ID A0A0D3BPU5_BRAOL Unreviewed; 200 AA.
AC A0A0D3BPU5;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
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:Bo4g021750.1, ECO:0000313|Proteomes:UP000032141};
RN [1] {ECO:0000313|EnsemblPlants:Bo4g021750.1, 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:Bo4g021750.1}
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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
CC {ECO:0000256|ARBA:ARBA00010838, ECO:0000256|RuleBase:RU003690}.
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DR AlphaFoldDB; A0A0D3BPU5; -.
DR STRING; 109376.A0A0D3BPU5; -.
DR EnsemblPlants; Bo4g021750.1; Bo4g021750.1; Bo4g021750.
DR Gramene; Bo4g021750.1; Bo4g021750.1; Bo4g021750.
DR eggNOG; KOG0626; Eukaryota.
DR HOGENOM; CLU_001859_3_0_1; -.
DR OMA; WEIFICK; -.
DR Proteomes; UP000032141; Chromosome C4.
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; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR10353; GLYCOSYL HYDROLASE; 1.
DR PANTHER; PTHR10353:SF281; THIOGLUCOSIDASE; 1.
DR Pfam; PF00232; Glyco_hydro_1; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000032141}.
SQ SEQUENCE 200 AA; 21986 MW; 8D0F0D58DCF97903 CRC64;
MPFSDNGYTS GIKPFATIFH WDTPQSLEDA FGGFRGAEIV NDFQNYADIC FKNFGDRVKH
WMTLNEPLTV VQQGYVAGGM APGRCSNFTK SNCKGGDGIT EPYIVGHNLL LAHGAAVKVY
REKYKASQKG QVGIALSAGW YLPYTESAAD RLAAARIMAF TFDYFLEPLV TGKYPVDMVN
NVKGGRLPTF TAQQSKMLKG
//
