ID   BKDB_MYCTO              Reviewed;         348 AA.
AC   P9WIS0; F2GH62; L0T9T3; O06160; Q7D715;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 38.
DE   RecName: Full=3-methyl-2-oxobutanoate dehydrogenase subunit beta;
DE            EC=1.2.4.4;
DE   AltName: Full=Branched-chain alpha-ketoacid dehydrogenase E1 component subunit beta;
DE            Short=BCKADH E1-beta;
GN   Name=bkdB; Synonyms=pdhB; OrderedLocusNames=MT2571;
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=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; AAK46875.1; -; Genomic_DNA.
DR   PIR; H70549; H70549.
DR   RefSeq; WP_003412757.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WIS0; -.
DR   SMR; P9WIS0; -.
DR   EnsemblBacteria; AAK46875; AAK46875; MT2571.
DR   GeneID; 45426490; -.
DR   KEGG; mtc:MT2571; -.
DR   PATRIC; fig|83331.31.peg.2773; -.
DR   HOGENOM; CLU_012907_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   Gene3D; 3.40.50.920; -; 1.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   InterPro; IPR033248; Transketolase_C.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   Pfam; PF02780; Transketolase_C; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52518; SSF52518; 1.
DR   SUPFAM; SSF52922; SSF52922; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase; Thiamine pyrophosphate.
FT   CHAIN           1..348
FT                   /note="3-methyl-2-oxobutanoate dehydrogenase subunit beta"
FT                   /id="PRO_0000427956"
FT   ACT_SITE        151
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         51
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000250"
FT   BINDING         80..82
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000250"
FT   BINDING         104
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000250"
FT   BINDING         105..108
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         108..111
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000250"
FT   BINDING         151
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   348 AA;  38064 MW;  71D54633EEEB9A3E CRC64;
     MTQIADRPAR PDETLAVAVS DITQSLTMVQ AINRALYDAM AADERVLVFG EDVAVEGGVF
     RVTEGLADTF GADRCFDTPL AESAIIGIAV GLALRGFVPV PEIQFDGFSY PAFDQVVSHL
     AKYRTRTRGE VDMPVTVRIP SFGGIGAAEH HSDSTESYWV HTAGLKVVVP STPGDAYWLL
     RHAIACPDPV MYLEPKRRYH GRGMVDTSRP EPPIGHAMVR RSGTDVTVVT YGNLVSTALS
     SADTAEQQHD WSLEVIDLRS LAPLDFDTIA ASIQRTGRCV VMHEGPRSLG YGAGLAARIQ
     EEMFYQLEAP VLRACGFDTP YPPARLEKLW LPGPDRLLDC VERVLRQP