IED ID | IndEnz0011000265 |
Enzyme Type ID | glucanase000265 |
Protein Name |
Beta-glucanase EC 3.2.1.73 1,3-1,4-beta-D-glucan 4-glucanohydrolase Endo-beta-1,3-1,4 glucanase Laminarinase Lichenase |
Gene Name | licB lam1 |
Organism | Acetivibrio thermocellus (Hungateiclostridium thermocellum) (Clostridium thermocellum) |
Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Clostridia Eubacteriales Oscillospiraceae Acetivibrio Acetivibrio thermocellus (Hungateiclostridium thermocellum) (Clostridium thermocellum) |
Enzyme Sequence | MKNRVISLLMASLLLVLSVIVAPFYKAEAATVVNTPFVAVFSNFDSSQWEKADWANGSVFNCVWKPSQVTFSNGKMILTLDREYGGSYPYKSGEYRSKSFFGYGYYEVRMKAAKNVGIVSSFFTYTGPSDNNPWDEIDIEFLGKDTTKAQFNWYKNEVGGNEYLHNLGFDASQDFHTYGFEWRPDYIDFYVDGKKVYRGTRNIPVTPGKIMMNLWPGKGVDEWLGRYDGRTPLQAEYEYVKYYPNGVPQDNPTPTPTIAPSTPTNPNLPLKGDVNGDGHVNSSDYSLFKRYLLRVIDRFPVGDQSVADVNRDGRIDSTDLTMLKRYLIRAIPSL |
Enzyme Length | 334 |
Uniprot Accession Number | Q84C00 |
Absorption | |
Active Site | ACT_SITE 136; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU10064; ACT_SITE 140; /note=Proton donor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10064 |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->4)-beta-D-glucosidic linkages in beta-D-glucans containing (1->3)- and (1->4)-bonds.; EC=3.2.1.73; |
DNA Binding | |
EC Number | 3.2.1.73 |
Enzyme Function | |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Chain (1); Compositional bias (1); Domain (2); Region (1); Sequence conflict (9); Signal peptide (1) |
Keywords | Glycosidase;Hydrolase;Signal |
Interact With | |
Induction | |
Subcellular Location | |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..27; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 37,942 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda | 3.2.1.73; |