ID C5X143_SORBI Unreviewed; 636 AA.
AC C5X143;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=SORBI_3001G089300 {ECO:0000313|EMBL:EER93454.1};
OS Sorghum bicolor (Sorghum) (Sorghum vulgare).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Sorghinae; Sorghum.
OX NCBI_TaxID=4558 {ECO:0000313|EMBL:EER93454.1, ECO:0000313|Proteomes:UP000000768};
RN [1] {ECO:0000313|EMBL:EER93454.1, ECO:0000313|Proteomes:UP000000768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX PubMed=19189423; DOI=10.1038/nature07723;
RA Paterson A.H., Bowers J.E., Bruggmann R., Dubchak I., Grimwood J.,
RA Gundlach H., Haberer G., Hellsten U., Mitros T., Poliakov A., Schmutz J.,
RA Spannagl M., Tang H., Wang X., Wicker T., Bharti A.K., Chapman J.,
RA Feltus F.A., Gowik U., Grigoriev I.V., Lyons E., Maher C.A., Martis M.,
RA Narechania A., Otillar R.P., Penning B.W., Salamov A.A., Wang Y., Zhang L.,
RA Carpita N.C., Freeling M., Gingle A.R., Hash C.T., Keller B., Klein P.,
RA Kresovich S., McCann M.C., Ming R., Peterson D.G., Mehboob-ur-Rahman,
RA Ware D., Westhoff P., Mayer K.F., Messing J., Rokhsar D.S.;
RT "The Sorghum bicolor genome and the diversification of grasses.";
RL Nature 457:551-556(2009).
RN [2] {ECO:0000313|Proteomes:UP000000768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX PubMed=29161754; DOI=10.1111/tpj.13781;
RA McCormick R.F., Truong S.K., Sreedasyam A., Jenkins J., Shu S., Sims D.,
RA Kennedy M., Amirebrahimi M., Weers B.D., McKinley B., Mattison A.,
RA Morishige D.T., Grimwood J., Schmutz J., Mullet J.E.;
RT "The Sorghum bicolor reference genome: improved assembly, gene annotations,
RT a transcriptome atlas, and signatures of genome organization.";
RL Plant J. 93:338-354(2018).
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};
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DR EMBL; CM000760; EER93454.1; -; Genomic_DNA.
DR RefSeq; XP_002466456.1; XM_002466411.1.
DR AlphaFoldDB; C5X143; -.
DR STRING; 4558.C5X143; -.
DR EnsemblPlants; EER93454; EER93454; SORBI_3001G089300.
DR GeneID; 8085936; -.
DR Gramene; EER93454; EER93454; SORBI_3001G089300.
DR KEGG; sbi:8085936; -.
DR eggNOG; ENOG502QQ55; Eukaryota.
DR HOGENOM; CLU_004542_9_3_1; -.
DR InParanoid; C5X143; -.
DR OMA; VNDTYAC; -.
DR OrthoDB; 5485475at2759; -.
DR Proteomes; UP000000768; Chromosome 1.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0008422; F:beta-glucosidase activity; IBA:GO_Central.
DR GO; GO:0009251; P:glucan catabolic process; IBA:GO_Central.
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 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 PANTHER; PTHR30620:SF46; GLYCOSYL HYDROLASE FAMILY 3 N TERMINAL DOMAIN CONTAINING PROTEIN, EXPRESSED; 1.
DR PANTHER; PTHR30620; PERIPLASMIC BETA-GLUCOSIDASE-RELATED; 1.
DR Pfam; PF00933; Glyco_hydro_3; 1.
DR Pfam; PF01915; Glyco_hydro_3_C; 1.
DR PRINTS; PR00133; GLHYDRLASE3.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
PE 4: Predicted;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000000768};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..636
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002956654"
FT DOMAIN 50..379
FT /note="Glycoside hydrolase family 3 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00933"
FT DOMAIN 416..629
FT /note="Glycoside hydrolase family 3 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01915"
SQ SEQUENCE 636 AA; 69826 MW; 8DD57A6D9A3273DA CRC64;
MTRSTAATAV ACLVLAFLLP SAASAKERVK YKDPKQSVND RVQDLLSRMT LEEKIGQMSQ
IERANATTEV IEKYFVGSVL SGGGSVPAEK ASASVWQKMV TKMQKAALKT RLGIPIIYGI
DAVHGNNDVY NATIFPHNVG LGATRDAHLV KKIGEATAHE TRATGIPYTF APCVAVCRDP
RWGRCYESFS EETKLVQLMT SNMVAGLQGD VPKKHPKGVP FVGGSKKVAG CAKHFVGDGG
TTRGMDENNT ALSFHDLMRI HMPPYDNAVI KGISSVMISY SSWNGVKMHE NKFLITETLK
NKMDFRGFVI TDWQAVDRIT NPPHKHYYHS IKETIHAGID MVMIPYDYPE FVADLVKQVK
DGQIMLDRIN DAVSRILRVK FTMGLFEDPI PDPRLTKELG AQDHRALARE AVRKSLVLLK
NKKKGQKDPM LPLDKKAKKI LVAGSHAHDL GSQCGGWTIK WQGETGNNLT GVGTTILEAI
KKAVDKKTTV DYVERPDKDD LAKSASDYEY AVVAVGEPPY AETAGDSKNL TIPSPGPEVI
KDVCGLVKCV VLIVSGRPLV LQPYVDYMDA LVAAWLPGTE AEGITDVLFG DYGFTGKLPR
TWFKSVDQLP MNYGDKHYDP LFPFGFGLTT KAAGHK
//
