SDH2 (YLL041C) encodes the iron-sulfur protein (Ip) subunit of mitochondrial succinate dehydrogenase (SDH; respiratory complex II; succinate:quinone oxidoreductase, EC 1.3.5.1). Sdh2p and the covalent-FAD flavoprotein Sdh1p form the matrix-facing catalytic dimer, which the integral membrane subunits Sdh3p and Sdh4p anchor to the inner mitochondrial membrane. Electrons from succinate oxidation at the Sdh1p FAD pass through the three Sdh2p iron-sulfur clusters ([2Fe-2S], [4Fe-4S], [3Fe-4S]) to the ubiquinone site formed with Sdh3p/Sdh4p. Complex II thus couples the TCA-cycle oxidation of succinate to fumarate with reduction of ubiquinone in the respiratory chain. Sdh2p is required for holocomplex assembly and for growth on non-fermentable carbon sources; assembly depends on factors including Sdh8 (for the Sdh1-Sdh2 dimer) and Tcm62.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0005515 protein binding | IPI PMID:16429126 Proteome survey reveals modularity of the yeast cell machine... | REMOVE | Summary: Sdh2p co-purified with Sdh1p (Q00711) in the Gavin et al. genome-wide TAP-MS complex survey. This is the expected Sdh1-Sdh2 catalytic dimer of complex II. Reason: 'protein binding' is uninformative. The Sdh2-Sdh1 contact is the catalytic dimer of complex II, which is already captured by part_of GO:0045273; removing the term does not dispute the interaction. Supporting Evidence: PMID:24954416 The Sdh3/Sdh4 dimer binds the peripheral membrane protein Sdh2 (SDHB), which tethers the catalytic Sdh1 (SDHA) subunit to the complex. |
| GO:0005515 protein binding | IPI PMID:24954416 SDHAF4 promotes mitochondrial succinate dehydrogenase activi... | REMOVE | Summary: Sdh2p-Sdh1p interaction reported in the Sdh8/SDHAF4 study (Van Vranken et al. 2014), where Sdh8 is shown to promote association of Sdh1 with Sdh2. The interaction is real and well characterised (soluble Sdh1-Sdh2 dimer accumulates without the Sdh4 anchor), but the GO term adds nothing beyond complex membership. Reason: 'protein binding' is uninformative. The Sdh2-Sdh1 contact is the catalytic dimer of complex II, which is already captured by part_of GO:0045273; removing the term does not dispute the interaction. Supporting Evidence: PMID:24954416 The Sdh3/Sdh4 dimer binds the peripheral membrane protein Sdh2 (SDHB), which tethers the catalytic Sdh1 (SDHA) subunit to the complex. |
| GO:0005515 protein binding | IPI PMID:37968396 The social and structural architecture of the yeast protein ... | REMOVE | Summary: Sdh2p-Sdh1p co-enrichment in the Michaelis et al. 2023 proteome-wide affinity-enrichment MS interactome; reflects the complex II catalytic dimer. Reason: 'protein binding' is uninformative. The Sdh2-Sdh1 contact is the catalytic dimer of complex II, which is already captured by part_of GO:0045273; removing the term does not dispute the interaction. Supporting Evidence: PMID:24954416 The Sdh3/Sdh4 dimer binds the peripheral membrane protein Sdh2 (SDHB), which tethers the catalytic Sdh1 (SDHA) subunit to the complex. |
| GO:0005739 mitochondrion | HDA PMID:16823961 Toward the complete yeast mitochondrial proteome: multidimen... | ACCEPT | Summary: High-throughput localization of SDH2p to mitochondria in the PROMITO multidimensional MS survey of purified yeast mitochondria (Reinders et al. 2006). Correct but less specific than the experimentally supported sub-mitochondrial location. Sdh2p is a matrix-facing peripheral subunit of the inner-membrane complex II. Supporting Evidence: PMID:16823961 A total of 851 different proteins (PROMITO dataset) were identified by use of multidimensional LC-MS/MS |
