Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Myrosinase 1

Gene
N/A
Organism
Brevicoryne brassicae (Cabbage aphid)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

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

Kineticsi

  1. KM=0.613 mM for allylglucosinolate1 Publication
  2. KM=0.915 mM for benzylglucosinolate1 Publication

    pH dependencei

    Optimum pH is 5.5 with sinigrin as substrate.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei19 – 191SubstrateBy similarity
    Metal bindingi39 – 391Zinc; shared with dimeric partnerBy similarity
    Metal bindingi52 – 521Zinc; shared with dimeric partnerBy similarity
    Binding sitei122 – 1221SubstrateBy similarity
    Binding sitei166 – 1661SubstrateBy similarity
    Active sitei167 – 1671Nucleophile1 Publication
    Active sitei374 – 3741Proton donor1 Publication

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BRENDAi3.2.1.147. 981.

    Protein family/group databases

    CAZyiGH1. Glycoside Hydrolase Family 1.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Myrosinase 11 Publication (EC:3.2.1.147)
    Alternative name(s):
    Beta-glucosidase 11 Publication
    Beta-thioglucosidase 11 Publication
    Beta-thioglucosidase glucohydrolase 11 Publication
    Sinigrinase 11 Publication
    Thioglucosidase 1Imported
    OrganismiBrevicoryne brassicae (Cabbage aphid)
    Taxonomic identifieri69196 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraParaneopteraHemipteraSternorrhynchaAphidiformesAphidoideaAphididaeMacrosiphiniBrevicoryne

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 464464Myrosinase 1PRO_0000392945Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi397 – 3971N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Expressioni

    Tissue specificityi

    Expressed in the skeletal muscle tissues surrounding the head, abdomen and thorax. Not expressed in flight muscles (at protein level).2 Publications

    Developmental stagei

    Expression in the head and thoracic muscle starts during embryonic development and levels continue to accumulate after the nymphs are born (at protein level).1 Publication

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Structurei

    Secondary structure

    1
    464
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi10 – 145Combined sources
    Helixi17 – 204Combined sources
    Helixi33 – 408Combined sources
    Helixi42 – 443Combined sources
    Beta strandi51 – 533Combined sources
    Helixi57 – 7115Combined sources
    Beta strandi74 – 796Combined sources
    Helixi82 – 854Combined sources
    Helixi96 – 11116Combined sources
    Beta strandi115 – 1239Combined sources
    Helixi127 – 1315Combined sources
    Helixi134 – 1363Combined sources
    Helixi140 – 15516Combined sources
    Turni156 – 1583Combined sources
    Beta strandi161 – 1666Combined sources
    Helixi168 – 1769Combined sources
    Beta strandi177 – 1804Combined sources
    Helixi187 – 21226Combined sources
    Helixi214 – 2174Combined sources
    Beta strandi220 – 2256Combined sources
    Beta strandi229 – 2346Combined sources
    Helixi238 – 25114Combined sources
    Helixi253 – 2608Combined sources
    Beta strandi262 – 2643Combined sources
    Helixi266 – 27813Combined sources
    Helixi291 – 2977Combined sources
    Beta strandi302 – 3076Combined sources
    Beta strandi311 – 3177Combined sources
    Helixi326 – 3283Combined sources
    Beta strandi330 – 3334Combined sources
    Helixi336 – 3383Combined sources
    Helixi351 – 36515Combined sources
    Beta strandi370 – 3756Combined sources
    Helixi386 – 40621Combined sources
    Beta strandi410 – 4167Combined sources
    Helixi424 – 4296Combined sources
    Beta strandi434 – 4374Combined sources
    Beta strandi446 – 4483Combined sources
    Helixi450 – 46112Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1WCGX-ray1.10A/B1-464[»]
    ProteinModelPortaliQ95X01.
    SMRiQ95X01. Positions 3-464.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ95X01.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 1 family.1 Publication

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    InterProiIPR001360. Glyco_hydro_1.
    IPR018120. Glyco_hydro_1_AS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PANTHERiPTHR10353. PTHR10353. 1 hit.
    PfamiPF00232. Glyco_hydro_1. 1 hit.
    [Graphical view]
    PRINTSiPR00131. GLHYDRLASE1.
    SUPFAMiSSF51445. SSF51445. 1 hit.
    PROSITEiPS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q95X01-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MDYKFPKDFM FGTSTASYQI EGGWNEDGKG ENIWDRLVHT SPEVIKDGTN
    60 70 80 90 100
    GDIACDSYHK YKEDVAIIKD LNLKFYRFSI SWARIAPSGV MNSLEPKGIA
    110 120 130 140 150
    YYNNLINELI KNDIIPLVTM YHWDLPQYLQ DLGGWVNPIM SDYFKEYARV
    160 170 180 190 200
    LFTYFGDRVK WWITFNEPIA VCKGYSIKAY APNLNLKTTG HYLAGHTQLI
    210 220 230 240 250
    AHGKAYRLYE EMFKPTQNGK ISISISGVFF MPKNAESDDD IETAERANQF
    260 270 280 290 300
    ERGWFGHPVY KGDYPPIMKK WVDQKSKEEG LPWSKLPKFT KDEIKLLKGT
    310 320 330 340 350
    ADFYALNHYS SRLVTFGSDP NPNFNPDASY VTSVDEAWLK PNETPYIIPV
    360 370 380 390 400
    PEGLRKLLIW LKNEYGNPQL LITENGYGDD GQLDDFEKIS YLKNYLNATL
    410 420 430 440 450
    QAMYEDKCNV IGYTVWSLLD NFEWFYGYSI HFGLVKIDFN DPQRTRTKRE
    460
    SYTYFKNVVS TGKP
    Length:464
    Mass (Da):53,736
    Last modified:December 1, 2001 - v1
    Checksum:i02E76E24504C393A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti107 – 1071N → P AA sequence (PubMed:11102829).Curated
    Sequence conflicti322 – 3221P → N AA sequence (PubMed:11102829).Curated

    Mass spectrometryi

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

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF203780 mRNA. Translation: AAL25999.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF203780 mRNA. Translation: AAL25999.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1WCGX-ray1.10A/B1-464[»]
    ProteinModelPortaliQ95X01.
    SMRiQ95X01. Positions 3-464.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein family/group databases

    CAZyiGH1. Glycoside Hydrolase Family 1.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Enzyme and pathway databases

    BRENDAi3.2.1.147. 981.

    Miscellaneous databases

    EvolutionaryTraceiQ95X01.

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    InterProiIPR001360. Glyco_hydro_1.
    IPR018120. Glyco_hydro_1_AS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PANTHERiPTHR10353. PTHR10353. 1 hit.
    PfamiPF00232. Glyco_hydro_1. 1 hit.
    [Graphical view]
    PRINTSiPR00131. GLHYDRLASE1.
    SUPFAMiSSF51445. SSF51445. 1 hit.
    PROSITEiPS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    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. Cited for: FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.

    Entry informationi

    Entry nameiMYRO1_BREBR
    AccessioniPrimary (citable) accession number: Q95X01
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 23, 2010
    Last sequence update: December 1, 2001
    Last modified: April 1, 2015
    This is version 57 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.