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P29736

- MYRA_SINAL

UniProt

P29736 - MYRA_SINAL

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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

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 – 1871Ascorbate
Binding sitei259 – 2591Ascorbate
Binding sitei330 – 3301Substrate By similarity
Active sitei409 – 4091Nucleophile
Binding sitei457 – 4571Substrate By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
Complete GO annotation...

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
Complete GO annotation...

Keywords - Cellular componenti

Vacuole

Pathology & Biotechi

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 501501Myrosinase MA1
PRO_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

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.

Miscellaneous databases

EvolutionaryTraceiP29736.

Family & Domainsi

Region

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

Sequence similaritiesi

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti373 – 3742KD → EN in CAA42533. 1 Publication
Sequence conflicti378 – 3803STD → ETK in CAA42533. 1 Publication
Sequence conflicti497 – 4971S → K in CAA42533. 1 Publication
Sequence conflicti501 – 5011P → PGIKSPLKKDFLRSSLTFEK NKKLADA1 Publication

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...

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: February 19, 2014
This is version 89 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

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