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P37702

- BGL38_ARATH

UniProt

P37702 - BGL38_ARATH

Protein

Myrosinase 1

Gene

TGG1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 123 (01 Oct 2014)
      Sequence version 1 (01 Oct 1994)
      Previous versions | rss
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    Functioni

    Degradation of 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 TGG2. Hydrolyzes sinigrin and, with lower efficiency, p-nitrophenyl beta-D-glucoside.4 Publications

    Catalytic activityi

    A thioglucoside + H2O = a sugar + a thiol.
    Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.

    Kineticsi

    1. KM=45 µM for sinigrin (at pH 4.5)1 Publication
    2. KM=34 mM for p-nitrophenyl beta-D-glucoside (at pH 4.5)1 Publication

    Vmax=2.3 µmol/min/mg enzyme with sinigrin as substrate (at pH 4.5)1 Publication

    Vmax=1.2 µmol/min/mg enzyme with p-nitrophenyl beta-D-glucoside as substrate (at pH 4.5)1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei57 – 571SubstrateBy similarity
    Metal bindingi74 – 741Zinc; shared with dimeric partnerBy similarity
    Metal bindingi88 – 881Zinc; shared with dimeric partnerBy similarity
    Binding sitei159 – 1591SubstrateBy similarity
    Binding sitei204 – 2041SubstrateBy similarity
    Binding sitei205 – 2051AscorbateBy similarity
    Binding sitei278 – 2781AscorbateBy similarity
    Binding sitei348 – 3481SubstrateBy similarity
    Active sitei420 – 4201NucleophilePROSITE-ProRule annotation
    Binding sitei468 – 4681SubstrateBy similarity

    GO - Molecular functioni

    1. beta-glucosidase activity Source: TAIR
    2. metal ion binding Source: UniProtKB-KW
    3. thioglucosidase activity Source: UniProtKB

    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
    7. response to insect Source: TAIR

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Abscisic acid signaling pathway, Plant defense

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciARA:GQT-1321-MONOMER.
    MetaCyc:AT5G26000-MONOMER.
    SABIO-RKP37702.

    Protein family/group databases

    CAZyiGH1. Glycoside Hydrolase Family 1.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Myrosinase 1 (EC:3.2.1.147)
    Alternative name(s):
    Beta-glucosidase 38 (EC:3.2.1.21)
    Short name:
    AtBGLU38
    Sinigrinase 1
    Thioglucosidase 1
    Gene namesi
    Name:TGG1
    Synonyms:BGLU38
    Ordered Locus Names:At5g26000
    ORF Names:T1N24.7
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 5

    Organism-specific databases

    TAIRiAT5G26000.

    Subcellular locationi

    Vacuole By similarity

    GO - Cellular componenti

    1. apoplast Source: TAIR
    2. chloroplast Source: TAIR
    3. cytosolic ribosome Source: TAIR
    4. peroxisome Source: TAIR
    5. plant-type cell wall Source: TAIR
    6. thylakoid Source: TAIR
    7. vacuole Source: TAIR

    Keywords - Cellular componenti

    Vacuole

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1919Sequence AnalysisAdd
    BLAST
    Chaini20 – 541522Myrosinase 1PRO_0000011773Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi24 ↔ 449By similarity
    Disulfide bondi32 ↔ 445By similarity
    Glycosylationi33 – 331N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi108 – 1081N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi175 – 1751N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi224 ↔ 232By similarity
    Glycosylationi236 – 2361N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi356 – 3561N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi379 – 3791N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi493 – 4931N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi512 – 5121N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PRIDEiP37702.

    2D gel databases

    SWISS-2DPAGEP37702.

    Expressioni

    Tissue specificityi

    Expressed in guard cells, phloem-associated cells and myrosin cells.1 Publication

    Gene expression databases

    GenevestigatoriP37702.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    BioGridi17944. 5 interactions.
    IntActiP37702. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliP37702.
    SMRiP37702. Positions 21-512.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni475 – 4762Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 1 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    InParanoidiP37702.
    KOiK01237.
    OMAiNWITINQ.
    PhylomeDBiP37702.

