| IED ID | IndEnz0004000072 |
| Enzyme Type ID | xylanase000072 |
| Protein Name |
Endo-1,4-beta-xylanase Y Xylanase Y EC 3.2.1.8 1,4-beta-D-xylan xylanohydrolase Y XylY |
| Gene Name | xynY |
| Organism | Acetivibrio thermocellus (Hungateiclostridium thermocellum) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Clostridia Eubacteriales Oscillospiraceae Acetivibrio Acetivibrio thermocellus (Hungateiclostridium thermocellum) |
| Enzyme Sequence | MKNKRVLAKITALVVLLGVFFVLPSNISQLYADYEVVHDTFEVNFDGWCNLGVDTYLTAVENEGNNGTRGMMVINRSSASDGAYSEKGFYLDGGVEYKYSVFVKHNGTGTETFKLSVSYLDSETEEENKEVIATKDVVAGEWTEISAKYKAPKTAVNITLSITTDSTVDFIFDDVTITRKGMAEANTVYAANAVLKDMYANYFRVGSVLNSGTVNNSSIKALILREFNSITCENEMKPDATLVQSGSTNTNIRVSLNRAASILNFCAQNNIAVRGHTLVWHSQTPQWFFKDNFQDNGNWVSQSVMDQRLESYIKNMFAEIQRQYPSLNLYAYDVVNEAVSDDANRTRYYGGAREPGYGNGRSPWVQIYGDNKFIEKAFTYARKYAPANCKLYYNDYNEYWDHKRDCIASICANLYNKGLLDGVGMQSHINADMNGFSGIQNYKAALQKYINIGCDVQITELDISTENGKFSLQQQADKYKAVFQAAVDINRTSSKGKVTAVCVWGPNDANTWLGSQNAPLLFNANNQPKPAYNAVASIIPQSEWGDGNNPAGGGGGGKPEEPDANGYYYHDTFEGSVGQWTARGPAEVLLSGRTAYKGSESLLVRNRTAAWNGAQRALNPRTFVPGNTYCFSVVASFIEGASSTTFCMKLQYVDGSGTQRYDTIDMKTVGPNQWVHLYNPQYRIPSDATDMYVYVETADDTINFYIDEAIGAVAGTVIEGPAPQPTQPPVLLGDVNGDGTINSTDLTMLKRSVLRAITLTDDAKARADVDKNGSINSTDVLLLSRYLLRVIDKFPVAENPSSSFKYESAVQYRPAPDSYLNPCPQAGRIVKETYTGINGTKSLNVYLPYGYDPNKKYNIFYLMHGGGENENTIFSNDVKLQNILDHAIMNGELEPLIVVTPTFNGGNCTAQNFYQEFRQNVIPFVESKYSTYAESTTPQGIAASRMHRGFGGFSMGGLTTWYVMVNCLDYVAYFMPLSGDYWYGNSPQDKANSIAEAINRSGLSKREYFVFAATGSDHIAYANMNPQIEAMKALPHFDYTSDFSKGNFYFLVAPGATHWWGYVRHYIYDALPYFFHE |
| Enzyme Length | 1077 |
| Uniprot Accession Number | P51584 |
| Absorption | |
| Active Site | ACT_SITE 337; /note=Proton donor; /evidence=ECO:0000250; ACT_SITE 460; /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; |
| DNA Binding | |
| EC Number | 3.2.1.8 |
| Enzyme Function | |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 75 degrees Celsius.; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.8.; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (54); Chain (1); Domain (4); Helix (31); Region (1); Signal peptide (1); Turn (10) |
| Keywords | 3D-structure;Carbohydrate metabolism;Glycosidase;Hydrolase;Polysaccharide degradation;Repeat;Signal;Xylan degradation |
| Interact With | Q06851 |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..26; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (19) |
| Cross Reference PDB | 1DYO; 1GKK; 1GKL; 1H6X; 1H6Y; 1OHZ; 1WB4; 1WB5; 1WB6; 2CCL; 2W5F; 2WYS; 2WZE; 3ZI7; 4BAG; 4H35; 5FXM; 6FJ4; 6Y8G; |
| Mapped Pubmed ID | 10819965; 11478884; 11738044; 14623971; 15681871; 17360613; 18678939; 20682344; 23178456; 23656378; 27487827; 29979188; 32381789; |
| Motif | |
| Gene Encoded By | |
| Mass | 119,673 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.2.1.8; |