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P29736

- MYRA_SINAL

UniProt

P29736 - MYRA_SINAL

Protein

Myrosinase MA1

Gene
N/A
Organism
Sinapis alba (White mustard) (Brassica hirta)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 90 (01 Oct 2014)
      Sequence version 2 (16 May 2006)
      Previous versions | rss
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    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.

    Catalytic activityi

    A thioglucoside + H2O = a sugar + a thiol.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei39 – 391Substrate
    Metal bindingi56 – 561Zinc; shared with dimeric partner
    Metal bindingi70 – 701Zinc; shared with dimeric partner
    Binding sitei141 – 1411Substrate
    Binding sitei186 – 1861Substrate
    Binding sitei187 – 1871Ascorbate1 Publication
    Binding sitei259 – 2591Ascorbate1 Publication
    Binding sitei330 – 3301SubstrateBy similarity
    Active sitei409 – 4091Nucleophile
    Binding sitei457 – 4571SubstrateBy similarity

    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 MA1 (EC:3.2.1.147)
    Alternative name(s):
    Sinigrinase
    Thioglucosidase
    OrganismiSinapis alba (White mustard) (Brassica hirta)
    Taxonomic identifieri3728 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeBrassiceaeSinapis

    Subcellular locationi

    GO - Cellular componenti

    1. vacuole Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Vacuole

    Pathology & Biotechi

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 501501Myrosinase MA1PRO_0000063901Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi6 ↔ 438
    Disulfide bondi14 ↔ 434
    Glycosylationi21 – 211N-linked (GlcNAc...)3 Publications
    Glycosylationi60 – 601N-linked (GlcNAc...)3 Publications
    Glycosylationi90 – 901N-linked (GlcNAc...)3 Publications
    Disulfide bondi206 ↔ 214
    Glycosylationi218 – 2181N-linked (GlcNAc...)3 Publications
    Glycosylationi244 – 2441N-linked (GlcNAc...)3 Publications
    Glycosylationi265 – 2651N-linked (GlcNAc...)3 Publications
    Glycosylationi292 – 2921N-linked (GlcNAc...)3 Publications
    Glycosylationi343 – 3431N-linked (GlcNAc...)3 Publications
    Glycosylationi346 – 3461N-linked (GlcNAc...)3 Publications
    Glycosylationi361 – 3611N-linked (GlcNAc...)3 Publications
    Glycosylationi482 – 4821N-linked (GlcNAc...)3 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Expressioni

    Tissue specificityi

    In vacuoles called myrosin grains of a certain class of cells, myrosin cells, distributed in the cotyledons and the axis of the embryo as well as in different organs of the growing plant.

    Interactioni

    Subunit structurei

    Homodimer.3 Publications

    Structurei

    Secondary structure

    1
    501
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi9 – 113
    Turni17 – 193
    Helixi22 – 243
    Beta strandi30 – 345
    Helixi37 – 404
    Helixi50 – 578
    Helixi59 – 624
    Beta strandi69 – 713
    Helixi75 – 8915
    Beta strandi92 – 976
    Helixi100 – 1034
    Helixi109 – 1113
    Helixi115 – 13016
    Beta strandi134 – 1429
    Helixi146 – 1527
    Helixi154 – 1563
    Helixi160 – 17516
    Turni176 – 1783
    Beta strandi181 – 1866
    Helixi190 – 1967
    Turni208 – 2103
    Turni219 – 2213
    Helixi222 – 24423
    Helixi246 – 2483
    Beta strandi251 – 2533
    Beta strandi255 – 26511
    Helixi269 – 28214
    Helixi284 – 2929
    Helixi297 – 3037
    Helixi304 – 3063
    Helixi312 – 3187
    Beta strandi323 – 33715
    Helixi349 – 3535
    Beta strandi355 – 3606
    Beta strandi368 – 3725
    Helixi378 – 3803
    Helixi387 – 39913
    Beta strandi405 – 4095
    Helixi420 – 4245
    Helixi427 – 44721
    Beta strandi451 – 4577
    Turni465 – 4673
    Beta strandi470 – 4723
    Beta strandi475 – 4795
    Beta strandi482 – 4887
    Helixi490 – 49910

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1DWAX-ray2.00M3-501[»]
    1DWFX-ray2.00M3-501[»]
    1DWGX-ray2.00M3-501[»]
    1DWHX-ray2.00M3-501[»]
    1DWIX-ray2.00M3-501[»]
    1DWJX-ray2.40M3-501[»]
    1E4MX-ray1.20M1-501[»]
    1E6QX-ray1.35M1-501[»]
    1E6SX-ray1.35M1-501[»]
    1E6XX-ray1.60M1-501[»]
    1E70X-ray1.65M1-501[»]
    1E71X-ray1.50M1-501[»]
    1E72X-ray1.60M1-501[»]
    1E73X-ray1.50M1-501[»]
    1MYRX-ray1.64A1-501[»]
    1W9BX-ray1.70M1-501[»]
    1W9DX-ray1.60M1-501[»]
    2WXDX-ray1.60M1-501[»]
    ProteinModelPortaliP29736.
    SMRiP29736. Positions 3-501.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP29736.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni464 – 4652Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 1 family.Curated

    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.
    PROSITEiPS00572. GLYCOSYL_HYDROL_F1_1. 1 hit.
    PS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P29736-1 [UniParc]FASTAAdd to Basket

