Gene_Locus Report

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Gene_locus Report for: aspor-cutas

Aspergillus oryzae (Yellow koji mold), Aspergillus flavus, CutL1 gene for cutinase cutinase 1 precursor (EC 3.1.1.74) (cutin hydrolase 1) (l1)

Comment
Aspergillus oryzae grown in a liquid medium containing the polyester polybutylene succinate co-adipate (PBSA), produces RolA, a hydrophobin, and CutL1, a PBSA-degrading cutinase. Secreted RolA attaches to PBSA particles and recruits CutL1, which stimulates the hydrolysis of PBSA. Asp142, Asp171, Glu31 and Asp30 are involved in the ionic interaction with RolA CutL1 (Takahashi et al.2015, Terauchi 2017). Structures of CutL alone or in complex with paraoxon were solved(Liu et al. 2009). Other strains: Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold), Aspergillus flavus (strain ATCC 200026/FGSC A1120/NRRL 3357/JC12722/SRRC 167)


Relationship
Family|Cutinase
Block| X
Position in NCBI Life Tree|Aspergillus oryzae
(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 oryzae: 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
2 structures: 3GBS, 3QPD
No kinetic





3 substrates: Cutin, Polybutylene-succinate-co-adipate, Polycaprolactone
1 inhbitor:
Paraoxon
>3 Genbank links 1 more: D38311, AP007151, EQ963472
2 UniProt : P52956, B8MVS3
1 Ncbi-nid : 949812
1 Ncbi-pid : 949813
2 Structure : 3QPD, 3GBS
2 UniProt : P52956, B8MVS3
2 Interpro : P52956, B8MVS3
2 Prodom : P52956, B8MVS3
2 Pfam : P52956, B8MVS3
2 PIRSF : P52956, B8MVS3
2 SUPERFAM : P52956, B8MVS3
Sequence
Graphical view for this peptide sequence: aspor-cutas
Colored MSA for Cutinase (raw)
MHLRNIVIALAATAVASPVDLQDRQLTGGDELRDGPCKPITFIFARASTE
PGLLGISTGPAVCNRLKLARSGDVACQGVGPRYTADLPSNALPEGTSQAA
IAEAQGLFEQAVSKCPDTQIVAGGYSQGTAVMNGAIKRLSADVQDKIKGV
VLFGYTRNAQERGQIANFPKDKVKVYCAVGDLVCLGTLIVAPPHFSYLSD
TGDASDFLLSQLG
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

MHLRNIVIALAATAVASPVDLQDRQLTGGDELRDGPCKPITFIFARASTE
PGLLGISTGPAVCNRLKLARSGDVACQGVGPRYTADLPSNALPEGTSQAA
IAEAQGLFEQAVSKCPDTQIVAGGYSQGTAVMNGAIKRLSADVQDKIKGV
VLFGYTRNAQERGQIANFPKDKVKVYCAVGDLVCLGTLIVAPPHFSYLSD
TGDASDFLLSQLG


References
3 more
    Title: Asp30 of Aspergillus oryzae cutinase CutL1 is involved in the ionic interaction with fungal hydrophobin RolA
    Terauchi Y, Kim YK, Tanaka T, Nanatani K, Takahashi T, Abe K
    Ref: Biosci Biotechnol Biochem, :1, 2017 : PubMed

            

    Title: Ionic interaction of positive amino acid residues of fungal hydrophobin RolA with acidic amino acid residues of cutinase CutL1
    Takahashi T, Tanaka T, Tsushima Y, Muragaki K, Uehara K, Takeuchi S, Maeda H, Yamagata Y, Nakayama M and Abe K <1 more author(s)>
    Ref: Molecular Microbiology, 96:14, 2015 : PubMed

            

    Title: Structural and functional studies of Aspergillus oryzae cutinase: enhanced thermostability and hydrolytic activity of synthetic ester and polyester degradation
    Liu Z, Gosser Y, Baker PJ, Ravee Y, Lu Z, Alemu G, Li H, Butterfoss GL, Kong XP and Montclare JK <1 more author(s)>
    Ref: Journal of the American Chemical Society, 131:15711, 2009 : PubMed

            


Other Papers


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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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