Identification
Name:Lipoate-protein ligase A
Synonyms:
  • Lipoate--protein ligase
Gene Name:lplA
Enzyme Class:
Biological Properties
General Function:Involved in catalytic activity
Specific Function:Catalyzes both the ATP-dependent activation of exogenously supplied lipoate to lipoyl-AMP and the transfer of the activated lipoyl onto the lipoyl domains of lipoate-dependent enzymes. Is also able to catalyze very poorly the transfer of lipoyl and octanoyl moiety from their acyl carrier protein
Cellular Location:Cytoplasm
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb
1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb
1.0Thumb+1.0Apoprotein1.0Protein N6-(lipoyl)lysine+1.0Thumb
1.0Lipoyl-AMP + 1.0Apoprotein ↔ 1.0Protein N6-(lipoyl)lysine + 1.0Adenosine monophosphate
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb+1.0Apoprotein1.0Thumb+1.0Protein N6-(lipoyl)lysine+1.0Thumb
1.0Adenosine triphosphate + 1.0lipoate + 1.0Lipoyl-AMP + 1.0Apoprotein ↔ 1.0Pyrophosphate + 1.0Protein N6-(lipoyl)lysine + 1.0Adenosine monophosphate
ReactionCard
SMPDB Reactions:
1.0Thumb+1.0Thumb1.0Lipoyl-AMP+1.0Pyrophosphate+1.0Thumb
1.0lipoate + 1.0Adenosine triphosphate → 1.0Lipoyl-AMP + 1.0Pyrophosphate + 1.0Lipoyl-AMP
ReactionCard
1.0Lipoyl-AMP+1.0apoprotein+1.0Thumb1.0Protein N6-(lipoyl)lysine+1.0Thumb
1.0Lipoyl-AMP + 1.0apoprotein + 1.0Lipoyl-AMP → 1.0Protein N6-(lipoyl)lysine + 1.0Adenosine monophosphate
ReactionCard
1.0(R)-lipoic acid+1.0Thumb+1.0Thumb+1.0Thumb1.0Pyrophosphate+1.0Lipoyl-AMP+1.0Thumb
1.0(R)-lipoic acid + 1.0Adenosine triphosphate + 1.0Hydrogen ion + 1.0Lipoic acid → 1.0Pyrophosphate + 1.0Lipoyl-AMP + 1.0Lipoyl-AMP
ReactionCard
1.0Lipoyl-AMP+1.0a [lipoyl-carrier protein]-L-lysine+1.0Thumb1.0Thumb+1.0Thumb+1.0Protein N6-(lipoyl)lysine
1.0Lipoyl-AMP + 1.0a [lipoyl-carrier protein]-L-lysine + 1.0Lipoyl-AMP → 1.0Adenosine monophosphate + 1.0Hydrogen ion + 1.0Protein N6-(lipoyl)lysine
ReactionCard
1.0Thumb+1.0Thumb+1.0a [lipoyl-carrier protein]-L-lysine1.0Thumb+1.0Pyrophosphate+1.0Thumb+1.0Protein N6-(octanoyl)lysine
1.0Caprylic acid + 1.0Adenosine triphosphate + 1.0a [lipoyl-carrier protein]-L-lysine → 1.0Hydrogen ion + 1.0Pyrophosphate + 1.0Adenosine monophosphate + 1.0Protein N6-(octanoyl)lysine
ReactionCard
1.0Protein N6-(octanoyl)lysine+2.0Reduced ferredoxin+2.0a sulfurated [sulfur carrier] +2.0S-adenosyl-L-methionine2.0Thumb+2.0Thumb+1.0Oxidized ferredoxin+1.0Protein N6-(lipoyl)lysine+1.0an unsulfurated [sulfur carrier]
1.0Protein N6-(octanoyl)lysine + 2.0Reduced ferredoxin + 2.0a sulfurated [sulfur carrier]  + 2.0S-adenosyl-L-methionine → 2.0L-Methionine + 2.05'-Deoxyadenosine + 1.0Oxidized ferredoxin + 1.0Protein N6-(lipoyl)lysine + 1.0an unsulfurated [sulfur carrier]
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb
1.0Thumb+1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb
Complex Reactions:
1.0Thumb+1.0Thumb+1.0Thumb1.0Thumb+1.0octanoate (protein bound)+1.0Thumb
1.0Thumb1.0Thumb+1.0lipoate (protein bound)
1.0Lipoyl-AMP → 1.0Adenosine monophosphate + 1.0lipoate (protein bound)
ReactionCard
1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb
1.0Thumb+1.0protein1.0protein N(6)-(lipoyl)lysine+1.0Thumb
1.0Lipoyl-AMP + 1.0protein → 1.0protein N(6)-(lipoyl)lysine + 1.0Adenosine monophosphate
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB211745'-DeoxyadenosineMetaboCard
ECMDB00045Adenosine monophosphateMetaboCard
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB00482Caprylic acidMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB00696L-MethionineMetaboCard
ECMDB23028lipoateMetaboCard
ECMDB01451Lipoic acidMetaboCard
ECMDB20170Lipoyl-AMPMetaboCard
ECMDB04142PyrophosphateMetaboCard
GO Classification:
Function
catalytic activity
transferase activity
Process
macromolecule metabolic process
macromolecule modification
metabolic process
post-translational protein modification
protein lipoylation
protein modification process
protein-cofactor linkage
Gene Properties
Blattner:b4386
Gene OrientationCounterclockwise
Centisome Percentage:99.60
Left Sequence End4621124
Right Sequence End4622140
Gene Sequence:
>1017 bp
ATGTTTGTCATCTGGAGCCATAGAACAGGGTTCATCATGAGTCATCAACTTACCTTCGCC
GACAGTGAATTCAGCAGTAAGCGCCGTCAGACCAGAAAAGAGATTTTCTTGTCCCGCATG
GAGCAGATTCTGCCATGGCAAAACATGGTGGAAGTCATCGAGCCGTTTTACCCCAAGGCT
GGTAATGGCCGGCGACCTTATCCGCTGGAAACCATGCTACGCATTCACTGCATGCAGCAT
TGGTACAACCTGAGCGATGGCGCGATGGAAGATGCTCTGTACGAAATCGCCTCCATGCGT
CTGTTTGCCCGGTTATCCCTGGATAGCGCCTTGCCGGACCGCACCACCATCATGAATTTC
CGCCACCTGCTGGAGCAGCATCAACTGGCCCGCCAATTGTTCAAGACCATCAATCGCTGG
CTGGCCGAAGCAGGCGTCATGATGACTCAAGGCACCTTGGTCGATGCCACCATCATTGAG
GCACCCAGCTCGACCAAGAACAAAGAGCAGCAACGCGATCCGGAGATGCATCAGACCAAG
AAAGGCAATCAGTGGCACTTTGGCATGAAGGCCCACATTGGTGTCGATGCCAAGAGTGGC
CTGACCCACAGCCTGGTCACCACCGCGGCCAACGAGCATGACCTCAATCAGCTGGGTAAT
CTGCTGCATGGAGAGGAGCAATTTGTCTCAGCCGATGCCGGCTACCAAGGGGCGCCACAG
CGCGAGGAGCTGGCCGAGGTGGATGTGGACTGGCTGATCGCCGAGCGCCCCGGCAAGGTA
AGAACCTTGAAACAGCATCCACGCAAGAACAAAACGGCCATCAACATCGAATACATGAAA
GCCAGCATCCGGGCCAGGGTGGAGCACCCATTTCGCATCATCAAGCGACAGTTCGGCTTC
GTGAAAGCCAGATACAAGGGGTTGCTGAAAAACGATAACCAACTGGCGATGTTATTCACG
CTGGCCAACCTGTTTCGGGCGGACCAAATGATACGTCAGTGGGAGAGATCTCACTAA
Protein Properties
Pfam Domain Function:
Protein Residues:338
Protein Molecular Weight:37926
Protein Theoretical pI:6
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Lipoate-protein ligase A
MSTLRLLISDSYDPWFNLAVEECIFRQMPATQRVLFLWRNADTVVIGRAQNPWKECNTRR
MEEDNVRLARRSSGGGAVFHDLGNTCFTFMAGKPEYDKTISTSIVLNALNALGVSAEASG
RNDLVVKTVEGDRKVSGSAYRETKDRGFHHGTLLLNADLSRLANYLNPDKKKLAAKGITS
VRSRVTNLTELLPGITHEQVCEAITEAFFAHYGERVEAEIISPNKTPDLPNFAETFARQS
SWEWNFGQAPAFSHLLDERFTWGGVELHFDVEKGHITRAQVFTDSLNPAPLEALAGRLQG
CLYRADMLQQECEALLVDFPEQEKELRELSAWMAGAVR
References
External Links:
ResourceLink
Uniprot ID:P32099
Uniprot Name:LPLA_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:1742188
Ecogene ID:EG11796
Ecocyc:EG11796
ColiBase:b4386
Kegg Gene:b4386
EchoBASE ID:EB1744
CCDB:LPLA_ECOLI
BacMap:16132203
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Burland, V., Plunkett, G. 3rd, Sofia, H. J., Daniels, D. L., Blattner, F. R. (1995). "Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes." Nucleic Acids Res 23:2105-2119. Pubmed: 7610040
  • Fujiwara, K., Toma, S., Okamura-Ikeda, K., Motokawa, Y., Nakagawa, A., Taniguchi, H. (2005). "Crystal structure of lipoate-protein ligase A from Escherichia coli. Determination of the lipoic acid-binding site." J Biol Chem 280:33645-33651. Pubmed: 16043486
  • Green, D. E., Morris, T. W., Green, J., Cronan, J. E. Jr, Guest, J. R. (1995). "Purification and properties of the lipoate protein ligase of Escherichia coli." Biochem J 309 ( Pt 3):853-862. Pubmed: 7639702
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Jordan, S. W., Cronan, J. E. Jr (2003). "The Escherichia coli lipB gene encodes lipoyl (octanoyl)-acyl carrier protein:protein transferase." J Bacteriol 185:1582-1589. Pubmed: 12591875
  • Morris, T. W., Reed, K. E., Cronan, J. E. Jr (1994). "Identification of the gene encoding lipoate-protein ligase A of Escherichia coli. Molecular cloning and characterization of the lplA gene and gene product." J Biol Chem 269:16091-16100. Pubmed: 8206909
  • Morris, T. W., Reed, K. E., Cronan, J. E. Jr (1995). "Lipoic acid metabolism in Escherichia coli: the lplA and lipB genes define redundant pathways for ligation of lipoyl groups to apoprotein." J Bacteriol 177:1-10. Pubmed: 8002607
  • Neuwald, A. F., Stauffer, G. V. (1989). "An Escherichia coli membrane protein with a unique signal sequence." Gene 82:219-228. Pubmed: 2684780