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Database: UniProt/TrEMBL
Entry: U5QAT3_9BACT
LinkDB: U5QAT3_9BACT
Original site: U5QAT3_9BACT 
ID   U5QAT3_9BACT            Unreviewed;       420 AA.
AC   U5QAT3;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 37.
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:AGY54535.1};
GN   ORFNames=BRDCF_p1908 {ECO:0000313|EMBL:AGY54535.1};
OS   Bacteroidales bacterium CF.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales.
OX   NCBI_TaxID=1400053 {ECO:0000313|EMBL:AGY54535.1, ECO:0000313|Proteomes:UP000017642};
RN   [1] {ECO:0000313|EMBL:AGY54535.1, ECO:0000313|Proteomes:UP000017642}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CF {ECO:0000313|EMBL:AGY54535.1};
RX   PubMed=24356833;
RA   Tang S., Edwards E.A.;
RT   "Complete Genome Sequence of Bacteroidales Strain CF from a Chloroform-
RT   Dechlorinating Enrichment Culture.";
RL   Genome Announc. 1:e01066-13(2013).
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; CP006772; AGY54535.1; -; Genomic_DNA.
DR   AlphaFoldDB; U5QAT3; -.
DR   STRING; 1400053.BRDCF_p1908; -.
DR   KEGG; bacc:BRDCF_p1908; -.
DR   HOGENOM; CLU_016733_10_0_10; -.
DR   OrthoDB; 9805770at2; -.
DR   Proteomes; UP000017642; 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; 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; 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   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:RU003423,
KW   ECO:0000313|EMBL:AGY54535.1};
KW   Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW   Pyruvate {ECO:0000313|EMBL:AGY54535.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017642};
KW   Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:AGY54535.1}.
FT   DOMAIN          2..77
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          136..173
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
SQ   SEQUENCE   420 AA;  45045 MW;  10281A5B3F9F12DC CRC64;
     MRYIFKFPDI GEGLDEGTIV EWHVEKGSTV KMGDPLCTME TDKVVTAIPS PKDGAIAAKF
     GKPGEVIHVG DALVEIEIAG VSGEAAVEEA NKVEAVNEEG AGVVGTLEVA GNSVVLSASK
     EGVKETETVK PERKALATPV ARALAKELGI DINRVKGSGP AGRITKEDVN NFSAAPPAKP
     ERSQAPGNDT IEIEQLSQIR KSIARHMTQS KHNAAHMTLF EEVEISELER VRSRYKESLQ
     KEGVKLTYLS FIVKAVALAL KKHRSLNAEM DLEGGKMIYK KYYNIGIATD TEKGLVVPVI
     RNADILSVRE IAAEIAALSE KARLGQLTME DMKGGTFTIT SYGNIGGLFA VPVINYPEAG
     ILGVGRISKQ PVVKGDELAI GLILPLSLSV DHRIADGGET ARFMNSVMAY LGDPVTLLFN
//
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