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O08342 (GUNA_PAEBA) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 57. 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:
Endoglucanase A

EC=3.2.1.4
Alternative name(s):
Cellulase A
Endo-1,4-beta-D-glucanase A
Gene names
Name:celA
OrganismPaenibacillus barcinonensis
Taxonomic identifier198119 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesPaenibacillaceaePaenibacillus

Protein attributes

Sequence length400 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Endoglucanase with high activity on carboxymethylcellulose (CMC) and lichenan, but not active on Avicel. Ref.1

Catalytic activity

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

Enzyme regulation

Strongly inhibited by Hg2+, Ag+ and Fe3+. To a lesser extent, is also inhibited by Pb2+, Mn2+, Sn2+ and Cu2+. By contrast, Ni2+, Zn2+, Co2+, Ba2+ and NH4+ do not affect enzyme activity, while 10 mM Ca2+, and Mg2+ produce a stimulating effect. Is also strongly inhibited by chemicals such as N-bromosuccinimide and dimethyl(2-dihydroxy-5-nitrobenzyl)sulphonium bromide. Is not affected by N-acetylimidazole. Ref.1

Subcellular location

Secreted Ref.1.

Biotechnological use

Study of the performance of endoglucanase A on paper manufacture from agricultural fibers shows that treatment with the enzyme improves the properties of the pulp and the quality of paper. CelA treatment enhances the physical properties (stretch and tensile index) of paper from wheat straw, while dewatering properties are slightly diminished. Ref.1

Sequence similarities

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

Biophysicochemical properties

pH dependence:

Optimum pH is 4.0. Highly stable at acid pH. Retains 100% of its activity after 90 minutes incubation at pH 4.5 and 45 degrees Celsius, and 95% of the initial activity is found after 15 days incubation at room temperature and pH 4.5. Ref.1

Temperature dependence:

Optimum temperature is 40 degrees Celsius. Shows 98% and 51% of its maximum activity at 45 and 55 degrees Celsius, respectively.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cellulose degradation
Polysaccharide degradation
   Cellular componentSecreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
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 – 3232 Probable
Chain33 – 400368Endoglucanase A
PRO_0000371421

Sites

Active site1871Proton donor By similarity
Active site3281Nucleophile By similarity

Sequences

Sequence LengthMass (Da)Tools
O08342 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: E89CB35BBC6F8AE5

FASTA40044,799
        10         20         30         40         50         60 
MTKTFKKFSI AGLALLFMAT AAFAGWSTKA SAADMRSLTA AQITAEMGAG WNLGNQLEAT 

        70         80         90        100        110        120 
VNGTPNETSW GNPTITPELI KKVKAAGFKT IRIPVSYLNY IGSAPNYTVN ASWLNRIQQV 

       130        140        150        160        170        180 
VDYAYNEGLY VVINMHGDGF HSIPGSWLHV NSSNQNVIRD KYQKVWQQVA TRFSAYNERL 

       190        200        210        220        230        240 
IFESMNEVFD GNYNNPNTSY YGNLNAYNQI FVDTVRKTGG NNNARWLLVP GWNTNIDYTV 

       250        260        270        280        290        300 
GNYGFVVPTD NFRSSAIPSS QKRIMISAHY YSPWDFAGEE NGNITQWGAT ATNPAKRSTW 

       310        320        330        340        350        360 
GQEDYLDSQF KSMYDKFVTQ GYPVVMGEFG SIDKSSYDSS NNNYRAVYAK AVTATAKKYK 

       370        380        390        400 
LVPVYWDNGF NGQHGFALFN RFNNTVTQQN IINAIMQGMQ 

« Hide

References

[1]"Cloning of a new endoglucanase gene from Bacillus sp. BP-23 and characterisation of the enzyme. Performance in paper manufacture from cereal straw."
Blanco A., Diaz P., Martinez J., Vidal T., Torres A.L., Pastor F.I.J.
Appl. Microbiol. Biotechnol. 50:48-54(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOTECHNOLOGY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION.
Strain: DSM 15478 / CECT 7022 / BP-23.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y12512 Genomic DNA. Translation: CAA73113.1.

3D structure databases

ProteinModelPortalO08342.
SMRO08342. Positions 40-400.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH5. Glycoside Hydrolase Family 5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF00150. Cellulase. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
PROSITEPS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGUNA_PAEBA
AccessionPrimary (citable) accession number: O08342
Entry history
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: July 1, 1997
Last modified: October 16, 2013
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries