ID   A0A075AII8_9TREM        Unreviewed;       427 AA.
AC   A0A075AII8;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=dihydrolipoyllysine-residue acetyltransferase {ECO:0000256|ARBA:ARBA00013114};
DE            EC=2.3.1.12 {ECO:0000256|ARBA:ARBA00013114};
DE   AltName: Full=Pyruvate dehydrogenase complex component E2 {ECO:0000256|ARBA:ARBA00032943};
GN   ORFNames=T265_02080 {ECO:0000313|EMBL:KER31709.1};
OS   Opisthorchis viverrini.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Opisthorchiida; Opisthorchiata; Opisthorchiidae; Opisthorchis.
OX   NCBI_TaxID=6198 {ECO:0000313|EMBL:KER31709.1, ECO:0000313|Proteomes:UP000054324};
RN   [1] {ECO:0000313|EMBL:KER31709.1, ECO:0000313|Proteomes:UP000054324}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Young N.D., Nagarajan N., Lin S.J., Korhonen P.K., Jex A.R., Hall R.S.,
RA   Safavi-Hemami H., Kaewkong W., Bertrand D., Gao S., Seet Q., Wongkham S.,
RA   Teh B.T., Wongkham C., Intapan P.M., Maleewong W., Yang X., Hu M., Wang Z.,
RA   Hofmann A., Sternberg P.W., Tan P., Wang J., Gasser R.B.;
RT   "Opisthorchis viverrini - life in the bile duct.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC         Evidence={ECO:0000256|ARBA:ARBA00001938};
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00007317}.
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DR   EMBL; KL596642; KER31709.1; -; Genomic_DNA.
DR   RefSeq; XP_009164503.1; XM_009166239.1.
DR   AlphaFoldDB; A0A075AII8; -.
DR   STRING; 6198.A0A075AII8; -.
DR   GeneID; 20316268; -.
DR   KEGG; ovi:T265_02080; -.
DR   CTD; 20316268; -.
DR   OrthoDB; 5483022at2759; -.
DR   Proteomes; UP000054324; Unassembled WGS sequence.
DR   GO; GO:0045254; C:pyruvate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:UniProtKB-EC.
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; 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; IPR006257; LAT1.
DR   InterPro; IPR004167; PSBD.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   NCBIfam; TIGR01349; PDHac_trf_mito; 1.
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; PS51826; PSBD; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000054324}.
FT   DOMAIN          137..176
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
FT   REGION          98..133
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        102..126
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   427 AA;  45414 MW;  D8A8C8A7134809BE CRC64;
     MRVMRYQVAA QIILLQVNEG DLLAEIETDK ATMSFDANDS GILAKILVPS GTRDIPVGTV
     GSIVMILLPF QPLCIIVPDP DSVAAFKEYV ASAAPSTPAA KAEPAPHAPP ATPAPPTAPT
     PVPTLRTPKP ATGDRVFISP LARRLAAEQG IDINQLSGLG TGIRGMVRAA DLANARPSTA
     DVSASTAMAG SFVDIPTSGL RAVIASRLTE SNQTIPHYYL TTDIIMDDVL EFRQDVNAKL
     AKRVAKAEDA VKVTVNDIIV KAIAVTCRKV PECNSSWQGD FIRQFNTVDV NVAVATSQGL
     ITPIVYGADS KGLVEINQEV RALAAKAKEN KLQLHEFQGG TFTVSNLGMF GISSFCAIIN
     PPQACLLAVG NTQQQIFPDE TTSSGFRKRQ VMSVTLCCDH RVVDGAVGAQ WLAEFKSLLE
     NPALMLV
//