P0A3C5 · FABH_STRPN

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 (PubMed:11375394).
Utilizes short straight and branched-chain acyl-CoAs, with a preference for acetyl-CoA (PubMed:11375394).

Catalytic activity

Activity regulation

Inhibited by the SB418011 antibiotic (PubMed:11375394).
Not inhibited by cerulenin, and weakly inhibited by thiolactomycin (PubMed:11375394).

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
40.3 μMacetyl-CoA
18.6 μMmalonyl-ACP

Pathway

Lipid metabolism; fatty acid biosynthesis.

Features

Showing features for active site.

TypeIDPosition(s)Description
Active site112
Active site249
Active site279

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

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
    • Branched-chain beta-ketoacyl-[acyl-carrier-protein] synthase
    • SpFabH

Gene names

    • Name
      fabH
    • Ordered locus names
      SP_0417

Organism names

Accessions

  • Primary accession
    P0A3C5
  • Secondary accessions
    • Q93NA1
    • Q9FBC7

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001104911-324Beta-ketoacyl-[acyl-carrier-protein] synthase III

Proteomic databases

Interaction

Subunit

Homodimer.

Structure

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region250-254ACP-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
    324
  • Mass (Da)
    34,904
  • Last updated
    2005-03-15 v1
  • Checksum
    53E529125B392C70
MAFAKISQVAHYVPEQVVTNHDLAQIMDTNDEWISSRTGIRQRHISRTESTSDLATEVAKKLMAKAGITGEELDFIILATITPDSMMPSTAARVQANIGANKAFAFDLTAACSGFVFALSTAEKFIASGRFQKGLVIGSETLSKAVDWSDRSTAVLFGDGAGGVLLEASEQEHFLAESLNSDGSRSECLTYGHSGLHSPFSDQESADSFLKMDGRTVFDFAIRDVAKSIKQTIDESPIEVTDLDYLLLHQANDRILDKMARKIGVDRAKLPANMMEYGNTSAASIPILLSECVEQGLIPLDGSQTVLLSGFGGGLTWGTLILTI

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict71in Ref. 1; AAK91994

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF384041
EMBL· GenBank· DDBJ
AAK91994.1
EMBL· GenBank· DDBJ
Genomic DNA
AE005672
EMBL· GenBank· DDBJ
AAK74580.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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