    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: P37702-1) [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

    MKLLMLAFVF LLALATCKGD EFVCEENEPF TCNQTKLFNS GNFEKGFIFG    50
    VASSAYQVEG GRGRGLNVWD SFTHRFPEKG GADLGNGDTT CDSYTLWQKD 100
    IDVMDELNST GYRFSIAWSR LLPKGKRSRG VNPGAIKYYN GLIDGLVAKN 150
    MTPFVTLFHW DLPQTLQDEY NGFLNKTIVD DFKDYADLCF ELFGDRVKNW 200
    ITINQLYTVP TRGYALGTDA PGRCSPKIDV RCPGGNSSTE PYIVAHNQLL 250
    AHAAAVDVYR TKYKDDQKGM IGPVMITRWF LPFDHSQESK DATERAKIFF 300
    HGWFMGPLTE GKYPDIMREY VGDRLPEFSE TEAALVKGSY DFLGLNYYVT 350
    QYAQNNQTIV PSDVHTALMD SRTTLTSKNA TGHAPGPPFN AASYYYPKGI 400
    YYVMDYFKTT YGDPLIYVTE NGFSTPGDED FEKATADYKR IDYLCSHLCF 450
    LSKVIKEKNV NVKGYFAWSL GDNYEFCNGF TVRFGLSYVD FANITGDRDL 500
    KASGKWFQKF INVTDEDSTN QDLLRSSVSS KNRDRKSLAD A 541
    Length:541
    Mass (Da):61,133
    Last modified:October 1, 1994 - v1
    Checksum:i3736B735DE7A5BD1
    GO
    Isoform 2 (identifier: P37702-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         457-541: Missing.

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

    Show »
    Length:456
    Mass (Da):51,481
    Checksum:iDE7CE563F352A0BB
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti385 – 3851P → H in AAL06896. (PubMed:14593172)Curated
    Sequence conflicti426 – 4261P → A in AAL25596. (PubMed:14593172)Curated
    Sequence conflicti434 – 4341A → T in BAH20253. (PubMed:19423640)Curated
    Sequence conflicti441 – 4411I → N in BAH20253. (PubMed:19423640)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti128 – 1281S → N in strain: cv. Ta-0. 1 Publication
    Natural varianti261 – 2611T → K in strain: cv. Ba-1. 1 Publication
    Natural varianti264 – 2641K → Q in strain: cv. Ba-1. 1 Publication
    Natural varianti427 – 4271G → A in strain: cv. Ag-0, cv. Ba-1, cv. Mh-0, cv. Mr-0 and Tac-0. 1 Publication
    Natural varianti459 – 4591N → G in strain: cv. Su-0. 1 Publication
    Natural varianti489 – 4891V → I in strain: cv. No-0, cv. Rsch-0 and cv. Ta-0. 1 Publication

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei457 – 54185Missing in isoform 2. CuratedVSP_038446Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L11454 mRNA. Translation: AAC18869.1.
    X79194 Genomic DNA. Translation: CAA55786.1.
    AF149413 Genomic DNA. Translation: AAD40143.1.
    CP002688 Genomic DNA. Translation: AED93511.1.
    CP002688 Genomic DNA. Translation: AED93512.1.
    AY045681 mRNA. Translation: AAK74039.1.
    AY054237 mRNA. Translation: AAL06896.1.
    AY058182 mRNA. Translation: AAL25596.1.
    AY090382 mRNA. Translation: AAL91284.1.
    AF083677 mRNA. Translation: AAN60236.1.
    AJ831440 Genomic DNA. Translation: CAH40799.1.
    AJ831441 Genomic DNA. Translation: CAH40800.1.
    AJ831442 Genomic DNA. Translation: CAH40801.1.
    AJ831443 Genomic DNA. Translation: CAH40802.1.
    AJ831444 Genomic DNA. Translation: CAH40803.1.
    AJ831445 Genomic DNA. Translation: CAH40804.1.
    AJ831446 Genomic DNA. Translation: CAH40805.1.
    AJ831447 Genomic DNA. Translation: CAH40806.1.
    AJ831448 Genomic DNA. Translation: CAH40807.1.
    AJ831449 Genomic DNA. Translation: CAH40808.1.
    AJ831450 Genomic DNA. Translation: CAH40809.1.
    AJ831451 Genomic DNA. Translation: CAH40810.1.
    AJ831452 Genomic DNA. Translation: CAH40811.1.
    AJ831453 Genomic DNA. Translation: CAH40812.1.
    AJ831454 Genomic DNA. Translation: CAH40813.1.
    AJ831455 Genomic DNA. Translation: CAH40814.1.
    AJ831456 Genomic DNA. Translation: CAH40815.1.
    AJ831457 Genomic DNA. Translation: CAH40816.1.
    AJ831458 Genomic DNA. Translation: CAH40817.1.
    AJ831459 Genomic DNA. Translation: CAH40818.1.
    AJ831460 Genomic DNA. Translation: CAH40819.1.
    AJ831461 Genomic DNA. Translation: CAH40820.1.
    AJ831462 Genomic DNA. Translation: CAH40821.1.
    AJ831463 Genomic DNA. Translation: CAH40822.1.
    AJ831464 Genomic DNA. Translation: CAH40823.1.
    AJ831465 Genomic DNA. Translation: CAH40824.1.
    AJ831466 Genomic DNA. Translation: CAH40825.1.
    AJ831467 Genomic DNA. Translation: CAH40826.1.
    AK317589 mRNA. Translation: BAH20253.1.
    Z18232 mRNA. Translation: CAA79143.1.
    PIRiS56653.
    RefSeqiNP_197972.2. NM_122501.3. [P37702-2]
    NP_851077.1. NM_180746.2. [P37702-1]
    UniGeneiAt.23592.
    At.47944.
    At.73176.

