ID A0A0D3CKP2_BRAOL Unreviewed; 400 AA.
AC A0A0D3CKP2;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
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:Bo5g132800.1, ECO:0000313|Proteomes:UP000032141};
RN [1] {ECO:0000313|EnsemblPlants:Bo5g132800.1, 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:Bo5g132800.1}
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; A0A0D3CKP2; -.
DR STRING; 109376.A0A0D3CKP2; -.
DR EnsemblPlants; Bo5g132800.1; Bo5g132800.1; Bo5g132800.
DR Gramene; Bo5g132800.1; Bo5g132800.1; Bo5g132800.
DR eggNOG; KOG0626; Eukaryota.
DR HOGENOM; CLU_001859_3_0_1; -.
DR OMA; HSYNRGN; -.
DR Proteomes; UP000032141; Chromosome C5.
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:SF211; BETA-GLUCOSIDASE 10-RELATED; 1.
DR PANTHER; PTHR10353; GLYCOSYL HYDROLASE; 1.
DR Pfam; PF00232; Glyco_hydro_1; 1.
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..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..400
FT /note="thioglucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002258790"
SQ SEQUENCE 400 AA; 45713 MW; 180F51B02052D941 CRC64;
MRAFSHLFFS FLVILFAISC SDAFTRNDFP EEFLFGAATS AYQWEGAVDE DGRTPSVWDT
FSHSYNRGNG DIACDGYHKY KEDVKLMAEM GLEAFRFSIS WTRLIPKGRG HINPKGLLFY
KNLIQELRTH GIKPHVTLYH YDLPQSLEDE YGGWINRKII KDFTAFADVC FREFGDDVKL
WTTINEANIF AIASYSEGFA PPGHCSPTSF FNCSTGNSST EPYLAGHNML LAHASASKLY
KLEYKSKQRG SIGLSIYAFG LTPYSNSKED EIATQRAKDF LFGWMLKPLV FGDYPDAMKR
VWGSRLPVFS EEESEKVKGS SDFVGIIHYT TVYVRNSTST TPSLIPRRQD FFTDMGAETI
CKIYFLFHSS MDQNMASWFL YLIKYSCSSF WISHGEFYIL
//
