ID A0A1B6PC92_SORBI Unreviewed; 501 AA.
AC A0A1B6PC92;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Beta-glucosidase {ECO:0008006|Google:ProtNLM};
GN ORFNames=SORBI_3008G080600 {ECO:0000313|EMBL:KXG23299.1};
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:KXG23299.1, ECO:0000313|Proteomes:UP000000768};
RN [1] {ECO:0000313|EMBL:KXG23299.1, 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=DIBOA beta-D-glucoside + H2O = D-glucose + DIBOA;
CC Xref=Rhea:RHEA:33979, ChEBI:CHEBI:4167, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:63558, ChEBI:CHEBI:63670; EC=3.2.1.182;
CC Evidence={ECO:0000256|ARBA:ARBA00001037};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=DIMBOA beta-D-glucoside + H2O = D-glucose + DIMBOA;
CC Xref=Rhea:RHEA:33975, ChEBI:CHEBI:4167, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:18048, ChEBI:CHEBI:37573; EC=3.2.1.182;
CC Evidence={ECO:0000256|ARBA:ARBA00001799};
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 -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000256|ARBA:ARBA00004229}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
CC {ECO:0000256|ARBA:ARBA00010838, ECO:0000256|RuleBase:RU003690}.
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DR EMBL; CM000767; KXG23299.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B6PC92; -.
DR EnsemblPlants; KXG23299; KXG23299; SORBI_3008G080600.
DR Gramene; KXG23299; KXG23299; SORBI_3008G080600.
DR eggNOG; KOG0626; Eukaryota.
DR InParanoid; A0A1B6PC92; -.
DR OMA; CHEYPER; -.
DR Proteomes; UP000000768; Chromosome 8.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0008422; F:beta-glucosidase activity; IBA:GO_Central.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR001360; Glyco_hydro_1.
DR InterPro; IPR018120; Glyco_hydro_1_AS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR10353:SF326; 4-HYDROXY-7-METHOXY-3-OXO-3,4-DIHYDRO-2H-1,4-BENZOXAZIN-2-YL GLUCOSIDE BETA-D-GLUCOSIDASE 2, CHLOROPLASTIC; 1.
DR PANTHER; PTHR10353; GLYCOSYL HYDROLASE; 1.
DR Pfam; PF00232; Glyco_hydro_1; 2.
DR PRINTS; PR00131; GLHYDRLASE1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR PROSITE; PS00572; GLYCOSYL_HYDROL_F1_1; 1.
PE 3: Inferred from homology;
KW Chloroplast {ECO:0000256|ARBA:ARBA00022528};
KW Plastid {ECO:0000256|ARBA:ARBA00022640};
KW Reference proteome {ECO:0000313|Proteomes:UP000000768};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT REGION 12..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 404
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10055"
SQ SEQUENCE 501 AA; 56987 MW; 4474F2F81D81BEB4 CRC64;
MALLLASAMN HSAHPAGLRS QSNNQSFSRH HLCSSPKNIS KRRCKLSFRP RAERVGSENG
NHRLSPREIP RKDWFPPSFL VSAATSAYHI EGAWNEDGKG PSTWDHFCHE YPERIADRSN
GDVAADSYHM YADDVKLLKE MGMDAYRFSI SWSRILPKGT IAGGINEKGV EYYNKLIDLL
LENGIEPYIT IFHWDTPQAL VDAYGGFLDD RIITDYTDFA KVCFQKFGTK VKNWFTFNEP
ETFCSVSYGT GVLAPGRCSP GVNCAVPTGN SLTEPYTVAH HLLLAHAETV DLYNKHHKGR
VPYTNTFLDQ QAQERSMDNC LGWFLEPVVR GDYPFSMRAS AKDRVPYFKE IEQEKLVGSY
DMIGIKLLHL NTGNAWINMY PKGLHDILMT MKNKYGNPPM YITENGIGDI DKGDLPKALA
LEDHTRLDYI QRHLSVLKQS IDLGANVRGY FAWSLLDNFE WSSGYTERFG IVYVDRDNGC
ERTMKRSAWW LQEFNGAAMK R
//
