E2 component (Kgd2p, YDR148C; dihydrolipoyllysine-residue succinyltransferase, KE2) of the mitochondrial 2-oxoglutarate dehydrogenase complex (KGDH). Kgd2 carries a covalently attached lipoyl group and forms the oligomeric core of the complex to which the E1 Kgd1 and, via the adaptor Kgd4, the E3 Lpd1 bind. It transfers the succinyl group from the S-succinyldihydrolipoyl arm to coenzyme A, producing succinyl-CoA in the TCA cycle in the mitochondrial matrix (EC 2.3.1.61). kgd2 mutants lack KGDH activity and are respiratory-deficient. KGD2 is glucose-repressed and HAP2/3-activated. Kgd2 also associates with mitochondrial nucleoids and crosslinks to mtDNA, and its loss enhances mtDNA instability in abf2 mutants.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0004149 dihydrolipoyllysine-residue succinyltransferase activity | IBA GO_REF:0000033 | ACCEPT | Summary: IBA from PANTHER PTN000567956 (E2o clade; donors include E. coli SucB, human DLST and yeast Kgd2). Succinyltransferase activity is the conserved E2o function and is supported by yeast genetics. Supporting Evidence: file:yeast/KGD2/KGD2-uniprot.txt Reaction=N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] + succinyl-CoA = PMID:2115121 42% identities to the KE2 component of Escherichia coli alpha-ketoglutarate dehydrogenase complex |
| GO:0004149 dihydrolipoyllysine-residue succinyltransferase activity | IEA GO_REF:0000120 | ACCEPT | Summary: IEA from InterPro IPR006255 / Rhea RHEA:15213 / EC 2.3.1.61. Correct for the E2 component. Supporting Evidence: file:yeast/KGD2/KGD2-uniprot.txt Reaction=N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] + succinyl-CoA = |
| GO:0004149 dihydrolipoyllysine-residue succinyltransferase activity | IMP PMID:2115121 Structure and regulation of KGD2, the structural gene for ye... | ACCEPT | Summary: IMP from Repetto & Tzagoloff 1990: kgd2 (pet G104) mutants and disruptants lack 2-oxoglutarate dehydrogenase activity. The phenotype reflects loss of the whole complex, but Kgd2 is the E2 succinyltransferase core. Supporting Evidence: PMID:2115121 Yeast mutants assigned to the pet complementation group G104 were found to lack alpha-ketoglutarate dehydrogenase activity as a result of mutations in the dihydrolipoyl transsuccinylase (KE2) component of the complex PMID:2115121 Disruption of the chromosomal copy of KGD2 in a respiratory-competent haploid yeast strain elicited a growth phenotype similar to that of G104 mutants and abolished the ability to mitochondria to catalyze the reduction of NAD+ by alpha-ketoglutarate |
| GO:0004149 dihydrolipoyllysine-residue succinyltransferase activity | ISA PMID:2115121 Structure and regulation of KGD2, the structural gene for ye... | ACCEPT | Summary: ISA from Repetto & Tzagoloff 1990 based on sequence alignment with E. coli KE2 (SucB). Correct. Supporting Evidence: PMID:2115121 42% identities to the KE2 component of Escherichia coli alpha-ketoglutarate dehydrogenase complex |
| GO:0004149 dihydrolipoyllysine-residue succinyltransferase activity | RCA GO_REF:0000123 | ACCEPT | Summary: RCA from YeastPathways PWY-5084 (E2 succinyl transfer from dihydrolipoyl-lysine to CoA). Correct. Supporting Evidence: file:yeast/KGD2/KGD2-uniprot.txt Reaction=N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] + succinyl-CoA = |
| GO:0004591 oxoglutarate dehydrogenase (succinyl-transferring) activity | RCA GO_REF:0000123 | ACCEPT | Summary: RCA from YeastPathways TCA-EUK-PWY with contributes_to for the overall KGDH reaction. GO uses GO:0004591 for the complex-level reaction; Kgd2 contributes the lipoyl carrier and succinyltransferase core, so contributes_to is appropriate. Supporting Evidence: PMID:2072900 The reconstitution of enzymatic activity correlates with binding of KE1 to the KE2-E3 particle to form a complex with the same sedimentation properties as wild-type KGDC PMID:25165143 confirming that Kgd2 forms the core of KGDH around which the other subunits assemble |
| GO:0005515 protein binding | IPI PMID:16429126 Proteome survey reveals modularity of the yeast cell machine... | REMOVE | Summary: IPI Kgd2-Lpd1 from the Krogan et al. 2006 TAP-MS survey. The interaction is genuine (both are subunits of the 2-oxoglutarate dehydrogenase complex) and removal does not mean it is false; 'protein binding' carries no functional information and the relationship is captured by part_of oxoglutarate dehydrogenase complex (GO:0045252). Supporting Evidence: PMID:16429126 Proteome survey reveals modularity of the yeast cell machinery. PMID:25165143 This led to the identification of four proteins that specifically copurified: Kgd1, Kgd2, and Lpd1, the catalytic subunits of KGDH |
| GO:0005515 protein binding | IPI PMID:16429126 Proteome survey reveals modularity of the yeast cell machine... | REMOVE | Summary: IPI Kgd2-Kgd1 from the Krogan et al. 2006 TAP-MS survey. The interaction is genuine (both are subunits of the 2-oxoglutarate dehydrogenase complex) and removal does not mean it is false; 'protein binding' carries no functional information and the relationship is captured by part_of oxoglutarate dehydrogenase complex (GO:0045252). Supporting Evidence: PMID:16429126 Proteome survey reveals modularity of the yeast cell machinery. PMID:25165143 This led to the identification of four proteins that specifically copurified: Kgd1, Kgd2, and Lpd1, the catalytic subunits of KGDH |
| GO:0005515 protein binding | IPI PMID:25165143 The novel component Kgd4 recruits the E3 subunit to the mito... | REMOVE | Summary: IPI Kgd2-Lpd1 from Heublein et al. 2014 copurification/co-migration. The interaction is genuine (both are subunits of the 2-oxoglutarate dehydrogenase complex) and removal does not mean it is false; 'protein binding' carries no functional information and the relationship is captured by part_of oxoglutarate dehydrogenase complex (GO:0045252). Supporting Evidence: PMID:25165143 In lysates from wild-type mitochondria, Kgd1, Kgd2, Lpd1, and Kgd4 comigrated PMID:25165143 This led to the identification of four proteins that specifically copurified: Kgd1, Kgd2, and Lpd1, the catalytic subunits of KGDH |
| GO:0005515 protein binding | IPI PMID:25165143 The novel component Kgd4 recruits the E3 subunit to the mito... | REMOVE | Summary: IPI Kgd2-Kgd1 from Heublein et al. 2014 copurification. The interaction is genuine (both are subunits of the 2-oxoglutarate dehydrogenase complex) and removal does not mean it is false; 'protein binding' carries no functional information and the relationship is captured by part_of oxoglutarate dehydrogenase complex (GO:0045252). Supporting Evidence: PMID:25165143 This led to the identification of four proteins that specifically copurified: Kgd1, Kgd2, and Lpd1, the catalytic subunits of KGDH PMID:25165143 This led to the identification of four proteins that specifically copurified: Kgd1, Kgd2, and Lpd1, the catalytic subunits of KGDH |
| GO:0005515 protein binding | IPI PMID:37968396 The social and structural architecture of the yeast protein ... | REMOVE | Summary: IPI Kgd2-Lpd1 from the Michaelis et al. 2023 interactome. The interaction is genuine (both are subunits of the 2-oxoglutarate dehydrogenase complex) and removal does not mean it is false; 'protein binding' carries no functional information and the relationship is captured by part_of oxoglutarate dehydrogenase complex (GO:0045252). Supporting Evidence: PMID:37968396 The social and structural architecture of the yeast protein interactome. PMID:25165143 This led to the identification of four proteins that specifically copurified: Kgd1, Kgd2, and Lpd1, the catalytic subunits of KGDH |
