IED ID | IndEnz0004000035 |
Enzyme Type ID | xylanase000035 |
Protein Name |
Intracellular endo-alpha- 1- 5 -L-arabinanase ABN EC 3.2.1.99 Endo-1,5-alpha-L-arabinanase |
Gene Name | abnB |
Organism | Geobacillus stearothermophilus (Bacillus stearothermophilus) |
Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Geobacillus Geobacillus stearothermophilus (Bacillus stearothermophilus) |
Enzyme Sequence | MVHFHPFGNVNFYEMDWSLKGDLWAHDPVIAKEGSRWYVFHTGSGIQIKTSEDGVHWENMGWVFPSLPDWYKQYVPEKDEDHLWAPDICFYNGIYYLYYSVSTFGKNTSVIGLATNQTLDPRDPDYEWKDMGPVIHSTASDNYNAIDPNVVFDQEGQPWLSFGSFWSGIQLIQLDTETMKPAAQAELLTIASRGEEPNAIEAPFIVCRNGYYYLFVSFDFCCRGIESTYKIAVGRSKDITGPYVDKNGVSMMQGGGTILDEGNDRWIGPGHCAVYFSGVSAILVNHAYDALKNGEPTLQIRPLYWDDEGWPYLSV |
Enzyme Length | 315 |
Uniprot Accession Number | B3EYM8 |
Absorption | |
Active Site | ACT_SITE 27; /note=Proton acceptor; /evidence=ECO:0000305|PubMed:19505290; ACT_SITE 201; /note=Proton donor; /evidence=ECO:0000305|PubMed:19505290 |
Activity Regulation | |
Binding Site | BINDING 27; /note=Substrate; /evidence=ECO:0000269|PubMed:19505290; BINDING 105; /note=Substrate; via amide nitrogen; /evidence=ECO:0000269|PubMed:19505290 |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->5)-alpha-arabinofuranosidic linkages in (1->5)-arabinans.; EC=3.2.1.99; Evidence={ECO:0000269|PubMed:19505290}; |
DNA Binding | |
EC Number | 3.2.1.99 |
Enzyme Function | FUNCTION: Involved in the degradation of arabinan and is a key enzyme in the complete degradation of the plant cell wall. Catalyzes the internal cleavage of alpha-(1->5)-L-arabinofuranosyl residues of debranched arabinan, linear arabinan and short arabino-oligosaccharides (degree of polymerization from 2 to 8). It exhibits marginal activity toward sugar beet arabinan. {ECO:0000269|PubMed:19505290}. |
Temperature Dependency | |
PH Dependency | |
Pathway | PATHWAY: Glycan metabolism; L-arabinan degradation. |
nucleotide Binding | |
Features | Active site (2); Beta strand (22); Binding site (2); Chain (1); Helix (4); Metal binding (1); Region (2); Site (2); Turn (2) |
Keywords | 3D-structure;Calcium;Carbohydrate metabolism;Cytoplasm;Glycosidase;Hydrolase;Metal-binding |
Interact With | |
Induction | INDUCTION: Transcription is repressed by glucose and by the binding of AraR to the operon promoter. L-arabinose acts as an inducer by inhibiting the binding of AraR to the DNA, thus allowing expression of the gene. {ECO:0000269|PubMed:21460081}. |
Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:19505290}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | X-ray crystallography (6) |
Cross Reference PDB | 3CU9; 3D5Y; 3D5Z; 3D60; 3D61; 6F1G; |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 35,763 |
Kinetics | |
Metal Binding | METAL 271; /note=Calcium; /evidence=ECO:0000255 |
Rhea ID | |
Cross Reference Brenda | 3.2.1.99; |