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Q2UPQ4 (EGLB_ASPOR) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 50. 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:
Probable endo-beta-1,4-glucanase B

Short name=Endoglucanase B
EC=3.2.1.4
Alternative name(s):
Carboxymethylcellulase B
Cellulase B
Gene names
Name:eglB
Synonyms:celE
ORF Names:AO090005001553
OrganismAspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold) [Complete proteome]
Taxonomic identifier510516 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length333 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Has endoglucanase activity on substrates containing beta-1,4 glycosidic bonds, like in carboxymethylcellulose (CMC), hydroxyethylcellulose (HEC) and beta-glucan. Involved in the degradation of complex natural cellulosic substrates By similarity.

Catalytic activity

Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.

Subcellular location

Secreted By similarity.

Sequence similarities

Belongs to the glycosyl hydrolase 5 (cellulase A) family.

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-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncellulase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Potential
Chain18 – 333316Probable endo-beta-1,4-glucanase B
PRO_0000394057

Sites

Active site1601Proton donor By similarity
Active site2671Nucleophile By similarity

Amino acid modifications

Glycosylation371N-linked (GlcNAc...) Potential
Glycosylation1001N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict1451G → E in BAD72778. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q2UPQ4 [UniParc].

Last modified January 24, 2006. Version 1.
Checksum: EA1271CB19A55C7A

FASTA33336,958
        10         20         30         40         50         60 
MKFRNLFFAA VAGSAVAAPL AKEQKKRDSV FQWIGANESG AEFGENNLPG VWGTDYIFPD 

        70         80         90        100        110        120 
VSAITTLIDK GMNIFRIQFK MERLVPDSMT GAYDEAYLQN LTTVVNAVTD AGVHAILDPH 

       130        140        150        160        170        180 
NYGRFNGEIM STPSDFQTFW KNLAGQFQSN SLVIFDTNNE YHDMDQELVL NLNQAAIDGI 

       190        200        210        220        230        240 
REAGATEQYI FVEGNSYTGA WTWTDVNDNM KNLEDPQDKI VYQMHQYLDS DGSGTSETCV 

       250        260        270        280        290        300 
SGTIGQERVT SATQWLKDNK KVGIIGEFAG GNNDQCKTAV KGMLDYLAEN TDVWKGALWW 

       310        320        330 
AAGPWWGDYM YSLEPPNGVA FTGMLDVLQA YLG 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB195229 Genomic DNA. Translation: BAD72778.1.
AP007151 Genomic DNA. Translation: BAE56461.1.
RefSeqXP_001818463.1. XM_001818411.1.

3D structure databases

ProteinModelPortalQ2UPQ4.
SMRQ2UPQ4. Positions 30-332.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5062.CADAORAP00003359.

Protein family/group databases

CAZyGH5. Glycoside Hydrolase Family 5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAORAT00003416; CADAORAP00003359; CADAORAG00003416.
GeneID5990408.
KEGGaor:AOR_1_2698174.

Phylogenomic databases

eggNOGCOG2730.
HOGENOMHOG000111120.
KOK01179.
OMAFWQNLAG.
OrthoDBEOG776T0S.

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR001547. Glyco_hydro_5.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF00150. Cellulase. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
ProtoNetSearch...

Entry information

Entry nameEGLB_ASPOR
AccessionPrimary (citable) accession number: Q2UPQ4
Secondary accession number(s): Q5TKT6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 18, 2010
Last sequence update: January 24, 2006
Last modified: November 13, 2013
This is version 50 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