| GO:0005515 protein binding | IPI PMID:37968396 The social and structural architecture of the yeast protein ... | REMOVE | Summary: IPI Kgd2-Kgd1 from the Michaelis et al. 2023 interactome. The interaction is genuine (both are subunits of the 2-oxoglutarate dehydrogenase complex) and removal does not mean it is false; 'protein binding' carries no functional information and the relationship is captured by part_of oxoglutarate dehydrogenase complex (GO:0045252). Supporting Evidence: PMID:37968396 The social and structural architecture of the yeast protein interactome. PMID:25165143 This led to the identification of four proteins that specifically copurified: Kgd1, Kgd2, and Lpd1, the catalytic subunits of KGDH |
| GO:0005739 mitochondrion | HDA PMID:16823961 Toward the complete yeast mitochondrial proteome: multidimen... | ACCEPT | Summary: HDA from a mitochondrial proteomics study detecting Kgd2. Consistent with the matrix localisation of the 2-oxoglutarate dehydrogenase complex. Supporting Evidence: PMID:16823961 Toward the complete yeast mitochondrial proteome: multidimensional separation techniques for mitochondrial proteomics. PMID:25165143 Mitochondrial KGDH was purified using a C-terminal His7-tag on Kgd1 |
| GO:0005739 mitochondrion | HDA PMID:16823961 Toward the complete yeast mitochondrial proteome: multidimen... | ACCEPT | Summary: HDA from a mitochondrial proteomics study detecting Kgd2. Consistent with the matrix localisation of the 2-oxoglutarate dehydrogenase complex. Supporting Evidence: PMID:16823961 Toward the complete yeast mitochondrial proteome: multidimensional separation techniques for mitochondrial proteomics. PMID:25165143 Mitochondrial KGDH was purified using a C-terminal His7-tag on Kgd1 |
| GO:0005739 mitochondrion | HDA PMID:24769239 Quantitative variations of the mitochondrial proteome and ph... | ACCEPT | Summary: HDA from a mitochondrial proteomics study detecting Kgd2. Consistent with the matrix localisation of the 2-oxoglutarate dehydrogenase complex. Supporting Evidence: PMID:24769239 Quantitative variations of the mitochondrial proteome and phosphoproteome during fermentative and respiratory growth in Saccharomyces cerevisiae. PMID:25165143 Mitochondrial KGDH was purified using a C-terminal His7-tag on Kgd1 |
| GO:0005739 mitochondrion | IBA GO_REF:0000033 | ACCEPT | Summary: IBA from PANTHER PTN000567957 (eukaryotic E2o; donors include human DLST, Arabidopsis, Plasmodium and yeast Kgd2). Correct and inherited. Supporting Evidence: file:yeast/KGD2/KGD2-uniprot.txt SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:25165143}. |
| GO:0005739 mitochondrion | IDA PMID:25165143 The novel component Kgd4 recruits the E3 subunit to the mito... | ACCEPT | Summary: IDA from Heublein et al. 2014: Kgd2 copurifies with KGDH isolated from mitochondria. Supporting Evidence: PMID:25165143 This led to the identification of four proteins that specifically copurified: Kgd1, Kgd2, and Lpd1, the catalytic subunits of KGDH PMID:25165143 Mitochondrial KGDH was purified using a C-terminal His7-tag on Kgd1 |
| GO:0005739 mitochondrion | IEA GO_REF:0000044 | ACCEPT | Summary: IEA from UniProt subcellular location (SL-0173). Correct. Supporting Evidence: file:yeast/KGD2/KGD2-uniprot.txt SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:25165143}. |
| GO:0005739 mitochondrion | RCA GO_REF:0000123 | ACCEPT | Summary: RCA from YeastPathways PWY-5084, mitochondrial placement of the E2 reaction. Correct. Supporting Evidence: PMID:25165143 Mitochondrial KGDH was purified using a C-terminal His7-tag on Kgd1 |
