Detail Information for IndEnz0010000732
IED ID IndEnz0010000732
Enzyme Type ID esterase000732
Protein Name Probable feruloyl esterase B
EC 3.1.1.73
Ferulic acid esterase B
FAEB
Gene Name faeB An12g10390
Organism Aspergillus niger (strain CBS 513.88 / FGSC A1513)
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 niger Aspergillus niger (strain CBS 513.88 / FGSC A1513)
Enzyme Sequence MKVSSLLSVALPGAALAATDSFQSRCNEFQNKIDIANVTVRSVAYVAAGQNISQAEVASVCKASVQASVDLCRVTMNISTSDRSHLWAEAWLPRNYTGRFVSTGNGGLAGCVQETDLNFAANFGFATVGTNGGHDGDTAKYFLNNSEVLADFAYRSVHEGTVVGKQLTQLFYDEGYNYSYYLGCSTGGRQGYQQVQRFPDDYDGVIAGSAAMNFINLISWGAFLWKATGLADDPDFISADLWSVIHQEIVRQCDLVDGALDGIIEDPDFCAPVIERLICDGTTNGTSCITGAQAAKVNRALSDFYGPDGTVYYPRLNYGGEADSAYLYFTGSMYSRTEEWYKYVVYNDTNWNSSQWTLESAKLALEQNPFNIQAFDPNITAFRDRGGKLLSYHGTQDPIISSTDSKLYYRRVANALNAAPSELDEFYRFFQISGMGHCGDGTGASYIGQGYGTYTSKAPQVNLLRTMVDWVENGKAPEYMPGNKLNANGSIEYMRKHCRYPKHNVHTGPGNYTDPNSWTCV
Enzyme Length 521
Uniprot Accession Number A2R0Z6
Absorption
Active Site ACT_SITE 185; /note=Acyl-ester intermediate; /evidence=ECO:0000250|UniProtKB:Q2UP89; ACT_SITE 397; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:Q2UP89; ACT_SITE 437; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:Q2UP89
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Feruloyl-polysaccharide + H(2)O = ferulate + polysaccharide.; EC=3.1.1.73; Evidence={ECO:0000250|UniProtKB:Q8WZI8};
DNA Binding
EC Number 3.1.1.73
Enzyme Function FUNCTION: Involved in degradation of plant cell walls. Hydrolyzes the feruloyl-arabinose ester bond in arabinoxylans as well as the feruloyl-galactose and feruloyl-arabinose ester bonds in pectin. {ECO:0000250|UniProtKB:Q8WZI8}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Chain (1); Disulfide bond (6); Glycosylation (12); Metal binding (5); Signal peptide (1)
Keywords Calcium;Carbohydrate metabolism;Disulfide bond;Glycoprotein;Hydrolase;Metal-binding;Polysaccharide degradation;Reference proteome;Secreted;Serine esterase;Signal;Xylan degradation
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..17; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 57,208
Kinetics
Metal Binding METAL 254; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q2UP89; METAL 257; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q2UP89; METAL 259; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q2UP89; METAL 261; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q2UP89; METAL 263; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q2UP89
Rhea ID
Cross Reference Brenda