IED ID | IndEnz0011000345 |
Enzyme Type ID | glucanase000345 |
Protein Name |
Endoglucanase N EC 3.2.1.4 Cellulase N Endo-1,4-beta-glucanase N |
Gene Name | celN |
Organism | Pectobacterium atrosepticum (Erwinia carotovora subsp. atroseptica) |
Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Pectobacteriaceae Pectobacterium Pectobacterium atrosepticum (Erwinia carotovora subsp. atroseptica) |
Enzyme Sequence | MWMRRNQIVRKLTLGVVTTVLGMSLSFSALSATPVETHGQLSIENGRLVDEQGKRVQLRGVSSHGLQWFGDYVNKDSMKWLRDDWGINVFRVAMYTAADGYISNPSLANKVKEAVAAAQSLGVYIIIDWHILSDNDPNIYKAQAKTFFAEMAGLYGSSPNVIYEIANEPNGGVTWNGQIRPYALEVTDTIRSKDPDNLIIVGTGTWSQDIHDAADNQLPDPNTLYALHFYAGTHGQFLRDRIDYAQSRGAAIFVSEWGTSDASGNGGPFLPESQTWIDFLNNRGVSWVNWSLTDKSEASAALAPGASKSGGWTEQNLSTSGKFVREQIRAGANLGGGDTPTTPTTPTEPTNPGNGTTGDVVLQYRNVDNNPSDDAIRMAVNIKNTGSTPIKLSDLQVRYYFHDDGKPGANLFVDWANVGPNNIVTSTGTPAASTDKANRYVLVT |
Enzyme Length | 444 |
Uniprot Accession Number | Q59394 |
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 | |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Binding site (5); Chain (1); Compositional bias (1); Domain (1); Region (4); 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 | 48,301 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |