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Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex (EC 2.3.1.12) (Component of peroxynitrite reductase/peroxidase complex) (Component of PNR/P) (Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex) (Pyruvate dehydrogenase complex component E2) (PDH component E2)

 ODP2_MYCTU              Reviewed;         553 AA.
P9WIS7; L0TBM6; P65633; Q10381;
16-APR-2014, integrated into UniProtKB/Swiss-Prot.
16-APR-2014, sequence version 1.
25-OCT-2017, entry version 28.
RecName: Full=Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex;
EC=2.3.1.12;
AltName: Full=Component of peroxynitrite reductase/peroxidase complex;
Short=Component of PNR/P;
AltName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex;
AltName: Full=Pyruvate dehydrogenase complex component E2;
Short=PDH component E2;
Name=dlaT; Synonyms=sucB; OrderedLocusNames=Rv2215;
ORFNames=MTCY190.26;
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
Mycobacterium; Mycobacterium tuberculosis complex.
NCBI_TaxID=83332;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 25618 / H37Rv;
PubMed=9634230; DOI=10.1038/31159;
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M.,
Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III,
Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T.,
Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N.,
Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S.,
Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A.,
Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R.,
Sulston J.E., Taylor K., Whitehead S., Barrell B.G.;
"Deciphering the biology of Mycobacterium tuberculosis from the
complete genome sequence.";
Nature 393:537-544(1998).
[2]
IDENTIFICATION, FUNCTION AS AN ANTIOXIDANT, LIPOYLATION AT LYS-43 AND
LYS-162, AND SUBUNIT.
STRAIN=ATCC 25618 / H37Rv;
PubMed=11799204; DOI=10.1126/science.1067798;
Bryk R., Lima C.D., Erdjument-Bromage H., Tempst P., Nathan C.;
"Metabolic enzymes of mycobacteria linked to antioxidant defense by a
thioredoxin-like protein.";
Science 295:1073-1077(2002).
[3]
FUNCTION AS A PDH COMPONENT, PH DEPENDENCE, LIPOYLATION, DISRUPTION
PHENOTYPE, GENE NAME, AND IDENTIFICATION IN THE PDH COMPLEX.
STRAIN=ATCC 25618 / H37Rv;
PubMed=16045627; DOI=10.1111/j.1365-2958.2005.04741.x;
Tian J., Bryk R., Shi S., Erdjument-Bromage H., Tempst P., Nathan C.;
"Mycobacterium tuberculosis appears to lack alpha-ketoglutarate
dehydrogenase and encodes pyruvate dehydrogenase in widely separated
genes.";
Mol. Microbiol. 57:859-868(2005).
[4]
DISRUPTION PHENOTYPE.
STRAIN=ATCC 25618 / H37Rv;
PubMed=16368957; DOI=10.1128/IAI.74.1.56-63.2006;
Shi S., Ehrt S.;
"Dihydrolipoamide acyltransferase is critical for Mycobacterium
tuberculosis pathogenesis.";
Infect. Immun. 74:56-63(2006).
[5]
ROLE IN VIRULENCE, INHIBITORS, ENZYME REGULATION, AND DISRUPTION
PHENOTYPE.
STRAIN=ATCC 25618 / H37Rv;
PubMed=18329613; DOI=10.1016/j.chom.2008.02.003;
Bryk R., Gold B., Venugopal A., Singh J., Samy R., Pupek K., Cao H.,
Popescu C., Gurney M., Hotha S., Cherian J., Rhee K., Ly L.,
Converse P.J., Ehrt S., Vandal O., Jiang X., Schneider J., Lin G.,
Nathan C.;
"Selective killing of nonreplicating mycobacteria.";
Cell Host Microbe 3:137-145(2008).
[6]
DISRUPTION PHENOTYPE.
STRAIN=ATCC 25618 / H37Rv;
PubMed=21238944; DOI=10.1016/j.chom.2010.12.004;
Venugopal A., Bryk R., Shi S., Rhee K., Rath P., Schnappinger D.,
Ehrt S., Nathan C.;
"Virulence of Mycobacterium tuberculosis depends on lipoamide
dehydrogenase, a member of three multienzyme complexes.";
Cell Host Microbe 9:21-31(2011).
[7]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ATCC 25618 / H37Rv;
PubMed=21969609; DOI=10.1074/mcp.M111.011627;
Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B.,
Yadav A.K., Shrivastava P., Marimuthu A., Anand S., Sundaram H.,
Kingsbury R., Harsha H.C., Nair B., Prasad T.S., Chauhan D.S.,
Katoch K., Katoch V.M., Kumar P., Chaerkady R., Ramachandran S.,
Dash D., Pandey A.;
"Proteogenomic analysis of Mycobacterium tuberculosis by high
resolution mass spectrometry.";
Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
-!- FUNCTION: Component of the pyruvate dehydrogenase (PDH) complex,
that catalyzes the overall conversion of pyruvate to acetyl-CoA
and CO(2).
-!- FUNCTION: Together with AhpC, AhpD and Lpd, constitutes an NADH-
dependent peroxidase active against hydrogen and alkyl peroxides
as well as serving as a peroxynitrite reductase, thus protecting
the bacterium against reactive nitrogen intermediates and
oxidative stress generated by the host immune system.
-!- FUNCTION: Appears to be essential for Mtb pathogenesis.
-!- CATALYTIC ACTIVITY: Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine
= CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine.
-!- COFACTOR:
Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
Note=Binds 2 lipoyl cofactors covalently.;
-!- ENZYME REGULATION: Inhibited by rhodanine compounds. Some of them
almost exclusively kill non-replicating mycobacteria in synergy
with products of host immunity, such as nitric oxide and hypoxia,
and are effective on bacteria within macrophages.
