Identification
Name:Succinate dehydrogenase iron-sulfur subunit
Synonyms:Not Available
Gene Name:sdhB
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
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
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
binding
catalytic activity
electron carrier activity
iron-sulfur cluster binding
metal cluster binding
oxidoreductase activity
Process
acetyl-CoA catabolic process
acetyl-CoA metabolic process
cellular metabolic process
coenzyme metabolic process
cofactor metabolic process
metabolic process
oxidation reduction
tricarboxylic acid cycle
Gene Properties
Blattner:b0724
Gene OrientationClockwise
Centisome Percentage:16.31
Left Sequence End756912
Right Sequence End757628
Gene Sequence:
>717 bp
ATGAGACTCGAGTTTTCAATTTATCGCTATAACCCGGATGTTGATGATGCTCCGCGTATG
CAGGATTACACCCTGGAAGCGGATGAAGGTCGCGACATGATGCTGCTGGATGCGCTTATC
CAGCTAAAAGAGAAAGATCCCAGCCTGTCGTTCCGCCGCTCCTGCCGTGAAGGTGTGTGC
GGTTCCGACGGTCTGAACATGAACGGCAAGAATGGTCTGGCCTGTATTACCCCGATTTCG
GCACTCAACCAGCCGGGCAAGAAGATTGTGATTCGCCCGCTGCCAGGTTTACCGGTGATC
CGCGATTTGGTGGTAGACATGGGACAATTCTATGCGCAATATGAGAAAATTAAGCCTTAC
CTGTTGAATAATGGACAAAATCCGCCAGCTCGCGAGCATTTACAGATGCCAGAGCAGCGC
GAAAAACTCGACGGGCTGTATGAATGTATTCTCTGCGCATGTTGTTCAACCTCTTGTCCG
TCTTTCTGGTGGAATCCCGATAAGTTTATCGGCCCGGCAGGCTTGTTAGCGGCATATCGT
TTCCTGATTGATAGCCGTGATACCGAGACTGACAGCCGCCTCGACGGTTTGAGTGATGCA
TTCAGCGTATTCCGCTGTCACAGCATCATGAACTGCGTCAGTGTATGTCCGAAGGGGCTG
AACCCGACGCGCGCCATCGGCCATATCAAGTCGATGTTGTTGCAACGTAATGCGTAA
Protein Properties
Pfam Domain Function:Not Available
Protein Residues:238
Protein Molecular Weight:26770
Protein Theoretical pI:7
PDB File:1NEN
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Succinate dehydrogenase iron-sulfur subunit
MRLEFSIYRYNPDVDDAPRMQDYTLEADEGRDMMLLDALIQLKEKDPSLSFRRSCREGVC
GSDGLNMNGKNGLACITPISALNQPGKKIVIRPLPGLPVIRDLVVDMGQFYAQYEKIKPY
LLNNGQNPPAREHLQMPEQREKLDGLYECILCACCSTSCPSFWWNPDKFIGPAGLLAAYR
FLIDSRDTETDSRLDGLSDAFSVFRCHSIMNCVSVCPKGLNPTRAIGHIKSMLLQRNA
References
External Links:
ResourceLink
Uniprot ID:P07014
Uniprot Name:DHSB_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:1651320
PDB ID:1NEN
Ecogene ID:EG10932
Ecocyc:EG10932
ColiBase:b0724
Kegg Gene:b0724
EchoBASE ID:EB0925
CCDB:DHSB_ECOLI
BacMap:16128699
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
  • 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
  • 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
  • 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