| GO:0005739 mitochondrion | RCA GO_REF:0000123 | ACCEPT | Summary: RCA from YeastPathways TCA-EUK-PWY, mitochondrial placement of the KGDH step. Correct. Supporting Evidence: PMID:25165143 Mitochondrial KGDH was purified using a C-terminal His7-tag on Kgd1 |
| GO:0006099 tricarboxylic acid cycle | IBA GO_REF:0000033 | ACCEPT | Summary: IBA from PANTHER PTN000567956 (E2o clade incl. human DLST, E. coli SucB, fly, S. pombe). TCA-cycle participation is the conserved role. Supporting Evidence: PMID:2115121 Yeast mutants assigned to the pet complementation group G104 were found to lack alpha-ketoglutarate dehydrogenase activity as a result of mutations in the dihydrolipoyl transsuccinylase (KE2) component of the complex |
| GO:0006099 tricarboxylic acid cycle | IEA GO_REF:0000002 | ACCEPT | Summary: IEA from InterPro IPR006255 (2-oxoglutarate dehydrogenase E2 component). Correct. Supporting Evidence: PMID:2115121 42% identities to the KE2 component of Escherichia coli alpha-ketoglutarate dehydrogenase complex |
| GO:0006099 tricarboxylic acid cycle | NAS PMID:25165143 The novel component Kgd4 recruits the E3 subunit to the mito... | ACCEPT | Summary: NAS from Heublein et al. 2014, which frames KGDH as the TCA-cycle enzyme. Correct. Supporting Evidence: PMID:25165143 The mitochondrial citric acid cycle is a central hub of cellular metabolism PMID:25165143 confirming that Kgd2 forms the core of KGDH around which the other subunits assemble |
| GO:0006103 2-oxoglutarate metabolic process | IDA PMID:25165143 The novel component Kgd4 recruits the E3 subunit to the mito... | ACCEPT | Summary: IDA from Heublein et al. 2014: KGDH activity (2-oxoglutarate oxidation) in mitochondrial lysates; Kgd2 forms the core of the complex. Supporting Evidence: PMID:25165143 Robust KGDH activity was observed in lysates from wild-type cells PMID:25165143 confirming that Kgd2 forms the core of KGDH around which the other subunits assemble |
| GO:0006103 2-oxoglutarate metabolic process | IMP PMID:2115121 Structure and regulation of KGD2, the structural gene for ye... | ACCEPT | Summary: IMP from Repetto & Tzagoloff 1990: KGD2 disruption abolishes 2-oxoglutarate-dependent NAD+ reduction by mitochondria. Supporting Evidence: PMID:2115121 Disruption of the chromosomal copy of KGD2 in a respiratory-competent haploid yeast strain elicited a growth phenotype similar to that of G104 mutants and abolished the ability to mitochondria to catalyze the reduction of NAD+ by alpha-ketoglutarate |
| GO:0009060 aerobic respiration | RCA GO_REF:0000123 | ACCEPT | Summary: RCA from YeastPathways TCA-EUK-PWY. Correct; kgd2 mutants are respiratory-deficient. Supporting Evidence: PMID:2115121 Disruption of the chromosomal copy of KGD2 in a respiratory-competent haploid yeast strain elicited a growth phenotype similar to that of G104 mutants and abolished the ability to mitochondria to catalyze the reduction of NAD+ by alpha-ketoglutarate |
| GO:0016746 acyltransferase activity | IEA GO_REF:0000002 | MODIFY | Summary: IEA from InterPro IPR001078 (2-oxoacid dehydrogenase acyltransferase catalytic domain). Correct but too general; the specific activity is dihydrolipoyllysine-residue succinyltransferase activity. Proposed replacements: dihydrolipoyllysine-residue succinyltransferase activity Supporting Evidence: file:yeast/KGD2/KGD2-uniprot.txt Reaction=N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] + succinyl-CoA = |
