BKDC_MYCTU
ID BKDC_MYCTU Reviewed; 393 AA.
AC O06159; L0TBD7;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Dihydrolipoyllysine-residue acyltransferase component of branched-chain alpha-ketoacid dehydrogenase complex;
DE EC=2.3.1.168;
DE AltName: Full=Branched-chain alpha-ketoacid dehydrogenase complex component E2;
DE Short=BCKADH E2;
DE AltName: Full=Dihydrolipoyllysine-residue (2-methylpropanoyl)transferase;
GN Name=bkdC; Synonyms=pdhC; OrderedLocusNames=Rv2495c;
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.
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, LIPOYLATION, COFACTOR, GENE
RP NAME, AND IDENTIFICATION IN 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).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 154-393.
RG New York structural genomics research consortium (NYSGRC);
RT "Crystal structure of branched-chain alpha-keto acid dehydrogenase subunit
RT E2 from Mycobacterium tuberculosis.";
RL Submitted (JAN-2010) to the PDB data bank.
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)-dihydrolipoyl-L-lysyl-[protein] + 2-methylpropanoyl-
CC CoA = (R)-N(6)-(S(8)-2-methylpropanoyldihydrolipoyl)-L-lysyl-
CC [protein] + CoA; Xref=Rhea:RHEA:18865, Rhea:RHEA-COMP:10475,
CC Rhea:RHEA-COMP:10497, ChEBI:CHEBI:57287, ChEBI:CHEBI:57338,
CC ChEBI:CHEBI:83100, ChEBI:CHEBI:83142; EC=2.3.1.168;
CC -!- COFACTOR:
CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC Evidence={ECO:0000269|PubMed:21238944};
CC Note=Binds 1 lipoyl cofactor covalently. {ECO:0000269|PubMed:21238944};
CC -!- SUBUNIT: Forms a 24-polypeptide structural core with octahedral
CC symmetry (By similarity). Part of the BCKADH complex, consisting of
CC multiple copies of BkdA/BkdB (E1), BkdC (E2) and Lpd (E3).
CC {ECO:0000250, 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}.
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AL123456; CCP45289.1; -; Genomic_DNA.
DR PIR; G70549; G70549.
DR RefSeq; NP_217011.1; NC_000962.3.
DR RefSeq; WP_010886148.1; NC_000962.3.
DR PDB; 3L60; X-ray; 2.00 A; A=154-393.
DR PDB; 6ZZN; X-ray; 1.50 A; A=165-393.
DR PDBsum; 3L60; -.
DR PDBsum; 6ZZN; -.
DR AlphaFoldDB; O06159; -.
DR SMR; O06159; -.
DR STRING; 83332.Rv2495c; -.
DR PaxDb; O06159; -.
DR DNASU; 888237; -.
DR GeneID; 888237; -.
DR KEGG; mtu:Rv2495c; -.
DR PATRIC; fig|83332.12.peg.2797; -.
DR TubercuList; Rv2495c; -.
DR eggNOG; COG0508; Bacteria.
DR InParanoid; O06159; -.
DR OMA; HPCIMAP; -.
DR PhylomeDB; O06159; -.
DR EvolutionaryTrace; O06159; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0016407; F:acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0043754; F:dihydrolipoyllysine-residue (2-methylpropanoyl)transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0031405; F:lipoic acid binding; IBA:GO_Central.
DR Gene3D; 3.30.559.10; -; 1.
DR Gene3D; 4.10.320.10; -; 1.
DR InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR036625; E3-bd_dom_sf.
DR InterPro; IPR004167; PSBD.
DR InterPro; IPR011053; Single_hybrid_motif.
DR Pfam; PF00198; 2-oxoacid_dh; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF02817; E3_binding; 1.
DR SUPFAM; SSF47005; SSF47005; 1.
DR SUPFAM; SSF51230; SSF51230; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS51826; PSBD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Lipoyl; Reference proteome; Transferase.
FT CHAIN 1..393
FT /note="Dihydrolipoyllysine-residue acyltransferase
FT component of branched-chain alpha-ketoacid dehydrogenase
FT complex"
FT /id="PRO_0000420520"
FT DOMAIN 7..82
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT DOMAIN 119..157
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01170"
FT ACT_SITE 364
FT /evidence="ECO:0000255"
FT ACT_SITE 368
FT /evidence="ECO:0000255"
FT MOD_RES 48
FT /note="N6-lipoyllysine"
FT /evidence="ECO:0000250, ECO:0000255|PROSITE-
FT ProRule:PRU01066"
FT HELIX 172..187
FT /evidence="ECO:0007829|PDB:6ZZN"
FT STRAND 190..198
FT /evidence="ECO:0007829|PDB:6ZZN"
FT HELIX 200..209
FT /evidence="ECO:0007829|PDB:6ZZN"
FT TURN 210..212
FT /evidence="ECO:0007829|PDB:6ZZN"
FT HELIX 218..231
FT /evidence="ECO:0007829|PDB:6ZZN"
FT HELIX 234..236
FT /evidence="ECO:0007829|PDB:6ZZN"
FT STRAND 237..241
FT /evidence="ECO:0007829|PDB:6ZZN"
FT TURN 243..245
FT /evidence="ECO:0007829|PDB:3L60"
FT STRAND 248..251
FT /evidence="ECO:0007829|PDB:6ZZN"
FT STRAND 257..259
FT /evidence="ECO:0007829|PDB:6ZZN"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:6ZZN"
FT STRAND 266..268
FT /evidence="ECO:0007829|PDB:6ZZN"
FT HELIX 275..277
FT /evidence="ECO:0007829|PDB:6ZZN"
FT HELIX 280..296
FT /evidence="ECO:0007829|PDB:6ZZN"
FT HELIX 301..304
FT /evidence="ECO:0007829|PDB:6ZZN"
FT STRAND 308..312
FT /evidence="ECO:0007829|PDB:6ZZN"
FT HELIX 314..317
FT /evidence="ECO:0007829|PDB:6ZZN"
FT STRAND 331..336
FT /evidence="ECO:0007829|PDB:6ZZN"
FT STRAND 340..346
FT /evidence="ECO:0007829|PDB:6ZZN"
FT STRAND 349..363
FT /evidence="ECO:0007829|PDB:6ZZN"
FT TURN 364..366
FT /evidence="ECO:0007829|PDB:6ZZN"
FT HELIX 369..384
FT /evidence="ECO:0007829|PDB:6ZZN"
FT HELIX 386..392
FT /evidence="ECO:0007829|PDB:6ZZN"
SQ SEQUENCE 393 AA; 41061 MW; 555F4941FC7B487E CRC64;
MSGEDSIRSF PVPDLGEGLQ EVTVTCWSVA VGDDVEINQT LCSVETAKAE VEIPSPYAGR
IVELGGAEGD VLKVGAELVR IDTGPTAVAQ PNGEGAVPTL VGYGADTAIE TSRRTSRPLA
APVVRKLAKE LAVDLAALQR GSGAGGVITR ADVLAAARGG VGAGPDVRPV HGVHARMAEK
MTLSHKEIPT AKASVEVICA ELLRLRDRFV SAAPEITPFA LTLRLLVIAL KHNVILNSTW
VDSGEGPQVH VHRGVHLGFG AATERGLLVP VVTDAQDKNT RELASRVAEL ITGAREGTLT
PAELRGSTFT VSNFGALGVD DGVPVINHPE AAILGLGAIK PRPVVVGGEV VARPTMTLTC
VFDHRVVDGA QVAQFMCELR DLIESPETAL LDL
