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Q95X01

- MYRO1_BREBR

UniProt

Q95X01 - MYRO1_BREBR

Protein

Myrosinase 1

Gene
N/A
Organism
Brevicoryne brassicae (Cabbage aphid)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 55 (01 Oct 2014)
      Sequence version 1 (01 Dec 2001)
      Previous versions | rss
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    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

    1. metal ion binding Source: UniProtKB-KW
    2. thioglucosidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. carbohydrate metabolic process Source: InterPro

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Ligandi

    Metal-binding, Zinc

    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 – 145
    Helixi17 – 204
    Helixi33 – 408
    Helixi42 – 443
    Beta strandi51 – 533
    Helixi57 – 7115
    Beta strandi74 – 796
    Helixi82 – 854
    Helixi96 – 11116
    Beta strandi115 – 1239
    Helixi127 – 1315
    Helixi134 – 1363
    Helixi140 – 15516
    Turni156 – 1583
    Beta strandi161 – 1666
    Helixi168 – 1769
    Beta strandi177 – 1804
    Helixi187 – 21226
    Helixi214 – 2174
    Beta strandi220 – 2256
    Beta strandi229 – 2346
    Helixi238 – 25114
    Helixi253 – 2608
    Beta strandi262 – 2643
    Helixi266 – 27813
    Helixi291 – 2977
    Beta strandi302 – 3076
    Beta strandi311 – 3177
    Helixi326 – 3283
    Beta strandi330 – 3334
    Helixi336 – 3383
    Helixi351 – 36515
    Beta strandi370 – 3756
    Helixi386 – 40621
    Beta strandi410 – 4167
    Helixi424 – 4296
    Beta strandi434 – 4374
    Beta strandi446 – 4483
    Helixi450 – 46112

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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

    MDYKFPKDFM FGTSTASYQI EGGWNEDGKG ENIWDRLVHT SPEVIKDGTN    50
    GDIACDSYHK YKEDVAIIKD LNLKFYRFSI SWARIAPSGV MNSLEPKGIA 100
    YYNNLINELI KNDIIPLVTM YHWDLPQYLQ DLGGWVNPIM SDYFKEYARV 150
    LFTYFGDRVK WWITFNEPIA VCKGYSIKAY APNLNLKTTG HYLAGHTQLI 200
    AHGKAYRLYE EMFKPTQNGK ISISISGVFF MPKNAESDDD IETAERANQF 250
    ERGWFGHPVY KGDYPPIMKK WVDQKSKEEG LPWSKLPKFT KDEIKLLKGT 300
    ADFYALNHYS SRLVTFGSDP NPNFNPDASY VTSVDEAWLK PNETPYIIPV 350
    PEGLRKLLIW LKNEYGNPQL LITENGYGDD GQLDDFEKIS YLKNYLNATL 400
    QAMYEDKCNV IGYTVWSLLD NFEWFYGYSI HFGLVKIDFN DPQRTRTKRE 450
    SYTYFKNVVS TGKP 464
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF203780 mRNA. Translation: AAL25999.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF203780 mRNA. Translation: AAL25999.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1WCG X-ray 1.10 A/B 1-464 [» ]
    ProteinModelPortali Q95X01.
    SMRi Q95X01. Positions 3-464.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH1. Glycoside Hydrolase Family 1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei Q95X01.

    Family and domain databases

    Gene3Di 3.20.20.80. 1 hit.
    InterProi IPR001360. Glyco_hydro_1.
    IPR018120. Glyco_hydro_1_AS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    PANTHERi PTHR10353. PTHR10353. 1 hit.
    Pfami PF00232. Glyco_hydro_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00131. GLHYDRLASE1.
    SUPFAMi SSF51445. SSF51445. 1 hit.
    PROSITEi PS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    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: October 1, 2014
    This is version 55 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