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Q9C5C2 (BGL37_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 87. 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 2

EC=3.2.1.147
Alternative name(s):
Beta-glucosidase 37
Short name=AtBGLU37
Sinigrinase 2
Thioglucosidase 2
Gene names
Name:TGG2
Synonyms:BGLU37
Ordered Locus Names:At5g25980
ORF Names:T1N24.18
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length547 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May degrade 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. These toxic degradation products can deter insect herbivores. Seems to function in abscisic acid (ABA) and methyl jasmonate (MeJA) signaling in guard cells. Functionally redundant with TGG1. Ref.8 Ref.9

Catalytic activity

A thioglucoside + H2O = a sugar + a thiol.

Subunit structure

Interacts with MVP1. Ref.10

Tissue specificity

Expressed in phloem-associated cells. Ref.8

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.

Sequence caution

The sequence AAD40134.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAK32833.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAN60275.1 differs from that shown. Reason: Frameshift at position 193.

The sequence BAD94532.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence CAA55787.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9C5C2-1)

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.
Isoform 2 (identifier: Q9C5C2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     468-547: Missing.
Note: Derived from EST data. No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2828 Potential
Chain29 – 547519Myrosinase 2
PRO_0000389599

Regions

Region486 – 4872Substrate binding By similarity

Sites

Active site4301Nucleophile By similarity
Binding site691Substrate By similarity
Binding site1711Substrate By similarity
Binding site2161Substrate By similarity
Binding site2171Ascorbate By similarity
Binding site2891Ascorbate By similarity
Binding site3591Substrate By similarity
Binding site4791Substrate By similarity

Amino acid modifications

Glycosylation3401N-linked (GlcNAc...) Potential
Glycosylation3841N-linked (GlcNAc...) Potential
Glycosylation5041N-linked (GlcNAc...) Potential
Disulfide bond36 ↔ 460 By similarity
Disulfide bond44 ↔ 456 By similarity
Disulfide bond236 ↔ 244 By similarity

Natural variations

Alternative sequence468 – 54780Missing in isoform 2.
VSP_038466

Experimental info

Sequence conflict1001D → N in AAN60275. Ref.6
Sequence conflict1811E → K in AAN60275. Ref.6
Sequence conflict2551I → N in AAL77743. Ref.4
Sequence conflict2551I → N in AAK32833. Ref.4
Sequence conflict3561L → P in BAE98479. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 3902D25F45B9DFAA

FASTA54762,732
        10         20         30         40         50         60 
MQHNTYIYIL TMKLLGFALA ILLVVATCKP EEEITCEENV PFTCSQTDRF NKQDFESDFI 

        70         80         90        100        110        120 
FGVASSAYQI EGGRGRGLNV WDGFTHRYPE KGGADLGNGD TTCDSYRTWQ KDLDVMEELG 

       130        140        150        160        170        180 
VKGYRFSFAW SRILPKGKRS RGINEDGINY YSGLIDGLIA RNITPFVTLF HWDLPQSLQD 

       190        200        210        220        230        240 
EYEGFLDRTI IDDFKDYADL CFERFGDRVK HWITINQLFT VPTRGYALGT DAPGRCSQWV 

       250        260        270        280        290        300 
DKRCYGGDSS TEPYIVAHNQ LLAHATVVDL YRTRYKYQGG KIGPVMITRW FLPYDDTLES 

       310        320        330        340        350        360 
KQATWRAKEF FLGWFMEPLT KGKYPYIMRK LVGNRLPKFN STEARLLKGS YDFLGLNYYV 

       370        380        390        400        410        420 
TQYAHALDPS PPEKLTAMTD SLANLTSLDA NGQPPGPPFS KGSYYHPRGM LNVMEHFKTK 

       430        440        450        460        470        480 
YGDPLIYVTE NGFSTSGGPI PFTEAFHDYN RIDYLCSHLC FLRKAIKEKR VNVKGYFVWS 

       490        500        510        520        530        540 
LGDNYEFCNG YTVRFGLSYV DFNNVTADRD LKASGLWYQS FLRDTTKNQD ILRSSLPFKN 


GDRKSLT 

« Hide

Isoform 2 [UniParc].

Checksum: 84CD68F147AA326C
Show »

FASTA46753,423

References

« Hide 'large scale' references
[1]"The myrosinase gene family in Arabidopsis thaliana: gene organization, expression and evolution."
Xue J., Joergensen M., Pihlgren U., Rask L.
Plant Mol. Biol. 27:911-922(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: cv. Columbia.
Tissue: Leaf.
[2]"Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K. expand/collapse author list , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.
Nature 408:823-826(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] (ISOFORM 1).
Strain: cv. Columbia.
[5]"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. expand/collapse author list , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: cv. Columbia.
[6]"Signal peptide selection derived cDNAs from Arabidopsis thaliana leaves and guard cells."
Stracke R., Palme K.
Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 6-208.
[7]"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.
[8]"Arabidopsis myrosinases TGG1 and TGG2 have redundant function in glucosinolate breakdown and insect defense."
Barth C., Jander G.
Plant J. 46:549-562(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
[9]"Myrosinases, TGG1 and TGG2, redundantly function in ABA and MeJA signaling in Arabidopsis guard cells."
Islam M.M., Tani C., Watanabe-Sugimoto M., Uraji M., Jahan M.S., Masuda C., Nakamura Y., Mori I.C., Murata Y.
Plant Cell Physiol. 50:1171-1175(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[10]"MODIFIED VACUOLE PHENOTYPE1 is an Arabidopsis myrosinase-associated protein involved in endomembrane protein trafficking."
Agee A.E., Surpin M., Sohn E.J., Girke T., Rosado A., Kram B.W., Carter C., Wentzell A.M., Kliebenstein D.J., Jin H.C., Park O.K., Jin H., Hicks G.R., Raikhel N.V.
Plant Physiol. 152:120-132(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MVP1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X79195 Genomic DNA. Translation: CAA55787.1. Different initiation.
AF149413 Genomic DNA. Translation: AAD40134.1. Different initiation.
CP002688 Genomic DNA. Translation: AED93507.1.
CP002688 Genomic DNA. Translation: AED93508.1.
CP002688 Genomic DNA. Translation: AED93509.1.
AF360348 mRNA. Translation: AAK28645.1.
AF361821 mRNA. Translation: AAK32833.1. Different initiation.
AY078042 mRNA. Translation: AAL77743.1.
AY113880 mRNA. Translation: AAM44928.1.
AK221048 mRNA. Translation: BAD94810.1.
AK221982 mRNA. Translation: BAD94532.1. Different initiation.
AK226328 mRNA. Translation: BAE98479.1.
AF083717 mRNA. Translation: AAN60275.1. Sequence problems.
PIRS56654.
RefSeqNP_001031940.1. NM_001036863.1. [Q9C5C2-2]
NP_568479.1. NM_122499.3. [Q9C5C2-1]
NP_851076.2. NM_180745.2. [Q9C5C2-2]
UniGeneAt.22698.

3D structure databases

ProteinModelPortalQ9C5C2.
SMRQ9C5C2. Positions 33-522.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid17942. 8 interactions.
STRING3702.AT5G25980.2-P.

Protein family/group databases

CAZyGH1. Glycoside Hydrolase Family 1.

Proteomic databases

PaxDbQ9C5C2.
PRIDEQ9C5C2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G25980.2; AT5G25980.2; AT5G25980. [Q9C5C2-1]
GeneID832667.
KEGGath:AT5G25980.

Organism-specific databases

TAIRAT5G25980.

Phylogenomic databases

eggNOGCOG2723.
InParanoidQ9C5C2.
KOK01237.
PhylomeDBQ9C5C2.

Enzyme and pathway databases

BioCycARA:GQT-2713-MONOMER.
ARA:GQT-2714-MONOMER.
MetaCyc:AT5G25980-MONOMER.

Gene expression databases

GenevestigatorQ9C5C2.

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 nameBGL37_ARATH
AccessionPrimary (citable) accession number: Q9C5C2
Secondary accession number(s): Q0WWL9 expand/collapse secondary AC list , Q3E943, Q42595, Q56WQ3, Q56ZB8, Q8H7E3, Q9ASV0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 24, 2009
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 87 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