Identification
Name:Succinate dehydrogenase flavoprotein subunit
Synonyms:Not Available
Gene Name:sdhA
Enzyme Class:
Biological Properties
General Function:Involved in electron carrier activity
Specific Function:Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; the fumarate reductase is used in anaerobic growth, and the succinate dehydrogenase is used in aerobic growth
Cellular Location:Cell inner membrane; Peripheral membrane protein; Cytoplasmic side
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
Thumb+ThumbThumb+Thumb
Thumb+AcceptorThumb+Reduced acceptor
Succinic acid + Acceptor ↔ Fumaric acid + Reduced acceptor
ReactionCard
Thumb+ThumbThumb+Thumb
SMPDB Reactions:
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Ubiquinol 8+Thumb
Thumb+Coenzyme Q9Thumb+Thumb
Thumb+ThumbThumb+Ubiquinol-10+Thumb
Thumb+ThumbUbiquinol-0+Thumb
Complex Reactions:
Thumb+ThumbThumb+Thumb
Thumb+acceptorThumb+reduced acceptor
Succinic acid + acceptor → Fumaric acid + reduced acceptor
ReactionCard
Thumb+acceptorThumb+reduced acceptor
Succinic acid + acceptor → Fumaric acid + reduced acceptor
ReactionCard
Thumb+acceptorThumb+reduced acceptor
Succinic acid + acceptor → Fumaric acid + reduced acceptor
ReactionCard
Thumb+acceptorThumb+reduced acceptor
Succinic acid + acceptor → Fumaric acid + reduced acceptor
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB01248FADMetaboCard
ECMDB01197FADH2MetaboCard
ECMDB00176Fumaric acidMetaboCard
ECMDB02434HydroquinoneMetaboCard
ECMDB23060QuinoneMetaboCard
ECMDB00254Succinic acidMetaboCard
ECMDB21574Ubiquinol-1MetaboCard
ECMDB20619Ubiquinol-10MetaboCard
ECMDB21575Ubiquinol-2MetaboCard
ECMDB21576Ubiquinol-3MetaboCard
ECMDB21577Ubiquinol-4MetaboCard
ECMDB21578Ubiquinol-5MetaboCard
ECMDB21460Ubiquinol-6MetaboCard
ECMDB21579Ubiquinol-7MetaboCard
ECMDB01060Ubiquinol-8MetaboCard
ECMDB21580Ubiquinol-9MetaboCard
ECMDB20487Ubiquinone-0MetaboCard
ECMDB21438Ubiquinone-1MetaboCard
ECMDB01072Ubiquinone-10MetaboCard
ECMDB21581Ubiquinone-2MetaboCard
ECMDB21582Ubiquinone-3MetaboCard
ECMDB23735Ubiquinone-4MetaboCard
ECMDB23734Ubiquinone-5MetaboCard
ECMDB20620Ubiquinone-6MetaboCard
ECMDB21584Ubiquinone-7MetaboCard
ECMDB21296Ubiquinone-8MetaboCard
GO Classification:
Function
adenyl nucleotide binding
binding
catalytic activity
electron carrier activity
FAD or FADH2 binding
nucleoside binding
oxidoreductase activity
oxidoreductase activity, acting on the CH-CH group of donors
purine nucleoside binding
Process
acetyl-CoA catabolic process
acetyl-CoA metabolic process
cellular metabolic process
