Identification
Name:Succinate dehydrogenase cytochrome b556 subunit
Synonyms:
  • Cytochrome b-556
Gene Name:sdhC
Enzyme Class:Not Available
Biological Properties
General Function:Involved in succinate dehydrogenase activity
Specific Function:Membrane-anchoring subunit of succinate dehydrogenase (SDH)
Cellular Location:Cell inner membrane; Multi-pass membrane protein
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
Thumb+ThumbThumb+Thumb
Thumb+AcceptorThumb+Reduced acceptor
Succinic acid + Acceptor ↔ Fumaric acid + Reduced acceptor
ReactionCard
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
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:
Component
cell part
membrane
membrane part
plasma membrane part
plasma membrane succinate dehydrogenase complex
Function
catalytic activity
electron carrier activity
oxidoreductase activity
oxidoreductase activity, acting on the CH-CH group of donors
succinate dehydrogenase activity
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:b0721
Gene OrientationClockwise
Centisome Percentage:16.26
Left Sequence End754400
Right Sequence End754789
Gene Sequence:
>390 bp
ATGAAAAAGCTGCAAATTGCGGTAGGTATTATTCGCAACGAGAACAATGAAATCTTTATA
ACGCGTCGCGCAGCAGATGCGCACATGGCGAATAAACTGGAGTTTCCCGGCGGTAAAATT
GAAATGGGTGAAACGCCGGAACAGGCGGTGGTGCGTGAACTTCAGGAAGAAGTCGGGATT
ACCCCCCAACATTTTTCGCTATTTGAAAAACTGGAATATGAATTCCCGGACAGGCATATA
ACACTGTGGTTTTGGCTGGTCGAACGCTGGGAAGGGGAGCCGTGGGGTAAAGAAGGGCAA
CCCGGTGAGTGGATGTCGCTGGTCGGTCTTAATGCCGATGATTTTCCGCCAGCCAATGAA
CCGGTAATTGCGAAGCTTAAACGTCTGTAG
Protein Properties
Pfam Domain Function:
Protein Residues:129
Protein Molecular Weight:14299
Protein Theoretical pI:10
PDB File:1NEN
Signaling Regions:
  • None
Transmembrane Regions:
  • 27-52
  • 69-89
  • 109-129
Protein Sequence:
>Succinate dehydrogenase cytochrome b556 subunit
MIRNVKKQRPVNLDLQTIRFPITAIASILHRVSGVITFVAVGILLWLLGTSLSSPEGFEQ
ASAIMGSFFVKFIMWGILTALAYHVVVGIRHMMMDFGYLEETFEAGKRSAKISFVITVVL
SLLAGVLVW
References
External Links:
ResourceLink
Uniprot ID:P69054
Uniprot Name:DHSC_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:21321980
PDB ID:1NEN
Ecogene ID:EG10933
Ecocyc:EG10933
ColiBase:b0721
Kegg Gene:b0721
EchoBASE ID:EB0926
CCDB:DHSC_ECOLI
BacMap:16128696
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
  • Daley, D. O., Rapp, M., Granseth, E., Melen, K., Drew, D., von Heijne, G. (2005). "Global topology analysis of the Escherichia coli inner membrane proteome." Science 308:1321-1323. Pubmed: 15919996
  • 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
  • Maklashina, E., Rothery, R. A., Weiner, J. H., Cecchini, G. (2001). "Retention of heme in axial ligand mutants of succinate-ubiquinone xxidoreductase (complex II) from Escherichia coli." J Biol Chem 276:18968-18976. Pubmed: 11259408
  • 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
  • Vibat, C. R., Cecchini, G., Nakamura, K., Kita, K., Gennis, R. B. (1998). "Localization of histidine residues responsible for heme axial ligation in cytochrome b556 of complex II (succinate:ubiquinone oxidoreductase) in Escherichia coli." Biochemistry 37:4148-4159. Pubmed: 9521736
  • Wilde, R. J., Guest, J. R. (1986). "Transcript analysis of the citrate synthase and succinate dehydrogenase genes of Escherichia coli K12." J Gen Microbiol 132:3239-3251. Pubmed: 3309132
  • 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
  • Yang, X., Yu, L., He, D., Yu, C. A. (1998). "The quinone-binding site in succinate-ubiquinone reductase from Escherichia coli. Quinone-binding domain and amino acid residues involved in quinone binding." J Biol Chem 273:31916-31923. Pubmed: 9822661
  • 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