ID A0PU60_MYCUA Unreviewed; 389 AA.
AC A0PU60;
DT 09-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE RecName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU003423};
DE EC=2.3.1.- {ECO:0000256|RuleBase:RU003423};
GN Name=pdhC {ECO:0000313|EMBL:ABL05879.1};
GN OrderedLocusNames=MUL_3773 {ECO:0000313|EMBL:ABL05879.1};
OS Mycobacterium ulcerans (strain Agy99).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium ulcerans group.
OX NCBI_TaxID=362242 {ECO:0000313|EMBL:ABL05879.1, ECO:0000313|Proteomes:UP000000765};
RN [1] {ECO:0000313|EMBL:ABL05879.1, ECO:0000313|Proteomes:UP000000765}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Agy99 {ECO:0000313|EMBL:ABL05879.1,
RC ECO:0000313|Proteomes:UP000000765};
RX PubMed=17210928; DOI=10.1101/gr.5942807;
RA Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T.,
RA Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., Ryan J.,
RA Johnson P.D., Davies J.K., Jenkin G.A., Small P.L., Jones L.M., Tekaia F.,
RA Laval F., Daffe M., Parkhill J., Cole S.T.;
RT "Reductive evolution and niche adaptation inferred from the genome of
RT Mycobacterium ulcerans, the causative agent of Buruli ulcer.";
RL Genome Res. 17:192-200(2007).
CC -!- COFACTOR:
CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC Evidence={ECO:0000256|ARBA:ARBA00001938,
CC ECO:0000256|RuleBase:RU003423};
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00007317, ECO:0000256|RuleBase:RU003423}.
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DR EMBL; CP000325; ABL05879.1; -; Genomic_DNA.
DR RefSeq; WP_011741484.1; NC_008611.1.
DR AlphaFoldDB; A0PU60; -.
DR KEGG; mul:MUL_3773; -.
DR eggNOG; COG0508; Bacteria.
DR HOGENOM; CLU_016733_10_0_11; -.
DR Proteomes; UP000000765; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0016746; F:acyltransferase activity; 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; IPR001078; 2-oxoacid_DH_actylTfrase.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR036625; E3-bd_dom_sf.
DR InterPro; IPR004167; PSBD.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR43178; DIHYDROLIPOAMIDE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX; 1.
DR PANTHER; PTHR43178:SF5; LIPOAMIDE ACYLTRANSFERASE COMPONENT OF BRANCHED-CHAIN ALPHA-KETO ACID DEHYDROGENASE COMPLEX, MITOCHONDRIAL; 1.
DR Pfam; PF00198; 2-oxoacid_dh; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS51826; PSBD; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003423};
KW Lipoyl {ECO:0000256|RuleBase:RU003423};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:ABL05879.1}.
FT DOMAIN 7..82
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 119..154
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
SQ SEQUENCE 389 AA; 40926 MW; B5DDF34E97FCA739 CRC64;
MSTGDRLKCF QVPDLGEGLE EVTVTSWAVA VGDDVELNQV LCSVETAKAE VEIPSPYAGR
IVELGGAEGD VIKVGAALVR IDTAPELSAP TNGEIAVPTL VGYGADAAID TSRRPGRPRA
APPVRKLAKE LMVDLASLQR GSTVITRADV LAAAKGAGAS ARVREVRGVQ AHMAEKMSLS
HQEIPAAKAS VEVDCTELLG LSEQFRAVVP PATPFALALR MLVIALKNNE ILNSTWVDSP
GGPQVHLHPG VHLGFGVATE RGLLVPVIAD AHRMTTRELV CRAAELITGA REGTLAPGQL
RGWTFTVSNY GALGVDDGVP VINHPDAAIL GMGSIKPRPV VRGDEVVVRP TMSLTCVFDH
RVADGAQVAR FICELRGLIE APETALLDL
//
