MYRO_BRANA
ID MYRO_BRANA Reviewed; 548 AA.
AC Q00326;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Myrosinase;
DE EC=3.2.1.147;
DE AltName: Full=Sinigrinase;
DE AltName: Full=Thioglucosidase;
DE Flags: Precursor;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Svalofs Karat;
RA Falk A., Xue J., Lenman M., Rask L.;
RT "Sequence of a cDNA clone encoding the enzyme myrosinase, and expression of
RT myrosinase in different tissues of Brassica napus.";
RL Plant Sci. 83:181-186(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 -!- 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; X60214; CAA42775.1; -; mRNA.
DR PIR; S26149; S26149.
DR RefSeq; NP_001302796.1; NM_001315867.1.
DR AlphaFoldDB; Q00326; -.
DR SMR; Q00326; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR GeneID; 106382674; -.
DR KEGG; bna:106382674; -.
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 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Metal-binding;
KW Signal; Vacuole; Zinc.
FT SIGNAL 1..20
FT /evidence="ECO:0000250"
FT CHAIN 21..548
FT /note="Myrosinase"
FT /id="PRO_0000011774"
FT ACT_SITE 429
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 352
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 477
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 484..485
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 520
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 26..458
FT /evidence="ECO:0000250"
FT DISULFID 34..454
FT /evidence="ECO:0000250"
FT DISULFID 226..236
FT /evidence="ECO:0000250"
SQ SEQUENCE 548 AA; 62736 MW; F3034C6A01CD732A CRC64;
MKLLHGLALV FLLAAASCKA DEEITCEENN PFTCSNTDIL SSKNFGKDFI FGVASSAYQI
EGGRGRGVNV WDGFSHRYPE KAGSDLKNGD TTCESYTRWQ KDVDVMGELN ATGYRFSFAW
SRIIPKGKVS RGVNQGGLDY YHKLIDALLE KNITPFVTLF HWDLPQTLQD EYEGFLDRQI
IQDFKDYADL CFKEFGGKVK HWITINQLYT VPTRGYAIGT DAPGRCSPMV DTKHRCYGGN
SSTEPYIVAH NQLLAHATVV DLYRTKYKFQ KGKIGPVMIT RWFLPFDESD PASIEAAERM
NQFFHGWYME PLTKGRYPDI MRQIVGSRLP NFTEEEAELV AGSYDFLGLN YYVTQYAQPK
PNPYPSETHT AMMDAGVKLT YDNSRGEFLG PLFVEDKVNG NSYYYPKGIY YVMDYFKTKY
GDPLIYVTEN GFSTPSSENR EQAIADYKRI DYLCSHLCFL RKVIKEKGVN VRGYFAWALG
DNYEFCKGFT VRFGLSYVNW EDLDDRNLKE SGKWYQRFIN GTVKNAVKQD FLRSSLSSQS
QKKRFADA
