Letunic et al. (2017) Nucleic Acids Res doi: 10.1093/nar/gkx922
Letunic et al. (2020) Nucleic Acids Res doi: 10.1093/nar/gkaa937

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PKS_KS Beta-ketoacyl synthase

SMART accession number:	SM00825
Description:	The structure of beta-ketoacyl synthase is similar to that of the thiolase family and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.
Interpro abstract (IPR020841):	This entry represents the the beta-ketoacyl synthase region from a number of polyketide synthases including erythronolide synthase and the lovastatin nonaketide chain synthase. 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.
Family alignment:	View or CHROMA formatHMM/Web logoCLUSTALW formatMSF formatFASTA formatPIR format

There are 35981 PKS_KS domains in 21913 proteins in SMART's nrdb database.

Click on the following links for more information.

• Evolution (species in which this domain is found)

• Taxonomic distribution of proteins containing PKS_KS domain.

  This tree includes only several representative species. The complete taxonomic breakdown of all proteins with PKS_KS domain is also avaliable.

  Click on the protein counts, or double click on taxonomic names to display all proteins containing PKS_KS domain in the selected taxonomic class.

• Cellular role (predicted cellular role)

• Cellular role: metabolism
  

• Metabolism (metabolic pathways involving proteins which contain this domain)

• Click the image to view the interactive version of the map in iPath

  % proteins involved KEGG pathway ID Description 10.00 map00632 Benzoate degradation via CoA ligation 9.23 map00350 Tyrosine metabolism 9.23 map00564 Glycerophospholipid metabolism 9.23 map00903 Limonene and pinene degradation 9.23 map00960 Alkaloid biosynthesis II 9.23 map00310 Lysine degradation 9.23 map00624 1- and 2-Methylnaphthalene degradation 9.23 map00360 Phenylalanine metabolism 9.23 map00340 Histidine metabolism 9.23 map00642 Ethylbenzene degradation 2.31 map00061 Fatty acid biosynthesis 1.54 map01053 Biosynthesis of siderophore group nonribosomal peptides 0.77 map00562 Inositol phosphate metabolism 0.77 map03320 PPAR signaling pathway 0.77 map04920 Adipocytokine signaling pathway 0.77 map00071 Fatty acid metabolism This information is based on mapping of SMART genomic protein database to KEGG orthologous groups. Percentage points are related to the number of proteins with PKS_KS domain which could be assigned to a KEGG orthologous group, and not all proteins containing PKS_KS domain. Please note that proteins can be included in multiple pathways, ie. the numbers above will not always add up to 100%.

• Structure (3D structures containing this domain)

• 3D Structures of PKS_KS domains in PDB

  PDB code	Main view	Title
  2hg4		Structure of the ketosynthase-acyltransferase didomain of module 5 from DEBS.
  2qo3		Crystal Structure of [KS3][AT3] didomain from module 3 of 6-deoxyerthronolide B synthase
  4mz0		Structure of a ketosynthase-acyltransferase di-domain from module CurL of the curacin A polyketide synthase
  4na1		Crystal Structure of the second ketosynthase from the bacillaene polyketide synthase
  4na2		Crystal Structure of the second ketosynthase from the bacillaene polyketide synthase bound to its natural intermediate
  4na3		Crystal Structure of the second ketosynthase from the bacillaene polyketide synthase bound to a hexanoyl substrate mimic
  4tkt		4TKT
  4z37		4Z37
  4zdn		4ZDN
  5bp1		5BP1
  5e5n		5E5N
  5e6k		5E6K
  5eny		5ENY
  5erb		5ERB
  5erf		5ERF

• Links (links to other resources describing this domain)

• INTERPRO	IPR020841
  PFAM	ketoacyl-synt

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