ID   MYR2_SINAL              Reviewed;         243 AA.
AC   P29738;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Myrosinase MB2;
DE            EC=3.2.1.147;
DE   AltName: Full=Sinigrinase;
DE   AltName: Full=Thioglucosidase;
DE   Flags: Fragment;
OS   Sinapis alba (White mustard) (Brassica hirta).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Sinapis.
OX   NCBI_TaxID=3728;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=cv. Maxi; TISSUE=Seed;
RX   PubMed=1731996; DOI=10.1007/bf00034965;
RA   Xue J., Lenman M., Falk A., Rask L.;
RT   "The glucosinolate-degrading enzyme myrosinase in Brassicaceae is encoded
RT   by a gene family.";
RL   Plant Mol. Biol. 18:387-398(1992).
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=a thioglucoside + H2O = a sugar + a thiol.; EC=3.2.1.147;
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Vacuole.
CC   -!- TISSUE SPECIFICITY: In vacuoles called myrosin grains of a certain
CC       class of cells, myrosin cells, distributed in the cotyledons and the
CC       axis of the embryo as well as in different organs of the growing plant.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}.
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DR   EMBL; X59880; CAA42535.1; -; mRNA.
DR   PIR; S19148; S19148.
DR   AlphaFoldDB; P29738; -.
DR   SMR; P29738; -.
DR   CAZy; GH1; Glycoside Hydrolase Family 1.
DR   PRIDE; P29738; -.
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   InterPro; IPR001360; Glyco_hydro_1.
DR   InterPro; IPR018120; Glyco_hydro_1_AS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR10353; PTHR10353; 1.
DR   Pfam; PF00232; Glyco_hydro_1; 1.
DR   PRINTS; PR00131; GLHYDRLASE1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS00572; GLYCOSYL_HYDROL_F1_1; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycoprotein; Glycosidase; Hydrolase; Vacuole.
FT   CHAIN           <1..243
FT                   /note="Myrosinase MB2"
FT                   /id="PRO_0000063903"
FT   ACT_SITE        125
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10055"
FT   BINDING         51
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         173
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         180..181
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        30
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        216
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   NON_TER         1
SQ   SEQUENCE   243 AA;  28184 MW;  F79CE00FD7FDB4D7 CRC64;
     EFFHGWYMEP LTKGRYPDIM RQIVGTRLPN FTEDEAELVA GSYDFLGLNY YVTQYAKPKP
     NPYPSEKHTA MDDAGVDLTF KNSRGEYPGP VFAEDANSYY YPKGIYYVMD YFKTKYGNPL
     IYITENGIST PGSESRCERI ADYKRINYHC SHLCFLSKVI KEKGVNVRGY FAWALGDNYE
     FGKGFTVRFG LSYVNWDDLN DRNLKESGKW YQRFINGTAK NPVKQNFLRS SLSSQNQKKR
     LAC