ODP2_CAEEL
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 03-AUG-2022, entry version 170.
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=(R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + acetyl-CoA = (R)-
CC N(6)-(S(8)-acetyldihydrolipoyl)-L-lysyl-[protein] + CoA;
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}.
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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; 59.
DR DIP; DIP-24773N; -.
DR IntAct; Q19749; 23.
DR STRING; 6239.F23B12.5; -.
DR World-2DPAGE; 0020:Q19749; -.
DR EPD; Q19749; -.
DR PaxDb; Q19749; -.
DR PeptideAtlas; Q19749; -.
DR EnsemblMetazoa; F23B12.5.1; F23B12.5.1; WBGene00009082.
DR GeneID; 179945; -.
DR UCSC; F23B12.5; c. elegans.
DR CTD; 179945; -.
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; 747232at2759; -.
DR PhylomeDB; Q19749; -.
DR Reactome; R-CEL-204174; Regulation of pyruvate dehydrogenase (PDH) complex.
DR Reactome; R-CEL-389661; Glyoxylate metabolism and glycine degradation.
DR Reactome; R-CEL-5362517; Signaling by Retinoic Acid.
DR Reactome; R-CEL-70268; Pyruvate metabolism.
DR SignaLink; Q19749; -.
DR PRO; PR:Q19749; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00009082; Expressed in adult organism and 4 other 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 Gene3D; 3.30.559.10; -; 1.
DR Gene3D; 4.10.320.10; -; 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 PANTHER; PTHR23151; PTHR23151; 1.
DR Pfam; PF00198; 2-oxoacid_dh; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF02817; E3_binding; 1.
DR SUPFAM; SSF47005; SSF47005; 1.
DR SUPFAM; SSF51230; SSF51230; 1.
DR TIGRFAMs; TIGR01349; PDHac_trf_mito; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00189; LIPOYL; 1.
DR PROSITE; PS51826; PSBD; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Direct protein sequencing; Glycolysis; Lipoyl;
KW Mitochondrion; 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
