ID D3PMS9_MEIRD Unreviewed; 431 AA. AC D3PMS9; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 27-MAR-2024, entry version 85. DE RecName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU003423}; DE EC=2.3.1.- {ECO:0000256|RuleBase:RU003423}; GN OrderedLocusNames=Mrub_0477 {ECO:0000313|EMBL:ADD27254.1}; GN ORFNames=K649_02010 {ECO:0000313|EMBL:AGK03706.1}; OS Meiothermus ruber (strain ATCC 35948 / DSM 1279 / VKM B-1258 / 21) (Thermus OS ruber). OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Meiothermus. OX NCBI_TaxID=504728 {ECO:0000313|EMBL:AGK03706.1, ECO:0000313|Proteomes:UP000013026}; RN [1] {ECO:0000313|EMBL:ADD27254.1, ECO:0000313|Proteomes:UP000006655} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35948 / DSM 1279 / VKM B-1258 / 21 RC {ECO:0000313|Proteomes:UP000006655}, and DSM 1279 RC {ECO:0000313|EMBL:ADD27254.1}; RX PubMed=21304689; DOI=10.4056/sigs.1032748; RA Tindall B.J., Sikorski J., Lucas S., Goltsman E., Copeland A., RA Glavina Del Rio T., Nolan M., Tice H., Cheng J.F., Han C., Pitluck S., RA Liolios K., Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., RA Fahnrich R., Goodwin L., Chen A., Palaniappan K., Land M., Hauser L., RA Chang Y.J., Jeffries C.D., Rohde M., Goker M., Woyke T., Bristow J., RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., RA Lapidus A.; RT "Complete genome sequence of Meiothermus ruber type strain (21)."; RL Stand. Genomic Sci. 3:26-36(2010). RN [2] {ECO:0000313|EMBL:AGK03706.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 1279 {ECO:0000313|EMBL:AGK03706.1}; RA Klammer A., Drake J., Heiner C., Clum A., Copeland A., Huddleston J., RA Eichler E., Turner S.W.; RT "Non-Hybrid, Finished Microbial Genome Assemblies from Long-Read SMRT RT Sequencing Data."; RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:AGK03706.1, ECO:0000313|Proteomes:UP000013026} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35948 / DSM 1279 / VKM B-1258 / 21 RC {ECO:0000313|Proteomes:UP000013026}, and DSM 1279 RC {ECO:0000313|EMBL:AGK03706.1}; RA Chin J., Alexander D.H., Marks P., Korlach J., Clum A., Copeland A.; RL Submitted (APR-2013) 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 --------------------------------------------------------------------------- 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; CP001743; ADD27254.1; -; Genomic_DNA. DR EMBL; CP005385; AGK03706.1; -; Genomic_DNA. DR RefSeq; WP_013012773.1; NC_021081.1. DR AlphaFoldDB; D3PMS9; -. DR STRING; 504728.K649_02010; -. DR KEGG; mrb:Mrub_0477; -. DR KEGG; mre:K649_02010; -. DR PATRIC; fig|504728.9.peg.416; -. DR eggNOG; COG0508; Bacteria. DR OrthoDB; 9805770at2; -. DR Proteomes; UP000006655; Chromosome. DR Proteomes; UP000013026; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProt. DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW. DR GO; GO:0006096; P:glycolytic process; 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:SF2; DIHYDROLIPOYLLYSINE-RESIDUE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX; 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|RuleBase:RU003423}; KW Glycolysis {ECO:0000256|ARBA:ARBA00023152}; KW Lipoyl {ECO:0000256|RuleBase:RU003423}; KW Transferase {ECO:0000256|RuleBase:RU003423}. FT DOMAIN 1..76 FT /note="Lipoyl-binding" FT /evidence="ECO:0000259|PROSITE:PS50968" FT DOMAIN 135..172 FT /note="Peripheral subunit-binding (PSBD)" FT /evidence="ECO:0000259|PROSITE:PS51826" FT REGION 77..133 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 175..194 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 82..97 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 99..122 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 431 AA; 45638 MW; 3C4B8E18A02A81C0 CRC64; MAELKLPDLG DNVTSAVVVG VLIKEGDTIA AGQPVLELET DKAVMEAPAS EGGTVSKVLV KPGDEVKSGQ VIAVLGDAAP SAEKQEPKEK QEPKEEKAAP APAPTPAPAA TPSAPAAAPR PPASAAPAGQ RRLIPAAPSV RRLAREMGIN LMEVVGSGPA YRISENDLKR FAAGEAPTTA APQPSSAPAL PDFSKFGPVR REAMSGVRRA TVRSMAQAWS TIPMVTHFDR ADITEMEALR KRMAPRAEQR GAKVTMTAIL LKIAAAALKQ FPKFNASIDT ASNEIIYKDY IHIGVAVDTP TGLLVPVVRD VDKKGVIALA KELGEIAAKA RERKLTPEEM QGATFTISNL GGIGGTGFTP IVNWPEVAIM GVSRSSMEPV WSAEKGVFEP RNIMPFSLSY DHRLIDGADA ARFCRFVAEL LEDPFLLGFE G //