ID E6YHD8_BARC7 Unreviewed; 441 AA.
AC E6YHD8;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 70.
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:CBI76276.1};
GN OrderedLocusNames=BARCL_0595 {ECO:0000313|EMBL:CBI76276.1};
OS Bartonella clarridgeiae (strain CCUG 45776 / CIP 104772 / 73).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Bartonellaceae; Bartonella.
OX NCBI_TaxID=696125 {ECO:0000313|EMBL:CBI76276.1, ECO:0000313|Proteomes:UP000009101};
RN [1] {ECO:0000313|Proteomes:UP000009101}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 104772 / 73 {ECO:0000313|Proteomes:UP000009101};
RA Engel P., Salzburger W., Marius L., Chao-Chin C., Soichi M., Christa L.,
RA Alexandra C., Aurelie L., Claudine M., Stephan S.C., Christoph D.;
RT "Genome sequencing of Bartonella species and comparative genomics.";
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBI76276.1, ECO:0000313|Proteomes:UP000009101}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 104772 / 73 {ECO:0000313|Proteomes:UP000009101};
RX PubMed=21347280; DOI=10.1371/journal.pgen.1001296;
RA Engel P., Salzburger W., Liesch M., Chang C.C., Maruyama S., Lanz C.,
RA Calteau A., Lajus A., Medigue C., Schuster S.C., Dehio C.;
RT "Parallel evolution of a type IV secretion system in radiating lineages of
RT the host-restricted bacterial pathogen Bartonella.";
RL PLoS Genet. 7:E1001296-E1001296(2011).
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; FN645454; CBI76276.1; -; Genomic_DNA.
DR RefSeq; WP_013544938.1; NC_014932.1.
DR AlphaFoldDB; E6YHD8; -.
DR STRING; 696125.BARCL_0595; -.
DR KEGG; bcd:BARCL_0595; -.
DR eggNOG; COG0508; Bacteria.
DR HOGENOM; CLU_016733_10_2_5; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000009101; 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:CBI76276.1};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU361137};
KW Transferase {ECO:0000256|RuleBase:RU361137, ECO:0000313|EMBL:CBI76276.1}.
FT DOMAIN 2..78
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 135..172
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
SQ SEQUENCE 441 AA; 48069 MW; 15775995F442917D CRC64;
MPIKITMPAL SPTMEEGNLS KWNVKEGDKV TCGDIIAEIE TDKATMEIEA IDEGTVAKIV
VPAGTQRVKV NSLIVVLAEE GEDLSEAAKI AEETSSIMVK EPVIKQSMNS ASVQASHSSK
NQQLIQRNGN NRRLFASPLA RRLAAQVGID LSLISGTGPH GRIIKHDVEK VLNNGLESSR
SLHINQSITS SISDRHILQL FKESEYTFAP HDNMRKTIAK RLVASKQMVP HFYVTIDCEL
DALLKLRTQL NAVVPMVEMQ EGTKKPAYKL SVNDMVIKAV ALSLKAVPDA NVSWLEDGML
YHKHCDVGVA VSVPNGLMVP IIRCAEEKSL SIISNEMKDL ATRARERKLR MEEYQGGTTA
VSNMGMYGIK NFSAIINPPH ATIFAIGSGE KRAIVKDGAL AIATVMSVTL SVDHRAVDGA
LAAEVAQTFK KIIENPLTML I
//
