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Reviewed, UniProtKB/Swiss-Prot P29736 (MYRA_SINAL)

Last modified June 16, 2009. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Myrosinase MA1
    EC=3.2.1.147
Alternative name(s):
    Sinigrinase
    Thioglucosidase
OrganismSinapis alba (White mustard) (Brassica hirta)
Taxonomic identifier3728 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Sinapis

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Protein attributes

Sequence length501 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Degradation of glucosinolates (glucose residue linked by a thioglucoside bound to an amino acid derivative) to glucose, sulfate and any of the products: thiocyanates, isothiocyanates, nitriles, epithionitriles or oxazolidine-2-thiones.

Catalytic activity

A thioglucoside + H2O = a sugar + a thiol.

Cofactor

Binds 1 ascorbate molecule per subunit. Ref.3

Subunit structure

Homodimer. Ref.3 Ref.2 Ref.4

Subcellular location

Vacuole.

Tissue specificity

In vacuoles called myrosin grains of a certain class of cells, myrosin cells, distributed in the cotyledons and the axis of the embryo as well as in different organs of the growing plant.

Sequence similarities

Belongs to the glycosyl hydrolase 1 family.

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Ontologies

Keywords
   Cellular componentVacuole
   LigandMetal-binding
Zinc
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentvacuole

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionthioglucosidase activity

Inferred from electronic annotation. Source: EC

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 501501Myrosinase MA1
PRO_0000063901

Regions

Region186 – 1872Substrate
Region464 – 4652Substrate

Sites

Active site4091Nucleophile
Metal binding561Zinc; shared with dimeric partner
Metal binding701Zinc; shared with dimeric partner
Binding site391Substrate
Binding site1411Substrate
Binding site1871Ascorbate cofactor
Binding site2591Ascorbate cofactor
Binding site3301Substrate
Binding site3711Substrate
Binding site4091Substrate
Binding site4571Substrate
Binding site4731Substrate

Amino acid modifications

Glycosylation211N-linked (GlcNAc...) Ref.3 Ref.2 Ref.4
Glycosylation601N-linked (GlcNAc...) Ref.3 Ref.2 Ref.4
Glycosylation901N-linked (GlcNAc...) Ref.3 Ref.2 Ref.4
Glycosylation2181N-linked (GlcNAc...) Ref.3 Ref.2 Ref.4
Glycosylation2441N-linked (GlcNAc...) Ref.3 Ref.2 Ref.4
Glycosylation2651N-linked (GlcNAc...) Ref.3 Ref.2 Ref.4
Glycosylation2921N-linked (GlcNAc...) Ref.3 Ref.2 Ref.4
Glycosylation3431N-linked (GlcNAc...) Ref.3 Ref.2 Ref.4
Glycosylation3461N-linked (GlcNAc...) Ref.3 Ref.2 Ref.4
Glycosylation3611N-linked (GlcNAc...) Ref.3 Ref.2 Ref.4
Glycosylation4821N-linked (GlcNAc...) Ref.3 Ref.2 Ref.4
Disulfide bond6 ↔ 438
Disulfide bond14 ↔ 434
Disulfide bond206 ↔ 214

Experimental info

Sequence conflict373 – 3742KD → EN in CAA42533. Ref.1
Sequence conflict378 – 3803STD → ETK in CAA42533. Ref.1
Sequence conflict4971S → K in CAA42533. Ref.1
Sequence conflict5011P → PGIKSPLKKDFLRSSLTFEK NKKLADA Ref.1

Secondary structure

1 .......................................................................................... 501
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P29736-1 [UniParc].

Last modified May 16, 2006. Version 2.
Checksum: 23EAA1FEFFDEBF02

FASTA50157,023
        10         20         30         40         50         60 
DEEITCQENL PFTCGNTDAL NSSSFSSDFI FGVASSAYQI EGTIGRGLNI WDGFTHRYPN 

        70         80         90        100        110        120 
KSGPDHGNGD TTCDSFSYWQ KDIDVLDELN ATGYRFSIAW SRIIPRGKRS RGVNEKGIDY 

       130        140        150        160        170        180 
YHGLISGLIK KGITPFVTLF HWDLPQTLQD EYEGFLDPQI IDDFKDYADL CFEEFGDSVK 

       190        200        210        220        230        240 
YWLTINQLYS VPTRGYGSAL DAPGRCSPTV DPSCYAGNSS TEPYIVAHHQ LLAHAKVVDL 

       250        260        270        280        290        300 
YRKNYTHQGG KIGPTMITRW FLPYNDTDRH SIAATERMKE FFLGWFMGPL TNGTYPQIMI 

       310        320        330        340        350        360 
DTVGERLPSF SPEESNLVKG SYDFLGLNYY FTQYAQPSPN PVNSTNHTAM MDAGAKLTYI 

