| IED ID | IndEnz0011000347 |
| Enzyme Type ID | glucanase000347 |
| Protein Name |
Endoglucanase 5 EC 3.2.1.4 Cellulase V Endo-1,4-beta-glucanase V Endoglucanase V |
| Gene Name | celV |
| Organism | Pectobacterium carotovorum subsp. carotovorum (Erwinia carotovora subsp. carotovora) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Pectobacteriaceae Pectobacterium Pectobacterium carotovorum (Erwinia carotovora) Pectobacterium carotovorum subsp. carotovorum (Erwinia carotovora subsp. carotovora) |
| Enzyme Sequence | MWMRRNQIVRKLTLGVVTTVLGMSLSFSALSATPVETHGQLSIENGRLVDEQGKRVQLRGISSHGLQWFGDYVNKDSMKWLRDDWGINVFRVAMYTAADGYISNPSLANKVKEAVAAAQSLGVYIIIDWHILSDNDPNIYKAQAKTFFAEMAGLYGSSPNVIYEIANEPNGGVTWNGQIRPYALEVTDTIRSKDPDNLIIVGTGTWSQDIHDAADNQLPDPNTMYALHFYAGTHGQFLRDRIDYAQSRGAAIFVSEWGTSDASGNGGPFLPESQTWIDFLNNRGVSWVNWSLTDKSEASAALAPGASKSGGWTEQNLSTSGKFVREQIRAGANLGGGDTPTTPTEPTNPGNGTTGDVVLQYRNVDNNPSDDAIRMAVNIKNTGSTPIKLSDLQVRYYFHDDGKPGANLFVDWANVGPNNIVTSTGTPAASTDKANRYVLVTFSSGAGSLQPGAETGEVQVRIHAGDWSNVNETNDYSYGANVTSYANWDKITVHDKGTLVWGVEP |
| Enzyme Length | 505 |
| Uniprot Accession Number | Q47096 |
| Absorption | |
| Active Site | ACT_SITE 168; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:O85465; ACT_SITE 256; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:O85465 |
| Activity Regulation | |
| Binding Site | BINDING 64; /note=Substrate; /evidence=ECO:0000250|UniProtKB:O85465; BINDING 95; /note=Substrate; /evidence=ECO:0000250|UniProtKB:O85465; BINDING 130; /note=Substrate; /evidence=ECO:0000250|UniProtKB:O85465; BINDING 230; /note=Substrate; /evidence=ECO:0000250|UniProtKB:O85465; BINDING 290; /note=Substrate; /evidence=ECO:0000250|UniProtKB:O85465 |
| Calcium Binding | |
| catalytic Activity | 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 | 3.2.1.4 |
| Enzyme Function | FUNCTION: Endoglucanase with some exoglucanase activity. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is about 42 degrees Celsius.; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is about 7.0.; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Binding site (5); Chain (1); Compositional bias (1); Domain (1); Region (6); Signal peptide (1) |
| Keywords | Carbohydrate metabolism;Cellulose degradation;Glycosidase;Hydrolase;Polysaccharide degradation;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..31; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 54,900 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |