ID   MYR3_SINAL              Reviewed;         544 AA.
AC   P29092;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   02-SEP-2026, entry version 105.
DE   RecName: Full=Myrosinase MB3;
DE            EC=3.2.1.147;
DE   AltName: Full=Sinigrinase;
DE   AltName: Full=Thioglucosidase;
DE   Flags: Precursor;
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   -!- COFACTOR:
CC       Name=L-ascorbate; Xref=ChEBI:CHEBI:38290; Evidence={ECO:0000250};
CC       Note=Binds 1 ascorbate molecule per subunit. {ECO:0000250};
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   -!- MISCELLANEOUS: It seems that the absence of a catalytic proton donor in
CC       plant myrosinases is not impairing the hydrolysis of glucosinolates.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}.
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DR   EMBL; X59879; CAA42534.1; -; mRNA.
DR   PIR; S19149; S19149.
DR   AlphaFoldDB; P29092; -.
DR   SMR; P29092; -.
DR   OrthoDB; 1029817at2759; -.
DR   GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
DR   GO; GO:0008422; F:beta-glucosidase activity; IEA:TreeGrafter.
DR   GO; GO:0019137; F:thioglucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   FunFam; 3.20.20.80:FF:000041; Beta-glucosidase 7; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR033132; GH_1_N_CS.
DR   InterPro; IPR017853; GH_hydrolase_sf.
DR   InterPro; IPR001360; Glyco_hydro_1.
DR   InterPro; IPR018120; Glyco_hydro_1_AS.
DR   PANTHER; PTHR10353; GLYCOSYL HYDROLASE; 1.
DR   PANTHER; PTHR10353:SF231; 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.
DR   PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein; Glycosidase;
KW   Hydrolase; Metal-binding; Signal; Vacuole; Zinc.
FT   SIGNAL          1..20
FT   CHAIN           21..544
FT                   /note="Myrosinase MB3"
FT                   /id="PRO_0000011775"
FT   ACT_SITE        426
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10055"
FT   BINDING         59
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         76
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250"
FT   BINDING         90
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250"
FT   BINDING         161
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         206
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         207
FT                   /ligand="L-ascorbate"
FT                   /ligand_id="ChEBI:CHEBI:38290"
FT                   /evidence="ECO:0000250"
FT   BINDING         281
FT                   /ligand="L-ascorbate"
FT                   /ligand_id="ChEBI:CHEBI:38290"
FT                   /evidence="ECO:0000250"
FT   BINDING         426
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         481
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        110
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        240
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        331
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        382
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        517
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        26..455
FT                   /evidence="ECO:0000250"
FT   DISULFID        34..451
FT                   /evidence="ECO:0000250"
FT   DISULFID        226..236
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   544 AA;  62050 MW;  3971D3304CF75C28 CRC64;
     MKLLHGLALV FLLAAASCKA DEEITCEENE PFTCSNTDIL SSKNFGKDFI FGVASSAYQI
     EGGRGRGVNV WDGFSHRYPE KSGSDLKNGD TSCESYTRWK KDVEIMGELN ATGYRFSFAW
     SRIVPKGKVS RGVDQAGLDY YHNLIDALLE KNITPFVTLF HWDLPQTLQD EYEGFLDRQI
     IQDFKDYADL CFKEFGGKVK NWITINQLYT VPTRGYALGT DAPGRCSPKV DTKQRCYGGN
     SSTEPYIVAH NQLLAHAAIV DLYRTNYAFQ NGKIGPVMIT RWFLPYDESD PACIEAAERM
     NQFFHGWYME PLTKGRYPDI MRQIVGSRLP NFTEAEAELV AGSYDFLGLN YYVTQYAKPK
     PNPYPSETHT ALMDAGVDLT FNNSRGEYPG PVFAEDANSY YYPKGIYYVM DYFKTKYNNP
     LIYITENGIS TPGSESRCEA IADYKRINYL CSHLCFLRKV IREKGVNIRG YFAWALGDNY
     EFCKGFTVRF GLSYVNWDDL DDRNLKESGK WYQRFINGTA KNPVKQDFLR SSLSSQSQKK
     RLAC
//