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Q25BW5

- BGL1A_PHACH

UniProt

Q25BW5 - BGL1A_PHACH

Protein

Beta-glucosidase 1A

Gene

BGL1A

Organism
Phanerochaete chrysosporium (White-rot fungus) (Sporotrichum pruinosum)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 38 (01 Oct 2014)
      Sequence version 1 (18 Apr 2006)
      Previous versions | rss
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    Functioni

    Plays an important role in cellulose degradation. Shows hydrolytic activity against several glycosidic compounds.1 Publication

    Catalytic activityi

    Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.1 Publication

    Kineticsi

    1. KM=6.80 mM for cellobiose2 Publications
    2. KM=0.229 mM for p-nitrophenyl-beta-D-glucoside (pNP-Glu)2 Publications
    3. KM=10.2 mM for p-nitrophenyl-beta-D-galactoside (pNP-Gal)2 Publications
    4. KM=0.752 mM for p-nitrophenyl-beta-D-xyloside (pNP-Xyl)2 Publications

    pH dependencei

    Optimum pH is 6.0-6.5.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei20 – 201Substrate1 Publication
    Binding sitei123 – 1231Substrate1 Publication
    Binding sitei169 – 1691Substrate1 Publication
    Active sitei170 – 1701Proton donor1 Publication
    Binding sitei301 – 3011Substrate1 Publication
    Active sitei365 – 3651Nucleophile1 Publication
    Binding sitei415 – 4151Substrate1 Publication

    GO - Molecular functioni

    1. beta-glucosidase activity Source: UniProtKB
    2. cellobiose glucosidase activity Source: UniProtKB

    GO - Biological processi

    1. cellulose catabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

    Enzyme and pathway databases

    BRENDAi3.2.1.21. 4722.
    SABIO-RKQ25BW5.

    Protein family/group databases

    CAZyiGH1. Glycoside Hydrolase Family 1.
    mycoCLAPiBGL1A_PHACH.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-glucosidase 1AImported1 Publication (EC:3.2.1.21)
    Alternative name(s):
    Cellobiase 1A1 Publication
    Gene namesi
    Name:BGL1AImported
    OrganismiPhanerochaete chrysosporium (White-rot fungus) (Sporotrichum pruinosum)
    Taxonomic identifieri5306 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesCorticialesCorticiaceaePhanerochaete

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi173 – 1731V → C: 2-fold decrease in affinity for cellobiose. 1 Publication
    Mutagenesisi177 – 1771M → L: Small decrease in affinity for cellobiose. 1 Publication
    Mutagenesisi229 – 2291D → N: 17-fold decrease in affinity for cellobiose and displays more acidic optimum pH than wild-type. No effect on optimum pH; when associated with A-253. 1 Publication
    Mutagenesisi231 – 2311H → D: 3-fold decrease in affinity for cellobiose. 1 Publication
    Mutagenesisi253 – 2531K → A: 7-fold decrease in affinity for cellobiose. No effect on optimum pH; when associated with N-229. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 462462Beta-glucosidase 1APRO_0000390787Add
    BLAST

    Proteomic databases

    PRIDEiQ25BW5.

    Expressioni

    Inductioni

    Expressed constitutively in cellobiose and glucose cultures.1 Publication

    Structurei

    Secondary structure

    1
    462
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi11 – 155
    Helixi18 – 214
    Helixi27 – 293
    Helixi34 – 385
    Beta strandi51 – 533
    Turni57 – 604
    Helixi61 – 7010
    Beta strandi74 – 796
    Helixi82 – 854
    Helixi97 – 11317
    Beta strandi116 – 1249
    Helixi128 – 1347
    Helixi136 – 1383
    Helixi140 – 15819
    Turni159 – 1613
    Beta strandi164 – 1696
    Helixi171 – 1799
    Helixi193 – 21523
    Helixi217 – 2204
    Beta strandi223 – 2297
    Beta strandi232 – 2398
    Helixi240 – 25314
    Helixi255 – 2639
    Helixi268 – 2747
    Helixi275 – 2773
    Helixi283 – 2897
    Beta strandi294 – 2996
    Beta strandi303 – 3086
    Helixi313 – 3153
    Beta strandi317 – 3237
    Beta strandi329 – 3313
    Beta strandi333 – 3364
    Helixi343 – 35715
    Beta strandi361 – 3666
    Helixi373 – 3753
    Helixi378 – 3814
    Helixi385 – 40319
    Beta strandi409 – 4157
    Helixi423 – 4253
    Beta strandi433 – 4364
    Turni438 – 4403
    Beta strandi443 – 4453
    Helixi447 – 45913

