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UniProt functional annotation for P0AEK4 | ||
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| UniProt code: P0AEK4. |
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| Organism: | |
Escherichia coli (strain K12). |
| Taxonomy: | |
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia. |
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| Function: | |
Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism and in the biotin biosynthesis. {ECO:0000269|PubMed:10629181, ECO:0000269|PubMed:20693992, ECO:0000269|PubMed:7592873, ECO:0000269|PubMed:8119879, ECO:0000269|PubMed:8910376}. |
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| Catalytic activity: | |
Reaction=a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] + H(+) + NADH; Xref=Rhea:RHEA:10240, Rhea:RHEA-COMP:9925, Rhea:RHEA- COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.9; Evidence={ECO:0000269|PubMed:10629181, ECO:0000269|PubMed:11007778, ECO:0000269|PubMed:7592873, ECO:0000269|PubMed:8119879, ECO:0000269|PubMed:8910376}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:10242; Evidence={ECO:0000269|PubMed:10629181, ECO:0000269|PubMed:11007778, ECO:0000269|PubMed:7592873, ECO:0000269|PubMed:8119879, ECO:0000269|PubMed:8910376}; |
| Catalytic activity: | |
Reaction=(2E)-butenoyl-[ACP] + H(+) + NADH = butanoyl-[ACP] + NAD(+); Xref=Rhea:RHEA:54868, Rhea:RHEA-COMP:9627, Rhea:RHEA-COMP:9628, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78453, ChEBI:CHEBI:78454; Evidence={ECO:0000269|PubMed:10629181, ECO:0000269|PubMed:11007778, ECO:0000269|PubMed:7592873, ECO:0000269|PubMed:8119879, ECO:0000269|PubMed:8910376}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54869; Evidence={ECO:0000269|PubMed:10629181, ECO:0000269|PubMed:11007778, ECO:0000269|PubMed:7592873, ECO:0000269|PubMed:8119879, ECO:0000269|PubMed:8910376}; |
| Catalytic activity: | |
Reaction=(2E)-decenoyl-[ACP] + H(+) + NADH = decanoyl-[ACP] + NAD(+); Xref=Rhea:RHEA:54936, Rhea:RHEA-COMP:9639, Rhea:RHEA-COMP:9640, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78467, ChEBI:CHEBI:78468; Evidence={ECO:0000269|PubMed:8910376}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54937; Evidence={ECO:0000269|PubMed:8910376}; |
| Catalytic activity: | |
Reaction=(2E)-hexadecenoyl-[ACP] + H(+) + NADH = hexadecanoyl-[ACP] + NAD(+); Xref=Rhea:RHEA:54900, Rhea:RHEA-COMP:9651, Rhea:RHEA- COMP:9652, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78481, ChEBI:CHEBI:78483; Evidence={ECO:0000269|PubMed:7592873, ECO:0000269|PubMed:8910376}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54901; Evidence={ECO:0000269|PubMed:7592873, ECO:0000269|PubMed:8910376}; |
| Catalytic activity: | |
Reaction=(2E,9Z)-hexadecadienoyl-[ACP] + H(+) + NADH = (9Z)- hexadecenoyl-[ACP] + NAD(+); Xref=Rhea:RHEA:54904, Rhea:RHEA- COMP:10800, Rhea:RHEA-COMP:14036, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:83989, ChEBI:CHEBI:138403; Evidence={ECO:0000269|PubMed:7592873, ECO:0000269|PubMed:8910376}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54905; Evidence={ECO:0000269|PubMed:7592873, ECO:0000269|PubMed:8910376}; |
| Catalytic activity: | |
Reaction=(2E)-5-methylhexenoyl-[ACP] + H(+) + NADH = 5-methylhexanoyl- [ACP] + NAD(+); Xref=Rhea:RHEA:55124, Rhea:RHEA-COMP:14097, Rhea:RHEA-COMP:14098, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:138610, ChEBI:CHEBI:138611; Evidence={ECO:0000269|PubMed:10629181}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55125; Evidence={ECO:0000269|PubMed:10629181}; |
| Activity regulation: | |
Inhibited by diazaborines, triclosan (5-chloro-2- 2,4-dichlorophenoxyphenol), 1,4-disubstituted imidazoles, 1,4- benzodiazepine derivatives, naphthyridinone derivatives, luteolin and curcumin (PubMed:10398587, PubMed:10493822, PubMed:11514139, PubMed:12109908, PubMed:12699381, PubMed:19959361, PubMed:8119879, PubMed:8953047, PubMed:9707111). The antibiotic diazaborine interferes with the activity by binding to the protein and NAD (PubMed:8119879). {ECO:0000269|PubMed:10398587, ECO:0000269|PubMed:10493822, ECO:0000269|PubMed:11514139, ECO:0000269|PubMed:12109908, ECO:0000269|PubMed:12699381, ECO:0000269|PubMed:19959361, ECO:0000269|PubMed:8119879, ECO:0000269|PubMed:8953047, ECO:0000269|PubMed:9707111}. |
| Biophysicochemical properties: | |
Kinetic parameters: KM=3.3 uM for trans-2-dodecenoyl-ACP (DD-ACP)(at 25 degrees Celsius and pH 8) {ECO:0000269|PubMed:17012233}; KM=22 uM for crotonyl-ACP (at 30 degrees Celsius and pH 7.5) {ECO:0000269|PubMed:8119879}; KM=24 uM for trans-2-dodecenoyl-CoA (DD-CoA)(at 25 degrees Celsius and pH 8) {ECO:0000269|PubMed:17012233}; KM=2700 uM for crotonyl-CoA (at 30 degrees Celsius and pH 7.5) {ECO:0000269|PubMed:8119879}; |
| Pathway: | |
Lipid metabolism; fatty acid biosynthesis. {ECO:0000269|PubMed:7592873}. |
| Pathway: | |
Cofactor biosynthesis; biotin biosynthesis. {ECO:0000305|PubMed:20693992}. |
| Subunit: | |
Homotetramer. {ECO:0000269|PubMed:10201369, ECO:0000269|PubMed:10398587, ECO:0000269|PubMed:10493822, ECO:0000269|PubMed:10595560, ECO:0000269|PubMed:11514139, ECO:0000269|PubMed:12109908, ECO:0000269|PubMed:12699381, ECO:0000269|PubMed:8953047}. |
| Similarity: | |
Belongs to the short-chain dehydrogenases/reductases (SDR) family. FabI subfamily. {ECO:0000305}. |
Annotations taken from UniProtKB at the EBI.