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Q9SVS1

- BGL47_ARATH

UniProt

Q9SVS1 - BGL47_ARATH

Protein

Beta-glucosidase 47

Gene

BGLU47

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 82 (01 Oct 2014)
      Sequence version 2 (15 Dec 2009)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei73 – 731SubstrateBy similarity
    Binding sitei175 – 1751SubstrateBy similarity
    Binding sitei220 – 2201SubstrateBy similarity
    Active sitei221 – 2211Proton donorBy similarity
    Binding sitei363 – 3631SubstrateBy similarity
    Active sitei426 – 4261NucleophilePROSITE-ProRule annotation
    Binding sitei470 – 4701SubstrateBy similarity

    GO - Molecular functioni

    1. beta-glucosidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. carbohydrate metabolic process Source: InterPro

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Enzyme and pathway databases

    BioCyciARA:AT4G21760-MONOMER.

    Protein family/group databases

    CAZyiGH1. Glycoside Hydrolase Family 1.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-glucosidase 47 (EC:3.2.1.21)
    Short name:
    AtBGLU47
    Gene namesi
    Name:BGLU47
    Ordered Locus Names:At4g21760
    ORF Names:F17L22.220
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 4

    Organism-specific databases

    TAIRiAT4G21760.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3838Sequence AnalysisAdd
    BLAST
    Chaini39 – 535497Beta-glucosidase 47PRO_0000390319Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi93 – 931N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi240 ↔ 247By similarity
    Glycosylationi246 – 2461N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi419 – 4191N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi432 – 4321N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ9SVS1.
    PRIDEiQ9SVS1.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9SVS1.
    SMRiQ9SVS1. Positions 59-513.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni477 – 4782Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 1 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG2723.
    HOGENOMiHOG000088630.
    InParanoidiQ9SVS1.
    KOiK05350.
    OMAiIDEYRIN.
    PhylomeDBiQ9SVS1.

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    InterProiIPR001360. Glyco_hydro_1.
    IPR018120. Glyco_hydro_1_AS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PANTHERiPTHR10353. PTHR10353. 1 hit.
    PfamiPF00232. Glyco_hydro_1. 1 hit.
    [Graphical view]
    PRINTSiPR00131. GLHYDRLASE1.
    SUPFAMiSSF51445. SSF51445. 1 hit.
    PROSITEiPS00572. GLYCOSYL_HYDROL_F1_1. 1 hit.
    PS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9SVS1-1 [UniParc]FASTAAdd to Basket

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    MKKSIVYEIM ETKSSMYLSQ FRLWLCFIIT TLVSLSSSTR WYDDHISLKE    50
    IHAEETFHFP KNFLFGTASS AYQYEGAYLT DGKTLSNWDV FTNISGKIAD 100
    GSHGKVAVDH YHRYPGDLDL MEDLGVNSYR LSLSWARILP KGRFGDVNMG 150
    GIDHYNRMIN DILKTGIEPF VTLTHYDIPQ ELEYRYGSWL NPQIREDFEH 200
    YANICFRHFG DRVKFWSTFN EPNVQVILGY RTGTYPPSRC SKPFGNCSCG 250
    DSYIEPLVAA HNIILSHLAA VNLYRTKFQE QQRGQIGIVM NTIWFEPISD 300
    SLADRLAADR AQAFYLTWFL DPVVFGRYPR EMREILGDDL PEFTKDDLKS 350
    SKNALDFIGI NQYTSRYAKD CLHSVCEPGK GGSRAEGFVY ANALKDGLRL 400
    GEPVGMEEML MYATERYKNI TLYVTENGFG ENNTGVLLND YQRVKFMSNY 450
    LDALKRAMRK GADVRGYFAW SLLDNFEWIS GYTIRFGMYH VDFSTQERTP 500
    RLSASWYKNF IFQHRALSKD DWCLKQKEDT NFFLI 535
    Length:535
    Mass (Da):61,962
    Last modified:December 15, 2009 - v2
    Checksum:i399BF7E254501870
    GO

    Sequence cautioni

    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.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL035527 Genomic DNA. Translation: CAB36820.1. Sequence problems.
    AL161555 Genomic DNA. Translation: CAB81283.1. Sequence problems.
    CP002687 Genomic DNA. Translation: AEE84500.1.
    PIRiT05851.
    RefSeqiNP_193907.2. NM_118296.3.
    UniGeneiAt.32601.

    Genome annotation databases

    EnsemblPlantsiAT4G21760.1; AT4G21760.1; AT4G21760.
    GeneIDi828264.
    KEGGiath:AT4G21760.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL035527 Genomic DNA. Translation: CAB36820.1 . Sequence problems.
    AL161555 Genomic DNA. Translation: CAB81283.1 . Sequence problems.
    CP002687 Genomic DNA. Translation: AEE84500.1 .
    PIRi T05851.
    RefSeqi NP_193907.2. NM_118296.3.
    UniGenei At.32601.

    3D structure databases

    ProteinModelPortali Q9SVS1.
    SMRi Q9SVS1. Positions 59-513.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH1. Glycoside Hydrolase Family 1.

    Proteomic databases

    PaxDbi Q9SVS1.
    PRIDEi Q9SVS1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT4G21760.1 ; AT4G21760.1 ; AT4G21760 .
    GeneIDi 828264.
    KEGGi ath:AT4G21760.

    Organism-specific databases

    TAIRi AT4G21760.

    Phylogenomic databases

    eggNOGi COG2723.
    HOGENOMi HOG000088630.
    InParanoidi Q9SVS1.
    KOi K05350.
    OMAi IDEYRIN.
    PhylomeDBi Q9SVS1.

    Enzyme and pathway databases

    BioCyci ARA:AT4G21760-MONOMER.

    Family and domain databases

    Gene3Di 3.20.20.80. 1 hit.
    InterProi IPR001360. Glyco_hydro_1.
    IPR018120. Glyco_hydro_1_AS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    PANTHERi PTHR10353. PTHR10353. 1 hit.
    Pfami PF00232. Glyco_hydro_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00131. GLHYDRLASE1.
    SUPFAMi SSF51445. SSF51445. 1 hit.
    PROSITEi PS00572. GLYCOSYL_HYDROL_F1_1. 1 hit.
    PS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. Cited for: GENE FAMILY, NOMENCLATURE.

    Entry informationi

    Entry nameiBGL47_ARATH
    AccessioniPrimary (citable) accession number: Q9SVS1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 2009
    Last sequence update: December 15, 2009
    Last modified: October 1, 2014
    This is version 82 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3