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Q9SVS1 (BGL47_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 80. 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 47

Short name=AtBGLU47
EC=3.2.1.21
Gene names
Name:BGLU47
Ordered Locus Names:At4g21760
ORF Names:F17L22.220
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length535 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 CAB36820.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAB81283.1 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 – 3838 Potential
Chain39 – 535497Beta-glucosidase 47
PRO_0000390319

Regions

Region477 – 4782Substrate binding By similarity

Sites

Active site2211Proton donor By similarity
Active site4261Nucleophile By similarity
Binding site731Substrate By similarity
Binding site1751Substrate By similarity
Binding site2201Substrate By similarity
Binding site3631Substrate By similarity
Binding site4701Substrate By similarity

Amino acid modifications

Glycosylation931N-linked (GlcNAc...) Potential
Glycosylation2461N-linked (GlcNAc...) Potential
Glycosylation4191N-linked (GlcNAc...) Potential
Glycosylation4321N-linked (GlcNAc...) Potential
Disulfide bond240 ↔ 247 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9SVS1 [UniParc].

Last modified December 15, 2009. Version 2.
Checksum: 399BF7E254501870

FASTA53561,962
        10         20         30         40         50         60 
MKKSIVYEIM ETKSSMYLSQ FRLWLCFIIT TLVSLSSSTR WYDDHISLKE IHAEETFHFP 

        70         80         90        100        110        120 
KNFLFGTASS AYQYEGAYLT DGKTLSNWDV FTNISGKIAD GSHGKVAVDH YHRYPGDLDL 

       130        140        150        160        170        180 
MEDLGVNSYR LSLSWARILP KGRFGDVNMG GIDHYNRMIN DILKTGIEPF VTLTHYDIPQ 

       190        200        210        220        230        240 
ELEYRYGSWL NPQIREDFEH YANICFRHFG DRVKFWSTFN EPNVQVILGY RTGTYPPSRC 

       250        260        270        280        290        300 
SKPFGNCSCG DSYIEPLVAA HNIILSHLAA VNLYRTKFQE QQRGQIGIVM NTIWFEPISD 

       310        320        330        340        350        360 
SLADRLAADR AQAFYLTWFL DPVVFGRYPR EMREILGDDL PEFTKDDLKS SKNALDFIGI 

       370        380        390        400        410        420 
NQYTSRYAKD CLHSVCEPGK GGSRAEGFVY ANALKDGLRL GEPVGMEEML MYATERYKNI 

       430        440        450        460        470        480 
TLYVTENGFG ENNTGVLLND YQRVKFMSNY LDALKRAMRK GADVRGYFAW SLLDNFEWIS 

       490        500        510        520        530 
GYTIRFGMYH VDFSTQERTP RLSASWYKNF IFQHRALSKD DWCLKQKEDT NFFLI 

« 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL035527 Genomic DNA. Translation: CAB36820.1. Sequence problems.
AL161555 Genomic DNA. Translation: CAB81283.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE84500.1.
PIRT05851.
RefSeqNP_193907.2. NM_118296.3.
UniGeneAt.32601.

3D structure databases

ProteinModelPortalQ9SVS1.
SMRQ9SVS1. Positions 59-513.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH1. Glycoside Hydrolase Family 1.

Proteomic databases

PaxDbQ9SVS1.
PRIDEQ9SVS1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G21760.1; AT4G21760.1; AT4G21760.
GeneID828264.
KEGGath:AT4G21760.

Organism-specific databases

TAIRAT4G21760.

Phylogenomic databases

eggNOGCOG2723.
HOGENOMHOG000088630.
InParanoidQ9SVS1.
KOK05350.
OMAWISGYTI.
PhylomeDBQ9SVS1.
ProtClustDBCLSN2915051.

Enzyme and pathway databases

BioCycARA:AT4G21760-MONOMER.

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 nameBGL47_ARATH
AccessionPrimary (citable) accession number: Q9SVS1
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2009
Last sequence update: December 15, 2009
Last modified: February 19, 2014
This is version 80 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