ID A0A0D3E2W7_BRAOL Unreviewed; 136 AA.
AC A0A0D3E2W7;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=thioglucosidase {ECO:0000256|ARBA:ARBA00012250};
DE EC=3.2.1.147 {ECO:0000256|ARBA:ARBA00012250};
DE AltName: Full=Sinigrinase {ECO:0000256|ARBA:ARBA00032643};
DE AltName: Full=Thioglucosidase {ECO:0000256|ARBA:ARBA00032797};
OS Brassica oleracea var. oleracea.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=109376 {ECO:0000313|EnsemblPlants:Bo9g022660.1, ECO:0000313|Proteomes:UP000032141};
RN [1] {ECO:0000313|EnsemblPlants:Bo9g022660.1, ECO:0000313|Proteomes:UP000032141}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. TO1000 {ECO:0000313|Proteomes:UP000032141};
RX PubMed=24916971; DOI=10.1186/gb-2014-15-6-r77;
RA Parkin I.A., Koh C., Tang H., Robinson S.J., Kagale S., Clarke W.E.,
RA Town C.D., Nixon J., Krishnakumar V., Bidwell S.L., Denoeud F., Belcram H.,
RA Links M.G., Just J., Clarke C., Bender T., Huebert T., Mason A.S.,
RA Pires J.C., Barker G., Moore J., Walley P.G., Manoli S., Batley J.,
RA Edwards D., Nelson M.N., Wang X., Paterson A.H., King G., Bancroft I.,
RA Chalhoub B., Sharpe A.G.;
RT "Transcriptome and methylome profiling reveals relics of genome dominance
RT in the mesopolyploid Brassica oleracea.";
RL Genome Biol. 15:R77-R77(2014).
RN [2] {ECO:0000313|EnsemblPlants:Bo9g022660.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2015) to UniProtKB.
CC -!- FUNCTION: Degradation of glucosinolates (glucose residue linked by a
CC thioglucoside bound to an amino acid derivative) to glucose, sulfate
CC and any of the products: thiocyanates, isothiocyanates, nitriles,
CC epithionitriles or oxazolidine-2-thiones.
CC {ECO:0000256|ARBA:ARBA00003014}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a thioglucoside + H2O = a sugar + a thiol.; EC=3.2.1.147;
CC Evidence={ECO:0000256|ARBA:ARBA00034026};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000256|ARBA:ARBA00004116}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
CC {ECO:0000256|ARBA:ARBA00010838, ECO:0000256|RuleBase:RU003690}.
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DR AlphaFoldDB; A0A0D3E2W7; -.
DR STRING; 109376.A0A0D3E2W7; -.
DR EnsemblPlants; Bo9g022660.1; Bo9g022660.1; Bo9g022660.
DR Gramene; Bo9g022660.1; Bo9g022660.1; Bo9g022660.
DR eggNOG; KOG0626; Eukaryota.
DR HOGENOM; CLU_001859_6_0_1; -.
DR OMA; KDNYANP; -.
DR Proteomes; UP000032141; Chromosome C9.
DR GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
DR GO; GO:0102799; F:glucosinolate glucohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0019137; F:thioglucosidase activity; IEA:UniProtKB-EC.
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; GLYCOSYL HYDROLASE; 1.
DR PANTHER; PTHR10353:SF218; MYROSINASE 1-RELATED; 1.
DR Pfam; PF00232; Glyco_hydro_1; 1.
DR PRINTS; PR00131; GLHYDRLASE1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR PROSITE; PS00572; GLYCOSYL_HYDROL_F1_1; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000032141};
KW Vacuole {ECO:0000256|ARBA:ARBA00022554}.
FT ACT_SITE 17
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10055"
SQ SEQUENCE 136 AA; 15873 MW; C250399ADCD4EAF2 CRC64;
MDYFKNKYNN PLIYITENGF STPGEETRCK AVADSKRIDY LCSHLCFLRK VIKEKGVNIK
GYFAWALGDN YEFCKGFTVR FGLSYVNWTN LDDRNLKESG KWYQSFINGT TKNPAKQDFR
RPNLSLRNQK KNLADA
//
