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Q25BW5 (BGL1A_PHACH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 37. 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 1A

EC=3.2.1.21
Alternative name(s):
Cellobiase 1A
Gene names
Name:BGL1A
OrganismPhanerochaete chrysosporium (White-rot fungus) (Sporotrichum pruinosum)
Taxonomic identifier5306 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesCorticialesCorticiaceaePhanerochaete

Protein attributes

Sequence length462 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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

Induction

Expressed constitutively in cellobiose and glucose cultures. Ref.1

Sequence similarities

Belongs to the glycosyl hydrolase 1 family.

Biophysicochemical properties

Kinetic parameters:

KM=6.80 mM for cellobiose Ref.1 Ref.2

KM=0.229 mM for p-nitrophenyl-beta-D-glucoside (pNP-Glu)

KM=10.2 mM for p-nitrophenyl-beta-D-galactoside (pNP-Gal)

KM=0.752 mM for p-nitrophenyl-beta-D-xyloside (pNP-Xyl)

pH dependence:

Optimum pH is 6.0-6.5. Ref.2

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 462462Beta-glucosidase 1A
PRO_0000390787

Regions

Region422 – 4232Substrate binding

Sites

Active site1701Proton donor Ref.3
Active site3651Nucleophile Ref.3
Binding site201Substrate
Binding site1231Substrate
Binding site1691Substrate
Binding site3011Substrate Ref.3
Binding site4151Substrate Ref.3

Experimental info

Mutagenesis1731V → C: 2-fold decrease in affinity for cellobiose. Ref.2
Mutagenesis1771M → L: Small decrease in affinity for cellobiose. Ref.2
Mutagenesis2291D → 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. Ref.2
Mutagenesis2311H → D: 3-fold decrease in affinity for cellobiose. Ref.2
Mutagenesis2531K → A: 7-fold decrease in affinity for cellobiose. No effect on optimum pH; when associated with N-229. Ref.2

Secondary structure

................................................................................... 462
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q25BW5 [UniParc].

Last modified April 18, 2006. Version 1.
Checksum: 25C864094A8F5007

FASTA46252,599
        10         20         30         40         50         60 
MSAAKLPKSF VWGYATAAYQ IEGSPDKDGR EPSIWDTFCK APGKIADGSS GDVATDSYNR 

        70         80         90        100        110        120 
WREDVQLLKS YGVKAYRFSL SWSRIIPKGG RSDPVNGAGI KHYRTLIEEL VKEGITPFVT 

       130        140        150        160        170        180 
LYHWDLPQAL DDRYGGWLNK EEAIQDFTNY AKLCFESFGD LVQNWITFNE PWVISVMGYG 

       190        200        210        220        230        240 
NGIFAPGHVS NTEPWIVSHH IILAHAHAVK LYRDEFKEKQ GGQIGITLDS HWLIPYDDTD 

       250        260        270        280        290        300 
ASKEATLRAM EFKLGRFANP IYKGEYPPRI KKILGDRLPE FTPEEIELVK GSSDFFGLNT 

       310        320        330        340        350        360 
YTTHLVQDGG SDELAGFVKT GHTRADGTQL GTQSDMGWLQ TYGPGFRWLL NYLWKAYDKP 

       370        380        390        400        410        420 
VYVTENGFPV KGENDLPVEQ AVDDTDRQAY YRDYTEALLQ AVTEDGADVR GYFGWSLLDN 

       430        440        450        460 
FEWAEGYKVR FGVTHVDYET QKRTPKKSAE FLSRWFKEHI EE 

« Hide

References

[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-3.
Tissue: Mycelium.
[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-3.
Tissue: Mycelium.
[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-3.
Tissue: Mycelium.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB253326 mRNA. Translation: BAE87008.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2E3ZX-ray1.50A/B1-462[»]
2E40X-ray1.90A/B1-462[»]
ProteinModelPortalQ25BW5.
SMRQ25BW5. Positions 3-462.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH1. Glycoside Hydrolase Family 1.
mycoCLAPBGL1A_PHACH.

Proteomic databases

PRIDEQ25BW5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BRENDA3.2.1.21. 4722.
SABIO-RKQ25BW5.

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR001360. 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]
PANTHERPTHR10353. PTHR10353. 1 hit.
PfamPF00232. Glyco_hydro_1. 1 hit.
[Graphical view]
PRINTSPR00131. GLHYDRLASE1.
SUPFAMSSF51445. SSF51445. 1 hit.
TIGRFAMsTIGR03356. BGL. 1 hit.
PROSITEPS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ25BW5.

Entry information

Entry nameBGL1A_PHACH
AccessionPrimary (citable) accession number: Q25BW5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 19, 2010
Last sequence update: April 18, 2006
Last modified: April 16, 2014
This is version 37 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries