Detail Information for IndEnz0011000353
IED ID IndEnz0011000353
Enzyme Type ID glucanase000353
Protein Name Endoglucanase Z
EC 3.2.1.4
Avicelase I
Endo-1,4-beta-glucanase
Thermoactive cellulase
Gene Name celZ
Organism Thermoclostridium stercorarium (Clostridium stercorarium)
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Firmicutes Clostridia Eubacteriales Oscillospiraceae Thermoclostridium Thermoclostridium stercorarium (Clostridium stercorarium)
Enzyme Sequence MRKFYSFAIIISLLVTGLFIHTPKAEAAGYNYGEALQKAIMFYEFQRSGKLPENKRDNWRGDSGLNDGADVGLDLTGGWYDAGDHVKFNLPMAYSQTMLAWAAYEAEEALERSGQMGYLLDAIKWVSDYLIKCHPSPNVFYYQVGDGHLDHSWWGPAEVMQMDRPAYKVDLANPGSTVVAEAAAALASAAVVFADRDPAYAATCIQHAKELYNFAEITKSDSGYTAASGFYDSHSGFYDELSWAGVWLYLATGDETYLNKAEQYVAYWGTEPQTNIISYKWAHCWDDVHYGACLLLAKITGKQIYKEAIERHLDYWSVGYNGERVHYTPKGLAWLDSWGSLRYATTTAFLASVYADWEGCSREKAAIYNDFAKQQIDYALGSSGRSYVVGFGVNPPKRPHHRTAHSSWADSMSVPDYHRHVLIGALVGGPGKDDSYTDDINNYINNEVACDYNAGFVGALAKMYEDYGGSPIPDLNAFEEITNDEFFVMAGINASGQNFIEIKALLHNQSGWPARVADKLSFRYFVDLTELIEAGYSASDVTITTNYNAGAKVTGLHPWNEAENIYYVNVDFTGTKIYPGGQSAYRKEVQFRIAAPQNTNFWNNDNDYSFRDIKGVTSGNTVKTVYIPVYDDGVLVFGVEPEGGSGENNSSISITNATFDKNPAKQENIQVVMNLNGNTLNGIKYGNTYLREGTDYTVSGDTVTILKSFLNSFDTSTVQLIFDFSAGRDPVLTVNIIDTTTSASIVPTTADFDKNPDASRDVKVKLVPNGNTLLAVKKDGEALVLGRDYSIDGDEVTIFREYLADQPVGRVTLTFDFDRGTDPVLTINITDSRQVETGVIQIQMFNGNTSDKTNGIMPRYRLTNTGTTPIRLSDVKIRYYYTIDGEKDQNFWCDWSSVGSNNITGTFVKMAEPKEGADYYLETGFTDGAGYLQPNQSIEVQNRFSKADWTDYIQTNDYSFSTNTSYGSNDRITVYISGVLVSGIEP
Enzyme Length 986
Uniprot Accession Number P23659
Absorption
Active Site ACT_SITE 84; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU10140; ACT_SITE 400; /evidence=ECO:0000255|PROSITE-ProRule:PRU10059; ACT_SITE 438; /evidence=ECO:0000255|PROSITE-ProRule:PRU10060; ACT_SITE 447; /evidence=ECO:0000255|PROSITE-ProRule:PRU10060
Activity Regulation
Binding Site
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 (4); Chain (1); Domain (2); Repeat (2); Signal peptide (1)
Keywords Carbohydrate metabolism;Cellulose degradation;Direct protein sequencing;Glycosidase;Hydrolase;Polysaccharide degradation;Repeat;Signal
Interact With
Induction
Subcellular Location
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..25; /evidence=ECO:0000269|PubMed:2250652
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 109,512
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda