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Q25BW4 (BGL1B_PHACH) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 36. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 1B

EC=3.2.1.21
Alternative name(s):
Cellobiase 1B
Gene names
Name:BGL1B
OrganismPhanerochaete chrysosporium (White-rot fungus) (Sporotrichum pruinosum)
Taxonomic identifier5306 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesCorticialesCorticiaceaePhanerochaete

Protein attributes

Sequence length540 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 in cellobiose culture, but repressed in glucose culture. Ref.1

Sequence similarities

Belongs to the glycosyl hydrolase 1 family.

Biophysicochemical properties

Kinetic parameters:

KM=0.218 mM for cellobiose Ref.1 Ref.2

KM=0.619 mM for p-nitrophenyl-beta-D-glucoside (pNP-Glu)

KM=4.02 mM for p-nitrophenyl-beta-D-galactoside (pNP-Gal)

KM=1.07 mM for cellobionolactone Ref.1

pH dependence:

Optimum pH is 6.0-6.5. Ref.2

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 540540Beta-glucosidase 1B
PRO_0000390788

Regions

Region437 – 4382Substrate binding By similarity

Sites

Active site1751Proton donor By similarity UniProtKB Q25BW5
Active site3801Nucleophile By similarity UniProtKB Q25BW5
Binding site251Substrate By similarity
Binding site1281Substrate By similarity
Binding site1741Substrate By similarity
Binding site3161Substrate By similarity UniProtKB Q25BW5
Binding site4301Substrate By similarity UniProtKB Q25BW5

Sequences

Sequence LengthMass (Da)Tools
Q25BW4 [UniParc].

Last modified April 18, 2006. Version 1.
Checksum: D0B4518C9A11C071

FASTA54060,665
        10         20         30         40         50         60 
MSASAAPPNK LPADFLWGFA TASFQIEGAT DVDGRGKSIW DDFSKIPGKT LDGKNGDVAT 

        70         80         90        100        110        120 
DSYNRWREDV DLLVQYGVKS YRFSISWSRI IPLGGRNDPV NEAGIKFYSD LIDALLERGI 

       130        140        150        160        170        180 
VPFVTLYHWD LPQALHDRYL GWLNKDEIVQ DYVRYAGVCF ERFGDRVKHW LTMNEPWCIS 

       190        200        210        220        230        240 
ILGYGRGVFA PGRSSDRMRS PEGDSSTEPW IVGHSVILAH AYAVKLYREQ FKANRGGQIG 

       250        260        270        280        290        300 
ITLNGDWAMP YDDSPQNIEA AQHALDVAIG WFADPIYLGQ YPAYMKEMLG DRLPEFTPEE 

       310        320        330        340        350        360 
LAVVKGSSDF YGMNTYTTNL CKAGGEDEFQ GNVEYTFTRP DGTQLGTAAH CSWLQDYAPG 

       370        380        390        400        410        420 
FRDLLNYLYK RYRKPIYVTE NGFAVKDENS KPLEEALKDD DRVHYYQGVT DSLLAAVKED 

       430        440        450        460        470        480 
GVDVRGYFGW SLLDNFEWAD GYITRFGVTY VDYDTQKRYP KDSGKFLSQW FPAHIAESPK 

       490        500        510        520        530        540 
PAAETKKAAT PSPLKPHGAI SNGVSKKSSA TKEPKSASRK KGRKAPFARF TAYISAFLGL 

« 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.
Strain: K-3.
Tissue: Mycelium.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB253327 mRNA. Translation: BAE87009.1.

3D structure databases

ProteinModelPortalQ25BW4.
SMRQ25BW4. Positions 10-477.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5306.JGI99870.

Protein family/group databases

CAZyGH1. Glycoside Hydrolase Family 1.
mycoCLAPBGL1B_PHACH.

Proteomic databases

PRIDEQ25BW4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG2723.

Enzyme and pathway databases

BRENDA3.2.1.21. 4722.
SABIO-RKQ25BW4.

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR001360. Glyco_hydro_1.
IPR018120. Glyco_hydro_1_AS.
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.
PROSITEPS00572. GLYCOSYL_HYDROL_F1_1. 1 hit.
PS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameBGL1B_PHACH
AccessionPrimary (citable) accession number: Q25BW4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 19, 2010
Last sequence update: April 18, 2006
Last modified: October 16, 2013
This is version 36 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

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries