| IED ID | IndEnz0008000023 |
| Enzyme Type ID | cellulase000023 |
| Protein Name |
Endoglucanase A EC 3.2.1.4 Cellulase A EGCCA Endo-1,4-beta-glucanase A |
| Gene Name | celCCA Ccel_1099 |
| Organism | Ruminiclostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 / H10) (Clostridium cellulolyticum) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Clostridia Eubacteriales Oscillospiraceae Ruminiclostridium Ruminiclostridium cellulolyticum Ruminiclostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 / H10) (Clostridium cellulolyticum) |
| Enzyme Sequence | MKKTTAFLLCFLMIFTALLPMQNANAYDASLIPNLQIPQKNIPNNDGMNFVKGLRLGWNLGNTFDAFNGTNITNELDYETSWSGIKTTKQMIDAIKQKGFNTVRIPVSWHPHVSGSDYKISDVWMNRVQEVVNYCIDNKMYVILNTHHDVDKVKGYFPSSQYMASSKKYITSVWAQIAARFANYDEHLIFEGMNEPRLVGHANEWWPELTNSDVVDSINCINQLNQDFVNTVRATGGKNASRYLMCPGYVASPDGATNDYFRMPNDISGNNNKIIVSVHAYCPWNFAGLAMADGGTNAWNINDSKDQSEVTWFMDNIYNKYTSRGIPVIIGECGAVDKNNLKTRVEYMSYYVAQAKARGILCILWDNNNFSGTGELFGFFDRRSCQFKFPEIIDGMVKYAFEAKTDPDPVIVYGDYNNDGNVDALDFAGLKKYIMAADHAYVKNLDVNLDNEVNAFDLAILKKYLLGMVSKLPSN |
| Enzyme Length | 475 |
| Uniprot Accession Number | P17901 |
| Absorption | |
| Active Site | ACT_SITE 147; /evidence=ECO:0000305; ACT_SITE 195; /note=Proton donor; ACT_SITE 332; /note=Nucleophile |
| Activity Regulation | |
| 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; |
| DNA Binding | |
| EC Number | 3.2.1.4 |
| Enzyme Function | FUNCTION: The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: (1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the disaccharide cellobiose from the non-reducing end of the cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the cellobiose and other short cello-oligosaccharides to glucose. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (11); Chain (1); Domain (1); Helix (22); Mutagenesis (4); Signal peptide (1); Turn (6) |
| Keywords | 3D-structure;Carbohydrate metabolism;Cellulose degradation;Direct protein sequencing;Glycosidase;Hydrolase;Polysaccharide degradation;Reference proteome;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..26; /evidence=ECO:0000269|PubMed:2558058 |
| Structure 3D | X-ray crystallography (3) |
| Cross Reference PDB | 1EDG; 2VN5; 2VN6; |
| Mapped Pubmed ID | 18445585; |
| Motif | |
| Gene Encoded By | |
| Mass | 53,625 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |