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Database: UniProt
Entry: A0A183KHD3_9TREM
LinkDB: A0A183KHD3_9TREM
Original site: A0A183KHD3_9TREM 
ID   A0A183KHD3_9TREM        Unreviewed;       308 AA.
AC   A0A183KHD3;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU003423};
DE            EC=2.3.1.- {ECO:0000256|RuleBase:RU003423};
GN   ORFNames=SCUD_LOCUS14433 {ECO:0000313|EMBL:VDP56402.1};
OS   Schistosoma curassoni.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX   NCBI_TaxID=6186 {ECO:0000313|Proteomes:UP000050789, ECO:0000313|WBParaSite:SCUD_0001443601-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:SCUD_0001443601-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (JUN-2016) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDP56402.1, ECO:0000313|Proteomes:UP000279833}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Dakar {ECO:0000313|EMBL:VDP56402.1}, and Dakar, Senegal
RC   {ECO:0000313|Proteomes:UP000279833};
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC         Evidence={ECO:0000256|ARBA:ARBA00001938,
CC         ECO:0000256|RuleBase:RU003423};
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00007317, ECO:0000256|RuleBase:RU003423}.
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DR   EMBL; UZAK01036710; VDP56402.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A183KHD3; -.
DR   STRING; 6186.A0A183KHD3; -.
DR   WBParaSite; SCUD_0001443601-mRNA-1; SCUD_0001443601-mRNA-1; SCUD_0001443601.
DR   Proteomes; UP000050789; Unplaced.
DR   Proteomes; UP000279833; Unassembled WGS sequence.
DR   GO; GO:0045254; C:pyruvate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IEA:InterPro.
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   Gene3D; 4.10.320.10; E3-binding 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; IPR045257; E2/Pdx1.
DR   InterPro; IPR036625; E3-bd_dom_sf.
DR   InterPro; IPR004167; PSBD.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   PANTHER; PTHR23151; DIHYDROLIPOAMIDE ACETYL/SUCCINYL-TRANSFERASE-RELATED; 1.
DR   PANTHER; PTHR23151:SF90; DIHYDROLIPOYLLYSINE-RESIDUE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX, MITOCHONDRIAL; 1.
DR   Pfam; PF00198; 2-oxoacid_dh; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF02817; E3_binding; 1.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
DR   SUPFAM; SSF47005; Peripheral subunit-binding domain of 2-oxo acid dehydrogenase complex; 1.
DR   SUPFAM; SSF51230; Single hybrid motif; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS00189; LIPOYL; 1.
DR   PROSITE; PS51826; PSBD; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU003423};
KW   Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW   Reference proteome {ECO:0000313|Proteomes:UP000279833};
KW   Transferase {ECO:0000256|RuleBase:RU003423};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          1..65
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          127..164
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
FT   REGION          82..124
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        92..117
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   308 AA;  33030 MW;  06E44AF1551E6C1A CRC64;
     METGTVVSWA KNEGDEVSEG DLLAEIETDK ATMSFDANES GYLAKILAPA GSKDIPVGTA
     LCIIVQDESA VPAFKDYVTG PTEQVSTPKT EVPKPQVPPA AAPQPSPATP KPITPTPKAP
     ATGERAVVSP FARRLAAEKG LDLSNVVGTG MYGMIRSTDL NLESIDQKAS TMTGGPMLNY
     GKFEDINVSN MRSVIAKRLT ESKQTIPHYY LTMDIQVDEI LEIRSKINSN LSNLNDSKSD
     EPVPKISLND ILIKAASLTC LKVPECNSSW HGDFIRQYHT VDVSVAVAIP SGLITPIIFS
     ADTKVTKI
//
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