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
- Functionselectron carrier activity / heme binding / metal ion binding / succinate dehydrogenase (ubiquinone) activity / ubiquinone bindingProcessesaerobic respiration / cytochrome complex assembly / tricarboxylic acid cycleComponentsintegral component of membrane / plasma membrane / succinate dehydrogenase complex
- General Function
- Ubiquinone binding
- Specific Function
- Membrane-anchoring subunit of succinate dehydrogenase (SDH).
- Pfam Domain Function
- Sdh_cyt (PF01127)
- 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
Resource Link UniProtKB ID P69054 UniProtKB Entry Name DHSC_ECOLI GenBank Protein ID 146196 GenBank Gene ID J01619 - General References
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- 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]
- 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]
- 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]
- 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]
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- 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]