ODO1_BOVIN
ID ODO1_BOVIN Reviewed; 1023 AA.
AC Q148N0;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 111.
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;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Uterus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
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 -!- 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; BC118106; AAI18107.1; -; mRNA.
DR RefSeq; NP_001069498.1; NM_001076030.1.
DR RefSeq; XP_005205655.1; XM_005205598.3.
DR AlphaFoldDB; Q148N0; -.
DR SMR; Q148N0; -.
DR IntAct; Q148N0; 1.
DR STRING; 9913.ENSBTAP00000007922; -.
DR PaxDb; Q148N0; -.
DR PeptideAtlas; Q148N0; -.
DR PRIDE; Q148N0; -.
DR Ensembl; ENSBTAT00000007922; ENSBTAP00000007922; ENSBTAG00000006029.
DR GeneID; 534599; -.
DR KEGG; bta:534599; -.
DR CTD; 4967; -.
DR VEuPathDB; HostDB:ENSBTAG00000006029; -.
DR VGNC; VGNC:32406; OGDH.
DR eggNOG; KOG0450; Eukaryota.
DR GeneTree; ENSGT00950000183125; -.
DR HOGENOM; CLU_004709_1_1_1; -.
DR InParanoid; Q148N0; -.
DR OrthoDB; 134699at2759; -.
DR TreeFam; TF300695; -.
DR Proteomes; UP000009136; Chromosome 4.
DR Bgee; ENSBTAG00000006029; Expressed in corpus luteum and 105 other tissues.
DR ExpressionAtlas; Q148N0; baseline and differential.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0045252; C:oxoglutarate dehydrogenase complex; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR GO; GO:0106077; P:histone succinylation; ISS:UniProtKB.
DR GO; GO:0006104; P:succinyl-CoA metabolic process; ISS: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 2: Evidence at transcript level;
KW Acetylation; Calcium; 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_0000310981"
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; 115808 MW; 46C5D3161D41F551 CRC64;
MFHLRTCAAK LRPLTASQTV KTFSQNRPAA ARTFGQIRCY TAPVAAEPFL SGTSSNYVEE
MYYAWLENPK SVHKSWDIFF RNTNAGAPPG TAYQSPLPLS PGSLSAVARA GPLVEAQPNV
DKLVEDHLAV QSLIRAYQIR GHHVAQLDPL GILDADLDSS VPADIISSTD KLGFYGLDES
DLDKVFHLPT TTFIGGQESA LPLREIIRRL EMAYCQHIGV EFMFINDLEQ CQWIRQKFET
PGVMQFTNEE KRTLLARLVR STRFEEFLQR KWSSEKRFGL EGCEVLIPAL KTIIDKSSEN
GVDYVIMGMP HRGRLNVLAN VIRKELEQIF CQFDSKLEAA DEGSGDVKYH LGMYHRRINR
VTDRNITLSL VANPSHLEAA DPVVMGKTKA EQFYCGDTEG KKVMSILLHG DAAFAGQGIV
YETFHLSDLP SYTTHGTVHV VVNNQIGFTT DPRMARSSPY PTDVARVVNA PIFHVNSDDP
EAVMYVCKVA AEWRSTFHKD VVVDLVCYRR NGHNEMDEPM FTQPLMYKQI RKQKPVLQKY
AELLVSQGVV NQPEYEEEIS KYDKICEEAF ARSKDEKILH IKHWLDSPWP GFFTLDGQPR
SMTCPSTGLT EDILTHIGNV ASSVPVEDFT IHGGLSRILK TRGELVKNRT VDWALAEYMA
FGSLLKEGIH IRLSGQDVER GTFSHRHHVL HDQNVDKRTC IPMNHLWPNQ APYTVCNSSL
SEYGVLGFEL GFAMASPNAL VLWEAQFGDF HNTAQCIIDQ FICPGQAKWV RQNGIVLLLP
HGMEGMGPEH SSARPERFLQ MCNDDPDVLP DLKEANFDIN QLYDCNWVVV NCSTPGNFFH
VLRRQILLPF RKPLIIFTPK SLLRHPEARS NFDEMLPGTH FQRVIPEDGP AAQNPGNVKR
LLFCTGKVYY DLTRERKARD MVEQVAITRI EQLSPFPFDL LLQEVQKYPS AELAWCQEEH
KNQGYYDYVK PRLRTTISRA KPVWYAGRDP AAAPATGNKK THLTELQRLL DTAFDLDAFK
NFS
