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Q3ECS3 (BGL35_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Myrosinase 5
EC=3.2.1.147
Alternative name(s):
Beta-glucosidase 35
Short name=AtBGLU35
EC=3.2.1.21
Sinigrinase 5
Thioglucosidase 5
Gene names
Name:TGG5
Synonyms:BGLU35
Ordered Locus Names:At1g51470
ORF Names:F5D21.17
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length511 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Hydrolyzes sinigrin and, with lower efficiency, p-nitrophenyl beta-D-glucoside. Ref.5

Catalytic activity

A thioglucoside + H2O = a sugar + a thiol.

Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.

Tissue specificity

Specifically expressed in roots. Ref.5

Miscellaneous

It seems that the absence of a catalytic proton donor in plant myrosinases is not impairing the hydrolysis of glucosinolates.

Sequence similarities

Belongs to the glycosyl hydrolase 1 family.

Biophysicochemical properties

Kinetic parameters:

KM=547 µM for sinigrin (at pH 4.5) Ref.5

KM=80 mM for p-nitrophenyl beta-D-glucoside (at pH 4.5)

Vmax=48.1 µmol/min/mg enzyme with sinigrin as substrate (at pH 4.5)

Vmax=17 µmol/min/mg enzyme with p-nitrophenyl beta-D-glucoside as substrate (at pH 4.5)

Sequence caution

The sequence AAG52628.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 511488Myrosinase 5
PRO_0000389597

Regions

Region474 – 4752Substrate binding By similarity

Sites

Active site4181Nucleophile By similarity
Binding site641Substrate By similarity
Binding site1651Substrate By similarity
Binding site2101Substrate By similarity
Binding site2111Ascorbate By similarity
Binding site2801Ascorbate By similarity
Binding site3511Substrate By similarity
Binding site4671Substrate By similarity

Amino acid modifications

Glycosylation461N-linked (GlcNAc...) Potential
Glycosylation531N-linked (GlcNAc...) Potential
Glycosylation2221N-linked (GlcNAc...) Potential
Glycosylation4281N-linked (GlcNAc...) Potential
Glycosylation4891N-linked (GlcNAc...) Potential
Disulfide bond31 ↔ 450 By similarity
Disulfide bond39 ↔ 445 By similarity
Disulfide bond230 ↔ 233 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3ECS3 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: 0CEA34FA0DFB95B5

FASTA51157,468
        10         20         30         40         50         60 
MAIPKAHYSL AVLVLLFVVV SSSQKVCNPE CKAKEPFHCD NTHAFNRSGF PKNFTFGAAT 

        70         80         90        100        110        120 
SAYQIEGAAH RALNGWDYFT HRYPEKVPDR SSADLACDSY DLYKDDVKLL KRMNVQAYRL 

       130        140        150        160        170        180 
SIAWSRVLPK GRLTGGVDEN GITYYNNLIN ELKANGIEPY VTIFHWDVPQ TLEDEYGGFL 

       190        200        210        220        230        240 
STRIVEDYTN YAELLFQRFG DRVKFWITLN QPLSLALKGY GNGSYPPGRC TGCELGGDSG 

       250        260        270        280        290        300 
VEPYTVAHNQ LLAHAKTVSL YRKRYQKFQG GKIGTTLIGR WFVPLNEFSE LDKAAAKRAF 

       310        320        330        340        350        360 
DFFVGWFLDP LVYGKYPTIM REMVGDRLPE FTPEESALVK GSLDFLGLNY YVSQYATDAP 

       370        380        390        400        410        420 
PPTQPNAITD ARVTLGFYRN GSPIGVVASS FVYYPPGFRQ ILNYIKDNYK NPLTYITENG 

       430        440        450        460        470        480 
VADLDLGNVT LATALADNGR IQNHCSHLSC LKCAMKDGCN VAGYFAWSLM DNYEFGNGYT 

       490        500        510 
LRFGMNWVNF TNPADRKEKA SGKWFSKFLA K

« Hide

References

« Hide 'large scale' references
[1]"Characterization of a new subfamily of thioglucoside glucohydrolases."
Zhang J.
Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: cv. Columbia.
[2]"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. expand/collapse author list , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"Functional genomic analysis of Arabidopsis thaliana glycoside hydrolase family 1."
Xu Z., Escamilla-Trevino L.L., Zeng L., Lalgondar M., Bevan D.R., Winkel B.S.J., Mohamed A., Cheng C.-L., Shih M.-C., Poulton J.E., Esen A.
Plant Mol. Biol. 55:343-367(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: GENE FAMILY, NOMENCLATURE.
[5]"Myrosinases from root and leaves of Arabidopsis thaliana have different catalytic properties."
Andersson D., Chakrabarty R., Bejai S., Zhang J., Rask L., Meijer J.
Phytochemistry 70:1345-1354(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		FJ268796 Genomic DNA. Translation: ACO95140.1.
AC024261 Genomic DNA. Translation: AAG52628.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE32671.1.
IPIIPI00520777.
PIRA96553.
RefSeqNP_175558.3. NM_104025.3.
UniGeneAt.25235.
At.48300.

3D structure databases

HSSPHSSP built from PDB template 1WCG based on UniProtKB Q95X01.
ProteinModelPortalQ3ECS3.
SMRQ3ECS3. Positions 46-511.
ModBaseSearch...

Protein-protein interaction databases

STRING3702.AT1G51470.1-P.

Protein family/group databases

CAZyGH1. Glycoside Hydrolase Family 1.

Proteomic databases

PaxDbQ3ECS3.
PRIDEQ3ECS3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G51470.1; AT1G51470.1; AT1G51470.
GeneID841572.
KEGGath:AT1G51470.

Organism-specific databases

TAIRAt1g51470.

Phylogenomic databases

eggNOGCOG2723.
HOGENOMHOG000088630.
InParanoidQ3ECS3.
OMAVDSRANT.
PhylomeDBQ3ECS3.
ProtClustDBCLSN2680410.

Enzyme and pathway databases

SABIO-RKQ3ECS3.

Gene expression databases

GenevestigatorQ3ECS3.

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR001360. Glyco_hydro_1.
IPR018120. Glyco_hydro_1_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERPTHR10353. PTHR10353. 1 hit.
PfamPF00232. Glyco_hydro_1. 1 hit.
[Graphical view]
PRINTSPR00131. GLHYDRLASE1.
SUPFAMSSF51445. Glyco_hydro_cat. 1 hit.
PROSITEPS00572. GLYCOSYL_HYDROL_F1_1. 1 hit.
PS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameBGL35_ARATH
AccessionPrimary (citable) accession number: Q3ECS3
Secondary accession number(s): Q9C8J9
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2009
Last sequence update: November 8, 2005
Last modified: May 1, 2013
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

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