A1V6D0 · FABH_BURMS

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.

Pathway

Lipid metabolism; fatty acid biosynthesis.

Features

Showing features for active site.

132950100150200250300
TypeIDPosition(s)Description
Active site123
Active site256
Active site286

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

Gene names

    • Name
      fabH
    • Ordered locus names
      BMASAVP1_A2479

Organism names

Accessions

  • Primary accession
    A1V6D0

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_10000702201-329Beta-ketoacyl-[acyl-carrier-protein] synthase III

Interaction

Subunit

Homodimer.

Structure

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region257-261ACP-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
    329
  • Mass (Da)
    34,823
  • Last updated
    2007-02-06 v1
  • Checksum
    3098E02DA5714697
MAQSTLYSRVLGTGSYLPPDRVTNQELADRLAKDGIETSDEWIVARTGIRARHFAAPDVTTSDLALVAAQRAIEAADVDPQSIDLIIVATSTPDFVFPSTACLLQNKLGIKNGGAAFDVQAVCSGFAYALATADSFIRTGQHRTALVIGAEAFSRILDFKDRTTCVLFGDGAGAVVLSASEEPGILGSALHADGSYSNILCTPGNVNRGVIAGSAFLHMDGQAVFKLAVNVLEKVAVEALSKAELASEQVDWLIPHQANIRIMTSTCRKLGLPQERMIVTVDEHGNTSAASIPLALDVAVRDGRIKRGQHVLIEGVGGGFTWGASVFRF

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP000526
EMBL· GenBank· DDBJ
ABM49968.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

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.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp