ODO2_MESAU
ID ODO2_MESAU Reviewed; 145 AA.
AC P86219;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 1.
DT 25-MAY-2022, entry version 36.
DE RecName: Full=Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial {ECO:0000250|UniProtKB:Q01205};
DE EC=2.3.1.61 {ECO:0000250|UniProtKB:P36957};
DE AltName: Full=2-oxoglutarate dehydrogenase complex component E2 {ECO:0000250|UniProtKB:Q01205};
DE Short=OGDC-E2 {ECO:0000250|UniProtKB:Q01205};
DE AltName: Full=Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex {ECO:0000250|UniProtKB:Q01205};
DE AltName: Full=E2K {ECO:0000250|UniProtKB:Q01205};
DE Flags: Fragments;
GN Name=DLST {ECO:0000250|UniProtKB:Q01205};
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: Dihydrolipoamide succinyltransferase (E2) component of the 2-
CC oxoglutarate dehydrogenase complex (By similarity). The 2-oxoglutarate
CC dehydrogenase complex catalyzes the overall conversion of 2-
CC oxoglutarate to succinyl-CoA and CO(2) (By similarity). The 2-
CC oxoglutarate dehydrogenase complex is mainly active in the
CC mitochondrion. A fraction of the 2-oxoglutarate dehydrogenase complex
CC also localizes in the nucleus and is required for lysine succinylation
CC of histones: associates with KAT2A on chromatin and provides succinyl-
CC CoA to histone succinyltransferase KAT2A (By similarity).
CC {ECO:0000250|UniProtKB:P36957, ECO:0000250|UniProtKB:Q9N0F1}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-N(6)-dihydrolipoyl-L-lysyl-[2-oxoglutarate dehydrogenase
CC complex component E2] + succinyl-CoA = (R)-N(6)-(S(8)-
CC succinyldihydrolipoyl)-L-lysyl-[2-oxoglutarate dehydrogenase complex
CC component E2] + CoA; Xref=Rhea:RHEA:15213, Rhea:RHEA-COMP:10581,
CC Rhea:RHEA-COMP:10582, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292,
CC ChEBI:CHEBI:83100, ChEBI:CHEBI:83120; EC=2.3.1.61;
CC Evidence={ECO:0000250|UniProtKB:P36957};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:15215;
CC Evidence={ECO:0000250|UniProtKB:P36957};
CC -!- COFACTOR:
CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC Evidence={ECO:0000250|UniProtKB:P11179};
CC Note=Binds 1 lipoyl cofactor covalently.
CC {ECO:0000250|UniProtKB:P11179};
CC -!- PATHWAY: Amino-acid degradation; L-lysine degradation via saccharopine
CC pathway; glutaryl-CoA from L-lysine: step 6/6.
CC {ECO:0000250|UniProtKB:Q01205}.
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle.
CC {ECO:0000250|UniProtKB:P36957}.
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:P36957}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:P36957}. Nucleus {ECO:0000250|UniProtKB:P36957}.
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:P36957}.
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {ECO:0000305}.
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DR AlphaFoldDB; P86219; -.
DR SMR; P86219; -.
DR STRING; 10036.XP_005086433.1; -.
DR eggNOG; KOG0559; Eukaryota.
DR UniPathway; UPA00223; -.
DR UniPathway; UPA00868; UER00840.
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:0016746; F:acyltransferase activity; ISS:UniProtKB.
DR GO; GO:0004149; F:dihydrolipoyllysine-residue succinyltransferase activity; ISS:UniProtKB.
DR GO; GO:0006103; P:2-oxoglutarate metabolic process; ISS:UniProtKB.
DR GO; GO:0106077; P:histone succinylation; ISS:UniProtKB.
DR GO; GO:0033512; P:L-lysine catabolic process to acetyl-CoA via saccharopine; IEA:UniProtKB-UniPathway.
DR GO; GO:0006104; P:succinyl-CoA metabolic process; ISS:UniProtKB.
DR GO; GO:0006099; P:tricarboxylic acid cycle; ISS:UniProtKB.
DR Gene3D; 3.30.559.10; -; 2.
DR InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR Pfam; PF00198; 2-oxoacid_dh; 2.
PE 1: Evidence at protein level;
KW Acetylation; Acyltransferase; Lipoyl; Mitochondrion; Nucleus;
KW Phosphoprotein; Reference proteome; Transferase; Tricarboxylic acid cycle.
FT CHAIN <1..145
FT /note="Dihydrolipoyllysine-residue succinyltransferase
FT component of 2-oxoglutarate dehydrogenase complex,
FT mitochondrial"
FT /id="PRO_0000394748"
FT DOMAIN 4..31
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000255"
FT ACT_SITE 119
FT /evidence="ECO:0000250|UniProtKB:Q9N0F1"
FT ACT_SITE 123
FT /evidence="ECO:0000250|UniProtKB:Q9N0F1"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D2G2"
FT MOD_RES 36
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9D2G2"
FT MOD_RES 66
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9D2G2"
FT NON_CONS 21..22
FT /evidence="ECO:0000305"
FT NON_CONS 32..33
FT /evidence="ECO:0000305"
FT NON_CONS 104..105
FT /evidence="ECO:0000305"
FT NON_CONS 132..133
FT /evidence="ECO:0000305"
FT NON_TER 1
SQ SEQUENCE 145 AA; 16122 MW; 32D674B5DD798BBD CRC64;
NDVITVQTPA FAESVTEGDV RVEGGTPLFT LRHNLKLGFM SAFVKASAFA LQEQPVVNAV
IDDATKEVVY RDYIDISVAV ATPRGLVVPV IRNVETMNYA DIERVEVRPM MYVALTYDHR
LIDGREAVTF LRAAVEDPRV LLLDL
