BKDB_MYCTU
ID BKDB_MYCTU Reviewed; 348 AA.
AC P9WIS1; 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 39.
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=Rv2496c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP INDUCTION BY STARVATION.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=11929527; DOI=10.1046/j.1365-2958.2002.02779.x;
RA Betts J.C., Lukey P.T., Robb L.C., McAdam R.A., Duncan K.;
RT "Evaluation of a nutrient starvation model of Mycobacterium tuberculosis
RT persistence by gene and protein expression profiling.";
RL Mol. Microbiol. 43:717-731(2002).
RN [3]
RP NO FUNCTION AS A PDH COMPONENT, AND SUBUNIT.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=16045627; DOI=10.1111/j.1365-2958.2005.04741.x;
RA Tian J., Bryk R., Shi S., Erdjument-Bromage H., Tempst P., Nathan C.;
RT "Mycobacterium tuberculosis appears to lack alpha-ketoglutarate
RT dehydrogenase and encodes pyruvate dehydrogenase in widely separated
RT genes.";
RL Mol. Microbiol. 57:859-868(2005).
RN [4]
RP FUNCTION AS A BCKADH COMPONENT, INDUCTION, GENE NAME, AND IDENTIFICATION IN
RP THE BCKADH COMPLEX.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21238944; DOI=10.1016/j.chom.2010.12.004;
RA Venugopal A., Bryk R., Shi S., Rhee K., Rath P., Schnappinger D., Ehrt S.,
RA Nathan C.;
RT "Virulence of Mycobacterium tuberculosis depends on lipoamide
RT dehydrogenase, a member of three multienzyme complexes.";
RL Cell Host Microbe 9:21-31(2011).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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).
CC {ECO:0000269|PubMed:21238944}.
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). {ECO:0000269|PubMed:16045627,
CC ECO:0000269|PubMed:21238944}.
CC -!- INDUCTION: Up-regulated upon nutrient starvation. Is also highly up-
CC regulated in a DlaT-deficient strain. Part of the bkdABC operon.
CC {ECO:0000269|PubMed:11929527, ECO:0000269|PubMed:21238944}.
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DR EMBL; AL123456; CCP45290.1; -; Genomic_DNA.
DR PIR; H70549; H70549.
DR RefSeq; NP_217012.1; NC_000962.3.
DR RefSeq; WP_003412757.1; NZ_NVQJ01000063.1.
DR AlphaFoldDB; P9WIS1; -.
DR SMR; P9WIS1; -.
DR STRING; 83332.Rv2496c; -.
DR PaxDb; P9WIS1; -.
DR GeneID; 45426490; -.
DR GeneID; 888571; -.
DR KEGG; mtu:Rv2496c; -.
DR TubercuList; Rv2496c; -.
DR eggNOG; COG0022; Bacteria.
DR OMA; SEAYYMA; -.
DR PhylomeDB; P9WIS1; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
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 GO; GO:0009083; P:branched-chain amino acid catabolic process; IBA:GO_Central.
DR GO; GO:0007584; P:response to nutrient; IBA:GO_Central.
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 1: Evidence at protein level;
KW Oxidoreductase; Reference proteome; Thiamine pyrophosphate.
FT CHAIN 1..348
FT /note="3-methyl-2-oxobutanoate dehydrogenase subunit beta"
FT /id="PRO_0000420519"
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
