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Q25BW5

- BGL1A_PHACH

UniProt

Q25BW5 - BGL1A_PHACH

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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

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
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-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

        10         20         30         40         50
MSAAKLPKSF VWGYATAAYQ IEGSPDKDGR EPSIWDTFCK APGKIADGSS
60 70 80 90 100
GDVATDSYNR WREDVQLLKS YGVKAYRFSL SWSRIIPKGG RSDPVNGAGI
110 120 130 140 150
KHYRTLIEEL VKEGITPFVT LYHWDLPQAL DDRYGGWLNK EEAIQDFTNY
160 170 180 190 200
AKLCFESFGD LVQNWITFNE PWVISVMGYG NGIFAPGHVS NTEPWIVSHH
210 220 230 240 250
IILAHAHAVK LYRDEFKEKQ GGQIGITLDS HWLIPYDDTD ASKEATLRAM
260 270 280 290 300
EFKLGRFANP IYKGEYPPRI KKILGDRLPE FTPEEIELVK GSSDFFGLNT
310 320 330 340 350
YTTHLVQDGG SDELAGFVKT GHTRADGTQL GTQSDMGWLQ TYGPGFRWLL
360 370 380 390 400
NYLWKAYDKP VYVTENGFPV KGENDLPVEQ AVDDTDRQAY YRDYTEALLQ
410 420 430 440 450
AVTEDGADVR GYFGWSLLDN FEWAEGYKVR FGVTHVDYET QKRTPKKSAE
460
FLSRWFKEHI EE
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