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   24-JAN-2024, entry version 38.
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=N(6)-[(R)-dihydrolipoyl]-L-lysyl-[2-oxoglutarate dehydrogenase
CC         complex component E2] + succinyl-CoA = CoA + N(6)-[(R)-S(8)-
CC         succinyldihydrolipoyl]-L-lysyl-[2-oxoglutarate dehydrogenase complex
CC         component E2]; Xref=Rhea:RHEA:15213, Rhea:RHEA-COMP:10581, Rhea:RHEA-
CC         COMP:10582, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292, ChEBI:CHEBI:83100,
CC         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), DLD (dihydrolipoamide dehydrogenase; E3) and
CC       the assembly factor KGD4 (By similarity). It contains multiple copies
CC       of the three enzymatic components (E1, E2 and E3). In the nucleus, the
CC       2-oxoglutarate dehydrogenase complex associates with KAT2A. Interacts
CC       with ABHD11; this interaction maintains the functional lipoylation of
CC       the 2-oxoglutarate dehydrogenase complex (By similarity).
CC       {ECO:0000250|UniProtKB:P36957, ECO:0000250|UniProtKB:Q9D2G2}.
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.ENSMAUP00000001145; -.
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; Chloramphenicol acetyltransferase-like domain; 2.
DR   InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   PANTHER; PTHR43416:SF5; DIHYDROLIPOYLLYSINE-RESIDUE SUCCINYLTRANSFERASE COMPONENT OF 2-OXOGLUTARATE DEHYDROGENASE COMPLEX, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43416; DIHYDROLIPOYLLYSINE-RESIDUE SUCCINYLTRANSFERASE COMPONENT OF 2-OXOGLUTARATE DEHYDROGENASE COMPLEX, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF00198; 2-oxoacid_dh; 1.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
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
//