Detail Information for IndEnz0011000331
IED ID IndEnz0011000331
Enzyme Type ID glucanase000331
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