| IED ID | IndEnz0011000330 |
| Enzyme Type ID | glucanase000330 |
| Protein Name |
Endoglucanase C EC 3.2.1.4 Cellulase C EGCCC Endo-1,4-beta-glucanase C |
| Gene Name | celCCC Ccel_0730 |
| 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 | MIKGSSLKRFKSLVMAAIFSVSIISTAIASSAADQIPFPYDAKYPNGAYSCLADSQSIGNNLVRSEWEQWKSAHITSNGARGYKRVQRDASTNYDTVSEGLGYGLLLSVYFGEQQLFDDLYRYVKVFLNSNGLMSWRIDSSGNIMGKDSIGAATDADEDIAVSLVFAHKKWGTSGGFNYQTEAKNYINNIYNKMVEPGTYVIKAGDTWGGSNVTNPSYFAPAWYRIFADFTGNSGWINVANKCYEIADKARNSNTGLVPDWCTANGTPASGQGFDFYYDAIRYQWRAAIDYSWYGTAKAKTHCDAISNFFKNIGYANIKDGYTISGSQISSNHTATFVSCAAAAAMTGTDTTYAKNIYNECVKVKDSGNYTYFGNTLRMMVLLYTTGNFPNLYTYNSQPKPDLKGDVNNDGAIDALDIAALKKAILTQTTSNISLTNADMNNDGNIDAIDFAQLKVKLLN |
| Enzyme Length | 460 |
| Uniprot Accession Number | P37699 |
| Absorption | |
| Active Site | ACT_SITE 99; /note=Proton donor; /evidence=ECO:0000250; ACT_SITE 155; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU10058 |
| 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 | PATHWAY: Glycan metabolism; cellulose degradation. |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Domain (1); Sequence conflict (1); Signal peptide (1) |
| Keywords | Carbohydrate metabolism;Cellulose degradation;Direct protein sequencing;Glycosidase;Hydrolase;Polysaccharide degradation;Reference proteome;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | PTM: There are two forms of the cellulase. The shorter form lacks probably the C-terminal reiterated domains. |
| Signal Peptide | SIGNAL 1..32; /evidence=ECO:0000269|PubMed:8223599 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 50,483 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |