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Q2TX26 (CELB_ASPOR) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 48. 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:
Endo-beta-1,4-glucanase celB

Short name=Endoglucanase celB
EC=3.2.1.4
Alternative name(s):
Carboxymethylcellulase celB
Cellulase B
Gene names
Name:celB
ORF Names:AO090010000314
OrganismAspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold) [Complete proteome]
Taxonomic identifier510516 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length416 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

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. Ref.1

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 7 (cellulase C) family.

Biophysicochemical properties

pH dependence:

Optimum pH is 4.0. Stable between pH 3.0 and 7.0. Ref.1

Temperature dependence:

Optimum temperature is 45 degrees Celsius. Stable up to 50 degrees Celsius.

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

glucan catabolic process

Inferred from direct assay PubMed 18640601. Source: ASPGD

   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 – 416399Endo-beta-1,4-glucanase celB
PRO_0000395157

Sites

Active site2141Nucleophile By similarity
Active site2191Proton donor By similarity

Amino acid modifications

Glycosylation451N-linked (GlcNAc...) Potential
Glycosylation1041N-linked (GlcNAc...) Potential
Glycosylation1171N-linked (GlcNAc...) Potential
Glycosylation1351N-linked (GlcNAc...) Potential
Glycosylation2331N-linked (GlcNAc...) Potential
Glycosylation2781N-linked (GlcNAc...) Potential
Glycosylation2921N-linked (GlcNAc...) Potential
Glycosylation3821N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict481V → L in BAA22589. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q2TX26 [UniParc].

Last modified January 24, 2006. Version 1.
Checksum: 437ADE03BF84AB53

FASTA41644,448
        10         20         30         40         50         60 
MIWTLAPFVA LLPLVTAQQV GTTADAHPRL TTYKCTSQNG CTRQNTSVVL DAATHFIHKK 

        70         80         90        100        110        120 
GTQTSCTNSN GLDTAICPDK QTCADNCVVD GITDYASYGV QTKNDTLTLQ QYLQTGNATK 

       130        140        150        160        170        180 
SLSPRVYLLA EDGENYSMLK LLNQEFTFDV DASTLVCGMN GALYLSEMEA SGGKSSLNQA 

       190        200        210        220        230        240 
GAKYGTGYCD AQCYTTPWIN GEGNTESVGS CCQEMDIWEA NARATGLTPH PCNTTGLYEC 

       250        260        270        280        290        300 
SGSGCGDSGV CDKAGCGFNP YGLGAKDYYG YGLKVNTNET FTVVTQFLTN DNTTSGQLSE 

       310        320        330        340        350        360 
IRRLYIQNGQ VIQNAAVTSG GKTVDSITKD FCSGEGSAFN RLGGLEEMGH ALGRGMVLAL 

       370        380        390        400        410 
SIWNDAGSFM QWLDGGSAGP CNATEGNPAL IEKLYPDTHV KFSKIRWGDI GSTYRH 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D83732 Genomic DNA. Translation: BAA22589.1.
AP007175 Genomic DNA. Translation: BAE66197.1.
RefSeqXP_001827330.1. XM_001827278.1.

3D structure databases

ProteinModelPortalQ2TX26.
SMRQ2TX26. Positions 18-413.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5062.CADAORAP00004325.

Protein family/group databases

CAZyGH7. Glycoside Hydrolase Family 7.
mycoCLAPEGL7B_ASPOR.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAORAT00004400; CADAORAP00004325; CADAORAG00004400.
GeneID5999464.
KEGGaor:AOR_1_514024.

Phylogenomic databases

eggNOGNOG138370.
HOGENOMHOG000182210.
OMAEGHADDI.
OrthoDBEOG7Q8CXJ.

Family and domain databases

Gene3D2.70.100.10. 1 hit.
InterProIPR008985. ConA-like_lec_gl_sf.
IPR001722. Glyco_hydro_7.
[Graphical view]
PfamPF00840. Glyco_hydro_7. 1 hit.
[Graphical view]
PRINTSPR00734. GLHYDRLASE7.
SUPFAMSSF49899. SSF49899. 1 hit.
ProtoNetSearch...

Entry information

Entry nameCELB_ASPOR
AccessionPrimary (citable) accession number: Q2TX26
Secondary accession number(s): O13455
Entry history
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: January 24, 2006
Last modified: November 13, 2013
This is version 48 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