ID S6D6E8_ACEPA Unreviewed; 414 AA.
AC S6D6E8;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU361137};
DE EC=2.3.1.12 {ECO:0000256|RuleBase:RU361137};
GN Name=pdhC {ECO:0000313|EMBL:CCT60768.1};
GN ORFNames=APA386B_2736 {ECO:0000313|EMBL:CCT60768.1};
OS Acetobacter pasteurianus 386B.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acetobacter.
OX NCBI_TaxID=1266844 {ECO:0000313|EMBL:CCT60768.1, ECO:0000313|Proteomes:UP000015386};
RN [1] {ECO:0000313|EMBL:CCT60768.1, ECO:0000313|Proteomes:UP000015386}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=386B {ECO:0000313|EMBL:CCT60768.1};
RX PubMed=23902333;
RA Illeghems K., De Vuyst L., Weckx S.;
RT "Complete genome sequence and comparative analysis of Acetobacter
RT pasteurianus 386B, a strain well-adapted to the cocoa bean fermentation
RT ecosystem.";
RL BMC Genomics 14:526-526(2013).
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:0000256|ARBA:ARBA00025211}.
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;
CC Evidence={ECO:0000256|ARBA:ARBA00043782,
CC ECO:0000256|RuleBase:RU361137};
CC -!- COFACTOR:
CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC Evidence={ECO:0000256|RuleBase:RU361137};
CC Note=Binds 1 lipoyl cofactor covalently.
CC {ECO:0000256|RuleBase:RU361137};
CC -!- SUBUNIT: Forms a 24-polypeptide structural core with octahedral
CC symmetry. {ECO:0000256|ARBA:ARBA00011484}.
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00007317, ECO:0000256|RuleBase:RU361137}.
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DR EMBL; HF677570; CCT60768.1; -; Genomic_DNA.
DR RefSeq; WP_012812901.1; NC_021991.1.
DR AlphaFoldDB; S6D6E8; -.
DR GeneID; 60375786; -.
DR KEGG; apk:APA386B_2736; -.
DR PATRIC; fig|1266844.4.peg.2736; -.
DR HOGENOM; CLU_016733_10_2_5; -.
DR Proteomes; UP000015386; Chromosome.
DR GO; GO:0045254; C:pyruvate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:UniProtKB-UniRule.
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; 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.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU361137,
KW ECO:0000313|EMBL:CCT60768.1};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU361137};
KW Pyruvate {ECO:0000313|EMBL:CCT60768.1};
KW Transferase {ECO:0000256|RuleBase:RU361137, ECO:0000313|EMBL:CCT60768.1}.
FT DOMAIN 2..78
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 129..166
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
SQ SEQUENCE 414 AA; 43264 MW; 70CEC00BE9637960 CRC64;
MATEILMPAL SPTMTEGKLA RWLKKEGDTV NSGDVLAEIE TDKATMEVEA IEEGILGRIL
IQEGAEGVAV NTPIAILVEE GEAVPDNIDT PKNVASAEPA PVPQPVASAP VAAQAAPAQR
ADKPVGRVVA SPLARRIARQ KNIDLAAIKG TGPNGRIVKR DVEAALNKAP SAGQVASALP
ASGGSSAVPH TTMRKVIARR LSESKATIPH FYVSIDVELD ALLALRAQLN AMSPAEGADA
FKLSVNDMLI KASAVALKQV PEVNASYTED AMILHEDADI SVAVSLDDGL ITPIVKQADR
KSLKDISQEA KDLIARARAG KLKPEEFQGG TFSISNMGMY GVKDFAAIVN PPQAAILAIA
AGKKQAVVKG NELAIATVMT VTLSVDHRVV DGAAAARWLS AFRTAVESPL SLVL
//
