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
//
