ODO1_MESAU
ID ODO1_MESAU Reviewed; 180 AA.
AC P86231;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 1.
DT 25-MAY-2022, entry version 34.
DE RecName: Full=2-oxoglutarate dehydrogenase, mitochondrial {ECO:0000250|UniProtKB:Q02218};
DE EC=1.2.4.2 {ECO:0000250|UniProtKB:Q02218};
DE AltName: Full=2-oxoglutarate dehydrogenase complex component E1 {ECO:0000250|UniProtKB:Q02218};
DE Short=OGDC-E1 {ECO:0000250|UniProtKB:Q02218};
DE AltName: Full=Alpha-ketoglutarate dehydrogenase {ECO:0000250|UniProtKB:Q02218};
DE Flags: Fragments;
GN Name=OGDH {ECO:0000250|UniProtKB:Q02218};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=20400973; DOI=10.1038/aja.2010.19;
RA Kameshwari D.B., Bhande S., Sundaram C.S., Kota V., Siva A.B., Shivaji S.;
RT "Glucose-regulated protein precursor (GRP78) and tumor rejection antigen
RT (GP96) are unique to hamster caput epididymal spermatozoa.";
RL Asian J. Androl. 12:344-355(2010).
CC -!- FUNCTION: 2-oxoglutarate dehydrogenase (E1) component of the 2-
CC oxoglutarate dehydrogenase complex (OGDHC), which mediates the
CC decarboxylation of alpha-ketoglutarate. The 2-oxoglutarate
CC dehydrogenase complex catalyzes the overall conversion of 2-
CC oxoglutarate to succinyl-CoA and CO(2). The 2-oxoglutarate
CC dehydrogenase complex is mainly active in the mitochondrion. A fraction
CC of the 2-oxoglutarate dehydrogenase complex also localizes in the
CC 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 matrix
CC {ECO:0000250|UniProtKB:Q02218}. Nucleus {ECO:0000250|UniProtKB:Q02218}.
CC Note=Mainly localizes in the mitochondrion. A small fraction localizes
CC to the nucleus, where the 2-oxoglutarate dehydrogenase complex is
CC required for histone succinylation. {ECO:0000250|UniProtKB:Q02218}.
CC -!- SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase family.
CC {ECO:0000305}.
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DR AlphaFoldDB; P86231; -.
DR SMR; P86231; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
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: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; IEA:InterPro.
DR InterPro; IPR011603; 2oxoglutarate_DH_E1.
DR PANTHER; PTHR23152; PTHR23152; 3.
PE 1: Evidence at protein level;
KW Glycolysis; Mitochondrion; Nucleus; Oxidoreductase; Phosphoprotein;
KW Reference proteome; Thiamine pyrophosphate.
FT CHAIN 1..>180
FT /note="2-oxoglutarate dehydrogenase, mitochondrial"
FT /id="PRO_0000394738"
FT MOD_RES 14
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q60597"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q60597"
FT NON_CONS 10..11
FT /evidence="ECO:0000305"
FT NON_CONS 41..42
FT /evidence="ECO:0000305"
FT NON_CONS 54..55
FT /evidence="ECO:0000305"
FT NON_CONS 64..65
FT /evidence="ECO:0000305"
FT NON_CONS 75..76
FT /evidence="ECO:0000305"
FT NON_CONS 84..85
FT /evidence="ECO:0000305"
FT NON_CONS 94..95
FT /evidence="ECO:0000305"
FT NON_CONS 102..103
FT /evidence="ECO:0000305"
FT NON_CONS 142..143
FT /evidence="ECO:0000305"
FT NON_CONS 149..150
FT /evidence="ECO:0000305"
FT NON_CONS 158..159
FT /evidence="ECO:0000305"
FT NON_TER 180
SQ SEQUENCE 180 AA; 21097 MW; 6C78EA048791E270 CRC64;
MFHLRTCAAK SVHKSWDIFF RNTNAGAPPG TAYQSPLSLS RLGFYGLHES DLDKSTRFEE
FLQRGRLNVL ANVIRYHLGM YHRRSSPYPT DVARICEEAF TRRQILLPFR KPLIVFTPKS
LLRHPEARTS FDEMLPGTHF QRVYYDLTRA KPVWYAGRKT HLTELQRFLD TAFDLDAFKK
