ID A0A2Y9NBK4_DELLE Unreviewed; 455 AA.
AC A0A2Y9NBK4;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2021, sequence version 2.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial {ECO:0000256|ARBA:ARBA00020294};
DE EC=2.3.1.61 {ECO:0000256|ARBA:ARBA00012945};
DE AltName: Full=E2K {ECO:0000256|ARBA:ARBA00031331};
GN Name=DLST {ECO:0000313|RefSeq:XP_022432249.2};
OS Delphinapterus leucas (Beluga whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Delphinapterus.
OX NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022432249.2};
RN [1] {ECO:0000313|RefSeq:XP_022432249.2}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022432249.2};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00043722};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:15215;
CC Evidence={ECO:0000256|ARBA:ARBA00043722};
CC -!- COFACTOR:
CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC Evidence={ECO:0000256|ARBA:ARBA00001938};
CC -!- PATHWAY: Amino-acid degradation; L-lysine degradation via saccharopine
CC pathway; glutaryl-CoA from L-lysine: step 6/6.
CC {ECO:0000256|ARBA:ARBA00005145}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000256|ARBA:ARBA00004305}.
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00007317}.
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DR RefSeq; XP_022432249.2; XM_022576541.2.
DR STRING; 9749.A0A2Y9NBK4; -.
DR KEGG; dle:111176248; -.
DR InParanoid; A0A2Y9NBK4; -.
DR OrthoDB; 672at2759; -.
DR UniPathway; UPA00223; -.
DR UniPathway; UPA00868; UER00840.
DR Proteomes; UP000248483; Unplaced.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0045252; C:oxoglutarate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0004149; F:dihydrolipoyllysine-residue succinyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0033512; P:L-lysine catabolic process to acetyl-CoA via saccharopine; IEA:UniProtKB-UniPathway.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
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 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823};
KW Reference proteome {ECO:0000313|Proteomes:UP000248483};
KW Transferase {ECO:0000256|ARBA:ARBA00023315};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 71..145
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 153..232
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"
SQ SEQUENCE 455 AA; 49055 MW; C914C15BBC8A2B6E CRC64;
MLSRSRFLSR AFSRSVSAFQ KGNCPLGRRS LPGISLCQGP GYPDSRKTVI NSGSVFIVRF
FRTTAVCKDD VITVKTPAFA ESVTEGDVRW EKAVGDTVAE DEVVCEIETD KTSVQVPSPA
NGMIEALLVP DGGKVEGGTP LFTLRKTGAV PAKARPAEAP AAAAPKAEPA ASAVPPPPAA
SIPTQMPPVP SPSQPLTSKP VSAVKPAAAP PVAEPGAGTG LRSEHREKMN RMRQRIAQRL
KEAQNTCAML TTFNEIDMSN IQEMRSRHKD AFLKKHNLKL GFMSAFVKAS AFALQEQPVV
NAVIDDTTKE VVYRDYIDIS VAVATPRGLV VPVIRNVETM NYGDIERTIS ELGEKARKNE
LAIEDMDGGT FTISNGGXFG SLFGTPIINP PQSAILGMHA IFDRPVVVGG KVEVRPMMYV
ALTYDHRLID GREAVTFLRK IKAAVEDPRV LLLDL
//
