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Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial (Q00711)

Identification
NameSuccinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial
Synonyms
  • Flavoprotein subunit of complex II
  • FP
Gene NameSDH1
Enzyme Class
Biological Properties
General FunctionInvolved in electron carrier activity
Specific FunctionCatalytic subunit 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
Oxidative phosphorylationPW002461 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG Pathways
Citrate cycle (TCA cycle)ec00020 Map00020
Oxidative phosphorylationec00190 Map00190
SMPDB ReactionsNot Available
KEGG ReactionsNot Available
Metabolites
YMDB IDNameView
YMDB00088Ubiquinone Q1Show
YMDB00101Fumaric acidShow
YMDB00338Succinic acidShow
YMDB00902ubiquinolShow
GO Classification
Component
Not Available
Function
catalytic activity
oxidoreductase activity, acting on the CH-CH group of donors
binding
nucleoside binding
purine nucleoside binding
adenyl nucleotide binding
FAD or FADH2 binding
oxidoreductase activity
electron carrier activity
Process
tricarboxylic acid cycle
metabolic process
generation of precursor metabolites and energy
electron transport chain
cellular metabolic process
oxidation reduction
cofactor metabolic process
coenzyme metabolic process
acetyl-CoA metabolic process
acetyl-CoA catabolic process
Gene Properties
Chromosome Locationchromosome 11
LocusYKL148C
Gene Sequence>1923 bp ATGCTATCGCTAAAAAAATCAGCGCTCTCCAAGTTGACTTTGCTCAGAAACACAAGAACA TTTACATCGTCAGCTTTGGTGCGCCAAACGCAGGGCTCTGTAAACGGTTCCGCGTCCAGA TCTGCAGACGGGAAGTACCACATAATAGATCACGAGTATGACTGTGTGGTAATCGGTGCC GGTGGTGCCGGCCTTAGAGCGGCCTTTGGTCTTGCCGAGGCGGGCTACAAGACTGCTTGT ATATCCAAGCTTTTCCCCACCAGATCCCACACTGTTGCTGCTCAGGGTGGTATCAATGCC GCTCTGGGAAATATGCACAAGGATAACTGGAAATGGCATATGTACGATACTGTGAAAGGA TCTGATTGGCTAGGTGACCAGGACTCCATCCATTACATGACCAGGGAAGCGCCCAAATCG ATCATTGAACTGGAACACTATGGTGTTCCTTTTTCAAGAACTGAAAACGGTAAGATCTAC CAAAGAGCCTTTGGTGGTCAGACCAAGGAGTACGGTAAGGGTGCTCAGGCCTATAGAACA TGCGCTGTCGCAGACAGGACAGGACATGCTCTTTTACACACGCTTTATGGCCAAGCTTTA AGACATGACACACATTTCTTTATTGAGTACTTTGCCCTCGATCTGTTGACCCATAATGGC GAGGTCGTTGGTGTCATCGCTTATAATCAGGAAGACGGTACCATCCACAGATTCAGAGCA CACAAGACCATTATTGCCACTGGTGGCTATGGTAGAGCATACTTCTCTTGTACCTCTGCT CACACATGTACGGGTGACGGTAATGCCATGGTTTCGCGTGCTGGTTTCCCCTTGCAAGAT TTAGAGTTTGTTCAATTCCATCCTTCAGGTATATATGGGTCTGGTTGCTTAATCACTGAA GGTGCTCGTGGTGAAGGTGGTTTTTTGGTTAATTCTGAAGGTGAAAGATTCATGGAACGT TACGCTCCTACGGCCAAGGATCTAGCTTGTAGAGATGTCGTTTCCAGAGCAATCACCATG GAGATCAGAGAAGGCAGAGGTGTTGGTAAGAAAAAGGACCACATGTACTTACAATTGAGC CATCTACCTCCGGAAGTTCTAAAGGAAAGATTGCCAGGTATCTCTGAAACAGCAGCCATT TTTGCTGGTGTAGACGTCACTAAGGAACCTATTCCCATTATTCCTACCGTCCACTATAAC ATGGGTGGTATTCCCACGAAGTGGAATGGTGAGGCATTAACCATTGATGAAGAAACTGGC GAAGACAAGGTTATTCCCGGTTTAATGGCTTGTGGTGAAGCCGCTTGTGTTTCTGTCCAT GGTGCCAATAGATTAGGTGCCAATTCCTTGTTGGATCTTGTTGTCTTTGGTCGTGCTGTT GCCCATACGGTTGCTGACACTTTACAGCCTGGGTTGCCACACAAACCACTACCTTCTGAT TTGGGTAAAGAATCCATCGCAAACTTGGATAAACTAAGAAATGCTAATGGTTCAAGATCT ACGGCAGAAATTAGAATGAATATGAAACAAACTATGCAAAAGGATGTTTCCGTCTTTAGA ACACAATCATCTTTAGATGAAGGTGTTCGGAACATTACTGCAGTAGAGAAGACCTTTGAT GATGTGAAGACGACCGATAGATCAATGATCTGGAATTCTGACTTGGTTGAAACTCTGGAG CTACAGAACTTATTAACCTGTGCCTCCCAAACAGCTGTTTCCGCTGCTAATAGAAAGGAA TCCCGTGGTGCTCATGCAAGAGAGGATTATCCAAATAGAGATGACGAACATTGGATGAAG CATACATTATCCTGGCAAAAGGACGTCGCTGCCCCAGTGACTTTGAAATACAGAAGGGTT ATCGATCACACTTTGGACGAAAAGGAATGTCCTTCCGTACCTCCAACTGTAAGAGCCTAC TAA
