Identification
Name:2-oxoglutarate dehydrogenase E1 component
Synonyms:
  • Alpha-ketoglutarate dehydrogenase
Gene Name:sucA
Enzyme Class:
Biological Properties
General Function:Involved in oxoglutarate dehydrogenase (succinyl-transferring) activity
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+1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0Thumb+1.0Enzyme N6-(lipoyl)lysine1.0[Dihydrolipoyllysine-residue succinyltransferase] S-glutaryldihydrolipoyllysine+1.0Thumb
1.0Oxoadipic acid + 1.0Enzyme N6-(lipoyl)lysine ↔ 1.0[Dihydrolipoyllysine-residue succinyltransferase] S-glutaryldihydrolipoyllysine + 1.0Carbon dioxide
ReactionCard
1.0Thumb1.0[Dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine+1.0Thumb
1.0alpha-Ketoglutarate ↔ 1.0[Dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + 1.0Carbon dioxide
ReactionCard
SMPDB Reactions:
1.0Thumb+1.0Thumb+1.0Thumb1.0Thumb+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-lipoyl-L-lysine+1.0Thumb+1.0Thumb1.0a [2-oxoglutarate dehydrogenase E2 protein] N6-S-succinyldihydrolipoyl-L-lysine+1.0Thumb
1.0a [2-oxoglutarate dehydrogenase E2 protein] N6-lipoyl-L-lysine + 1.0Oxoglutaric acid + 1.0Hydrogen ion → 1.0a [2-oxoglutarate dehydrogenase E2 protein] N6-S-succinyldihydrolipoyl-L-lysine + 1.0Carbon dioxide
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb+1.0Thumb
1.0Thumb+1.0[dihydrolipoyllysine-residue succinyltransferase] lipoyllysine1.0[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine+1.0Thumb
1.0Oxoglutaric acid + 1.0[dihydrolipoyllysine-residue succinyltransferase] lipoyllysine → 1.0[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + 1.0Carbon dioxide
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB02812alpha-KetoglutarateMetaboCard
ECMDB04030Carbon dioxideMetaboCard
ECMDB01423Coenzyme AMetaboCard
ECMDB01339Glutaryl-CoAMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB00902NADMetaboCard
ECMDB01487NADHMetaboCard
ECMDB00225Oxoadipic acidMetaboCard
ECMDB04123Oxoglutaric acidMetaboCard
ECMDB01022Succinyl-CoAMetaboCard
ECMDB01372Thiamine pyrophosphateMetaboCard
GO Classification:
Function
binding
catalytic activity
oxidoreductase activity
oxidoreductase activity, acting on the aldehyde or oxo group of donors
oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor
oxoglutarate dehydrogenase (succinyl-transferring) activity
thiamin pyrophosphate binding
