Succinate dehydrogenase cytochrome b556 subunit

Details

Name
Succinate dehydrogenase cytochrome b556 subunit
Synonyms
  • cybA
  • Cytochrome b-556
Gene Name
sdhC
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0012683|Succinate dehydrogenase cytochrome b556 subunit
MIRNVKKQRPVNLDLQTIRFPITAIASILHRVSGVITFVAVGILLWLLGTSLSSPEGFEQ
ASAIMGSFFVKFIMWGILTALAYHVVVGIRHMMMDFGYLEETFEAGKRSAKISFVITVVL
SLLAGVLVW
Number of residues
129
Molecular Weight
14299.03
Theoretical pI
10.46
GO Classification
Functions
electron carrier activity / heme binding / metal ion binding / succinate dehydrogenase (ubiquinone) activity / ubiquinone binding
Processes
aerobic respiration / cytochrome complex assembly / tricarboxylic acid cycle
Components
integral component of membrane / plasma membrane / succinate dehydrogenase complex
General Function
Ubiquinone binding
Specific Function
Membrane-anchoring subunit of succinate dehydrogenase (SDH).
Pfam Domain Function
Transmembrane Regions
27-52 69-89 109-129
Cellular Location
Cell inner membrane
Gene sequence
>lcl|BSEQ0012684|Succinate dehydrogenase cytochrome b556 subunit (sdhC)
ATGATAAGAAATGTGAAAAAACAAAGACCTGTTAATCTGGACCTACAGACCATCCGGTTC
CCCATCACGGCGATAGCGTCCATTCTCCATCGCGTTTCCGGTGTGATCACCTTTGTTGCA
GTGGGCATCCTGCTGTGGCTTCTGGGTACCAGCCTCTCTTCCCCTGAAGGTTTCGAGCAA
GCTTCCGCGATTATGGGCAGCTTCTTCGTCAAATTTATCATGTGGGGCATCCTTACCGCT
CTGGCGTATCACGTCGTCGTAGGTATTCGCCACATGATGATGGATTTTGGCTATCTGGAA
GAAACATTCGAAGCGGGTAAACGCTCCGCCAAAATCTCCTTTGTTATTACTGTCGTGCTT
TCACTTCTCGCAGGAGTCCTCGTATGGTAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP69054
UniProtKB Entry NameDHSC_ECOLI
GenBank Protein ID146196
GenBank Gene IDJ01619
General References
  1. Wood D, Darlison MG, Wilde RJ, Guest JR: Nucleotide sequence encoding the flavoprotein and hydrophobic subunits of the succinate dehydrogenase of Escherichia coli. Biochem J. 1984 Sep 1;222(2):519-34. [Article]
  2. Wilde RJ, Guest JR: Transcript analysis of the citrate synthase and succinate dehydrogenase genes of Escherichia coli K12. J Gen Microbiol. 1986 Dec;132(12):3239-51. [Article]
  3. 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 al.: 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. 1996 Jun 30;3(3):137-55. [Article]
  4. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
  5. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
  6. Yang X, Yu L, He D, Yu CA: 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. 1998 Nov 27;273(48):31916-23. [Article]
  7. Vibat CR, Cecchini G, Nakamura K, Kita K, Gennis RB: Localization of histidine residues responsible for heme axial ligation in cytochrome b556 of complex II (succinate:ubiquinone oxidoreductase) in Escherichia coli. Biochemistry. 1998 Mar 24;37(12):4148-59. [Article]
  8. Maklashina E, Rothery RA, Weiner JH, Cecchini G: Retention of heme in axial ligand mutants of succinate-ubiquinone xxidoreductase (complex II) from Escherichia coli. J Biol Chem. 2001 Jun 1;276(22):18968-76. Epub 2001 Mar 19. [Article]
  9. Daley DO, Rapp M, Granseth E, Melen K, Drew D, von Heijne G: Global topology analysis of the Escherichia coli inner membrane proteome. Science. 2005 May 27;308(5726):1321-3. [Article]
  10. Yankovskaya V, Horsefield R, Tornroth S, Luna-Chavez C, Miyoshi H, Leger C, Byrne B, Cecchini G, Iwata S: Architecture of succinate dehydrogenase and reactive oxygen species generation. Science. 2003 Jan 31;299(5607):700-4. [Article]
  11. Horsefield R, Yankovskaya V, Sexton G, Whittingham W, Shiomi K, Omura S, Byrne B, Cecchini G, Iwata S: 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. 2006 Mar 17;281(11):7309-16. Epub 2005 Dec 27. [Article]
  12. Ruprecht J, Yankovskaya V, Maklashina E, Iwata S, Cecchini G: Structure of Escherichia coli succinate:quinone oxidoreductase with an occupied and empty quinone-binding site. J Biol Chem. 2009 Oct 23;284(43):29836-46. doi: 10.1074/jbc.M109.010058. Epub 2009 Aug 25. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB04631Atpenin A5experimentalunknownDetails
DB076712-[1-METHYLHEXYL]-4,6-DINITROPHENOLexperimentalunknownDetails
DB08690Ubiquinone Q2experimentalunknownDetails