| IED ID | IndEnz0004000248 |
| Enzyme Type ID | xylanase000248 |
| Protein Name |
Beta-xylosidase/alpha-L-arabinofuranosidase 1 Xylan 1,4-beta-xylosidase/Alpha-L-arabinofuranosidase 1 MsXyl1 Includes: Beta-xylosidase EC 3.2.1.37 1,4-beta-D-xylan xylohydrolase Xylan 1,4-beta-xylosidase ; Alpha-L-arabinofuranosidase Arabinosidase EC 3.2.1.55 Fragment |
| Gene Name | Xyl1 |
| Organism | Medicago sativa subsp. varia (Alfalfa) (Medicago varia) |
| Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae rosids fabids Fabales Fabaceae Papilionoideae 50 kb inversion clade NPAAA clade Hologalegina IRL clade Trifolieae Medicago (medics) Medicago sativa (Alfalfa) Medicago sativa subsp. varia (Alfalfa) (Medicago varia) |
| Enzyme Sequence | ANTKNREPKVSSVFLCFSIFYVTVLLNCNHVYGQTSTVFACDVAKNTNVSSYGFCDNSLSVEDRVSDLVKRLTLQEKIGNLGNSAVEVSRLGIPKYEWWSEALHGVSNIGPGTHFSSLVPGATNFPMPILTAASFNTSLFQAIGSVVSNEARAMYNVGLAGLTYWSPNINIFRDPRWGRGQETPGEDPLLSSKYAAGYVKGLQQTDDGDSDKLKVAACCKHYTAYDVDNWKGVQRYTFDAVVSQQDLDDTFQPPFKSCVIDGNVASVMCSYNKVNGKPTCADPDLLKGVIRGKWKLNGYIVSDCDSVEVLYKDQHYTKTPEEAAAKTILSGLDLDCGSYLGQYTGGAVKQGLVDEASITNAVSNNFATLMRLGFFDGDPSKQPYGNLGPKDVCTPENQELAREAARQGIVLLKNSPRSLPLSSKAIKSLAVIGPNANATRVMIGNYEGIPCKYTSPLQGLTAFVPTSYAPGCPDVQCANAQIDDAAKIAASADATIIVVGANLAIEAESLDRVNILLPGQQQQLVNEVANVSKGPVILVIMSGGGMDVSFAKTNDKITSILWVGYPGEAGGAAIADVIFGSYNPSGRLPMTWYPQSYVEKVPMTNMNMRADPATGYPGRTYRFYKGETVFSFGDGMSFGTVEHKIVKAPQLVSVPLAEDHECRSLECKSLDVADKHCQNLAFDIHLSVKNMGKMSSSHSVLLFFTPPNVHNAPQKHLLGFEKVQLAGKSEGMVRFKVDVCNDLSVVDELGNRKVPLGDHMLHVGNLKHSLSVRI |
| Enzyme Length | 774 |
| Uniprot Accession Number | A5JTQ2 |
| Absorption | |
| Active Site | ACT_SITE 303; /evidence=ECO:0000250|UniProtKB:Q9FGY1 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->4)-beta-D-xylans, to remove successive D-xylose residues from the non-reducing termini.; EC=3.2.1.37; Evidence={ECO:0000269|PubMed:17615411}; CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides.; EC=3.2.1.55; Evidence={ECO:0000269|PubMed:17615411}; |
| DNA Binding | |
| EC Number | 3.2.1.37; 3.2.1.55 |
| Enzyme Function | FUNCTION: A bifunctional beta-xylosidase/alpha-L-arabinosidase, exo-enzyme that acts synergistically with endohydrolases. Releases xylose and arabinose from cell walls. Does not cleave xylan from oat spelts although xylan from oat spelts was degraded to xylose when this enzyme was used in combination with xylanase. Also releases xylose and arabinose from aryl glycosides, xylo-oligosaccharides, arabinan from sugar beet and arabino-oligosaccharides, arabinan from sugar beet and arabinoxylan from wheat. {ECO:0000269|PubMed:17615411}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Glycosylation (4); Non-terminal residue (1); Signal peptide (1) |
| Keywords | Carbohydrate metabolism;Extracellular matrix;Glycoprotein;Glycosidase;Hydrolase;Multifunctional enzyme;Polysaccharide degradation;Secreted;Signal;Xylan degradation |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:Q9FLG1}. |
| Modified Residue | |
| Post Translational Modification | PTM: Proteolytically cleaved in roots to form a 65 kDa protein. {ECO:0000269|PubMed:17615411}. |
| Signal Peptide | SIGNAL <1..33; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 83,727 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.59 mM for pNP-beta-D-xlyoside (at 37 degrees Celsius) {ECO:0000269|PubMed:17615411}; KM=0.94 mM for pNP-alpha-L-arabinofuranoside (at 37 degrees Celsius) {ECO:0000269|PubMed:17615411}; KM=1.20 mM for pNP-alpha-L-arabinopyranoside (at 37 degrees Celsius) {ECO:0000269|PubMed:17615411}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |