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P22073

- BGLA_PAEPO

UniProt

P22073 - BGLA_PAEPO

Protein

Beta-glucosidase A

Gene

bglA

Organism
Paenibacillus polymyxa (Bacillus polymyxa)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 88 (01 Oct 2014)
      Sequence version 1 (01 Aug 1991)
      Previous versions | rss
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    Functioni

    BglA is intracellular and cleaves cellobiose probably through inorganic phosphate mediated hydrolysis.

    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 sitei166 – 1661Proton donorSequence Analysis
    Active sitei352 – 3521NucleophilePROSITE-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

    Protein family/group databases

    CAZyiGH1. Glycoside Hydrolase Family 1.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-glucosidase A (EC:3.2.1.21)
    Short name:
    BGA
    Alternative name(s):
    Amygdalase
    Beta-D-glucoside glucohydrolase
    Cellobiase
    Gentiobiase
    Gene namesi
    Name:bglA
    OrganismiPaenibacillus polymyxa (Bacillus polymyxa)
    Taxonomic identifieri1406 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesPaenibacillaceaePaenibacillus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 448448Beta-glucosidase APRO_0000063871Add
    BLAST

    Interactioni

    Subunit structurei

    Homooctamer.

    Structurei

    Secondary structure

    1
    448
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 53
    Beta strandi11 – 155
    Helixi18 – 214
    Helixi27 – 293
    Helixi34 – 396
    Turni42 – 443
    Helixi46 – 483
    Beta strandi51 – 533
    Helixi54 – 563
    Helixi57 – 7115
    Beta strandi74 – 796
    Helixi82 – 854
    Beta strandi89 – 913
    Helixi95 – 11016
    Beta strandi114 – 1229
    Helixi126 – 1305
    Turni131 – 1344
    Helixi138 – 15316
    Helixi155 – 1573
    Beta strandi160 – 1656
    Helixi167 – 1759
    Helixi187 – 21125
    Beta strandi214 – 2207
    Beta strandi226 – 2316
    Helixi233 – 24614
    Helixi248 – 2569
    Helixi261 – 2699
    Helixi280 – 2845
    Beta strandi289 – 2946
    Beta strandi299 – 3035
    Turni308 – 3114
    Beta strandi312 – 3143
    Helixi331 – 3399
    Helixi340 – 3434
    Beta strandi348 – 3536
    Helixi369 – 38719
    Beta strandi392 – 3987
    Helixi406 – 4116
    Beta strandi416 – 4194
    Turni421 – 4233
    Beta strandi426 – 4283
    Helixi430 – 44112
    Beta strandi443 – 4453

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BGAX-ray2.40A/B/C/D2-448[»]
    1BGGX-ray2.30A/B/C/D1-448[»]
    1E4IX-ray2.00A2-448[»]
    1TR1X-ray2.20A/B/C/D2-448[»]
    1UYQX-ray2.20A2-448[»]
    ProteinModelPortaliP22073.
    SMRiP22073. Positions 2-448.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP22073.

    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.

    P22073-1 [UniParc]FASTAAdd to Basket

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    MTIFQFPQDF MWGTATAAYQ IEGAYQEDGR GLSIWDTFAH TPGKVFNGDN    50
    GNVACDSYHR YEEDIRLMKE LGIRTYRFSV SWPRIFPNGD GEVNQEGLDY 100
    YHRVVDLLND NGIEPFCTLY HWDLPQALQD AGGWGNRRTI QAFVQFAETM 150
    FREFHGKIQH WLTFNEPWCI AFLSNMLGVH APGLTNLQTA IDVGHHLLVA 200
    HGLSVRRFRE LGTSGQIGIA PNVSWAVPYS TSEEDKAACA RTISLHSDWF 250
    LQPIYQGSYP QFLVDWFAEQ GATVPIQDGD MDIIGEPIDM IGINYYSMSV 300
    NRFNPEAGFL QSEEINMGLP VTDIGWPVES RGLYEVLHYL QKYGNIDIYI 350
    TENGACINDE VVNGKVQDDR RISYMQQHLV QVHRTIHDGL HVKGYMAWSL 400
    LDNFEWAEGY NMRFGMIHVD FRTQVRTPKE SYYWYRNVVS NNWLETRR 448
    Length:448
    Mass (Da):51,649
    Last modified:August 1, 1991 - v1
    Checksum:iD971D2E61B6627C1
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M60210 Genomic DNA. Translation: AAA22263.1.
    PIRiJW0037.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M60210 Genomic DNA. Translation: AAA22263.1 .
    PIRi JW0037.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BGA X-ray 2.40 A/B/C/D 2-448 [» ]
    1BGG X-ray 2.30 A/B/C/D 1-448 [» ]
    1E4I X-ray 2.00 A 2-448 [» ]
    1TR1 X-ray 2.20 A/B/C/D 2-448 [» ]
    1UYQ X-ray 2.20 A 2-448 [» ]
    ProteinModelPortali P22073.
    SMRi P22073. Positions 2-448.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH1. Glycoside Hydrolase Family 1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P22073.

    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. "Sequences and homology analysis of two genes encoding beta-glucosidases from Bacillus polymyxa."
      Gonzalez-Candelas L., Ramon D., Polaina J.
      Gene 95:31-38(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Crystal structure of beta-glucosidase A from Bacillus polymyxa: insights into the catalytic activity in family 1 glycosyl hydrolases."
      Sanz-Aparicio J., Hermoso J.A., Martinez-Ripoll M., Lequerica J.L., Polaina J.
      J. Mol. Biol. 275:491-502(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
      Strain: ATCC 842 / DSM 36 / JCM 2507 / NBRC 15309 / NCIMB 8158 / NCTC 10343 / NRRL B-4317 / VKM B-514.

    Entry informationi

    Entry nameiBGLA_PAEPO
    AccessioniPrimary (citable) accession number: P22073
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1991
    Last sequence update: August 1, 1991
    Last modified: October 1, 2014
    This is version 88 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3