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2E3ZX-ray1.50A/B1-462[»]
    2E40X-ray1.90A/B1-462[»]
    ProteinModelPortaliQ25BW5.
    SMRiQ25BW5. Positions 3-462.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ25BW5.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni422 – 4232Substrate binding

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 1 family.Sequence Analysis

    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.
    PROSITEiPS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q25BW5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSAAKLPKSF VWGYATAAYQ IEGSPDKDGR EPSIWDTFCK APGKIADGSS    50
    GDVATDSYNR WREDVQLLKS YGVKAYRFSL SWSRIIPKGG RSDPVNGAGI 100
    KHYRTLIEEL VKEGITPFVT LYHWDLPQAL DDRYGGWLNK EEAIQDFTNY 150
    AKLCFESFGD LVQNWITFNE PWVISVMGYG NGIFAPGHVS NTEPWIVSHH 200
    IILAHAHAVK LYRDEFKEKQ GGQIGITLDS HWLIPYDDTD ASKEATLRAM 250
    EFKLGRFANP IYKGEYPPRI KKILGDRLPE FTPEEIELVK GSSDFFGLNT 300
    YTTHLVQDGG SDELAGFVKT GHTRADGTQL GTQSDMGWLQ TYGPGFRWLL 350
    NYLWKAYDKP VYVTENGFPV KGENDLPVEQ AVDDTDRQAY YRDYTEALLQ 400
    AVTEDGADVR GYFGWSLLDN FEWAEGYKVR FGVTHVDYET QKRTPKKSAE 450
    FLSRWFKEHI EE 462
    Length:462
    Mass (Da):52,599
    Last modified:April 18, 2006 - v1
    Checksum:i25C864094A8F5007
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB253326 mRNA. Translation: BAE87008.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB253326 mRNA. Translation: BAE87008.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2E3Z X-ray 1.50 A/B 1-462 [» ]
    2E40 X-ray 1.90 A/B 1-462 [» ]
    ProteinModelPortali Q25BW5.
    SMRi Q25BW5. Positions 3-462.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH1. Glycoside Hydrolase Family 1.
    mycoCLAPi BGL1A_PHACH.

    Proteomic databases

    PRIDEi Q25BW5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    BRENDAi 3.2.1.21. 4722.
    SABIO-RK Q25BW5.

    Miscellaneous databases

    EvolutionaryTracei Q25BW5.

    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 PS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and characterization of two intracellular beta-glucosidases belonging to glycoside hydrolase family 1 from the basidiomycete Phanerochaete chrysosporium."
      Tsukada T., Igarashi K., Yoshida M., Samejima M.
      Appl. Microbiol. Biotechnol. 73:807-814(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION.
      Strain: K-3Imported.
      Tissue: Mycelium1 Publication.
    2. "Role of subsite +1 residues in pH dependence and catalytic activity of the glycoside hydrolase family 1 beta-glucosidase BGL1A from the basidiomycete Phanerochaete chrysosporium."
      Tsukada T., Igarashi K., Fushinobu S., Samejima M.
      Biotechnol. Bioeng. 99:1295-1302(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF VAL-173; MET-177; ASP-229; HIS-231 AND LYS-253.
      Strain: K-31 Publication.
      Tissue: Mycelium1 Publication.
    3. "Crystal structure of intracellular family 1 beta-glucosidase BGL1A from the basidiomycete Phanerochaete chrysosporium."
      Nijikken Y., Tsukada T., Igarashi K., Samejima M., Wakagi T., Shoun H., Fushinobu S.
      FEBS Lett. 581:1514-1520(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH SUBSTRATE.
      Strain: K-31 Publication.
      Tissue: Mycelium1 Publication.

    Entry informationi

    Entry nameiBGL1A_PHACH
    AccessioniPrimary (citable) accession number: Q25BW5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 19, 2010
    Last sequence update: April 18, 2006
    Last modified: October 1, 2014
    This is version 38 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal 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