Detail Information for IndEnz0004000179
IED ID IndEnz0004000179
Enzyme Type ID xylanase000179
Protein Name Bifunctional endo-1,4-beta-xylanase XylA
EC 3.2.1.8
Gene Name xynA
Organism Ruminococcus flavefaciens
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Firmicutes Clostridia Eubacteriales Oscillospiraceae Ruminococcus Ruminococcus flavefaciens
Enzyme Sequence MKLSKIKKVLSGTVSALMIASAAPVVASAADQQTRGNVGGYDYEMWNQNGQGQASMNPGAGSFTCSWSNIENFLARMGKNYDSQKKNYKAFGNIVLTYDVEYTPRGNSYMCVYGWTRNPLMEYYIVEGWGDWRPPGNDGEVKGTVSANGNTYDIRKTMRYNQPSLDGTATFPQYWSVRQTSGSANNQTNYMKGTIDVTKHFDAWSAAGLDMSGTLYEVSLNIEGYRSNGSANVKSVSVTQGGSSDNGGQQQNNDWNQQNNNQQQNNDWNNWGQQNNDWNQWNNQGQQNNDWNNWGQQNNDWNQWNNQGQQQNNDWNNWGQQNNDWNQWNNQGQQQNNDWNNWGQQNNDWNQWNNQGQQQNNDWNNWGQQNNDWNQWNNQNNNQQNAWNGWDNNNNWNQNNQQQNNWDWNNQNNWNNNQQQNNDWNQWNNQNNWNNNQQQNNDWNQWNNQGQQNNDWNQWNNQNNWNQNNNQQNAWNGWDNNNNWNQWDQNNQWNNQQQNNTWDWNNQNNWNNNQQNNDWNQWNNQGQQQNNDWNQWNNQNNNQNNGWDWNNQNNWNQNNNQQNAWNGWDNNNNWNQWGGQNNDWNNQQQNNDWNQWNNQGQQQNNDWNNQNNWNQGQQNNNNSAGSSDSLKGAFSKYFKIGTSVSPHELNSGADFLKKHYNSITPENELKPESILDQGACQQKGNNVNTQISLSRAAQTLKFCEQNGIALRGHTFVWYSQTPDWFFRENFSQNGAYVSKDIMNQRLESMIKNTFAALKSQYPNLDVYSYDVCNELFLNNGGGMRGADNSNWVKIYGDDSFVINAFKYARQYAPAGCKLYLNDYNEYIPAKTNDIYNMAMKLKQLGYIDGIGMQSHLATNYPDANTYETALKKFLSTGLEVQITELDITCTNSAEQADLYEKIFKLAMQNSAQIPAVTIWGTQDTVSWRSSQNPLLFSAGYQPKPAYDRVMALAK
Enzyme Length 954
Uniprot Accession Number P29126
Absorption
Active Site ACT_SITE 122; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 223; /note=Proton donor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10063; ACT_SITE 774; /note=Proton donor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10063; ACT_SITE 884; /note=Nucleophile; /evidence=ECO:0000250
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;
DNA Binding
EC Number 3.2.1.8
Enzyme Function FUNCTION: Xylanase domain releases more xylo-oligosaccharides and GH10 domain more xylose.
Temperature Dependency
PH Dependency
Pathway PATHWAY: Glycan degradation; xylan degradation.
nucleotide Binding
Features Active site (4); Chain (1); Domain (2); Region (1); Signal peptide (1)
Keywords Carbohydrate metabolism;Glycosidase;Hydrolase;Multifunctional enzyme;Polysaccharide degradation;Repeat;Signal;Xylan degradation
Interact With
Induction
Subcellular Location
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..27; /note="Or 28, or 29"; /evidence="ECO:0000255"
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 111,362
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda