| IED ID | IndEnz0011000266 |
| Enzyme Type ID | glucanase000266 |
| Protein Name |
Beta-mannanase/endoglucanase A Includes: Mannan endo-1,4-beta-mannosidase A EC 3.2.1.78 Beta-mannanase Endo-1,4-mannanase ; Endo-1,4-beta-glucanase EC 3.2.1.4 Cellulase |
| Gene Name | manA |
| Organism | Caldicellulosiruptor saccharolyticus (Caldocellum saccharolyticum) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Clostridia Thermoanaerobacterales Thermoanaerobacterales Family III. Incertae Sedis Caldicellulosiruptor Caldicellulosiruptor saccharolyticus (Caldocellum saccharolyticum) |
| Enzyme Sequence | MRLKTKIRKKWLSVLCTVVFLLNILFIANVTILPKVGAATSNDGVVKIDTSTLIGTNHAHCWYRDRLDTALRGIRSWGMNSVRVVLSNGYRWTKIPASEVANIISLSRSLGFKAIILEVHDTTGYGEDGAACSLAQAVEYWKEIKSVLDGNEDFVIINIGNEPYGNNNYQNWVNDTKNAIKALRDAGFKHTIMVDAPNWGQDWSNTMRDNAQSIMEADPLRNLVFSIHMYGVYNTASKVEEYIKSFVDKGLPLVIGEFGHQHTDGDPDEEAIVRYAKQYKIGLFSWSWCGNSSYVGYLDMVNNWDPNNPTPWGQWYKTNAIGTSSTPTPTSTVTPTPTPTPTPTPTVTATPTPTPTPVSTPATSGQIKVLYANKETNSTTNTIRPWLKVVNSGSSSIDLSRVTIRYWYTVDGERAQSAISDWAQIGASNVTFKFVKLSSSVSGADYYLEIGFKSGAGQLQPGKDTGEIQMRFNKDDWSNYNQGNDWSWIQSMTSYGENEKVTAYIDGVLVWGQEPSGATPAPAPTATPTPTPTVTPTPTVTPTPTVTATPTPTPTPTPTPVSTPATGGQIKVLYANKETNSTTNTIRPWLKVVNSGSSSIDLSRVTIRYWYTVDGERAQSAISDWAQIGASNVTFKFVKLSSSVSGADYYLEIGFKSGAGQLQPGKDTGEIQIRFNKSDWSNYNQGNDWSWIQSMTSYGENEKVTAYIDGVLVWGQEPSGTTPSPTSTPTVTVTPTPTPTPTPTPTPTVTPTPTVTPTPTVTATPTPTPTPIPTVTPLPTISPSPSVVEITINTNAGRTQISPYIYGANQDIEGVVHSARRLGGNRLTGYNWENNFSNAGNDWYHSSDDYLCWSMGISGEDAKVPAAVVSKFHEYSLKNNAYSAVTLQMAGYVSKDNYGTVSENETAPSNRWAEVKFKKDAPLSLNPDLNDNFVYMDEFINYLINKYGMASSPTGIKGYILDNEPDLWASTHPRIHPNKVTCKELIEKSVELAKVIKTLDPSAEVFGYASYGFMGYYSLQDAPDWNQVKGEHRWFISWYLEQMKKASDSFGKRLLDVLDLHWYPEARGGNIRVCFDGENDTSKEVVIARMQAPRTLWDPTYKTSVKGQITAGENSWINQWFSDYLPIIPNVKADIEKYYPGTKLAISEFDYGGRNHISGGIALADVLGIFGKYGVNFAARWGDSGSYAAAAYNIYLNYDGKGSKYGNTNVSANTSDVENMPVYASINGQDDSELHIILINRNYDQKLQVKINITSTPKYTKAEIYGFDSNSPEYKKMGNIDNIESNVFTLEVPKFNGVSHSITLDFNVSIKIIQNEVIKFIRNLVFMRALV |
| Enzyme Length | 1331 |
| Uniprot Accession Number | P22533 |
| Absorption | |
| Active Site | ACT_SITE 162; /note=Proton donor; /evidence=ECO:0000250; ACT_SITE 257; /note=Nucleophile; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | |
| 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; 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 | 3.2.1.78; 3.2.1.4 |
| Enzyme Function | FUNCTION: Degradation of hemicelluloses, the second most abundant polysaccharides in nature. Contains two catalytic domains with mannanase and endoglucanase activities. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 80 degrees Celsius.; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Compositional bias (3); Domain (2); Region (5); Sequence conflict (2); Signal peptide (1) |
| Keywords | Carbohydrate metabolism;Cellulose degradation;Glycosidase;Hydrolase;Multifunctional enzyme;Polysaccharide degradation;Repeat;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..41; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 146,893 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.2.1.78; |