| GO:0005739 mitochondrion | HDA PMID:24769239 Quantitative variations of the mitochondrial proteome and ph... | ACCEPT | Summary: High-throughput localization of SDH2p to mitochondria in the carbon-source quantitative mitochondrial proteome/phosphoproteome study (Renvoise et al. 2014). Correct but less specific than the experimentally supported sub-mitochondrial location. Supporting Evidence: PMID:24769239 we performed an overall quantitative proteomic and phosphoproteomic study of isolated mitochondria extracted from yeast grown on fermentative (glucose or galactose) and respiratory (lactate) media |
| GO:0005743 mitochondrial inner membrane | IDA PMID:9929002 The Saccharomyces cerevisiae succinate-ubiquinone reductase ... | ACCEPT | Summary: Oyedotun & Lemire 1999 characterised the yeast succinate-ubiquinone reductase in mitochondrial membranes; Sdh2p is the iron-sulfur subunit of this inner-membrane tetramer. Correct location, consistent with UniProt (peripheral, matrix side). Supporting Evidence: PMID:9929002 The Saccharomyces cerevisiae succinate-ubiquinone reductase or succinate dehydrogenase (SDH) is a tetramer of non-equivalent subunits encoded by the SDH1, SDH2, SDH3, and SDH4 genes. file:yeast/SDH2/SDH2-uniprot.txt SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane |
| GO:0005743 mitochondrial inner membrane | IEA GO_REF:0000044 | ACCEPT | Summary: UniProt subcellular-location mapping (SL-0168) to mitochondrial inner membrane; matches the experimental location of Sdh2p as a matrix-side peripheral subunit of complex II. Supporting Evidence: file:yeast/SDH2/SDH2-uniprot.txt SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane |
| GO:0005743 mitochondrial inner membrane | RCA GO_REF:0000123 | ACCEPT | Summary: YeastPathways TCA-EUK-PWY conversion places the SQR reaction in the inner membrane. Correct for Sdh2p, which acts as part of membrane-bound complex II. Supporting Evidence: file:yeast/SDH2/SDH2-uniprot.txt SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane PMID:24954416 The Sdh3/Sdh4 dimer binds the peripheral membrane protein Sdh2 (SDHB), which tethers the catalytic Sdh1 (SDHA) subunit to the complex. |
| GO:0006099 tricarboxylic acid cycle | IDA PMID:9929002 The Saccharomyces cerevisiae succinate-ubiquinone reductase ... | ACCEPT | Summary: IDA from the Oyedotun & Lemire 1999 characterisation of yeast SDH (succinate-ubiquinone reductase), the TCA-cycle succinate-to-fumarate step. Sdh2p is an obligate subunit of this enzyme, so TCA cycle is a correct core process. Supporting Evidence: PMID:9929002 The Saccharomyces cerevisiae succinate-ubiquinone reductase or succinate dehydrogenase (SDH) is a tetramer of non-equivalent subunits encoded by the SDH1, SDH2, SDH3, and SDH4 genes. |
| GO:0006099 tricarboxylic acid cycle | IEA GO_REF:0000120 | ACCEPT | Summary: Combined IEA (InterPro IPR004489 SDH iron-sulfur subunit; UniPathway UPA00223) to TCA cycle. Correct for Sdh2p, the iron-sulfur subunit of the TCA-cycle succinate dehydrogenase. Supporting Evidence: file:yeast/SDH2/SDH2-uniprot.txt PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; fumarate |
| GO:0006099 tricarboxylic acid cycle | IMP PMID:10224250 Genetic and biochemical interactions involving tricarboxylic... | ACCEPT | Summary: IMP from the McCammon lab collection of mutants in all 15 TCA cycle genes, which included sdh2; the sdh2 null is defective for growth on non-fermentable carbon. Supports TCA-cycle involvement. Supporting Evidence: PMID:10224250 The 15 major TCA cycle genes can be sorted into five phenotypic categories on the basis of their growth on nonfermentable carbon sources. |
