ODBA_THET8
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 03-AUG-2022, entry version 100.
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; Deinococcus-Thermus; 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=(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: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}.
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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 STRING; 300852.55771611; -.
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 OMA; LQYWGGD; -.
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 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 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
