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Q95X01 (MYRO1_BREBR) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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 1

EC=3.2.1.147
Alternative name(s):
Beta-glucosidase 1
Beta-thioglucosidase 1
Beta-thioglucosidase glucohydrolase 1
Sinigrinase 1
Thioglucosidase 1
OrganismBrevicoryne brassicae (Cabbage aphid)
Taxonomic identifier69196 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraParaneopteraHemipteraSternorrhynchaAphidiformesAphidoideaAphididaeMacrosiphiniBrevicoryne

Protein attributes

Sequence length464 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Hydrolyzes glucosinolates to a labile aglycone. This rapidly undergoes spontaneous rearrangement, eliminating sulfur to yield a number of toxic metabolites. Thereby developing a chemical defense system that exploits and mimics the host plant. Ref.1 Ref.5

Catalytic activity

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

Subunit structure

Homodimer. Ref.2

Tissue specificity

Expressed in the skeletal muscle tissues surrounding the head, abdomen and thorax. Not expressed in flight muscles (at protein level). Ref.4 Ref.5

Developmental stage

Expression in the head and thoracic muscle starts during embryonic development and levels continue to accumulate after the nymphs are born (at protein level). Ref.5

Sequence similarities

Belongs to the glycosyl hydrolase 1 family. Ref.1

Biophysicochemical properties

Kinetic parameters:

KM=0.613 mM for allylglucosinolate Ref.3

KM=0.915 mM for benzylglucosinolate Ref.3

pH dependence:

Optimum pH is 5.5 with sinigrin as substrate. Ref.3

Mass spectrometry

Molecular mass is 54000±500 Da from positions 1 - 464. Determined by MALDI. Ref.3

Ontologies

Keywords
   LigandMetal-binding
Zinc
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

thioglucosidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 464464Myrosinase 1
PRO_0000392945

Sites

Active site1671Nucleophile Ref.2
Active site3741Proton donor Ref.2
Metal binding391Zinc; shared with dimeric partner By similarity UniProtKB P29736
Metal binding521Zinc; shared with dimeric partner By similarity UniProtKB P29736
Binding site191Substrate By similarity UniProtKB P29736
Binding site1221Substrate By similarity UniProtKB P29736
Binding site1661Substrate By similarity UniProtKB P29736

Amino acid modifications

Glycosylation3971N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict1071N → P AA sequence Ref.3
Sequence conflict3221P → N AA sequence Ref.3

Secondary structure

............................................................................. 464
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q95X01 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 02E76E24504C393A

FASTA46453,736
        10         20         30         40         50         60 
MDYKFPKDFM FGTSTASYQI EGGWNEDGKG ENIWDRLVHT SPEVIKDGTN GDIACDSYHK 

        70         80         90        100        110        120 
YKEDVAIIKD LNLKFYRFSI SWARIAPSGV MNSLEPKGIA YYNNLINELI KNDIIPLVTM 

       130        140        150        160        170        180 
YHWDLPQYLQ DLGGWVNPIM SDYFKEYARV LFTYFGDRVK WWITFNEPIA VCKGYSIKAY 

       190        200        210        220        230        240 
APNLNLKTTG HYLAGHTQLI AHGKAYRLYE EMFKPTQNGK ISISISGVFF MPKNAESDDD 

       250        260        270        280        290        300 
IETAERANQF ERGWFGHPVY KGDYPPIMKK WVDQKSKEEG LPWSKLPKFT KDEIKLLKGT 

       310        320        330        340        350        360 
ADFYALNHYS SRLVTFGSDP NPNFNPDASY VTSVDEAWLK PNETPYIIPV PEGLRKLLIW 

       370        380        390        400        410        420 
LKNEYGNPQL LITENGYGDD GQLDDFEKIS YLKNYLNATL QAMYEDKCNV IGYTVWSLLD 

       430        440        450        460 
NFEWFYGYSI HFGLVKIDFN DPQRTRTKRE SYTYFKNVVS TGKP 

« Hide

References

[1]"Characterization and evolution of a myrosinase from the cabbage aphid Brevicoryne brassicae."
Jones A.M., Winge P., Bones A.M., Cole R., Rossiter J.T.
Insect Biochem. Mol. Biol. 32:275-284(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PROTEIN SEQUENCE OF 98-111; 188-197; 253-261; 313-327 AND 389-393.
[2]"Crystal structure at 1.1 Angstroms resolution of an insect myrosinase from Brevicoryne brassicae shows its close relationship to beta-glucosidases."
Husebye H., Arzt S., Burmeister W.P., Hartel F.V., Brandt A., Rossiter J.T., Bones A.M.
Insect Biochem. Mol. Biol. 35:1311-1320(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, ACTIVE SITE GLU-167, ACTIVE SITE GLU-374, X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS).
[3]"Purification and characterisation of a non-plant myrosinase from the cabbage aphid Brevicoryne brassicae (L.)."
Jones A.M., Bridges M., Bones A.M., Cole R., Rossiter J.T.
Insect Biochem. Mol. Biol. 31:1-5(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MASS SPECTROMETRY, PROTEIN SEQUENCE OF 98-111; 188-197; 253-261; 313-327 AND 389-393.
[4]"Spatial organization of the glucosinolate-myrosinase system in brassica specialist aphids is similar to that of the host plant."
Bridges M., Jones A.M., Bones A.M., Hodgson C., Cole R., Bartlet E., Wallsgrove R., Karapapa V.K., Watts N., Rossiter J.T.
Proc. R. Soc. B 269:187-191(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[5]"The cabbage aphid: a walking mustard oil bomb."
Kazana E., Pope T.W., Tibbles L., Bridges M., Pickett J.A., Bones A.M., Powell G., Rossiter J.T.
Proc. R. Soc. B 274:2271-2277(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF203780 mRNA. Translation: AAL25999.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1WCGX-ray1.10A/B1-464[»]
ProteinModelPortalQ95X01.
SMRQ95X01. Positions 3-464.
ModBaseSearch...
MobiDBSearch...

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. SSF51445. 1 hit.
PROSITEPS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ95X01.

Entry information

Entry nameMYRO1_BREBR
AccessionPrimary (citable) accession number: Q95X01
Entry history
Integrated into UniProtKB/Swiss-Prot: March 23, 2010
Last sequence update: December 1, 2001
Last modified: February 19, 2014
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries