BKDA_MYCTO
ID BKDA_MYCTO Reviewed; 367 AA.
AC P9WIS2; F2GH61; L0T9Z4; O06161; Q7D714;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 37.
DE RecName: Full=3-methyl-2-oxobutanoate dehydrogenase subunit alpha;
DE EC=1.2.4.4;
DE AltName: Full=Branched-chain alpha-ketoacid dehydrogenase E1 component subunit alpha;
DE Short=BCKADH E1-alpha;
GN Name=bkdA; Synonyms=pdhA; OrderedLocusNames=MT2572;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
CC -!- FUNCTION: Component of the branched-chain alpha-ketoacid dehydrogenase
CC (BCKADH) complex, that catalyzes the overall conversion of branched-
CC chain alpha-ketoacids to acyl-CoA and CO(2). {ECO:0000250}.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000250};
CC -!- SUBUNIT: Heteromer of E1 alpha (BkdA) and beta (BkdB) subunits. Part of
CC the BCKADH complex, consisting of multiple copies of BkdA/BkdB (E1),
CC BkdC (E2) and Lpd (E3) (By similarity). {ECO:0000250}.
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DR EMBL; AE000516; AAK46876.1; -; Genomic_DNA.
DR PIR; A70550; A70550.
DR RefSeq; WP_003412761.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WIS2; -.
DR SMR; P9WIS2; -.
DR EnsemblBacteria; AAK46876; AAK46876; MT2572.
DR GeneID; 45426491; -.
DR KEGG; mtc:MT2572; -.
DR PATRIC; fig|83331.31.peg.2774; -.
DR HOGENOM; CLU_029393_1_0_11; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0003863; F:3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR InterPro; IPR001017; DH_E1.
DR InterPro; IPR017596; PdhA/BkdA.
DR InterPro; IPR029061; THDP-binding.
DR PANTHER; PTHR11516:SF41; PTHR11516:SF41; 1.
DR Pfam; PF00676; E1_dh; 1.
DR SUPFAM; SSF52518; SSF52518; 1.
DR TIGRFAMs; TIGR03181; PDH_E1_alph_x; 1.
PE 3: Inferred from homology;
KW Magnesium; Metal-binding; Oxidoreductase; Thiamine pyrophosphate.
FT CHAIN 1..367
FT /note="3-methyl-2-oxobutanoate dehydrogenase subunit alpha"
FT /id="PRO_0000427955"
FT BINDING 99..101
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 100
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 141..142
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 170..176
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 171
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 200..204
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 200
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 269
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
SQ SEQUENCE 367 AA; 40616 MW; BB7EC516F2C55829 CRC64;
MGEGSRRPSG MLMSVDLEPV QLVGPDGTPT AERRYHRDLP EETLRWLYEM MVVTRELDTE
FVNLQRQGEL ALYTPCRGQE AAQVGAAACL RKTDWLFPQY RELGVYLVRG IPPGHVGVAW
RGTWHGGLQF TTKCCAPMSV PIGTQTLHAV GAAMAAQRLD EDSVTVAFLG DGATSEGDVH
EALNFAAVFT TPCVFYVQNN QWAISMPVSR QTAAPSIAHK AIGYGMPGIR VDGNDVLACY
AVMAEAAARA RAGDGPTLIE AVTYRLGPHT TADDPTRYRS QEEVDRWATL DPIPRYRTYL
QDQGLWSQRL EEQVTARAKH VRSELRDAVF DAPDFDVDEV FTTVYAEITP GLQAQREQLR
AELARTD
