ID A0A078HDP2_BRANA Unreviewed; 575 AA.
AC A0A078HDP2;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, 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=BnaA01g32790D {ECO:0000313|EMBL:CDY34948.1};
GN ORFNames=GSBRNA2T00057530001 {ECO:0000313|EMBL:CDY34948.1};
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:CDY34948.1, ECO:0000313|Proteomes:UP000028999};
RN [1] {ECO:0000313|EMBL:CDY34948.1, 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).
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; LK032343; CDY34948.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A078HDP2; -.
DR STRING; 3708.A0A078HDP2; -.
DR PaxDb; 3708-A0A078HDP2; -.
DR EnsemblPlants; CDY34948; CDY34948; GSBRNA2T00057530001.
DR Gramene; CDY34948; CDY34948; GSBRNA2T00057530001.
DR OMA; LHERYKH; -.
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; 2.
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:SF332; THIOGLUCOSIDASE; 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 386
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10055"
SQ SEQUENCE 575 AA; 65348 MW; 647A2CC5AB8716B9 CRC64;
MNIVALLVKV AGLFATITVG ANAFSYTRFR RRNLGKIRSP IDESKEVLAD FNSHEHKEGK
FFFGLATAPA HSEDELDDAW LQFAKETPSS PSDAVPGSEA ANRKKIKLAV GAITKGLAKN
KHIKEVKASA SADVKPPTNN VAAWHNAPHA EDRLMFWSDP DKEVKLAKET GVTVFRMGID
WSRIMPKEPT EGIKEAVDYE ALEHYKWILN RVRSNGMKVM LTLFHHSLPP WAADYGGWKI
EKTVDYFMDF TRLVVDSMFE LVDSWVTFNE PHVFTLLTYI CLKKPLVGIA HHVSFIRPYG
LFDTGAVTIS NSLTVYPYID SISKKLDFIG INYYGQESVC GVGIKLVETD EYSESGRGIY
PDGLYRVLLM LHERYKHLKI PFIVTENGVS DETDVIRRPY LIEHLLALYA AMLKGVPVLG
YIFWTVSDNW EWADGYGPKF GLVAVDRSNN LARTLRPSYH LFSKIVKSGK ITRKDRSLAW
NELQKAAKSG KLRPFYRAVD NHGLMYADGL DKPQWRPYVD RDWRFGHYRV DGLQDPLSRV
ARVLLIWPLI MNKRIRKVKV KHTDDTGAAY ASPFN
//
