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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 – 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
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-KW
Complete GO annotation...

Keywords - Cellular componenti

Vacuole

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        10         20         30         40         50
DEEITCQENL PFTCGNTDAL NSSSFSSDFI FGVASSAYQI EGTIGRGLNI
60 70 80 90 100
WDGFTHRYPN KSGPDHGNGD TTCDSFSYWQ KDIDVLDELN ATGYRFSIAW
110 120 130 140 150
SRIIPRGKRS RGVNEKGIDY YHGLISGLIK KGITPFVTLF HWDLPQTLQD
160 170 180 190 200
EYEGFLDPQI IDDFKDYADL CFEEFGDSVK YWLTINQLYS VPTRGYGSAL
210 220 230 240 250
DAPGRCSPTV DPSCYAGNSS TEPYIVAHHQ LLAHAKVVDL YRKNYTHQGG
260 270 280 290 300
KIGPTMITRW FLPYNDTDRH SIAATERMKE FFLGWFMGPL TNGTYPQIMI
310 320 330 340 350
DTVGERLPSF SPEESNLVKG SYDFLGLNYY FTQYAQPSPN PVNSTNHTAM
360 370 380 390 400
MDAGAKLTYI NASGHYIGPL FEKDKADSTD NIYYYPKGIY SVMDYFKNKY
410 420 430 440 450
YNPLIYVTEN GISTPGDENR NQSMLDYTRI DYLCSHLCFL NKVIKEKDVN
460 470 480 490 500
VKGYLAWALG DNYEFNKGFT VRFGLSYIDW NNVTDRDLKK SGQWYQSFIS

P
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:
EMBLi
GenBanki
DDBJi
Links Updated
X59878 mRNA. Translation: CAA42533.1.
PIRiS19146.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59878 mRNA. Translation: CAA42533.1 .
PIRi S19146.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

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: November 26, 2014
This is version 92 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