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A2QPK4 (BGLD_ASPNC) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 39. 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 D

EC=3.2.1.21
Alternative name(s):
Beta-D-glucoside glucohydrolase D
Cellobiase D
Gentiobiase D
Gene names
Name:bglD
ORF Names:An07g09760
OrganismAspergillus niger (strain CBS 513.88 / FGSC A1513) [Complete proteome]
Taxonomic identifier425011 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length754 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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.

Sequence caution

The sequence CAK39741.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cellulose degradation
Polysaccharide degradation
   Cellular componentSecreted
   DomainSignal
   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

Signal peptide1 – 2020 Potential
Chain21 – 754734Probable beta-glucosidase D
PRO_5000220231

Sites

Active site2671 By similarity

Amino acid modifications

Glycosylation661N-linked (GlcNAc...) Potential
Glycosylation691N-linked (GlcNAc...) Potential
Glycosylation1861N-linked (GlcNAc...) Potential
Glycosylation2391N-linked (GlcNAc...) Potential
Glycosylation3011N-linked (GlcNAc...) Potential
Glycosylation3451N-linked (GlcNAc...) Potential
Glycosylation4431N-linked (GlcNAc...) Potential
Glycosylation5121N-linked (GlcNAc...) Potential
Glycosylation5341N-linked (GlcNAc...) Potential
Glycosylation5731N-linked (GlcNAc...) Potential
Glycosylation5881N-linked (GlcNAc...) Potential
Glycosylation6551N-linked (GlcNAc...) Potential
Glycosylation7451N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
A2QPK4 [UniParc].

Last modified May 18, 2010. Version 2.
Checksum: 6D106BFA5464A759

FASTA75480,738
        10         20         30         40         50         60 
MKVLSFIVAA ALLGLTGASS NSSPGLLKSD GVVLGDWESA YQKASSFVAG LTTDQKLALI 

        70         80         90        100        110        120 
TGSSVNSTNG SFSGLTFLDG DMGLQNFFYV SAFSLSSALA MTWDRDAIYA QAKAVGSEFY 

       130        140        150        160        170        180 
NKGIQVVAGP TSQPLGRTPW GGRIVEGFGP DPYLNGLASG LTAKGYIDAG VIPGAKHFLL 

       190        200        210        220        230        240 
YEQETNRTGG GGGGGGDSGS APYSSNADDK TLHETYLWPF YDAVKHGLGA VMCAMTKVNG 

       250        260        270        280        290        300 
TLSCQNSDLL MKHLKTELGF PGLVWPDTNG QSSALESAVN GEDYGSSSIW STSTMETLLS 

       310        320        330        340        350        360 
NGSLSEARLD DMAVRNLMGY YYVNLDNGLQ PEEQSEDAYV DVRGNHSKLI RENGAKSMAL 

       370        380        390        400        410        420 
LKNKNALPLR KPRVMSVFGA HAGPVLGGPN TAMDIEGSGP TYQGHLATGT GSAQASLPYL 

       430        440        450        460        470        480 
VPPYVALTNR IIEDGTMMRW VLNDTYSSSS TSGLITEGTD STAVDPSFAD YATNSDACLV 

       490        500        510        520        530        540 
FLNALSGEGA DRTELYNDDQ DTMVNTVADN CNNTIVIINT VGPRLMDQWI EHDNVTAVLY 

       550        560        570        580        590        600 
GSLLGQESGN SIVDILYGDV NPSGRLIHTI AKNESDYNVK ICYTAQCNFT EGVYLDYRYF 

       610        620        630        640        650        660 
DAHNVTPRYP FGHGLSYTTF SYSDLNIEKP STLSKYPTGE KAVGGNSDLW DIVGNVSVKV 

       670        680        690        700        710        720 
ANTGSLDGAE VPQLYLGFPT AAQQPVRQLR GFERVEIASG KQSQVTFQLR RRDISYWDVP 

       730        740        750 
AQQWLVASGD YKVYVGASSR DLKLNGTFTV QTSS 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM270153 Genomic DNA. Translation: CAK39741.1. Sequence problems.

3D structure databases

ProteinModelPortalA2QPK4.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH3. Glycoside Hydrolase Family 3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG1472.
HOGENOMHOG000031215.
OrthoDBEOG7XH6ZD.

Enzyme and pathway databases

UniPathwayUPA00696.

Family and domain databases

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

Entry information

Entry nameBGLD_ASPNC
AccessionPrimary (citable) accession number: A2QPK4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 18, 2010
Last sequence update: May 18, 2010
Last modified: February 19, 2014
This is version 39 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