ID A0A0N5BCC7_STREA Unreviewed; 461 AA.
AC A0A0N5BCC7;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
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};
OS Strongyloides papillosus (Intestinal threadworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Strongyloides.
OX NCBI_TaxID=174720 {ECO:0000313|Proteomes:UP000046392, ECO:0000313|WBParaSite:SPAL_0000367600.1};
RN [1] {ECO:0000313|WBParaSite:SPAL_0000367600.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
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 -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00007317}.
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DR AlphaFoldDB; A0A0N5BCC7; -.
DR STRING; 174720.A0A0N5BCC7; -.
DR WBParaSite; SPAL_0000367600.1; SPAL_0000367600.1; SPAL_0000367600.
DR UniPathway; UPA00868; UER00840.
DR Proteomes; UP000046392; Unplaced.
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-KW.
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 Transferase {ECO:0000256|ARBA:ARBA00023315};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 64..138
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 132..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..170
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 461 AA; 50184 MW; 44E9294591D8F4F4 CRC64;
MSYRSGFTRT LKQISNISLK STRPLSIRTI ALKKNLELSK AIKPIPFNGC TRNIYMSPIF
CSDTVIIEGP AFAESISEGD IRWIKAVGDF VNEDDLVAEI ETDKTSVEVP APRAGTIVKF
LVQDGEKVGP KQKLYELKPG DASQTAAAPK KEEAPAKEQA PVKKEEAAPK SGPKPVTAAP
VKSNAGAIPK SAPVAPRPVS SPMSSVDVSG IPLNKLPAGV TPEQSVSGSR EEFRVKMNRM
RIRTAERLKN SQNENASLTT FNEIDMSNVM EMRSKYQQAF TKKHGIKLGL MSPFVKASAY
ALTNQPIVNA VIDHGEIVYR KFVDISVAVA TPRGLVVPVL RNVETMNYAD IESTLFQLGE
KARDNKLAVE DMEGGTFTIS NGGVYGSLFG TPIINPPQCA ILGMHGIFDK PVAINGKVEI
RPIMTVALTY DHRLIDGREA VTFLKTIKSA VEDPRTMLMN L
//