vitamin binding
Process
alcohol metabolic process
glucose catabolic process
glucose metabolic process
glycolysis
hexose metabolic process
metabolic process
monosaccharide metabolic process
small molecule metabolic process
Gene Properties
Blattner:b0726
Gene OrientationClockwise
Centisome Percentage:16.34
Left Sequence End757929
Right Sequence End760730
Gene Sequence:
>2802 bp
ATGCAGAACAGCGCTTTGAAAGCCTGGTTGGACTCTTCTTACCTCTCTGGCGCAAACCAG
AGCTGGATAGAACAGCTCTATGAAGACTTCTTAACCGATCCTGACTCGGTTGACGCTAAC
TGGCGTTCGACGTTCCAGCAGTTACCTGGTACGGGAGTCAAACCGGATCAATTCCACTCT
CAAACGCGTGAATATTTCCGCCGCCTGGCGAAAGACGCTTCACGTTACTCTTCAACGATC
TCCGACCCTGACACCAATGTGAAGCAGGTTAAAGTCCTGCAGCTCATTAACGCATACCGC
TTCCGTGGTCACCAGCATGCGAATCTCGATCCGCTGGGACTGTGGCAGCAAGATAAAGTG
GCCGATCTGGATCCGTCTTTCCACGATCTGACCGAAGCAGACTTCCAGGAGACCTTCAAC
GTCGGTTCATTTGCCAGCGGCAAAGAAACCATGAAACTCGGCGAGCTGCTGGAAGCCCTC
AAGCAAACCTACTGCGGCCCGATTGGTGCCGAGTATATGCACATTACCAGCACCGAAGAA
AAACGCTGGATCCAACAGCGTATCGAGTCTGGTCGCGCGACTTTCAATAGCGAAGAGAAA
AAACGCTTCTTAAGCGAACTGACCGCCGCTGAAGGTCTTGAACGTTACCTCGGCGCAAAA
TTCCCTGGCGCAAAACGCTTCTCGCTGGAAGGCGGTGACGCGTTAATCCCGATGCTTAAA
GAGATGATCCGCCACGCTGGCAACAGCGGCACCCGCGAAGTGGTTCTCGGGATGGCGCAC
CGTGGTCGTCTGAACGTGCTGGTGAACGTGCTGGGTAAAAAACCGCAAGACTTGTTCGAC
GAGTTCGCCGGTAAACATAAAGAACACCTCGGCACGGGTGACGTGAAATACCACATGGGC
TTCTCGTCTGACTTCCAGACCGATGGCGGCCTGGTGCACCTGGCGCTGGCGTTTAACCCG
TCTCACCTTGAGATTGTAAGCCCGGTAGTTATCGGTTCTGTTCGTGCCCGTCTGGACAGA
CTTGATGAGCCGAGCAGCAACAAAGTGCTGCCAATCACCATCCACGGTGACGCCGCAGTG
ACCGGGCAGGGCGTGGTTCAGGAAACCCTGAACATGTCGAAAGCGCGTGGTTATGAAGTT
GGCGGTACGGTACGTATCGTTATCAACAACCAGGTTGGTTTCACCACCTCTAATCCGCTG
GATGCCCGTTCTACGCCGTACTGTACTGATATCGGTAAGATGGTTCAGGCCCCGATTTTC
CACGTTAACGCGGACGATCCGGAAGCCGTTGCCTTTGTGACCCGTCTGGCGCTCGATTTC
CGTAACACCTTTAAACGTGATGTCTTCATCGACCTGGTGTGCTACCGCCGTCACGGCCAC
AACGAAGCCGACGAGCCGAGCGCAACCCAGCCGCTGATGTATCAGAAAATCAAAAAACAT
CCGACACCGCGCAAAATCTACGCTGACAAGCTGGAGCAGGAAAAAGTGGCGACGCTGGAA
GATGCCACCGAGATGGTTAACCTGTACCGCGATGCGCTGGATGCTGGCGATTGCGTAGTG
GCAGAGTGGCGTCCGATGAACATGCACTCTTTCACCTGGTCGCCGTACCTCAACCACGAA
TGGGACGAAGAGTACCCGAACAAAGTTGAGATGAAGCGCCTGCAGGAGCTGGCGAAACGC
ATCAGCACGGTGCCGGAAGCAGTTGAAATGCAGTCTCGCGTTGCCAAGATTTATGGCGAT
CGCCAGGCGATGGCTGCCGGTGAGAAACTGTTCGACTGGGGCGGTGCGGAAAACCTCGCT
TACGCCACGCTGGTTGATGAAGGCATTCCGGTTCGCCTGTCGGGTGAAGACTCCGGTCGC
GGTACCTTCTTCCACCGCCACGCGGTGATCCACAACCAGTCTAACGGTTCCACTTACACG
CCGCTGCAACATATCCATAACGGGCAGGGCGCGTTCCGTGTCTGGGACTCCGTACTGTCT
