Dihydrolipoyl dehydrogenase (P0A9P0)

Identification
Name:Dihydrolipoyl dehydrogenase
Synonyms:
  • Dihydrolipoamide dehydrogenase
  • E3 component of pyruvate and 2-oxoglutarate dehydrogenases complexes
  • Glycine cleavage system L protein
Gene Name:lpdA
Enzyme Class:
Biological Properties
General Function:Involved in oxidoreductase activity
Specific Function:Lipoamide dehydrogenase is a component of the glycine cleavage system as well as of the alpha-ketoacid dehydrogenase complexes
Cellular Location:Cytoplasm. Cell inner membrane; Peripheral membrane protein
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0Dihydrolipoamide + 1.0NAD ↔ 1.0Lipoamide + 1.0NADH + 1.0Hydrogen ion
ReactionCard
1.0Dihydrolipoylprotein+1.0Thumb ↔ 1.0Lipoylprotein+1.0Thumb+1.0Thumb
1.0Dihydrolipoylprotein + 1.0NAD ↔ 1.0Lipoylprotein + 1.0NADH + 1.0Hydrogen ion
ReactionCard
1.0Enzyme N6-(dihydrolipoyl)lysine+1.0Thumb ↔ 1.0Enzyme N6-(lipoyl)lysine+1.0Thumb+1.0Thumb
1.0Enzyme N6-(dihydrolipoyl)lysine + 1.0NAD ↔ 1.0Enzyme N6-(lipoyl)lysine + 1.0NADH + 1.0Hydrogen ion
ReactionCard
1.0Protein N6-(dihydrolipoyl)lysine+1.0Thumb ↔ 1.0Protein N6-(lipoyl)lysine+1.0Thumb+1.0Thumb
1.0Protein N6-(dihydrolipoyl)lysine + 1.0NAD ↔ 1.0Protein N6-(lipoyl)lysine + 1.0NADH + 1.0Hydrogen ion
ReactionCard
SMPDB Reactions:
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Succinyl-CoA+1.0Thumb
1.0Oxoglutaric acid + 1.0NAD + 1.0Coenzyme A → 1.0NADH + 1.0Carbon dioxide + 1.0Succinyl-CoA + 1.0Succinyl-CoA
ReactionCard
1.0a [pyruvate dehydrogenase E2 protein] N6-dihydrolipoyl-L-lysine+1.0Thumb → 1.0a [pyruvate dehydrogenase E2 protein] N6-lipoyl-L-lysine+1.0Thumb+1.0Thumb
1.0a [pyruvate dehydrogenase E2 protein] N6-dihydrolipoyl-L-lysine + 1.0NAD → 1.0a [pyruvate dehydrogenase E2 protein] N6-lipoyl-L-lysine + 1.0NADH + 1.0Hydrogen ion
ReactionCard
1.0a [2-oxoglutarate dehydrogenase E2 protein] N6-dihydrolipoyl-L-lysine+1.0Thumb → 1.0a [2-oxoglutarate dehydrogenase E2 protein] N6-lipoyl-L-lysine+1.0Thumb+1.0Thumb
1.0a [2-oxoglutarate dehydrogenase E2 protein] N6-dihydrolipoyl-L-lysine + 1.0NAD → 1.0a [2-oxoglutarate dehydrogenase E2 protein] N6-lipoyl-L-lysine + 1.0NADH + 1.0Hydrogen ion
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0Coenzyme A + 1.0NAD + 1.0Pyruvic acid → 1.0Acetyl-CoA + 1.0Carbon dioxide + 1.0NADH
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0alpha-Ketoglutarate + 1.0Coenzyme A + 1.0NAD → 1.0Carbon dioxide + 1.0NADH + 1.0Succinyl-CoA
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0Glycine + 1.0NAD + 1.0Tetrahydrofolic acid → 1.0Carbon dioxide + 1.05,10-Methylene-THF + 1.0NADH + 1.0Ammonium
ReactionCard
1.0Protein N(6)-(dihydrolipoyl)lysine+1.0Thumb → 1.0protein N(6)-(lipoyl)lysine+1.0Thumb
1.0Protein N(6)-(dihydrolipoyl)lysine + 1.0NAD → 1.0protein N(6)-(lipoyl)lysine + 1.0NADH
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB013545,10-Methylene-THFMetaboCard
ECMDB01206Acetyl-CoAMetaboCard
ECMDB02812alpha-KetoglutarateMetaboCard
ECMDB00051AmmoniaMetaboCard
ECMDB21186AmmoniumMetaboCard
ECMDB04030Carbon dioxideMetaboCard
ECMDB01423Coenzyme AMetaboCard
ECMDB00985DihydrolipoamideMetaboCard
ECMDB24000DihydrolipoylproteinMetaboCard
ECMDB23785Enzyme N6-(dihydrolipoyl)lysineMetaboCard
ECMDB00123GlycineMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB00962LipoamideMetaboCard
ECMDB00902NADMetaboCard
ECMDB01487NADHMetaboCard
ECMDB04123Oxoglutaric acidMetaboCard
ECMDB00243Pyruvic acidMetaboCard
ECMDB01022Succinyl-CoAMetaboCard
ECMDB01846Tetrahydrofolic acidMetaboCard
GO Classification:
Component
cell part
cytoplasm
intracellular part
Function
adenyl nucleotide binding
binding
catalytic activity
dihydrolipoyl dehydrogenase activity
FAD or FADH2 binding
nucleoside binding
oxidoreductase activity
oxidoreductase activity, acting on a sulfur group of donors, NAD or NADP as acceptor
oxidoreductase activity, acting on NADH or NADPH
purine nucleoside binding
Process
cell redox homeostasis
cellular homeostasis
cellular process
metabolic process
oxidation reduction
Gene Properties
Blattner:b0116
Gene OrientationClockwise
Centisome Percentage:2.76
Left Sequence End127912
Right Sequence End129336
Gene Sequence:
>1425 bp
ATGAGTACTGAAATCAAAACTCAGGTCGTGGTACTTGGGGCAGGCCCCGCAGGTTACTCC
GCTGCCTTCCGTTGCGCTGATTTAGGTCTGGAAACCGTAATCGTAGAACGTTACAACACC
CTTGGCGGTGTTTGCCTGAACGTCGGCTGTATCCCTTCTAAAGCACTGCTGCACGTAGCA
AAAGTTATCGAAGAAGCCAAAGCGCTGGCTGAACACGGTATCGTCTTCGGCGAACCGAAA
ACCGATATCGACAAGATTCGTACCTGGAAAGAGAAAGTGATCAATCAGCTGACCGGTGGT
CTGGCTGGTATGGCGAAAGGCCGCAAAGTCAAAGTGGTCAACGGTCTGGGTAAATTCACC
GGGGCTAACACCCTGGAAGTTGAAGGTGAGAACGGCAAAACCGTGATCAACTTCGACAAC
GCGATCATTGCAGCGGGTTCTCGCCCGATCCAACTGCCGTTTATTCCGCATGAAGATCCG
CGTATCTGGGACTCCACTGACGCGCTGGAACTGAAAGAAGTACCAGAACGCCTGCTGGTA
ATGGGTGGCGGTATCATCGGTCTGGAAATGGGCACCGTTTACCACGCGCTGGGTTCACAG
ATTGACGTGGTTGAAATGTTCGACCAGGTTATCCCGGCAGCTGACAAAGACATCGTTAAA
GTCTTCACCAAGCGTATCAGCAAGAAATTCAACCTGATGCTGGAAACCAAAGTTACCGCC
GTTGAAGCGAAAGAAGACGGCATTTATGTGACGATGGAAGGCAAAAAAGCACCCGCTGAA
CCGCAGCGTTACGACGCCGTGCTGGTAGCGATTGGTCGTGTGCCGAACGGTAAAAACCTC
GACGCAGGCAAAGCAGGCGTGGAAGTTGACGACCGTGGTTTCATCCGCGTTGACAAACAG
CTGCGTACCAACGTACCGCACATCTTTGCTATCGGCGATATCGTCGGTCAACCGATGCTG
GCACACAAAGGTGTTCACGAAGGTCACGTTGCCGCTGAAGTTATCGCCGGTAAGAAACAC
