| IED ID | IndEnz0011000307 |
| Enzyme Type ID | glucanase000307 |
| Protein Name |
Endoglucanase A EC 3.2.1.4 Cellulase A Endo-1,4-beta-D-glucanase A |
| Gene Name | celA |
| Organism | Paenibacillus barcinonensis |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Paenibacillaceae Paenibacillus Paenibacillus barcinonensis |
| Enzyme Sequence | MTKTFKKFSIAGLALLFMATAAFAGWSTKASAADMRSLTAAQITAEMGAGWNLGNQLEATVNGTPNETSWGNPTITPELIKKVKAAGFKTIRIPVSYLNYIGSAPNYTVNASWLNRIQQVVDYAYNEGLYVVINMHGDGFHSIPGSWLHVNSSNQNVIRDKYQKVWQQVATRFSAYNERLIFESMNEVFDGNYNNPNTSYYGNLNAYNQIFVDTVRKTGGNNNARWLLVPGWNTNIDYTVGNYGFVVPTDNFRSSAIPSSQKRIMISAHYYSPWDFAGEENGNITQWGATATNPAKRSTWGQEDYLDSQFKSMYDKFVTQGYPVVMGEFGSIDKSSYDSSNNNYRAVYAKAVTATAKKYKLVPVYWDNGFNGQHGFALFNRFNNTVTQQNIINAIMQGMQ |
| Enzyme Length | 400 |
| Uniprot Accession Number | O08342 |
| Absorption | |
| Active Site | ACT_SITE 187; /note=Proton donor; /evidence=ECO:0000250; ACT_SITE 328; /note=Nucleophile; /evidence=ECO:0000250 |
| Activity Regulation | ACTIVITY REGULATION: Strongly inhibited by Hg(2+), Ag(+) and Fe(3+). To a lesser extent, is also inhibited by Pb(2+), Mn(2+), Sn(2+) and Cu(2+). By contrast, Ni(2+), Zn(2+), Co(2+), Ba(2+) and NH(4)(+) do not affect enzyme activity, while 10 mM Ca(2+), and Mg(2+) 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. {ECO:0000269|PubMed:9720200}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.; EC=3.2.1.4; Evidence={ECO:0000269|PubMed:9720200}; |
| DNA Binding | |
| EC Number | 3.2.1.4 |
| Enzyme Function | FUNCTION: Endoglucanase with high activity on carboxymethylcellulose (CMC) and lichenan, but not active on Avicel. {ECO:0000269|PubMed:9720200}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40 degrees Celsius. Shows 98% and 51% of its maximum activity at 45 and 55 degrees Celsius, respectively. {ECO:0000269|PubMed:9720200}; |
| PH Dependency | 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. {ECO:0000269|PubMed:9720200}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Signal peptide (1) |
| Keywords | Carbohydrate metabolism;Cellulose degradation;Glycosidase;Hydrolase;Polysaccharide degradation;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9720200}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..32; /evidence=ECO:0000305 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 44,799 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |