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O74706 (EGLB_ASPNG) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 69. 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 B

Short name=Endoglucanase B
EC=3.2.1.4
Alternative name(s):
Carboxymethylcellulase B
Cellulase B
Gene names
Name:eglB
Synonyms:eng1
OrganismAspergillus niger
Taxonomic identifier5061 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length331 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.2

Catalytic activity

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

Subcellular location

Secreted By similarity.

Induction

Expression is under the control of the xylanolytic transcriptional activator xlnR. Ref.1

Sequence similarities

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

Biophysicochemical properties

pH dependence:

Optimum pH is 6.0. Ref.2

Temperature dependence:

Optimum temperature is 70 degrees Celsius.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cellulose degradation
Polysaccharide degradation
   Cellular componentSecreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
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 – 1818 Potential
Chain19 – 331313Endo-beta-1,4-glucanase B
PRO_5000065052

Sites

Active site1601Proton donor By similarity
Active site2661Nucleophile By similarity

Amino acid modifications

Glycosylation381N-linked (GlcNAc...) Potential
Glycosylation1001N-linked (GlcNAc...) Potential
Glycosylation2111N-linked (GlcNAc...) Potential
Glycosylation2881N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict131A → G in AAG50051. Ref.2
Sequence conflict231S → P in AAG50051. Ref.2
Sequence conflict631T → A in AAG50051. Ref.2
Sequence conflict691G → D in AAG50051. Ref.2
Sequence conflict1051V → I in AAG50051. Ref.2
Sequence conflict1171I → V in AAG50051. Ref.2
Sequence conflict1411Q → E in AAG50051. Ref.2
Sequence conflict1621Y → H in AAG50051. Ref.2
Sequence conflict1851A → AT in AAG50051. Ref.2
Sequence conflict2411G → E in AAG50051. Ref.2
Sequence conflict248 – 2503ITD → VTE in AAG50051. Ref.2
Sequence conflict3291T → A in AAG50051. Ref.2

Sequences

Sequence LengthMass (Da)Tools
O74706 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: F3AE4BF70007C707

FASTA33136,559
        10         20         30         40         50         60 
MKFQSTLLLA AAAGSALAVP HGSGHKKRAS VFEWFGSNES GAEFGTNIPG VWGTDYIFPD 

        70         80         90        100        110        120 
PSTISTLIGK GMNFFRVQFM MERLLPDSMT GSYDEEYLAN LTTVVKAVTD GGAHALIDPH 

       130        140        150        160        170        180 
NYGRYNGEII SSTSDFQTFW QNLAGQYKDN DLVMFDTNNE YYDMDQDLVL NLNQAAINGI 

       190        200        210        220        230        240 
RAAGASQYIF VEGNSWTGAW TWVDVNDNMK NLTDPEDKIV YEMHQYLDSD GSGTSETCVS 

       250        260        270        280        290        300 
GTIGKERITD ATQWLKDNKK VGFIGEYAGG SNDVCRSAVS GMLEYMANNT DVWKGASWWA 

       310        320        330 
AGPWWGDYIF SLEPPDGTAY TGMLDILETY L 

« Hide

References

[1]"The transcriptional activator XlnR regulates both xylanolytic and endoglucanase gene expression in Aspergillus niger."
van Peij N.N., Gielkens M.M., de Vries R.P., Visser J., de Graaff L.H.
Appl. Environ. Microbiol. 64:3615-3619(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION.
Strain: ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400.
[2]"Cloning of a gene encoding a highly stable endo-beta-1,4-glucanase from Aspergillus niger and its expression in yeast."
Hong J., Tamaki H., Akiba S., Yamamoto K., Kumagai H.
J. Biosci. Bioeng. 92:434-441(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
Strain: IFO 31125.
[3]Hsing-Ren W., Trong-Rong Y.
Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: BCRC 31494.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
GQ292753 Genomic DNA. Translation: ACT68011.1.
AF331518 mRNA. Translation: AAG50051.1.
AJ224452 Genomic DNA. Translation: CAA11965.1.

3D structure databases

ProteinModelPortalO74706.
SMRO74706. Positions 31-331.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5061.CADANGAP00006047.

Protein family/group databases

CAZyGH5. Glycoside Hydrolase Family 5.
mycoCLAPEGL5A_ASPNG.
EGL5B_ASPNG.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG2730.

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_ASPNG
AccessionPrimary (citable) accession number: O74706
Secondary accession number(s): Q9C3Z7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 18, 2010
Last sequence update: November 1, 1998
Last modified: November 13, 2013
This is version 69 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