ID   ODO2_RAT                Reviewed;         454 AA.
AC   Q01205; Q5XI35;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   12-APR-2005, sequence version 2.
DT   27-MAR-2024, entry version 170.
DE   RecName: Full=Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial {ECO:0000305};
DE            EC=2.3.1.61 {ECO:0000250|UniProtKB:P36957};
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   Flags: Precursor;
GN   Name=Dlst {ECO:0000312|RGD:1359615};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 3-454, AND PROTEIN SEQUENCE OF 69-83.
RC   TISSUE=Heart;
RX   PubMed=1918017; DOI=10.1016/s0021-9258(18)55164-4;
RA   Nakano K., Matuda S., Yamanaka T., Tsubouchi H., Nakagawa S., Titani K.,
RA   Ohta S., Miyata T.;
RT   "Purification and molecular cloning of succinyltransferase of the rat
RT   alpha-ketoglutarate dehydrogenase complex. Absence of a sequence motif of
RT   the putative E3 and/or E1 binding site.";
RL   J. Biol. Chem. 266:19013-19017(1991).
RN   [3]
RP   PROTEIN SEQUENCE OF 69-89; 135-145; 262-308 AND 314-326, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY.
RC   STRAIN=Sprague-Dawley; TISSUE=Hippocampus, and Spinal cord;
RA   Lubec G., Chen W.-Q., Afjehi-Sadat L., Diao W.;
RL   Submitted (JAN-2009) to UniProtKB.
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   -!- 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   EMBL; BC083858; AAH83858.1; -; mRNA.
DR   EMBL; D90401; BAA14397.1; -; mRNA.
DR   PIR; A41015; A41015.
DR   RefSeq; NP_001006982.2; NM_001006981.2.
DR   AlphaFoldDB; Q01205; -.
DR   SMR; Q01205; -.
DR   BioGRID; 256153; 3.
DR   IntAct; Q01205; 2.
DR   MINT; Q01205; -.
DR   STRING; 10116.ENSRNOP00000007298; -.
DR   GlyGen; Q01205; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q01205; -.
DR   PhosphoSitePlus; Q01205; -.
DR   jPOST; Q01205; -.
DR   PaxDb; 10116-ENSRNOP00000007298; -.
DR   GeneID; 299201; -.
DR   KEGG; rno:299201; -.
DR   UCSC; RGD:1359615; rat.
DR   AGR; RGD:1359615; -.
DR   CTD; 1743; -.
DR   RGD; 1359615; Dlst.
DR   eggNOG; KOG0559; Eukaryota.
DR   InParanoid; Q01205; -.
DR   OrthoDB; 672at2759; -.
DR   PhylomeDB; Q01205; -.
DR   BRENDA; 2.3.1.61; 5301.
DR   Reactome; R-RNO-389661; Glyoxylate metabolism and glycine degradation.
DR   Reactome; R-RNO-71064; Lysine catabolism.
DR   Reactome; R-RNO-71403; Citric acid cycle (TCA cycle).
DR   SABIO-RK; Q01205; -.
DR   UniPathway; UPA00223; -.
DR   UniPathway; UPA00868; UER00840.
DR   PRO; PR:Q01205; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; ISO:RGD.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0045252; C:oxoglutarate dehydrogenase complex; IDA:RGD.
DR   GO; GO:0016746; F:acyltransferase activity; ISO:RGD.
DR   GO; GO:0004149; F:dihydrolipoyllysine-residue succinyltransferase activity; IDA:RGD.
DR   GO; GO:0031072; F:heat shock protein binding; IPI:RGD.
DR   GO; GO:0051087; F:protein-folding chaperone binding; IPI:RGD.
DR   GO; GO:0006103; P:2-oxoglutarate metabolic process; IDA:RGD.
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:0006734; P:NADH metabolic process; IDA:RGD.
DR   GO; GO:0006104; P:succinyl-CoA metabolic process; ISS: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.
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                   /evidence="ECO:0000269|PubMed:1918017, ECO:0000269|Ref.3"
FT   CHAIN           69..454
FT                   /note="Dihydrolipoyllysine-residue succinyltransferase
FT                   component of 2-oxoglutarate dehydrogenase complex,
FT                   mitochondrial"
FT                   /id="PRO_0000020475"
FT   DOMAIN          71..145
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT   REGION          148..227
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        169..198
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        425
FT                   /evidence="ECO:0000250|UniProtKB:Q9N0F1"
FT   ACT_SITE        429
FT                   /evidence="ECO:0000250|UniProtKB:Q9N0F1"
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         268
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D2G2"
FT   MOD_RES         273
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         278
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D2G2"
FT   MOD_RES         308
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D2G2"
FT   CONFLICT        13
FT                   /note="S -> M (in Ref. 2; BAA14397)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        52..54
FT                   /note="NSS -> TVA (in Ref. 2; BAA14397)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        164
FT                   /note="Y -> H (in Ref. 2; BAA14397)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        281
FT                   /note="F -> L (in Ref. 2; BAA14397)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        448
FT                   /note="R -> A (in Ref. 2; BAA14397)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   454 AA;  48925 MW;  2818F530F4B7C683 CRC64;
     MLSRSRCVSR AFSRSLSAFQ KGNCPLGRRS LPGVSLCQGP GYPDSRKMVI NNSSVFSVRF
     FQTTAVCKND VITVQTPAFA ESVTEGDVRW EKAVGDAVAE DEVVCEIETD KTSVQVPSPA
     NGIIEALLVP DGGKVEGGTP LFTLRKTGAA PAKAKPAEAP ATAYKAAPEA PAAPPPPVAP
     VPTQMPPVPS PSQPPSSKPV SAIKPTAAPP LAEAGAAKGL RSEHREKMNR MRQRIAQRLK
     EAQNTCAMLT TFNEVDMSNI QEMRARHKDA FLKKHNLKLG FMSAFVKASA FALQEQPVVN
     AVIDDATKEV VYRDYIDISV AVATPRGLVV PVIRNVETMN YADIERTINE LGEKARKNEL
     AIEDMDGGTF TISNGGVFGS LFGTPIINPP QSAILGMHGI FDRPVAVGGK VEVRPMMYVA
     LTYDHRLIDG REAVTFLRKI KAAVEDPRVL LLDL
//