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P37702

- BGL38_ARATH

UniProt

P37702 - BGL38_ARATH

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Protein

Myrosinase 1

Gene
TGG1, BGLU38, At5g26000, T1N24.7
Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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)

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

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei57 – 571Substrate By similarity
Metal bindingi74 – 741Zinc; shared with dimeric partner By similarity
Metal bindingi88 – 881Zinc; shared with dimeric partner By similarity
Binding sitei159 – 1591Substrate By similarity
Binding sitei204 – 2041Substrate By similarity
Binding sitei205 – 2051Ascorbate By similarity
Binding sitei278 – 2781Ascorbate By similarity
Binding sitei348 – 3481Substrate By similarity
Active sitei420 – 4201Nucleophile By similarity
Binding sitei468 – 4681Substrate By 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
Complete GO annotation...

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
Complete GO annotation...

Keywords - Cellular componenti

Vacuole

PTM / Processingi

Molecule processing

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

Amino acid modifications

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

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.

Family & Domainsi

Region

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

Sequence similaritiesi

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

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. VSP_038446Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti385 – 3851P → H in AAL06896. 1 Publication
Sequence conflicti426 – 4261P → A in AAL25596. 1 Publication
Sequence conflicti434 – 4341A → T in BAH20253. 1 Publication
Sequence conflicti441 – 4411I → N in BAH20253. 1 Publication

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

« Hide 'large scale' publications
  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: May 14, 2014
This is version 122 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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