Q9C5C2 (BGL37_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	547 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript 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.
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. The sequence AAK32833.1 differs from that shown. Reason: Erroneous initiation. The sequence AAN60275.1 differs from that shown. Reason: Frameshift at position 193. The sequence BAD94532.1 differs from that shown. Reason: Erroneous initiation. The sequence CAA55787.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Abscisic acid signaling pathway Plant defense
Coding sequence diversity	Alternative splicing
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	abscisic acid mediated signaling pathway Inferred from electronic annotation. Source: UniProtKB-KW carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro defense response to insect Inferred from mutant phenotype Ref.8. Source: UniProtKB glucosinolate catabolic process Inferred from mutant phenotype Ref.8. Source: TAIR regulation of stomatal movement Inferred from mutant phenotype Ref.9. Source: UniProtKB response to abscisic acid stimulus Inferred from mutant phenotype Ref.9. Source: UniProtKB
Cellular_component	apoplast Inferred from direct assay PubMed 18538804. Source: TAIR chloroplast Inferred from direct assay PubMed 15028209PubMed 18431481. Source: TAIR cytosolic ribosome Inferred from direct assay PubMed 15821981. Source: TAIR peroxisome Inferred from direct assay PubMed 17951448. Source: TAIR plasmodesma Inferred from direct assay PubMed 21533090. Source: TAIR vacuole Inferred from direct assay PubMed 15539469. Source: TAIR
Molecular_function	thioglucosidase activity Inferred from mutant phenotype Ref.8. Source: TAIR
Complete GO annotation...

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 28	28	Potential
	Chain	29 – 547	519	Myrosinase 2		PRO_0000389599
Regions
	Region	486 – 487	2	Substrate binding By similarity
Sites
	Active site	430	1	Nucleophile By similarity
	Binding site	69	1	Substrate By similarity
	Binding site	171	1	Substrate By similarity
	Binding site	216	1	Substrate By similarity
	Binding site	217	1	Ascorbate By similarity
	Binding site	289	1	Ascorbate By similarity
	Binding site	359	1	Substrate By similarity
	Binding site	479	1	Substrate By similarity
Amino acid modifications
	Glycosylation	340	1	N-linked (GlcNAc...) Potential
	Glycosylation	384	1	N-linked (GlcNAc...) Potential
	Glycosylation	504	1	N-linked (GlcNAc...) Potential
	Disulfide bond	36 ↔ 460		By similarity
	Disulfide bond	44 ↔ 456		By similarity
	Disulfide bond	236 ↔ 244		By similarity
Natural variations
	Alternative sequence	468 – 547	80	Missing in isoform 2.		VSP_038466
Experimental info
	Sequence conflict	100	1	D → N in AAN60275. Ref.6
	Sequence conflict	181	1	E → K in AAN60275. Ref.6
	Sequence conflict	255	1	I → N in AAL77743. Ref.4
	Sequence conflict	255	1	I → N in AAK32833. Ref.4
	Sequence conflict	356	1	L → P in BAE98479. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 3902D25F45B9DFAA	FASTA	547	62,732
	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
	Isoform 2 [UniParc]. Checksum: 84CD68F147AA326C	FASTA	467	53,423
	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 YGDPLIYVTE NGFSTSGGPI PFTEAFHDYN RIDYLCSHLC FLRKAIK

References

	« Hide 'large scale' referencesShow '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. , 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]	"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.
+	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.
IPI	IPI00525561. IPI00535583.
PIR	S56654.
RefSeq	NP_001031940.1. NM_001036863.1. NP_568479.1. NM_122499.3. NP_851076.2. NM_180745.2.
UniGene	At.22698.
3D structure databases
HSSP	HSSP built from PDB template 1MYR based on UniProtKB P29736.
ProteinModelPortal	Q9C5C2.
SMR	Q9C5C2. Positions 33-522.
ModBase	Search...
Protein-protein interaction databases
STRING	3702.AT5G25980.2-P.
Protein family/group databases
CAZy	GH1. Glycoside Hydrolase Family 1.
Proteomic databases
PaxDb	Q9C5C2.
PRIDE	Q9C5C2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT5G25980.2; AT5G25980.2; AT5G25980.
GeneID	832667.
KEGG	ath:AT5G25980.
Organism-specific databases
TAIR	At5g25980.
Phylogenomic databases
eggNOG	COG2723.
InParanoid	Q9C5C2.
OMA	RDWITIN.
PhylomeDB	Q9C5C2.
ProtClustDB	CLSN2689871.
Enzyme and pathway databases
BioCyc	MetaCyc:AT5G25980-MONOMER.
Gene expression databases
Genevestigator	Q9C5C2.
Family and domain databases
Gene3D	3.20.20.80. 1 hit.
InterPro	IPR001360. Glyco_hydro_1. IPR018120. Glyco_hydro_1_AS. IPR013781. Glyco_hydro_catalytic_dom. IPR017853. Glycoside_hydrolase_SF. [Graphical view]
PANTHER	PTHR10353. PTHR10353. 1 hit.
Pfam	PF00232. Glyco_hydro_1. 1 hit. [Graphical view]
PRINTS	PR00131. GLHYDRLASE1.
SUPFAM	SSF51445. Glyco_hydro_cat. 1 hit.
PROSITE	PS00572. GLYCOSYL_HYDROL_F1_1. 1 hit. PS00653. GLYCOSYL_HYDROL_F1_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

BGL37_ARATH

Accession

Primary (citable) accession number: Q9C5C2
Secondary accession number(s): Q0WWL9 , Q3E943, Q42595, Q56WQ3, Q56ZB8, Q8H7E3, Q9ASV0

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 24, 2009
Last sequence update:	June 1, 2001
Last modified:	May 1, 2013
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program