MYRA_SINAL
ID MYRA_SINAL Reviewed; 501 AA.
AC P29736; Q7SIB0;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Myrosinase MA1;
DE EC=3.2.1.147;
DE AltName: Full=Sinigrinase;
DE AltName: Full=Thioglucosidase;
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] OF 280-501, 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).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.64 ANGSTROMS), SUBUNIT, AND GLYCOSYLATION AT
RP ASN-21; ASN-60; ASN-90; ASN-218; ASN-244; ASN-265; ASN-292; ASN-343;
RP ASN-346; ASN-361 AND ASN-482.
RC STRAIN=cv. Emergo; TISSUE=Seed;
RX PubMed=9195886; DOI=10.1016/s0969-2126(97)00221-9;
RA Burmeister W.P., Cottaz S., Driguez H., Iori R., Palmieri S., Henrissat B.;
RT "The crystal structures of Sinapis alba myrosinase and a covalent glycosyl-
RT enzyme intermediate provide insights into the substrate recognition and
RT active-site machinery of an S-glycosidase.";
RL Structure 5:663-675(1997).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) IN COMPLEX WITH ASCORBATE AND
RP TRANSITION STATE ANALOGS, SUBUNIT, AND GLYCOSYLATION AT ASN-21; ASN-60;
RP ASN-90; ASN-218; ASN-244; ASN-265; ASN-292; ASN-343; ASN-346; ASN-361 AND
RP ASN-482.
RC STRAIN=cv. Emergo; TISSUE=Seed;
RX PubMed=10978344; DOI=10.1074/jbc.m006796200;
RA Burmeister W.P., Cottaz S., Rollin P., Vasella A., Henrissat B.;
RT "High resolution X-ray crystallography shows that ascorbate is a cofactor
RT for myrosinase and substitutes for the function of the catalytic base.";
RL J. Biol. Chem. 275:39385-39393(2000).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS), SUBUNIT, AND GLYCOSYLATION AT
RP ASN-21; ASN-60; ASN-90; ASN-218; ASN-244; ASN-265; ASN-292; ASN-343;
RP ASN-346; ASN-361 AND ASN-482.
RX PubMed=15889170; DOI=10.1039/b502990b;
RA Bourderioux A., Lefoix M., Gueyrard D., Tatibouet A., Cottaz S., Arzt S.,
RA Burmeister W.P., Rollin P.;
RT "The glucosinolate-myrosinase system. New insights into enzyme-substrate
RT interactions by use of simplified inhibitors.";
RL Org. Biomol. Chem. 3:1872-1879(2005).
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. {ECO:0000269|PubMed:10978344,
CC ECO:0000269|PubMed:15889170, ECO:0000269|PubMed:9195886}.
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; X59878; CAA42533.1; -; mRNA.
DR PIR; S19146; S19146.
DR PDB; 1DWA; X-ray; 2.00 A; M=3-501.
DR PDB; 1DWF; X-ray; 2.00 A; M=3-501.
DR PDB; 1DWG; X-ray; 2.00 A; M=3-501.
DR PDB; 1DWH; X-ray; 2.00 A; M=3-501.
DR PDB; 1DWI; X-ray; 2.00 A; M=3-501.
DR PDB; 1DWJ; X-ray; 2.40 A; M=3-501.
DR PDB; 1E4M; X-ray; 1.20 A; M=1-501.
DR PDB; 1E6Q; X-ray; 1.35 A; M=1-501.
DR PDB; 1E6S; X-ray; 1.35 A; M=1-501.
DR PDB; 1E6X; X-ray; 1.60 A; M=1-501.
DR PDB; 1E70; X-ray; 1.65 A; M=1-501.
DR PDB; 1E71; X-ray; 1.50 A; M=1-501.
DR PDB; 1E72; X-ray; 1.60 A; M=1-501.
DR PDB; 1E73; X-ray; 1.50 A; M=1-501.
DR PDB; 1MYR; X-ray; 1.64 A; A=1-501.
DR PDB; 1W9B; X-ray; 1.70 A; M=1-501.
DR PDB; 1W9D; X-ray; 1.60 A; M=1-501.
DR PDB; 2WXD; X-ray; 1.60 A; M=1-501.
DR PDBsum; 1DWA; -.
DR PDBsum; 1DWF; -.
DR PDBsum; 1DWG; -.
DR PDBsum; 1DWH; -.
DR PDBsum; 1DWI; -.
DR PDBsum; 1DWJ; -.
DR PDBsum; 1E4M; -.
