Succinate dehydrogenase [ubiquinone] cytochrome b small subunit, mitochondrial (P37298)

Identification
NameSuccinate dehydrogenase [ubiquinone] cytochrome b small subunit, mitochondrial
Synonyms
  • CybS
  • Succinate-ubiquinone reductase membrane anchor subunit
Gene NameSDH4
Enzyme ClassNot Available
Biological Properties
General FunctionInvolved in heme binding
Specific FunctionMembrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in system II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q). SDH3 and SDH4 form the membrane dimer that anchors the catalytic dimer formed by SDH1 and SDH2 to the matrix surface of the mitochondrial inner membrane. Electrons originating from the catalytic dimer enter the membrane dimer for ubiquinone reduction
Cellular LocationMitochondrion inner membrane; Multi-pass membrane protein
SMPDB PathwaysNot Available
KEGG PathwaysNot Available
SMPDB ReactionsNot Available
KEGG ReactionsNot Available
Metabolites
YMDB IDNameView
GO Classification
Component
mitochondrial envelope
cell part
membrane part
intrinsic to membrane
integral to membrane
envelope
organelle envelope
Function
binding
ion binding
cation binding
metal ion binding
transition metal ion binding
heme binding
iron ion binding
Process
acetyl-CoA metabolic process
acetyl-CoA catabolic process
tricarboxylic acid cycle
cellular metabolic process
cofactor metabolic process
coenzyme metabolic process
metabolic process
Gene Properties
Chromosome LocationNot Available
Locus
Gene Sequence>546 bp ATGATGTTGCCAAGATCCATGAAATTTATGACTGGAAGGAGAATTTTCCATACTGCCACA GTAAGGGCCTTCCAGTCTACCGCTAAGAAGAGCTTAACTATCCCATTTTTGCCCGTATTA CCCCAGAAACCAGGTGGTGTTAGGGGCACTCCCAATGATGCCTACGTCCCCCCCCCTGAG AATAAATTAGAGGGCTCATACCACTGGTATATGGAAAAAATCTTTGCCTTGTCCGTCGTT CCATTGGCTACGACGGCTATGCTGACAACCGGTCCGTTATCCACTGCAGCTGATTCTTTC TTTTCTGTCATGCTTTTGGGATATTGTTACATGGAATTTAACTCTTGTATCACCGATTAT ATTTCTGAAAGAGTTTATGGTGTTTGGCACAAGTACGCCATGTATATGTTGGGCCTTGGT TCTGCGGTCTCCCTTTTTGGAATCTATAAACTAGAAACCGAGAATGATGGTGTTGTTGGT TTAGTAAAAAGTCTATGGGATTCTTCCGAGAAAGACAACAGTCAAAAGATTGAAGCCAAG AAGTAG
Protein Properties
Pfam Domain Function
Protein Residues181
Protein Molecular Weight20248.40039
Protein Theoretical pI9.22
Signalling Regions
  • None
Transmembrane Regions
  • 67-88
  • 99-118
  • 128-148
Protein Sequence>Succinate dehydrogenase [ubiquinone] cytochrome b small subunit, mitochondrial MMLPRSMKFMTGRRIFHTATVRAFQSTAKKSLTIPFLPVLPQKPGGVRGTPNDAYVPPPE NKLEGSYHWYMEKIFALSVVPLATTAMLTTGPLSTAADSFFSVMLLGYCYMEFNSCITDY ISERVYGVWHKYAMYMLGLGSAVSLFGIYKLETENDGVVGLVKSLWDSSEKDNSQKIEAK K
References
External Links
ResourceLink
Saccharomyces Genome Database SDH4
Uniprot IDP37298
Uniprot NameDHSD_YEAST
GenBank Gene IDAY557671
Genebank Protein ID45269235
General Reference
  • Bullis, B. L., Lemire, B. D. (1994). "Isolation and characterization of the Saccharomyces cerevisiae SDH4 gene encoding a membrane anchor subunit of succinate dehydrogenase." J Biol Chem 269:6543-6549.8120006
  • Jacq, C., Alt-Morbe, J., Andre, B., Arnold, W., Bahr, A., Ballesta, J. P., Bargues, M., Baron, L., Becker, A., Biteau, N., Blocker, H., Blugeon, C., Boskovic, J., Brandt, P., Bruckner, M., Buitrago, M. J., Coster, F., Delaveau, T., del Rey, F., Dujon, B., Eide, L. G., Garcia-Cantalejo, J. M., Goffeau, A., Gomez-Peris, A., Zaccaria, P., et, a. l. .. (1997). "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV." Nature 387:75-78.9169867
  • Hu, Y., Rolfs, A., Bhullar, B., Murthy, T. V., Zhu, C., Berger, M. F., Camargo, A. A., Kelley, F., McCarron, S., Jepson, D., Richardson, A., Raphael, J., Moreira, D., Taycher, E., Zuo, D., Mohr, S., Kane, M. F., Williamson, J., Simpson, A., Bulyk, M. L., Harlow, E., Marsischky, G., Kolodner, R. D., LaBaer, J. (2007). "Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Genome Res 17:536-543.17322287
  • Oyedotun, K. S., Lemire, B. D. (2001). "The Quinone-binding sites of the Saccharomyces cerevisiae succinate-ubiquinone oxidoreductase." J Biol Chem 276:16936-16943.11279023
  • Lemire, B. D., Oyedotun, K. S. (2002). "The Saccharomyces cerevisiae mitochondrial succinate:ubiquinone oxidoreductase." Biochim Biophys Acta 1553:102-116.11803020
  • Ghaemmaghami, S., Huh, W. K., Bower, K., Howson, R. W., Belle, A., Dephoure, N., O'Shea, E. K., Weissman, J. S. (2003). "Global analysis of protein expression in yeast." Nature 425:737-741.14562106
  • Oyedotun, K. S., Yau, P. F., Lemire, B. D. (2004). "Identification of the heme axial ligands in the cytochrome b562 of the Saccharomyces cerevisiae succinate dehydrogenase." J Biol Chem 279:9432-9439.14672930
  • Silkin, Y., Oyedotun, K. S., Lemire, B. D. (2007). "The role of Sdh4p Tyr-89 in ubiquinone reduction by the Saccharomyces cerevisiae succinate dehydrogenase." Biochim Biophys Acta 1767:143-150.17208193
  • Oyedotun, K. S., Lemire, B. D. (2004). "The quaternary structure of the Saccharomyces cerevisiae succinate dehydrogenase. Homology modeling, cofactor docking, and molecular dynamics simulation studies." J Biol Chem 279:9424-9431.14672929