| GO:0042645 mitochondrial nucleoid | IDA PMID:10869431 In organello formaldehyde crosslinking of proteins to mtDNA:... | KEEP AS NON CORE | Summary: IDA from Kaufman et al. 2000: Kgd2 was crosslinked to mtDNA in organello, and kgd2-null enhances the petite phenotype of abf2-null. A genuine but secondary association with nucleoids. Supporting Evidence: PMID:10869431 such as the molecular chaperone Hsp60p and a Krebs cycle protein, Kgd2p PMID:10869431 a kgd2Delta mutation increases the petite-inducing phenotype of an abf2Delta mutation |
| GO:0042645 mitochondrial nucleoid | IDA PMID:11926067 Identification of the YMN-1 antigen protein and biochemical ... | KEEP AS NON CORE | Summary: IDA from Sato et al. 2002: the YMN-1 nucleoid antigen is KE2 (Kgd2). Real association, peripheral to the TCA-cycle role. Supporting Evidence: PMID:11926067 recognizes dihydrolipoyl transsuccinylase (KE2), which is one of the constituents of the alpha-ketoglutarate dehydrogenase complex (KGDC) PMID:11926067 These results suggested that a part of KGDC in the mitochondrial matrix is associated with mt-nucleoids in vivo |
| GO:0045252 oxoglutarate dehydrogenase complex | IDA PMID:2072900 In vivo assembly of yeast mitochondrial alpha-ketoglutarate ... | ACCEPT | Summary: IDA from Repetto & Tzagoloff 1991: KE2 forms the core particle to which E3 and KE1 bind to reconstitute KGDC. Supporting Evidence: PMID:2072900 Thus mutants lacking KE1 assemble a high-molecular-weight subcomplex consisting of a KE2 core particle with bound dihydrolipoyl dehydrogenase (E3) PMID:2072900 The reconstitution of enzymatic activity correlates with binding of KE1 to the KE2-E3 particle to form a complex with the same sedimentation properties as wild-type KGDC |
| GO:0045252 oxoglutarate dehydrogenase complex | IEA GO_REF:0000002 | ACCEPT | Summary: IEA from InterPro IPR006255 (E2o). Correct. Supporting Evidence: PMID:2115121 42% identities to the KE2 component of Escherichia coli alpha-ketoglutarate dehydrogenase complex |
| GO:0045252 oxoglutarate dehydrogenase complex | IPI PMID:25165143 The novel component Kgd4 recruits the E3 subunit to the mito... | ACCEPT | Summary: IPI from Heublein et al. 2014: Kgd2 copurifies with Kgd1-His7 and forms the core around which other subunits assemble. Supporting Evidence: PMID:25165143 This led to the identification of four proteins that specifically copurified: Kgd1, Kgd2, and Lpd1, the catalytic subunits of KGDH PMID:25165143 confirming that Kgd2 forms the core of KGDH around which the other subunits assemble |
| GO:0045333 cellular respiration | IMP PMID:2115121 Structure and regulation of KGD2, the structural gene for ye... | TOO GENERAL | Summary: IMP from Repetto & Tzagoloff 1990: kgd2 disruption gives a respiratory-deficient (pet) growth phenotype. Correct but general. Supporting Evidence: PMID:2115121 Disruption of the chromosomal copy of KGD2 in a respiratory-competent haploid yeast strain elicited a growth phenotype similar to that of G104 mutants and abolished the ability to mitochondria to catalyze the reduction of NAD+ by alpha-ketoglutarate |
| GO:0045333 cellular respiration | RCA GO_REF:0000123 | TOO GENERAL | Summary: RCA from YeastPathways PWY-5084. Correct but general. Supporting Evidence: PMID:2115121 Yeast mutants assigned to the pet complementation group G104 were found to lack alpha-ketoglutarate dehydrogenase activity as a result of mutations in the dihydrolipoyl transsuccinylase (KE2) component of the complex |
Loading supporting content…
Download this section (compressed HTML)Dihydrolipoyl transsuccinylase; component of the mitochondrial alpha-ketoglutarate dehydrogenase complex, which catalyzes the oxidative decarboxylation of alpha-ketoglutarate to succinyl-CoA in the TCA cycle; phosphorylated
Loading supporting content…
Download this section (compressed HTML)Loading supporting content…
Download this section (compressed HTML)