| IED ID | IndEnz0008000014 |
| Enzyme Type ID | cellulase000014 |
| Protein Name |
Cellulase CelDZ1 EC 3.2.1.4 |
| Gene Name | celDZ1a |
| Organism | Thermoanaerobacterium sp. |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Clostridia Thermoanaerobacterales Thermoanaerobacterales Family III. Incertae Sedis Thermoanaerobacterium unclassified Thermoanaerobacterium Thermoanaerobacterium sp. |
| Enzyme Sequence | MNKWHINKWYFFVGMLVIFAVIISLILKDTSLTFSSYDREKFPHLIGNSMVKKPSLAGRLKIIEIDGRKTLGDQHGNPIQLRGMSTHGLQWFPQIINNNAFSALSKDWEANVIRLAMYVGEGGYSTDPSVKEKVIEGINLAIKNDMYVIVDWHILNPGDPNAKIYSGAKEFFKEIASKYPNDLHIIYELANEPNPTESDITNDIAGWEKVKKYAEPIIKMLRDMGNENIIIVGNPEWSTRPDLAVNDPIDDKNVMYSAHFYTGSASVWENGNKGHIARNIEKALENGLTVFVTEWGTSEASGDGGPYLNEADEWLEFLNSNNISWVNWSLANKNEASAAFLPTTSLDPGNGKVWAVNQLSLSGEYVRARIKGIPYKPISRETMGK |
| Enzyme Length | 385 |
| Uniprot Accession Number | A0A0U4EBH5 |
| Absorption | |
| Active Site | ACT_SITE 192; /note=Proton donor; /evidence=ECO:0000305|PubMed:26741138; ACT_SITE 294; /note=Nucleophile; /evidence=ECO:0000305|PubMed:26741138 |
| Activity Regulation | ACTIVITY REGULATION: Activity is enhanced by 1mM Mn(2+), but is not affected by 1mM Ca(2+), Mg(2+), Zn(2+), K(+), Na(+) or Li(+). Activity is not inhibited by EDTA (in vitro). {ECO:0000269|PubMed:26741138}. |
| Binding Site | BINDING 87; /note=Substrate; /evidence=ECO:0000250|UniProtKB:O85465; BINDING 118; /note=Substrate; /evidence=ECO:0000250|UniProtKB:O85465; BINDING 153; /note=Substrate; /evidence=ECO:0000250|UniProtKB:O85465; BINDING 261; /note=Substrate; /evidence=ECO:0000250|UniProtKB:O85465; BINDING 328; /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; Evidence={ECO:0000269|PubMed:26741138}; |
| DNA Binding | |
| EC Number | 3.2.1.4 |
| Enzyme Function | FUNCTION: Thermostable endoglucanase that has high activity with soluble polymeric substrates containing beta-1,4-glycosidic bonds, such as carboxymethyl cellulose (CMC) and barley beta-D-glucan (in vitro). Has no activity with cellobiose and filter paper. Has no activity with substrates containing beta-1,3-linked glycans, such as laminarin. Likewise, lacks activity with xylan, galactomannan and pectin. {ECO:0000269|PubMed:26741138}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 70 degrees Celsius. Retains about 85% activity after 24 hours at 65 degrees Celsius. Retains at least 50% activity after 4 hours at 70 degrees Celsius. Rapidly looses activity at 75 degrees Celsius. {ECO:0000269|PubMed:26741138}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5 with carboxymethyl cellulose as substrate. Retains 80% activity at pH 6, and about 50% at pH 7. Inactive at pH values below 4 and above 9. {ECO:0000269|PubMed:26741138}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Binding site (5); Chain (1); Region (3); Transmembrane (1) |
| Keywords | 3D-structure;Carbohydrate metabolism;Cell membrane;Cellulose degradation;Glycosidase;Hydrolase;Membrane;Polysaccharide degradation;Transmembrane;Transmembrane helix |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 5FIP; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 43,215 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=6.1 mg/ml for carboxymethyl cellulose {ECO:0000269|PubMed:26741138}; Note=kcat is 46.3 sec(-1) with carboxymethyl cellulose as substrate. {ECO:0000269|PubMed:26741138}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |