| IED ID | IndEnz0008000093 |
| Enzyme Type ID | cellulase000093 |
| Protein Name |
Mannan endo-1,4-beta-mannosidase EC 3.2.1.78 Beta-mannanase CaMan Endo-beta-1,4-D-mannanase |
| 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 | MVKLFSFLLLVWVASPAFSSEFLKASGSNFYYGGQKVFLSGVNFAWRSYGSDFGNGQYASNGPALKDWINKVKASGGNTARVWVHVEGQVSPAFDSHGFVTSTDSKKTLINDLSDLLDYANGQNVFLILVLFNGALQNNSNVQNLFWDESKLNSYINNALTPMVNALKSKPSLAAWEVLNEPEGTLQPGSDQNSCYDTSTLAAQGAGWGGKKFPMKQILKTINWISSAIHNADSKALVTVGSWSELTQTDSFGYRNHYKDSCLTGAGGKSNGIINFYQMHTYSHSGKWNQNAPFKVNRWAYNVNDKPLLIGEFASVCSQNEGIQNLYKYAYNNGYNGALTWQFNSGGDCSDTYSNQMYGMQALKGQNDQSGGKGGMVSVNIN |
| Enzyme Length | 382 |
| Uniprot Accession Number | B4XC07 |
| Absorption | |
| Active Site | ACT_SITE 181; /note=Proton donor/acceptor; /evidence=ECO:0000250|UniProtKB:Q99036; ACT_SITE 312; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:Q99036 |
| Activity Regulation | ACTIVITY REGULATION: Activated particularly by Ca(2+) and Zn(2+), and to a lesser extent by Na(+), K(+), Mg(2+) and Cu(2+). Activation effect of the divalent metal ions Ca(2+), Zn(2+), Mg(2+) and Cu(2+) is reduced significantly by the addition of EDTA. Strongly inhibited by Mn(2+), Hg(2+) and Ag(+). {ECO:0000269|PubMed:18579426}. |
| Binding Site | BINDING 83; /note="Substrate"; /evidence="ECO:0000269|PubMed:25082572, ECO:0007744|PDB:4OOZ"; BINDING 144; /note="Substrate"; /evidence="ECO:0000269|PubMed:25082572, ECO:0007744|PDB:4OOZ"; BINDING 180; /note="Substrate"; /evidence="ECO:0000269|PubMed:25082572, ECO:0007744|PDB:4OOZ"; BINDING 187; /note="Substrate"; /evidence="ECO:0000269|PubMed:25082572, ECO:0007744|PDB:4OOZ"; BINDING 204; /note="Substrate"; /evidence="ECO:0000269|PubMed:25082572, ECO:0007744|PDB:4OOZ"; BINDING 208; /note="Substrate"; /evidence="ECO:0000269|PubMed:25082572, ECO:0007744|PDB:4OOZ"; BINDING 243; /note="Substrate"; /evidence="ECO:0000269|PubMed:25082572, ECO:0007744|PDB:4OOZ"; BINDING 282; /note="Substrate"; /evidence="ECO:0000269|PubMed:25082572, ECO:0007744|PDB:4OOZ"; BINDING 284; /note="Substrate"; /evidence="ECO:0000269|PubMed:25082572, ECO:0007744|PDB:4OOZ"; BINDING 341; /note="Substrate"; /evidence="ECO:0000269|PubMed:25082572, ECO:0007744|PDB:4OOZ"; BINDING 348; /note="Substrate; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:25082572, ECO:0007744|PDB:4OOZ" |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans.; EC=3.2.1.78; Evidence={ECO:0000269|PubMed:18579426, ECO:0000269|PubMed:22333528, ECO:0000269|PubMed:25082572}; |
| DNA Binding | |
| EC Number | 3.2.1.78 |
| Enzyme Function | FUNCTION: Hydrolyzes 1,4-beta linked polysaccharide backbones of mannans. Has high activity toward locust bean gum (PubMed:18579426, PubMed:25082572). Also active toward konjac and beta-1,4-mannan. Hydrolyzes mannotetraose (M4) and mannopentaose (M5) to mannobiose (M2) and mannotriose (M3) with a little production of mannose (M1). Hydrolyzes beta-1,4-mannan to M2, M3 and M4. Hardly hydrolyzes M2 and M3. Does not hydrolyze p-nitrophenyl-beta-D-mannopyranoside, gua-gum, carboxymethyl cellulose, soluble starch or laminarin (PubMed:18579426). {ECO:0000269|PubMed:18579426, ECO:0000269|PubMed:25082572}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 30 degrees Celsius. Retains approximately 20-40% of its maximum activity even at 0-5 degrees Celsius. Drastic loss of activity at temperatures above 45 degrees Celsius, at which the half-life of the enzyme activity is less than 10 min. {ECO:0000269|PubMed:18579426}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 3.5. Maintains more than 50% of the maximum activity at pH 2.5-6.0. Not active at a pH above 7.0. {ECO:0000269|PubMed:18579426}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (16); Binding site (11); Chain (1); Disulfide bond (2); Helix (14); Mutagenesis (5); Region (2); Signal peptide (1); Turn (3) |
| Keywords | 3D-structure;Carbohydrate metabolism;Disulfide bond;Glycosidase;Hydrolase;Polysaccharide degradation;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..19; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 4OOU; 4OOZ; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 41,833 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=5.61 mg/ml for 0.5% locust bean gum (at pH 3.5 and 10 degrees Celsius in the presence of 50mM sodium citrate) {ECO:0000269|PubMed:25082572}; Vmax=2477.22 mol/min/mg enzyme with 0.5% locust bean gum as substrate (at pH 3.5 and 10 degrees Celsius in the presence of 50mM sodium citrate) {ECO:0000269|PubMed:25082572}; Note=kcat is 1659.90 sec(-1) for 0.5% locust bean gum (at pH 3.5 and 10 degrees Celsius in the presence of 50mM sodium citrate). {ECO:0000269|PubMed:25082572}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.2.1.78; |