| IED ID | IndEnz0008000035 |
| Enzyme Type ID | cellulase000035 |
| Protein Name |
Xyloglucan-specific endo-beta-1,4-glucanase BoGH9A EC 3.2.1.151 Glycosyl hydrolase family protein 9A BoGH9A |
| Gene Name | BACOVA_02649 |
| Organism | Bacteroides ovatus (strain ATCC 8483 / DSM 1896 / JCM 5824 / BCRC 10623 / CCUG 4943 / NCTC 11153) |
| Taxonomic Lineage | cellular organisms Bacteria FCB group Bacteroidetes/Chlorobi group Bacteroidetes Bacteroidia Bacteroidales Bacteroidaceae Bacteroides Bacteroides ovatus Bacteroides ovatus (strain ATCC 8483 / DSM 1896 / JCM 5824 / BCRC 10623 / CCUG 4943 / NCTC 11153) |
| Enzyme Sequence | MKIVRYIALFGILSGLAVACTPSTSVIPNDAIRLNQLGYYPNQEKIAVVDSGKVEEFVIWDAVSGEQVFVGKSLYTAKSAWSDKTRTTLDFSAVTTPGKYILKVNGASVTFLIKDSVLSPLADAALKSFYYQRTAMPIEEQYAGQWHRMAGHPDNHVLIHPSAASPDRPAGTIVSSSKGWYDAGDYNKYIVNSGYSIGLMQSIYQLFLDYFSRQKINIPESNNHTPDLLDEMQFNLDWMLTMQDPEDGGVYHKLTTPFFEGFVKPVDCKQQRYVVQKSVTAALDFAAVMAQSSRLFASYEEDYPGFSKRALLAAEKAYAWAEKHPEAYYNQNLLNQKYQPAIATGEYGDTHADDEFFWAASELYFSTGKEIYREEAIKKAPQIYTAPGWGNTFALGIFAWLQPGRELNEADRRFADSLKTELLKYADKVIEGAEQTPFHAPYGNDAKDFFWGCLAEKCMNQGVSLMYAYLQTGKDVYLTNAYRNMDYILGRNATGFCYVTGLGTKSPKHPHHRLSASDDIEDPIPGFLVGGPNPGQQDGAFYPTASPDESYVDTEDSYASNEVAINWNAALVALASSLDALAVYSVK |
| Enzyme Length | 587 |
| Uniprot Accession Number | A7LXT3 |
| Absorption | |
| Active Site | ACT_SITE 185; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU10140; ACT_SITE 511; /evidence=ECO:0000255|PROSITE-ProRule:PRU10059; ACT_SITE 553; /evidence=ECO:0000255|PROSITE-ProRule:PRU10060; ACT_SITE 562; /note=Proton donor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10060 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Xyloglucan + H(2)O = xyloglucan oligosaccharides.; EC=3.2.1.151; Evidence={ECO:0000269|PubMed:24463512}; |
| DNA Binding | |
| EC Number | 3.2.1.151 |
| Enzyme Function | FUNCTION: Catalyzes endohydrolysis of 1,4-beta-D-glucosidic linkages in xyloglucan with retention of the beta-configuration of the glycosyl residues in xyloglucan degradation. Cleaves the backbone of the 3 major types of natural xyloglucans (seed galactoxyloglucan from tamarind kernel, dicot fucogalactoxyloglucan from lettuce leaves, and solanaceous arabinogalactoxyloglucan from tomato fruit), to produce xyloglucan oligosaccharides. May be superfluous in xyloglucan degradation compared to BoGH5A (AC A7LXT7), the other Xyloglucan-specific endo-beta-1,4-glucanase. {ECO:0000269|PubMed:24463512}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.0-7.0. {ECO:0000269|PubMed:24463512}; |
| Pathway | PATHWAY: Glucan metabolism; xyloglucan degradation. {ECO:0000269|PubMed:24463512}. |
| nucleotide Binding | |
| Features | Active site (4); Beta strand (14); Chain (1); Helix (24); Lipidation (2); Signal peptide (1); Turn (6) |
| Keywords | 3D-structure;Carbohydrate metabolism;Cell outer membrane;Glycosidase;Hydrolase;Lipoprotein;Membrane;Palmitate;Polysaccharide degradation;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000305}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}. Note=Cell outer membrane localization is predicted by analogy with the archetypal sus locus. {ECO:0000269|PubMed:24463512}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..19; /evidence=ECO:0000255|PROSITE-ProRule:PRU00303 |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 6DHT; |
| Mapped Pubmed ID | 30668971; |
| Motif | |
| Gene Encoded By | |
| Mass | 65,325 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |