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Protein

Myrosinase MA1

Gene
N/A
Organism
Sinapis alba (White mustard) (Brassica hirta)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Binding sitei39Substrate1
Metal bindingi56Zinc; shared with dimeric partner1
Metal bindingi70Zinc; shared with dimeric partner1
Binding sitei141Substrate1
Binding sitei186Substrate1
Binding sitei187Ascorbate1 Publication1
Binding sitei259Ascorbate1 Publication1
Binding sitei330SubstrateBy similarity1
Active sitei409Nucleophile1
Binding sitei457SubstrateBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.2.1.147. 5734.

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

Complete GO annotation...

Keywords - Cellular componenti

Vacuole

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000639011 – 501Myrosinase MA1Add BLAST501

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi6 ↔ 438
Disulfide bondi14 ↔ 434
Glycosylationi21N-linked (GlcNAc...)3 Publications1
Glycosylationi60N-linked (GlcNAc...)3 Publications1
Glycosylationi90N-linked (GlcNAc...)3 Publications1
Disulfide bondi206 ↔ 214
Glycosylationi218N-linked (GlcNAc...)3 Publications1
Glycosylationi244N-linked (GlcNAc...)3 Publications1
Glycosylationi265N-linked (GlcNAc...)3 Publications1
Glycosylationi292N-linked (GlcNAc...)3 Publications1
Glycosylationi343N-linked (GlcNAc...)3 Publications1
Glycosylationi346N-linked (GlcNAc...)3 Publications1
Glycosylationi361N-linked (GlcNAc...)3 Publications1
Glycosylationi482N-linked (GlcNAc...)3 Publications1

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

1501
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi9 – 11Combined sources3
Turni17 – 19Combined sources3
Helixi22 – 24Combined sources3
Beta strandi30 – 34Combined sources5
Helixi37 – 40Combined sources4
Helixi50 – 57Combined sources8
Helixi59 – 62Combined sources4
Beta strandi69 – 71Combined sources3
Helixi75 – 89Combined sources15
Beta strandi92 – 97Combined sources6
Helixi100 – 103Combined sources4
Helixi109 – 111Combined sources3
Helixi115 – 130Combined sources16
Beta strandi134 – 142Combined sources9
Helixi146 – 152Combined sources7
Helixi154 – 156Combined sources3
Helixi160 – 175Combined sources16
Turni176 – 178Combined sources3
Beta strandi181 – 186Combined sources6
Helixi190 – 196Combined sources7
Turni208 – 210Combined sources3
Turni219 – 221Combined sources3
Helixi222 – 244Combined sources23
Helixi246 – 248Combined sources3
Beta strandi251 – 253Combined sources3
Beta strandi255 – 265Combined sources11
Helixi269 – 282Combined sources14
Helixi284 – 292Combined sources9
Helixi297 – 303Combined sources7
Helixi304 – 306Combined sources3
Helixi312 – 318Combined sources7
Beta strandi323 – 337Combined sources15
Helixi349 – 353Combined sources5
Beta strandi355 – 360Combined sources6
Beta strandi368 – 372Combined sources5
Helixi378 – 380Combined sources3
Helixi387 – 399Combined sources13
Beta strandi405 – 409Combined sources5
Helixi420 – 424Combined sources5
Helixi427 – 447Combined sources21
Beta strandi451 – 457Combined sources7
Turni465 – 467Combined sources3
Beta strandi470 – 472Combined sources3
Beta strandi475 – 479Combined sources5
Beta strandi482 – 488Combined sources7
Helixi490 – 499Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP29736.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni464 – 465Substrate bindingBy similarity2

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.
IPR033132. Glyco_hydro_1_N_CS.
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)DescriptionActionsGraphical viewLength
Sequence conflicti373 – 374KD → EN in CAA42533 (PubMed:1731996).Curated2
Sequence conflicti378 – 380STD → ETK in CAA42533 (PubMed:1731996).Curated3
Sequence conflicti497S → K in CAA42533 (PubMed:1731996).Curated1
Sequence conflicti501P → PGIKSPLKKDFLRSSLTFEK NKKLADA (PubMed:1731996).Curated1

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.
PIRiS19146.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH1. Glycoside Hydrolase Family 1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.2.1.147. 5734.

Miscellaneous databases

EvolutionaryTraceiP29736.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001360. Glyco_hydro_1.
IPR018120. Glyco_hydro_1_AS.
IPR033132. Glyco_hydro_1_N_CS.
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]
ProtoNetiSearch...

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 2, 2016
This is version 98 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

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.