; XM_006684091.1.
DR   AlphaFoldDB; G3AZH6; -.
DR   STRING; 590646.G3AZH6; -.
DR   GeneID; 18245508; -.
DR   KEGG; cten:CANTEDRAFT_101864; -.
DR   eggNOG; ENOG502QR4D; Eukaryota.
DR   HOGENOM; CLU_004542_4_0_1; -.
DR   OrthoDB; 5486783at2759; -.
DR   UniPathway; UPA00696; -.
DR   Proteomes; UP000000707; Unassembled WGS sequence.
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:UP000000707}.
FT   DOMAIN          398..560
FT                   /note="PA14"
FT                   /evidence="ECO:0000259|PROSITE:PS51820"
SQ   SEQUENCE   838 AA;  93035 MW;  06CEF331B6BF7174 CRC64;
     MADIDVEYTL SQLELSEKIG LIAGIDFWHT FAVKRLNIPS LRLSDGPNGT RGTRFFDGVP
     AACFPCGTGL GSTFNKELLQ KAGQLMGVEA KHKGAHVILG PTTNMQRGPL GGRGFESFSE
     DPYLAGIASA AIINGIQDED IAATIKHFVC NDLENERQSS DVIVTQRALR EIYLEPFRLA
     IKYSNPACFM TAYNKVNGTH VSNNSKILKD ILRDEWKFEG LVMSDWFGVY TSEKAIQSGL
     DLEMPGPTIF RSVEIIKHMI ESRELHIDDL DDRVRNVLNL VKWCAKSGVP ENGEEDTDND
     TKETSALLRQ IAAESVVLLK NEDNVLPLKK DDKIAVIGPN AKYPAYSGGG SASLRPYYTT
     TPFESISKKL STTPEYTVGA YAFKSMPSLA TQLTNFSTGK TGYNMKFYKH PRDYKGDREN
     IDELNINTSF IFLVDYKNDK LDSNLYYIDI EGDFVPESSG EYEFGLTVQG TALLYVNDQL
     VVDNKTKQEK GEAFFNMGST EITNKINLKG GEKYRVRVEF GSAPTFTASN GENVDFGGGG
     GLFFGCAKVI DDDEEIANAV KLAKSVDKVV LAIGLNQEWE SEGYDRKDMD LPLRTNDLVE
     AVLKANPNTV IVNQSGTPVE MPWLSKAKGL LQAWYGGNEG GNGIADVLFG DHNPSGKLSL
     TFPFKNIDNP AYLNFKTERG RVLYGEDIFI GYRYYDKLQK KVAFPFGYGL SYTNFEYSDL
     KINVDEAKDK LTASLSVKNV GKVDGAEVVQ LYISHKGGKT ILPVKELKGF EKVSIKAGKS
     VTVSFDLCLK DTCSWFDEYF DKWILETGDY EVQIGKSSDD IELIAPFEIK NQKLWKGI
//
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