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Q25BW4

- BGL1B_PHACH

UniProt

Q25BW4 - BGL1B_PHACH

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Protein

Beta-glucosidase 1B

Gene
BGL1B
Organism
Phanerochaete chrysosporium (White-rot fungus) (Sporotrichum pruinosum)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

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=0.218 mM for cellobiose2 Publications
  2. KM=0.619 mM for p-nitrophenyl-beta-D-glucoside (pNP-Glu)
  3. KM=4.02 mM for p-nitrophenyl-beta-D-galactoside (pNP-Gal)
  4. KM=1.07 mM for cellobionolactone1 Publication

pH dependencei

Optimum pH is 6.0-6.5.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei25 – 251Substrate By similarity
Binding sitei128 – 1281Substrate By similarity
Binding sitei174 – 1741Substrate By similarity
Active sitei175 – 1751Proton donor By similarityBy similarity
Binding sitei316 – 3161Substrate By similarityBy similarity
Active sitei380 – 3801Nucleophile By similarityBy similarity
Binding sitei430 – 4301Substrate By similarityBy similarity

GO - Molecular functioni

  1. cellobiose glucosidase activity Source: UniProtKB

GO - Biological processi

  1. cellulose catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

Enzyme and pathway databases

BRENDAi3.2.1.21. 4722.
SABIO-RKQ25BW4.

Protein family/group databases

CAZyiGH1. Glycoside Hydrolase Family 1.
mycoCLAPiBGL1B_PHACH.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-glucosidase 1B (EC:3.2.1.21)
Alternative name(s):
Cellobiase 1B
Gene namesi
Name:BGL1B
OrganismiPhanerochaete chrysosporium (White-rot fungus) (Sporotrichum pruinosum)
Taxonomic identifieri5306 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesCorticialesCorticiaceaePhanerochaete

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 540540Beta-glucosidase 1BPRO_0000390788Add
BLAST

Proteomic databases

PRIDEiQ25BW4.

Expressioni

Inductioni

Expressed in cellobiose culture, but repressed in glucose culture.1 Publication

Interactioni

Protein-protein interaction databases

STRINGi5306.JGI99870.

Structurei

3D structure databases

ProteinModelPortaliQ25BW4.
SMRiQ25BW4. Positions 10-477.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni437 – 4382Substrate binding By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG2723.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001360. Glyco_hydro_1.
IPR018120. Glyco_hydro_1_AS.
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.
PROSITEiPS00572. GLYCOSYL_HYDROL_F1_1. 1 hit.
PS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q25BW4-1 [UniParc]FASTAAdd to Basket

« Hide

MSASAAPPNK LPADFLWGFA TASFQIEGAT DVDGRGKSIW DDFSKIPGKT    50
LDGKNGDVAT DSYNRWREDV DLLVQYGVKS YRFSISWSRI IPLGGRNDPV 100
NEAGIKFYSD LIDALLERGI VPFVTLYHWD LPQALHDRYL GWLNKDEIVQ 150
DYVRYAGVCF ERFGDRVKHW LTMNEPWCIS ILGYGRGVFA PGRSSDRMRS 200
PEGDSSTEPW IVGHSVILAH AYAVKLYREQ FKANRGGQIG ITLNGDWAMP 250
YDDSPQNIEA AQHALDVAIG WFADPIYLGQ YPAYMKEMLG DRLPEFTPEE 300
LAVVKGSSDF YGMNTYTTNL CKAGGEDEFQ GNVEYTFTRP DGTQLGTAAH 350
CSWLQDYAPG FRDLLNYLYK RYRKPIYVTE NGFAVKDENS KPLEEALKDD 400
DRVHYYQGVT DSLLAAVKED GVDVRGYFGW SLLDNFEWAD GYITRFGVTY 450
VDYDTQKRYP KDSGKFLSQW FPAHIAESPK PAAETKKAAT PSPLKPHGAI 500
SNGVSKKSSA TKEPKSASRK KGRKAPFARF TAYISAFLGL 540
Length:540
Mass (Da):60,665
Last modified:April 18, 2006 - v1
Checksum:iD0B4518C9A11C071
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB253327 mRNA. Translation: BAE87009.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB253327 mRNA. Translation: BAE87009.1 .

3D structure databases

ProteinModelPortali Q25BW4.
SMRi Q25BW4. Positions 10-477.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 5306.JGI99870.

Protein family/group databases

CAZyi GH1. Glycoside Hydrolase Family 1.
mycoCLAPi BGL1B_PHACH.

Proteomic databases

PRIDEi Q25BW4.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi COG2723.

Enzyme and pathway databases

BRENDAi 3.2.1.21. 4722.
SABIO-RK Q25BW4.

Family and domain databases

Gene3Di 3.20.20.80. 1 hit.
InterProi IPR001360. Glyco_hydro_1.
IPR018120. Glyco_hydro_1_AS.
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.
PROSITEi PS00572. GLYCOSYL_HYDROL_F1_1. 1 hit.
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-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.

Entry informationi

Entry nameiBGL1B_PHACH
AccessioniPrimary (citable) accession number: Q25BW4
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal 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

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