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P29736 (MYRA_SINAL) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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 › malvids › Brassicales › Brassicaceae › Brassiceae › Sinapis

Protein attributes

Sequence length501 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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.

Subunit structure

Homodimer. Ref.2 Ref.3 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.

Miscellaneous

It seems that the absence of a catalytic proton donor in plant myrosinases is not impairing the hydrolysis of glucosinolates.

Sequence similarities

Belongs to the glycosyl hydrolase 1 family.

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_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

thioglucosidase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 501501Myrosinase MA1
PRO_0000063901

Regions

Region464 – 4652Substrate binding By similarity

Sites

Active site4091Nucleophile
Metal binding561Zinc; shared with dimeric partner
Metal binding701Zinc; shared with dimeric partner
Binding site391Substrate
Binding site1411Substrate
Binding site1861Substrate
Binding site1871Ascorbate
Binding site2591Ascorbate
Binding site3301Substrate By similarity
Binding site4571Substrate By similarity

Amino acid modifications

Glycosylation211N-linked (GlcNAc...) Ref.2 Ref.3 Ref.4
Glycosylation601N-linked (GlcNAc...) Ref.2 Ref.3 Ref.4
Glycosylation901N-linked (GlcNAc...) Ref.2 Ref.3 Ref.4
Glycosylation2181N-linked (GlcNAc...) Ref.2 Ref.3 Ref.4
Glycosylation2441N-linked (GlcNAc...) Ref.2 Ref.3 Ref.4
Glycosylation2651N-linked (GlcNAc...) Ref.2 Ref.3 Ref.4
Glycosylation2921N-linked (GlcNAc...) Ref.2 Ref.3 Ref.4
Glycosylation3431N-linked (GlcNAc...) Ref.2 Ref.3 Ref.4
Glycosylation3461N-linked (GlcNAc...) Ref.2 Ref.3 Ref.4
Glycosylation3611N-linked (GlcNAc...) Ref.2 Ref.3 Ref.4
Glycosylation4821N-linked (GlcNAc...) Ref.2 Ref.3 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...

Sequences

Sequence LengthMass (Da)Tools
P29736 [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

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) IN COMPLEX WITH ASCORBATE AND TRANSITION STATE ANALOGS, 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] [Europe PMC] [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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X59878 mRNA. Translation: CAA42533.1.
PIRS19146.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
2WXDX-ray1.60M1-501[»]
ProteinModelPortalP29736.
SMRP29736. Positions 3-501.
ModBaseSearch...

Protein family/group databases

CAZyGH1. Glycoside Hydrolase Family 1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR001360. Glyco_hydro_1.
IPR018120. Glyco_hydro_1_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERPTHR10353. PTHR10353. 1 hit.
PfamPF00232. Glyco_hydro_1. 1 hit.
[Graphical view]
PRINTSPR00131. GLHYDRLASE1.
SUPFAMSSF51445. Glyco_hydro_cat. 1 hit.
PROSITEPS00572. GLYCOSYL_HYDROL_F1_1. 1 hit.
PS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

DrugBankDB00126. Vitamin C.
EvolutionaryTraceP29736.

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: April 3, 2013
This is version 86 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents