ODO1_MOUSE
ID ODO1_MOUSE Reviewed; 1023 AA.
AC Q60597; Q3UDM7; Q5DTI4; Q5SVX7; Q5SVX9; Q6PFZ2; Q80Y57; Q8K0K7; Q8K2Z3;
AC Q8R3M2; Q91WP2;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 3.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=2-oxoglutarate dehydrogenase complex component E1;
DE Short=E1o;
DE Short=OGDC-E1;
DE Short=OGDH-E1;
DE EC=1.2.4.2 {ECO:0000250|UniProtKB:Q02218};
DE AltName: Full=2-oxoglutarate dehydrogenase, mitochondrial;
DE AltName: Full=Alpha-ketoglutarate dehydrogenase;
DE Short=Alpha-KGDH-E1;
DE AltName: Full=Thiamine diphosphate (ThDP)-dependent 2-oxoglutarate dehydrogenase;
DE Flags: Precursor;
GN Name=Ogdh; Synonyms=Kiaa4192;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Brain;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4).
RC STRAIN=C57BL/6J, and FVB/N;
RC TISSUE=Brain, Colon, Mammary tumor, and Salivary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 123-135; 185-204; 311-319; 561-568; 616-633 AND
RP 916-925, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus;
RA Lubec G., Klug S., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 829-958 (ISOFORMS 1/2/3/4).
RC STRAIN=BALB/cJ;
RX PubMed=8248240; DOI=10.1073/pnas.90.23.11272;
RA Udaka K., Tsomides T.J., Walden P., Fukusen N., Eisen H.N.;
RT "A ubiquitous protein is the source of naturally occurring peptides that
RT are recognized by a CD8+ T-cell clone.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:11272-11276(1993).
RN [7]
RP PROTEIN SEQUENCE OF 933-939.
RX PubMed=1606619; DOI=10.1016/0092-8674(92)90617-l;
RA Udaka K., Tsomides T.J., Eisen H.N.;
RT "A naturally occurring peptide recognized by alloreactive CD8+ cytotoxic T
RT lymphocytes in association with a class I MHC protein.";
RL Cell 69:989-998(1992).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-74 AND LYS-564, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-401, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
CC -!- FUNCTION: 2-oxoglutarate dehydrogenase (E1o) component of the 2-
CC oxoglutarate dehydrogenase complex (OGDHC). Participates in the first
CC step, rate limiting for the overall conversion of 2-oxoglutarate to
CC succinyl-CoA and CO(2) catalyzed by the whole OGDHC. Catalyzes the
CC irreversible decarboxylation of 2-oxoglutarate (alpha-ketoglutarate)
CC via the thiamine diphosphate (ThDP) cofactor and subsequent transfer of
CC the decarboxylated acyl intermediate on an oxidized dihydrolipoyl group
CC that is covalently amidated to the E2 enzyme (dihydrolipoyllysine-
CC residue succinyltransferase or DLST). Plays a key role in the Krebs
CC (citric acid) cycle, which is a common pathway for oxidation of fuel
CC molecules, including carbohydrates, fatty acids, and amino acids. Can
CC catalyze the decarboxylation of 2-oxoadipate in vitro, but at a much
CC lower rate than 2-oxoglutarate. Mainly active in the mitochondrion. A
CC fraction of the 2-oxoglutarate dehydrogenase complex also localizes in
CC the nucleus and is required for lysine succinylation of histones:
CC associates with KAT2A on chromatin and provides succinyl-CoA to histone
CC succinyltransferase KAT2A. {ECO:0000250|UniProtKB:Q02218}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue
CC succinyltransferase] + 2-oxoglutarate + H(+) = (R)-N(6)-(S(8)-
CC succinyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue
CC succinyltransferase] + CO2; Xref=Rhea:RHEA:12188, Rhea:RHEA-
CC COMP:10483, Rhea:RHEA-COMP:10484, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:83099,
CC ChEBI:CHEBI:83120; EC=1.2.4.2;
CC Evidence={ECO:0000250|UniProtKB:Q02218};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12189;
CC Evidence={ECO:0000250|UniProtKB:Q02218};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000250|UniProtKB:Q02218};
CC -!- ACTIVITY REGULATION: Calcium ions and ADP stimulate, whereas ATP and
CC NADH reduce catalytic activity. {ECO:0000250|UniProtKB:Q02218}.
CC -!- SUBUNIT: The 2-oxoglutarate dehydrogenase complex is composed of OGDH
CC (2-oxoglutarate dehydrogenase; E1), DLST (dihydrolipoamide
CC succinyltransferase; E2) and DLD (dihydrolipoamide dehydrogenase; E3).
CC It contains multiple copies of the three enzymatic components (E1, E2
CC and E3). In the nucleus, the 2-oxoglutarate dehydrogenase complex
CC associates with KAT2A. {ECO:0000250|UniProtKB:Q02218}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q5XI78}.
CC Nucleus {ECO:0000250|UniProtKB:Q02218}. Note=Mainly localizes in the
CC mitochondrion. A small fraction localizes to the nucleus, where the 2-
CC oxoglutarate dehydrogenase complex is required for histone
CC succinylation. {ECO:0000250|UniProtKB:Q02218}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q60597-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q60597-2; Sequence=VSP_024799;
CC Name=3;
CC IsoId=Q60597-3; Sequence=VSP_024801;
CC Name=4;
CC IsoId=Q60597-4; Sequence=VSP_024800;
CC -!- MISCELLANEOUS: The mitochondrial 2-oxoglutarate and 2-oxoadipate
CC dehydrogenase complexes (OGDHC and OADHC, respectively) share their E2
CC (DLST) and E3 (dihydrolipoyl dehydrogenase or DLD) components, but the
CC E1 component is specific to each complex (E1o and E1a (DHTK1),
CC respectively). {ECO:0000250|UniProtKB:Q96HY7}.
CC -!- SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH31165.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAD90530.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK147289; BAE27824.1; -; mRNA.
DR EMBL; AK150009; BAE29234.1; -; mRNA.
DR EMBL; AK169286; BAE41044.1; -; mRNA.
DR EMBL; AK220536; BAD90530.1; ALT_INIT; mRNA.
DR EMBL; AL607152; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC025040; AAH25040.1; -; mRNA.
DR EMBL; BC013670; AAH13670.1; -; mRNA.
DR EMBL; BC029143; AAH29143.1; -; mRNA.
DR EMBL; BC031165; AAH31165.1; ALT_INIT; mRNA.
DR EMBL; BC049104; AAH49104.1; -; mRNA.
DR EMBL; BC057354; AAH57354.1; -; mRNA.
DR EMBL; U02971; AAC52130.1; -; mRNA.
DR CCDS; CCDS36106.1; -. [Q60597-1]
DR CCDS; CCDS56758.1; -. [Q60597-4]
DR PIR; I48884; A41911.
DR RefSeq; NP_001239211.1; NM_001252282.1. [Q60597-3]
DR RefSeq; NP_001239212.1; NM_001252283.1. [Q60597-4]
DR RefSeq; NP_001239216.1; NM_001252287.1. [Q60597-1]
DR RefSeq; NP_001239217.1; NM_001252288.1.
DR RefSeq; NP_035086.2; NM_010956.4. [Q60597-1]
DR RefSeq; XP_006514645.1; XM_006514582.2. [Q60597-4]
DR RefSeq; XP_006514646.1; XM_006514583.3.
DR RefSeq; XP_006514647.1; XM_006514584.3. [Q60597-4]
DR RefSeq; XP_006514648.1; XM_006514585.2.
DR RefSeq; XP_017169826.1; XM_017314337.1.
DR PDB; 3E2H; X-ray; 3.80 A; Q=932-940.
DR PDB; 3TF7; X-ray; 2.75 A; B/F=932-940.
DR PDBsum; 3E2H; -.
DR PDBsum; 3TF7; -.
DR AlphaFoldDB; Q60597; -.
DR SMR; Q60597; -.
DR BioGRID; 201905; 24.
DR IntAct; Q60597; 7.
DR MINT; Q60597; -.
DR STRING; 10090.ENSMUSP00000003461; -.
DR ChEMBL; CHEMBL2176831; -.
DR iPTMnet; Q60597; -.
DR PhosphoSitePlus; Q60597; -.
DR SwissPalm; Q60597; -.
DR REPRODUCTION-2DPAGE; Q60597; -.
DR EPD; Q60597; -.
DR jPOST; Q60597; -.
DR MaxQB; Q60597; -.
DR PaxDb; Q60597; -.
DR PeptideAtlas; Q60597; -.
DR PRIDE; Q60597; -.
DR ProteomicsDB; 289960; -. [Q60597-1]
DR ProteomicsDB; 289961; -. [Q60597-2]
DR ProteomicsDB; 289962; -. [Q60597-3]
DR ProteomicsDB; 289963; -. [Q60597-4]
DR ABCD; Q60597; 1 sequenced antibody.
