Reviewed, UniProtKB/Swiss-Prot P37702 (MYRO_ARATH)

Names and origin

Protein names

Recommended name:
    Myrosinase
    EC=3.2.1.147
Alternative name(s):
    Sinigrinase
    Thioglucosidase

Gene names

Name:	TGG1
Ordered Locus Names:	At5g26000
ORF Names:	T1N24.7

Organism

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

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	541 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	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.
Catalytic activity	A thioglucoside + H2O = a sugar + a thiol.
Cofactor	Binds 1 ascorbate molecule per subunit By similarity.
Subunit structure	Homodimer By similarity.
Subcellular location	Vacuole By similarity.
Sequence similarities	Belongs to the glycosyl hydrolase 1 family.

Ontologies

Keywords
Cellular component	Vacuole
Coding sequence diversity	Alternative splicing
Domain	Signal
Ligand	Metal-binding Zinc
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	glucosinolate catabolic process Ref.2 Inferred from mutant phenotype. Source: TAIR
Cellular component	apoplast Inferred from direct assay. Source: TAIR chloroplast Inferred from direct assay. Source: TAIR cytosolic ribosome Inferred from direct assay. Source: TAIR peroxisome Inferred from direct assay. Source: TAIR plant-type cell wall Inferred from direct assay. Source: TAIR thylakoid Inferred from direct assay. Source: TAIR vacuole Inferred from direct assay. Source: TAIR
Molecular function	protein binding Inferred from physical interaction. Source: IntAct thioglucosidase activity Inferred from direct assay. Source: TAIR zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
TRX3	Q42403	1	EBI-449510,EBI-449157

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: P37702-1)

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.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 19	19	Potential
	Chain	20 – 541	522	Myrosinase		PRO_0000011773
Regions
	Region	204 – 205	2	Substrate By similarity
	Region	475 – 476	2	Substrate By similarity
Sites
	Active site	420	1	Nucleophile By similarity
	Metal binding	74	1	Zinc; shared with dimeric partner By similarity
	Metal binding	88	1	Zinc; shared with dimeric partner By similarity
	Binding site	57	1	Substrate By similarity
	Binding site	159	1	Substrate By similarity
	Binding site	205	1	Ascorbate cofactor By similarity
	Binding site	278	1	Ascorbate cofactor By similarity
	Binding site	348	1	Substrate By similarity
	Binding site	389	1	Substrate By similarity
	Binding site	420	1	Substrate By similarity
	Binding site	468	1	Substrate By similarity
	Binding site	484	1	Substrate By similarity
Amino acid modifications
	Glycosylation	33	1	N-linked (GlcNAc...) Potential
	Glycosylation	108	1	N-linked (GlcNAc...) Potential
	Glycosylation	175	1	N-linked (GlcNAc...) Potential
	Glycosylation	236	1	N-linked (GlcNAc...) Potential
	Glycosylation	356	1	N-linked (GlcNAc...) Potential
	Glycosylation	379	1	N-linked (GlcNAc...) Potential
	Glycosylation	493	1	N-linked (GlcNAc...) Potential
	Glycosylation	512	1	N-linked (GlcNAc...) Potential
	Disulfide bond	24 ↔ 449		By similarity
	Disulfide bond	32 ↔ 445		By similarity
	Disulfide bond	224 ↔ 232		By similarity
Experimental info
	Sequence conflict	385	1	P → H in AAL06896. Ref.4
	Sequence conflict	426	1	P → A in AAL25596. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 1994. Version 1. Checksum: 3736B735DE7A5BD1	FASTA	541	61,133
	10 20 30 40 50 60 MKLLMLAFVF LLALATCKGD EFVCEENEPF TCNQTKLFNS GNFEKGFIFG VASSAYQVEG 70 80 90 100 110 120 GRGRGLNVWD SFTHRFPEKG GADLGNGDTT CDSYTLWQKD IDVMDELNST GYRFSIAWSR 130 140 150 160 170 180 LLPKGKRSRG VNPGAIKYYN GLIDGLVAKN MTPFVTLFHW DLPQTLQDEY NGFLNKTIVD 190 200 210 220 230 240 DFKDYADLCF ELFGDRVKNW ITINQLYTVP TRGYALGTDA PGRCSPKIDV RCPGGNSSTE 250 260 270 280 290 300 PYIVAHNQLL AHAAAVDVYR TKYKDDQKGM IGPVMITRWF LPFDHSQESK DATERAKIFF 310 320 330 340 350 360 HGWFMGPLTE GKYPDIMREY VGDRLPEFSE TEAALVKGSY DFLGLNYYVT QYAQNNQTIV 370 380 390 400 410 420 PSDVHTALMD SRTTLTSKNA TGHAPGPPFN AASYYYPKGI YYVMDYFKTT YGDPLIYVTE 430 440 450 460 470 480 NGFSTPGDED FEKATADYKR IDYLCSHLCF LSKVIKEKNV NVKGYFAWSL GDNYEFCNGF 490 500 510 520 530 540 TVRFGLSYVD FANITGDRDL KASGKWFQKF INVTDEDSTN QDLLRSSVSS KNRDRKSLAD A

