ID A0A0D9QN15_PLAFR Unreviewed; 419 AA.
AC A0A0D9QN15;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=dihydrolipoyllysine-residue succinyltransferase {ECO:0000256|ARBA:ARBA00012945};
DE EC=2.3.1.61 {ECO:0000256|ARBA:ARBA00012945};
GN ORFNames=AK88_02114 {ECO:0000313|EMBL:KJP88167.1};
OS Plasmodium fragile.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX NCBI_TaxID=5857 {ECO:0000313|EMBL:KJP88167.1, ECO:0000313|Proteomes:UP000054561};
RN [1] {ECO:0000313|EMBL:KJP88167.1, ECO:0000313|Proteomes:UP000054561}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=nilgiri {ECO:0000313|Proteomes:UP000054561};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Neafsey D., Duraisingh M., Young S.K., Zeng Q., Gargeya S., Abouelleil A.,
RA Alvarado L., Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., Pearson M.,
RA Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Plasmodium fragile nilgiri.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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 EMBL; KQ001664; KJP88167.1; -; Genomic_DNA.
DR RefSeq; XP_012335171.1; XM_012479748.1.
DR AlphaFoldDB; A0A0D9QN15; -.
DR EnsemblProtists; KJP88167; KJP88167; AK88_02114.
DR GeneID; 24267428; -.
DR VEuPathDB; PlasmoDB:AK88_02114; -.
DR OMA; MKVPSPG; -.
DR OrthoDB; 672at2759; -.
DR UniPathway; UPA00868; UER00840.
DR Proteomes; UP000054561; Unassembled WGS sequence.
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; 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.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Transferase {ECO:0000256|ARBA:ARBA00023315};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 44..119
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 126..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..170
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 419 AA; 47021 MW; 611CF432261BD501 CRC64;
MTQNLVLRLN KPLFYNAKGI SRILNLESKQ CVKCHAKFKR CFSIETIKVP RLGDSITEGT
ISEWKKKVGD YVKVDETITI IDTDKVSVDI NSQFSGEISN IFAEAGEIVL VDAPLCEIDT
SVEAPAHISE EKDDVAQSKA ANANEETGTE KENDEDDHNS AHKESKRGLS ENNNTKMLYE
SVSERTETRV RMLPIRKRIA ERLKESQNTC ALLTTFNECD MSKVIALRSE LKDIFQKKYG
CKLGFVSLFM HASTLALKKM PQVNAYIDND EIVYRNYVDI SVAVATPNGL TVPIIRDCQN
KKLPELEQAL SELATKARNN KLSLEDFMGG TFTISNGGVF GSMLSTPIVN MPQSAILGMH
TIKDRAVVVN NQIVIRPIMY LALTYDHRLL DGRDAVQFLS AIKEYIENPN LMLIDWLTD
//
