The domain within your query sequence starts at position 1 and ends at position 239; the E-value for the ketoacyl-synt domain shown below is 6.8e-73.

MEEVVIAGMSGKLPESENLQEFWANLIGGVDMVTDDDRRWKAGLYGLPKRSGKLKDLSKF
DASFFGVHPKQAHTMDPQLRLLLEVSYEAIVDGGINPASLRGTNTGVWVGVSGSEASEAL
SRDPETLLGYSMVGCQRAMMANRLSFFFDFKGPSIALDTACSSSLLALQNAYQAIRSGEC
PAALVGGINLLLKPNTSVQFMKLGMLSPDGTCRSFDDSGSGYCRSEAVVAVLLTKKSLA

ketoacyl-synt

ketoacyl-synt
PFAM accession number:PF00109
Interpro abstract (IPR014030):

Beta-ketoacyl-ACP synthase EC 2.3.1.41 (KAS) [(PUBMED:3076376)] is the enzyme that catalyzes the condensation of malonyl-ACP with the growing fatty acid chain. It is found as a component of a number of enzymatic systems, including fatty acid synthetase (FAS), which catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH; the multi-functional 6-methysalicylic acid synthase (MSAS) from Penicillium patulum [(PUBMED:2209605)], which is involved in the biosynthesis of a polyketide antibiotic; polyketide antibiotic synthase enzyme systems; Emericella nidulans multifunctional protein Wa, which is involved in the biosynthesis of conidial green pigment; Rhizobium nodulation protein nodE, which probably acts as a beta-ketoacyl synthase in the synthesis of the nodulation Nod factor fatty acyl chain; and yeast mitochondrial protein CEM1. The condensation reaction is a two step process, first the acyl component of an activated acyl primer is transferred to a cysteine residue of the enzyme and is then condensed with an activated malonyl donor with the concomitant release of carbon dioxide.

This entry represents the N-terminal domain of beta-ketoacyl-ACP synthases.

This is a PFAM domain. For full annotation and more information, please see the PFAM entry ketoacyl-synt