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Database: UniProt
Entry: A0A078J5J3_BRANA
LinkDB: A0A078J5J3_BRANA
Original site: A0A078J5J3_BRANA 
ID   A0A078J5J3_BRANA        Unreviewed;       528 AA.
AC   A0A078J5J3;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 30.
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=BnaC01g43700D {ECO:0000313|EMBL:CDY59555.1};
GN   ORFNames=DARMORV10_C01P42900.1 {ECO:0000313|EMBL:CAF2077208.1},
GN   GSBRNA2T00027371001 {ECO:0000313|EMBL:CDY59555.1};
OS   Brassica napus (Rape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=3708 {ECO:0000313|EMBL:CDY59555.1, ECO:0000313|Proteomes:UP000028999};
RN   [1] {ECO:0000313|EMBL:CDY59555.1, ECO:0000313|Proteomes:UP000028999}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Darmor-bzh {ECO:0000313|Proteomes:UP000028999};
RX   PubMed=25146293; DOI=10.1126/science.1253435;
RA   Chalhoub B., Denoeud F., Liu S., Parkin I.A., Tang H., Wang X., Chiquet J.,
RA   Belcram H., Tong C., Samans B., Correa M., Da Silva C., Just J.,
RA   Falentin C., Koh C.S., Le Clainche I., Bernard M., Bento P., Noel B.,
RA   Labadie K., Alberti A., Charles M., Arnaud D., Guo H., Daviaud C.,
RA   Alamery S., Jabbari K., Zhao M., Edger P.P., Chelaifa H., Tack D.,
RA   Lassalle G., Mestiri I., Schnel N., Le Paslier M.C., Fan G., Renault V.,
RA   Bayer P.E., Golicz A.A., Manoli S., Lee T.H., Thi V.H., Chalabi S., Hu Q.,
RA   Fan C., Tollenaere R., Lu Y., Battail C., Shen J., Sidebottom C.H.,
RA   Wang X., Canaguier A., Chauveau A., Berard A., Deniot G., Guan M., Liu Z.,
RA   Sun F., Lim Y.P., Lyons E., Town C.D., Bancroft I., Wang X., Meng J.,
RA   Ma J., Pires J.C., King G.J., Brunel D., Delourme R., Renard M., Aury J.M.,
RA   Adams K.L., Batley J., Snowdon R.J., Tost J., Edwards D., Zhou Y., Hua W.,
RA   Sharpe A.G., Paterson A.H., Guan C., Wincker P.;
RT   "Plant genetics. Early allopolyploid evolution in the post-Neolithic
RT   Brassica napus oilseed genome.";
RL   Science 345:950-953(2014).
RN   [2] {ECO:0000313|EMBL:CDY59555.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Genoscope - CEA;
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:CAF2077208.1}
RP   NUCLEOTIDE SEQUENCE.
RG   Genoscope - CEA;
RA   William W.;
RL   Submitted (JAN-2021) to the EMBL/GenBank/DDBJ databases.
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   EMBL; HG994365; CAF2077208.1; -; Genomic_DNA.
DR   EMBL; LK033778; CDY59555.1; -; Genomic_DNA.
DR   STRING; 3708.A0A078J5J3; -.
DR   PaxDb; 3708-A0A078J5J3; -.
DR   EnsemblPlants; CDY59555; CDY59555; GSBRNA2T00027371001.
DR   Gramene; CDY59555; CDY59555; GSBRNA2T00027371001.
DR   OMA; SYFLWSL; -.
DR   Proteomes; UP000028999; Unassembled WGS sequence.
DR   GO; GO:0008422; F:beta-glucosidase activity; IBA:GO_Central.
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   GO; GO:0019762; P:glucosinolate catabolic process; IBA:GO_Central.
DR   GO; GO:0009651; P:response to salt stress; IBA:GO_Central.
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:SF163; BETA-GLUCOSIDASE 19; 1.
DR   PANTHER; PTHR10353; GLYCOSYL HYDROLASE; 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.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028999};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..528
FT                   /note="thioglucosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5040561433"
SQ   SEQUENCE   528 AA;  60245 MW;  AA4DCA33B39D2386 CRC64;
     MKFPLLGLLL LVTLVGSPTR AEEGPVCPKT ETLSRASFPE GFMFGTATAS YQVEGAVNEG
     CRGPSLWDIY TKKFPHRVKN HNADVAVDFY HRFREDIKLM KKLNTDAFRL SIAWPRIFPH
     GRMEKGISKE GVQFYHDLID ELLKNDLTPL VTIFHWDMPA DLEDEYGGFL SERVVPDFVE
     YANFTFHEYG DKVKNWITFN EPWVFSRSGY DVGKKAPGRC SPYIKDFGHL CQDGRSGFEA
     YVVSHNLLVS HAEAVDAFRK CEKCKGGKIG IAHSPAWFEP EDVEGGQRTV DRVLDFIMGW
     HLDPTTYGDY PQSMKDAVGA RLPKFTKAQK AKLKGSADFV GINYYSSFYA KASEKPDYRQ
     PSWATDSLVE FEPKTVDGSV KIGSQPSTAK MAVYAAGLRK LVKYIKDRYG NPEIIITENG
     YGEDLGEKDT DHSVALNDHN RKYYHQRHLL ALHQAICEDK VNVTSYFVWS LMDNFEWQDG
     YTARFGLYYI DFQNNLTRME KESAKWFSEF LKPGLKQKSS KSTFSEEL
//
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