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Q95X01

- MYRO1_BREBR

UniProt

Q95X01 - MYRO1_BREBR

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Protein
Myrosinase 1
Gene
N/A
Organism
Brevicoryne brassicae (Cabbage aphid)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Hydrolyzes glucosinolates to a labile aglycone. This rapidly undergoes spontaneous rearrangement, eliminating sulfur to yield a number of toxic metabolites. Thereby developing a chemical defense system that exploits and mimics the host plant.2 Publications

Catalytic activityi

A thioglucoside + H2O = a sugar + a thiol.1 Publication

Kineticsi

  1. KM=0.613 mM for allylglucosinolate1 Publication
  2. KM=0.915 mM for benzylglucosinolate1 Publication

pH dependencei

Optimum pH is 5.5 with sinigrin as substrate.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei19 – 191Substrate By similarityBy similarity
Metal bindingi39 – 391Zinc; shared with dimeric partner By similarityBy similarity
Metal bindingi52 – 521Zinc; shared with dimeric partner By similarityBy similarity
Binding sitei122 – 1221Substrate By similarityBy similarity
Binding sitei166 – 1661Substrate By similarityBy similarity
Active sitei167 – 1671Nucleophile1 Publication
Active sitei374 – 3741Proton donor1 Publication

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 1 (EC:3.2.1.147)
Alternative name(s):
Beta-glucosidase 1
Beta-thioglucosidase 1
Beta-thioglucosidase glucohydrolase 1
Sinigrinase 1
Thioglucosidase 1
OrganismiBrevicoryne brassicae (Cabbage aphid)
Taxonomic identifieri69196 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraParaneopteraHemipteraSternorrhynchaAphidiformesAphidoideaAphididaeMacrosiphiniBrevicoryne

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 464464Myrosinase 1
PRO_0000392945Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi397 – 3971N-linked (GlcNAc...) Reviewed prediction

Keywords - PTMi

Glycoprotein

Expressioni

Tissue specificityi

Expressed in the skeletal muscle tissues surrounding the head, abdomen and thorax. Not expressed in flight muscles (at protein level).2 Publications

Developmental stagei

Expression in the head and thoracic muscle starts during embryonic development and levels continue to accumulate after the nymphs are born (at protein level).1 Publication

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi10 – 145
Helixi17 – 204
Helixi33 – 408
Helixi42 – 443
Beta strandi51 – 533
Helixi57 – 7115
Beta strandi74 – 796
Helixi82 – 854
Helixi96 – 11116
Beta strandi115 – 1239
Helixi127 – 1315
Helixi134 – 1363
Helixi140 – 15516
Turni156 – 1583
Beta strandi161 – 1666
Helixi168 – 1769
Beta strandi177 – 1804
Helixi187 – 21226
Helixi214 – 2174
Beta strandi220 – 2256
Beta strandi229 – 2346
Helixi238 – 25114
Helixi253 – 2608
Beta strandi262 – 2643
Helixi266 – 27813
Helixi291 – 2977
Beta strandi302 – 3076
Beta strandi311 – 3177
Helixi326 – 3283
Beta strandi330 – 3334
Helixi336 – 3383
Helixi351 – 36515
Beta strandi370 – 3756
Helixi386 – 40621
Beta strandi410 – 4167
Helixi424 – 4296
Beta strandi434 – 4374
Beta strandi446 – 4483
Helixi450 – 46112

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WCGX-ray1.10A/B1-464[»]
ProteinModelPortaliQ95X01.
SMRiQ95X01. Positions 3-464.

Miscellaneous databases

EvolutionaryTraceiQ95X01.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 1 family.1 Publication

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.
PROSITEiPS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q95X01-1 [UniParc]FASTAAdd to Basket

« Hide

MDYKFPKDFM FGTSTASYQI EGGWNEDGKG ENIWDRLVHT SPEVIKDGTN    50
GDIACDSYHK YKEDVAIIKD LNLKFYRFSI SWARIAPSGV MNSLEPKGIA 100
YYNNLINELI KNDIIPLVTM YHWDLPQYLQ DLGGWVNPIM SDYFKEYARV 150
LFTYFGDRVK WWITFNEPIA VCKGYSIKAY APNLNLKTTG HYLAGHTQLI 200
AHGKAYRLYE EMFKPTQNGK ISISISGVFF MPKNAESDDD IETAERANQF 250
ERGWFGHPVY KGDYPPIMKK WVDQKSKEEG LPWSKLPKFT KDEIKLLKGT 300
ADFYALNHYS SRLVTFGSDP NPNFNPDASY VTSVDEAWLK PNETPYIIPV 350
PEGLRKLLIW LKNEYGNPQL LITENGYGDD GQLDDFEKIS YLKNYLNATL 400
QAMYEDKCNV IGYTVWSLLD NFEWFYGYSI HFGLVKIDFN DPQRTRTKRE 450
SYTYFKNVVS TGKP 464
Length:464
Mass (Da):53,736
Last modified:December 1, 2001 - v1
Checksum:i02E76E24504C393A
GO

Mass spectrometryi

Molecular mass is 54000±500 Da from positions 1 - 464. Determined by MALDI. 1 Publication

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti107 – 1071N → P AA sequence 1 Publication
Sequence conflicti322 – 3221P → N AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF203780 mRNA. Translation: AAL25999.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF203780 mRNA. Translation: AAL25999.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1WCG X-ray 1.10 A/B 1-464 [» ]
ProteinModelPortali Q95X01.
SMRi Q95X01. Positions 3-464.
ModBasei Search...

Protein family/group databases

CAZyi GH1. Glycoside Hydrolase Family 1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei Q95X01.

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

Publicationsi

  1. "Characterization and evolution of a myrosinase from the cabbage aphid Brevicoryne brassicae."
    Jones A.M., Winge P., Bones A.M., Cole R., Rossiter J.T.
    Insect Biochem. Mol. Biol. 32:275-284(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PROTEIN SEQUENCE OF 98-111; 188-197; 253-261; 313-327 AND 389-393.
  2. "Crystal structure at 1.1 Angstroms resolution of an insect myrosinase from Brevicoryne brassicae shows its close relationship to beta-glucosidases."
    Husebye H., Arzt S., Burmeister W.P., Hartel F.V., Brandt A., Rossiter J.T., Bones A.M.
    Insect Biochem. Mol. Biol. 35:1311-1320(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, ACTIVE SITE GLU-167, ACTIVE SITE GLU-374, X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS).
  3. "Purification and characterisation of a non-plant myrosinase from the cabbage aphid Brevicoryne brassicae (L.)."
    Jones A.M., Bridges M., Bones A.M., Cole R., Rossiter J.T.
    Insect Biochem. Mol. Biol. 31:1-5(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MASS SPECTROMETRY, PROTEIN SEQUENCE OF 98-111; 188-197; 253-261; 313-327 AND 389-393.
  4. "Spatial organization of the glucosinolate-myrosinase system in brassica specialist aphids is similar to that of the host plant."
    Bridges M., Jones A.M., Bones A.M., Hodgson C., Cole R., Bartlet E., Wallsgrove R., Karapapa V.K., Watts N., Rossiter J.T.
    Proc. R. Soc. B 269:187-191(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  5. Cited for: FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.

Entry informationi

Entry nameiMYRO1_BREBR
AccessioniPrimary (citable) accession number: Q95X01
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 23, 2010
Last sequence update: December 1, 2001
Last modified: February 19, 2014
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

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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