DR Antibodypedia; 13451; 241 antibodies from 27 providers.
DR DNASU; 18293; -.
DR Ensembl; ENSMUST00000003461; ENSMUSP00000003461; ENSMUSG00000020456. [Q60597-1]
DR Ensembl; ENSMUST00000093350; ENSMUSP00000091041; ENSMUSG00000020456. [Q60597-4]
DR Ensembl; ENSMUST00000101554; ENSMUSP00000099090; ENSMUSG00000020456. [Q60597-1]
DR GeneID; 18293; -.
DR KEGG; mmu:18293; -.
DR UCSC; uc007hyf.2; mouse. [Q60597-1]
DR UCSC; uc007hyg.2; mouse. [Q60597-3]
DR UCSC; uc007hyh.2; mouse. [Q60597-4]
DR CTD; 4967; -.
DR MGI; MGI:1098267; Ogdh.
DR VEuPathDB; HostDB:ENSMUSG00000020456; -.
DR eggNOG; KOG0450; Eukaryota.
DR GeneTree; ENSGT00950000183125; -.
DR HOGENOM; CLU_004709_1_1_1; -.
DR InParanoid; Q60597; -.
DR OMA; RDSYCRT; -.
DR OrthoDB; 134699at2759; -.
DR PhylomeDB; Q60597; -.
DR TreeFam; TF300695; -.
DR Reactome; R-MMU-389661; Glyoxylate metabolism and glycine degradation.
DR Reactome; R-MMU-71064; Lysine catabolism.
DR Reactome; R-MMU-71403; Citric acid cycle (TCA cycle).
DR BioGRID-ORCS; 18293; 25 hits in 72 CRISPR screens.
DR ChiTaRS; Ogdh; mouse.
DR PRO; PR:Q60597; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q60597; protein.
DR Bgee; ENSMUSG00000020456; Expressed in myocardium of ventricle and 280 other tissues.
DR ExpressionAtlas; Q60597; baseline and differential.
DR Genevisible; Q60597; MM.
DR GO; GO:0031966; C:mitochondrial membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0045252; C:oxoglutarate dehydrogenase complex; ISS:UniProtKB.
DR GO; GO:0051087; F:chaperone binding; IEA:Ensembl.
DR GO; GO:0031072; F:heat shock protein binding; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0034602; F:oxoglutarate dehydrogenase (NAD+) activity; IDA:MGI.
DR GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; ISS:UniProtKB.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; ISS:UniProtKB.
DR GO; GO:0006103; P:2-oxoglutarate metabolic process; ISS:UniProtKB.
DR GO; GO:0021695; P:cerebellar cortex development; IEP:UniProtKB.
DR GO; GO:0006091; P:generation of precursor metabolites and energy; ISS:UniProtKB.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR GO; GO:0021766; P:hippocampus development; IEP:UniProtKB.
DR GO; GO:0106077; P:histone succinylation; ISS:UniProtKB.
DR GO; GO:0006734; P:NADH metabolic process; IEA:Ensembl.
DR GO; GO:0061034; P:olfactory bulb mitral cell layer development; IEP:UniProtKB.
DR GO; GO:0021860; P:pyramidal neuron development; IEP:UniProtKB.
DR GO; GO:0021756; P:striatum development; IEP:UniProtKB.
DR GO; GO:0006104; P:succinyl-CoA metabolic process; ISS:UniProtKB.
DR GO; GO:0022028; P:tangential migration from the subventricular zone to the olfactory bulb; IEP:UniProtKB.
DR GO; GO:0021794; P:thalamus development; IEP:UniProtKB.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
DR Gene3D; 3.40.50.11610; -; 1.
DR InterPro; IPR032106; 2-oxogl_dehyd_N.
DR InterPro; IPR011603; 2oxoglutarate_DH_E1.
DR InterPro; IPR001017; DH_E1.
DR InterPro; IPR031717; KGD_C.
DR InterPro; IPR042179; KGD_C_sf.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR PANTHER; PTHR23152; PTHR23152; 1.
DR Pfam; PF16078; 2-oxogl_dehyd_N; 1.
DR Pfam; PF00676; E1_dh; 1.
DR Pfam; PF16870; OxoGdeHyase_C; 1.
DR Pfam; PF02779; Transket_pyr; 1.
DR PIRSF; PIRSF000157; Oxoglu_dh_E1; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52518; SSF52518; 2.