    Genome annotation databases

    EnsemblPlantsiAT5G26000.1; AT5G26000.1; AT5G26000. [P37702-1]
    GeneIDi832669.
    KEGGiath:AT5G26000.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L11454 mRNA. Translation: AAC18869.1 .
    X79194 Genomic DNA. Translation: CAA55786.1 .
    AF149413 Genomic DNA. Translation: AAD40143.1 .
    CP002688 Genomic DNA. Translation: AED93511.1 .
    CP002688 Genomic DNA. Translation: AED93512.1 .
    AY045681 mRNA. Translation: AAK74039.1 .
    AY054237 mRNA. Translation: AAL06896.1 .
    AY058182 mRNA. Translation: AAL25596.1 .
    AY090382 mRNA. Translation: AAL91284.1 .
    AF083677 mRNA. Translation: AAN60236.1 .
    AJ831440 Genomic DNA. Translation: CAH40799.1 .
    AJ831441 Genomic DNA. Translation: CAH40800.1 .
    AJ831442 Genomic DNA. Translation: CAH40801.1 .
    AJ831443 Genomic DNA. Translation: CAH40802.1 .
    AJ831444 Genomic DNA. Translation: CAH40803.1 .
    AJ831445 Genomic DNA. Translation: CAH40804.1 .
    AJ831446 Genomic DNA. Translation: CAH40805.1 .
    AJ831447 Genomic DNA. Translation: CAH40806.1 .
    AJ831448 Genomic DNA. Translation: CAH40807.1 .
    AJ831449 Genomic DNA. Translation: CAH40808.1 .
    AJ831450 Genomic DNA. Translation: CAH40809.1 .
    AJ831451 Genomic DNA. Translation: CAH40810.1 .
    AJ831452 Genomic DNA. Translation: CAH40811.1 .
    AJ831453 Genomic DNA. Translation: CAH40812.1 .
    AJ831454 Genomic DNA. Translation: CAH40813.1 .
    AJ831455 Genomic DNA. Translation: CAH40814.1 .
    AJ831456 Genomic DNA. Translation: CAH40815.1 .
    AJ831457 Genomic DNA. Translation: CAH40816.1 .
    AJ831458 Genomic DNA. Translation: CAH40817.1 .
    AJ831459 Genomic DNA. Translation: CAH40818.1 .
    AJ831460 Genomic DNA. Translation: CAH40819.1 .
    AJ831461 Genomic DNA. Translation: CAH40820.1 .
    AJ831462 Genomic DNA. Translation: CAH40821.1 .
    AJ831463 Genomic DNA. Translation: CAH40822.1 .
    AJ831464 Genomic DNA. Translation: CAH40823.1 .
    AJ831465 Genomic DNA. Translation: CAH40824.1 .
    AJ831466 Genomic DNA. Translation: CAH40825.1 .
    AJ831467 Genomic DNA. Translation: CAH40826.1 .
    AK317589 mRNA. Translation: BAH20253.1 .
    Z18232 mRNA. Translation: CAA79143.1 .
    PIRi S56653.
    RefSeqi NP_197972.2. NM_122501.3. [P37702-2 ]
    NP_851077.1. NM_180746.2. [P37702-1 ]
    UniGenei At.23592.
    At.47944.
    At.73176.

