| IED ID | IndEnz0008000533 |
| Enzyme Type ID | cellulase000533 |
| Protein Name |
Endo-1,4-beta-xylanase A EC 3.2.1.8 1,4-beta-D-xylan xylanohydrolase A |
| Gene Name | xynA1 xynA Pjdr2_0221 |
| Organism | Paenibacillus sp. (strain JDR-2) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Paenibacillaceae Paenibacillus unclassified Paenibacillus Paenibacillus sp. (strain JDR-2) |
| Enzyme Sequence | MSRSLKKFVSILLAAALLIPIGRLAPVAEAAENPTIVYHEDFAIDKGKAIQSGGASLTQVTGKVFDGNNDGSALYVSNRANTWDAADFKFADIGLQNGKTYTVTVKGYVDQDATVPSGAQAFLQAVDSNNYGFLASANFAAGTAFTLTKEFTVDTSVSTQLRVQSSEEGKAVPFYIGDILITANPTTTTNTVYHEDFATDKGKAVQSGGANLAQVADKVFDGNDDGKALYVSNRANTWDAADFKFADIGLQNGKTYTVTVKGYVDQDATVPSGAQAFLQAVDSNNYGFLASANFAARSAFTLTKEFTVDTSVSTQLRVQSSEEGKAVPFYIGDILITETVNSGGGQEDPPRPPALPFNTITFEDQTAGGFTGRAGTETLTVTNESNHTADGSYSLKVEGRTTSWHGPSLRVEKYVDKGYEYKVTAWVKLLSPETSTKLELASQVGDGGSANYPSLASKTITAADGWVQLQGNYRYNSVGGEYLTIYVQSSNATASYYIDDISFESTGSGPVGIQKDLAPLKDVYKNDFLIGNAISAEDLEGTRLELLKMHHDVVTAGNAMKPDALQPTKGNFTFTAADAMIDKVLAEGMKMHGHVLVWHQQSPAWLNTKKDDNNNTVPLGRDEALDNLRTHIQTVMKHFGNKVISWDVVNEAMNDNPSNPADYKASLRQTPWYQAIGSDYVEQAFLAAREVLDENPSWNIKLYYNDYNEDNQNKATAIYNMVKDINDRYAAAHNGKLLIDGVGMQGHYNINTNPDNVKLSLEKFISLGVEVSVSELDVTAGNNYTLPENLAVGQAYLYAQLFKLYKEHADHIARVTFWGMDDNTSWRAENNPLLFDKNLQAKPAYYGVIDPDKYMEEHAPESKDANQAEAQYGTPVIDGTVDSIWSNAQAMPVNRYQMAWQGATGTAKALWDDQNLYVLIQVSDSQLNKANENAWEQDSVEVFLDQNNGKTTFYQNDDGQYRVNFDNETSFSPASIAAGFESQTKKTANSYTVELKIPLTAVTPANQKKLGFDVQINDATDGARTSVAAWNDTTGNGYQDTSVYGELTLAGKGTGGTGTVGTTVPQTGNVVKNPDGSTTLKPEVKTTNGNAVGTVTGDDLKKALDQAAPAAGGKKQVIIDVPLQANAATYAVQLPTQSLKSQDGYQLTAKIANAFIQIPSNMLANTNVTTDQVSIRVAKASLDNVDAATRELIGNRPVIDLSLVAGGNVIAWNNPTAPVTVAVPYAPTAEELKHPEHILIWYIDGSGKATPVPNSRYDAALGAVVFQTTHFSTYAAVSVFTTFGDLAKVPWAKEAIDAMASRGVIKGTGENTFSPAASIKRADFIALLVRALELHGTGTTDTAMFSDVPANAYYYNELAVAKQLGIATGFEDNTFKPDSSISRQDMMVLTTRALAVLGKQLPAGGSLNAFSDAASVAGYAQDSVAALVKAGVVQGSGSKLAPNDQLTRAEAAVILYRIWKLQ |
| Enzyme Length | 1462 |
| Uniprot Accession Number | C6CRV0 |
| Absorption | |
| Active Site | ACT_SITE 651; /note=Proton donor; /evidence=ECO:0000250; ACT_SITE 706; /evidence=ECO:0000250; ACT_SITE 775; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU10061 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.; EC=3.2.1.8; Evidence={ECO:0000269|PubMed:16461704}; |
| DNA Binding | |
| EC Number | 3.2.1.8 |
| Enzyme Function | FUNCTION: Catalyzes the depolymerization of methylglucuronoxylan (MeGAXn), a beta-1,4 xylan in which 10% to 20% of the xylose residues are substituted with alpha-1,2-4-O-methylglucuronate (MeGA) residues, which is predominant in hemicellulose fractions of hardwood and crop residues. Generates xylobiose (X2) and aldotetrauronate (MeGAX3) as the predominant products of MeGAXn hydrolysis; these products are then directly assimilated by the bacterium for subsequent metabolism. Thus, allows the bacterium to efficiently use polymeric MeGAXn as a growth substrate. {ECO:0000269|PubMed:16461704}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 45 degrees Celsius with sweet gum methylglucuronoxylan as substrate. {ECO:0000269|PubMed:16461704}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5 with sweet gum methylglucuronoxylan as substrate. {ECO:0000269|PubMed:16461704}; |
| Pathway | PATHWAY: Glycan degradation; xylan degradation. |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (13); Chain (1); Domain (7); Helix (18); Sequence conflict (2); Signal peptide (1); Turn (3) |
| Keywords | 3D-structure;Carbohydrate metabolism;Cell wall;Glycosidase;Hydrolase;Polysaccharide degradation;Repeat;Secreted;Signal;Xylan degradation |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:16461704}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..30; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (3) |
| Cross Reference PDB | 3RDK; 3RO8; 4E4P; |
| Mapped Pubmed ID | 23000703; |
| Motif | |
| Gene Encoded By | |
| Mass | 157,322 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Vmax=8.0 umol/min/mg enzyme with sweet gum methylglucuronoxylan as substrate {ECO:0000269|PubMed:16461704}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |