Succinate dehydrogenase flavoprotein subunit

Details

Name
Succinate dehydrogenase flavoprotein subunit
Synonyms
  • 1.3.5.1
Gene Name
sdhA
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0012336|Succinate dehydrogenase flavoprotein subunit
MKLPVREFDAVVIGAGGAGMRAALQISQSGQTCALLSKVFPTRSHTVSAQGGITVALGNT
HEDNWEWHMYDTVKGSDYIGDQDAIEYMCKTGPEAILELEHMGLPFSRLDDGRIYQRPFG
GQSKNFGGEQAARTAAAADRTGHALLHTLYQQNLKNHTTIFSEWYALDLVKNQDGAVVGC
TALCIETGEVVYFKARATVLATGGAGRIYQSTTNAHINTGDGVGMAIRAGVPVQDMEMWQ
FHPTGIAGAGVLVTEGCRGEGGYLLNKHGERFMERYAPNAKDLAGRDVVARSIMIEIREG
RGCDGPWGPHAKLKLDHLGKEVLESRLPGILELSRTFAHVDPVKEPIPVIPTCHYMMGGI
PTKVTGQALTVNEKGEDVVVPGLFAVGEIACVSVHGANRLGGNSLLDLVVFGRAAGLHLQ
ESIAEQGALRDASESDVEASLDRLNRWNNNRNGEDPVAIRKALQECMQHNFSVFREGDAM
AKGLEQLKVIRERLKNARLDDTSSEFNTQRVECLELDNLMETAYATAVSANFRTESRGAH
SRFDFPDRDDENWLCHSLYLPESESMTRRSVNMEPKLRPAFPPKIRTY
Number of residues
588
Molecular Weight
64421.385
Theoretical pI
6.21
GO Classification
Functions
electron carrier activity / flavin adenine dinucleotide binding / succinate dehydrogenase (ubiquinone) activity / succinate dehydrogenase activity
Processes
aerobic respiration / electron transport chain / oxidation-reduction process / tricarboxylic acid cycle
Components
plasma membrane / plasma membrane succinate dehydrogenase complex
General Function
Succinate dehydrogenase 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.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cell inner membrane
Gene sequence
>lcl|BSEQ0012337|Succinate dehydrogenase flavoprotein subunit (sdhA)
ATGAAATTGCCAGTCAGAGAATTTGATGCAGTTGTGATTGGTGCCGGTGGCGCAGGTATG
CGCGCGGCGCTGCAAATTTCCCAGAGCGGCCAGACCTGTGCGCTGCTCTCTAAAGTCTTC
CCGACCCGTTCCCATACCGTTTCTGCGCAAGGCGGCATTACCGTTGCGCTGGGTAATACC
CATGAAGATAACTGGGAATGGCATATGTACGACACCGTGAAAGGGTCGGACTATATCGGT
GACCAGGACGCGATTGAATATATGTGTAAAACCGGGCCGGAAGCGATTCTGGAACTCGAA
CACATGGGCCTGCCGTTCTCGCGTCTCGATGATGGTCGTATCTATCAACGTCCGTTTGGC
GGTCAGTCGAAAAACTTCGGCGGCGAGCAGGCGGCACGCACTGCGGCAGCAGCTGACCGT
ACCGGTCACGCACTGTTGCACACGCTTTATCAGCAGAACCTGAAAAACCACACCACCATT
TTCTCCGAGTGGTATGCGCTGGATCTGGTGAAAAACCAGGATGGCGCGGTGGTGGGTTGT
ACCGCACTGTGCATCGAAACCGGTGAAGTGGTTTATTTCAAAGCCCGCGCTACCGTGCTG
GCGACTGGCGGAGCAGGGCGTATTTATCAGTCCACCACCAACGCCCACATTAACACCGGC
GACGGTGTCGGCATGGCTATCCGTGCCGGCGTACCGGTGCAGGATATGGAAATGTGGCAG
TTCCACCCGACCGGCATTGCCGGTGCGGGCGTACTGGTCACCGAAGGTTGCCGTGGTGAA
GGCGGTTATCTGCTGAACAAACATGGCGAACGTTTTATGGAGCGTTATGCGCCGAACGCC
AAAGACCTGGCGGGCCGTGACGTGGTTGCGCGTTCCATCATGATCGAAATCCGTGAAGGT
CGCGGCTGTGATGGTCCGTGGGGGCCACACGCGAAACTGAAACTCGATCACCTGGGTAAA
GAAGTTCTCGAATCCCGTCTGCCGGGTATCCTGGAGCTTTCCCGTACCTTCGCTCACGTC
GATCCGGTGAAAGAGCCGATTCCGGTTATCCCAACCTGTCACTACATGATGGGCGGTATT
CCGACCAAAGTTACCGGTCAGGCACTGACTGTGAATGAGAAAGGCGAAGATGTGGTTGTT
CCGGGACTGTTTGCCGTTGGTGAAATCGCTTGTGTATCGGTACACGGCGCTAACCGTCTG
GGCGGCAACTCGCTGCTGGACCTGGTGGTCTTTGGTCGCGCGGCAGGTCTGCATCTGCAA
GAGTCTATCGCCGAGCAGGGCGCACTGCGCGATGCCAGCGAGTCTGATGTTGAAGCGTCT
CTGGATCGCCTGAACCGCTGGAACAATAATCGTAACGGTGAAGATCCGGTGGCGATCCGT
AAAGCGCTGCAAGAATGTATGCAGCATAACTTCTCGGTCTTCCGTGAAGGTGATGCGATG
GCGAAAGGGCTTGAGCAGTTGAAAGTGATCCGCGAGCGTCTGAAAAATGCCCGTCTGGAT
GACACTTCCAGCGAGTTCAACACCCAGCGCGTTGAGTGCCTGGAACTGGATAACCTGATG
GAAACGGCGTATGCAACGGCTGTTTCTGCCAACTTCCGTACCGAAAGCCGTGGCGCGCAT
AGCCGCTTCGACTTCCCGGATCGTGATGATGAAAACTGGCTGTGCCACTCCCTGTATCTG
CCAGAGTCGGAATCCATGACGCGCCGAAGCGTCAACATGGAACCGAAACTGCGCCCGGCA
TTCCCGCCGAAGATTCGTACTTACTAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP0AC41
UniProtKB Entry NameSDHA_ECOLI
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. 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]
  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. [Article]
  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. [Article]
  5. 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. [Article]
  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. [Article]
  7. Wilkins MR, Gasteiger E, Tonella L, Ou K, Tyler M, Sanchez JC, Gooley AA, Walsh BJ, Bairoch A, Appel RD, Williams KL, Hochstrasser DF: Protein identification with N and C-terminal sequence tags in proteome projects. J Mol Biol. 1998 May 8;278(3):599-608. [Article]
  8. VanBogelen RA, Abshire KZ, Moldover B, Olson ER, Neidhardt FC: Escherichia coli proteome analysis using the gene-protein database. Electrophoresis. 1997 Aug;18(8):1243-51. [Article]
  9. 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. [Article]
  10. Zhang J, Sprung R, Pei J, Tan X, Kim S, Zhu H, Liu CF, Grishin NV, Zhao Y: Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli. Mol Cell Proteomics. 2009 Feb;8(2):215-25. doi: 10.1074/mcp.M800187-MCP200. Epub 2008 Aug 23. [Article]
  11. 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]
  12. 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]
  13. 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