ID A0A0P6Y3T9_9CHLR Unreviewed; 327 AA.
AC A0A0P6Y3T9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=2-oxoisovalerate dehydrogenase subunit alpha {ECO:0000256|RuleBase:RU365014};
DE EC=1.2.4.4 {ECO:0000256|RuleBase:RU365014};
DE AltName: Full=Branched-chain alpha-keto acid dehydrogenase E1 component alpha chain {ECO:0000256|RuleBase:RU365014};
GN ORFNames=SE15_00265 {ECO:0000313|EMBL:KPL83745.1};
OS Thermanaerothrix daxensis.
OC Bacteria; Chloroflexota; Anaerolineae; Anaerolineales; Anaerolineaceae;
OC Thermanaerothrix.
OX NCBI_TaxID=869279 {ECO:0000313|EMBL:KPL83745.1, ECO:0000313|Proteomes:UP000050544};
RN [1] {ECO:0000313|EMBL:KPL83745.1, ECO:0000313|Proteomes:UP000050544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GNS-1 {ECO:0000313|EMBL:KPL83745.1,
RC ECO:0000313|Proteomes:UP000050544};
RA Hemp J., Ward L.M., Pace L.A., Fischer W.W.;
RT "Whole genome sequence of Thermanaerothrix daxensis DSM 23592.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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). {ECO:0000256|RuleBase:RU365014}.
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:0000256|RuleBase:RU365014};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964,
CC ECO:0000256|RuleBase:RU365014};
CC -!- SIMILARITY: Belongs to the BCKDHA family.
CC {ECO:0000256|RuleBase:RU365014}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPL83745.1}.
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DR EMBL; LGKO01000002; KPL83745.1; -; Genomic_DNA.
DR RefSeq; WP_054520119.1; NZ_LGKO01000002.1.
DR AlphaFoldDB; A0A0P6Y3T9; -.
DR STRING; 869279.SE15_00265; -.
DR PATRIC; fig|869279.4.peg.53; -.
DR OrthoDB; 9766715at2; -.
DR Proteomes; UP000050544; Unassembled WGS sequence.
DR GO; GO:0003863; F:3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity; IEA:UniProtKB-EC.
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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU365014};
KW Reference proteome {ECO:0000313|Proteomes:UP000050544};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU365014}.
FT DOMAIN 14..313
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
SQ SEQUENCE 327 AA; 36353 MW; 6CB0E47AB84E4127 CRC64;
MHLSEPKQVE MFWMMLLARR LDERAWVLHR QGKIAFHISG IGQEAAQVGA AFALRRGEDW
VVPYYRDLAL MLCLGYTPRE FMLSLMGKRE DPSSGGRQMP SHWSLRRVNV VSHSAPVATQ
TPHAVGVALA IKLRREDKVV LTTIGEGATS QGEWYEAVNW AAVHRLPVVF MVENNGYAIS
EPVEKQMAVE GAAARACGLG LEGVAVDGTD ALAVYAAVAR SVEKARSGEG PTLIEARMYR
LTPHSSDDDD RTYRTREEVE AAKRRDPLLR MRQHLEAQGW LTPEGLERME AEAKALVEDA
VDYATRAPYP APEEAAYPVF SAEVRRG
//
