ID A0A0D3C687_BRAOL Unreviewed; 533 AA.
AC A0A0D3C687;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
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};
GN Name=106340598 {ECO:0000313|EnsemblPlants:Bo4g195000.1};
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:Bo4g195000.1, ECO:0000313|Proteomes:UP000032141};
RN [1] {ECO:0000313|EnsemblPlants:Bo4g195000.1, 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:Bo4g195000.1}
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 RefSeq; XP_013634904.1; XM_013779450.1.
DR AlphaFoldDB; A0A0D3C687; -.
DR STRING; 109376.A0A0D3C687; -.
DR EnsemblPlants; Bo4g195000.1; Bo4g195000.1; Bo4g195000.
DR GeneID; 106340598; -.
DR Gramene; Bo4g195000.1; Bo4g195000.1; Bo4g195000.
DR KEGG; boe:106340598; -.
DR eggNOG; KOG0626; Eukaryota.
DR HOGENOM; CLU_001859_1_0_1; -.
DR OMA; SEWGWTI; -.
DR OrthoDB; 640576at2759; -.
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; IPR033132; Glyco_hydro_1_N_CS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR10353; GLYCOSYL HYDROLASE; 1.
DR PANTHER; PTHR10353:SF288; THIOGLUCOSIDASE; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000032141};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..533
FT /note="thioglucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002273595"
SQ SEQUENCE 533 AA; 61894 MW; 9B6A1BA48717B21C CRC64;
MAIKLALVVT LLLVSCAISK GRSLRFSTKQ LDRYSFPPGF SFGVGSSAYQ YEGAVAEGGR
TPSIWDNFTH AYPERTNMEN GDIAVDFYHR YKDDIKLIKK MNMDTFRFSI SWSRILPSGK
LSGGINKVGI QFYKNLIDEI IKNGIKPFVT IYHWDIPQAL DDEYGGFLSP RIIDDFRNFA
RVCFQEFGDK VDMWITFNEP YIYSVAGYDK GNKAMGRCSK WVNSLCVAGD SSIEPYLVSH
HLLLAHAAAV DEFRNCDKIS QDGKIGIVLS PFWVEPYDVD SDADKEAVER ALDYYLGWHL
DPLIFGDYPK TLRKNAGNRL PSFTQKQSEM IKDSFDFIGI NYYSARYVTR QLRSDPSRLR
FTTDQHVEYK VKNRSGDYIS TESDELGFIY VYPEGIRKLL NHIKNKYNNP TIYITENGYD
DYDVGTKPRE QLLKDIKRIE YHEQHLQELH KAITVDGCDV RGYSTWSLLD NFEWERGYTM
RFGLYYVDYA DDLKRYAKDS AKWFKKFLEK REQSTPLDMY KSIKKWLSVL QTI
//
