Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex (P0AFG6)

Identification
Name:Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex
Synonyms:
  • 2-oxoglutarate dehydrogenase complex component E2
  • OGDC-E2
  • Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex
Gene Name:sucB
Enzyme Class:
Biological Properties
General Function:Involved in transferase activity, transferring acyl groups
Specific Function:The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It contains multiple copies of three enzymatic components:2- oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3)
Cellular Location:Not Available
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Enzyme N6-(dihydrolipoyl)lysine+1.0Thumb ↔ 1.0Thumb+1.0[Dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine
1.0Succinyl-CoA + 1.0Enzyme N6-(dihydrolipoyl)lysine + 1.0Enzyme N6-(dihydrolipoyl)lysine ↔ 1.0Coenzyme A + 1.0[Dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine
ReactionCard
1.0Thumb+1.0Enzyme N6-(dihydrolipoyl)lysine ↔ 1.0Thumb+1.0[Dihydrolipoyllysine-residue succinyltransferase] S-glutaryldihydrolipoyllysine
1.0Glutaryl-CoA + 1.0Enzyme N6-(dihydrolipoyl)lysine ↔ 1.0Coenzyme A + 1.0[Dihydrolipoyllysine-residue succinyltransferase] S-glutaryldihydrolipoyllysine
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 [2-oxoglutarate dehydrogenase E2 protein] N6-S-succinyldihydrolipoyl-L-lysine+1.0Thumb → 1.0a [2-oxoglutarate dehydrogenase E2 protein] N6-dihydrolipoyl-L-lysine+1.0Thumb
1.0a [2-oxoglutarate dehydrogenase E2 protein] N6-S-succinyldihydrolipoyl-L-lysine + 1.0Succinyl-CoA → 1.0a [2-oxoglutarate dehydrogenase E2 protein] N6-dihydrolipoyl-L-lysine + 1.0Coenzyme A
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
Metabolites:
ECMDB IDNameView
ECMDB02812alpha-KetoglutarateMetaboCard
ECMDB04030Carbon dioxideMetaboCard
ECMDB01423Coenzyme AMetaboCard
ECMDB23785Enzyme N6-(dihydrolipoyl)lysineMetaboCard
ECMDB01339Glutaryl-CoAMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB00902NADMetaboCard
ECMDB01487NADHMetaboCard
ECMDB04123Oxoglutaric acidMetaboCard
ECMDB01022Succinyl-CoAMetaboCard
GO Classification:
Component
macromolecular complex
oxoglutarate dehydrogenase complex
protein complex
Function
acyltransferase activity
binding
catalytic activity
dihydrolipoyllysine-residue succinyltransferase activity
protein binding
S-acyltransferase activity
S-succinyltransferase activity
transferase activity
transferase activity, transferring acyl groups
transferase activity, transferring acyl groups other than amino-acyl groups
Process
acetyl-CoA catabolic process
acetyl-CoA metabolic process
cellular metabolic process
coenzyme metabolic process
cofactor metabolic process
metabolic process
tricarboxylic acid cycle
Gene Properties
Blattner:b0727
Gene OrientationClockwise
Centisome Percentage:16.40
Left Sequence End760745
Right Sequence End761962
Gene Sequence:
>1218 bp
ATGAGTAGCGTAGATATTCTGGTCCCTGACCTGCCTGAATCCGTAGCCGATGCCACCGTC
GCAACCTGGCATAAAAAACCCGGCGACGCAGTCGTACGTGATGAAGTGCTGGTAGAAATC
GAAACTGACAAAGTGGTACTGGAAGTACCGGCATCAGCAGACGGCATTCTGGATGCGGTT
CTGGAAGATGAAGGTACAACGGTAACGTCTCGTCAGATCCTTGGTCGCCTGCGTGAAGGC
AACAGCGCCGGTAAAGAAACCAGCGCCAAATCTGAAGAGAAAGCGTCCACTCCGGCGCAA
CGCCAGCAGGCGTCTCTGGAAGAGCAAAACAACGATGCGTTAAGCCCGGCGATCCGTCGC
CTGCTGGCTGAACACAATCTCGACGCCAGCGCCATTAAAGGCACCGGTGTGGGTGGTCGT
CTGACTCGTGAAGATGTGGAAAAACATCTGGCGAAAGCCCCGGCGAAAGAGTCTGCTCCG
GCAGCGGCTGCTCCGGCGGCGCAACCGGCTCTGGCTGCACGTAGTGAAAAACGTGTCCCG
ATGACTCGCCTGCGTAAGCGTGTGGCAGAGCGTCTGCTGGAAGCGAAAAACTCCACCGCC
ATGCTGACCACGTTCAACGAAGTCAACATGAAGCCGATTATGGATCTGCGTAAGCAGTAC
GGTGAAGCGTTTGAAAAACGCCACGGCATCCGTCTGGGCTTTATGTCCTTCTACGTGAAA
GCGGTGGTTGAAGCCCTGAAACGTTACCCGGAAGTGAACGCTTCTATCGACGGCGATGAC
GTGGTTTACCACAACTATTTCGACGTCAGCATGGCGGTTTCTACGCCGCGCGGCCTGGTG
ACGCCGGTTCTGCGTGATGTCGATACCCTCGGCATGGCAGACATCGAGAAGAAAATCAAA
GAGCTGGCAGTCAAAGGCCGTGACGGCAAGCTGACCGTTGAAGATCTGACCGGTGGTAAC
TTCACCATCACCAACGGTGGTGTGTTCGGTTCCCTGATGTCTACGCCGATCATCAACCCG
CCGCAGAGCGCAATTCTGGGTATGCACGCTATCAAAGATCGTCCGATGGCGGTGAATGGT
CAGGTTGAGATCCTGCCGATGATGTACCTGGCGCTGTCCTACGATCACCGTCTGATCGAT
GGTCGCGAATCCGTGGGCTTCCTGGTAACGATCAAAGAGTTGCTGGAAGATCCGACGCGT
CTGCTGCTGGACGTGTAG
Protein Properties
Pfam Domain Function:
Protein Residues:405
Protein Molecular Weight:44011
Protein Theoretical pI:6
PDB File:1SCZ
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex
MSSVDILVPDLPESVADATVATWHKKPGDAVVRDEVLVEIETDKVVLEVPASADGILDAV
LEDEGTTVTSRQILGRLREGNSAGKETSAKSEEKASTPAQRQQASLEEQNNDALSPAIRR
LLAEHNLDASAIKGTGVGGRLTREDVEKHLAKAPAKESAPAAAAPAAQPALAARSEKRVP
MTRLRKRVAERLLEAKNSTAMLTTFNEVNMKPIMDLRKQYGEAFEKRHGIRLGFMSFYVK
AVVEALKRYPEVNASIDGDDVVYHNYFDVSMAVSTPRGLVTPVLRDVDTLGMADIEKKIK
ELAVKGRDGKLTVEDLTGGNFTITNGGVFGSLMSTPIINPPQSAILGMHAIKDRPMAVNG
QVEILPMMYLALSYDHRLIDGRESVGFLVTIKELLEDPTRLLLDV
References
External Links:
ResourceLink
Uniprot ID:P0AFG6
Uniprot Name:ODO2_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:1651322
PDB ID:1SCZ
Ecogene ID:EG10980
Ecocyc:EG10980
ColiBase:b0727
Kegg Gene:b0727
EchoBASE ID:EB0973
CCDB:ODO2_ECOLI
BacMap:16128702
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
  • Darlison, M. G., Spencer, M. E., Guest, J. R. (1984). "Nucleotide sequence of the sucA gene encoding the 2-oxoglutarate dehydrogenase of Escherichia coli K12." Eur J Biochem 141:351-359. Pubmed: 6376123
  • 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
  • Knapp, J. E., Carroll, D., Lawson, J. E., Ernst, S. R., Reed, L. J., Hackert, M. L. (2000). "Expression, purification, and structural analysis of the trimeric form of the catalytic domain of the Escherichia coli dihydrolipoamide succinyltransferase." Protein Sci 9:37-48. Pubmed: 10739245
  • Knapp, J. E., Mitchell, D. T., Yazdi, M. A., Ernst, S. R., Reed, L. J., Hackert, M. L. (1998). "Crystal structure of the truncated cubic core component of the Escherichia coli 2-oxoglutarate dehydrogenase multienzyme complex." J Mol Biol 280:655-668. Pubmed: 9677295
  • 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
  • Oshima, T., Aiba, H., Baba, T., Fujita, K., Hayashi, K., Honjo, A., Ikemoto, K., Inada, T., Itoh, T., Kajihara, M., Kanai, K., Kashimoto, K., Kimura, S., Kitagawa, M., Makino, K., Masuda, S., Miki, T., Mizobuchi, K., Mori, H., Motomura, K., Nakamura, Y., Nashimoto, H., Nishio, Y., Saito, N., Horiuchi, T., et, a. l. .. (1996). "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." DNA Res 3:137-155. Pubmed: 8905232
  • Ricaud, P. M., Howard, M. J., Roberts, E. L., Broadhurst, R. W., Perham, R. N. (1996). "Three-dimensional structure of the lipoyl domain from the dihydrolipoyl succinyltransferase component of the 2-oxoglutarate dehydrogenase multienzyme complex of Escherichia coli." J Mol Biol 264:179-190. Pubmed: 8950276
  • Robien, M. A., Clore, G. M., Omichinski, J. G., Perham, R. N., Appella, E., Sakaguchi, K., Gronenborn, A. M. (1992). "Three-dimensional solution structure of the E3-binding domain of the dihydrolipoamide succinyltransferase core from the 2-oxoglutarate dehydrogenase multienzyme complex of Escherichia coli." Biochemistry 31:3463-3471. Pubmed: 1554728
  • Spencer, M. E., Darlison, M. G., Stephens, P. E., Duckenfield, I. K., Guest, J. R. (1984). "Nucleotide sequence of the sucB gene encoding the dihydrolipoamide succinyltransferase of Escherichia coli K12 and homology with the corresponding acetyltransferase." Eur J Biochem 141:361-374. Pubmed: 6376124
  • 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