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UniProt functional annotation for P0AAI5 | ||
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| UniProt code: P0AAI5. |
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| Organism: | |
Escherichia coli (strain K12). |
| Taxonomy: | |
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia. |
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| Function: | |
Involved in the type II fatty acid elongation cycle (PubMed:9013860, PubMed:6988423). Catalyzes the elongation of a wide range of acyl-ACP by the addition of two carbons from malonyl-ACP to an acyl acceptor (PubMed:9013860, PubMed:22017312). Can efficiently catalyze the conversion of palmitoleoyl-ACP (cis-hexadec-9-enoyl-ACP) to cis-vaccenoyl-ACP (cis-octadec-11-enoyl-ACP), an essential step in the thermal regulation of fatty acid composition (PubMed:9013860, PubMed:6988423). Can use acyl chains from C-6 to C-16 (PubMed:9013860, PubMed:22017312). Is able to catalyze the condensation reaction when CoA is the carrier for both substrates (PubMed:22017312). {ECO:0000269|PubMed:22017312, ECO:0000269|PubMed:6988423, ECO:0000269|PubMed:9013860}. |
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| Catalytic activity: | |
Reaction=a fatty acyl-[ACP] + H(+) + malonyl-[ACP] = a 3-oxoacyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:22836, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9916, Rhea:RHEA-COMP:14125, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78776, ChEBI:CHEBI:138651; Evidence={ECO:0000269|PubMed:22017312, ECO:0000269|PubMed:9013860}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22837; Evidence={ECO:0000269|PubMed:22017312, ECO:0000269|PubMed:9013860}; |
| Catalytic activity: | |
Reaction=(9Z)-hexadecenoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxo-(11Z)- octadecenoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:55040, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:10800, Rhea:RHEA-COMP:14074, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:83989, ChEBI:CHEBI:138538; EC=2.3.1.179; Evidence={ECO:0000269|PubMed:9013860, ECO:0000305|PubMed:6988423}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55041; Evidence={ECO:0000269|PubMed:9013860, ECO:0000305|PubMed:6988423}; |
| Catalytic activity: | |
Reaction=H(+) + hexanoyl-[ACP] + malonyl-[ACP] = 3-oxooctanoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:41836, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9632, Rhea:RHEA-COMP:9633, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78459, ChEBI:CHEBI:78460; Evidence={ECO:0000269|PubMed:9013860}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41837; Evidence={ECO:0000269|PubMed:9013860}; |
| Catalytic activity: | |
Reaction=H(+) + malonyl-[ACP] + octanoyl-[ACP] = 3-oxodecanoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:41852, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9636, Rhea:RHEA-COMP:9637, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78463, ChEBI:CHEBI:78464; Evidence={ECO:0000269|PubMed:9013860}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41853; Evidence={ECO:0000269|PubMed:9013860}; |
| Catalytic activity: | |
Reaction=decanoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxododecanoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:41868, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9640, Rhea:RHEA-COMP:9641, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78468, ChEBI:CHEBI:78469; Evidence={ECO:0000269|PubMed:9013860}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41869; Evidence={ECO:0000269|PubMed:9013860}; |
| Catalytic activity: | |
Reaction=dodecanoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxotetradecanoyl- [ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:41884, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9644, Rhea:RHEA-COMP:9645, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:65264, ChEBI:CHEBI:78449, ChEBI:CHEBI:78473; Evidence={ECO:0000269|PubMed:22017312, ECO:0000269|PubMed:9013860}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41885; Evidence={ECO:0000269|PubMed:22017312, ECO:0000269|PubMed:9013860}; |
| Catalytic activity: | |
Reaction=H(+) + malonyl-[ACP] + tetradecanoyl-[ACP] = 3- oxohexadecanoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:41900, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9648, Rhea:RHEA-COMP:9649, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78477, ChEBI:CHEBI:78478; Evidence={ECO:0000269|PubMed:9013860}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41901; Evidence={ECO:0000269|PubMed:9013860}; |
| Biophysicochemical properties: | |
Kinetic parameters: KM=8.2 uM for malonyl-[ACP] (in the presence of dodecanoyl-[ACP]) {ECO:0000269|PubMed:22017312}; KM=510 uM for malonyl-CoA (in the presence of dodecanoyl-CoA) {ECO:0000269|PubMed:22017312}; KM=53.7 uM for dodecanoyl-CoA (in the presence of malonyl-CoA) {ECO:0000269|PubMed:22017312}; |
| Pathway: | |
Lipid metabolism; fatty acid biosynthesis. {ECO:0000269|PubMed:6988423}. |
| Subunit: | |
Homodimer. {ECO:0000269|PubMed:9013860, ECO:0000269|PubMed:9482715}. |
| Miscellaneous: | |
Identified as a drug target (PubMed:10037680, PubMed:16710421, PubMed:19233644, PubMed:19581087). Inhibited by platensimycin and platencin, which are antibiotic produced by various strains of Streptomyces platensis, and by several platensimycin/platencin analogs (PubMed:16710421, PubMed:19233644, PubMed:19581087). Also inhibited by the fungal mycotoxin cerulenin that binds in a hydrophobic pocket formed at the dimer interface (PubMed:10037680). {ECO:0000269|PubMed:10037680, ECO:0000269|PubMed:16710421, ECO:0000269|PubMed:19233644, ECO:0000269|PubMed:19581087}. |
| Similarity: | |
Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP synthases family. {ECO:0000305}. |
Annotations taken from UniProtKB at the EBI.