ID   A0A183T1F4_SCHSO        Unreviewed;       471 AA.
AC   A0A183T1F4;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   22-FEB-2023, entry version 27.
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=SSLN_LOCUS10302 {ECO:0000313|EMBL:VDL96687.1};
OS   Schistocephalus solidus (Tapeworm).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC   Eucestoda; Diphyllobothriidea; Diphyllobothriidae; Schistocephalus.
OX   NCBI_TaxID=70667 {ECO:0000313|Proteomes:UP000050788, ECO:0000313|WBParaSite:SSLN_0001070101-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:SSLN_0001070101-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (JUN-2016) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDL96687.1, ECO:0000313|Proteomes:UP000275846}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NST_G2 {ECO:0000313|EMBL:VDL96687.1,
RC   ECO:0000313|Proteomes:UP000275846};
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|RuleBase:RU003423};
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00007317, ECO:0000256|RuleBase:RU003423}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; UYSU01035788; VDL96687.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A183T1F4; -.
DR   STRING; 70667.A0A183T1F4; -.
DR   WBParaSite; SSLN_0001070101-mRNA-1; SSLN_0001070101-mRNA-1; SSLN_0001070101.
DR   Proteomes; UP000050788; Unplaced.
DR   Proteomes; UP000275846; 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:SF9; PYRUVATE DEHYDROGENASE PROTEIN X COMPONENT, MITOCHONDRIAL; 1.
DR   Pfam; PF00198; 2-oxoacid_dh; 2.
DR   Pfam; PF00364; Biotin_lipoyl; 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:UP000275846};
KW   Transferase {ECO:0000256|RuleBase:RU003423};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          1..74
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          129..167
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
FT   REGION          95..128
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        102..125
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   471 AA;  49081 MW;  ED6277E7A86E63C4 CRC64;
     MPSLSPTMES GTIVKWHKKE GDEIASGDVL CDVQTDKAVV SMETEEEGVM AKIIKEVGTT
     NIVQETIAII ATADEDWKEV AANADAFLAS LGGAASPTAA APPTVSAPPT AAAPSEPPPV
     KPSEGKQLPL GPAVRLLLSS FGLTADQIPG TGPHGGQVLK GDVLNYVASK GLQKLPPSQP
     AAAPVASQPS PAVQAGAGFV DVPVSSMRAT IAKRLSESKA TIPHTYTRTK VRVDRLFALQ
     EAINKVAAPN KISVNDLIVK ACAFGLRQSL AVQGVFFTLA SSPPPLLQLV PDMNGISNPS
     GDSLQRLVNV DICVAVSTPS GLITPIVPSA DTRPISGIST LVKELAAKAR DNKLQPHEFT
     GGSFTISNLG MFGIRDFTAI INPPQVAILA VGGGMKSMTA SKVPDQGLES LTELTLTLST
     DARFVDEAMA AQFLRHVKRY LEVDPEALFA DDPDLTTATD SSADELAMMA L
//