    « Hide

    DEEITCQENL PFTCGNTDAL NSSSFSSDFI FGVASSAYQI EGTIGRGLNI    50
    WDGFTHRYPN KSGPDHGNGD TTCDSFSYWQ KDIDVLDELN ATGYRFSIAW 100
    SRIIPRGKRS RGVNEKGIDY YHGLISGLIK KGITPFVTLF HWDLPQTLQD 150
    EYEGFLDPQI IDDFKDYADL CFEEFGDSVK YWLTINQLYS VPTRGYGSAL 200
    DAPGRCSPTV DPSCYAGNSS TEPYIVAHHQ LLAHAKVVDL YRKNYTHQGG 250
    KIGPTMITRW FLPYNDTDRH SIAATERMKE FFLGWFMGPL TNGTYPQIMI 300
    DTVGERLPSF SPEESNLVKG SYDFLGLNYY FTQYAQPSPN PVNSTNHTAM 350
    MDAGAKLTYI NASGHYIGPL FEKDKADSTD NIYYYPKGIY SVMDYFKNKY 400
    YNPLIYVTEN GISTPGDENR NQSMLDYTRI DYLCSHLCFL NKVIKEKDVN 450
    VKGYLAWALG DNYEFNKGFT VRFGLSYIDW NNVTDRDLKK SGQWYQSFIS 500
    P 501
    Length:501
    Mass (Da):57,023
    Last modified:May 16, 2006 - v2
    Checksum:i23EAA1FEFFDEBF02
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti373 – 3742KD → EN in CAA42533. (PubMed:1731996)Curated
    Sequence conflicti378 – 3803STD → ETK in CAA42533. (PubMed:1731996)Curated
    Sequence conflicti497 – 4971S → K in CAA42533. (PubMed:1731996)Curated
    Sequence conflicti501 – 5011P → PGIKSPLKKDFLRSSLTFEK NKKLADA(PubMed:1731996)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X59878 mRNA. Translation: CAA42533.1.
    PIRiS19146.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X59878 mRNA. Translation: CAA42533.1 .
    PIRi S19146.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1DWA X-ray 2.00 M 3-501 [» ]
    1DWF X-ray 2.00 M 3-501 [» ]
    1DWG X-ray 2.00 M 3-501 [» ]
    1DWH X-ray 2.00 M 3-501 [» ]
    1DWI X-ray 2.00 M 3-501 [» ]
    1DWJ X-ray 2.40 M 3-501 [» ]
    1E4M X-ray 1.20 M 1-501 [» ]
    1E6Q X-ray 1.35 M 1-501 [» ]
    1E6S X-ray 1.35 M 1-501 [» ]
    1E6X X-ray 1.60 M 1-501 [» ]
    1E70 X-ray 1.65 M 1-501 [» ]
    1E71 X-ray 1.50 M 1-501 [» ]
    1E72 X-ray 1.60 M 1-501 [» ]
    1E73 X-ray 1.50 M 1-501 [» ]
    1MYR X-ray 1.64 A 1-501 [» ]
    1W9B X-ray 1.70 M 1-501 [» ]
    1W9D X-ray 1.60 M 1-501 [» ]
    2WXD X-ray 1.60 M 1-501 [» ]
    ProteinModelPortali P29736.
    SMRi P29736. Positions 3-501.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    DrugBanki DB00126. Vitamin C.

    Protein family/group databases

    CAZyi GH1. Glycoside Hydrolase Family 1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P29736.

    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 PS00572. GLYCOSYL_HYDROL_F1_1. 1 hit.
    PS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The glucosinolate-degrading enzyme myrosinase in Brassicaceae is encoded by a gene family."
      Xue J., Lenman M., Falk A., Rask L.
      Plant Mol. Biol. 18:387-398(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 280-501, PARTIAL PROTEIN SEQUENCE.
      Strain: cv. Maxi.
      Tissue: Seed.
    2. "The crystal structures of Sinapis alba myrosinase and a covalent glycosyl-enzyme intermediate provide insights into the substrate recognition and active-site machinery of an S-glycosidase."
      Burmeister W.P., Cottaz S., Driguez H., Iori R., Palmieri S., Henrissat B.
      Structure 5:663-675(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.64 ANGSTROMS), SUBUNIT, GLYCOSYLATION AT ASN-21; ASN-60; ASN-90; ASN-218; ASN-244; ASN-265; ASN-292; ASN-343; ASN-346; ASN-361 AND ASN-482.
      Strain: cv. Emergo.
      Tissue: Seed.
    3. "High resolution X-ray crystallography shows that ascorbate is a cofactor for myrosinase and substitutes for the function of the catalytic base."
      Burmeister W.P., Cottaz S., Rollin P., Vasella A., Henrissat B.
      J. Biol. Chem. 275:39385-39393(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) IN COMPLEX WITH ASCORBATE AND TRANSITION STATE ANALOGS, SUBUNIT, GLYCOSYLATION AT ASN-21; ASN-60; ASN-90; ASN-218; ASN-244; ASN-265; ASN-292; ASN-343; ASN-346; ASN-361 AND ASN-482.
      Strain: cv. Emergo.
      Tissue: Seed.
    4. "The glucosinolate-myrosinase system. New insights into enzyme-substrate interactions by use of simplified inhibitors."
      Bourderioux A., Lefoix M., Gueyrard D., Tatibouet A., Cottaz S., Arzt S., Burmeister W.P., Rollin P.
      Org. Biomol. Chem. 3:1872-1879(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS), SUBUNIT, GLYCOSYLATION AT ASN-21; ASN-60; ASN-90; ASN-218; ASN-244; ASN-265; ASN-292; ASN-343; ASN-346; ASN-361 AND ASN-482.

    Entry informationi

    Entry nameiMYRA_SINAL
    AccessioniPrimary (citable) accession number: P29736
    Secondary accession number(s): Q7SIB0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: May 16, 2006
    Last modified: October 1, 2014
    This is version 90 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    It seems that the absence of a catalytic proton donor in plant myrosinases is not impairing the hydrolysis of glucosinolates.

    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