Succinate dehydrogenase iron-sulfur subunit

NameSuccinate dehydrogenase iron-sulfur subunit
Synonyms1.3.5.1
Gene NamesdhB
OrganismEscherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0019477|Succinate dehydrogenase iron-sulfur subunit
MRLEFSIYRYNPDVDDAPRMQDYTLEADEGRDMMLLDALIQLKEKDPSLSFRRSCREGVC
GSDGLNMNGKNGLACITPISALNQPGKKIVIRPLPGLPVIRDLVVDMGQFYAQYEKIKPY
LLNNGQNPPAREHLQMPEQREKLDGLYECILCACCSTSCPSFWWNPDKFIGPAGLLAAYR
FLIDSRDTETDSRLDGLSDAFSVFRCHSIMNCVSVCPKGLNPTRAIGHIKSMLLQRNA
Number of residues238
Molecular Weight26769.545
Theoretical pI6.72
GO Classification
Functions
    3 iron, 4 sulfur cluster binding
succinate dehydrogenase (ubiquinone) activity
metal ion binding
electron carrier activity
4 iron, 4 sulfur cluster binding
iron-sulfur cluster binding
2 iron, 2 sulfur cluster binding
Processes
    tricarboxylic acid cycle
aerobic respiration
Components
    plasma membrane
General FunctionSuccinate dehydrogenase (ubiquinone) activity
Specific FunctionTwo 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.
Transmembrane Regions
GenBank Protein ID146196
UniProtKB IDP07014
UniProtKB Entry NameSDHB_ECOLI
Cellular LocationCell inner membrane
Gene sequence
>lcl|BSEQ0019478|Succinate dehydrogenase iron-sulfur subunit (sdhB)
ATGAGACTCGAGTTTTCAATTTATCGCTATAACCCGGATGTTGATGATGCTCCGCGTATG
CAGGATTACACCCTGGAAGCGGATGAAGGTCGCGACATGATGCTGCTGGATGCGCTTATC
CAGCTAAAAGAGAAAGATCCCAGCCTGTCGTTCCGCCGCTCCTGCCGTGAAGGTGTGTGC
GGTTCCGACGGTCTGAACATGAACGGCAAGAATGGTCTGGCCTGTATTACCCCGATTTCG
GCACTCAACCAGCCGGGCAAGAAGATTGTGATTCGCCCGCTGCCAGGTTTACCGGTGATC
CGCGATTTGGTGGTAGACATGGGACAATTCTATGCGCAATATGAGAAAATTAAGCCTTAC
CTGTTGAATAATGGACAAAATCCGCCAGCTCGCGAGCATTTACAGATGCCAGAGCAGCGC
GAAAAACTCGACGGGCTGTATGAATGTATTCTCTGCGCATGTTGTTCAACCTCTTGTCCG
TCTTTCTGGTGGAATCCCGATAAGTTTATCGGCCCGGCAGGCTTGTTAGCGGCATATCGT
TTCCTGATTGATAGCCGTGATACCGAGACTGACAGCCGCCTCGACGGTTTGAGTGATGCA
TTCAGCGTATTCCGCTGTCACAGCATCATGAACTGCGTCAGTGTATGTCCGAAGGGGCTG
AACCCGACGCGCGCCATCGGCCATATCAAGTCGATGTTGTTGCAACGTAATGCGTAA
GenBank Gene IDJ01619
GeneCard IDNone
GenAtlas ID
HGNC ID
Chromosome LocationNone
LocusNone
References
  1. Darlison MG, Guest JR: Nucleotide sequence encoding the iron-sulphur protein subunit of the succinate dehydrogenase of Escherichia coli. Biochem J. 1984 Oct 15;223(2):507-17.[6388571 ]
  2. 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.[8905232 ]
  3. 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.[9278503 ]
  4. 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.[16738553 ]
  5. Darlison MG, Spencer ME, Guest JR: Nucleotide sequence of the sucA gene encoding the 2-oxoglutarate dehydrogenase of Escherichia coli K12. Eur J Biochem. 1984 Jun 1;141(2):351-9.[6376123 ]
  6. Link AJ, Robison K, Church GM: Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12. Electrophoresis. 1997 Aug;18(8):1259-313.[9298646 ]
  7. Stenberg F, Chovanec P, Maslen SL, Robinson CV, Ilag LL, von Heijne G, Daley DO: Protein complexes of the Escherichia coli cell envelope. J Biol Chem. 2005 Oct 14;280(41):34409-19. Epub 2005 Aug 3.[16079137 ]
  8. 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.[12560550 ]
  9. 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.[16407191 ]
  10. 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.[19710024 ]

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