ID ODBA_THET8 Reviewed; 367 AA. AC Q5SLR4; P84129; DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot. DT 21-DEC-2004, sequence version 1. DT 27-MAR-2024, entry version 105. DE RecName: Full=2-oxoisovalerate dehydrogenase subunit alpha; DE EC=1.2.4.4; DE AltName: Full=Branched-chain alpha-keto acid dehydrogenase E1 component alpha chain; DE Short=BCKDH E1-alpha; GN OrderedLocusNames=TTHA0229; OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8). OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus. OX NCBI_TaxID=300852; RN [1] {ECO:0000312|EMBL:BAD70052.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27634 / DSM 579 / HB8; RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.; RT "Complete genome sequence of Thermus thermophilus HB8."; RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000305, ECO:0000312|PDB:1UM9} RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH ODBB AND THIAMINE RP PYROPHOSPHATE, CATALYTIC ACTIVITY, COFACTOR, AND SUBUNIT. RX PubMed=15033367; DOI=10.1016/j.jmb.2004.02.011; RA Nakai T., Nakagawa N., Maoka N., Masui R., Kuramitsu S., Kamiya N.; RT "Ligand-induced conformational changes and a reaction intermediate in RT branched-chain 2-oxo acid dehydrogenase (E1) from Thermus thermophilus HB8, RT as revealed by X-ray crystallography."; RL J. Mol. Biol. 337:1011-1033(2004). CC -!- FUNCTION: The branched-chain alpha-keto dehydrogenase complex catalyzes CC the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It CC contains multiple copies of three enzymatic components: branched-chain CC alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and CC lipoamide dehydrogenase (E3) (By similarity). CC {ECO:0000250|UniProtKB:P37940}. CC -!- CATALYTIC ACTIVITY: CC Reaction=3-methyl-2-oxobutanoate + H(+) + N(6)-[(R)-lipoyl]-L-lysyl- CC [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] = CO2 + CC N(6)-[(R)-S(8)-2-methylpropanoyldihydrolipoyl]-L-lysyl- CC [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase]; CC Xref=Rhea:RHEA:13457, Rhea:RHEA-COMP:10488, Rhea:RHEA-COMP:10489, CC ChEBI:CHEBI:11851, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, CC ChEBI:CHEBI:83099, ChEBI:CHEBI:83142; EC=1.2.4.4; CC Evidence={ECO:0000269|PubMed:15033367}; CC -!- COFACTOR: CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; CC Evidence={ECO:0000269|PubMed:15033367}; CC -!- SUBUNIT: Heterotetramer of two alpha and two beta chains. Directly CC associated with ODBB in the E1 complex. {ECO:0000269|PubMed:15033367}. CC -!- INTERACTION: CC Q5SLR4; Q5SLR3: TTHA0230; NbExp=4; IntAct=EBI-1038222, EBI-1038230; CC -!- SIMILARITY: Belongs to the BCKDHA family. {ECO:0000305}. 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; AP008226; BAD70052.1; -; Genomic_DNA. DR RefSeq; WP_011227793.1; NC_006461.1. DR RefSeq; YP_143495.1; NC_006461.1. DR PDB; 1UM9; X-ray; 2.20 A; A/C=1-367. DR PDB; 1UMB; X-ray; 2.10 A; A/C=1-367. DR PDB; 1UMC; X-ray; 2.40 A; A/C=1-367. DR PDB; 1UMD; X-ray; 1.90 A; A/C=1-367. DR PDBsum; 1UM9; -. DR PDBsum; 1UMB; -. DR PDBsum; 1UMC; -. DR PDBsum; 1UMD; -. DR AlphaFoldDB; Q5SLR4; -. DR SMR; Q5SLR4; -. DR IntAct; Q5SLR4; 1. DR EnsemblBacteria; BAD70052; BAD70052; BAD70052. DR GeneID; 3168003; -. DR KEGG; ttj:TTHA0229; -. DR PATRIC; fig|300852.9.peg.227; -. DR eggNOG; COG1071; Bacteria. DR HOGENOM; CLU_029393_1_0_0; -. DR PhylomeDB; Q5SLR4; -. DR EvolutionaryTrace; Q5SLR4; -. DR Proteomes; UP000000532; Chromosome. DR GO; GO:0003863; F:3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR CDD; cd02000; TPP_E1_PDC_ADC_BCADC; 1. DR Gene3D; 3.40.50.970; -; 1. DR InterPro; IPR001017; DH_E1. DR InterPro; IPR029061; THDP-binding. DR PANTHER; PTHR43380; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT