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Protein

Myrosinase 2

Gene
N/A
Organism
Brevicoryne brassicae (Mealy cabbage aphid)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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 similarity1 Publication

Catalytic activityi

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

Enzyme regulationi

Inhibited by ascorbate.1 Publication

Kineticsi

  1. KM=0.41 mM for sinigrin (at pH 4.5 and 37 degrees Celsius)1 Publication
  2. KM=0.52 mM for p-nitrophenyl-beta-glucopyranoside (at pH 4.5 and 37 degrees Celsius)1 Publication

    Temperature dependencei

    Optimum temperature is about 40 degrees Celsius.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei70 – 701NucleophilePROSITE-ProRule annotation

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Names & Taxonomyi

    Protein namesi
    Recommended 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
    OrganismiBrevicoryne brassicae (Mealy cabbage aphid)Curated
    Taxonomic identifieri69196 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraParaneopteraHemipteraSternorrhynchaAphidiformesAphidoideaAphididaeMacrosiphiniBrevicoryne

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini‹1 – ›140›140Myrosinase 2PRO_0000063904Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi114 – 1141N-linked (GlcNAc...)Sequence analysis
    Glycosylationi127 – 1271N-linked (GlcNAc...)Sequence analysis

    Keywords - PTMi

    Glycoprotein

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 1 family.Curated

    Family and domain databases

    InterProiIPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.

    Sequencei

    Sequence statusi: Fragments.

    P83179-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    DFMFGTSTAS GGLAPSGVMN SLEPKGLAYY NNLLNELLKV LFTYFGDRAY
    60 70 80 90 100
    APNSPQRLSL SLSGVFHLLR GTADFYALNH YSSRDKYGLP KLLLTEDGYG
    110 120 130 140
    DDGQLDDFEK NYLNATLQAM YLMKEQNVTS VHYTVNKCMN
    Length:140
    Mass (Da):15,646
    Last modified:March 23, 2010 - v2
    Checksum:iA03EF5F737CD8ABD
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei1 – 111 Publication
    Non-adjacent residuesi12 – 1321 Publication
    Non-adjacent residuesi26 – 2721 Publication
    Non-adjacent residuesi35 – 3621 Publication
    Non-adjacent residuesi44 – 4521 Publication
    Non-adjacent residuesi58 – 5921 Publication
    Non-adjacent residuesi84 – 8521 Publication
    Non-adjacent residuesi97 – 9821 Publication
    Non-adjacent residuesi111 – 11221 Publication
    Non-adjacent residuesi124 – 12521 Publication
    Non-terminal residuei140 – 14011 Publication

    Cross-referencesi

    3D structure databases

    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Family and domain databases

    InterProiIPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiMYRO2_BREBR
    AccessioniPrimary (citable) accession number: P83179
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 17, 2003
    Last sequence update: March 23, 2010
    Last modified: July 6, 2016
    This is version 41 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Caution

    The order of the peptides shown is unknown.Curated

    Keywords - Technical termi

    Direct protein sequencing

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    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 one 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.