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UniProt functional annotation for P0A6R0 | ||
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| UniProt codes: P0A6R0, P24249. |
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| Organism: | |
Escherichia coli (strain K12). |
| Taxonomy: | |
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia. |
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| 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. Has some substrate specificity for acetyl-CoA. Its substrate specificity determines the biosynthesis of straight-chain of fatty acids instead of branched-chain (PubMed:7592873, PubMed:8631920, PubMed:8910376, PubMed:10629181). Can also use propionyl-CoA, with lower efficiency (PubMed:8631920, PubMed:10629181). {ECO:0000269|PubMed:10629181, ECO:0000269|PubMed:7592873, ECO:0000269|PubMed:8631920, ECO:0000269|PubMed:8910376}. |
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| Catalytic activity: | |
Reaction=acetyl-CoA + H(+) + malonyl-[ACP] = 3-oxobutanoyl-[ACP] + CO2 + CoA; Xref=Rhea:RHEA:12080, Rhea:RHEA-COMP:9623, Rhea:RHEA- COMP:9625, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:78449, ChEBI:CHEBI:78450; EC=2.3.1.180; Evidence={ECO:0000255|HAMAP-Rule:MF_01815, ECO:0000269|PubMed:10629181, ECO:0000269|PubMed:7592873, ECO:0000269|PubMed:8631920, ECO:0000269|PubMed:8910376}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12081; Evidence={ECO:0000269|PubMed:10629181, ECO:0000269|PubMed:7592873, ECO:0000269|PubMed:8631920, ECO:0000269|PubMed:8910376}; |
| Catalytic activity: | |
Reaction=H(+) + malonyl-[ACP] + propanoyl-CoA = 3-oxopentanoyl-[ACP] + CO2 + CoA; Xref=Rhea:RHEA:42244, Rhea:RHEA-COMP:9623, Rhea:RHEA- COMP:9939, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57392, ChEBI:CHEBI:78449, ChEBI:CHEBI:78818; Evidence={ECO:0000269|PubMed:10629181, ECO:0000269|PubMed:8631920}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42245; Evidence={ECO:0000269|PubMed:10629181, ECO:0000269|PubMed:8631920}; |
| Activity regulation: | |
Negatively regulated by acyl-ACP, possibly by binding to either the free enzyme or the acyl-enzyme intermediate. {ECO:0000269|PubMed:8631920}. |
| Biophysicochemical properties: | |
Kinetic parameters: KM=40 uM for acetyl-CoA {ECO:0000269|PubMed:8631920}; KM=5 uM for malonyl-[ACP] {ECO:0000269|PubMed:8631920}; |
| Pathway: | |
Lipid metabolism; fatty acid biosynthesis. {ECO:0000255|HAMAP- Rule:MF_01815}. |
| Subunit: | |
Homodimer. {ECO:0000255|HAMAP-Rule:MF_01815}. |
| Subcellular location: | |
Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01815}. |
| Domain: | |
The last Arg residue of the ACP-binding site is essential for the weak association between ACP/AcpP and FabH. {ECO:0000255|HAMAP- Rule:MF_01815, ECO:0000269|PubMed:11078736}. |
| Miscellaneous: | |
Inhibited by the SB418011 antibiotic. Not inhibited by cerulenin and thiolactomycin. |
| Similarity: | |
Belongs to the thiolase-like superfamily. FabH family. {ECO:0000255|HAMAP-Rule:MF_01815, ECO:0000305}. |
Annotations taken from UniProtKB at the EBI.