Q8GRX1 (BGL34_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Myrosinase 4
EC=3.2.1.147

Alternative name(s):
Beta-glucosidase 34
Short name=AtBGLU34
EC=3.2.1.21
Sinigrinase 4
Thioglucosidase 4

Gene names

Name:	TGG4
Synonyms:	BGLU34
Ordered Locus Names:	At1g47600
ORF Names:	F16N3.11

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	511 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	Hydrolyzes sinigrin and, with lower efficiency, p-nitrophenyl beta-D-glucoside. Ref.6
Catalytic activity	A thioglucoside + H2O = a sugar + a thiol. Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.
Tissue specificity	Specifically expressed in roots. Ref.6
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.
Biophysicochemical properties	Kinetic parameters: KM=245 µM for sinigrin (at pH 4.5) Ref.6 KM=28 mM for p-nitrophenyl beta-D-glucoside (at pH 4.5) Vmax=12.2 µmol/min/mg enzyme with sinigrin as substrate (at pH 4.5) Vmax=7.3 µmol/min/mg enzyme with p-nitrophenyl beta-D-glucoside as substrate (at pH 4.5)
Sequence caution	The sequence AAD46026.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
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	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro glucosinolate metabolic process Inferred from mutant phenotype PubMed 19095900. Source: TAIR response to salt stress Inferred from expression pattern PubMed 17916636. Source: TAIR
Molecular_function	beta-glucosidase activity Inferred from direct assay Ref.6. Source: TAIR thioglucosidase activity Inferred from direct assay Ref.6. Source: TAIR
Complete GO annotation...

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: Q8GRX1-1)

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 – 23	23	Potential
	Chain	24 – 511	488	Myrosinase 4		PRO_0000389596
Regions
	Region	474 – 475	2	Substrate binding By similarity
Sites
	Active site	418	1	Nucleophile By similarity
	Binding site	64	1	Substrate By similarity
	Binding site	165	1	Substrate By similarity
	Binding site	210	1	Substrate By similarity
	Binding site	211	1	Ascorbate By similarity
	Binding site	280	1	Ascorbate By similarity
	Binding site	351	1	Substrate By similarity
	Binding site	467	1	Substrate By similarity
Amino acid modifications
	Glycosylation	46	1	N-linked (GlcNAc...) Potential
	Glycosylation	53	1	N-linked (GlcNAc...) Potential
	Glycosylation	428	1	N-linked (GlcNAc...) Potential
	Glycosylation	489	1	N-linked (GlcNAc...) Potential
	Disulfide bond	31 ↔ 450		By similarity
	Disulfide bond	39 ↔ 445		By similarity
	Disulfide bond	230 ↔ 233		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: A977148B22E21D0E	FASTA	511	57,542
	10 20 30 40 50 60 MAIPKAHYSL AVLVLLFVVV SSSQKVCNPE CKAKEPFHCD NTHAFNRTGF PRNFTFGAAT 70 80 90 100 110 120 SAYQIEGAAH RALNGWDYFT HRYPEKVPDR SSGDLACDSY DLYKDDVKLL KRMNVQAYRL 130 140 150 160 170 180 SIAWSRVLPK GRLTGGVDEN GITYYNNLIN ELKANGIEPY VTIFHWDVPQ TLEDEYGGFL 190 200 210 220 230 240 STRIVEDYTN YAELLFQRFG DRVKFWITLN QPFSLATKGY GDGSYPPGRC TGCELGGDSG 250 260 270 280 290 300 VEPYTVAHNQ LLAHAKTVSL YRKRYQKFQG GKIGTTLIGR WFAPLNEFSE LDKAAAKRAF 310 320 330 340 350 360 DFFVGWFLDP LVYGKYPTIM REMVGDRLPE FTPEQSALVK GSLDFLGLNY YVTQYATDAP 370 380 390 400 410 420 PPTQLNAITD ARVTLGFYRN GVPIGVVAPS FVYYPPGFRQ ILNYIKDNYK NPLTYITENG 430 440 450 460 470 480 VADLDLGNVT LATALADNGR IQNHCSHLSC LKCAMKDGCN VAGYFAWSLM DNYEFGNGYT 490 500 510 LRFGMNWVNF TNPADRKEKA SGKWFSKFLA K

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of a new subfamily of thioglucoside glucohydrolases." Zhang J. Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: cv. Columbia.
[2]	"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana." Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W. Nature 408:816-820(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]. Strain: cv. Columbia.
[5]	"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.
[6]	"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, TISSUE SPECIFICITY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	FJ268795 Genomic DNA. Translation: ACO95139.1. AC007519 Genomic DNA. Translation: AAD46026.1. Sequence problems. CP002684 Genomic DNA. Translation: AEE32191.1. BT000471 mRNA. Translation: AAN17448.1. BT002202 mRNA. Translation: AAN72213.1. BT002458 mRNA. Translation: AAO00818.1.
IPI	IPI00522382.
PIR	G96516.
RefSeq	NP_175191.2. NM_103653.2.
UniGene	At.25235.
3D structure databases
HSSP	HSSP built from PDB template 1CBG based on UniProtKB P26205.
ProteinModelPortal	Q8GRX1.
SMR	Q8GRX1. Positions 46-511.
ModBase	Search...
Protein-protein interaction databases
STRING	3702.AT1G47600.1-P.
Protein family/group databases
CAZy	GH1. Glycoside Hydrolase Family 1.
Proteomic databases
PaxDb	Q8GRX1.
PRIDE	Q8GRX1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT1G47600.1; AT1G47600.1; AT1G47600.
GeneID	841169.
KEGG	ath:AT1G47600.
Organism-specific databases
TAIR	At1g47600.
Phylogenomic databases
eggNOG	COG2723.
HOGENOM	HOG000088630.
InParanoid	Q8GRX1.
OMA	AFNIMLA.
PhylomeDB	Q8GRX1.
ProtClustDB	CLSN2680410.
Enzyme and pathway databases
SABIO-RK	Q8GRX1.
Gene expression databases
ArrayExpress	Q8GRX1.
Genevestigator	Q8GRX1.
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

BGL34_ARATH

Accession

Primary (citable) accession number: Q8GRX1
Secondary accession number(s): Q9SX92

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 2009
Last sequence update:	March 1, 2003
Last modified:	May 1, 2013
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program