Detail Information for IndEnz0008000260
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