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Gene_locus Report for: bacbr-q70lm8

Bacillus brevis (Brevibacillus brevis) type II thioesterase

Relationship
Family|Thioesterase
Block| X
Position in NCBI Life Tree|Bacillus brevis
(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.)
> cellular organisms: N E > Bacteria: N E > Terrabacteria group: N E > Firmicutes: N E > Bacilli: N E > Bacillales: N E > Paenibacillaceae: N E > Brevibacillus: N E > Brevibacillus brevis: 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
No structure
No kinetic





No Substrate
No inhibitor
1 Genbank : AJ566197
1 UniProt : Q70LM8
1 UniProt : Q70LM8
1 Interpro : Q70LM8
1 Prodom : Q70LM8
1 Pfam : Q70LM8
1 PIRSF : Q70LM8
1 SUPERFAM : Q70LM8
Sequence
Graphical view for this peptide sequence: bacbr-q70lm8
Colored MSA for Thioesterase (raw)
MQKTHVSPSRWLLSPKMTAEAEVLLFSFHYAGGHAGIYREWQKKLPVQIG
VCPVQLPGRSNRFMEPYYTDLSVMIRELAEALLPHLNRPFAFFGHSMGAL
VSFELARYLRNQYGIKPRHMFASGRHAPHLPDPGEAIHHLPDAEFLKGLR
TLNGTPKELFENEENEEILQMLLPMLRADFTICEQYQYQEEEPLGCGLTA
IGGWQDPDITVAHMEAWRKHTSASFQMHMLQGDHFFLHSEQEQLLAIIES
TLQSYLVGYRGIG
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

MQKTHVSPSRWLLSPKMTAEAEVLLFSFHYAGGHAGIYREWQKKLPVQIG
VCPVQLPGRSNRFMEPYYTDLSVMIRELAEALLPHLNRPFAFFGHSMGAL
VSFELARYLRNQYGIKPRHMFASGRHAPHLPDPGEAIHHLPDAEFLKGLR
TLNGTPKELFENEENEEILQMLLPMLRADFTICEQYQYQEEEPLGCGLTA
IGGWQDPDITVAHMEAWRKHTSASFQMHMLQGDHFFLHSEQEQLLAIIES
TLQSYLVGYRGIG


References
    Title: Synthesis of linear gramicidin requires the cooperation of two independent reductases
    Schracke N, Linne U, Mahlert C, Marahiel MA
    Ref: Biochemistry, 44:8507, 2005 : PubMed

            

    Title: The linear pentadecapeptide gramicidin is assembled by four multimodular nonribosomal peptide synthetases that comprise 16 modules with 56 catalytic domains
    Kessler N, Schuhmann H, Morneweg S, Linne U, Marahiel MA
    Ref: Journal of Biological Chemistry, 279:7413, 2004 : 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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