LMPD Database

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LMP007706

UniProt Annotations

Entry Information
Gene Nameoctanoyltransferase; octanoyl-[ACP]:protein N-octanoyltransferase
Protein EntryLIPB_ECOLI
UniProt IDP60720
SpeciesE. coli
Comments
Comment typeDescription
Biophysicochemical PropertiesKinetic parameters: KM=10.2 uM for octanoyl-ACP {ECO:0000269|PubMed:15642479}; KM=13.2 uM for apo-H protein {ECO:0000269|PubMed:15642479}; pH dependence: Optimum pH is about 7.5. {ECO:0000269|PubMed:15642479};
Catalytic ActivityOctanoyl-[acyl-carrier-protein] + protein = protein N(6)-(octanoyl)lysine + [acyl-carrier-protein]. {ECO:0000255|HAMAP-Rule:MF_00013}.
FunctionCatalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate. {ECO:0000255|HAMAP-Rule:MF_00013, ECO:0000269|PubMed:15642479, ECO:0000269|PubMed:16342964}.
Mass SpectrometryMass=23880.45; Mass_error=1.31; Method=Electrospray; Range=1-213; Evidence={ECO:0000269|PubMed:15642479};
MiscellaneousIn the reaction, the free carboxyl group of octanoic acid is attached via an amide linkage to the epsilon- amino group of a specific lysine residue of lipoyl domains of lipoate-dependent enzymes.
PathwayProtein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier- protein]: step 1/2. {ECO:0000255|HAMAP-Rule:MF_00013}.
Sequence CautionSequence=AAA66342.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305}; Sequence=AAB40830.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
SimilarityBelongs to the LipB family. {ECO:0000255|HAMAP- Rule:MF_00013}.
SimilarityContains 1 BPL/LPL catalytic domain. {ECO:0000255|PROSITE-ProRule:PRU01067}.
Subcellular LocationCytoplasm {ECO:0000255|HAMAP-Rule:MF_00013}.
SubunitMonomer or homotrimer. Both forms are active. {ECO:0000269|PubMed:15642479}.