ECMDB

Identification

Name:

Lipoate-protein ligase A

Synonyms:

Lipoate--protein ligase

Gene Name:

lplA

Enzyme Class:

2.7.7.63

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:

Lipoic acid metabolism PW000770

KEGG Pathways:

Lipoic acid metabolism ec00785
Metabolic pathways eco01100

KEGG Reactions:

1.0

→

1.0

1.0Adenosine triphosphate + 1.0Lipoic acid → 1.0Lipoyl-AMP + 1.0Pyrophosphate
ReactionCard

1.0

↔

1.0

1.0Adenosine triphosphate + 1.0Lipoic acid ↔ 1.0Pyrophosphate + 1.0Lipoyl-AMP
ReactionCard

1.0

1.0Apoprotein

↔

1.0Protein N6-(lipoyl)lysine

1.0

1.0Lipoyl-AMP + 1.0Apoprotein ↔ 1.0Protein N6-(lipoyl)lysine + 1.0Adenosine monophosphate
ReactionCard

1.0

1.0Apoprotein

↔

1.0

1.0Protein N6-(lipoyl)lysine

1.0

1.0Adenosine triphosphate + 1.0lipoate + 1.0Lipoyl-AMP + 1.0Apoprotein ↔ 1.0Pyrophosphate + 1.0Protein N6-(lipoyl)lysine + 1.0Adenosine monophosphate
ReactionCard

SMPDB Reactions:

1.0

→

1.0Lipoyl-AMP

1.0Pyrophosphate

1.0

1.0lipoate + 1.0Adenosine triphosphate → 1.0Lipoyl-AMP + 1.0Pyrophosphate + 1.0Lipoyl-AMP
ReactionCard

1.0Lipoyl-AMP

1.0apoprotein

1.0

→

1.0Protein N6-(lipoyl)lysine

1.0

1.0Lipoyl-AMP + 1.0apoprotein + 1.0Lipoyl-AMP → 1.0Protein N6-(lipoyl)lysine + 1.0Adenosine monophosphate
ReactionCard

1.0(R)-lipoic acid

1.0

→

1.0Pyrophosphate

1.0Lipoyl-AMP

1.0

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

1.0

→

1.0

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

1.0

1.0a [lipoyl-carrier protein]-L-lysine

→

1.0

1.0Pyrophosphate

1.0

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-methionine

→

2.0

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:

1.0

→

1.0

1.0Adenosine triphosphate + 1.0Lipoic acid → 1.0Lipoyl-AMP + 1.0Pyrophosphate
ReactionCard

1.0

→

1.0

1.0Hydrogen ion + 1.0Lipoic acid + 1.0Adenosine triphosphate → 1.0Lipoyl-AMP + 1.0Pyrophosphate
ReactionCard

Complex Reactions:

1.0

→

1.0

1.0octanoate (protein bound)

1.0

1.0Adenosine triphosphate + 1.0Hydrogen ion + 1.0Caprylic acid → 1.0Adenosine monophosphate + 1.0octanoate (protein bound) + 1.0Pyrophosphate
ReactionCard

1.0

→

1.0

1.0lipoate (protein bound)

1.0Lipoyl-AMP → 1.0Adenosine monophosphate + 1.0lipoate (protein bound)
ReactionCard

1.0

→

1.0

1.0Adenosine triphosphate + 1.0lipoate → 1.0Pyrophosphate + 1.0Lipoyl-AMP
ReactionCard

1.0

1.0protein

→

1.0protein N(6)-(lipoyl)lysine

1.0

1.0Lipoyl-AMP + 1.0protein → 1.0protein N(6)-(lipoyl)lysine + 1.0Adenosine monophosphate
ReactionCard

Metabolites:

ECMDB ID	Name	View
ECMDB21174	5'-Deoxyadenosine	MetaboCard
ECMDB00045	Adenosine monophosphate	MetaboCard
ECMDB00538	Adenosine triphosphate	MetaboCard
ECMDB00482	Caprylic acid	MetaboCard
ECMDB21225	Hydrogen ion	MetaboCard
ECMDB00696	L-Methionine	MetaboCard
ECMDB23028	lipoate	MetaboCard
ECMDB01451	Lipoic acid	MetaboCard
ECMDB20170	Lipoyl-AMP	MetaboCard
ECMDB04142	Pyrophosphate	MetaboCard

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 Orientation

Counterclockwise

Centisome Percentage:

99.60

Left Sequence End

4621124

Right Sequence End

4622140

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:

BPL_LipA_LipB (PF03099 )
Lip_prot_lig_C (PF10437 )

Protein Residues:

338

Protein Molecular Weight:

37926

Protein Theoretical pI:

Signaling Regions:

None

Transmembrane Regions:

None

Protein Sequence:

>Lipoate-protein ligase A
MSTLRLLISDSYDPWFNLAVEECIFRQMPATQRVLFLWRNADTVVIGRAQNPWKECNTRR
MEEDNVRLARRSSGGGAVFHDLGNTCFTFMAGKPEYDKTISTSIVLNALNALGVSAEASG
RNDLVVKTVEGDRKVSGSAYRETKDRGFHHGTLLLNADLSRLANYLNPDKKKLAAKGITS
VRSRVTNLTELLPGITHEQVCEAITEAFFAHYGERVEAEIISPNKTPDLPNFAETFARQS
SWEWNFGQAPAFSHLLDERFTWGGVELHFDVEKGHITRAQVFTDSLNPAPLEALAGRLQG
CLYRADMLQQECEALLVDFPEQEKELRELSAWMAGAVR

References

External Links:

Resource	Link
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

Lipoate-protein ligase A (P32099)