DR PDBsum; 1E6Q; -.
DR PDBsum; 1E6S; -.
DR PDBsum; 1E6X; -.
DR PDBsum; 1E70; -.
DR PDBsum; 1E71; -.
DR PDBsum; 1E72; -.
DR PDBsum; 1E73; -.
DR PDBsum; 1MYR; -.
DR PDBsum; 1W9B; -.
DR PDBsum; 1W9D; -.
DR PDBsum; 2WXD; -.
DR AlphaFoldDB; P29736; -.
DR SMR; P29736; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR iPTMnet; P29736; -.
DR BRENDA; 3.2.1.147; 5734.
DR EvolutionaryTrace; P29736; -.
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 3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Glycosidase; Hydrolase; Metal-binding; Vacuole; Zinc.
FT CHAIN 1..501
FT /note="Myrosinase MA1"
FT /id="PRO_0000063901"
FT ACT_SITE 409
FT /note="Nucleophile"
FT BINDING 39
FT /ligand="substrate"
FT BINDING 56
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared between dimeric partners"
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared between dimeric partners"
FT BINDING 141
FT /ligand="substrate"
FT BINDING 186
FT /ligand="substrate"
FT BINDING 187
FT /ligand="L-ascorbate"
FT /ligand_id="ChEBI:CHEBI:38290"
FT /evidence="ECO:0000269|PubMed:10978344"
FT BINDING 259
FT /ligand="L-ascorbate"
FT /ligand_id="ChEBI:CHEBI:38290"
FT /evidence="ECO:0000269|PubMed:10978344"
FT BINDING 330
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 457
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 464..465
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 21
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:10978344,
FT ECO:0000269|PubMed:15889170, ECO:0000269|PubMed:9195886"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:10978344,
FT ECO:0000269|PubMed:15889170, ECO:0000269|PubMed:9195886"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:10978344,
FT ECO:0000269|PubMed:15889170, ECO:0000269|PubMed:9195886"
FT CARBOHYD 218
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:10978344,
FT ECO:0000269|PubMed:15889170, ECO:0000269|PubMed:9195886"
FT CARBOHYD 244
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:10978344,
FT ECO:0000269|PubMed:15889170, ECO:0000269|PubMed:9195886"
FT CARBOHYD 265
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:10978344,
FT ECO:0000269|PubMed:15889170, ECO:0000269|PubMed:9195886"
FT CARBOHYD 292
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:10978344,
FT ECO:0000269|PubMed:15889170, ECO:0000269|PubMed:9195886"
FT CARBOHYD 343
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:10978344,
FT ECO:0000269|PubMed:15889170, ECO:0000269|PubMed:9195886"
FT CARBOHYD 346
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:10978344,
FT ECO:0000269|PubMed:15889170, ECO:0000269|PubMed:9195886"
FT CARBOHYD 361
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:10978344,
FT ECO:0000269|PubMed:15889170, ECO:0000269|PubMed:9195886"
FT CARBOHYD 482
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:10978344,
FT ECO:0000269|PubMed:15889170, ECO:0000269|PubMed:9195886"
FT DISULFID 6..438
FT DISULFID 14..434
FT DISULFID 206..214
FT CONFLICT 373..374
FT /note="KD -> EN (in Ref. 1; CAA42533)"
FT /evidence="ECO:0000305"
FT CONFLICT 378..380
FT /note="STD -> ETK (in Ref. 1; CAA42533)"
FT /evidence="ECO:0000305"
FT CONFLICT 497
FT /note="S -> K (in Ref. 1; CAA42533)"
FT /evidence="ECO:0000305"
