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Gene_locus Report for: 9eury-q2pce5

Ferroplasma acidiphilum carboxylesterase (EC 3.1.1.1)

Relationship
Family|Hormone-sensitive_lipase_like
Block| H
Position in NCBI Life Tree|Ferroplasma acidiphilum
(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.)
> cellular organisms: N E > Archaea: N E > Euryarchaeota: N E > Thermoplasmata: N E > Thermoplasmatales: N E > Ferroplasmaceae: N E > Ferroplasma: N E > Ferroplasma acidiphilum: 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
1 structure:
3WJ2: Crystal structure of ESTFA (FE-lacking apo form)
No kinetic





No Substrate
No inhibitor
2 Genbank : AABC04000006, AJ850914
1 UniProt : Q2PCE5
1 Structure : 3WJ2
1 UniProt : Q2PCE5
1 Interpro : Q2PCE5
1 Prodom : Q2PCE5
1 Pfam : Q2PCE5
1 PIRSF : Q2PCE5
1 SUPERFAM : Q2PCE5
Sequence
Graphical view for this peptide sequence: 9eury-q2pce5
Colored MSA for Hormone-sensitive_lipase_like (raw)
MHLMNMVDPDFNSLIELSKSAGDMTKIEPAMLRNFLDESSLSSRGAPVEI
KEIKDYKIKLDGRTLNARMYDDNNAKSAILYYHGGGFLFGNIETYDNYCR
FLAKESGVKIISIEYRLAPEHKFPDAFNDAYDSFHYIAKKKKDFGIEGRI
GVAGDSAGANLAAALCLKCRDGKTEMPAVQVLFYPSLAPDNFSRSFIEYS
DNYVLTGKMIRYFGNMYSKNMQDLINPYFSPLVADDFSNLPPAIMVTNEY
DPLRDPEETYVKKLREAGVRAVGIRGIGMIHGSATDFEVSDGARNIVKMV
ARIIPDYL
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

MHLMNMVDPDFNSLIELSKSAGDMTKIEPAMLRNFLDESSLSSRGAPVEI
KEIKDYKIKLDGRTLNARMYDDNNAKSAILYYHGGGFLFGNIETYDNYCR
FLAKESGVKIISIEYRLAPEHKFPDAFNDAYDSFHYIAKKKKDFGIEGRI
GVAGDSAGANLAAALCLKCRDGKTEMPAVQVLFYPSLAPDNFSRSFIEYS
DNYVLTGKMIRYFGNMYSKNMQDLINPYFSPLVADDFSNLPPAIMVTNEY
DPLRDPEETYVKKLREAGVRAVGIRGIGMIHGSATDFEVSDGARNIVKMV
ARIIPDYL


References
    Title: Structural Insights into the Low pH Adaptation of a Unique Carboxylesterase from Ferroplasma: Altering the pH optima of two carboxylesterases
    Ohara K, Unno H, Oshima Y, Hosoya M, Fujino N, Hirooka K, Takahashi S, Yamashita S, Kusunoki M, Nakayama T
    Ref: Journal of Biological Chemistry, 289:24499, 2014 : PubMed

            

    Title: The 'pH optimum anomaly' of intracellular enzymes of Ferroplasma acidiphilum
    Golyshina OV, Golyshin PN, Timmis KN, Ferrer M
    Ref: Environ Microbiol, 8:416, 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.
For technical information about these pages see:
ESTHER Home Page and ACEDB Home Page
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