ALPHA, MITOCHONDRIAL; 1. DR PANTHER; PTHR43380:SF1; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT ALPHA, MITOCHONDRIAL; 1. DR Pfam; PF00676; E1_dh; 1. DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1. PE 1: Evidence at protein level; KW 3D-structure; Magnesium; Metal-binding; Oxidoreductase; Reference proteome; KW Thiamine pyrophosphate. FT CHAIN 1..367 FT /note="2-oxoisovalerate dehydrogenase subunit alpha" FT /id="PRO_0000294975" FT BINDING 66 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:15033367" FT BINDING 94..96 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /evidence="ECO:0000269|PubMed:15033367" FT BINDING 95 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:15033367" FT BINDING 128..131 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:15033367" FT BINDING 144..146 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /evidence="ECO:0000269|PubMed:15033367" FT BINDING 144 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:15033367" FT BINDING 174..180 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /evidence="ECO:0000269|PubMed:15033367" FT BINDING 175 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000269|PubMed:15033367" FT BINDING 204..208 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /evidence="ECO:0000269|PubMed:15033367" FT BINDING 204 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000269|PubMed:15033367" FT BINDING 206 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000269|PubMed:15033367" FT BINDING 273 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /evidence="ECO:0000269|PubMed:15033367" FT HELIX 35..60 FT /evidence="ECO:0007829|PDB:1UMD" FT HELIX 74..83 FT /evidence="ECO:0007829|PDB:1UMD" FT TURN 86..88 FT /evidence="ECO:0007829|PDB:1UMD" FT STRAND 89..92 FT /evidence="ECO:0007829|PDB:1UMD" FT TURN 95..97 FT /evidence="ECO:0007829|PDB:1UMD" FT HELIX 98..104 FT /evidence="ECO:0007829|PDB:1UMD" FT HELIX 108..116 FT /evidence="ECO:0007829|PDB:1UMD" FT TURN 122..125 FT /evidence="ECO:0007829|PDB:1UMD" FT TURN 135..138 FT /evidence="ECO:0007829|PDB:1UMD" FT TURN 146..149 FT /evidence="ECO:0007829|PDB:1UMD" FT HELIX 150..162 FT /evidence="ECO:0007829|PDB:1UMD" FT STRAND 169..174 FT /evidence="ECO:0007829|PDB:1UMD" FT HELIX 176..179 FT /evidence="ECO:0007829|PDB:1UMD" FT HELIX 181..192 FT /evidence="ECO:0007829|PDB:1UMD" FT STRAND 196..203 FT /evidence="ECO:0007829|PDB:1UMD" FT STRAND 205..207 FT /evidence="ECO:0007829|PDB:1UMD" FT HELIX 212..215 FT /evidence="ECO:0007829|PDB:1UMD" FT STRAND 217..219 FT /evidence="ECO:0007829|PDB:1UMD" FT HELIX 222..227 FT /evidence="ECO:0007829|PDB:1UMD" FT STRAND 232..236 FT /evidence="ECO:0007829|PDB:1UMD" FT HELIX 240..255 FT /evidence="ECO:0007829|PDB:1UMD" FT STRAND 261..266 FT /evidence="ECO:0007829|PDB:1UMD" FT HELIX 279..281 FT /evidence="ECO:0007829|PDB:1UMD" FT HELIX 285..292 FT /evidence="ECO:0007829|PDB:1UMD" FT HELIX 296..305 FT /evidence="ECO:0007829|PDB:1UMD" FT TURN 306..308 FT /evidence="ECO:0007829|PDB:1UMD" FT HELIX 312..335 FT /evidence="ECO:0007829|PDB:1UMD" FT HELIX 341..345 FT /evidence="ECO:0007829|PDB:1UMD" FT STRAND 348..351 FT /evidence="ECO:0007829|PDB:1UMD" FT HELIX 354..366 FT /evidence="ECO:0007829|PDB:1UMD" SQ SEQUENCE 367 AA; 41452 MW; 178B4EFE0CA5F1D1 CRC64; MVKETHRFET FTEEPIRLIG EEGEWLGDFP LDLEGEKLRR LYRDMLAARM LDERYTILIR TGKTSFIAPA AGHEAAQVAI AHAIRPGFDW VFPYYRDHGL ALALGIPLKE LLGQMLATKA DPNKGRQMPE HPGSKALNFF TVASPIASHV PPAAGAAISM KLLRTGQVAV CTFGDGATSE GDWYAGINFA AVQGAPAVFI AENNFYAISV DYRHQTHSPT IADKAHAFGI PGYLVDGMDV LASYYVVKEA VERARRGEGP SLVELRVYRY GPHSSADDDS RYRPKEEVAF WRKKDPIPRF RRFLEARGLW NEEWEEDVRE EIRAELERGL KEAEEAGPVP PEWMFEDVFA EKPWHLLRQE ALLKEEL //