O08342 (GUNA_PAEBA) Reviewed, UniProtKB/Swiss-Prot
Last modified May 1, 2013. Version 55. History...
Names and origin
|Sequence length||400 AA.|
|Sequence processing||The displayed sequence is further processed into a mature form.|
|Protein existence||Evidence at protein level|
General annotation (Comments)
Endoglucanase with high activity on carboxymethylcellulose (CMC) and lichenan, but not active on Avicel. Ref.1
Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans. Ref.1
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
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
Belongs to the glycosyl hydrolase 5 (cellulase A) family.
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
Optimum temperature is 40 degrees Celsius. Shows 98% and 51% of its maximum activity at 45 and 55 degrees Celsius, respectively.
|Biological process||Carbohydrate metabolism|
|Gene Ontology (GO)|
|Biological_process||cellulose catabolic process|
Inferred from electronic annotation. Source: UniProtKB-KW
Inferred from electronic annotation. Source: UniProtKB-SubCell
Inferred from electronic annotation. Source: EC
|Complete GO annotation...|
Sequence annotation (Features)
|||"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.
|Y12512 Genomic DNA. Translation: CAA73113.1.|
3D structure databases
|HSSP||HSSP built from PDB template 1EDG based on UniProtKB P17901. |
|SMR||O08342. Positions 40-400. |
Protein family/group databases
|CAZy||GH5. Glycoside Hydrolase Family 5. |
Protocols and materials databases
Family and domain databases
|Gene3D||188.8.131.52. 1 hit. |
|InterPro||IPR001547. Glyco_hydro_5. |
|Pfam||PF00150. Cellulase. 1 hit. |
|SUPFAM||SSF51445. Glyco_hydro_cat. 1 hit. |
|PROSITE||PS00659. GLYCOSYL_HYDROL_F5. 1 hit. |
|Accession||Primary (citable) accession number: O08342|
|Entry status||Reviewed (UniProtKB/Swiss-Prot)|
|Annotation program||Prokaryotic Protein Annotation Program|