Succinate dehydrogenase hydrophobic membrane anchor subunit
Details
- Name
- Succinate dehydrogenase hydrophobic membrane anchor subunit
- Synonyms
- Not Available
- Gene Name
- sdhD
- Organism
- Escherichia coli (strain K12)
- Amino acid sequence
>lcl|BSEQ0012685|Succinate dehydrogenase hydrophobic membrane anchor subunit MVSNASALGRNGVHDFILVRATAIVLTLYIIYMVGFFATSGELTYEVWIGFFASAFTKVF TLLALFSILIHAWIGMWQVLTDYVKPLALRLMLQLVIVVALVVYVIYGFVVVWGV
- Number of residues
- 115
- Molecular Weight
- 12867.44
- Theoretical pI
- 8.87
- GO Classification
- Functionselectron carrier activity / heme binding / metal ion binding / succinate dehydrogenase activityProcessesaerobic respiration / cytochrome complex assembly / tricarboxylic acid cycleComponentsintegral component of membrane / plasma membrane
- General Function
- Succinate dehydrogenase activity
- Specific Function
- Membrane-anchoring subunit of succinate dehydrogenase (SDH).
- Pfam Domain Function
- Sdh_cyt (PF01127)
- Transmembrane Regions
- 16-36 59-80 91-115
- Cellular Location
- Cell inner membrane
- Gene sequence
>lcl|BSEQ0012686|Succinate dehydrogenase hydrophobic membrane anchor subunit (sdhD) ATGGTAAGCAACGCCTCCGCATTAGGACGCAATGGCGTACATGATTTCATCCTCGTTCGC GCTACCGCTATCGTCCTGACGCTCTACATCATTTATATGGTCGGTTTTTTCGCTACCAGT GGCGAGCTGACATATGAAGTCTGGATCGGTTTCTTCGCCTCTGCGTTCACCAAAGTGTTC ACCCTGCTGGCGCTGTTTTCTATCTTGATCCATGCCTGGATCGGCATGTGGCAGGTGTTG ACCGACTACGTTAAACCGCTGGCTTTGCGCCTGATGCTGCAACTGGTGATTGTCGTTGCA CTGGTGGTTTACGTGATTTATGGATTCGTTGTGGTGTGGGGTGTGTGA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P0AC44 UniProtKB Entry Name DHSD_ECOLI GenBank Protein ID 146196 GenBank Gene ID J01619 - General References
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]