Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial (P21801)

Identification
NameSuccinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial
Synonyms
  • Iron-sulfur subunit of complex II
  • Ip
Gene NameSDH2
Enzyme Class
Biological Properties
General FunctionInvolved in 2 iron, 2 sulfur cluster binding
Specific FunctionSubunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q). SDH1 and SDH2 form the catalytic dimer. Electrons flow from succinate to the FAD bound to SDH1, and sequentially through the iron-sulfur clusters bound to SDH2 and enter the membrane dimer formed by SDH3 and SDH4
Cellular LocationMitochondrion inner membrane; Peripheral membrane protein; Matrix side
SMPDB Pathways
Citric Acid Cycle 1434561204PW000970 ThumbThumb?image type=greyscaleThumb?image type=simple
Oxidative phosphorylationPW002461 ThumbThumb?image type=greyscaleThumb?image type=simple
TCA CyclePW002377 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG Pathways
Citrate cycle (TCA cycle)ec00020 Map00020
Oxidative phosphorylationec00190 Map00190
SMPDB Reactions
Succinic acid + Coenzyme Q10 + FAD ↔ Fumaric acid + QH2 + FADH2
KEGG ReactionsNot Available
Metabolites
YMDB IDNameView
YMDB00088Ubiquinone Q1Show
YMDB00101Fumaric acidShow
YMDB00296FADShow
YMDB00338Succinic acidShow
YMDB00597FADH2Show
YMDB00660Ubiquinone-6Show
YMDB00902ubiquinolShow
YMDB00915Ubiquinol-6Show
YMDB16129Coenzyme Q10Show
GO Classification
Component
Not Available
Function
binding
metal cluster binding
iron-sulfur cluster binding
oxidoreductase activity
electron carrier activity
catalytic activity
Process
cellular metabolic process
oxidation reduction
cofactor metabolic process
coenzyme metabolic process
acetyl-CoA metabolic process
acetyl-CoA catabolic process
tricarboxylic acid cycle
metabolic process
Gene Properties
Chromosome Locationchromosome 12
LocusYLL041C
Gene Sequence>801 bp ATGTTGAACGTGCTATTGAGAAGGAAGGCCTTTTGTTTGGTGACGAAGAAGGGTATGGCT ACTGCCACAACAGCTGCAGCTACGCATACCCCCAGATTGAAAACTTTTAAAGTTTACAGA TGGAATCCAGACGAGCCAAGTGCTAAACCTCATTTACAGTCATATCAAGTGGATCTGAAT GACTGTGGGCCCATGGTACTTGATGCGCTGTTAAAGATCAAAGACGAACAGGATTCTACC CTAACTTTTAGAAGATCATGTAGAGAAGGTATCTGCGGTTCATGTGCCATGAACATTGGC GGTAGAAACACGCTAGCTTGTATATGTAAGATCGACCAGAACGAATCCAAACAACTCAAG ATCTATCCATTACCCCACATGTTTATTGTCAAAGATTTGGTACCTGATTTAACTAACTTC TACCAACAATACAAATCTATCCAACCTTACTTACAGAGATCATCGTTTCCAAAGGATGGA ACGGAAGTGCTACAAAGTATTGAAGATCGTAAGAAACTGGATGGTCTTTACGAATGTATT CTGTGTGCATGCTGCTCTACTTCATGTCCATCGTACTGGTGGAACCAAGAACAGTATTTG GGCCCTGCCGTGCTAATGCAAGCCTACCGTTGGCTAATTGACTCTAGAGACCAAGCTACA AAGACAAGAAAGGCCATGCTAAACAACTCCATGTCATTGTACAGATGTCACACCATCATG AACTGTACTAGAACTTGTCCAAAGGGCTTGAATCCTGGTTTGGCTATTGCTGAAATTAAG AAATCTTTGGCATTTGCCTAG
Protein Properties
Pfam Domain Function
Protein Residues266
Protein Molecular Weight30230.90039
Protein Theoretical pI8.97
Signalling Regions
  • None
Transmembrane Regions
  • None
Protein Sequence>Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial MLNVLLRRKAFCLVTKKGMATATTAAATHTPRLKTFKVYRWNPDEPSAKPHLQSYQVDLN DCGPMVLDALLKIKDEQDSTLTFRRSCREGICGSCAMNIGGRNTLACICKIDQNESKQLK IYPLPHMFIVKDLVPDLTNFYQQYKSIQPYLQRSSFPKDGTEVLQSIEDRKKLDGLYECI LCACCSTSCPSYWWNQEQYLGPAVLMQAYRWLIDSRDQATKTRKAMLNNSMSLYRCHTIM NCTRTCPKGLNPGLAIAEIKKSLAFA
References
External Links
ResourceLink
Saccharomyces Genome Database SDH2
Uniprot IDP21801
Uniprot NameDHSB_YEAST
GenBank Gene IDAY558189
Genebank Protein ID45270268
General Reference
  • Lombardo, A., Carine, K., Scheffler, I. E. (1990). "Cloning and characterization of the iron-sulfur subunit gene of succinate dehydrogenase from Saccharomyces cerevisiae." J Biol Chem 265:10419-10423.2191948
  • Johnston, M., Hillier, L., Riles, L., Albermann, K., Andre, B., Ansorge, W., Benes, V., Bruckner, M., Delius, H., Dubois, E., Dusterhoft, A., Entian, K. D., Floeth, M., Goffeau, A., Hebling, U., Heumann, K., Heuss-Neitzel, D., Hilbert, H., Hilger, F., Kleine, K., Kotter, P., Louis, E. J., Messenguy, F., Mewes, H. W., Hoheisel, J. D., et, a. l. .. (1997). "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII." Nature 387:87-90.9169871
  • 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
  • Gould, S. J., Subramani, S., Scheffler, I. E. (1989). "Use of the DNA polymerase chain reaction for homology probing: isolation of partial cDNA or genomic clones encoding the iron-sulfur protein of succinate dehydrogenase from several species." Proc Natl Acad Sci U S A 86:1934-1938.2494655
  • Schmidt, D. M., Saghbini, M., Scheffler, I. E. (1992). "The C-terminus of the succinate dehydrogenase IP peptide of Saccharomyces cerevisiae is significant for assembly of complex II." Biochemistry 31:8442-8448.1390628
  • 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., 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