| GO:0006121 mitochondrial electron transport, succinate to ubiquinone | IDA PMID:9929002 The Saccharomyces cerevisiae succinate-ubiquinone reductase ... | ACCEPT | Summary: IDA (Oyedotun & Lemire 1999) for succinate-to-ubiquinone electron transport. Sdh2p carries the three Fe-S clusters that relay electrons from Sdh1 FAD to the quinone site in Sdh3/Sdh4; this is a core process. Supporting Evidence: PMID:9929002 The Saccharomyces cerevisiae succinate-ubiquinone reductase or succinate dehydrogenase (SDH) is a tetramer of non-equivalent subunits encoded by the SDH1, SDH2, SDH3, and SDH4 genes. PMID:24954416 The two electrons that result from succinate oxidation are channeled through the three iron-sulfur clusters in Sdh2 to ubiquinone |
| GO:0008177 succinate dehydrogenase (quinone) activity | IDA PMID:13445213 Studies on succinic dehydrogenase. V. Isolation and properti... | ACCEPT | Summary: IDA from the Singer, Massey & Kearney 1957 purification of succinate dehydrogenase from baker's yeast. The purified enzyme contains Sdh2p. Strictly the activity belongs to the Sdh1-Sdh2 catalytic dimer and the quinone site needs Sdh3/Sdh4, so 'contributes_to' would be more exact, but the curator's assertion of SQR activity for the iron-sulfur subunit of the catalytic dimer is sound. Supporting Evidence: PMID:13445213 Isolation and properties of the dehydrogenase from baker's yeast file:yeast/SDH2/SDH2-uniprot.txt Reaction=a quinone + succinate = fumarate + a quinol; file:yeast/SDH2/SDH2-uniprot.txt SDH1 and SDH2 form the catalytic dimer. |
| GO:0008177 succinate dehydrogenase (quinone) activity | IEA GO_REF:0000120 | ACCEPT | Summary: Combined IEA from RHEA:40523 / EC 1.3.5.1 attached to the UniProt entry. Correct reaction for complex II, of which Sdh2p is part of the catalytic dimer. Supporting Evidence: file:yeast/SDH2/SDH2-uniprot.txt Reaction=a quinone + succinate = fumarate + a quinol; |
| GO:0008177 succinate dehydrogenase (quinone) activity | IGI PMID:16232921 Effect of gene disruption of succinate dehydrogenase on succ... | ACCEPT | Summary: IGI with SDH1 (S000001631) from Kubo et al. 2000: SDH activity was abolished only in sdh1 sdh2 double disruptants of a sake strain. Supports Sdh2p's requirement for SQR activity. Supporting Evidence: PMID:16232921 the activity disappeared in double disruptants of the SDH1 and SDH2 or SDH1b (the SDH1 homologue) genes PMID:16232921 Succinate dehydrogenase (SDH) of Saccharomyces cerevisiae consists of four subunits encoded by the SDH1, SDH2, SDH3, and SDH4 genes. |
| GO:0008177 succinate dehydrogenase (quinone) activity | IMP PMID:16232921 Effect of gene disruption of succinate dehydrogenase on succ... | ACCEPT | Summary: IMP from Kubo et al. 2000 (sdh2 disruption reduced SDH activity in a sake strain). Consistent with Sdh2p being a catalytic-dimer subunit of SQR. Supporting Evidence: PMID:16232921 The SDH activity of single disruptants was retained at 30-90% of that of the wild-type strain PMID:16232921 Succinate dehydrogenase (SDH) of Saccharomyces cerevisiae consists of four subunits encoded by the SDH1, SDH2, SDH3, and SDH4 genes. |
| GO:0008177 succinate dehydrogenase (quinone) activity | RCA GO_REF:0000123 | ACCEPT | Summary: YeastPathways RCA, contributes_to SQR activity (EC 1.3.5.1) from TCA-EUK-PWY. This qualifier describes Sdh2p's role in the heterotetramer best. Supporting Evidence: file:yeast/SDH2/SDH2-uniprot.txt Reaction=a quinone + succinate = fumarate + a quinol; file:yeast/SDH2/SDH2-uniprot.txt SDH1 and SDH2 form the catalytic dimer. |
| GO:0009055 electron transfer activity | IEA GO_REF:0000002 | ACCEPT | Summary: InterPro2GO (IPR025192, succinate dehydrogenase/fumarate reductase N-terminal ferredoxin domain) to electron transfer activity. Correct and specific to Sdh2p: its [2Fe-2S], [4Fe-4S] and [3Fe-4S] clusters relay electrons from FAD to ubiquinone. This is the subunit-specific MF. Supporting Evidence: PMID:24954416 The two electrons that result from succinate oxidation are channeled through the three iron-sulfur clusters in Sdh2 to ubiquinone file:yeast/SDH2/SDH2-uniprot.txt iron-sulfur clusters bound to SDH2 and enter the membrane dimer formed |
