ID ODBA_THET2 Reviewed; 367 AA. AC Q72GU1; DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 27-MAR-2024, entry version 99. 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=TT_C1757; OS Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27). OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus. OX NCBI_TaxID=262724; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27; RX PubMed=15064768; DOI=10.1038/nbt956; RA Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H., RA Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C., RA Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P., RA Kramer W., Merkl R., Gottschalk G., Fritz H.-J.; RT "The genome sequence of the extreme thermophile Thermus thermophilus."; RL Nat. Biotechnol. 22:547-553(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:Q5SLR4}. 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:0000250|UniProtKB:Q5SLR4}; CC -!- COFACTOR: CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; CC Evidence={ECO:0000250|UniProtKB:Q5SLR4}; CC -!- SUBUNIT: Heterotetramer of two alpha and two beta chains. Directly CC associated with ODBB in the E1 complex (By similarity). CC {ECO:0000250|UniProtKB:Q5SLR4}. 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; AE017221; AAS82099.1; -; Genomic_DNA. DR RefSeq; WP_011174115.1; NZ_CP133179.1. DR AlphaFoldDB; Q72GU1; -. DR SMR; Q72GU1; -. DR KEGG; tth:TT_C1757; -. DR eggNOG; COG1071; Bacteria. DR HOGENOM; CLU_029393_1_0_0; -. DR OrthoDB; 9766715at2; -. DR BRENDA; 1.2.4.4; 2305. DR Proteomes; UP000000592; 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 3: Inferred from homology; KW Magnesium; Metal-binding; Oxidoreductase; Thiamine pyrophosphate. FT CHAIN 1..367 FT /note="2-oxoisovalerate dehydrogenase subunit alpha" FT /id="PRO_0000294974" FT BINDING 66 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:Q5SLR4" FT BINDING 94..96 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /evidence="ECO:0000250|UniProtKB:Q5SLR4" FT BINDING 95 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:Q5SLR4" FT BINDING 128..131 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:Q5SLR4" FT BINDING 144..146 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /evidence="ECO:0000250|UniProtKB:Q5SLR4" FT BINDING 144 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:Q5SLR4" FT BINDING 174..180 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /evidence="ECO:0000250|UniProtKB:Q5SLR4" FT BINDING 175 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:Q5SLR4" FT BINDING 204..208 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /evidence="ECO:0000250|UniProtKB:Q5SLR4" FT BINDING 204 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:Q5SLR4" FT BINDING 206 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:Q5SLR4" FT BINDING 273 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /evidence="ECO:0000250|UniProtKB:Q5SLR4" SQ SEQUENCE 367 AA; 41442 MW; 726F33C315656E49 CRC64; MVKETHRFEP FTEEPIRLIG EEGEWLGDFP LDLEGEKLRR LYRDMLAARM LDERYTILIR TGKTSFIAPA AGHEAAQVAI AHAIRPGFDW VFPYYRDHGL ALALGIPLKE LFGQMLATKA DPNKGRQMPE HPGSKALNFF TVASPIASHV PPAAGAAISM KLLRTGQVAV CTFGDGATSE GDWYAGINFA AVQGAPAVFV CENNFYAISV DYRHQTHSPT IADKAHAFGI PGYLVDGMDV LASYYVVKEA VERARRGEGP SLVELRVYRY GPHSSADDDS RYRPKEEVAF WRKKDPIPRF RRFLEARGLW NEEWEEDVRE EIRAELERGL KEAEEAGPVP PEWMFADVFA EKPWHLLRQE ALLKEEL //