Detail Information for IndEnz0004000033
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;