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Family Report for: Duf_1100-R

Duf_1100-R



Relationship
Family Duf_1100-R
Block X
Parent Family : UPF0255

Comment
DUF1100 UPF0255. The family was split in two. Duf_1100-S with active site (S217 in (GXSXG) D300 H329) as in artni-Q93NG6, and Duf_1100-R with active site (R53, D203, R 272 (in GXRXG)) as in FrsA. The fermentation/respiration switch protein FrsA (product of the yafA gene in E. Coli (ecoli-yafa)(vibvy-y856) binds the dephosphorylated form of glucose-specific enzyme IIAGl the interaction increases the glucose fermentation under oxygen-limited conditions. FrsA is a pyruvate decarboxylase (Lee et al.)(In Scop 2,6-dihydropseudooxynicotine hydrolase) Thus there are two functions and two different active sites in this family (nucleophile elbow: GXSXG in hydrolase, GXRXG in decarboxylase). However (Kellett et al.) showed Computational, structural, and kinetic evidence that Vibrio vulnificus FrsA is not a cofactor-independent pyruvate decarboxylase. Other members of this family are still uncharacterised

Database
Sequences
Interpro
|
IPR010520 (Esterase FrsA-like Protein of unknown function DUF1100 UPF0255, hydrolase-like), IPR043423 (Esterase FrsA)
PIRSF
|
Pdoc
|
PFam
|
PF06500 (FrsA-like DUF1100)
Prints
|
Prosite
|
no EC number



Peptide in
|Fasta
Nucleotide in
|Fasta
Alignment with Multalin
|Text only/graphic display
Seed alignment with MAFFT
|No colour/coloured with Mview
Alignment with MAFFT
|No colour/coloured with Mview
Dendrogram
|Graphical display, obtained with the dnd file produced by Clustalw

References
3 more
    Title: FrsA functions as a cofactor-independent decarboxylase to control metabolic flux
    Lee KJ, Jeong CS, An YJ, Lee HJ, Park SJ, Seok YJ, Kim P, Lee JH, Lee KH, Cha SS
    Ref: Nat Chemical Biology, 7:434, 2011 : PubMed

            

    Title: Structure and action of a C-C bond cleaving alpha/beta-hydrolase involved in nicotine degradation
    Schleberger C, Sachelaru P, Brandsch R, Schulz GE
    Ref: Journal of Molecular Biology, 367:409, 2007 : PubMed

            

    Title: A novel fermentation/respiration switch protein regulated by enzyme IIAGlc in Escherichia coli
    Koo BM, Yoon MJ, Lee CR, Nam TW, Choe YJ, Jaffe H, Peterkofsky A, Seok YJ
    Ref: Journal of Biological Chemistry, 279:31613, 2004 : PubMed

            

Other Papers


No structure scheme yet for this family

Structures in Duf_1100-R family (3)

Genes Proteins in Duf_1100-R family (77)

Fragments of genes in Duf_1100-R family (1)

No Substrate

No Inhibitor



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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