IED ID | IndEnz0008000308 |
Enzyme Type ID | cellulase000308 |
Protein Name |
Endoglucanase D EGD EC 3.2.1.4 Cellulase D Endo-1,4-beta-glucanase |
Gene Name | celD Cthe_0825 |
Organism | Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) (Clostridium thermocellum) |
Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Clostridia Eubacteriales Oscillospiraceae Acetivibrio Acetivibrio thermocellus (Hungateiclostridium thermocellum) (Clostridium thermocellum) Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) (Clostridium thermocellum) |
Enzyme Sequence | MSRMTLKSSMKKRVLSLLIAVVFLSLTGVFPSGLIETKVSAAKITENYQFDSRIRLNSIGFIPNHSKKATIAANCSTFYVVKEDGTIVYTGTATSMFDNDTKETVYIADFSSVNEEGTYYLAVPGVGKSVNFKIAMNVYEDAFKTAMLGMYLLRCGTSVSATYNGIHYSHGPCHTNDAYLDYINGQHTKKDSTKGWHDAGDYNKYVVNAGITVGSMFLAWEHFKDQLEPVALEIPEKNNSIPDFLDELKYEIDWILTMQYPDGSGRVAHKVSTRNFGGFIMPENEHDERFFVPWSSAATADFVAMTAMAARIFRPYDPQYAEKCINAAKVSYEFLKNNPANVFANQSGFSTGEYATVSDADDRLWAAAEMWETLGDEEYLRDFENRAAQFSKKIEADFDWDNVANLGMFTYLLSERPGKNPALVQSIKDSLLSTADSIVRTSQNHGYGRTLGTTYYWGCNGTVVRQTMILQVANKISPNNDYVNAALDAISHVFGRNYYNRSYVTGLGINPPMNPHDRRSGADGIWEPWPGYLVGGGWPGPKDWVDIQDSYQTNEIAINWNAALIYALAGFVNYNSAQNEVLYGDVNDDGKVNSTDLTLLKRYVLKAVSTLPSSKAEKNADVNRDGRVNSSDVTILSRYLIRVIEKLPI |
Enzyme Length | 649 |
Uniprot Accession Number | A3DDN1 |
Absorption | |
Active Site | ACT_SITE 201; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU10140; ACT_SITE 516; /evidence=ECO:0000255|PROSITE-ProRule:PRU10059; ACT_SITE 546; /evidence=ECO:0000255|PROSITE-ProRule:PRU10060; ACT_SITE 555; /note=Proton donor; /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: This enzyme catalyzes the endohydrolysis of 1,4-beta-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans. {ECO:0000250}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (4); Beta strand (1); Chain (1); Domain (1); Helix (3); Sequence conflict (1); Signal peptide (1) |
Keywords | 3D-structure;Calcium;Carbohydrate metabolism;Cellulose degradation;Glycosidase;Hydrolase;Polysaccharide degradation;Reference proteome;Signal |
Interact With | |
Induction | |
Subcellular Location | |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..41; /evidence=ECO:0000250 |
Structure 3D | X-ray crystallography (1) |
Cross Reference PDB | 4FL4; |
Mapped Pubmed ID | 22707718; |
Motif | |
Gene Encoded By | |
Mass | 72,415 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |