ODO2_BOVIN
ID ODO2_BOVIN Reviewed; 455 AA.
AC P11179; Q0V8L1;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 25-MAY-2022, entry version 132.
DE RecName: Full=Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial;
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;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP PROTEIN SEQUENCE OF 107-122, AND LIPOYLATION AT LYS-111.
RC TISSUE=Kidney;
RX PubMed=3115829; DOI=10.1016/0014-5793(87)80221-1;
RA Bradford A.P., Aitken A., Beg F., Cook K.G., Yeaman S.J.;
RT "Amino acid sequence surrounding the lipoic acid cofactor of bovine kidney
RT 2-oxoglutarate dehydrogenase complex.";
RL FEBS Lett. 222:211-214(1987).
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=(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: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:0000269|PubMed:3115829};
CC Note=Binds 1 lipoyl cofactor covalently. {ECO:0000269|PubMed:3115829};
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) 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: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; BT026207; ABG67046.1; -; mRNA.
DR PIR; S00123; S00123.
DR RefSeq; NP_001068750.1; NM_001075282.1.
DR AlphaFoldDB; P11179; -.
DR SMR; P11179; -.
DR IntAct; P11179; 1.
DR STRING; 9913.ENSBTAP00000008473; -.
DR PeptideAtlas; P11179; -.
DR PRIDE; P11179; -.
DR GeneID; 506888; -.
DR KEGG; bta:506888; -.
DR CTD; 1743; -.
DR eggNOG; KOG0559; Eukaryota.
DR InParanoid; P11179; -.
DR OrthoDB; 850255at2759; -.
DR UniPathway; UPA00223; -.
DR UniPathway; UPA00868; UER00840.
DR Proteomes; UP000009136; 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; -; 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 /evidence="ECO:0000250"
FT CHAIN 69..455
FT /note="Dihydrolipoyllysine-residue succinyltransferase
FT component of 2-oxoglutarate dehydrogenase complex,
FT mitochondrial"
FT /id="PRO_0000162252"
FT DOMAIN 71..145
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT REGION 155..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..195
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 426
FT /evidence="ECO:0000250|UniProtKB:Q9N0F1"
FT ACT_SITE 430
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 ECO:0000269|PubMed:3115829"
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"
SQ SEQUENCE 455 AA; 48973 MW; DB2124A4D06C389B CRC64;
MLSRSRCASR AFSRSLSAFQ KGNCPLVRRS LPGISLCQGP GYPDSRKTVI NSSNIFSVRF
FRTTAVCKDD VITVKTPAFA ESVTEGDVRW EKAVGDTVAE DEVVCEIETD KTSVQVPSPA
NGVIEALLVP DGGKVEGGTP LFTLRKTGAA PAKAKPAAAP AAAAPKAEPT VSAVPPPPAA
PIPTQMPPVP SPSQPLTSKP VSAVKPTAAP PRAEAGAGVG LRSEHREKMN RMRQRIAQRL
KEAQNTCAML TTFNEIDMSN IQEMRARHKD AFLKKHNLKL GFMSAFVKAS AFALQEQPVV
NAVIDDATKE VVYRDYIDIS VAVATPRGLV VPVIRNVETM NYADIERTIS ELGEKARKNE
LAIEDMDGGT FTISNGGVFG SLFGTPIINP PQSAILGMHA IVDRPVVIGG KVEVRPMMYV
ALTYDHRLID GREAVTFLRK IKAAVEDPRV LLLDL