    3D structure databases

    ProteinModelPortali P37702.
    SMRi P37702. Positions 21-512.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 17944. 5 interactions.
    IntActi P37702. 1 interaction.

    Protein family/group databases

    CAZyi GH1. Glycoside Hydrolase Family 1.

    2D gel databases

    SWISS-2DPAGE P37702.

    Proteomic databases

    PRIDEi P37702.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT5G26000.1 ; AT5G26000.1 ; AT5G26000 . [P37702-1 ]
    GeneIDi 832669.
    KEGGi ath:AT5G26000.

    Organism-specific databases

    TAIRi AT5G26000.

    Phylogenomic databases

    InParanoidi P37702.
    KOi K01237.
    OMAi NWITINQ.
    PhylomeDBi P37702.

    Enzyme and pathway databases

    BioCyci ARA:GQT-1321-MONOMER.
    MetaCyc:AT5G26000-MONOMER.
    SABIO-RK P37702.

    Gene expression databases

    Genevestigatori P37702.

    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. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Strain: cv. Columbia.
    2. "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.
    3. "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.
    4. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    5. "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].
      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 [LARGE SCALE MRNA] OF 1-226.
    7. "Nucleotide variation at the myrosinase-encoding locus, TGG1, and quantitative myrosinase enzyme activity variation in Arabidopsis thaliana."
      Stranger B.E., Mitchell-Olds T.
      Mol. Ecol. 14:295-309(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 18-497; 43-510; 43-511; 43-512; 43-513; 43-514; 44-511; 44-512; 44-514; 44-522; 45-511 AND 47-512, FUNCTION, VARIANTS ASN-128; LYS-261; GLN-264; ALA-427; GLY-459 AND ILE-489.
      Strain: cv. Abd-0, cv. Ag-0, cv. Ba-1, cv. Cal-0, cv. Columbia, cv. Cvi-0, cv. Db-1, cv. Ei-2, cv. HOG, cv. Ka-0, cv. Ler-1, cv. Lip-0, cv. Ll-0, cv. Mh-0, cv. Mr-0, cv. Mrk-0, cv. Mt-0, cv. No-0, cv. Per-1, cv. Petergof, cv. Pi-0, cv. Rsch-0, cv. Sei-0, cv. Su-0, cv. Ta-0, cv. Tac-0, cv. Tsu-1 and cv. Wl-0.
    8. "Analysis of multiple occurrences of alternative splicing events in Arabidopsis thaliana using novel sequenced full-length cDNAs."
      Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M., Shinozaki K.
      DNA Res. 16:155-164(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 101-541.
      Strain: cv. Columbia.
    9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 192-250.
      Strain: cv. C24.
      Tissue: Flower bud.
    10. "Cell specific, cross-species expression of myrosinases in Brassica napus, Arabidopsis thaliana and Nicotiana tabacum."
      Thangstad O.P., Gilde B., Chadchawan S., Seem M., Husebye H., Bradley D., Bones A.M.
      Plant Mol. Biol. 54:597-611(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    11. Cited for: GENE FAMILY, NOMENCLATURE.
    12. "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.
    13. "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.
    14. "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.

    Entry informationi

    Entry nameiBGL38_ARATH
    AccessioniPrimary (citable) accession number: P37702
    Secondary accession number(s): B9DHN6
    , Q3E942, Q3V5A7, Q3V5A8, Q3V5A9, Q3V5B1, Q3V5B2, Q3V5B3, Q3V5B4, Q3V5B5, Q3V5B6, Q3V5B7, Q3V5B8, Q3V5B9, Q3V5C0, Q3V5C2, Q3V5C3, Q3V5C4, Q3V5C5, Q3V5C8, Q3V5D1, Q3V5D2, Q8H7H2, Q93Z31, Q940N8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: October 1, 1994
    Last modified: October 1, 2014
    This is version 123 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