| GO:0009060 aerobic respiration | IBA GO_REF:0000033 | ACCEPT | Summary: IBA (PTN000229864) to aerobic respiration. Complex II feeds succinate-derived electrons into the respiratory chain; Sdh2p lies in the clade inheriting this. Correct, broader than the core process. Supporting Evidence: PMID:16232921 Two double disruptants showed no growth on a medium containing glycerol as the sole carbon source, while the single disruptants could utilize glycerol. |
| GO:0009060 aerobic respiration | RCA GO_REF:0000123 | ACCEPT | Summary: YeastPathways RCA from TCA-EUK-PWY to aerobic respiration. Correct parent-level process for complex II. Supporting Evidence: PMID:9929002 The Saccharomyces cerevisiae succinate-ubiquinone reductase or succinate dehydrogenase (SDH) is a tetramer of non-equivalent subunits encoded by the SDH1, SDH2, SDH3, and SDH4 genes. |
| GO:0016491 oxidoreductase activity | IEA GO_REF:0000002 | MODIFY | Summary: InterPro2GO (IPR004489) to generic oxidoreductase activity. Correct but uninformative given the specific SQR activity of the complex. Reason: Replace the root-level oxidoreductase term by the specific complex activity. Proposed replacements: succinate dehydrogenase (quinone) activity Supporting Evidence: file:yeast/SDH2/SDH2-uniprot.txt Reaction=a quinone + succinate = fumarate + a quinol; |
| GO:0022904 respiratory electron transport chain | IBA GO_REF:0000033 | ACCEPT | Summary: IBA (PTN000229864) to respiratory electron transport chain. Sdh2p transfers electrons from succinate to ubiquinone within complex II; correct, more general than GO:0006121. Supporting Evidence: PMID:24954416 The two electrons that result from succinate oxidation are channeled through the three iron-sulfur clusters in Sdh2 to ubiquinone |
| GO:0031966 mitochondrial membrane | IBA GO_REF:0000033 | ACCEPT | Summary: IBA (PTN000229867) is_active_in mitochondrial membrane. Correct parent of the inner-membrane location. Supporting Evidence: file:yeast/SDH2/SDH2-uniprot.txt SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane |
| GO:0031966 mitochondrial membrane | IDA PMID:1939170 Isolation and characterization of a Saccharomyces cerevisiae... | ACCEPT | Summary: IDA from Robinson et al. 1991: disruption of SDH1 caused loss of both the flavoprotein and the iron-sulfur (Sdh2p) subunits from mitochondrial membranes, showing Sdh2p is normally membrane-associated. Supporting Evidence: PMID:1939170 Disruption of the flavoprotein subunit gene results in the simultaneous loss of both the iron-sulfur and the flavoprotein subunits from mitochondrial membranes. |
| GO:0032991 protein-containing complex | RCA GO_REF:0000123 | MODIFY | Summary: YeastPathways RCA part_of generic 'protein-containing complex'. True but uninformative; the complex is complex II. Reason: Use the specific complex term. Proposed replacements: respiratory chain complex II (succinate dehydrogenase) Supporting Evidence: PMID:9929002 The Saccharomyces cerevisiae succinate-ubiquinone reductase or succinate dehydrogenase (SDH) is a tetramer of non-equivalent subunits encoded by the SDH1, SDH2, SDH3, and SDH4 genes. |
| GO:0045273 respiratory chain complex II (succinate dehydrogenase) | IDA PMID:9822678 The Saccharomyces cerevisiae TCM62 gene encodes a chaperone ... | ACCEPT | Summary: IDA from Dibrov et al. 1998: Tcm62p (an SDH assembly chaperone) forms a complex with at least three SDH subunits, and SDH subunit composition is described. Supports Sdh2p as a complex II subunit. Supporting Evidence: PMID:9822678 The membrane extrinsic domain, consisting of Sdh1p and Sdh2p, contains a covalent FAD cofactor and three iron-sulfur clusters. PMID:9822678 Tcm62p forms a complex containing at least three SDH subunits. |