GAAGAAGCAGTGCTGGCGTTTGAATATGGTTATGCCACCGCAGAACCACGCACTCTGACC
ATCTGGGAAGCGCAGTTCGGTGACTTCGCCAACGGTGCGCAGGTGGTTATCGACCAGTTC
ATCTCCTCTGGCGAACAGAAATGGGGCCGGATGTGTGGTCTGGTGATGTTGCTGCCGCAC
GGTTACGAAGGGCAGGGGCCGGAGCACTCCTCCGCGCGTCTGGAACGTTATCTGCAACTT
TGTGCTGAGCAAAACATGCAGGTTTGCGTACCGTCTACCCCGGCACAGGTTTACCACATG
CTGCGTCGTCAGGCGCTGCGCGGGATGCGTCGTCCGCTGGTCGTGATGTCGCCGAAATCC
CTGCTGCGTCATCCGCTGGCGGTTTCCAGCCTCGAAGAACTGGCGAACGGCACCTTCCTG
CCAGCCATCGGTGAAATCGACGAGCTTGATCCGAAGGGCGTGAAGCGCGTAGTGATGTGT
TCTGGTAAGGTTTATTACGACCTGCTGGAACAGCGTCGTAAGAACAATCAACACGATGTC
GCCATTGTGCGTATCGAGCAACTCTACCCGTTCCCGCATAAAGCGATGCAGGAAGTGTTG
CAGCAGTTTGCTCACGTCAAGGATTTTGTCTGGTGCCAGGAAGAGCCGCTCAACCAGGGC
GCATGGTACTGCAGCCAGCATCATTTCCGTGAAGTGATTCCGTTTGGGGCTTCTCTGCGT
TATGCAGGCCGCCCGGCCTCCGCCTCTCCGGCGGTAGGGTATATGTCCGTTCACCAGAAA
CAGCAACAAGATCTGGTTAATGACGCGCTGAACGTCGAATAA
Protein Properties
Pfam Domain Function:
Protein Residues:933
Protein Molecular Weight:105061
Protein Theoretical pI:6
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>2-oxoglutarate dehydrogenase E1 component
MQNSALKAWLDSSYLSGANQSWIEQLYEDFLTDPDSVDANWRSTFQQLPGTGVKPDQFHS
QTREYFRRLAKDASRYSSTISDPDTNVKQVKVLQLINAYRFRGHQHANLDPLGLWQQDKV
ADLDPSFHDLTEADFQETFNVGSFASGKETMKLGELLEALKQTYCGPIGAEYMHITSTEE
KRWIQQRIESGRATFNSEEKKRFLSELTAAEGLERYLGAKFPGAKRFSLEGGDALIPMLK
EMIRHAGNSGTREVVLGMAHRGRLNVLVNVLGKKPQDLFDEFAGKHKEHLGTGDVKYHMG
FSSDFQTDGGLVHLALAFNPSHLEIVSPVVIGSVRARLDRLDEPSSNKVLPITIHGDAAV
TGQGVVQETLNMSKARGYEVGGTVRIVINNQVGFTTSNPLDARSTPYCTDIGKMVQAPIF
HVNADDPEAVAFVTRLALDFRNTFKRDVFIDLVCYRRHGHNEADEPSATQPLMYQKIKKH
PTPRKIYADKLEQEKVATLEDATEMVNLYRDALDAGDCVVAEWRPMNMHSFTWSPYLNHE
WDEEYPNKVEMKRLQELAKRISTVPEAVEMQSRVAKIYGDRQAMAAGEKLFDWGGAENLA
YATLVDEGIPVRLSGEDSGRGTFFHRHAVIHNQSNGSTYTPLQHIHNGQGAFRVWDSVLS
EEAVLAFEYGYATAEPRTLTIWEAQFGDFANGAQVVIDQFISSGEQKWGRMCGLVMLLPH
GYEGQGPEHSSARLERYLQLCAEQNMQVCVPSTPAQVYHMLRRQALRGMRRPLVVMSPKS
LLRHPLAVSSLEELANGTFLPAIGEIDELDPKGVKRVVMCSGKVYYDLLEQRRKNNQHDV
AIVRIEQLYPFPHKAMQEVLQQFAHVKDFVWCQEEPLNQGAWYCSQHHFREVIPFGASLR
YAGRPASASPAVGYMSVHQKQQQDLVNDALNVE
References
External Links:
ResourceLink
Uniprot ID:P0AFG3
Uniprot Name:ODO1_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:1651321
Ecogene ID:EG10979
Ecocyc:EG10979
ColiBase:b0726
Kegg Gene:b0726
EchoBASE ID:EB0972
CCDB:ODO1_ECOLI
BacMap:16128701
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
  • 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