TACTTCGATCCGAAAGTTATCCCGTCCATCGCCTATACCGAACCAGAAGTTGCATGGGTG
GGTCTGACTGAGAAAGAAGCGAAAGAGAAAGGCATCAGCTATGAAACCGCCACCTTCCCG
TGGGCTGCTTCTGGTCGTGCTATCGCTTCCGACTGCGCAGACGGTATGACCAAGCTGATT
TTCGACAAAGAATCTCACCGTGTGATCGGTGGTGCGATTGTCGGTACTAACGGCGGCGAG
CTGCTGGGTGAAATCGGCCTGGCAATCGAAATGGGTTGTGATGCTGAAGACATCGCACTG
ACCATCCACGCGCACCCGACTCTGCACGAGTCTGTGGGCCTGGCGGCAGAAGTGTTCGAA
GGTAGCATTACCGACCTGCCGAACCCGAAAGCGAAGAAGAAGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:474
Protein Molecular Weight:50688
Protein Theoretical pI:6
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Dihydrolipoyl dehydrogenase
MSTEIKTQVVVLGAGPAGYSAAFRCADLGLETVIVERYNTLGGVCLNVGCIPSKALLHVA
KVIEEAKALAEHGIVFGEPKTDIDKIRTWKEKVINQLTGGLAGMAKGRKVKVVNGLGKFT
GANTLEVEGENGKTVINFDNAIIAAGSRPIQLPFIPHEDPRIWDSTDALELKEVPERLLV
MGGGIIGLEMGTVYHALGSQIDVVEMFDQVIPAADKDIVKVFTKRISKKFNLMLETKVTA
VEAKEDGIYVTMEGKKAPAEPQRYDAVLVAIGRVPNGKNLDAGKAGVEVDDRGFIRVDKQ
LRTNVPHIFAIGDIVGQPMLAHKGVHEGHVAAEVIAGKKHYFDPKVIPSIAYTEPEVAWV
GLTEKEAKEKGISYETATFPWAASGRAIASDCADGMTKLIFDKESHRVIGGAIVGTNGGE
LLGEIGLAIEMGCDAEDIALTIHAHPTLHESVGLAAEVFEGSITDLPNPKAKKK
References
External Links:
ResourceLink
Uniprot ID:P0A9P0
Uniprot Name:DLDH_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674337
Ecogene ID:EG10543
Ecocyc:EG10543
ColiBase:b0116
Kegg Gene:b0116
EchoBASE ID:EB0538
CCDB:DLDH_ECOLI
BacMap:16128109
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
  • Fujita, N., Mori, H., Yura, T., Ishihama, A. (1994). "Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region." Nucleic Acids Res 22:1637-1639. Pubmed: 8202364
  • 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
  • Link, A. J., Robison, K., Church, G. M. (1997). "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Electrophoresis 18:1259-1313. Pubmed: 9298646
  • Steiert, P. S., Stauffer, L. T., Stauffer, G. V. (1990). "The lpd gene product functions as the L protein in the Escherichia coli glycine cleavage enzyme system." J Bacteriol 172:6142-6144. Pubmed: 2211531
  • Stenberg, F., Chovanec, P., Maslen, S. L., Robinson, C. V., Ilag, L. L., von Heijne, G., Daley, D. O. (2005). "Protein complexes of the Escherichia coli cell envelope." J Biol Chem 280:34409-34419. Pubmed: 16079137
  • Stephens, P. E., Lewis, H. M., Darlison, M. G., Guest, J. R. (1983). "Nucleotide sequence of the lipoamide dehydrogenase gene of Escherichia coli K12." Eur J Biochem 135:519-527. Pubmed: 6352260
  • Zhang, J., Sprung, R., Pei, J., Tan, X., Kim, S., Zhu, H., Liu, C. F., Grishin, N. V., Zhao, Y. (2009). "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli." Mol Cell Proteomics 8:215-225. Pubmed: 18723842