| IED ID | IndEnz0008000260 |
| Enzyme Type ID | cellulase000260 |
| Protein Name |
Cellulose 1,4-beta-cellobiosidase EC 3.2.1.91 |
| Gene Name | celK |
| Organism | Acetivibrio thermocellus (Hungateiclostridium thermocellum) (Clostridium thermocellum) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Clostridia Eubacteriales Oscillospiraceae Acetivibrio Acetivibrio thermocellus (Hungateiclostridium thermocellum) (Clostridium thermocellum) |
| Enzyme Sequence | MNFRRMLCAAIVLTIVLSIMLPSTVFALEDKSSKLPDYKNDLLYERTFDEGLCFPWHTCEDSGGKCDFAVVDVPGEPGNKAFRLTVIDKGQNKWSVQMRHRGITLEQGHTYTVRFTIWSDKSCRVYAKIGQMGEPYTEYWNNNWNPFNLTPGQKLTVEQNFTMNYPTDDTCEFTFHLGGELAAGTPYYVYLDDVSLYDPRFVKPVEYVLPQPDVRVNQVGYLPFAKKYATVVSSSTSPLKWQLLNSANQVVLEGNTIPKGLDKDSQDYVHWIDFSNFKTEGKGYYFKLPTVNSDTNYSHPFDISADIYSKMKFDALAFFYHKRSGIPIEMPYAGGEQWTRPAGHIGIEPNKGDTNVPTWPQDDEYAGRPQKYYTKDVTGGWYDAGDHGKYVVNGGIAVWTLMNMYERAKIRGIANQGAYKDGGMNIPERNNGYPDILDEARWEIEFFKKMQVTEKEDPSIAGMVHHKIHDFRWTALGMLPHEDPQPRYLRPVSTAATLNFAATLAQSARLWKDYDPTFAADCLEKAEIAWQAALKHPDIYAEYTPGSGGPGGGPYNDDYVGDEFYWAACELYVTTGKDEYKNYLMNSPHYLEMPAKMGENGGANGEDNGLWGCFTWGTTQGLGTITLALVENGLPATDIQKARNNIAKAADRWLENIEEQGYRLPIKQAEDERGGYPWGSNSFILNQMIVMGYAYDFTGNSKYLDGMQDGMSYLLGRNGLDQSYVTGYGERPLQNPHDRFWTPQTSKKFPAPPPGIIAGGPNSRFEDPTITAAVKKDTPPQKCYIDHTDSWSTNEITVNWNAPFAWVTAYLDEIDLITPPGGVDPEEPEVIYGDCNGDGKVNSTDAVALKRYILRSGISINTDNADVNADGRVNSTDLAILKRYILKEIDVLPHK |
| Enzyme Length | 895 |
| Uniprot Accession Number | P0C2S1 |
| Absorption | |
| Active Site | ACT_SITE 386; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU10140; ACT_SITE 737; /evidence=ECO:0000255|PROSITE-ProRule:PRU10059; ACT_SITE 786; /evidence=ECO:0000255|PROSITE-ProRule:PRU10060; ACT_SITE 795; /evidence=ECO:0000255|PROSITE-ProRule:PRU10060 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by cellobiose. {ECO:0000269|PubMed:10464199}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing cellobiose from the non-reducing ends of the chains.; EC=3.2.1.91; Evidence={ECO:0000269|PubMed:10464199}; |
| DNA Binding | |
| EC Number | 3.2.1.91 |
| Enzyme Function | |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Retains 97% of original activity when incubated for 200 hours at 60 degrees Celsius. {ECO:0000269|PubMed:10464199}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.0. {ECO:0000269|PubMed:10464199}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (4); Beta strand (12); Chain (1); Domain (2); Helix (3); Region (2); Signal peptide (1) |
| Keywords | 3D-structure;Carbohydrate metabolism;Cellulose degradation;Direct protein sequencing;Glycosidase;Hydrolase;Polysaccharide degradation;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10464199, ECO:0000269|PubMed:8664281}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..27; /evidence=ECO:0000269|PubMed:8664281 |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 3P6B; |
| Mapped Pubmed ID | 21543854; |
| Motif | |
| Gene Encoded By | |
| Mass | 100,712 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.67 uM for PNP-cellobioside {ECO:0000269|PubMed:10464199}; Vmax=15.1 umol/min/mg enzyme {ECO:0000269|PubMed:10464199}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |