| IED ID | IndEnz0011000332 |
| Enzyme Type ID | glucanase000332 |
| Protein Name |
Endoglucanase D EGD EC 3.2.1.4 Cellulase D Endo-1,4-beta-glucanase Fragment |
| Gene Name | celD |
| Organism | Acetivibrio thermocellus (Hungateiclostridium thermocellum) (Clostridium thermocellum) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Clostridia Eubacteriales Oscillospiraceae Acetivibrio Acetivibrio thermocellus (Hungateiclostridium thermocellum) (Clostridium thermocellum) |
| Enzyme Sequence | SLTGVFPSGLIETKVSAAKITENYQFDSRIRLNSIGFIPNHSKKATIAANCSTFYVVKEDGTIVYTGTATSMFDNDTKETVYIADFSSVNEEGTYYLAVPGVGKSVNFKIAMNVYEDAFKTAMLGMYLLRCGTSVSATYNGIHYSHGPCHTNDAYLDYINGQHTKKDSTKGWHDAGDYNKYVVNAGITVGSMFLAWEHFKDQLEPVALEIPEKNNSIPDFLDELKYEIDWILTMQYPDGSGRVAHKVSTRNFGGFIMPENEHDERFFVPWSSAATADFVAMTAMAARIFRPYDPQYAEKCINAAKVSYEFLKNNPANVFANQSGFSTGEYATVSDADDRLWAAAEMWETLGDEEYLRDFENRAAQFSKKIEADFDWDNVANLGMFTYLLSERPGKNPALVQSIKDSLLSTADSIVRTSQNHGYGRTLGTTYYWGCNGTVVRQTMILQVANKISPNNDYVNAALDAISHVFGRNYYNRSYVTGLGINPPMNPHDRRSGADGIWEPWPGYLVGGGWPGPKDWVDIQDSYQTNEIAINWNAALIYALAGFVNYNSPQNEVLYGDVNDDGKVNSTDLTLLKRYVLKAVSTLPSSKAEKNADVNRDGRVNSSDVTILSRYLIRVIEKLPI |
| Enzyme Length | 625 |
| Uniprot Accession Number | P0C2S4 |
| Absorption | |
| Active Site | ACT_SITE 177; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10140"; ACT_SITE 492; /evidence="ECO:0000255|PROSITE-ProRule:PRU10059, ECO:0000269|PubMed:2037583"; ACT_SITE 522; /evidence="ECO:0000255|PROSITE-ProRule:PRU10060, ECO:0000269|PubMed:1637316"; ACT_SITE 531; /note="Proton donor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10060, ECO:0000269|PubMed:1537833" |
| 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: This enzyme catalyzes the endohydrolysis of 1,4-beta-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (4); Beta strand (16); Chain (1); Domain (1); Helix (18); Mutagenesis (24); Non-terminal residue (1); Signal peptide (1); Turn (7) |
| Keywords | 3D-structure;Calcium;Carbohydrate metabolism;Cellulose degradation;Glycosidase;Hydrolase;Polysaccharide degradation;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL <1..17 |
| Structure 3D | X-ray crystallography (3) |
| Cross Reference PDB | 1CLC; 4CJ0; 4CJ1; |
| Mapped Pubmed ID | 24823716; |
| Motif | |
| Gene Encoded By | |
| Mass | 69,707 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |