A0A016XG18 · A0A016XG18_9BURK

Function

function

Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Pathway

Lipid metabolism; fatty acid biosynthesis.

Features

Showing features for active site.

TypeIDPosition(s)Description
Active site119
Active site252
Active site282

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Function3-oxoacyl-[acyl-carrier-protein] synthase activity
Molecular Functionbeta-ketoacyl-acyl-carrier-protein synthase III activity
Biological Processfatty acid biosynthetic process
Biological Processsecondary metabolite biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Beta-ketoacyl-[acyl-carrier-protein] synthase III
  • EC number
  • Short names
    Beta-ketoacyl-ACP synthase III
    ; KAS III
  • Alternative names
    • 3-oxoacyl-[acyl-carrier-protein] synthase 3
    • 3-oxoacyl-[acyl-carrier-protein] synthase III

Gene names

    • Name
      fabH
    • ORF names
      AZ34_06725

Organism names

Accessions

  • Primary accession
    A0A016XG18

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain113-190Beta-ketoacyl-[acyl-carrier-protein] synthase III N-terminal
Domain236-324Beta-ketoacyl-[acyl-carrier-protein] synthase III C-terminal
Region253-257ACP-binding

Domain

The last Arg residue of the ACP-binding site is essential for the weak association between ACP/AcpP and FabH.

Sequence similarities

Belongs to the thiolase-like superfamily. FabH family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    325
  • Mass (Da)
    33,765
  • Last updated
    2014-06-11 v1
  • Checksum
    54E9E81A83AF0418
MRLYSRISGTGSFLPPQRLTNADLAARLAADGIETSDEWIVERTGIRARHFAAEGVMSSDLGAEAARRALQAAGLAASDIDLIIVATSTPDMIFPSTAVILQNKIGANGCQAFDVQAVCSGFIYALTVADSMIRAGAASKALVVGAEVFSRIIDFKDRTTCVLFGDGAGAVVLQASETPGILASDLKADGKHAGILCTPGTVAAGKVLGDPFLKMDGQAVFKQAVTVLDEASRAVLAKAGKTEADIDWLVPHQANIRIMMGAAKKLKLAPEKVVVTVDQHGNTSAASIPLALDHGVRQGQIKQGDTLLLEAVGGGLTWGAVLLTY

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JEMG01000001
EMBL· GenBank· DDBJ
EYC50791.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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