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O65458 (BGL03_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 78. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Beta-glucosidase 3

Short name=AtBGLU3
EC=3.2.1.21
Gene names
Name:BGLU3
Ordered Locus Names:At4g22100
ORF Names:F1N20.200
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length507 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

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

Sequence similarities

Belongs to the glycosyl hydrolase 1 family.

Sequence caution

The sequence CAA18113.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAB79165.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular_functionbeta-glucosidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 507484Beta-glucosidase 3
PRO_0000389565

Regions

Region446 – 4472Substrate binding By similarity

Sites

Active site1841Proton donor By similarity
Active site3941Nucleophile By similarity
Binding site411Substrate By similarity
Binding site1381Substrate By similarity
Binding site1831Substrate By similarity
Binding site3261Substrate By similarity
Binding site4391Substrate By similarity

Amino acid modifications

Glycosylation641N-linked (GlcNAc...) Potential
Glycosylation2091N-linked (GlcNAc...) Potential
Glycosylation2141N-linked (GlcNAc...) Potential
Glycosylation3611N-linked (GlcNAc...) Potential
Glycosylation4291N-linked (GlcNAc...) Potential
Glycosylation4611N-linked (GlcNAc...) Potential
Glycosylation4851N-linked (GlcNAc...) Potential
Glycosylation5001N-linked (GlcNAc...) Potential
Disulfide bond203 ↔ 210 By similarity

Sequences

Sequence LengthMass (Da)Tools
O65458 [UniParc].

Last modified November 24, 2009. Version 2.
Checksum: 528122A8333F0465

FASTA50757,307
        10         20         30         40         50         60 
MELTLSLLTI FLLFFALSGR CSDKNDFPEG FIFGSATSAY QWEGAFDEDG RKPSVWDTFL 

        70         80         90        100        110        120 
HTRNLSNGDI TSDGYHKYKE DVKLMVETGL DAFRFSISWS RLIPNGRGPV NPKGLQFYKN 

       130        140        150        160        170        180 
FIQELVSHGI EPHVTLFHYD HPQYLEDEYG GWINRRIIQD FTAYANVCFR EFGHHVKFWT 

       190        200        210        220        230        240 
TINEANIFTI GGYNDGITPP GRCSSPGRNC SSGNSSTEPY IVGHNLLLAH ASASRLYKQK 

       250        260        270        280        290        300 
YKDMQGGSVG FSLFSLGFTP STSSKDDDIA VQRAKDFYFG WMLEPFIFGD YPDEMKRTVG 

       310        320        330        340        350        360 
SRLPVFSKEE SEQVKGSSDF IGIIHYLAAS VTSIKIKPSI SGNPDFYSDM GVSMTWTVLG 

       370        380        390        400        410        420 
NFSAFEYAVA PWAMESVLEY IKQSYGNPPI YILENGTPMK QDLQLQQKDT PRIEYLHAYI 

       430        440        450        460        470        480 
AAVLKSIRNG SDTRGYFIWS FMDLYELVKG YEFSFGLYSV NFSDPHRTRS PKLSAHWYSA 

       490        500 
FLKGNTTFLG SQGIMQMQSN FSSSASS 

« Hide

References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. expand/collapse author list , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[3]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL022140 Genomic DNA. Translation: CAA18113.1. Sequence problems.
AL161556 Genomic DNA. Translation: CAB79165.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE84549.1.
PIRT49117.
RefSeqNP_193941.2. NM_118331.2.
UniGeneAt.32568.

3D structure databases

ProteinModelPortalO65458.
SMRO65458. Positions 24-482.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING3702.AT4G22100.1-P.

Protein family/group databases

CAZyGH1. Glycoside Hydrolase Family 1.

Proteomic databases

PaxDbO65458.
PRIDEO65458.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G22100.1; AT4G22100.1; AT4G22100.
GeneID828299.
KEGGath:AT4G22100.

Organism-specific databases

TAIRAT4G22100.

Phylogenomic databases

eggNOGCOG2723.
HOGENOMHOG000088630.
KOK01188.
OMAAPWAMES.
PhylomeDBO65458.

Enzyme and pathway databases

BioCycARA:AT4G22100-MONOMER.

Gene expression databases

GenevestigatorO65458.

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.
PROSITEPS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameBGL03_ARATH
AccessionPrimary (citable) accession number: O65458
Entry history
Integrated into UniProtKB/Swiss-Prot: November 24, 2009
Last sequence update: November 24, 2009
Last modified: May 14, 2014
This is version 78 of the entry and version 2 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