DR TIGRFAMs; TIGR00239; 2oxo_dh_E1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Calcium;
KW Direct protein sequencing; Glycolysis; Isopeptide bond; Metal-binding;
KW Mitochondrion; Nucleus; Oxidoreductase; Phosphoprotein; Reference proteome;
KW Thiamine pyrophosphate; Transit peptide; Ubl conjugation.
FT TRANSIT 1..40
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 41..1023
FT /note="2-oxoglutarate dehydrogenase complex component E1"
FT /id="PRO_0000020434"
FT REGION 933..939
FT /note="Recognized by alloreactive CD8 cytotoxic T-
FT lymphocytes in association with a class I MHC protein"
FT BINDING 154
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q02218"
FT BINDING 156
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q02218"
FT BINDING 158
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q02218"
FT BINDING 179
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q02218"
FT BINDING 181
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q02218"
FT BINDING 183
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q02218"
FT MOD_RES 74
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 401
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 564
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 970
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q02218"
FT CROSSLNK 534
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q02218"
FT VAR_SEQ 139..172
FT /note="IRGHHVAQLDPLGILDADLDSSVPADIISSTDKL -> VRGHHIAKSCVNFD
FT DAPVTVSSNV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_024799"
FT VAR_SEQ 139..172
FT /note="IRGHHVAQLDPLGILDADLDSSVPADIISSTDKL -> VRGHHIAKLDPLGI
FT SCVNFDDAPVTVSSNVDLAVFKERLRMLTVG (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_024800"
FT VAR_SEQ 172
FT /note="L -> LDLAVFKERLRMLTVG (in isoform 3)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_024801"
FT CONFLICT 416
FT /note="G -> V (in Ref. 4; AAH49104)"
FT /evidence="ECO:0000305"
FT CONFLICT 549
FT /note="V -> F (in Ref. 4; AAH49104)"
FT /evidence="ECO:0000305"
FT CONFLICT 552
FT /note="Q -> E (in Ref. 4; AAH57354)"
FT /evidence="ECO:0000305"
FT CONFLICT 576
FT /note="E -> K (in Ref. 1; BAE29234)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1023 AA; 116449 MW; A0F3F8D36C7A76BC CRC64;
MFHLRTCAAK LRPLTASQTV KTFSQNKPAA IRTFQQIRCY SAPVAAEPFL SGTSSNYVEE
MYCAWLENPK SVHKSWDIFF RNTNAGAPPG TAYQSPLSLS RSSLATMAHA QSLVEAQPNV
DKLVEDHLAV QSLIRAYQIR GHHVAQLDPL GILDADLDSS VPADIISSTD KLGFYGLHES
DLDKVFHLPT TTFIGGQEPA LPLREIIRRL EMAYCQHIGV EFMFINDLEQ CQWIRQKFET
PGIMQFTNEE KRTLLARLVR STRFEEFLQR KWSSEKRFGL EGCEVLIPAL KTIIDMSSAN
GVDYVIMGMP HRGRLNVLAN VIRKELEQIF CQFDSKLEAA DEGSGDMKYH LGMYHRRINR
VTDRNITLSL VANPSHLEAA DPVVMGKTKA EQFYCGDTEG KKVMSILLHG DAAFAGQGIV
YETFHLSDLP SYTTHGTVHV VVNNQIGFTT DPRMARSSPY PTDVARVVNA PIFHVNSDDP
EAVMYVCKVA AEWRNTFHKD VVVDLVCYRR NGHNEMDEPM FTQPLMYKQI RKQKPVLQKY
AELLVSQGVV NQPEYEEEIS KYDKICEEAF TRSKDEKILH IKHWLDSPWP GFFTLDGQPR
SMTCPSTGLE EDVLFHIGKV ASSVPVENFT IHGGLSRILK TRRELVTNRT VDWALAEYMA
FGSLLKEGIH VRLSGQDVER GTFSHRHHVL HDQNVDKRTC IPMNHLWPNQ APYTVCNSSL
SEYGVLGFEL GFAMASPNAL VLWEAQFGDF NNMAQCIIDQ FICPGQAKWV RQNGIVLLLP
HGMEGMGPEH SSARPERFLQ MCNDDPDVLP DLQEENFDIN QLYDCNWIVV NCSTPGNFFH
VLRRQILLPF RKPLIVFTPK SLLRHPEART SFDEMLPGTH FQRVIPENGP AAQDPHKVKR
LLFCTGKVYY DLTRERKARN MEEEVAITRI EQLSPFPFDL LLKEAQKYPN AELAWCQEEH
KNQGYYDYVK PRLRTTIDRA KPVWYAGRDP AAAPATGNKK THLTELQRFL DTAFDLDAFK
KFS