FT CONFLICT 501
FT /note="P -> PGIKSPLKKDFLRSSLTFEKNKKLADA (in Ref. 1)"
FT /evidence="ECO:0000305"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:1E4M"
FT TURN 17..19
FT /evidence="ECO:0007829|PDB:1E4M"
FT HELIX 22..24
FT /evidence="ECO:0007829|PDB:1E4M"
FT STRAND 30..34
FT /evidence="ECO:0007829|PDB:1E4M"
FT HELIX 37..40
FT /evidence="ECO:0007829|PDB:1E4M"
FT HELIX 50..57
FT /evidence="ECO:0007829|PDB:1E4M"
FT HELIX 59..62
FT /evidence="ECO:0007829|PDB:1E4M"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:1E4M"
FT HELIX 75..89
FT /evidence="ECO:0007829|PDB:1E4M"
FT STRAND 92..97
FT /evidence="ECO:0007829|PDB:1E4M"
FT HELIX 100..103
FT /evidence="ECO:0007829|PDB:1E4M"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:1E4M"
FT HELIX 115..130
FT /evidence="ECO:0007829|PDB:1E4M"
FT STRAND 134..142
FT /evidence="ECO:0007829|PDB:1E4M"
FT HELIX 146..152
FT /evidence="ECO:0007829|PDB:1E4M"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:1E4M"
FT HELIX 160..175
FT /evidence="ECO:0007829|PDB:1E4M"
FT TURN 176..178
FT /evidence="ECO:0007829|PDB:1E4M"
FT STRAND 181..186
FT /evidence="ECO:0007829|PDB:1E4M"
FT HELIX 190..196
FT /evidence="ECO:0007829|PDB:1E4M"
FT TURN 208..210
FT /evidence="ECO:0007829|PDB:1E4M"
FT TURN 219..221
FT /evidence="ECO:0007829|PDB:1E4M"
FT HELIX 222..244
FT /evidence="ECO:0007829|PDB:1E4M"
FT HELIX 246..248
FT /evidence="ECO:0007829|PDB:1E4M"
FT STRAND 251..253
FT /evidence="ECO:0007829|PDB:1E4M"
FT STRAND 255..265
FT /evidence="ECO:0007829|PDB:1E4M"
FT HELIX 269..282
FT /evidence="ECO:0007829|PDB:1E4M"
FT HELIX 284..292
FT /evidence="ECO:0007829|PDB:1E4M"
FT HELIX 297..303
FT /evidence="ECO:0007829|PDB:1E4M"
FT HELIX 304..306
FT /evidence="ECO:0007829|PDB:1E4M"
FT HELIX 312..318
FT /evidence="ECO:0007829|PDB:1E4M"
FT STRAND 323..337
FT /evidence="ECO:0007829|PDB:1E4M"
FT HELIX 349..353
FT /evidence="ECO:0007829|PDB:1E4M"
FT STRAND 355..360
FT /evidence="ECO:0007829|PDB:1E4M"
FT STRAND 368..372
FT /evidence="ECO:0007829|PDB:1E4M"
FT HELIX 378..380
FT /evidence="ECO:0007829|PDB:1E4M"
FT HELIX 387..399
FT /evidence="ECO:0007829|PDB:1E4M"
FT STRAND 405..409
FT /evidence="ECO:0007829|PDB:1E4M"
FT HELIX 420..424
FT /evidence="ECO:0007829|PDB:1E4M"
FT HELIX 427..447
FT /evidence="ECO:0007829|PDB:1E4M"
FT STRAND 451..457
FT /evidence="ECO:0007829|PDB:1E4M"
FT TURN 465..467
FT /evidence="ECO:0007829|PDB:1E4M"
FT STRAND 470..472
FT /evidence="ECO:0007829|PDB:1E4M"
FT STRAND 475..479
FT /evidence="ECO:0007829|PDB:1E4M"
FT STRAND 482..488
FT /evidence="ECO:0007829|PDB:1E4M"
FT HELIX 490..499
FT /evidence="ECO:0007829|PDB:1E4M"
SQ SEQUENCE 501 AA; 57023 MW; 23EAA1FEFFDEBF02 CRC64;
DEEITCQENL PFTCGNTDAL NSSSFSSDFI FGVASSAYQI EGTIGRGLNI WDGFTHRYPN
KSGPDHGNGD TTCDSFSYWQ KDIDVLDELN ATGYRFSIAW SRIIPRGKRS RGVNEKGIDY
YHGLISGLIK KGITPFVTLF HWDLPQTLQD EYEGFLDPQI IDDFKDYADL CFEEFGDSVK
YWLTINQLYS VPTRGYGSAL DAPGRCSPTV DPSCYAGNSS TEPYIVAHHQ LLAHAKVVDL
YRKNYTHQGG KIGPTMITRW FLPYNDTDRH SIAATERMKE FFLGWFMGPL TNGTYPQIMI
DTVGERLPSF SPEESNLVKG SYDFLGLNYY FTQYAQPSPN PVNSTNHTAM MDAGAKLTYI
NASGHYIGPL FEKDKADSTD NIYYYPKGIY SVMDYFKNKY YNPLIYVTEN GISTPGDENR
NQSMLDYTRI DYLCSHLCFL NKVIKEKDVN VKGYLAWALG DNYEFNKGFT VRFGLSYIDW
NNVTDRDLKK SGQWYQSFIS P
