ODBA_THET2
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 03-AUG-2022, entry version 94.
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; Deinococcus-Thermus; 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=(R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue (2-
CC methylpropanoyl)transferase] + 3-methyl-2-oxobutanoate + H(+) = (R)-
CC N(6)-(S(8)-2-methylpropanoyldihydrolipoyl)-L-lysyl-
CC [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] + CO2;
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}.
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DR EMBL; AE017221; AAS82099.1; -; Genomic_DNA.
DR RefSeq; WP_011174115.1; NC_005835.1.
DR AlphaFoldDB; Q72GU1; -.
DR SMR; Q72GU1; -.
DR STRING; 262724.TT_C1757; -.
DR EnsemblBacteria; AAS82099; AAS82099; TT_C1757.
DR KEGG; tth:TT_C1757; -.
DR eggNOG; COG1071; Bacteria.
DR HOGENOM; CLU_029393_1_0_0; -.
DR OMA; LQYWGGD; -.
DR OrthoDB; 1248201at2; -.
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 GO; GO:0009083; P:branched-chain amino acid catabolic process; IEA:InterPro.
DR InterPro; IPR034616; BCKDH_E1-a.
DR InterPro; IPR001017; DH_E1.
DR InterPro; IPR029061; THDP-binding.
DR PANTHER; PTHR43380:SF1; PTHR43380:SF1; 1.
DR Pfam; PF00676; E1_dh; 1.
DR SUPFAM; SSF52518; SSF52518; 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
