Gene_Locus Report

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Gene_locus Report for: aspni-FAEA

Aspergillus niger; A. usamii; A. phoenicis ; A. awamori; A. welwitschiae; A. vadensis; A. lacticoffeatus; A. phoenicis ferulic acid esterase a, AnFAEA

Comment
Other strains: Aspergillus niger (CBS 513.88/FGSC A1513; ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a / NRRL 328 / USDA 3528.7; ATCC 13496); Aspergillus usamii; Aspergillus phoenicis ATCC 13157; Aspergillus awamori (Black koji mold); Aspergillus welwitschiae; Aspergillus vadensis (strain CBS 113365 / IMI 142717 / IBT 24658); Aspergillus lacticoffeatus (strain CBS 101883); Aspergillus phoenicis ATCC 13157


Relationship
Family|Lipase_3
Block| L
Position in NCBI Life Tree|Aspergillus niger
(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.)
> cellular organisms: N E > Eukaryota: N E > Opisthokonta: N E > Fungi: N E > Dikarya: N E > Ascomycota: N E > saccharomyceta: N E > Pezizomycotina: N E > leotiomyceta: N E > Eurotiomycetes: N E > Eurotiomycetidae: N E > Eurotiales: N E > Aspergillaceae: N E > Aspergillus: N E > Aspergillus niger: N E
Warning: This entry is a compilation of different species or line or strain with more than 90% amino acide identity. You can retrieve all strain data


Molecular evidence
Database
No mutation
6 structures (e.g. : 1USW, 1UWC, 1UZA... more)
No kinetic





1 substrate:
Ferulic-acid
1 inhbitor:
CAPS
2 Genbank : Y09330, AM270190
>3 UniProt links 11 more: O42807, A2QSY5, V5TEY2
>3 Structure links 3 more: 2BJH, 2IX9, 2HL6
3 UniProt : O42807, A2QSY5, V5TEY2
3 Interpro : O42807, A2QSY5, V5TEY2
3 Prodom : O42807, A2QSY5, V5TEY2
3 Pfam : O42807, A2QSY5, V5TEY2
3 PIRSF : O42807, A2QSY5, V5TEY2
3 SUPERFAM : O42807, A2QSY5, V5TEY2
Sequence
Graphical view for this peptide sequence: aspni-FAEA
Colored MSA for Lipase_3 (raw)
MKQFSAKYALILLATAGQALAASTQGISEDLYNRLVEMATISQAAYADLC
NIPSTIIKGEKIYNAQTDINGWILRDDTSKEIITVFRGTGSDTNLQLDTN
YTLTPFDTLPQCNDCEVHGGYYIGWISVQDQVESLVKQQASQYPDYALTV
TGHSLGASMAALTAAQLSATYDNVRLYTFGEPRSGNQAFASYMNDAFQVS
SPETTQYFRVTHSNDGIPNLPPADEGYAHGGVEYWSVDPYSAQNTFVCTG
DEVQCCEAQGGQGVNDAHTTYFGMTSGACTW
Legend This sequence has been compared to family alignement (MSA)
red => minority aminoacid
blue => majority aminoacid
color intensity => conservation rate
title => sequence position(MSA position)aminoacid rate
Catalytic site
Catalytic site in the MSA

MKQFSAKYALILLATAGQALAASTQGISEDLYNRLVEMATISQAAYADLC
NIPSTIIKGEKIYNAQTDINGWILRDDTSKEIITVFRGTGSDTNLQLDTN
YTLTPFDTLPQCNDCEVHGGYYIGWISVQDQVESLVKQQASQYPDYALTV
TGHSLGASMAALTAAQLSATYDNVRLYTFGEPRSGNQAFASYMNDAFQVS
SPETTQYFRVTHSNDGIPNLPPADEGYAHGGVEYWSVDPYSAQNTFVCTG
DEVQCCEAQGGQGVNDAHTTYFGMTSGACTW


References
10 more
    Title: Transition Path Sampling Study of the Feruloyl Esterase Mechanism
    Silveira RL, Knott BC, Pereira CS, Crowley MF, Skaf MS, Beckham GT
    Ref: J Phys Chem B, :, 2021 : PubMed

            

    Title: Insights into substrate binding of ferulic acid esterases by arabinose and methyl hydroxycinnamate esters and molecular docking
    Hunt CJ, Antonopoulou I, Tanksale A, Rova U, Christakopoulos P, Haritos VS
    Ref: Sci Rep, 7:17315, 2017 : PubMed

            

    Title: Respective importance of protein folding and glycosylation in the thermal stability of recombinant feruloyl esterase A
    Benoit I, Asther M, Sulzenbacher G, Record E, Marmuse L, Parsiegla G, Gimbert I, Bignon C
    Ref: FEBS Letters, 580:5815, 2006 : PubMed

            


Other Papers


Send your questions or comments to :
Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
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