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B0Y8M8 (BGLJ_ASPFC) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 34. 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:
Probable beta-glucosidase J

EC=3.2.1.21
Alternative name(s):
Beta-D-glucoside glucohydrolase J
Cellobiase J
Gentiobiase J
Gene names
Name:bglJ
ORF Names:AFUB_077900
OrganismNeosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus fumigatus) [Complete proteome]
Taxonomic identifier451804 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length865 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Beta-glucosidases are one of a number of cellulolytic enzymes involved in the degradation of cellulosic biomass. Catalyzes the last step releasing glucose from the inhibitory cellobiose By similarity.

Catalytic activity

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

Pathway

Glycan metabolism; cellulose degradation.

Subcellular location

Secreted By similarity.

Sequence similarities

Belongs to the glycosyl hydrolase 3 family.

Contains 1 PA14 domain.

Sequence caution

The sequence EDP49759.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cellulose degradation
Polysaccharide degradation
   Cellular componentSecreted
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processcellulose catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionbeta-glucosidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 865865Probable beta-glucosidase J
PRO_0000394892

Regions

Domain415 – 548134PA14

Sites

Active site2331 By similarity

Amino acid modifications

Glycosylation3301N-linked (GlcNAc...) Potential
Glycosylation4471N-linked (GlcNAc...) Potential
Glycosylation5031N-linked (GlcNAc...) Potential
Glycosylation7641N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
B0Y8M8 [UniParc].

Last modified June 15, 2010. Version 2.
Checksum: 2F9E9C76E9BDAA20

FASTA86593,022
        10         20         30         40         50         60 
MGSIDTVGMG QRAIDQIISE LSLNEKVALL SGVDAWHTFA IPRLGIPSIR TTDGPNGARG 

        70         80         90        100        110        120 
TRYFNGVPSA CLPCGTALGA TFDRDLIFSL GQLLAAECRA KGAHVLLGPT INIQRGPLGG 

       130        140        150        160        170        180 
RGFESFSEDP VLSGLAAASY CSGVQDGGVV PTLKHLVCND QEHERVAVSA LVTPRALREI 

       190        200        210        220        230        240 
YLLPFQLAIQ GARPGAVMTS YNKVNGLHAS ENPGLIRDIL RGEWGYEGAV ISDWFGTYSV 

       250        260        270        280        290        300 
ADAVNAGLDL EMPGPTRFRG PALMHALTSN KVSEKTLNER VRKVLELVQL ASRAGVPEYA 

       310        320        330        340        350        360 
PERKLNRPED RALLRRAAGE SVVLLKNDKN DSTNSPILPL DREKTTLVIG PNADLAAYCG 

       370        380        390        400        410        420 
GGSASLLAYY TVTPRQGIAD KCGAEQVVFS QGCYGHKELP LLGEHLRTIE TGQPGYTFRV 

       430        440        450        460        470        480 
YTEPPPASGS FKGSDSRTPV DELHMTNSSA FLMDYSHPQI SGDTYYATLE GTFEPPESGV 

       490        500        510        520        530        540 
YEFGLTVAGT GLLYIDGVLV VDNKTVQRAG TSFFGIGTVE ERGERYLEAG KKHHVFVEFG 

       550        560        570        580        590        600 
TAPTSNLQHH HGVVSFGPGG LRLGGCRKLD TDTAIQQAVQ SAAQADQVVV CVGLSGDWES 

       610        620        630        640        650        660 
EGFDRPHMDL PPGTEELVNA VLAVQPNAVI VVQSGTPVTM PWADKAKALL QAWYGGNEAG 

       670        680        690        700        710        720 
NGIADVLFGD VNPSAKLPLT FPRELSQNPS YLSYRSERGR VLYSEDIYVG YRYYDTTGQP 

       730        740        750        760        770        780 
PLFRFGHGLS YSTFHLRDLT VRETAPYAAN IKESSLRVSV TVSNTSARPG AEVVLVYVRP 

       790        800        810        820        830        840 
PAAACSVGRP VRELKGYEKV MLQPGETREV SITIPLGLAT SFWDEGCDAW LSEKGLYFVE 

       850        860 
AVGTGEGNTL VAPLTVQVSR VWNGL 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DS499599 Genomic DNA. Translation: EDP49759.1. Sequence problems.

3D structure databases

ProteinModelPortalB0Y8M8.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOGENOMHOG000031215.
OrthoDBEOG7H799Q.
PhylomeDBB0Y8M8.

Enzyme and pathway databases

UniPathwayUPA00696.

Family and domain databases

Gene3D3.20.20.300. 1 hit.
3.40.50.1700. 2 hits.
InterProIPR026891. Fn3-like.
IPR026892. Glyco_hydro_3.
IPR002772. Glyco_hydro_3_C.
IPR001764. Glyco_hydro_3_N.
IPR017853. Glycoside_hydrolase_SF.
IPR011658. PA14.
[Graphical view]
PANTHERPTHR30620. PTHR30620. 1 hit.
PfamPF14310. Fn3-like. 1 hit.
PF00933. Glyco_hydro_3. 1 hit.
PF01915. Glyco_hydro_3_C. 1 hit.
PF07691. PA14. 1 hit.
[Graphical view]
PRINTSPR00133. GLHYDRLASE3.
SMARTSM00758. PA14. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
SSF52279. SSF52279. 2 hits.
ProtoNetSearch...

Entry information

Entry nameBGLJ_ASPFC
AccessionPrimary (citable) accession number: B0Y8M8
Entry history
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: June 15, 2010
Last modified: April 16, 2014
This is version 34 of the entry and version 2 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries