ID   ODO2_PIG                Reviewed;         455 AA.
AC   Q9N0F1;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   24-JAN-2024, entry version 143.
DE   RecName: Full=Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial {ECO:0000250|UniProtKB:P36957};
DE            EC=2.3.1.61 {ECO:0000269|PubMed:10806400};
DE   AltName: Full=2-oxoglutarate dehydrogenase complex component E2;
DE            Short=OGDC-E2;
DE   AltName: Full=Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex;
DE   AltName: Full=E2K;
DE   AltName: Full=E2o;
DE            Short=PE2o;
DE   Flags: Precursor;
GN   Name=DLST {ECO:0000250|UniProtKB:P36957};
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC
RP   ACTIVITY, PATHWAY, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-374; HIS-426;
RP   ASP-430 AND 451-LEU--LEU-453, AND ACTIVE SITE.
RC   TISSUE=Brain cortex, and Heart;
RX   PubMed=10806400; DOI=10.1046/j.1432-1033.2000.01320.x;
RA   Koike K., Suematsu T., Ehara M.;
RT   "Cloning, overexpression and mutagenesis of cDNA encoding dihydrolipoamide
RT   succinyltransferase component of the porcine 2-oxoglutarate dehydrogenase
RT   complex.";
RL   Eur. J. Biochem. 267:3005-3016(2000).
CC   -!- FUNCTION: Dihydrolipoamide succinyltransferase (E2) component of the 2-
CC       oxoglutarate dehydrogenase complex (PubMed:10806400). The 2-
CC       oxoglutarate dehydrogenase complex catalyzes the overall conversion of
CC       2-oxoglutarate to succinyl-CoA and CO(2) (PubMed:10806400). The 2-
CC       oxoglutarate dehydrogenase complex is mainly active in the
CC       mitochondrion (By similarity). 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:P36957,
CC       ECO:0000269|PubMed:10806400}.
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:0000269|PubMed:10806400};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:15215;
CC         Evidence={ECO:0000305|PubMed:10806400};
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   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle.
CC       {ECO:0000269|PubMed:10806400}.
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:0000305|PubMed:10806400}. 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   EMBL; AB035206; BAA95700.1; -; mRNA.
DR   RefSeq; NP_999562.1; NM_214397.1.
DR   AlphaFoldDB; Q9N0F1; -.
DR   SMR; Q9N0F1; -.
DR   STRING; 9823.ENSSSCP00000064766; -.
DR   PaxDb; 9823-ENSSSCP00000002572; -.
DR   PeptideAtlas; Q9N0F1; -.
DR   GeneID; 397690; -.
DR   KEGG; ssc:397690; -.
DR   CTD; 1743; -.
DR   eggNOG; KOG0559; Eukaryota.
DR   HOGENOM; CLU_016733_0_0_1; -.
DR   InParanoid; Q9N0F1; -.
DR   OMA; MKVPSPG; -.
DR   OrthoDB; 672at2759; -.
DR   TreeFam; TF314164; -.
DR   SABIO-RK; Q9N0F1; -.
DR   UniPathway; UPA00223; -.
DR   UniPathway; UPA00868; UER00840.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   Proteomes; UP000694570; Unplaced.
DR   Proteomes; UP000694571; Unplaced.
DR   Proteomes; UP000694720; Unplaced.
DR   Proteomes; UP000694722; Unplaced.
DR   Proteomes; UP000694723; Unplaced.
DR   Proteomes; UP000694724; Unplaced.
DR   Proteomes; UP000694725; Unplaced.
DR   Proteomes; UP000694726; Unplaced.
DR   Proteomes; UP000694727; Unplaced.
DR   Proteomes; UP000694728; 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:0004149; F:dihydrolipoyllysine-residue succinyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0006103; P:2-oxoglutarate metabolic process; IDA: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; IDA:UniProtKB.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; ISS:UniProtKB.
DR   CDD; cd06849; lipoyl_domain; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR   InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
DR   InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   InterPro; IPR006255; SucB.
DR   NCBIfam; TIGR01347; sucB; 1.
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   Pfam; PF00364; Biotin_lipoyl; 1.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
DR   SUPFAM; SSF51230; Single hybrid motif; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS00189; LIPOYL; 1.
DR   Genevisible; Q9N0F1; SS.
PE   1: Evidence at protein level;
KW   Acetylation; Acyltransferase; Direct protein sequencing; Lipoyl;
KW   Mitochondrion; Nucleus; Phosphoprotein; Reference proteome; Transferase;
KW   Transit peptide; Tricarboxylic acid cycle.
FT   TRANSIT         1..68
FT                   /note="Mitochondrion"
FT   CHAIN           69..455
FT                   /note="Dihydrolipoyllysine-residue succinyltransferase
FT                   component of 2-oxoglutarate dehydrogenase complex,
FT                   mitochondrial"
FT                   /id="PRO_0000020474"
FT   DOMAIN          71..145
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT   REGION          153..214
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          221..453
FT                   /note="Catalytic"
FT   COMPBIAS        170..199
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        426
FT                   /evidence="ECO:0000269|PubMed:10806400"
FT   ACT_SITE        430
FT                   /evidence="ECO:0000269|PubMed:10806400"
FT   MOD_RES         82
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D2G2"
FT   MOD_RES         111
FT                   /note="N6-lipoyllysine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT   MOD_RES         155
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D2G2"
FT   MOD_RES         269
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D2G2"
FT   MOD_RES         274
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D2G2"
FT   MOD_RES         275
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D2G2"
FT   MOD_RES         279
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D2G2"
FT   MOD_RES         309
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D2G2"
FT   MUTAGEN         374
FT                   /note="S->A: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:10806400"
FT   MUTAGEN         426
FT                   /note="H->C: 16% of activity."
FT                   /evidence="ECO:0000269|PubMed:10806400"
FT   MUTAGEN         430
FT                   /note="D->A,E,N: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:10806400"
FT   MUTAGEN         451..453
FT                   /note="LLL->AAA,DDD: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:10806400"
SQ   SEQUENCE   455 AA;  48977 MW;  563B5E7455C842FA CRC64;
     MLSRSRCVSR AFSRSLSAFQ KGNCPLGRRS LPGISLCQGP GYPDSRKIVI SNSSVLNVRF
     FRTTAVCKDD VITVKTPAFA ESVTEGDVRW EKAVGDTVAE DEVVCEIETD KTSVQVPSPA
     NGVIEALLVP DGGKVEGGTP LFTLRKTGAA PAKAKPAEAP AAAAPKAEPA VSAVPPPPAA
     SIPTQMPPVP SPPQPLTSKP VSAVKPTAAP PVAEPGAVKG LRAEHREKMN RMRQRIAQRL
     KEAQNTCAML TTFNEIDMSN IQDMRARHKE AFLKKHNLKL GFMSAFVKAS AFALQEQPVV
     NAVIDDTTKE VVYRDYIDIS VAVATPRGLV VPVIRNVETM NYADIERTIS ELGEKARKNE
     LAIEDMDGGT FTISNGGVFG SLFGTPIINP PQSAILGMHA IVDRPVAVGG KVEIRPMMYV
     ALTYDHRLID GREAVTFLRK IKAAVEDPRV LLLDL
//