ID A0A4Y7WKA5_BACHO Unreviewed; 426 AA. AC A0A4Y7WKA5; DT 18-SEP-2019, integrated into UniProtKB/TrEMBL. DT 18-SEP-2019, sequence version 1. DT 13-NOV-2019, entry version 3. 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=E2L07_17985 {ECO:0000313|EMBL:TES48942.1}; OS Bacillus halodurans. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=86665 {ECO:0000313|EMBL:TES48942.1, ECO:0000313|Proteomes:UP000297745}; RN [1] {ECO:0000313|EMBL:TES48942.1, ECO:0000313|Proteomes:UP000297745} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 497 {ECO:0000313|EMBL:TES48942.1, RC ECO:0000313|Proteomes:UP000297745}; RA Liu G.; RL Submitted (MAR-2019) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088; CC Evidence={ECO:0000256|RuleBase:RU003423}; CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family. CC {ECO:0000256|RuleBase:RU003423}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:TES48942.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; SNUY01000075; TES48942.1; -; Genomic_DNA. DR Proteomes; UP000297745; Unassembled WGS sequence. DR GO; GO:0016746; F:transferase activity, transferring acyl groups; IEA:UniProtKB-KW. DR Gene3D; 3.30.559.10; -; 1. DR Gene3D; 4.10.320.10; -; 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 Pfam; PF00198; 2-oxoacid_dh; 1. DR Pfam; PF00364; Biotin_lipoyl; 1. DR Pfam; PF02817; E3_binding; 1. DR SUPFAM; SSF47005; SSF47005; 1. DR SUPFAM; SSF51230; SSF51230; 1. DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1. DR PROSITE; PS51826; PSBD; 1. PE 3: Inferred from homology; KW Acyltransferase {ECO:0000256|RuleBase:RU003423}; KW Complete proteome {ECO:0000313|Proteomes:UP000297745}; KW Lipoyl {ECO:0000256|RuleBase:RU003423}; KW Transferase {ECO:0000256|RuleBase:RU003423}. FT DOMAIN 2 77 Lipoyl-binding. {ECO:0000259|PROSITE: FT PS50968}. FT DOMAIN 114 151 Peripheral subunit-binding (PSBD). FT {ECO:0000259|PROSITE:PS51826}. FT REGION 80 115 Disordered. {ECO:0000256|SAM:MobiDB- FT lite}. FT COMPBIAS 84 114 Polar. {ECO:0000256|SAM:MobiDB-lite}. SQ SEQUENCE 426 AA; 46342 MW; 8B16D545982B39BD CRC64; MATEITMPQL GESVTEGTIS RWLVKPGDKV NKYDPLAEVL TDKVNAEIPS SFSGTIQELL VEEDETVAVG HVICTMNVEG EAVEAETNDT SVSSAETTES PTETQEQSTS AKKRYSPAVL RLAEEHDIDL THVTGSGKGG RITRKDLQAI IEGGDIPKAA SMTEQKTALV QETMPLTEKV QEPVQVPTVS GDVEIPVSGV RKAIAQNMVK SKHEAPHAWT MVEVDVTNLV QLRNQLKEGF KKKEGFNLTF LPFFIKAVVE ALKAYPQLNS MWAGDKIIQK KDINISLAVA TDDALFVPVI KHADEKTIKG LAREVNELAH KVRTGKVTSS DMQGGTFTVN NTGSFGSVLS TPIINHPQAA ILSVESIVKR PVVIESEAGD MIAIRSMVNL CLSLDHRVLD GLICGRFLAK VKNILENMTI ENTSIY //