ID   C4K7S2_HAMD5            Unreviewed;       531 AA.
AC   C4K7S2;
DT   07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   07-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 80.
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=aceF {ECO:0000313|EMBL:ACQ68615.1};
GN   OrderedLocusNames=HDEF_2043 {ECO:0000313|EMBL:ACQ68615.1};
OS   Hamiltonella defensa subsp. Acyrthosiphon pisum (strain 5AT).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; aphid secondary symbionts; Hamiltonella.
OX   NCBI_TaxID=572265 {ECO:0000313|EMBL:ACQ68615.1, ECO:0000313|Proteomes:UP000002334};
RN   [1] {ECO:0000313|EMBL:ACQ68615.1, ECO:0000313|Proteomes:UP000002334}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=5AT {ECO:0000313|Proteomes:UP000002334};
RX   PubMed=19451630; DOI=10.1073/pnas.0900194106;
RA   Degnan P.H., Yu Y., Sisneros N., Wing R.A., Moran N.A.;
RT   "Hamiltonella defensa, genome evolution of protective bacterial
RT   endosymbiont from pathogenic ancestors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:9063-9068(2009).
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 2 lipoyl cofactors covalently.
CC       {ECO:0000256|RuleBase:RU361137};
CC   -!- SUBUNIT: Forms a 24-polypeptide structural core with octahedral
CC       symmetry. {ECO:0000256|ARBA:ARBA00011484,
CC       ECO:0000256|RuleBase:RU361137}.
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00007317, ECO:0000256|RuleBase:RU361137}.
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DR   EMBL; CP001277; ACQ68615.1; -; Genomic_DNA.
DR   RefSeq; WP_015874368.1; NC_012751.1.
DR   AlphaFoldDB; C4K7S2; -.
DR   STRING; 572265.HDEF_2043; -.
DR   GeneID; 66261592; -.
DR   KEGG; hde:HDEF_2043; -.
DR   eggNOG; COG0508; Bacteria.
DR   HOGENOM; CLU_016733_10_0_6; -.
DR   Proteomes; UP000002334; Chromosome.
DR   GO; GO:0045254; C:pyruvate dehydrogenase complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR   CDD; cd06849; lipoyl_domain; 2.
DR   Gene3D; 2.40.50.100; -; 2.
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; IPR006256; AcTrfase_Pyrv_DH_cplx.
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   NCBIfam; TIGR01348; PDHac_trf_long; 1.
DR   PANTHER; PTHR43178; DIHYDROLIPOAMIDE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX; 1.
DR   PANTHER; PTHR43178:SF2; DIHYDROLIPOYLLYSINE-RESIDUE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX; 1.
DR   Pfam; PF00198; 2-oxoacid_dh; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 2.
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; 2.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 2.
DR   PROSITE; PS00189; LIPOYL; 2.
DR   PROSITE; PS51826; PSBD; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU361137};
KW   Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|RuleBase:RU361137};
KW   Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU361137};
KW   Pyruvate {ECO:0000313|EMBL:ACQ68615.1};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|RuleBase:RU361137}.
FT   DOMAIN          2..75
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          101..174
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          230..267
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
FT   REGION          182..221
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        207..221
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   531 AA;  57709 MW;  1094740AB48E9E03 CRC64;
     MVIEIKMPDI GTDTPEVIEI MVKVGDVVVP EQTLLCVEGD KASMDIPSPQ EGTIKEIKVS
     VGDKVETGKL IMLFESSTEA VPEKKGKTQV PAPAIPAQEN TKTVSLPDVG SDELEVTEIL
     VKVGDSVTEE QSLITVEGDK ASMEVPAPFS GTVKEIQIKT GDKVKTGSMI MIMNTIEKIT
     PAPDQKIQKT ADALPEQKPE IPPSKPSAPS NTTTSIEKTT PSFTEEAYTH ATPVIRRLAR
     ELGVNLEKVA GTGRKGRILK EDVQSYVKNA VQTAESASSG QGNLTPLLPW PKIDFNQFGE
     TEEIALTRIQ KMSGDNLSRN WVMIPHVTQF DETDITDLED FRKKQNIEAE KRKLDVKITP
     VVFMMKAVAQ ALKTFPRFNS SLSLDGKKLI LKKYINIGVA VDTPNGLVVP VFRDVNKKGV
     IELSKELMLI SQKARSGKLT ASDMQGGCFT ISSLGGIGGT AFTPIVNAPE VAILGVSKSA
     IKPIWNGKEF LPRLMLPLSL SFDHRVIDGA AGARFVSHIS VIMADIRRLI M
//