ID A0A4Y7WKA5_ALKHA Unreviewed; 426 AA. AC A0A4Y7WKA5; DT 18-SEP-2019, integrated into UniProtKB/TrEMBL. DT 18-SEP-2019, sequence version 1. DT 29-SEP-2021, entry version 8. 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 Alkalihalobacillus halodurans (Bacillus halodurans). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus. 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|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: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:acyltransferase activity; 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 Lipoyl {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 114..151 FT /note="Peripheral subunit-binding (PSBD)" FT /evidence="ECO:0000259|PROSITE:PS51826" FT REGION 80..115 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 84..114 FT /note="Polar residues" FT /evidence="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 //