ODO2_PIG
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 03-AUG-2022, entry version 137.
DE RecName: Full=Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial;
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;
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=(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: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) 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: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.ENSSSCP00000002572; -.
DR PaxDb; Q9N0F1; -.
DR PeptideAtlas; Q9N0F1; -.
DR PRIDE; 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; 850255at2759; -.
DR TreeFam; TF314164; -.
DR SABIO-RK; Q9N0F1; -.
DR UniPathway; UPA00223; -.
DR UniPathway; UPA00868; UER00840.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR Genevisible; Q9N0F1; SS.
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 Gene3D; 3.30.559.10; -; 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 Pfam; PF00198; 2-oxoacid_dh; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR SUPFAM; SSF51230; SSF51230; 1.
DR TIGRFAMs; TIGR01347; sucB; 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 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