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Arabidopsis cDNA sequence encoding myrosinase." Chadchawan S., Bishop J., Thangstad O.P., Bones A.M., Mitchell-Olds T., Bradley D. Plant Physiol. 103:671-671(1993) [PubMed: 8029343] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. 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: 7766881] [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: 11130714] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[5]	"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.
[6]	"An inventory of 1152 expressed sequence tags obtained by partial sequencing of cDNAs from Arabidopsis thaliana." Hoefte H., Desprez T., Amselem J., Chiapello H., Rouze P., Caboche M., Moisan A., Jourjon M.-F., Charpenteau J.-L., Berthomieu P., Guerrier D., Giraudat J., Quigley F., Thomas F., Yu D.-Y., Mache R., Raynal M., Cooke R. , Grellet F., Delseny M., Parmentier Y., de Marcillac G., Gigot C., Fleck J., Philipps G., Axelos M., Bardet C., Tremousaygue D., Lescure B. Plant J. 4:1051-1061(1993) [PubMed: 8281187] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 192-250. Strain: cv. C24. Tissue: Flower bud.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L11454 mRNA. Translation: AAC18869.1. X79194 Genomic DNA. Translation: CAA55786.1. AF149413 Genomic DNA. Translation: AAD40143.1. 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. Z18232 mRNA. Translation: CAA79143.1.
IPI	IPI00539116.
PIR	S56653.
RefSeq	NP_851077.1.
UniGene	At.23592 At.47944 At.73176
3D structure databases
HSSP	HSSP built from PDB template 1E6X based on UniProtKB P29736.
ModBase	Search...
Protein-protein interaction databases
IntAct	P37702. 1 interaction.
Protein family/group databases
CAZy	GH1. Glycoside Hydrolase Family 1.
2-D gel databases
SWISS-2DPAGE	P37702.
Proteomic databases
PRIDE	P37702.
Genome annotation databases
GeneID	832669.
GenomeReviews	Gene locus AT5G26000 in contig BA000015_GR.
NMPDR	fig|3702.1.peg.24802.
Organism-specific databases
TAIR	At5g26000.
Phylogenomic databases
OMA	P37702. AVYITEN.
Enzyme and pathway databases
BRENDA	3.2.1.147. 302.
Family and domain databases
InterPro	IPR001360. Glyco_hydro_1. IPR018120. Glyco_hydro_1_AS. IPR013781. Glyco_hydro_sg_catalytic. [Graphical view]
Gene3D	G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
PANTHER	PTHR10353. Glyco_hydro_1. 1 hit.
Pfam	PF00232. Glyco_hydro_1. 1 hit. [Graphical view]
PRINTS	PR00131. GLHYDRLASE1.
PROSITE	PS00572. GLYCOSYL_HYDROL_F1_1. 1 hit. PS00653. GLYCOSYL_HYDROL_F1_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MYRO_ARATH

Accession

Primary (citable) accession number: P37702
Secondary accession number(s): Q8H7H2, Q93Z31, Q940N8

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	October 1, 1994
Last modified:	June 16, 2009
This is version 82 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)