Detail Information for IndEnz0004000072
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;