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P29092

- MYR3_SINAL

UniProt

P29092 - MYR3_SINAL

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Protein

Myrosinase MB3

Gene
N/A
Organism
Sinapis alba (White mustard) (Brassica hirta)
Status
Reviewed - 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.

Catalytic activityi

A thioglucoside + H2O = a sugar + a thiol.

Cofactori

L-ascorbateBy similarityNote: Binds 1 ascorbate molecule per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei59 – 591SubstrateBy similarity
Metal bindingi76 – 761Zinc; shared with dimeric partnerBy similarity
Metal bindingi90 – 901Zinc; shared with dimeric partnerBy similarity
Binding sitei161 – 1611SubstrateBy similarity
Binding sitei206 – 2061SubstrateBy similarity
Binding sitei207 – 2071AscorbateBy similarity
Binding sitei281 – 2811AscorbateBy similarity
Active sitei426 – 4261NucleophilePROSITE-ProRule annotation
Binding sitei426 – 4261SubstrateBy similarity
Binding sitei481 – 4811SubstrateBy 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 MB3 (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
Signal peptidei1 – 2020Add
BLAST
Chaini21 – 544524Myrosinase MB3PRO_0000011775Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi26 ↔ 455By similarity
Disulfide bondi34 ↔ 451By similarity
Glycosylationi110 – 1101N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi226 ↔ 236By similarity
Glycosylationi240 – 2401N-linked (GlcNAc...)Sequence Analysis
Glycosylationi331 – 3311N-linked (GlcNAc...)Sequence Analysis
Glycosylationi382 – 3821N-linked (GlcNAc...)Sequence Analysis
Glycosylationi517 – 5171N-linked (GlcNAc...)Sequence Analysis

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.

Structurei

3D structure databases

ProteinModelPortaliP29092.
SMRiP29092. Positions 23-517.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 1 family.Curated

Keywords - Domaini

Signal

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P29092-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKLLHGLALV FLLAAASCKA DEEITCEENE PFTCSNTDIL SSKNFGKDFI
60 70 80 90 100
FGVASSAYQI EGGRGRGVNV WDGFSHRYPE KSGSDLKNGD TSCESYTRWK
110 120 130 140 150
KDVEIMGELN ATGYRFSFAW SRIVPKGKVS RGVDQAGLDY YHNLIDALLE
160 170 180 190 200
KNITPFVTLF HWDLPQTLQD EYEGFLDRQI IQDFKDYADL CFKEFGGKVK
210 220 230 240 250
NWITINQLYT VPTRGYALGT DAPGRCSPKV DTKQRCYGGN SSTEPYIVAH
260 270 280 290 300
NQLLAHAAIV DLYRTNYAFQ NGKIGPVMIT RWFLPYDESD PACIEAAERM
310 320 330 340 350
NQFFHGWYME PLTKGRYPDI MRQIVGSRLP NFTEAEAELV AGSYDFLGLN
360 370 380 390 400
YYVTQYAKPK PNPYPSETHT ALMDAGVDLT FNNSRGEYPG PVFAEDANSY
410 420 430 440 450
YYPKGIYYVM DYFKTKYNNP LIYITENGIS TPGSESRCEA IADYKRINYL
460 470 480 490 500
CSHLCFLRKV IREKGVNIRG YFAWALGDNY EFCKGFTVRF GLSYVNWDDL
510 520 530 540
DDRNLKESGK WYQRFINGTA KNPVKQDFLR SSLSSQSQKK RLAC
Length:544
Mass (Da):62,050
Last modified:December 1, 1992 - v1
Checksum:i3971D3304CF75C28
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59879 mRNA. Translation: CAA42534.1.
PIRiS19149.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59879 mRNA. Translation: CAA42534.1 .
PIRi S19149.

3D structure databases

ProteinModelPortali P29092.
SMRi P29092. Positions 23-517.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH1. Glycoside Hydrolase Family 1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

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], PARTIAL PROTEIN SEQUENCE.
    Strain: cv. Maxi.
    Tissue: Seed.

Entry informationi

Entry nameiMYR3_SINAL
AccessioniPrimary (citable) accession number: P29092
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: November 26, 2014
This is version 81 of the entry and version 1 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

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

External Data

Dasty 3