| IED ID | IndEnz0011000014 |
| Enzyme Type ID | glucanase000014 |
| Protein Name |
Endoglucanase EC 3.2.1.4 CaCel Cellulase Endo-beta-1,4-glucanase |
| Gene Name | |
| Organism | Cryptopygus antarcticus (Antarctic springtail) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Panarthropoda Arthropoda Mandibulata Pancrustacea Hexapoda Collembola (springtails) Entomobryomorpha Isotomoidea Isotomidae (smooth springtails) Anurophorinae Cryptopygus Cryptopygus antarcticus complex Cryptopygus antarcticus (Antarctic springtail) |
| Enzyme Sequence | MKVFVVLAAIVAIANGLTSGSGVTTRYWDCCKPSCSWGGKASVTKPVRTCKANGNTTIDSNTQSGCNGGSSYVCNDQQPFTQGNVGYGFAAASISGQPESQTCCACYEMTFTNTAISGQKMIVQVTNTGSDLNGNHFDLMIPGGGVGIFNGCQSQWGAPSNGWGQRYGGISSQSECNQLPTSLRAGCNWRFGWFKNADNPSMKFTQVRCPTILTQKSQCVRTPGP |
| Enzyme Length | 225 |
| Uniprot Accession Number | D3GDK4 |
| Absorption | |
| Active Site | ACT_SITE 29; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10069, ECO:0000305|PubMed:28156112"; ACT_SITE 138; /note="Proton donor"; /evidence="ECO:0000305|PubMed:28156112" |
| Activity Regulation | ACTIVITY REGULATION: Activity is not affected by metal ions except Mn(2+), which reduces the activity by 40-50%. However, no significant change in activity in response to 1 mM EDTA. {ECO:0000269|PubMed:28156112}. |
| 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; Evidence={ECO:0000255|PROSITE-ProRule:PRU10069, ECO:0000269|PubMed:22333528, ECO:0000269|PubMed:24848382, ECO:0000269|PubMed:28156112}; |
| DNA Binding | |
| EC Number | 3.2.1.4 |
| Enzyme Function | FUNCTION: Hydrolyzes carboxymethylcellulose (CMC) (PubMed:24848382, PubMed:28156112). Hydrolyzes also lichenan and barley beta-1,4-D-glucan. CMC is hydrolyzed majorily to cellobiose (G2), cellotriose (G3) and cellotetraose (G4). Cellohexaose (G6) is hydrolyzed to G4 and G2 with traces of G3. Cellopentaose (G5) is completely hydrolyzed to G2 and G3, and G4 is partially hydrolyzed to G2. Does not hydrolyze G2 or G3. Does not hydrolyze crystalline cellulose, soluble starch, xylan, mannan or laminarin (PubMed:28156112). {ECO:0000269|PubMed:24848382, ECO:0000269|PubMed:28156112}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is around 40-50 degrees Celsius (PubMed:24848382, PubMed:28156112). Has more than 50% of the maximal activity between 10-70 degrees Celsius, and more than 30% of activity at 0 degrees Celsius. Stable at 50 degrees Celsius for 30 min (PubMed:24848382). 60-80% of the maximal activity is retained between 0-10 degrees Celsius. Displays 40% of its maximal activity at as high as 80 degrees Celsius. Remains active at 60 degrees Celsius for over 8 hours. Approximately 50% of the activity is still maintained after 4-hour incubation at 70 degrees Celsius (PubMed:28156112). {ECO:0000269|PubMed:24848382, ECO:0000269|PubMed:28156112}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 3.5 (PubMed:24848382, PubMed:28156112). More than 90% of the maximal activity is maintained between pH range 3-5 (PubMed:24848382). More than 60% of the maximal activity is maintained between pH range 2-8 (PubMed:24848382, PubMed:28156112). About 80% of the maximal activity is maintained even at pH 2.5 (PubMed:28156112). {ECO:0000269|PubMed:24848382, ECO:0000269|PubMed:28156112}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (11); Chain (1); Disulfide bond (7); Glycosylation (1); Helix (9); Sequence conflict (2); Signal peptide (1); Turn (2) |
| Keywords | 3D-structure;Carbohydrate metabolism;Cellulose degradation;Direct protein sequencing;Disulfide bond;Glycoprotein;Glycosidase;Hydrolase;Polysaccharide degradation;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24848382}. |
| Modified Residue | |
| Post Translational Modification | PTM: N- and O-glycosylated. Contains hybrid- and complex-type N-glycans. {ECO:0000269|PubMed:24848382}. |
| Signal Peptide | SIGNAL 1..15; /evidence=ECO:0000269|PubMed:24848382 |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 5H4U; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 23,795 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.2.1.4; |