Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9C5C2

- BGL37_ARATH

UniProt

Q9C5C2 - BGL37_ARATH

Protein

Myrosinase 2

Gene

TGG2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 88 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 – 691SubstrateBy similarity
    Binding sitei171 – 1711SubstrateBy similarity
    Binding sitei216 – 2161SubstrateBy similarity
    Binding sitei217 – 2171AscorbateBy similarity
    Binding sitei289 – 2891AscorbateBy similarity
    Binding sitei359 – 3591SubstrateBy similarity
    Active sitei430 – 4301NucleophilePROSITE-ProRule annotation
    Binding sitei479 – 4791SubstrateBy 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

    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

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2828Sequence AnalysisAdd
    BLAST
    Chaini29 – 547519Myrosinase 2PRO_0000389599Add
    BLAST

    Amino acid modifications

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

    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

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

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 1 family.Curated

    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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti100 – 1001D → N in AAN60275. 1 PublicationCurated
    Sequence conflicti181 – 1811E → K in AAN60275. 1 PublicationCurated
    Sequence conflicti255 – 2551I → N in AAL77743. (PubMed:14593172)Curated
    Sequence conflicti255 – 2551I → N in AAK32833. (PubMed:14593172)Curated
    Sequence conflicti356 – 3561L → P in BAE98479. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei468 – 54780Missing in isoform 2. CuratedVSP_038466Add
    BLAST

    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

    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: October 1, 2014
    This is version 88 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