Detail Information for IndEnz0010001824
IED ID IndEnz0010001824
Enzyme Type ID esterase001824
Protein Name Bifunctional acetylxylan esterase/xylanase XynS20E
Includes: Acetylxylan esterase
EC 3.1.1.72
; Endo-1,4-beta-xylanase
Xylanase
EC 3.2.1.8
1,4-beta-D-xylan xylanohydrolase
Gene Name xynS20E
Organism Neocallimastix patriciarum (Rumen fungus)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Fungi incertae sedis Chytridiomycota Chytridiomycota incertae sedis Neocallimastigomycetes Neocallimastigales Neocallimastigaceae Neocallimastix Neocallimastix patriciarum (Rumen fungus)
Enzyme Sequence MRLGVALSTIAVLLTATSARNLDKRQWGWPNFGGGNGGNGGNGGKTINDYKREQGAGRDIHVYAPSNLAPNSPLLLSLHGMDQDPNYQQSNTHWETLADSEGFVVVYPRGGTGMSTWDIQGTKDTQWVSQIIDQMKKEYNIDTKRVYLSGFSMGGMFTYHAMSQIANKIAAFAPCSGPNVFGASKAQRPVPIFHVHGTNDDVLNYQQVEGFLKNYRDQFHCPSQADTKTNYPNRENPNATLYTWGPCDKGVYIKHLKLQGRGHSPSSADIQDIWDFVSQWTVDGPVSASGNGGGNTTPTNPSTGGNGNGNGGGNTTPTNPSTGGNGNGNGGSTDKCSSNITKQGYKCCASNCEVVYTDSDGDWGVENDQWCGCGNRVTVGSGTCSAKILQQGYKCCPSGCIIYYTDEDGTWGVNGEEWCGCGSGSSSTGGGNDAPSSGSGYQGANGTNFCNNAKHSGESVTVTSNKVGDINGIGYELWADSGNNSATFYDDGSFSCSFQRAKDYLCRSGLSFDSTKTHKQIGHIYAEFKLVKQNIQNVDYSYVGIYGWTRNPLVEFYVVDNWLSQWRPGDWVGNKKHGDFTIGGAQYTVYENTRYGPSIDGDTNFKQYFSIRQQPRDCGTIDITAHFEQWEKLGMTMGKMHEAKVLGEAGSNNGGTSGTADFPFAKVYVKN
Enzyme Length 671
Uniprot Accession Number B8YG19
Absorption
Active Site ACT_SITE 152; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 555; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU10062; ACT_SITE 648; /note=Proton donor; /evidence=ECO:0000250
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Deacetylation of xylans and xylo-oligosaccharides.; EC=3.1.1.72; Evidence={ECO:0000269|PubMed:19690850}; CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.; EC=3.2.1.8; Evidence={ECO:0000269|PubMed:19690850};
DNA Binding
EC Number 3.1.1.72; 3.2.1.8
Enzyme Function FUNCTION: Bifunctional acetylxylan esterase/xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Degrades xylan from acetylxylan, beechwood, birchwood, and oat spelt, and releases acetate from 4-methylumbelliferyl acetate and beta-D-xylose tetraacetate. No activity is observed against carboxy methyl cellulose, beta-glucan, p-nitrophenol acetate, p-nitrophenol laurate, p-nitrophenol myristate, p-nitrophenol, palmitate, or beta-naphthol acetate. {ECO:0000269|PubMed:19690850}.
Temperature Dependency BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 58 degrees Celsius for acetylxylan esterase activity, and 49 degrees Celsius for endo-1,4-beta-xylanase activity.;
PH Dependency BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.8 for acetylxylan esterase activity, and 5.8 for endo-1,4-beta-xylanase activity.;
Pathway PATHWAY: Glycan degradation; xylan degradation.
nucleotide Binding
Features Active site (3); Chain (1); Domain (3); Glycosylation (4); Region (2); Signal peptide (1)
Keywords Carbohydrate metabolism;Glycoprotein;Glycosidase;Hydrolase;Polysaccharide degradation;Repeat;Secreted;Signal;Xylan degradation
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19690850}.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..19; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 72,469
Kinetics BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.48 mg/ml for birchwood xylan for endo-1,4-beta-xylanase activity; KM=16.72 mg/ml for birchwood xylan for acetylxylan esterase activity; Vmax=5.15 umol/min/mg enzyme toward birchwood xylan for acetylxylan esterase activity; Vmax=153.27 umol/min/mg enzyme toward birchwood xylan for Endo-1,4-beta-xylanase activity;
Metal Binding
Rhea ID
Cross Reference Brenda 3.1.1.72;