| IED ID | IndEnz0011000326 | 
| Enzyme Type ID | glucanase000326 | 
| Protein Name | 
                        
                            
                                Endoglucanase C  EC 3.2.1.4 Cellulase C Endo-1,4-beta-glucanase C  | 
                    
| Gene Name | cenC Celf_1537 | 
| Organism | Cellulomonas fimi (strain ATCC 484 / DSM 20113 / JCM 1341 / NBRC 15513 / NCIMB 8980 / NCTC 7547) | 
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Micrococcales Cellulomonadaceae Cellulomonas Cellulomonas fimi Cellulomonas fimi (strain ATCC 484 / DSM 20113 / JCM 1341 / NBRC 15513 / NCIMB 8980 / NCTC 7547) | 
| Enzyme Sequence | MVSRRSSQARGALTAVVATLALALAGSGTALAASPIGEGTFDDGPEGWVAYGTDGPLDTSTGALCVAVPAGSAQYGVGVVLNGVAIEEGTTYTLRYTATASTDVTVRALVGQNGAPYGTVLDTSPALTSEPRQVTETFTASATYPATPAADDPEGQIAFQLGGFSADAWTFCLDDVALDSEVELLPHTSFAESLGPWSLYGTSEPVFADGRMCVDLPGGQGNPWDAGLVYNGVPVGEGESYVLSFTASATPDMPVRVLVGEGGGAYRTAFEQGSAPLTGEPATREYAFTSNLTFPPDGDAPGQVAFHLGKAGAYEFCISQVSLTTSATPPPGYEPDTGPRVRVNQVGYLPFGPKRATLVTDAAEPVAWELRDADGVVVADGTSEPRGVEPSAAQAVHVLDFSDVTTQGAGYTLVADGETSRPFDIDGDLYQQLRYDALNYFYLARSGTEIEADVVGEEYAREAGHVGVAPNQGDTDVPCIGPRDYYDGWTCDYRLDVSGGWYDAGDHGKYVVNGGIAVGQLLQTYERALHAGTADALADGTLDVPEHGNDVPDVLDEARWELEWMLSMIVPEGEYAGMVHHKVHDEGWTGLPLLPADDPQARSLHRPSTAATLNLSAVAAQGARLLEPYDPQLAQTLLEAARTTWAAAQEHPALYAPGEAGADGGGAYNDSQVADEFYWAAAELYLTTGEDAFATAVTTSPLHTADVFTADGFGWGSVAALGRLDLATVPNELPGLDAVQSSVVEGAQEYLAAQAGQGFGSLYSPPGGEYVWGSSSQVANNLVVVATAYDLTGDERFRAATLEGLDYLFGRNALNQSYVTGWGEVASHQQHSRWFAHQLDPSLPSPPPGSLAGGPNSQAATWDPTTKAAFPDGCAPSACYVDEIQAWSTNELTVNWNSALSWVASWVADQGSAEPVPTAPVVTRQPVDATVALGADATFTAEASGVPAPTVRWQVRAGRGWKDVAGATGTTLTVRATARTDGTRYRAVFTNAAGSVESAVVRLTVERAAPVVTQHPADVRARVGTRAVFRAAADGYPTPCVVWQVRWGGGSWRPIPWATSTTLSVPVTVLAAGTEYRAVFTNAVGTAATEPAELAVQRPRS | 
| Enzyme Length | 1101 | 
| Uniprot Accession Number | P14090 | 
| Absorption | |
| Active Site | ACT_SITE 506; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU10140; ACT_SITE 831; /evidence=ECO:0000255|PROSITE-ProRule:PRU10059; ACT_SITE 882; /evidence=ECO:0000255|PROSITE-ProRule:PRU10060; ACT_SITE 891; /evidence=ECO:0000255|PROSITE-ProRule:PRU10060 | 
| 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 (4); Beta strand (22); Chain (1); Domain (4); Region (2); Signal peptide (1); Turn (1) | 
| Keywords | 3D-structure;Carbohydrate metabolism;Cellulose degradation;Direct protein sequencing;Glycosidase;Hydrolase;Immunoglobulin domain;Polysaccharide degradation;Reference proteome;Repeat;Signal | 
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..32; /evidence=ECO:0000269|PubMed:1956299 | 
| Structure 3D | X-ray crystallography (1); NMR spectroscopy (3) | 
| Cross Reference PDB | 1CX1; 1GU3; 1ULO; 1ULP; | 
| Mapped Pubmed ID | 10704194; 12079353; | 
| Motif | |
| Gene Encoded By | |
| Mass | 115,216 | 
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |