ID A0A0D3DLW1_BRAOL Unreviewed; 545 AA.
AC A0A0D3DLW1;
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};
GN Name=106309978 {ECO:0000313|EnsemblPlants:Bo8g039420.1};
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:Bo8g039420.1, ECO:0000313|Proteomes:UP000032141};
RN [1] {ECO:0000313|EnsemblPlants:Bo8g039420.1, 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:Bo8g039420.1}
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_013602611.1; XM_013747157.1.
DR AlphaFoldDB; A0A0D3DLW1; -.
DR EnsemblPlants; Bo8g039420.1; Bo8g039420.1; Bo8g039420.
DR GeneID; 106309978; -.
DR Gramene; Bo8g039420.1; Bo8g039420.1; Bo8g039420.
DR KEGG; boe:106309978; -.
DR eggNOG; KOG0626; Eukaryota.
DR HOGENOM; CLU_001859_1_0_1; -.
DR OMA; MRFLVED; -.
DR OrthoDB; 648908at2759; -.
DR Proteomes; UP000032141; Chromosome C8.
DR ExpressionAtlas; A0A0D3DLW1; baseline.
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:SF228; THIOGLUCOSIDASE; 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 Signal {ECO:0000256|SAM:SignalP}; Vacuole {ECO:0000256|ARBA:ARBA00022554}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..545
FT /note="thioglucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002274513"
FT ACT_SITE 427
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10055"
SQ SEQUENCE 545 AA; 62320 MW; 55607ABD65603D67 CRC64;
MKHLGLILAF LLALATCKAD EEITCEENLP FKCSQPDRLN SSSFEKDFIF GVASSAYQIE
GCLGRGLNVW DGFTHRYPNK SGPDHGNGDT TCDSFSYWQK DIDVLDELNA TGYRFSIAWS
RIIPRGKRSR GVNKDGINYY HGLIDGLIDK GITPFVTLFH WDLPQVLQDE YEGFLDPQII
HDFKDYANLC FQEFGHKVKN WLTINQLYTV PTRGYGAGSD APGRCSPMVD PTCYAGNSST
EPYIVAHNQL LAHATVVDLY RKNYSHQGGK IGPVMITRWF LPYNDTDPDS IAATERMKEF
FLGWFMGPLT NGTYPQIMID TVGERLPSFS PEESNLVKGS YDYLGLNYYV TQYAQPSHNP
VHWANHTAMM DAGAKLTYIN ASNHSIGPLF EANSDETKNS YYYPKGIYYV MDYFKTKYYN
PLIYVTENGI STPGNETRDE SMFDYKRIEY LCSHLCFLSK VIKEKHVNVK GYFAWSLGDN
YEFCKGFTVR FGLSYIDWNN VTDRDLKLSG KWYQKFISPA IKNPLKKDFL RSSLTFEKNK
KFEDA
//