Protein Properties
Pfam Domain Function
Protein Residues640
Protein Molecular Weight70228.79688
Protein Theoretical pI7.53
Signalling Regions
  • None
Transmembrane Regions
  • None
Protein Sequence>Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial MLSLKKSALSKLTLLRNTRTFTSSALVRQTQGSVNGSASRSADGKYHIIDHEYDCVVIGA GGAGLRAAFGLAEAGYKTACISKLFPTRSHTVAAQGGINAALGNMHKDNWKWHMYDTVKG SDWLGDQDSIHYMTREAPKSIIELEHYGVPFSRTENGKIYQRAFGGQTKEYGKGAQAYRT CAVADRTGHALLHTLYGQALRHDTHFFIEYFALDLLTHNGEVVGVIAYNQEDGTIHRFRA HKTIIATGGYGRAYFSCTSAHTCTGDGNAMVSRAGFPLQDLEFVQFHPSGIYGSGCLITE GARGEGGFLVNSEGERFMERYAPTAKDLACRDVVSRAITMEIREGRGVGKKKDHMYLQLS HLPPEVLKERLPGISETAAIFAGVDVTKEPIPIIPTVHYNMGGIPTKWNGEALTIDEETG EDKVIPGLMACGEAACVSVHGANRLGANSLLDLVVFGRAVAHTVADTLQPGLPHKPLPSD LGKESIANLDKLRNANGSRSTAEIRMNMKQTMQKDVSVFRTQSSLDEGVRNITAVEKTFD DVKTTDRSMIWNSDLVETLELQNLLTCASQTAVSAANRKESRGAHAREDYPNRDDEHWMK HTLSWQKDVAAPVTLKYRRVIDHTLDEKECPSVPPTVRAY
References
External Links
ResourceLink
Saccharomyces Genome Database SDH1
Uniprot IDQ00711
Uniprot NameDHSA_YEAST
GenBank Gene IDM86746
Genebank Protein ID172557
General Reference
  • Schulke, N., Blobel, G., Pain, D. (1992). "Primary structure, import, and assembly of the yeast homolog of succinate dehydrogenase flavoprotein." Proc Natl Acad Sci U S A 89:8011-8015.1518827
  • Chapman, K. B., Solomon, S. D., Boeke, J. D. (1992). "SDH1, the gene encoding the succinate dehydrogenase flavoprotein subunit from Saccharomyces cerevisiae." Gene 118:131-136.1511876
  • Robinson, K. M., Lemire, B. D. (1992). "Isolation and nucleotide sequence of the Saccharomyces cerevisiae gene for the succinate dehydrogenase flavoprotein subunit." J Biol Chem 267:10101-10107.1577780
  • Vandenbol, M., Bolle, P. A., Dion, C., Portetelle, D., Hilger, F. (1994). "DNA sequencing of a 36.2 kb fragment located between the FAS1 and LAP loci of chromosome XI of Saccharomyces cerevisiae." Yeast 10 Suppl A:S35-S40.8091859
  • Dujon, B., Alexandraki, D., Andre, B., Ansorge, W., Baladron, V., Ballesta, J. P., Banrevi, A., Bolle, P. A., Bolotin-Fukuhara, M., Bossier, P., et, a. l. .. (1994). "Complete DNA sequence of yeast chromosome XI." Nature 369:371-378.8196765
  • 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
  • Grandier-Vazeille, X., Bathany, K., Chaignepain, S., Camougrand, N., Manon, S., Schmitter, J. M. (2001). "Yeast mitochondrial dehydrogenases are associated in a supramolecular complex." Biochemistry 40:9758-9769.11502169
  • Robinson, K. M., Rothery, R. A., Weiner, J. H., Lemire, B. D. (1994). "The covalent attachment of FAD to the flavoprotein of Saccharomyces cerevisiae succinate dehydrogenase is not necessary for import and assembly into mitochondria." Eur J Biochem 222:983-990.8026509
  • 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
  • Hao, H. X., Khalimonchuk, O., Schraders, M., Dephoure, N., Bayley, J. P., Kunst, H., Devilee, P., Cremers, C. W., Schiffman, J. D., Bentz, B. G., Gygi, S. P., Winge, D. R., Kremer, H., Rutter, J. (2009). "SDH5, a gene required for flavination of succinate dehydrogenase, is mutated in paraganglioma." Science 325:1139-1142.19628817
  • 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