MYR3_SINAL
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 03-AUG-2022, entry version 96.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X59879; CAA42534.1; -; mRNA.
DR PIR; S19149; S19149.
DR AlphaFoldDB; P29092; -.
DR SMR; P29092; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
DR GO; GO:0102799; F:glucosinolate glucohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; IPR033132; Glyco_hydro_1_N_CS.
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.
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
