ID   E8UR06_THEBF            Unreviewed;       382 AA.
AC   E8UR06;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   RecName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU003423};
DE            EC=2.3.1.- {ECO:0000256|RuleBase:RU003423};
GN   OrderedLocusNames=Thebr_0815 {ECO:0000313|EMBL:ADV79403.1};
OS   Thermoanaerobacter brockii subsp. finnii (strain ATCC 43586 / DSM 3389 /
OS   AKO-1) (Thermoanaerobacter finnii).
OC   Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Thermoanaerobacter.
OX   NCBI_TaxID=509193 {ECO:0000313|EMBL:ADV79403.1, ECO:0000313|Proteomes:UP000002062};
RN   [1] {ECO:0000313|EMBL:ADV79403.1, ECO:0000313|Proteomes:UP000002062}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43586 / DSM 3389 / AKO-1
RC   {ECO:0000313|Proteomes:UP000002062};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Chertkov O., Munk C., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Mikhailova N., Pagani I., Hemme C.L., Woyke T.;
RT   "Complete sequence of Thermoanaerobacter brockii finnii Ako-1.";
RL   Submitted (JAN-2011) 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}.
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DR   EMBL; CP002466; ADV79403.1; -; Genomic_DNA.
DR   RefSeq; WP_004401863.1; NC_014964.1.
DR   AlphaFoldDB; E8UR06; -.
DR   KEGG; tbo:Thebr_0815; -.
DR   HOGENOM; CLU_016733_10_2_9; -.
DR   Proteomes; UP000002062; Chromosome.
DR   GO; GO:0045254; C:pyruvate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:RHEA.
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; 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; PS00189; LIPOYL; 1.
DR   PROSITE; PS51826; PSBD; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU003423};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW   Transferase {ECO:0000256|RuleBase:RU003423}.
FT   DOMAIN          2..77
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          95..132
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
FT   COILED          264..291
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   382 AA;  42392 MW;  D64F17E577CE7B3E CRC64;
     MPVNVVMPKL GLTMKEGRVD RWLKKVGDIV KKGEEIVEVS TDKITNVVES PADGILAKIL
     VNEGEIVPVA TPIGIITAEG EKLEEVEKSE EKFIKATPVA KRLAKENNID LSLITGTGPG
     GRITEEDVKK FISEQKVKTE EEGPKKEVAV IEGQALEKVE RMPMDNIRKT ISQRMKKSWS
     EIPHVTEDIK VDVTELVNLR ENLNHISDNK FTYTDLIAKA CVIAIKKNPV VNWSIEGEYI
     IKNSSINLGI AVALDNGLIV PVVKEADKKS LLELSKNIKE LSERARNNKL TPDEIIGSTF
     TITNLGMYEI DSFTPIINPP ESAILGVNKI YKEPVVLDDN IVIRHIIKLS LSFDHRLIDG
     ATAAKFLLDL KKTLENPLSL LI
//