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UniProt functional annotation for Q8ZFT7 | ||
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| UniProt code: Q8ZFT7. |
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| Organism: | |
Yersinia pestis. |
| Taxonomy: | |
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Yersiniaceae; Yersinia. |
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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. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids. {ECO:0000255|HAMAP-Rule:MF_01815}. |
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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}; |
| 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}. |
| Similarity: | |
Belongs to the thiolase-like superfamily. FabH family. {ECO:0000255|HAMAP-Rule:MF_01815}. |
Annotations taken from UniProtKB at the EBI.