ID   K0P1S8_9BACT            Unreviewed;       409 AA.
AC   K0P1S8;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 49.
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:CCM09829.1};
GN   ORFNames=CAHE_0047 {ECO:0000313|EMBL:CCM09829.1};
OS   Cardinium endosymbiont cEper1 of Encarsia pergandiella.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Amoebophilaceae;
OC   Cardinium.
OX   NCBI_TaxID=1231626 {ECO:0000313|EMBL:CCM09829.1, ECO:0000313|Proteomes:UP000003996};
RN   [1] {ECO:0000313|EMBL:CCM09829.1, ECO:0000313|Proteomes:UP000003996}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Zchori-Fein et al. 2004 {ECO:0000313|Proteomes:UP000003996};
RX   PubMed=23133394; DOI=10.1371/journal.pgen.1003012;
RA   Penz T., Schmitz-Esser S., Kelly S.E., Cass B.N., Muller A., Woyke T.,
RA   Malfatti S.A., Hunter M.S., Horn M.;
RT   "Comparative Genomics Suggests an Independent Origin of Cytoplasmic
RT   Incompatibility in Cardinium hertigii.";
RL   PLoS Genet. 8:e1003012-e1003012(2012).
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   -!- 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; HE983995; CCM09829.1; -; Genomic_DNA.
DR   RefSeq; WP_014934203.1; NC_018605.1.
DR   AlphaFoldDB; K0P1S8; -.
DR   STRING; 1231626.CAHE_0047; -.
DR   KEGG; che:CAHE_0047; -.
DR   PATRIC; fig|1231626.3.peg.49; -.
DR   eggNOG; COG0508; Bacteria.
DR   HOGENOM; CLU_016733_10_2_10; -.
DR   OrthoDB; 9805770at2; -.
DR   BioCyc; CEND1231626:AL022_RS00215-MONOMER; -.
DR   Proteomes; UP000003996; Chromosome.
DR   GO; GO:0045254; C:pyruvate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
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; 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; IPR004167; PSBD.
DR   InterPro; IPR011053; Single_hybrid_motif.
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; PS51826; PSBD; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU003423,
KW   ECO:0000313|EMBL:CCM09829.1}; Lipoyl {ECO:0000256|RuleBase:RU003423};
KW   Pyruvate {ECO:0000313|EMBL:CCM09829.1};
KW   Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:CCM09829.1}.
FT   DOMAIN          2..77
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          131..168
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
SQ   SEQUENCE   409 AA;  44949 MW;  9938747A87A85541 CRC64;
     MAECIRMPKM SDTMEYGIVS RWIKQVGDKV VAGDILAEVD TDKATMELES YEDGTLLYVG
     VAERAAARIN DIIAIIGDPE EDINTLLAST VAIDGDRPAD TRIDLPLPIV DDQPVVPTAH
     MQSHLPLERS IASPLAKKIA KEKGYDLSQI QGSGEAGRII KKDVIHFVPN RLDQFSISEQ
     STRTAYQDFP ISAMRQKIAE VLTESKMNIP HFYLTVDINM NKLVEIRAEL NQYASTKISI
     NDLIIKATAL ALIQHPKVNA AWLTDKIRSY QYVHIGVAVA VEDGLMVPVV RFADQKPLVQ
     ISKTVKILSK QAQQKTLTPK DYTGATFTIS NLGMFGITSF SAIINPPAAC ILAIGAMQQI
     PIFKDNQVVP AHMLQLTLSC DHRVVDGHAG ALFLATLKTL LEQPLSLLL
//