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Database: UniProt
Entry: A0A061EYK8_THECC
LinkDB: A0A061EYK8_THECC
Original site: A0A061EYK8_THECC 
ID   A0A061EYK8_THECC        Unreviewed;       494 AA.
AC   A0A061EYK8;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=Beta-glucosidase {ECO:0000256|ARBA:ARBA00012744, ECO:0000256|RuleBase:RU361175};
DE            EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744, ECO:0000256|RuleBase:RU361175};
GN   ORFNames=TCM_025115 {ECO:0000313|EMBL:EOY09723.1};
OS   Theobroma cacao (Cacao) (Cocoa).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Byttnerioideae; Theobroma.
OX   NCBI_TaxID=3641 {ECO:0000313|EMBL:EOY09723.1, ECO:0000313|Proteomes:UP000026915};
RN   [1] {ECO:0000313|EMBL:EOY09723.1, ECO:0000313|Proteomes:UP000026915}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Matina 1-6 {ECO:0000313|Proteomes:UP000026915};
RX   PubMed=23731509; DOI=10.1186/gb-2013-14-6-r53;
RA   Motamayor J.C., Mockaitis K., Schmutz J., Haiminen N., Iii D.L.,
RA   Cornejo O., Findley S.D., Zheng P., Utro F., Royaert S., Saski C.,
RA   Jenkins J., Podicheti R., Zhao M., Scheffler B.E., Stack J.C., Feltus F.A.,
RA   Mustiga G.M., Amores F., Phillips W., Marelli J.P., May G.D., Shapiro H.,
RA   Ma J., Bustamante C.D., Schnell R.J., Main D., Gilbert D., Parida L.,
RA   Kuhn D.N.;
RT   "The genome sequence of the most widely cultivated cacao type and its use
RT   to identify candidate genes regulating pod color.";
RL   Genome Biol. 14:R53.1-R53.24(2013).
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|RuleBase:RU361175};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
CC       {ECO:0000256|ARBA:ARBA00010838, ECO:0000256|RuleBase:RU361175}.
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DR   EMBL; CM001883; EOY09723.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A061EYK8; -.
DR   EnsemblPlants; EOY09723; EOY09723; TCM_025115.
DR   Gramene; EOY09723; EOY09723; TCM_025115.
DR   eggNOG; KOG0626; Eukaryota.
DR   HOGENOM; CLU_001859_1_3_1; -.
DR   InParanoid; A0A061EYK8; -.
DR   OMA; IGYCAWS; -.
DR   Proteomes; UP000026915; Chromosome 5.
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:InterPro.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR001360; Glyco_hydro_1.
DR   InterPro; IPR017736; Glyco_hydro_1_beta-glucosidase.
DR   InterPro; IPR033132; Glyco_hydro_1_N_CS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   NCBIfam; TIGR03356; BGL; 1.
DR   PANTHER; PTHR10353:SF210; BETA-GLUCOSIDASE; 1.
DR   PANTHER; PTHR10353; GLYCOSYL HYDROLASE; 1.
DR   Pfam; PF00232; Glyco_hydro_1; 1.
DR   PRINTS; PR00131; GLHYDRLASE1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|RuleBase:RU361175};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361175};
KW   Reference proteome {ECO:0000313|Proteomes:UP000026915}.
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        188
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-1"
FT   ACT_SITE        392
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-1"
FT   BINDING         40
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT   BINDING         142
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT   BINDING         187
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT   BINDING         321
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT   BINDING         441
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT   BINDING         448..449
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
SQ   SEQUENCE   494 AA;  56001 MW;  C43501537EF04B8C CRC64;
     MAKKKHVLKE DEEGGSSSKQ VSREDFPPDF VFGVATSSYQ IEGGCKEGGR GASIWDVFAH
     TEGKIIDGSN ADEAVDHYHR YKEDIDLISE LGFSAYRFSI SWPRIFPDGL GTKVNEEGIA
     FYNNVIDALL EKDIEPYVTL HHWDLPLHLH DSMGGWLNKQ IVEYFAIYAD TCFAHFGDRV
     KTWTTINEPL HIAVGGYDTG TSAPGRSENS STETYLAAHH MILANAAAVS LYHSKYKDKQ
     GGQIGIVLDC EWAEANSEKL EDKCAAVRRV EFQLGWFLHP LYFGDYPKSM RERLGDQLPE
     FTEEDQELLS SFMDFVGLNQ YTSRLVSHAA ESAEEGHFHK AQQIEKIVEW EDGEMIGEKA
     ASDWLYVVPW GMRKVLNYIA DAYSNLPIYI TENGMDDEEN DTAPLPEMLD DKLRVRFYKG
     YLAAVAQAIN DGVDVRGYFA WSLLDNFEWS HGYTKRFGLV YVDYKNGLTR HPKSSAMWFK
     QFLKGGGSNK DNEE
//
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