ODO1_RAT
ID ODO1_RAT Reviewed; 1023 AA.
AC Q5XI78;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=2-oxoglutarate dehydrogenase complex component E1;
DE Short=E1o {ECO:0000303|PubMed:18783430};
DE Short=OGDC-E1;
DE Short=OGDH-E1 {ECO:0000303|PubMed:18783430};
DE EC=1.2.4.2 {ECO:0000305|PubMed:18783430};
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 {ECO:0000303|PubMed:18783430};
DE Flags: Precursor;
GN Name=Ogdh; Synonyms=Ogdhl;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 [2]
RP PROTEIN SEQUENCE OF 82-101; 123-135; 172-184 AND 583-600, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Spinal cord;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (DEC-2006) to UniProtKB.
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=18783430; DOI=10.1111/j.1742-4658.2008.06632.x;
RA Bunik V., Kaehne T., Degtyarev D., Shcherbakova T., Reiser G.;
RT "Novel isoenzyme of 2-oxoglutarate dehydrogenase is identified in brain,
RT but not in heart.";
RL FEBS J. 275:4990-5006(2008).
CC -!- FUNCTION: 2-oxoglutarate dehydrogenase (E1o) component of the 2-
CC oxoglutarate dehydrogenase complex (OGDHC) (PubMed:18783430).
CC Participates in the first step, rate limiting for the overall
CC conversion of 2-oxoglutarate to succinyl-CoA and CO(2) catalyzed by the
CC whole OGDHC (Probable). Catalyzes the irreversible decarboxylation of
CC 2-oxoglutarate (alpha-ketoglutarate) via the thiamine diphosphate
CC (ThDP) cofactor and subsequent transfer of the decarboxylated acyl
CC intermediate on an oxidized dihydrolipoyl group that is covalently
CC amidated to the E2 enzyme (dihydrolipoyllysine-residue
CC succinyltransferase or DLST) (Probable). 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 (By
CC similarity). Can catalyze the decarboxylation of 2-oxoadipate in vitro,
CC but at a much lower rate than 2-oxoglutarate (By similarity). Mainly
CC active in the mitochondrion. A fraction of the 2-oxoglutarate
CC dehydrogenase complex also localizes in the nucleus and is required for
CC lysine succinylation of histones: associates with KAT2A on chromatin
CC and provides succinyl-CoA to histone succinyltransferase KAT2A (By
CC similarity). {ECO:0000250|UniProtKB:Q02218,
CC ECO:0000269|PubMed:18783430, ECO:0000305|PubMed:18783430}.
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:0000305|PubMed:18783430};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12189;
CC Evidence={ECO:0000305|PubMed:18783430};
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:0000269|PubMed:18783430}.
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 -!- TISSUE SPECIFICITY: The OGDH-containing OGDHC complex is present in the
CC brain and in the heart. {ECO:0000269|PubMed:18783430}.
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}.
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DR EMBL; BC083811; AAH83811.1; -; mRNA.
DR RefSeq; NP_001017461.1; NM_001017461.1.
DR RefSeq; XP_006251508.1; XM_006251446.3.
DR RefSeq; XP_006251509.1; XM_006251447.2.
DR RefSeq; XP_017460322.1; XM_017604833.1.
DR RefSeq; XP_017460323.1; XM_017604834.1.
DR AlphaFoldDB; Q5XI78; -.
DR SMR; Q5XI78; -.
DR BioGRID; 262341; 2.
DR STRING; 10116.ENSRNOP00000054026; -.
DR iPTMnet; Q5XI78; -.
DR PhosphoSitePlus; Q5XI78; -.
DR World-2DPAGE; 0004:Q5XI78; -.
DR jPOST; Q5XI78; -.
DR PaxDb; Q5XI78; -.
DR PRIDE; Q5XI78; -.
DR Ensembl; ENSRNOT00000057199; ENSRNOP00000054026; ENSRNOG00000005130.
DR GeneID; 360975; -.
DR KEGG; rno:360975; -.
DR CTD; 4967; -.
DR RGD; 1561359; Ogdh.
DR eggNOG; KOG0450; Eukaryota.
DR GeneTree; ENSGT00950000183125; -.
DR InParanoid; Q5XI78; -.
DR OMA; RDSYCRT; -.
DR OrthoDB; 134699at2759; -.
DR PhylomeDB; Q5XI78; -.
DR Reactome; R-RNO-389661; Glyoxylate metabolism and glycine degradation.
DR Reactome; R-RNO-71064; Lysine catabolism.
DR Reactome; R-RNO-71403; Citric acid cycle (TCA cycle).
DR SABIO-RK; Q5XI78; -.
DR PRO; PR:Q5XI78; -.
DR Proteomes; UP000002494; Chromosome 14.
DR Bgee; ENSRNOG00000005130; Expressed in skeletal muscle tissue and 18 other tissues.
DR GO; GO:0031966; C:mitochondrial membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0045252; C:oxoglutarate dehydrogenase complex; IDA:RGD.
DR GO; GO:0051087; F:chaperone binding; IPI:RGD.
DR GO; GO:0031072; F:heat shock protein binding; IPI:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0034602; F:oxoglutarate dehydrogenase (NAD+) activity; ISO:RGD.
DR GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; IDA:RGD.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; ISS:UniProtKB.
DR GO; GO:0006103; P:2-oxoglutarate metabolic process; IDA:RGD.
DR GO; GO:0021695; P:cerebellar cortex development; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0106077; P:histone succinylation; ISS:UniProtKB.
DR GO; GO:0006734; P:NADH metabolic process; IDA:RGD.
DR GO; GO:0061034; P:olfactory bulb mitral cell layer development; ISO:RGD.
DR GO; GO:0021860; P:pyramidal neuron development; ISO:RGD.
DR GO; GO:0021756; P:striatum development; ISO:RGD.
DR GO; GO:0006104; P:succinyl-CoA metabolic process; IDA:RGD.
DR GO; GO:0022028; P:tangential migration from the subventricular zone to the olfactory bulb; ISO:RGD.
DR GO; GO:0021794; P:thalamus development; ISO:RGD.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IDA:RGD.
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 Acetylation; Calcium; Direct protein sequencing; Glycolysis;
KW Isopeptide bond; Metal-binding; Mitochondrion; Nucleus; Oxidoreductase;
KW Phosphoprotein; Reference proteome; Thiamine pyrophosphate;
KW 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_0000271367"
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:0000250|UniProtKB:Q60597"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q60597"
FT MOD_RES 401
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q60597"
FT MOD_RES 564
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q60597"
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"
SQ SEQUENCE 1023 AA; 116296 MW; B258886383FBD98C 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 EDILTHIGNV ASSVPVENFT IHGGLSRILK TRRELVTNRT VDWALAEYMA
FGSLLKEGIH VRLSGQDVER GTFSHRHHVL HDQNVDKRTC IPMNHLWPNQ APYTVCNSSL
SEYGVLGFEL GFAMASPNAL VLWEAQFGDF NNMAQCIIDQ FICPGQAKWV RQNGIVLLLP
HGMEGMGPEH SSARPERFLQ MCNDDPDVLP NLQEENFDIS QLYDCNWIVV NCSTPGNFFH
VLRRQILLPF RKPLIVFTPK SLLRHPEART SFDEMLPGTH FQRVIPEDGP AAQNPDKVKR
LLFCTGKVYY DLTRERKARD MAEEVAITRI EQLSPFPFDL LLKEAQKYPN AELAWCQEEH
KNQGYYDYVK PRLRTTIDRA KPVWYAGRDP AAAPATGNKK THLTELQRFL DTAFDLDAFK
KFS
