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Database: UniProt
Entry: V7HXQ2_9LACO
LinkDB: V7HXQ2_9LACO
Original site: V7HXQ2_9LACO 
ID   V7HXQ2_9LACO            Unreviewed;       527 AA.
AC   V7HXQ2;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-MAR-2024, entry version 38.
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=LEQ_0681 {ECO:0000313|EMBL:ETA74667.1};
OS   Ligilactobacillus equi DPC 6820.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Ligilactobacillus.
OX   NCBI_TaxID=1392007 {ECO:0000313|EMBL:ETA74667.1, ECO:0000313|Proteomes:UP000018559};
RN   [1] {ECO:0000313|EMBL:ETA74667.1, ECO:0000313|Proteomes:UP000018559}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DPC 6820 {ECO:0000313|EMBL:ETA74667.1,
RC   ECO:0000313|Proteomes:UP000018559};
RX   PubMed=24435863;
RA   O'Donnell M.M., Harris H.M., O'Toole P.W., Ross R.P.;
RT   "The Genome of the Predominant Equine Lactobacillus Species, Lactobacillus
RT   equi, Is Reflective of Its Lifestyle Adaptations to an Herbivorous Host.";
RL   Genome Announc. 2:e01155-e01113(2014).
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:ETA74667.1}.
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DR   EMBL; AWWH01000048; ETA74667.1; -; Genomic_DNA.
DR   RefSeq; WP_023859050.1; NZ_AWWH01000048.1.
DR   AlphaFoldDB; V7HXQ2; -.
DR   PATRIC; fig|1392007.3.peg.447; -.
DR   Proteomes; UP000018559; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   CDD; cd06849; lipoyl_domain; 2.
DR   Gene3D; 2.40.50.100; -; 2.
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; 2.
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; 2.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 2.
DR   PROSITE; PS00189; LIPOYL; 2.
DR   PROSITE; PS51826; PSBD; 1.
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   Pyruvate {ECO:0000313|EMBL:ETA74667.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018559};
KW   Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:ETA74667.1}.
FT   DOMAIN          3..78
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          104..179
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          221..258
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
SQ   SEQUENCE   527 AA;  55906 MW;  A3E421AED5B749A8 CRC64;
     MSKYQFKLPD IGEGIAEGTI GEWHVKVGDT VKVDDDLVQI ENDKSVEEIP SPIAGKITAI
     LVSEGETAEV GQPLVELEVA EGEGNVDEVT TSATAATPAG GSDIYHFNLP DIGEGIAEGT
     VGEWHVKVGD TVKEDDDLVQ IENDKSVEEI PSPVTGTVTA ILVSEGETAE VGQPLVEFSV
     AAGQGNATAS AGIAPTAVAV PVASANVPAV GQPQDHSLPV LAMPSVRAYA REKGVDLAQI
     KGTGNHGQIL KVDVDKFLTN GPATPENKVV PEVDVREAAP AKETAVAAVA DAQFPEHREK
     MNGIRKATAK AVVRNVQEIP HIHLFDEVVV DKLWDHRKKY KELAASHDVK LTFLAYVVKA
     LSVVMKEYPI FNSTVDMANQ ESVFKDYINI GIATDTPKGL FMPNIKNADQ LSLFNIARAI
     SANTAKAKDG KLSSADMNHT GMSITNIGSV GGGFFTPLIN WPEVAILGIG KIAQEPVVDA
     EGEISVARVL KLSLAVDHRV IDGATAQKAL NRLKELLSDP ELLLMEG
//
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