       370        380        390        400        410        420 
NASGHYIGPL FEKDKADSTD NIYYYPKGIY SVMDYFKNKY YNPLIYVTEN GISTPGDENR 

       430        440        450        460        470        480 
NQSMLDYTRI DYLCSHLCFL NKVIKEKDVN VKGYLAWALG DNYEFNKGFT VRFGLSYIDW 

       490        500 
NNVTDRDLKK SGQWYQSFIS P

« Hide

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References

[1]"The glucosinolate-degrading enzyme myrosinase in Brassicaceae is encoded by a gene family."
Xue J., Lenman M., Falk A., Rask L.
Plant Mol. Biol. 18:387-398(1992) [PubMed: 1731996] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 280-501, PARTIAL PROTEIN SEQUENCE.
Strain: cv. Maxi.
Tissue: Seed.
[2]"The crystal structures of Sinapis alba myrosinase and a covalent glycosyl-enzyme intermediate provide insights into the substrate recognition and active-site machinery of an S-glycosidase."
Burmeister W.P., Cottaz S., Driguez H., Iori R., Palmieri S., Henrissat B.
Structure 5:663-675(1997) [PubMed: 9195886] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.64 ANGSTROMS), SUBUNIT, GLYCOSYLATION AT ASN-21; ASN-60; ASN-90; ASN-218; ASN-244; ASN-265; ASN-292; ASN-343; ASN-346; ASN-361 AND ASN-482.
Strain: cv. Emergo.
Tissue: Seed.
[3]"High resolution X-ray crystallography shows that ascorbate is a cofactor for myrosinase and substitutes for the function of the catalytic base."
Burmeister W.P., Cottaz S., Rollin P., Vasella A., Henrissat B.
J. Biol. Chem. 275:39385-39393(2000) [PubMed: 10978344] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) IN COMPLEX WITH ASCORBATE AND TRANSITION STATE ANALOGS, COFACTOR, SUBUNIT, GLYCOSYLATION AT ASN-21; ASN-60; ASN-90; ASN-218; ASN-244; ASN-265; ASN-292; ASN-343; ASN-346; ASN-361 AND ASN-482.
Strain: cv. Emergo.
Tissue: Seed.
[4]"The glucosinolate-myrosinase system. New insights into enzyme-substrate interactions by use of simplified inhibitors."
Bourderioux A., Lefoix M., Gueyrard D., Tatibouet A., Cottaz S., Arzt S., Burmeister W.P., Rollin P.
Org. Biomol. Chem. 3:1872-1879(2005) [PubMed: 15889170] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS), SUBUNIT, GLYCOSYLATION AT ASN-21; ASN-60; ASN-90; ASN-218; ASN-244; ASN-265; ASN-292; ASN-343; ASN-346; ASN-361 AND ASN-482.
+Additional computationally mapped references.

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Cross-references

Sequence databases

X59878 mRNA. Translation: CAA42533.1.
PIRS19146.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1DWAX-ray2.00M3-501[»]
1DWFX-ray2.00M3-501[»]
1DWGX-ray2.00M3-501[»]
1DWHX-ray2.00M3-501[»]
1DWIX-ray2.00M3-501[»]
1DWJX-ray2.40M3-501[»]
1E4MX-ray1.20M1-501[»]
1E6QX-ray1.35M1-501[»]
1E6SX-ray1.35M1-501[»]
1E6XX-ray1.60M1-501[»]
1E70X-ray1.65M1-501[»]
1E71X-ray1.50M1-501[»]
1E72X-ray1.60M1-501[»]
1E73X-ray1.50M1-501[»]
1MYRX-ray1.64A1-501[»]
1W9BX-ray1.70M1-501[»]
1W9DX-ray1.60M1-501[»]
ModBaseSearch...

Protein family/group databases

CAZyGH1. Glycoside Hydrolase Family 1.

Enzyme and pathway databases

BRENDA3.2.1.147. 20822.

Family and domain databases

InterProIPR001360. Glyco_hydro_1.
IPR018120. Glyco_hydro_1_AS.
IPR013781. Glyco_hydro_sg_catalytic.
[Graphical view]
Gene3DG3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
PANTHERPTHR10353. Glyco_hydro_1. 1 hit.
PfamPF00232. Glyco_hydro_1. 1 hit.
[Graphical view]
PRINTSPR00131. GLHYDRLASE1.
PROSITEPS00572. GLYCOSYL_HYDROL_F1_1. 1 hit.
PS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

DrugBankDB00126. Vitamin C.

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Entry information

Entry nameMYRA_SINAL
AccessionPrimary (citable) accession number: P29736
Secondary accession number(s): Q7SIB0
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: May 16, 2006
Last modified: June 16, 2009
This is version 69 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

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Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents