ID   ODP2_CAEEL              Reviewed;         507 AA.
AC   Q19749;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 179.
DE   RecName: Full=Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial;
DE            EC=2.3.1.12;
DE   AltName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex;
DE   AltName: Full=Pyruvate dehydrogenase complex component E2;
DE            Short=PDC-E2;
DE            Short=PDCE2;
DE   Flags: Precursor;
GN   Name=dlat-1 {ECO:0000312|WormBase:F23B12.5};
GN   ORFNames=F23B12.5 {ECO:0000312|WormBase:F23B12.5};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1] {ECO:0000312|EMBL:CAB01163.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [2] {ECO:0000305, ECO:0000312|EMBL:CAB01163.1}
RP   PROTEIN SEQUENCE OF 249-260; 334-350; 393-407 AND 482-493, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RA   Bienvenut W.V.;
RL   Submitted (MAR-2006) to UniProtKB.
CC   -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
CC       conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple
CC       copies of three enzymatic components: pyruvate dehydrogenase (E1),
CC       dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase
CC       (E3). {ECO:0000305}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] = CoA
CC         + N(6)-[(R)-S(8)-acetyldihydrolipoyl]-L-lysyl-[protein];
CC         Xref=Rhea:RHEA:17017, Rhea:RHEA-COMP:10475, Rhea:RHEA-COMP:10478,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:83100,
CC         ChEBI:CHEBI:83111; EC=2.3.1.12; Evidence={ECO:0000305};
CC   -!- COFACTOR:
CC       Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088; Evidence={ECO:0000250};
CC       Note=Binds 1 lipoyl cofactor covalently. {ECO:0000250};
CC   -!- INTERACTION:
CC       Q19749; Q9U9Y8: lit-1; NbExp=2; IntAct=EBI-320763, EBI-318513;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000255}.
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; Z77659; CAB01163.1; -; Genomic_DNA.
DR   PIR; T21287; T21287.
DR   RefSeq; NP_506579.1; NM_074178.6.
DR   AlphaFoldDB; Q19749; -.
DR   SMR; Q19749; -.
DR   BioGRID; 44949; 61.
DR   DIP; DIP-24773N; -.
DR   IntAct; Q19749; 23.
DR   STRING; 6239.F23B12.5.1; -.
DR   EPD; Q19749; -.
DR   PaxDb; 6239-F23B12-5; -.
DR   PeptideAtlas; Q19749; -.
DR   EnsemblMetazoa; F23B12.5.1; F23B12.5.1; WBGene00009082.
DR   UCSC; F23B12.5; c. elegans.
DR   AGR; WB:WBGene00009082; -.
DR   WormBase; F23B12.5; CE09597; WBGene00009082; dlat-1.
DR   eggNOG; KOG0557; Eukaryota.
DR   GeneTree; ENSGT00940000154943; -.
DR   HOGENOM; CLU_016733_10_2_1; -.
DR   InParanoid; Q19749; -.
DR   OMA; TMEFESF; -.
DR   OrthoDB; 5483022at2759; -.
DR   PhylomeDB; Q19749; -.
DR   SignaLink; Q19749; -.
DR   PRO; PR:Q19749; -.
DR   Proteomes; UP000001940; Chromosome V.
DR   Bgee; WBGene00009082; Expressed in adult organism and 4 other cell types or tissues.
DR   GO; GO:0005967; C:mitochondrial pyruvate dehydrogenase complex; IBA:GO_Central.
DR   GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IBA:GO_Central.
DR   GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IBA:GO_Central.
DR   GO; GO:0006096; P:glycolytic process; 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   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; 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; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS00189; LIPOYL; 1.
DR   PROSITE; PS51826; PSBD; 1.
DR   World-2DPAGE; 0020:Q19749; -.
PE   1: Evidence at protein level;
KW   Acyltransferase; Direct protein sequencing; Lipoyl; Mitochondrion;
KW   Reference proteome; Repeat; Transferase; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..507
FT                   /note="Dihydrolipoyllysine-residue acetyltransferase
FT                   component of pyruvate dehydrogenase complex, mitochondrial"
FT                   /id="PRO_0000244484"
FT   DOMAIN          77..153
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT   DOMAIN          221..258
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01170"
FT   REGION          168..223
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          248..270
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        480
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        484
FT                   /evidence="ECO:0000255"
FT   MOD_RES         118
FT                   /note="N6-lipoyllysine"
FT                   /evidence="ECO:0000250, ECO:0000255|PROSITE-
FT                   ProRule:PRU01066"
SQ   SEQUENCE   507 AA;  53467 MW;  2C546DA3828C5B09 CRC64;
     MSKFPVPLRT IGGLRPSTTA AISAANIGFT QSSRALSTGA AAKSSGLVGQ VARQYPNAAA
     FSIKQVRLYS SGNLPKHNRV ALPALSPTME LGTVVSWQKK EGDQLSEGDL LCEIETDKAT
     MGFETPEEGY LAKILIQEGS KDVPIGKLLC IIVDNEADVA AFKDFKDDGA SSGGSAPAAE
     KAPEPAKPAA SSQPSPPAQM YQAPSVPKSA PIPHSSSGRV SASPFAKKLA AENGLDLSGV
     SGSGPGGRIL ASDLSQAPAK GATSTTTQAV SGQDYTDIPL SNMRKTIAKR LTESKSTIPH
     YYLTSEIQLD TLLQVREKLN GLLAKGTSGQ ATKISINDFI IKASALACQR VPEANSYWMD
     SFIRENHHVD VSVAVSTPAG LITPIIFNAH AKGLATIASE IVELAQRARE GKLQPHEFQG
     GTFTVSNLGM FGSVSDFTAI INPPQSCILA IGGASDKLVP DEAEGYKKIK TMKVTLSCDH
     RTVDGAVGAV WLRHFKEFLE KPHTMLL
//