coenzyme metabolic process
cofactor metabolic process
electron transport chain
generation of precursor metabolites and energy
metabolic process
oxidation reduction
tricarboxylic acid cycle
Gene Properties
Blattner:b0723
Gene OrientationClockwise
Centisome Percentage:16.28
Left Sequence End755130
Right Sequence End756896
Gene Sequence:
>1767 bp
ATGAAAGCAGCGGCGAAAACGCAGAAACCAAAACGTCAGGAAGAACATGCCAACTTTATC
AGTTGGCGTTTTGCGTTGTTATGCGGCTGTATTCTCCTGGCGCTGGCTTTTCTGCTCGGA
CGCGTAGCGTGGTTACAAGTTATCTCCCCGGATATGCTGGTGAAAGAGGGCGACATGCGT
TCTCTTCGCGTTCAGCAAGTTTCCACCTCCCGCGGCATGATTACTGACCGTTCTGGTCGC
CCGTTAGCGGTGAGCGTGCCGGTAAAAGCGATTTGGGCTGACCCGAAAGAAGTGCATGAC
GCTGGCGGTATCAGCGTCGGTGACCGCTGGAAGGCGCTGGCTAACGCGCTCAATATTCCG
CTGGATCAGCTTTCAGCCCGCATTAACGCCAACCCGAAAGGGCGCTTTATTTATCTGGCG
CGTCAGGTGAACCCTGACATGGCGGACTACATCAAAAAACTGAAACTGCCGGGGATTCAT
CTGCGTGAAGAGTCTCGCCGTTACTATCCGTCCGGCGAAGTGACTGCTCACCTCATCGGC
TTTACTAACGTCGATAGTCAAGGGATTGAGGGCGTTGAGAAGAGTTTCGATAAATGGCTT
ACCGGGCAGCCGGGTGAGCGCATTGTGCGTAAAGACCGCTATGGTCGCGTAATTGAAGAT
ATTTCTTCTACTGACAGCCAGGCAGCGCACAACCTGGCGCTGAGTATTGATGAACGCCTG
CAGGCGCTGGTTTATCGCGAACTGAACAACGCGGTGGCCTTTAACAAGGCTGAATCTGGT
AGCGCCGTGCTGGTGGATGTCAACACCGGTGAAGTGCTGGCGATGGCTAACAGCCCGTCA
TACAACCCTAACAATCTGAGCGGCACGCCGAAAGAGGCGATGCGTAACCGTACCATCACC
GACGTGTTTGAACCGGGCTCAACGGTTAAACCGATGGTGGTAATGACCGCGTTGCAACGT
GGCGTGGTGCGGGAAAACTCGGTACTCAATACCATTCCTTATCGAATTAACGGCCACGAA
ATCAAAGACGTGGCACGCTACAGCGAATTAACCCTGACCGGGGTATTACAGAAGTCGAGT
AACGTCGGTGTTTCCAAGCTGGCGTTAGCGATGCCGTCCTCAGCGTTAGTAGATACTTAC
TCACGTTTTGGACTGGGAAAAGCGACCAATTTGGGGTTGGTCGGAGAACGCAGTGGCTTA
TATCCTCAAAAACAACGGTGGTCTGACATAGAGAGGGCCACCTTCTCTTTCGGCTACGGG
CTAATGGTAACACCATTACAGTTAGCGCGAGTCTACGCAACTATCGGCAGCTACGGCATT
TATCGCCCACTGTCGATTACCAAAGTTGACCCCCCGGTTCCCGGTGAACGTGTCTTCCCG
GAATCCATTGTCCGCACTGTGGTGCATATGATGGAAAGCGTGGCGCTACCAGGCGGCGGC
GGCGTGAAGGCGGCGATTAAAGGCTATCGTATCGCCATTAAAACCGGTACCGCGAAAAAG
GTCGGGCCGGACGGTCGCTACATCAATAAATATATTGCTTATACCGCAGGCGTTGCGCCT
GCGAGTCAGCCGCGCTTCGCGCTGGTTGTTGTTATCAACGATCCGCAGGCGGGTAAATAC
TACGGCGGCGCCGTTTCCGCGCCGGTCTTTGGTGCCATCATGGGCGGCGTATTGCGTACC
ATGAACATCGAGCCGGATGCGCTGACAACGGGCGATAAAAATGAATTTGTGATTAATCAA
GGCGAGGGGACAGGTGGCAGATCGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:588
Protein Molecular Weight:64421
Protein Theoretical pI:6
PDB File:1NEN
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Succinate dehydrogenase flavoprotein subunit
MKLPVREFDAVVIGAGGAGMRAALQISQSGQTCALLSKVFPTRSHTVSAQGGITVALGNT
HEDNWEWHMYDTVKGSDYIGDQDAIEYMCKTGPEAILELEHMGLPFSRLDDGRIYQRPFG
GQSKNFGGEQAARTAAAADRTGHALLHTLYQQNLKNHTTIFSEWYALDLVKNQDGAVVGC
