Detail Information for IndEnz0011000348
IED ID IndEnz0011000348
Enzyme Type ID glucanase000348
Protein Name Endoglucanase 6
EC 3.2.1.4
Cellulase V1
Endo-1,4-beta-glucanase V1
Endoglucanase V1
Gene Name celV1 W5S_2582
Organism Pectobacterium parmentieri
Taxonomic Lineage cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Pectobacteriaceae Pectobacterium Pectobacterium parmentieri
Enzyme Sequence MWLRRKQIVRKLTLGVVTTMLGMSLSFSALSATPVETHGQLSIENGRLVDEQGKRVQLRGISSNGLQWVGDYVNKDSMKWLRDDWGINVFRVAMYTAENGYIANPSLANKVKEAVAAAQGLGVYIIIDWHTLSDNDPNTYKAQAKIFFAEMAGLYGNSPNVIYEIANEPNGSVTWNGQIRPYALEVTDTIRSKDPDNLIIVGSGTWSQDIHDAADNQLPDPNTLYALHFYAGTHGQFLRDRIDYAQSRGAAIFVSEWGTSDASGNGGPFLPESQTWIDFLNNRGISWVNWSLSDKSETSAALVAGASKSGGWTEQNLSTSGKFVREQIRAGAGLSGGDTPTMPTEPTNPGNGTTGDIVLQYRNVDNNPSDDAIRMAFNIKNTGSTPIKLSDLQVRYYFHDDGKPGANLFVDWANVGPNNIVTSTGTPAASTDKANRYVLVTFASGAGSLQPGAETGEVQVRIHAGDWSNVNETNDYSYGPNVTSYTNWDKITVHDKGTLVWGTEP
Enzyme Length 505
Uniprot Accession Number Q59395
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 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 (4); Chain (1); Compositional bias (1); Domain (1); Region (6); Sequence conflict (2); 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 55,020
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda