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. 2012 Oct;194(19):5159–5161. doi: 10.1128/JB.01198-12

Fig 1.

Fig 1

The condensing enzymes in P. aeruginosa. The active site structures, locus tags, gene symbols, blocks of homology surrounding the key catalytic residues, and the functional annotations of the genes are provided for the three FabH (A) and four FabB/F (B) homologs in P. aeruginosa. The sequence alignment blocks surrounding the Cys-His-Asn triad of the FabH homologs and Cys-His-His of the FabB/F homologs of P. aeruginosa are compared to the active site residues of the prototypical E. coli FabH (EcFabH) and FabB (EcFabB), respectively. PqsD is sometimes annotated as FabH1. Identical residues are shown on a black background, and conservatively substituted residues are shown on a gray background. The depicted active site structures are derived from the crystal structures of E. coli FabH (Protein Data Bank [PBD] accession no. 1EBL) (3) and E. coli FabB (PDB accession no. 1G5X) (17). UFA, unsaturated fatty acid; 18:1Δ11, cis-vaccenic acid; C8-CoA, octanoyl-CoA; Ac-CoA, acetyl-CoA.