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Database: UniProt
Entry: G8N711_GEOTH
LinkDB: G8N711_GEOTH
Original site: G8N711_GEOTH 
ID   G8N711_GEOTH            Unreviewed;       436 AA.
AC   G8N711;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   RecName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU003423};
DE            EC=2.3.1.- {ECO:0000256|RuleBase:RU003423};
GN   ORFNames=GTCCBUS3UF5_7940 {ECO:0000313|EMBL:AEV18117.1};
OS   Geobacillus thermoleovorans CCB_US3_UF5.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC   Geobacillus thermoleovorans group.
OX   NCBI_TaxID=1111068 {ECO:0000313|EMBL:AEV18117.1, ECO:0000313|Proteomes:UP000005636};
RN   [1] {ECO:0000313|EMBL:AEV18117.1, ECO:0000313|Proteomes:UP000005636}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCB_US3_UF5 {ECO:0000313|EMBL:AEV18117.1,
RC   ECO:0000313|Proteomes:UP000005636};
RA   Muhd Sakaff M.K.L., Abdul Rahman A.Y., Saito J.A., Hou S., Alam M.;
RT   "Complete genome sequence of thermophilic Geobacillus thermoleovorans
RT   CCB_US3_UF5.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
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; CP003125; AEV18117.1; -; Genomic_DNA.
DR   RefSeq; WP_014195050.1; NC_016593.1.
DR   AlphaFoldDB; G8N711; -.
DR   KEGG; gte:GTCCBUS3UF5_7940; -.
DR   PATRIC; fig|1111068.3.peg.768; -.
DR   HOGENOM; CLU_016733_10_0_9; -.
DR   Proteomes; UP000005636; 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; 2.
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; 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; PS00189; LIPOYL; 1.
DR   PROSITE; PS51826; PSBD; 2.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW   ECO:0000256|RuleBase:RU003423};
KW   Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW   Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:AEV18117.1}.
FT   DOMAIN          2..77
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          93..130
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
FT   DOMAIN          143..180
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
SQ   SEQUENCE   436 AA;  47857 MW;  7C29D712383C7C70 CRC64;
     MVVEVTLPKL SDSHDESFIT FWHVSEGDAV EKGATLVEVQ TEKAVSEIHA PESGTVKEIK
     KKRGDTAKVG EVLAVIAVET FAPDGGDPQT EIKITPRVKK LAKELGVDWS TVTPTGANGK
     ITEEDIRRAA SAGKQRTPQK TFVAAPSVRK FAREQNVSLE EITPSGKNGR ILKSDIEAAL
     SVRQQKATDE AAASVEIVKK QESREKVRRV PLTGIRKAIA QAMVRSMRTI PQVTHFGEAD
     ATRLVQHRRR IKPLAEQQGV KLTYLAYVVK ALAAVLKKYP MLNASLDEER EEIVIHEFIH
     IGFAVDTDRG LLVPVIRDAD QKSLFQIAKE IEELTAKARA GTIQAVEMSG GTCTVSNIGS
     ANGSWFTPII HYPQSCLLGI GKVEKKPVVV DDSIEIASVM PLSLTYDHRL IDGMMAQHAL
     NECQTYLSEP DWLLVM
//
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