ODO2_TAKRU
ID ODO2_TAKRU Reviewed; 409 AA.
AC Q90512;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial;
DE EC=2.3.1.61 {ECO:0000250|UniProtKB:Q9N0F1};
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; Fragment;
GN Name=dlst;
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8643637; DOI=10.1073/pnas.93.4.1366;
RA Trower M.K., Orton S.M., Purvis I.J., Sanseau P., Riley J.,
RA Christodoulou C., Burt D., See C.G., Elgar G., Sherrington R., Rogaev E.I.,
RA St George-Hyslop P.H., Brenner S., Dykes C.W.;
RT "Conservation of synteny between the genome of the pufferfish (Fugu
RT rubripes) and the region on human chromosome 14 (14q24.3) associated with
RT familial Alzheimer disease (AD3 locus).";
RL Proc. Natl. Acad. Sci. U.S.A. 93:1366-1369(1996).
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:Q9N0F1};
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 -!- 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; U40758; AAC59779.1; -; Genomic_DNA.
DR AlphaFoldDB; Q90512; -.
DR SMR; Q90512; -.
DR PRIDE; Q90512; -.
DR eggNOG; KOG0559; Eukaryota.
DR InParanoid; Q90512; -.
DR UniPathway; UPA00868; UER00840.
DR Proteomes; UP000005226; 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; 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; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW Acyltransferase; Lipoyl; Mitochondrion; Nucleus; Reference proteome;
KW Transferase; Transit peptide; Tricarboxylic acid cycle.
FT TRANSIT <1..36
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 37..409
FT /note="Dihydrolipoyllysine-residue succinyltransferase
FT component of 2-oxoglutarate dehydrogenase complex,
FT mitochondrial"
FT /id="PRO_0000020476"
FT DOMAIN 39..113
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT REGION 121..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..168
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 380
FT /evidence="ECO:0000255"
FT ACT_SITE 384
FT /evidence="ECO:0000255"
FT MOD_RES 79
FT /note="N6-lipoyllysine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT NON_TER 1
SQ SEQUENCE 409 AA; 44112 MW; 5A429FD99DA43873 CRC64;
SSVCRRLIFR TSRPGERASS QNSFHVRYFR TSVVHRDDLV TVKTPAFAES VTEGDVRWEK
AVGDSVTEDE VVCEIETDKT SVQVPSPAAG VIEELLVPDG GKVEGGTPLF KLRKGAAAEA
APSSVTEPVT AAPPPPPPPV SAPTAMPSVP PVPTQALQAK PVPAPTLPEP STLGGRGESR
VKMSRMRLRI AQRLKEAQNT CAMLTTFNEV DMSNIQEMRT LHKDAFLKKH SIKLGFMSAF
VKAAAHALTD QPAVNAVIDG ATNEIVYRDY VDISVAVATP KGLVVPVIRN VETMNFADIE
RTINALGEKA RNNELAVEDM DGGTFTISNG GVFGSLFGTP IINPPQSAIL GMHGIFQRPV
AVDGKAEIRP MMYVALTYDH RLVDGREAVT FLRKIKAAVE DPRALLLDM