| GO:0045273 respiratory chain complex II (succinate dehydrogenase) | IMP PMID:24954416 SDHAF4 promotes mitochondrial succinate dehydrogenase activi... | ACCEPT | Summary: IMP from Van Vranken et al. 2014: deletion of SDH2 ablates the SDH holocomplex, showing Sdh2p is a required structural component of complex II. Supporting Evidence: PMID:24954416 We also observed that deletion of SDH2 or SDH4, which ablates the SDH holocomplex PMID:24954416 The Sdh3/Sdh4 dimer binds the peripheral membrane protein Sdh2 (SDHB), which tethers the catalytic Sdh1 (SDHA) subunit to the complex. |
| GO:0045273 respiratory chain complex II (succinate dehydrogenase) | IPI PMID:8120006 Isolation and characterization of the Saccharomyces cerevisi... | ACCEPT | Summary: IPI from Bullis & Lemire 1994, who purified SDH by blue native electrophoresis as a flavoprotein / iron-sulfur / two hydrophobic subunit heterotetramer. Supporting Evidence: PMID:8120006 It is a heterotetramer composed of a flavoprotein, an iron-sulfur, and two hydrophobic subunits. PMID:8120006 We purified succinate dehydrogenase by blue native gel electrophoresis |
| GO:0045333 cellular respiration | IGI PMID:16232921 Effect of gene disruption of succinate dehydrogenase on succ... | TOO GENERAL | Summary: IGI with SDH1 (Kubo et al. 2000): sdh1 sdh2 double disruptants cannot grow on glycerol. 'Cellular respiration' is correct but broad; the specific processes (TCA cycle, succinate-to-ubiquinone electron transport) are also annotated. Supporting Evidence: PMID:16232921 Two double disruptants showed no growth on a medium containing glycerol as the sole carbon source, while the single disruptants could utilize glycerol. |
| GO:0045333 cellular respiration | IMP PMID:16232921 Effect of gene disruption of succinate dehydrogenase on succ... | TOO GENERAL | Summary: IMP (Kubo et al. 2000) for cellular respiration. Correct, broad. Supporting Evidence: PMID:16232921 Two double disruptants showed no growth on a medium containing glycerol as the sole carbon source, while the single disruptants could utilize glycerol. |
| GO:0051536 iron-sulfur cluster binding | IEA GO_REF:0000002 | ACCEPT | Summary: InterPro2GO (several Fe-S domain entries) to iron-sulfur cluster binding. Correct: Sdh2p binds one [2Fe-2S], one [4Fe-4S] and one [3Fe-4S] cluster (by similarity in UniProt; three clusters noted in yeast by Dibrov et al.). Supporting Evidence: PMID:9822678 The membrane extrinsic domain, consisting of Sdh1p and Sdh2p, contains a covalent FAD cofactor and three iron-sulfur clusters. file:yeast/SDH2/SDH2-uniprot.txt Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000250}; |
| GO:0051537 2 iron, 2 sulfur cluster binding | IEA GO_REF:0000002 | ACCEPT | Summary: InterPro2GO (IPR006058, 2Fe-2S ferredoxin-type domain) to 2Fe-2S cluster binding. Correct for the N-terminal ferredoxin domain of Sdh2p. The 4Fe-4S and 3Fe-4S clusters are not separately annotated. Supporting Evidence: file:yeast/SDH2/SDH2-uniprot.txt Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000250}; |
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Download this section (compressed HTML)Iron-sulfur protein subunit of succinate dehydrogenase; the complex couples the oxidation of succinate to the transfer of electrons to ubiquinone as part of the TCA cycle and the mitochondrial respiratory chain; other members are Sdh1p, Sdh3p, and Sdh4p
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