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Table 2 Deviations in enzyme active sites in fabB and fabF paralogues in K. stuttgartiensis, R. baltica, G. sulfurreducens in comparison to 'typical' fabB/F sequences in e.g. Kustd1386 (CAJ72131) or the structurally determined EcfabB (YP_540234).

From: A comparative genomics study of genetic products potentially encoding ladderane lipid biosynthesis

Gene sequence Active site amino acids from fabB/Fsequence
Typical fabB/F sequence and function Active site Decarb-oxylation Unknown Unknown Electronic charge on histidine ring Decarb-oxylation Electronic charge on histidine ring Guides acyl chain entry into binding pocket
  Cys163s His298* Thr300 Thr302 Lys328* His333* Glu342 Phe392a
Val163 Asn298 Tyr300a Gly302 Lys328* Glu333 Gln342 Arg392*
Phe163a Asn298 Asn300 Cys302s Lys328* Glu333 Gln342 Phe392a
Ser163 Ser298 Pro300i Phe302a Asp328 Asn333 Asn342 Ser392
R. baltica
NP 865682
Asp163 His298* Met300s Asp302 Ile328 His333* Gly342 Ser392
R. baltica
NP 866153
Glu163 His298* Leu300 Asp302 Lys328* Asn333 Glu342 Pro392i
G. sulfurreducens
NP 951518
Phe163a Pro298i Ala300 Ala302 Gly328 Arg333* Ala342 -
  1. Functional role of amino acids taken from White et al. [21]. Key; Italics = hydrophilic (polar amino acids), Bold = hydrophobic (non-polar amino acids), (*) = Basic, (‡) = Acidic or amide, (s) = Sulphur containing, (a) = Aromatic, (i) = Imino acid.