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Database: UniProt
Entry: A0A150LDQ2_9BACI
LinkDB: A0A150LDQ2_9BACI
Original site: A0A150LDQ2_9BACI 
ID   A0A150LDQ2_9BACI        Unreviewed;       389 AA.
AC   A0A150LDQ2;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
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=B4102_2343 {ECO:0000313|EMBL:KYD10471.1};
OS   Heyndrickxia sporothermodurans.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Heyndrickxia.
OX   NCBI_TaxID=46224 {ECO:0000313|EMBL:KYD10471.1, ECO:0000313|Proteomes:UP000075666};
RN   [1] {ECO:0000313|EMBL:KYD10471.1, ECO:0000313|Proteomes:UP000075666}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4102 {ECO:0000313|EMBL:KYD10471.1,
RC   ECO:0000313|Proteomes:UP000075666};
RA   Berendsen E.M., Wells-Bennik M.H., Krawcyk A.O., De Jong A., Holsappel S.,
RA   Eijlander R.T., Kuipers O.P.;
RT   "Genome Sequences of Twelve Sporeforming Bacillus Species Isolated from
RT   Foods.";
RL   Submitted (JAN-2016) 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}.
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:KYD10471.1}.
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DR   EMBL; LQYN01000013; KYD10471.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A150LDQ2; -.
DR   STRING; 46224.B4102_2343; -.
DR   PATRIC; fig|46224.3.peg.953; -.
DR   OrthoDB; 9805770at2; -.
DR   Proteomes; UP000075666; 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; 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; 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; PS51826; PSBD; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW   ECO:0000256|RuleBase:RU003423}; Lipoyl {ECO:0000256|RuleBase:RU003423};
KW   Reference proteome {ECO:0000313|Proteomes:UP000075666};
KW   Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:KYD10471.1}.
FT   DOMAIN          1..76
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          104..141
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
SQ   SEQUENCE   389 AA;  43008 MW;  05C8E86176F8D76E CRC64;
     MVEVKLHDIG EGMTEGEIVS YLVKVGDPVQ SDQPLVEVQT DKMTAELPSP TTGIVKEILV
     KEGTLVPVGT TILIIESGQT KHVQQEVTVS SNRNKVEKTN RMILAAPYTR KIARELGIDI
     EKINGTGPAG RITDEDVYNY GKKAVEPMAA PIKEVIKNAV ESDEIPFKGR RKQIASLMSK
     SLFTIPHVTH FEEVDMTNLL DCKQQCKEDG INISVAAFFI KAIQLTLMKY PIFNSVLDED
     HGVIRLKKEY NIGVAVDAED GLIVPVIRNV EQKTVKTIHD EMKIAIEKAQ NNTLTKADIS
     NGTFTISNVG PLGGIGATPI INYPQTALIS FHKTKKKPVV INDEIVIRSM MNLSMSFDHR
     VADGATAVRF TNEFVQLIEN PTRMLLEMT
//
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