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P37702 (BGL38_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Myrosinase 1

EC=3.2.1.147
Alternative name(s):
Beta-glucosidase 38
Short name=AtBGLU38
EC=3.2.1.21
Sinigrinase 1
Thioglucosidase 1
Gene names
Name:TGG1
Synonyms:BGLU38
Ordered Locus Names:At5g26000
ORF Names:T1N24.7
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length541 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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. 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. Ref.7 Ref.12 Ref.13 Ref.14

Catalytic activity

A thioglucoside + H2O = a sugar + a thiol.

Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.

Subunit structure

Homodimer By similarity.

Subcellular location

Vacuole By similarity.

Tissue specificity

Expressed in guard cells, phloem-associated cells and myrosin cells. Ref.10

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=45 µM for sinigrin (at pH 4.5) Ref.13

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)

Ontologies

Keywords
   Biological processAbscisic acid signaling pathway
Plant defense
   Cellular componentVacuole
   Coding sequence diversityAlternative splicing
   DomainSignal
   LigandMetal-binding
Zinc
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processabscisic acid-activated 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.12. Source: UniProtKB

glucosinolate catabolic process

Inferred from mutant phenotype Ref.12. Source: TAIR

regulation of stomatal movement

Inferred from mutant phenotype Ref.14. Source: UniProtKB

response to abscisic acid

Inferred from mutant phenotype Ref.14. Source: UniProtKB

response to insect

Inferred from expression pattern PubMed 23144921. Source: TAIR

   Cellular_componentapoplast

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

plant-type cell wall

Inferred from direct assay PubMed 17526915. Source: TAIR

thylakoid

Inferred from direct assay PubMed 16648217. Source: TAIR

vacuole

Inferred from direct assay PubMed 15539469. Source: TAIR

   Molecular_functionbeta-glucosidase activity

Inferred from direct assay Ref.13. Source: TAIR

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

thioglucosidase activity

Inferred from mutant phenotype Ref.12. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
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.
Isoform 2 (identifier: P37702-2)

The sequence of this isoform differs from the canonical sequence as follows:
     457-541: Missing.
Note: Derived from EST data. No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 541522Myrosinase 1
PRO_0000011773

Regions

Region475 – 4762Substrate binding By similarity

Sites

Active site4201Nucleophile By similarity
Metal binding741Zinc; shared with dimeric partner By similarity
Metal binding881Zinc; shared with dimeric partner By similarity
Binding site571Substrate By similarity
Binding site1591Substrate By similarity
Binding site2041Substrate By similarity
Binding site2051Ascorbate By similarity
Binding site2781Ascorbate By similarity
Binding site3481Substrate By similarity
Binding site4681Substrate By similarity

Amino acid modifications

Glycosylation331N-linked (GlcNAc...) Potential
Glycosylation1081N-linked (GlcNAc...) Potential
Glycosylation1751N-linked (GlcNAc...) Potential
Glycosylation2361N-linked (GlcNAc...) Potential
Glycosylation3561N-linked (GlcNAc...) Potential
Glycosylation3791N-linked (GlcNAc...) Potential
Glycosylation4931N-linked (GlcNAc...) Potential
Glycosylation5121N-linked (GlcNAc...) Potential
Disulfide bond24 ↔ 449 By similarity
Disulfide bond32 ↔ 445 By similarity
Disulfide bond224 ↔ 232 By similarity

Natural variations

Alternative sequence457 – 54185Missing in isoform 2.
VSP_038446
Natural variant1281S → N in strain: cv. Ta-0. Ref.7
Natural variant2611T → K in strain: cv. Ba-1. Ref.7
Natural variant2641K → Q in strain: cv. Ba-1. Ref.7
Natural variant4271G → A in strain: cv. Ag-0, cv. Ba-1, cv. Mh-0, cv. Mr-0 and Tac-0. Ref.7
Natural variant4591N → G in strain: cv. Su-0. Ref.7
Natural variant4891V → I in strain: cv. No-0, cv. Rsch-0 and cv. Ta-0. Ref.7

Experimental info

Sequence conflict3851P → H in AAL06896. Ref.5
Sequence conflict4261P → A in AAL25596. Ref.5
Sequence conflict4341A → T in BAH20253. Ref.8
Sequence conflict4411I → N in BAH20253. Ref.8

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 1994. Version 1.
Checksum: 3736B735DE7A5BD1

FASTA54161,133
        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 

« Hide

Isoform 2 [UniParc].

Checksum: DE7CE563F352A0BB
Show »

FASTA45651,481

References

« Hide '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] [Europe PMC] [Abstract]
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. expand/collapse author list , 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. expand/collapse author list , 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]"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. expand/collapse author list , 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] [Europe PMC] [Abstract]
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]"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.
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS56653.
RefSeqNP_197972.2. NM_122501.3. [P37702-2]
NP_851077.1. NM_180746.2. [P37702-1]
UniGeneAt.23592.
At.47944.
At.73176.

3D structure databases

ProteinModelPortalP37702.
SMRP37702. Positions 21-512.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid17944. 5 interactions.
IntActP37702. 1 interaction.

Protein family/group databases

CAZyGH1. Glycoside Hydrolase Family 1.

2D gel databases

SWISS-2DPAGEP37702.

Proteomic databases

PRIDEP37702.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G26000.1; AT5G26000.1; AT5G26000. [P37702-1]
GeneID832669.
KEGGath:AT5G26000.

Organism-specific databases

TAIRAT5G26000.

Phylogenomic databases

InParanoidP37702.
KOK01237.
OMANWITINQ.
PhylomeDBP37702.

Enzyme and pathway databases

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

Gene expression databases

GenevestigatorP37702.

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR001360. Glyco_hydro_1.
IPR018120. Glyco_hydro_1_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERPTHR10353. PTHR10353. 1 hit.
PfamPF00232. Glyco_hydro_1. 1 hit.
[Graphical view]
PRINTSPR00131. GLHYDRLASE1.
SUPFAMSSF51445. SSF51445. 1 hit.
PROSITEPS00572. GLYCOSYL_HYDROL_F1_1. 1 hit.
PS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameBGL38_ARATH
AccessionPrimary (citable) accession number: P37702
Secondary accession number(s): B9DHN6 expand/collapse secondary AC list , 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 history
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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names