| IED ID | IndEnz0008000145 |
| Enzyme Type ID | cellulase000145 |
| Protein Name |
Mannan endo-1,4-beta-mannosidase EC 3.2.1.78 Beta-mannanase Endo-beta-1,4-mannanase Man5A ManA |
| Gene Name | |
| Organism | Mytilus edulis (Blue mussel) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Spiralia Lophotrochozoa Mollusca Bivalvia Autobranchia Pteriomorphia Mytiloida Mytiloidea Mytilidae Mytilinae Mytilus Mytilus edulis (Blue mussel) |
| Enzyme Sequence | MLLTALAVLFASTGCQARLSVSGTNLNYNGHHIFLSGANQAWVNYARDFGHNQYSKGKSTFESTLSDIQSHGGNSVRVWLHIEGESTPEFDNNGYVTGIDNTLISDMRAYLHAAQRHNILIFFTLWNGAVKQSTHYRLNGLMVDTRKLQSYIDHALKPMANALKNEKALGGWDIMNEPEGEIKPGESSSEPCFDTRHLSGSGAGWAGHLYSAQEIGRFVNWQAAAIKEVDPGAMVTVGSWNMKADTDAMGFHNLYSDHCLVKAGGKQSGTLSFYQVHTYDWQNHFGNESPFKHSFSNFRLKKPMVIGEFNQEHGAGMSSESMFEWAYTKGYSGAWTWSRTDVSWNNQLRGIQHLKSRTDHGQVQFGL |
| Enzyme Length | 367 |
| Uniprot Accession Number | Q8WPJ2 |
| Absorption | |
| Active Site | ACT_SITE 177; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:P07985; ACT_SITE 308; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P07985 |
| Activity Regulation | |
| Binding Site | BINDING 79; /note=Substrate; /evidence=ECO:0000250|UniProtKB:B4XC07; BINDING 176; /note=Substrate; /evidence=ECO:0000250|UniProtKB:B4XC07; BINDING 205; /note=Substrate; /evidence=ECO:0000250|UniProtKB:B4XC07; BINDING 240; /note=Substrate; /evidence=ECO:0000250|UniProtKB:B4XC07; BINDING 279; /note=Substrate; /evidence=ECO:0000250|UniProtKB:B4XC07; BINDING 337; /note=Substrate; /evidence=ECO:0000250|UniProtKB:B4XC07 |
| 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; |
| DNA Binding | |
| EC Number | 3.2.1.78 |
| Enzyme Function | FUNCTION: Hydrolyzes 1,4-beta linked polysaccharide backbones of mannans. Hydrolyzes mannohexaose (M6) preferentially to mannotriose (M4) and less preferentially to mannotetraose (M3), mannopentaose (M5), and mannobiose (M2); hydrolyzes M5 preferentially to M2, and M3, and less preferentially to mannotetraose M4; hydrolyzes M4 preferentially to M3, and less preferentially to mannose (M1), plus very little M2. Does not hydrolyze mannobiose or mannotriose. Does not hydrolyze xlyan, starch, cellulose or galactose. {ECO:0000269|PubMed:11689251, ECO:0000269|PubMed:11895446, ECO:0000269|PubMed:16487541}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is about 50 degrees Celsius. {ECO:0000269|PubMed:11689251, ECO:0000269|PubMed:16487541}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.2. {ECO:0000269|PubMed:11689251, ECO:0000269|PubMed:16487541}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (16); Binding site (6); Chain (1); Disulfide bond (1); Helix (15); Sequence conflict (2); Signal peptide (1); Turn (2) |
| Keywords | 3D-structure;Direct protein sequencing;Disulfide bond;Glycosidase;Hydrolase;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | PTM: The disulfide bond between Cys-192 and Cys-259 has not been observed in x-ray crystallograghy (PubMed:16487541). This may be a consequence of the X-ray radiation. {ECO:0000269|PubMed:16487541}. |
| Signal Peptide | SIGNAL 1..17; /evidence=ECO:0000269|PubMed:11689251 |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 2C0H; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 40,957 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.49 mM for mannotetraose {ECO:0000269|PubMed:11689251, ECO:0000269|PubMed:16487541}; KM=1.61 mM for mannopentaose {ECO:0000269|PubMed:11689251, ECO:0000269|PubMed:16487541}; KM=0.5 mM for mannohexaose {ECO:0000269|PubMed:11689251, ECO:0000269|PubMed:16487541}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.2.1.78; |