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Database: UniProt
Entry: A0A078GH46_BRANA
LinkDB: A0A078GH46_BRANA
Original site: A0A078GH46_BRANA 
ID   A0A078GH46_BRANA        Unreviewed;       615 AA.
AC   A0A078GH46;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 25.
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=BnaA05g30850D {ECO:0000313|EMBL:CDY24686.1};
GN   ORFNames=DARMORV10_A05P41510.1 {ECO:0000313|EMBL:CAF2102879.1},
GN   GSBRNA2T00027067001 {ECO:0000313|EMBL:CDY24686.1};
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:CDY24686.1, ECO:0000313|Proteomes:UP000028999};
RN   [1] {ECO:0000313|EMBL:CDY24686.1, 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:CDY24686.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Genoscope - CEA;
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:CAF2102879.1}
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   -!- 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}.
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DR   EMBL; HG994359; CAF2102879.1; -; Genomic_DNA.
DR   EMBL; LK032162; CDY24686.1; -; Genomic_DNA.
DR   RefSeq; XP_013750665.1; XM_013895211.1.
DR   STRING; 3708.A0A078GH46; -.
DR   PaxDb; 3708-A0A078GH46; -.
DR   EnsemblPlants; CDY24686; CDY24686; GSBRNA2T00027067001.
DR   GeneID; 106452997; -.
DR   Gramene; CDY24686; CDY24686; GSBRNA2T00027067001.
DR   KEGG; bna:106452997; -.
DR   OMA; ETSCDDN; -.
DR   OrthoDB; 359146at2759; -.
DR   Proteomes; UP000028999; Unassembled WGS sequence.
DR   GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
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   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:SF209; GALACTOLIPID GALACTOSYLTRANSFERASE SFR2, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR10353; GLYCOSYL HYDROLASE; 1.
DR   Pfam; PF00232; Glyco_hydro_1; 2.
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:UP000028999};
KW   Vacuole {ECO:0000256|ARBA:ARBA00022554}.
FT   ACT_SITE        428
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10055"
SQ   SEQUENCE   615 AA;  69932 MW;  BFE97E519A539328 CRC64;
     MSILTLLVKI AGLLGTITVG ANAVSYSRFR RRNLRNFRSP IDESKEVLAD FTSQEHNEGK
     FFFGLATAPA HAEDDLDDAW IRFAKETPCS AEDEEDKKAK RKKKVKLAVG AITKGLAKNT
     QGKEDNTVAD STPTKNVAAW HNTPHAEVRL KFWSDPDQEV KLAKDTGVTV FRMGVDWCRI
     MPKEPTKGIE EAVDYEALEH YKWILNRVRS NGMKVMLTLF HHSLPPWAAD YGGWKMEKTV
     DYFMDFTRLV VDSMFDLVDS WITFNEPHVF AMLTYMAGTW PGNTPDFLEM ATSTLPMGVF
     HRVMHWMAVA HSKAYDYIHA KTSLEKPLVG VAHHVSFMRP YGLFDVGSVT FSNSLTMFSY
     IDSICEKLDF IGINYYGQEA VCGVGLKLVE TDEYSESGRG VYPDGLYRVL LMFHQRYKHL
     NVPFIVTENG VSDETDVIRR PYMIEHLLAL YAAMLKGVPV LGYIFWTISD NWEWADGYGP
     KFGLVAVDRA NNLARTVRPS YHLFTKIVKS GKITRNDRSL AWEELQKAAK AGKVRPFYRA
     VDNHGLMYAD GLDKPQGRQF VDRDWRFGHY QVDGLQDPLS RLARALLIWP AITKKKIRKV
     KVKHTDESGL ALQPA
//
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