P0A3C5 · FABH_STRPN
- ProteinBeta-ketoacyl-[acyl-carrier-protein] synthase III
- GenefabH
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids324 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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).
Utilizes short straight and branched-chain acyl-CoAs, with a preference for acetyl-CoA (PubMed:11375394).
Catalytic activity
- acetyl-CoA + H+ + malonyl-[ACP] = 3-oxobutanoyl-[ACP] + CO2 + CoAThis reaction proceeds in the forward direction.
- butanoyl-CoA + H+ + malonyl-[ACP] = 3-oxohexanoyl-[ACP] + CO2 + CoAThis reaction proceeds in the forward direction.
Activity regulation
Inhibited by the SB418011 antibiotic (PubMed:11375394).
Not inhibited by cerulenin, and weakly inhibited by thiolactomycin (PubMed:11375394).
Not inhibited by cerulenin, and weakly inhibited by thiolactomycin (PubMed:11375394).
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
40.3 μM | acetyl-CoA | |||||
18.6 μM | malonyl-ACP |
Pathway
Lipid metabolism; fatty acid biosynthesis.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 112 | |||||
Sequence: C | ||||||
Active site | 249 | |||||
Sequence: H | ||||||
Active site | 279 | |||||
Sequence: N |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | 3-oxoacyl-[acyl-carrier-protein] synthase activity | |
Molecular Function | beta-ketoacyl-acyl-carrier-protein synthase III activity | |
Biological Process | fatty acid biosynthetic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameBeta-ketoacyl-[acyl-carrier-protein] synthase III
- EC number
- Short namesBeta-ketoacyl-ACP synthase III ; KAS III
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Lactobacillales > Streptococcaceae > Streptococcus
Accessions
- Primary accessionP0A3C5
- Secondary accessions
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000110491 | 1-324 | Beta-ketoacyl-[acyl-carrier-protein] synthase III | |||
Sequence: MAFAKISQVAHYVPEQVVTNHDLAQIMDTNDEWISSRTGIRQRHISRTESTSDLATEVAKKLMAKAGITGEELDFIILATITPDSMMPSTAARVQANIGANKAFAFDLTAACSGFVFALSTAEKFIASGRFQKGLVIGSETLSKAVDWSDRSTAVLFGDGAGGVLLEASEQEHFLAESLNSDGSRSECLTYGHSGLHSPFSDQESADSFLKMDGRTVFDFAIRDVAKSIKQTIDESPIEVTDLDYLLLHQANDRILDKMARKIGVDRAKLPANMMEYGNTSAASIPILLSECVEQGLIPLDGSQTVLLSGFGGGLTWGTLILTI |
Proteomic databases
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 250-254 | ACP-binding | ||||
Sequence: QANDR |
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 statusComplete
- Length324
- Mass (Da)34,904
- Last updated2005-03-15 v1
- Checksum53E529125B392C70
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 71 | in Ref. 1; AAK91994 | ||||
Sequence: E → K |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF384041 EMBL· GenBank· DDBJ | AAK91994.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE005672 EMBL· GenBank· DDBJ | AAK74580.1 EMBL· GenBank· DDBJ | Genomic DNA |