TALCIETGEVVYFKARATVLATGGAGRIYQSTTNAHINTGDGVGMAIRAGVPVQDMEMWQ
FHPTGIAGAGVLVTEGCRGEGGYLLNKHGERFMERYAPNAKDLAGRDVVARSIMIEIREG
RGCDGPWGPHAKLKLDHLGKEVLESRLPGILELSRTFAHVDPVKEPIPVIPTCHYMMGGI
PTKVTGQALTVNEKGEDVVVPGLFAVGEIACVSVHGANRLGGNSLLDLVVFGRAAGLHLQ
ESIAEQGALRDASESDVEASLDRLNRWNNNRNGEDPVAIRKALQECMQHNFSVFREGDAM
AKGLEQLKVIRERLKNARLDDTSSEFNTQRVECLELDNLMETAYATAVSANFRTESRGAH
SRFDFPDRDDENWLCHSLYLPESESMTRRSVNMEPKLRPAFPPKIRTY
References
External Links:
ResourceLink
Uniprot ID:P0AC41
Uniprot Name:DHSA_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:21321965
PDB ID:1NEN
Ecogene ID:EG10931
Ecocyc:EG10931
ColiBase:b0723
Kegg Gene:b0723
EchoBASE ID:EB0924
CCDB:DHSA_ECOLI
BacMap:16128698
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., Guest, J. R. (1984). "Nucleotide sequence encoding the iron-sulphur protein subunit of the succinate dehydrogenase of Escherichia coli." Biochem J 223:507-517. Pubmed: 6388571
  • 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
  • Horsefield, R., Yankovskaya, V., Sexton, G., Whittingham, W., Shiomi, K., Omura, S., Byrne, B., Cecchini, G., Iwata, S. (2006). "Structural and computational analysis of the quinone-binding site of complex II (succinate-ubiquinone oxidoreductase): a mechanism of electron transfer and proton conduction during ubiquinone reduction." J Biol Chem 281:7309-7316. Pubmed: 16407191
  • 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
  • Ruprecht, J., Yankovskaya, V., Maklashina, E., Iwata, S., Cecchini, G. (2009). "Structure of Escherichia coli succinate:quinone oxidoreductase with an occupied and empty quinone-binding site." J Biol Chem 284:29836-29846. Pubmed: 19710024
  • 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
  • Wilkins, M. R., Gasteiger, E., Tonella, L., Ou, K., Tyler, M., Sanchez, J. C., Gooley, A. A., Walsh, B. J., Bairoch, A., Appel, R. D., Williams, K. L., Hochstrasser, D. F. (1998). "Protein identification with N and C-terminal sequence tags in proteome projects." J Mol Biol 278:599-608. Pubmed: 9600841
  • Wood, D., Darlison, M. G., Wilde, R. J., Guest, J. R. (1984). "Nucleotide sequence encoding the flavoprotein and hydrophobic subunits of the succinate dehydrogenase of Escherichia coli." Biochem J 222:519-534. Pubmed: 6383359
  • Yankovskaya, V., Horsefield, R., Tornroth, S., Luna-Chavez, C., Miyoshi, H., Leger, C., Byrne, B., Cecchini, G., Iwata, S. (2003). "Architecture of succinate dehydrogenase and reactive oxygen species generation." Science 299:700-704. Pubmed: 12560550
  • 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