Detail Information for IndEnz0008000530
IED ID IndEnz0008000530
Enzyme Type ID cellulase000530
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) (Clostridium thermocellum)
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Firmicutes Clostridia Eubacteriales Oscillospiraceae Acetivibrio Acetivibrio thermocellus (Hungateiclostridium thermocellum) (Clostridium 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;