| IED ID | IndEnz0008000012 |
| Enzyme Type ID | cellulase000012 |
| Protein Name |
Cellulose 1,4-beta-cellobiosidase reducing end CelS EC 3.2.1.176 Cellobiohydrolase CelS Cellulase SS Endo-1,4-beta-glucanase Endoglucanase SS EGSS Exocellulase |
| Gene Name | celS Cthe_2089 |
| Organism | Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) (Clostridium thermocellum) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Clostridia Eubacteriales Oscillospiraceae Acetivibrio Acetivibrio thermocellus (Hungateiclostridium thermocellum) (Clostridium thermocellum) Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) (Clostridium thermocellum) |
| Enzyme Sequence | MVKSRKISILLAVAMLVSIMIPTTAFAGPTKAPTKDGTSYKDLFLELYGKIKDPKNGYFSPDEGIPYHSIETLIVEAPDYGHVTTSEAFSYYVWLEAMYGNLTGNWSGVETAWKVMEDWIIPDSTEQPGMSSYNPNSPATYADEYEDPSYYPSELKFDTVRVGSDPVHNDLVSAYGPNMYLMHWLMDVDNWYGFGTGTRATFINTFQRGEQESTWETIPHPSIEEFKYGGPNGFLDLFTKDRSYAKQWRYTNAPDAEGRAIQAVYWANKWAKEQGKGSAVASVVSKAAKMGDFLRNDMFDKYFMKIGAQDKTPATGYDSAHYLMAWYTAWGGGIGASWAWKIGCSHAHFGYQNPFQGWVSATQSDFAPKSSNGKRDWTTSYKRQLEFYQWLQSAEGGIAGGATNSWNGRYEKYPAGTSTFYGMAYVPHPVYADPGSNQWFGFQAWSMQRVMEYYLETGDSSVKNLIKKWVDWVMSEIKLYDDGTFAIPSDLEWSGQPDTWTGTYTGNPNLHVRVTSYGTDLGVAGSLANALATYAAATERWEGKLDTKARDMAAELVNRAWYNFYCSEGKGVVTEEARADYKRFFEQEVYVPAGWSGTMPNGDKIQPGIKFIDIRTKYRQDPYYDIVYQAYLRGEAPVLNYHRFWHEVDLAVAMGVLATYFPDMTYKVPGTPSTKLYGDVNDDGKVNSTDAVALKRYVLRSGISINTDNADLNEDGRVNSTDLGILKRYILKEIDTLPYKN |
| Enzyme Length | 741 |
| Uniprot Accession Number | A3DH67 |
| Absorption | |
| Active Site | ACT_SITE 87; /note=Proton donor; /evidence=ECO:0000250; ACT_SITE 255; /note=Nucleophile; /evidence=ECO:0000250 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by cellobiose and lactose, but not by glucose. {ECO:0000269|PubMed:8597541}. |
| Binding Site | BINDING 76; /note=Substrate; /evidence=ECO:0000250; BINDING 140; /note=Substrate; /evidence=ECO:0000250; BINDING 204; /note=Substrate; /evidence=ECO:0000250; BINDING 241; /note=Substrate; /evidence=ECO:0000250; BINDING 247; /note=Substrate; /evidence=ECO:0000250; BINDING 421; /note=Substrate; /evidence=ECO:0000250; BINDING 520; /note=Substrate; /evidence=ECO:0000250 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and similar substrates, releasing cellobiose from the reducing ends of the chains.; EC=3.2.1.176; Evidence={ECO:0000269|PubMed:7883725}; |
| DNA Binding | |
| EC Number | 3.2.1.176 |
| Enzyme Function | FUNCTION: This enzyme catalyzes the exohydrolysis of 1,4-beta-glucosidic linkages in cellulose with a preference for amorphous or crystalline cellulose over carboxymethyl cellulose. {ECO:0000269|PubMed:7883725}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 70 degrees Celsius. {ECO:0000269|PubMed:7883725}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5-6. {ECO:0000269|PubMed:7883725}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Binding site (7); Chain (1); Domain (1); Metal binding (15); Region (4); Signal peptide (1) |
| Keywords | Calcium;Carbohydrate metabolism;Cellulose degradation;Direct protein sequencing;Glycosidase;Hydrolase;Metal-binding;Polysaccharide degradation;Reference proteome;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..27; /evidence=ECO:0000269|PubMed:8444792 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 83,558 |
| Kinetics | |
| Metal Binding | METAL 679; /note=Calcium 1; /evidence=ECO:0000250; METAL 681; /note=Calcium 1; /evidence=ECO:0000250; METAL 683; /note=Calcium 1; /evidence=ECO:0000250; METAL 684; /note=Calcium 1; via amide nitrogen; /evidence=ECO:0000250; METAL 685; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 690; /note=Calcium 1; /evidence=ECO:0000250; METAL 711; /note=Calcium 2; /evidence=ECO:0000250; METAL 711; /note=Calcium 3; /evidence=ECO:0000250; METAL 712; /note=Calcium 2; via amide nitrogen; /evidence=ECO:0000250; METAL 713; /note=Calcium 3; /evidence=ECO:0000250; METAL 715; /note=Calcium 3; /evidence=ECO:0000250; METAL 717; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 717; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250; METAL 722; /note=Calcium 2; /evidence=ECO:0000250; METAL 722; /note=Calcium 3; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda | 3.2.1.176; |