ID A0A2T0BNX7_9CLOT Unreviewed; 452 AA.
AC A0A2T0BNX7;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
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:PRR85576.1};
GN ORFNames=CLLU_14970 {ECO:0000313|EMBL:PRR85576.1};
OS Clostridium luticellarii.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1691940 {ECO:0000313|EMBL:PRR85576.1, ECO:0000313|Proteomes:UP000237798};
RN [1] {ECO:0000313|EMBL:PRR85576.1, ECO:0000313|Proteomes:UP000237798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 29923 {ECO:0000313|EMBL:PRR85576.1,
RC ECO:0000313|Proteomes:UP000237798};
RA Poehlein A., Daniel R.;
RT "Genome sequence of Clostridium luticellarii DSM 29923.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PRR85576.1}.
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DR EMBL; PVXP01000015; PRR85576.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T0BNX7; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000237798; Unassembled WGS sequence.
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; 2.
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; 2.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
DR SUPFAM; SSF47005; Peripheral subunit-binding domain of 2-oxo acid dehydrogenase complex; 2.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS51826; PSBD; 2.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003423,
KW ECO:0000313|EMBL:PRR85576.1}; Lipoyl {ECO:0000256|RuleBase:RU003423};
KW Pyruvate {ECO:0000313|EMBL:PRR85576.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000237798};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:PRR85576.1}.
FT DOMAIN 2..77
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 125..162
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT DOMAIN 168..202
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
SQ SEQUENCE 452 AA; 49360 MW; 93D4EA93ECEE0E93 CRC64;
MSCIEVMPKL GLTMTEGTLV NWHKSEGEKI EKGEILFEVE TDKLTNEIEA KESGVLRKIL
VEEGETVKCL VPVGIIAGQN EDISELLKQA GAKSGESEEK EDKVQEEVIA EPGISATVGA
EGRIKISPLA KRLALQGGVS YEDIKGTGPQ GRIVKKDIEA YIESTRIKVS PAAAKLAKEF
NVDLSGIKKN GRIMKRDVLE AAEAAKAPET THEEKVEKEK TSPQQTVVRG EKAVKMSAMR
KVIAKRMSES VSVSPTVTYN MTMDTSELKR LKNSLKDVFK VTYTDLLIKI VSQVLKEFPL
ANCSVEGDTF ILKDYVNMGV AVALDGGLLV PVIKDTDIKG IKQITAEFKD LVKRARENKL
VPDDLSGGTF TITNLGMYGI DTFSPIINQP EVAILGVNKI VETPLVENGE IVIKPLISMS
LTADHRAIDG AYAAQILQRI KQYVEKPGLL IL
//
