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; |