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P12614

- BGLS_AGRSA

UniProt

P12614 - BGLS_AGRSA

Protein

Beta-glucosidase

Gene

abg

Organism
Agrobacterium sp. (strain ATCC 21400)
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
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    • History
      Entry version 76 (01 Oct 2014)
      Sequence version 1 (01 Oct 1989)
      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
    Active sitei171 – 1711Proton donorSequence Analysis
    Active sitei359 – 3591Nucleophile1 PublicationPROSITE-ProRule annotation

    GO - Molecular functioni

    1. beta-glucosidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. cellulose catabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

    Enzyme and pathway databases

    BioCyciRETL1328306-WGS:GSTH-3714-MONOMER.

    Protein family/group databases

    CAZyiGH1. Glycoside Hydrolase Family 1.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-glucosidase (EC:3.2.1.21)
    Alternative name(s):
    Amygdalase
    Beta-D-glucoside glucohydrolase
    Cellobiase
    Gentiobiase
    Gene namesi
    Name:abg
    OrganismiAgrobacterium sp. (strain ATCC 21400)
    Taxonomic identifieri74562 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeRhizobium/Agrobacterium groupAgrobacterium

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 459459Beta-glucosidasePRO_0000063869Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliP12614.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 1 family.Curated

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    InterProiIPR001360. Glyco_hydro_1.
    IPR018120. Glyco_hydro_1_AS.
    IPR017736. Glyco_hydro_1_beta-glucosidase.
    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.
    TIGRFAMsiTIGR03356. BGL. 1 hit.
    PROSITEiPS00572. GLYCOSYL_HYDROL_F1_1. 1 hit.
    PS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P12614-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTDPNTLAAR FPGDFLFGVA TASFQIEGST KADGRKPSIW DAFCNMPGHV    50
    FGRHNGDIAC DHYNRWEEDL DLIKEMGVEA YRFSLAWPRI IPDGFGPINE 100
    KGLDFYDRLV DGCKARGIKT YATLYHWDLP LTLMGDGGWA SRSTAHAFQR 150
    YAKTVMARLG DRLDAVATFN EPWCAVWLSH LYGVHAPGER NMEAALAAMH 200
    HINLAHGFGV EASRHVAPKV PVGLVLNAHS AIPASDGEAD LKAAERAFQF 250
    HNGAFFDPVF KGEYPAEMME ALGDRMPVVE AEDLGIISQK LDWWGLNYYT 300
    PMRVADDATP GVEFPATMPA PAVSDVKTDI GWEVYAPALH TLVETLYERY 350
    DLPECYITEN GACYNMGVEN GQVNDQPRLD YYAEHLGIVA DLIRDGYPMR 400
    GYFAWSLMDN FEWAEGYRMR FGLVHVDYQT QVRTVKNSGK WYSALASGFP 450
    KGNHGVAKG 459
    Length:459
    Mass (Da):51,170
    Last modified:October 1, 1989 - v1
    Checksum:iAAB799153493A682
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M19033 Genomic DNA. Translation: AAA22085.1.
    PIRiA28673. GLAG.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M19033 Genomic DNA. Translation: AAA22085.1 .
    PIRi A28673. GLAG.

    3D structure databases

    ProteinModelPortali P12614.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    ChEMBLi CHEMBL1075038.

    Protein family/group databases

    CAZyi GH1. Glycoside Hydrolase Family 1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    BioCyci RETL1328306-WGS:GSTH-3714-MONOMER.

    Family and domain databases

    Gene3Di 3.20.20.80. 1 hit.
    InterProi IPR001360. Glyco_hydro_1.
    IPR018120. Glyco_hydro_1_AS.
    IPR017736. Glyco_hydro_1_beta-glucosidase.
    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.
    TIGRFAMsi TIGR03356. BGL. 1 hit.
    PROSITEi PS00572. GLYCOSYL_HYDROL_F1_1. 1 hit.
    PS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Structure and transcription analysis of the gene encoding a cellobiase from Agrobacterium sp. strain ATCC 21400."
      Wakarchuk W.W., Greenberg N.M., Kilburn D.G., Miller R.C. Jr., Warren R.A.J.
      J. Bacteriol. 170:301-307(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Unequivocal demonstration of the involvement of a glutamate residue as a nucleophile in the mechanism of a 'retaining' glycosidase."
      Withers S.G., Warren R.A.J., Street I.P., Rupitz K., Kempton J.B., Aebersold R.
      J. Am. Chem. Soc. 112:5887-5889(1990)
      Cited for: ACTIVE SITE GLU-359.

    Entry informationi

    Entry nameiBGLS_AGRSA
    AccessioniPrimary (citable) accession number: P12614
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: October 1, 1989
    Last modified: October 1, 2014
    This is version 76 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3