| IED ID | IndEnz0005001016 |
| Enzyme Type ID | lipase001016 |
| Protein Name |
Cellulase/esterase CelE CtCel5C-CE2 Includes: Cellulase E EC 3.2.1.4 CtCel5C Endo-1,4-beta-glucanase E EGE Endoglucanase E ; Acetylxylan esterase / glucomannan deacetylase EC 3.1.1.- EC 3.1.1.72 CtCE2 |
| Gene Name | celE Cthe_0797 |
| Organism | Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) (Hungateiclostridium thermocellum) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Clostridia Eubacteriales Oscillospiraceae Acetivibrio Acetivibrio thermocellus (Hungateiclostridium thermocellum) Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) (Hungateiclostridium thermocellum) |
| Enzyme Sequence | MKKIVSLVCVLVMLVSILGSFSVVAASPVKGFQVSGTKLLDASGNELVMRGMRDISAIDLVKEIKIGWNLGNTLDAPTETAWGNPRTTKAMIEKVREMGFNAVRVPVTWDTHIGPAPDYKIDEAWLNRVEEVVNYVLDCGMYAIINVHHDNTWIIPTYANEQRSKEKLVKVWEQIATRFKDYDDHLLFETMNEPREVGSPMEWMGGTYENRDVINRFNLAVVNTIRASGGNNDKRFILVPTNAATGLDVALNDLVIPNNDSRVIVSIHAYSPYFFAMDVNGTSYWGSDYDKASLTSELDAIYNRFVKNGRAVIIGEFGTIDKNNLSSRVAHAEHYAREAVSRGIAVFWWDNGYYNPGDAETYALLNRKTLSWYYPEIVQALMRGAGVEPLVSPTPTPTLMPTPSPTVTANILYGDVNGDGKINSTDCTMLKRYILRGIEEFPSPSGIIAADVNADLKINSTDLVLMKKYLLRSIDKFPAEDSQTPDEDNPGILYNGRFDFSDPNGPKCAWSGSNVELNFYGTEASVTIKSGGENWFQAIVDGNPLPPFSVNATTSTVKLVSGLAEGAHHLVLWKRTEASLGEVQFLGFDFGSGKLLAAPKPLERKIEFIGDSITCAYGNEGTSKEQSFTPKNENSYMSYAAITARNLNASANMIAWSGIGLTMNYGGAPGPLIMDRYPYTLPYSGVRWDFSKYVPQVVVINLGTNDFSTSFADKTKFVTAYKNLISEVRRNYPDAHIFCCVGPMLWGTGLDLCRSYVTEVVNDCNRSGDLKVYFVEFPQQDGSTGYGEDWHPSIATHQLMAERLTAEIKNKLGW |
| Enzyme Length | 814 |
| Uniprot Accession Number | P10477 |
| Absorption | |
| Active Site | ACT_SITE 193; /note=Proton donor; for cellulase activity; /evidence=ECO:0000250; ACT_SITE 316; /note=Nucleophile; for cellulase activity; /evidence=ECO:0000250|UniProtKB:A7LXT7; ACT_SITE 612; /note=Nucleophile; for esterase activity; /evidence=ECO:0000305|PubMed:19338387 |
| Activity Regulation | ACTIVITY REGULATION: Esterase activity of the CE2 module is inhibited when this domain binds to cellohexaose or beta-glucan. {ECO:0000269|PubMed:19338387}. |
| 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; Evidence={ECO:0000269|PubMed:1991028, ECO:0000269|PubMed:3066698}; CATALYTIC ACTIVITY: Reaction=Deacetylation of xylans and xylo-oligosaccharides.; EC=3.1.1.72; Evidence={ECO:0000269|PubMed:19338387}; |
| DNA Binding | |
| EC Number | 3.2.1.4; 3.1.1.-; 3.1.1.72 |
| Enzyme Function | FUNCTION: Multifunctional enzyme involved in the degradation of plant cell wall polysaccharides. Displays endoglucanase activity against carboxymethyl cellulose (CMC) and barley beta-glucan (PubMed:3066698, PubMed:1991028). Also catalyzes the deacetylation of acetylated birchwood xylan and glucomannan, with a preference for the latter, and of the synthetic substrate 4-nitrophenyl acetate (4-NPAc) (PubMed:19338387). {ECO:0000269|PubMed:19338387, ECO:0000269|PubMed:1991028, ECO:0000269|PubMed:3066698}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Glycan metabolism; cellulose degradation. {ECO:0000269|PubMed:3066698}.; PATHWAY: Glycan degradation; xylan degradation. {ECO:0000269|PubMed:19338387}. |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (14); Chain (1); Domain (1); Helix (13); Metal binding (15); Mutagenesis (3); Region (2); Sequence conflict (1); Signal peptide (1); Site (3); Turn (2) |
| Keywords | 3D-structure;Calcium;Carbohydrate metabolism;Cellulose degradation;Direct protein sequencing;Glycosidase;Hydrolase;Metal-binding;Multifunctional enzyme;Polysaccharide degradation;Reference proteome;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..34; /evidence=ECO:0000269|PubMed:3066698 |
| Structure 3D | X-ray crystallography (3) |
| Cross Reference PDB | 2WAB; 2WAO; 4IM4; |
| Mapped Pubmed ID | 33454012; |
| Motif | |
| Gene Encoded By | |
| Mass | 90,230 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=165 uM for 4-nitrophenyl acetate {ECO:0000269|PubMed:19338387}; KM=2.7 mM for acetylated birchwood xylan {ECO:0000269|PubMed:19338387}; KM=0.019 mM for acetylated glucomannan {ECO:0000269|PubMed:19338387}; Note=kcat is 7032 min(-1) for the deacetylation of 4-nitrophenyl acetate. kcat is 12 min(-1) for the deacetylation of birchwood xylan. kcat is 1.1 min(-1) for the deacetylation of glucomannan. {ECO:0000269|PubMed:19338387}; |
| Metal Binding | METAL 415; /note=Calcium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU01102; METAL 417; /note=Calcium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU01102; METAL 419; /note=Calcium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU01102; METAL 420; /note=Calcium 1; via amide nitrogen; /evidence=ECO:0000255|PROSITE-ProRule:PRU01102; METAL 421; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000255|PROSITE-ProRule:PRU01102; METAL 426; /note=Calcium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU01102; METAL 451; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU01102; METAL 451; /note=Calcium 3; /evidence=ECO:0000255|PROSITE-ProRule:PRU01102; METAL 452; /note=Calcium 2; via amide nitrogen; /evidence=ECO:0000255|PROSITE-ProRule:PRU01102; METAL 453; /note=Calcium 3; /evidence=ECO:0000255|PROSITE-ProRule:PRU01102; METAL 455; /note=Calcium 3; /evidence=ECO:0000255|PROSITE-ProRule:PRU01102; METAL 457; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000255|PROSITE-ProRule:PRU01102; METAL 457; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000255|PROSITE-ProRule:PRU01102; METAL 462; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU01102; METAL 462; /note=Calcium 3; /evidence=ECO:0000255|PROSITE-ProRule:PRU01102 |
| Rhea ID | |
| Cross Reference Brenda | 3.2.1.4; |