| IED ID | IndEnz0004000162 |
| Enzyme Type ID | xylanase000162 |
| Protein Name |
GH30 family xylanase EC 3.2.1.- |
| Gene Name | Xyn30A MYCTH_38558 |
| Organism | Myceliophthora thermophila (strain ATCC 42464 / BCRC 31852 / DSM 1799) (Sporotrichum thermophile) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Sordariomycetes Sordariomycetidae Sordariales Chaetomiaceae Thermothelomyces Thermothelomyces thermophilus (Myceliophthora thermophila) Myceliophthora thermophila (strain ATCC 42464 / BCRC 31852 / DSM 1799) (Sporotrichum thermophile) |
| Enzyme Sequence | MYSLLIALLCAGTAVDAQALQQRQAGTTLTVDLSTTYQRIDGFGTSEAFQRAVQMSRLPEEGQRRALDVLFSTTNGAGLSILRNGIGSSPDMSSDHMVSIAPKSPGSPNNPLIYSWDGSDNKQLWVSQEAVHTYGVKTIYADAWSAPGYMKTNGNDANGGTLCGLSGAQCASGDWRQAYADYLTKYVEFYQESNVTVTHLGFINEPELTTSYASMRFSASQAAEFIRILYPTIQKSNLTYKPTIACCDAEGWNSQAGMLGALSSVNSMFGLVTAHAYTSQPGFSMNTPHPVWMTEAADLQGAWTSAWYSYGGAGEGWTWANNVYNAIVNGNASAYLYWIGAQTGNTNSHMVHIDANAGTVEPSKRLWALGQWSRFVRPGARRVAVSGASGSLRTAAFRNEDGSVAVVVINSGGDAAVNVRLASSSSADQQPASAKAWATDNSRAIEEIQASFADGVATVNVPSRSMTTVVLYPAADA |
| Enzyme Length | 477 |
| Uniprot Accession Number | G2Q1N4 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Activity is enhanced by 10 mM Co(2+), Cu 2(2+) and Mn(2+) to levels as high as 44% (PubMed:31110561). Partial inhibition of activity from 5 to 15% is observed in the presence of the following compouinds at a centration of 10 mM (from higher inhibition to lower): EDTA > Mg(2+) > urea, Zn(2+) > Fe(3+) (PubMed:31110561). {ECO:0000269|PubMed:31110561}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.2.1.- |
| Enzyme Function | FUNCTION: Xylanase exhibiting endo- and exo-xylanase activity (PubMed:31110561). Shows the highest activity toward beechwood glucuronoxylan, which consists of a beta-1,4-linked xylose backbone decorated with the methylated form of D-glucuronic acid (MeGlcA) attached directly to the main chain at xylose C2 (PubMed:31110561). Acts also against wheat arabinoxylan, a xylan without MeGlcA substituents along the main chain, but the xylanase activity is about two orders of magnitude lower than that achieved in the case of beechwood xylan (PubMed:31110561). Shows no activity against carob galactomannan, konjac glucomannan, or barley beta-glucan (PubMed:31110561). The recombinant xylanase also exhibits an exo-activity by releasing processively disaccharide units from the non-reducing end of linear and decorated xylooligosaccharides (XOS) (PubMed:31110561). {ECO:0000269|PubMed:31110561}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50 degrees Celsius. {ECO:0000269|PubMed:31110561}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.0. {ECO:0000269|PubMed:31110561}; |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Glycosylation (3); Signal peptide (1) |
| Keywords | Glycoprotein;Hydrolase;Reference proteome;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:31110561}. |
| 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 | 50,883 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.7 mg/ml for beechwood xylan {ECO:0000269|PubMed:31110561}; Vmax=7.1 umol/min/mg enzyme toward beechwood xylan {ECO:0000269|PubMed:31110561}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |