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P83179 (MYRO2_BREBR) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 38. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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 2

EC=3.2.1.147
Alternative name(s):
Beta-glucosidase 2
Beta-thioglucosidase 2
Beta-thioglucosidase glucohydrolase 2
Myrosinase
Sinigrinase 2
Thioglucosidase 2
OrganismBrevicoryne brassicae (Cabbage aphid)
Taxonomic identifier69196 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraParaneopteraHemipteraSternorrhynchaAphidiformesAphidoideaAphididaeMacrosiphiniBrevicoryne

Protein attributes

Sequence length140 AA.
Sequence statusFragments.
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 By similarity. Ref.1 UniProtKB P37702

Catalytic activity

A thioglucoside + H2O = a sugar + a thiol. Ref.1

Enzyme regulation

Inhibited by ascorbate. Ref.1

Subunit structure

Homodimer. Ref.1

Sequence similarities

Belongs to the glycosyl hydrolase 1 family.

Caution

The order of the peptides shown is unknown.

Biophysicochemical properties

Kinetic parameters:

KM=0.41 mM for sinigrin (at pH 4.5 and 37 degrees Celsius) Ref.1

KM=0.52 mM for p-nitrophenyl-beta-glucopyranoside (at pH 4.5 and 37 degrees Celsius)

Temperature dependence:

Optimum temperature is about 40 degrees Celsius.

Ontologies

Keywords
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Molecular_functionthioglucosidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – ›140›140Myrosinase 2
PRO_0000063904

Sites

Active site701Nucleophile By similarity UniProtKB P37702

Amino acid modifications

Glycosylation1141N-linked (GlcNAc...) Potential
Glycosylation1271N-linked (GlcNAc...) Potential

Experimental info

Non-adjacent residues12 – 132
Non-adjacent residues26 – 272
Non-adjacent residues35 – 362
Non-adjacent residues44 – 452
Non-adjacent residues58 – 592
Non-adjacent residues84 – 852
Non-adjacent residues97 – 982
Non-adjacent residues111 – 1122
Non-adjacent residues124 – 1252
Non-terminal residue11
Non-terminal residue1401

Sequences

Sequence LengthMass (Da)Tools
P83179 [UniParc].

Last modified March 23, 2010. Version 2.
Checksum: A03EF5F737CD8ABD

FASTA14015,646
        10         20         30         40         50         60 
DFMFGTSTAS GGLAPSGVMN SLEPKGLAYY NNLLNELLKV LFTYFGDRAY APNSPQRLSL 

        70         80         90        100        110        120 
SLSGVFHLLR GTADFYALNH YSSRDKYGLP KLLLTEDGYG DDGQLDDFEK NYLNATLQAM 

       130        140 
YLMKEQNVTS VHYTVNKCMN 

« Hide

References

[1]"Purification and characterization of myrosinase from the cabbage aphid (Brevicoryne brassicae), a brassica herbivore."
Pontoppidan B., Ekbom B., Eriksson S., Meijer J.
Eur. J. Biochem. 268:1041-1048(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.

Cross-references

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR017853. Glycoside_hydrolase_SF.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMYRO2_BREBR
AccessionPrimary (citable) accession number: P83179
Entry history
Integrated into UniProtKB/Swiss-Prot: January 17, 2003
Last sequence update: March 23, 2010
Last modified: February 19, 2014
This is version 38 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries