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Q9C5C2

- BGL37_ARATH

UniProt

Q9C5C2 - BGL37_ARATH

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Protein
Myrosinase 2
Gene
TGG2, BGLU37, At5g25980, T1N24.18
Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 TGG1.2 Publications

Catalytic activityi

A thioglucoside + H2O = a sugar + a thiol.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei69 – 691Substrate By similarity
Binding sitei171 – 1711Substrate By similarity
Binding sitei216 – 2161Substrate By similarity
Binding sitei217 – 2171Ascorbate By similarity
Binding sitei289 – 2891Ascorbate By similarity
Binding sitei359 – 3591Substrate By similarity
Active sitei430 – 4301Nucleophile By similarity
Binding sitei479 – 4791Substrate By similarity

GO - Molecular functioni

  1. thioglucosidase activity Source: TAIR

GO - Biological processi

  1. abscisic acid-activated signaling pathway Source: UniProtKB-KW
  2. carbohydrate metabolic process Source: InterPro
  3. defense response to insect Source: UniProtKB
  4. glucosinolate catabolic process Source: TAIR
  5. regulation of stomatal movement Source: UniProtKB
  6. response to abscisic acid Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Abscisic acid signaling pathway, Plant defense

Enzyme and pathway databases

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

Protein family/group databases

CAZyiGH1. Glycoside Hydrolase Family 1.

Names & Taxonomyi

Protein namesi
Recommended name:
Myrosinase 2 (EC:3.2.1.147)
Alternative name(s):
Beta-glucosidase 37
Short name:
AtBGLU37
Sinigrinase 2
Thioglucosidase 2
Gene namesi
Name:TGG2
Synonyms:BGLU37
Ordered Locus Names:At5g25980
ORF Names:T1N24.18
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 5

Organism-specific databases

TAIRiAT5G25980.

Subcellular locationi

GO - Cellular componenti

  1. apoplast Source: TAIR
  2. chloroplast Source: TAIR
  3. cytosolic ribosome Source: TAIR
  4. peroxisome Source: TAIR
  5. plasmodesma Source: TAIR
  6. vacuole Source: TAIR
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2828 Reviewed prediction
Add
BLAST
Chaini29 – 547519Myrosinase 2
PRO_0000389599Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi36 ↔ 460 By similarity
Disulfide bondi44 ↔ 456 By similarity
Disulfide bondi236 ↔ 244 By similarity
Glycosylationi340 – 3401N-linked (GlcNAc...) Reviewed prediction
Glycosylationi384 – 3841N-linked (GlcNAc...) Reviewed prediction
Glycosylationi504 – 5041N-linked (GlcNAc...) Reviewed prediction

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ9C5C2.
PRIDEiQ9C5C2.

Expressioni

Tissue specificityi

Expressed in phloem-associated cells.1 Publication

Gene expression databases

GenevestigatoriQ9C5C2.

Interactioni

Subunit structurei

Interacts with MVP1.1 Publication

Protein-protein interaction databases

BioGridi17942. 8 interactions.
STRINGi3702.AT5G25980.2-P.

Structurei

3D structure databases

ProteinModelPortaliQ9C5C2.
SMRiQ9C5C2. Positions 33-522.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni486 – 4872Substrate binding By similarity

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG2723.
InParanoidiQ9C5C2.
KOiK01237.
PhylomeDBiQ9C5C2.

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]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9C5C2-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MQHNTYIYIL TMKLLGFALA ILLVVATCKP EEEITCEENV PFTCSQTDRF    50
NKQDFESDFI FGVASSAYQI EGGRGRGLNV WDGFTHRYPE KGGADLGNGD 100
TTCDSYRTWQ KDLDVMEELG VKGYRFSFAW SRILPKGKRS RGINEDGINY 150
YSGLIDGLIA RNITPFVTLF HWDLPQSLQD EYEGFLDRTI IDDFKDYADL 200
CFERFGDRVK HWITINQLFT VPTRGYALGT DAPGRCSQWV DKRCYGGDSS 250
TEPYIVAHNQ LLAHATVVDL YRTRYKYQGG KIGPVMITRW FLPYDDTLES 300
KQATWRAKEF FLGWFMEPLT KGKYPYIMRK LVGNRLPKFN STEARLLKGS 350
YDFLGLNYYV TQYAHALDPS PPEKLTAMTD SLANLTSLDA NGQPPGPPFS 400
KGSYYHPRGM LNVMEHFKTK YGDPLIYVTE NGFSTSGGPI PFTEAFHDYN 450
RIDYLCSHLC FLRKAIKEKR VNVKGYFVWS LGDNYEFCNG YTVRFGLSYV 500
DFNNVTADRD LKASGLWYQS FLRDTTKNQD ILRSSLPFKN GDRKSLT 547
Length:547
Mass (Da):62,732
Last modified:June 1, 2001 - v1
Checksum:i3902D25F45B9DFAA
GO
Isoform 2 (identifier: Q9C5C2-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     468-547: Missing.

Note: Derived from EST data. No experimental confirmation available.

Show »
Length:467
Mass (Da):53,423
Checksum:i84CD68F147AA326C
GO

Sequence cautioni

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

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei468 – 54780Missing in isoform 2.
VSP_038466Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti100 – 1001D → N in AAN60275. 1 Publication
Sequence conflicti181 – 1811E → K in AAN60275. 1 Publication
Sequence conflicti255 – 2551I → N in AAL77743. 1 Publication
Sequence conflicti255 – 2551I → N in AAK32833. 1 Publication
Sequence conflicti356 – 3561L → P in BAE98479. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiS56654.
RefSeqiNP_001031940.1. NM_001036863.1. [Q9C5C2-2]
NP_568479.1. NM_122499.3. [Q9C5C2-1]
NP_851076.2. NM_180745.2. [Q9C5C2-2]
UniGeneiAt.22698.

Genome annotation databases

EnsemblPlantsiAT5G25980.2; AT5G25980.2; AT5G25980. [Q9C5C2-1]
GeneIDi832667.
KEGGiath:AT5G25980.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRi S56654.
RefSeqi NP_001031940.1. NM_001036863.1. [Q9C5C2-2 ]
NP_568479.1. NM_122499.3. [Q9C5C2-1 ]
NP_851076.2. NM_180745.2. [Q9C5C2-2 ]
UniGenei At.22698.

3D structure databases

ProteinModelPortali Q9C5C2.
SMRi Q9C5C2. Positions 33-522.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 17942. 8 interactions.
STRINGi 3702.AT5G25980.2-P.

Protein family/group databases

CAZyi GH1. Glycoside Hydrolase Family 1.

Proteomic databases

PaxDbi Q9C5C2.
PRIDEi Q9C5C2.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT5G25980.2 ; AT5G25980.2 ; AT5G25980 . [Q9C5C2-1 ]
GeneIDi 832667.
KEGGi ath:AT5G25980.

Organism-specific databases

TAIRi AT5G25980.

Phylogenomic databases

eggNOGi COG2723.
InParanoidi Q9C5C2.
KOi K01237.
PhylomeDBi Q9C5C2.

Enzyme and pathway databases

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

Gene expression databases

Genevestigatori Q9C5C2.

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

« Hide 'large scale' publications
  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.
    , 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.
    , 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.
    , 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. 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.

Entry informationi

Entry nameiBGL37_ARATH
AccessioniPrimary (citable) accession number: Q9C5C2
Secondary accession number(s): Q0WWL9
, Q3E943, Q42595, Q56WQ3, Q56ZB8, Q8H7E3, Q9ASV0
Entry historyi
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 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

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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