Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q8GRX1 (BGL34_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 80. Feed History...

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

Names and origin

Protein namesRecommended name:
Myrosinase 4

EC=3.2.1.147
Alternative name(s):
Beta-glucosidase 34
Short name=AtBGLU34
EC=3.2.1.21
Sinigrinase 4
Thioglucosidase 4
Gene names
Name:TGG4
Synonyms:BGLU34
Ordered Locus Names:At1g47600
ORF Names:F16N3.11
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

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.6

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.6

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=245 µM for sinigrin (at pH 4.5) Ref.6

KM=28 mM for p-nitrophenyl beta-D-glucoside (at pH 4.5)

Vmax=12.2 µmol/min/mg enzyme with sinigrin as substrate (at pH 4.5)

Vmax=7.3 µmol/min/mg enzyme with p-nitrophenyl beta-D-glucoside as substrate (at pH 4.5)

Sequence caution

The sequence AAD46026.1 differs from that shown. Reason: Erroneous gene model prediction.

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.
Isoform 1 (identifier: Q8GRX1-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 511488Myrosinase 4
PRO_0000389596

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
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
Isoform 1 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: A977148B22E21D0E

FASTA51157,542
        10         20         30         40         50         60 
MAIPKAHYSL AVLVLLFVVV SSSQKVCNPE CKAKEPFHCD NTHAFNRTGF PRNFTFGAAT 

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

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

       190        200        210        220        230        240 
STRIVEDYTN YAELLFQRFG DRVKFWITLN QPFSLATKGY GDGSYPPGRC TGCELGGDSG 

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

       310        320        330        340        350        360 
DFFVGWFLDP LVYGKYPTIM REMVGDRLPE FTPEQSALVK GSLDFLGLNY YVTQYATDAP 

       370        380        390        400        410        420 
PPTQLNAITD ARVTLGFYRN GVPIGVVAPS 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]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[5]"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.
[6]"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
FJ268795 Genomic DNA. Translation: ACO95139.1.
AC007519 Genomic DNA. Translation: AAD46026.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE32191.1.
BT000471 mRNA. Translation: AAN17448.1.
BT002202 mRNA. Translation: AAN72213.1.
BT002458 mRNA. Translation: AAO00818.1.
PIRG96516.
RefSeqNP_175191.2. NM_103653.2. [Q8GRX1-1]
UniGeneAt.25235.

3D structure databases

ProteinModelPortalQ8GRX1.
SMRQ8GRX1. Positions 46-511.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid26394. 1 interaction.
STRING3702.AT1G47600.1-P.

Protein family/group databases

CAZyGH1. Glycoside Hydrolase Family 1.

Proteomic databases

PaxDbQ8GRX1.
PRIDEQ8GRX1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G47600.1; AT1G47600.1; AT1G47600. [Q8GRX1-1]
GeneID841169.
KEGGath:AT1G47600.

Organism-specific databases

TAIRAT1G47600.

Phylogenomic databases

eggNOGCOG2723.
HOGENOMHOG000088630.
InParanoidQ8GRX1.
KOK01237.
OMANWSWINS.
PhylomeDBQ8GRX1.

Enzyme and pathway databases

BioCycARA:GQT-1575-MONOMER.
SABIO-RKQ8GRX1.

Gene expression databases

GenevestigatorQ8GRX1.

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. SSF51445. 1 hit.
PROSITEPS00572. GLYCOSYL_HYDROL_F1_1. 1 hit.
PS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameBGL34_ARATH
AccessionPrimary (citable) accession number: Q8GRX1
Secondary accession number(s): Q9SX92
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2009
Last sequence update: March 1, 2003
Last modified: May 14, 2014
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names