Detail Information for IndEnz0010001125
IED ID IndEnz0010001125
Enzyme Type ID esterase001125
Protein Name Probable feruloyl esterase B-1
EC 3.1.1.73
Ferulic acid esterase B-1
FAEB-1
Gene Name faeB-1 AFLA_128870
Organism Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167)
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 flavus Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167)
Enzyme Sequence MPSLRRLLPFLAAGSAALASQDTFQGKCTGFADKINLPDVRVNFVNYVPGGTNLSLPDNPTSCGTTSQVVSEDVCRIAMAVATSNSSEITLEAWLPQNYTGRFLSTGNGGLSGCIQYYDLAYTSGLGFATVGANSGHNGTSGEPFYHHPEVLEDFVHRSVHTGVVVGKQLTKLFYEEGFKKSYYLGCSTGGRQGFKSVQKYPNDFDGVVAGAPAFNMINLMSWSAHFYSITGPVGSDTYLSPDLWNITHKEILRQCDGIDGAEDGIIEDPSLCSPVLEAIICKPGQNTTECLTGKQAHTVREIFSPLYGVNGTLLYPRMQPGSEVMASSIMYNGQPFQYSADWYRYVVYENPNWDATKFSVRDAAVALKQNPFNLQTWDADISSFRKAGGKVLTYHGLMDQLISSENSKLYYARVAETMNVPPEELDEFYRFFQISGMAHCSGGDGAYGIGNQLVTYNDANPENNVLMAMVQWVEKGIAPETIRGAKFTNGTGSAVEYTRKHCRYPRRNVYKGPGNYTDENAWQCV
Enzyme Length 526
Uniprot Accession Number B8NPA4
Absorption
Active Site ACT_SITE 188; /note=Acyl-ester intermediate; /evidence=ECO:0000250|UniProtKB:Q2UP89; ACT_SITE 400; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:Q2UP89; ACT_SITE 440; /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 (9); 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..19; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 57,748
Kinetics
Metal Binding METAL 257; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q2UP89; METAL 260; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q2UP89; METAL 262; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q2UP89; METAL 264; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q2UP89; METAL 266; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q2UP89
Rhea ID
Cross Reference Brenda