| IED ID | IndEnz0004000033 |
| Enzyme Type ID | xylanase000033 |
| Protein Name |
Alpha-L-arabinofuranosidase B ABF B Arabinosidase B EC 3.2.1.55 |
| Gene Name | abfB AO090023000001 |
| Organism | Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Circumdati Aspergillus oryzae (Yellow koji mold) Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold) |
| Enzyme Sequence | MSSGLSLERACAVALGIVASASLVAAGPCDIYSSGGTPCVAAHSTTRALYSAYTGALYQVKRGSDGSTTDIAPLSAGGVADAAIQDSFCANTTCLITIIYDQSGRGNHLTQAPPGGFNGPESNGYDNLASAVGAPVTLNGKKAYGVFMSPGTGYRNNAASGTATGDKAEGMYAVLDGTHYNSACCFDYGNAEVSNTDTGNGHMEAIYYGDNTVWGSGAGSGPWIMADLENGLFSGLSSTNNAGDPSISYRFVTAVVKGEANQWSIRGANAASGSLSTYYSGARPSASGYNPMSKEGAIILGIGGDNSNGAQGTFYEGVMTSGYPSDATENSVQADIVAAKYAIASLTSGPALTVGSSISLQVTTAGYTTRYLAHDGSTVNTQVVSSSSTTALRQQASWTVRTGLANSACLSFESVDTPGSYIRHYNFALLLNANDGTKQFYEDATFCPQAGLNGQGNSIRSWSYPTRYFRHYENVLYVASNGGVQTFDATTSFNDDVSWVVSTGFA |
| Enzyme Length | 506 |
| Uniprot Accession Number | Q2UIM2 |
| Absorption | |
| Active Site | ACT_SITE 229; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 305; /note=Proton donor; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | BINDING 227; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q8NK89; BINDING 230; /note=Substrate; via amide nitrogen; /evidence=ECO:0000250|UniProtKB:Q8NK89; BINDING 304; /note=Substrate; via amide nitrogen; /evidence=ECO:0000250|UniProtKB:Q8NK89; BINDING 424; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q8NK89; BINDING 426; /note=Substrate; via amide nitrogen; /evidence=ECO:0000250|UniProtKB:Q8NK89; BINDING 427; /note=Substrate; via amide nitrogen; /evidence=ECO:0000250|UniProtKB:Q8NK89; BINDING 443; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q8NK89; BINDING 471; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q8NK89; BINDING 473; /note=Substrate; via amide nitrogen; /evidence=ECO:0000250|UniProtKB:Q8NK89; BINDING 476; /note=Substrate; via amide nitrogen; /evidence=ECO:0000250|UniProtKB:Q8NK89; BINDING 496; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q8NK89 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides.; EC=3.2.1.55; |
| DNA Binding | |
| EC Number | 3.2.1.55 |
| Enzyme Function | FUNCTION: Alpha-L-arabinofuranosidase involved in the degradation of arabinoxylan, a major component of plant hemicellulose. Able to hydrolyze 1,5-, 1,3- and 1,2-alpha-linkages not only in L-arabinofuranosyl oligosaccharides, but also in polysaccharides containing terminal non-reducing L-arabinofuranoses in side chains, like L-arabinan, arabinogalactan and arabinoxylan. {ECO:0000269|PubMed:16233386}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 60 degrees Celsius. {ECO:0000269|PubMed:16233386}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.5. Stable between pH 4.0 and 6.5. {ECO:0000269|PubMed:16233386}; |
| Pathway | PATHWAY: Glycan metabolism; L-arabinan degradation. |
| nucleotide Binding | |
| Features | Active site (2); Binding site (11); Chain (1); Disulfide bond (4); Glycosylation (1); Region (2); Sequence conflict (8); Signal peptide (1); Site (1) |
| Keywords | Carbohydrate metabolism;Disulfide bond;Glycoprotein;Glycosidase;Hydrolase;Polysaccharide degradation;Reference proteome;Secreted;Signal;Xylan degradation |
| Interact With | |
| Induction | INDUCTION: Repressed by glucose. {ECO:0000269|PubMed:16233386}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..26; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 52,195 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.2.1.55; |