{ECO:0000269|PubMed:18329613}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 8.0 for PDH complex activity. Half-maximal
activity is observed at pH 7.0 and pH 9.0. Activity is abolished
at pH < 5. {ECO:0000269|PubMed:16045627};
-!- SUBUNIT: Forms a 24-polypeptide structural core with octahedral
symmetry (By similarity). Identified in a complex with AhpC, AhpD
and Lpd. Part of the PDH complex, consisting of multiple copies of
AceE (E1), DlaT (E2) and Lpd (E3). {ECO:0000250,
ECO:0000269|PubMed:11799204, ECO:0000269|PubMed:16045627}.
-!- DISRUPTION PHENOTYPE: Cells lacking this gene show severely
retarded growth in vitro, and display no PDH activity. They are
also more sensitive to nitrosative stress caused by NaNO(2), and
to macrophage-induced killing in vitro. They also show at least
20-fold reduction in survival in a mouse tuberculosis model, and
are unable to cause disease in a guinea pig model of tuberculosis
infection. Disruption of dlaT leads to high up-regulation of the
expression of the bkdABC operon. {ECO:0000269|PubMed:16045627,
ECO:0000269|PubMed:16368957, ECO:0000269|PubMed:18329613,
ECO:0000269|PubMed:21238944}.
-!- MISCELLANEOUS: Is the only lipoylated protein in strain H37Rv
grown on a standard rich medium. However, in a DlaT-deficient
strain, another protein, BkdC, becomes lipoylated.
-!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
{ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AL123456; CCP44992.1; -; Genomic_DNA.
PIR; H70786; H70786.
RefSeq; NP_216731.1; NC_000962.3.
RefSeq; WP_003411450.1; NZ_KK339370.1.
ProteinModelPortal; P9WIS7; -.
SMR; P9WIS7; -.
STRING; 83332.Rv2215; -.
BindingDB; P9WIS7; -.
iPTMnet; P9WIS7; -.
PaxDb; P9WIS7; -.
EnsemblBacteria; CCP44992; CCP44992; Rv2215.
GeneID; 888777; -.
KEGG; mtu:Rv2215; -.
TubercuList; Rv2215; -.
eggNOG; COG0508; LUCA.
KO; K00658; -.
OMA; MKVPSPG; -.
PhylomeDB; P9WIS7; -.
Reactome; R-HSA-1222541; Cell redox homeostasis.
Proteomes; UP000001584; Chromosome.
GO; GO:0005618; C:cell wall; IDA:MTBBASE.
GO; GO:0005829; C:cytosol; IDA:MTBBASE.
GO; GO:0005886; C:plasma membrane; IDA:MTBBASE.
GO; GO:0045254; C:pyruvate dehydrogenase complex; IDA:MTBBASE.
GO; GO:0016209; F:antioxidant activity; IEA:UniProtKB-KW.
GO; GO:0004148; F:dihydrolipoyl dehydrogenase activity; IDA:MTBBASE.
GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0015036; F:disulfide oxidoreductase activity; TAS:Reactome.
GO; GO:0031405; F:lipoic acid binding; IDA:MTBBASE.
GO; GO:0045454; P:cell redox homeostasis; IDA:MTBBASE.
GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
GO; GO:0040007; P:growth; IMP:MTBBASE.
GO; GO:0009405; P:pathogenesis; IDA:MTBBASE.
Gene3D; 4.10.320.10; -; 1.
InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
InterPro; IPR014276; 2-oxoglutarate_DH_E2.
InterPro; IPR000089; Biotin_lipoyl.
InterPro; IPR004167; E3-bd.
InterPro; IPR036625; E3-bd_dom_sf.
InterPro; IPR011053; Single_hybrid_motif.
Pfam; PF00198; 2-oxoacid_dh; 1.
Pfam; PF00364; Biotin_lipoyl; 2.
Pfam; PF02817; E3_binding; 1.
SUPFAM; SSF47005; SSF47005; 1.
SUPFAM; SSF51230; SSF51230; 2.
TIGRFAMs; TIGR02927; SucB_Actino; 1.
PROSITE; PS50968; BIOTINYL_LIPOYL; 2.
PROSITE; PS00189; LIPOYL; 2.
PROSITE; PS51826; PSBD; 1.
1: Evidence at protein level;
Acetylation; Acyltransferase; Antioxidant; Complete proteome;
Glycolysis; Lipoyl; Reference proteome; Repeat; Transferase;
Virulence.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:21969609}.
CHAIN 2 553 Dihydrolipoyllysine-residue
acetyltransferase component of pyruvate
dehydrogenase complex.
/FTId=PRO_0000162266.
DOMAIN 2 77 Lipoyl-binding 1. {ECO:0000255|PROSITE-
ProRule:PRU01066}.
DOMAIN 121 196 Lipoyl-binding 2. {ECO:0000255|PROSITE-
ProRule:PRU01066}.
DOMAIN 243 280 Peripheral subunit-binding (PSBD).
{ECO:0000255|PROSITE-ProRule:PRU01170}.
ACT_SITE 523 523 {ECO:0000250}.
ACT_SITE 527 527 {ECO:0000250}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:21969609}.
MOD_RES 43 43 N6-lipoyllysine. {ECO:0000255|PROSITE-
ProRule:PRU01066,
ECO:0000305|PubMed:11799204}.
MOD_RES 162 162 N6-lipoyllysine. {ECO:0000255|PROSITE-
ProRule:PRU01066,
ECO:0000305|PubMed:11799204}.
SEQUENCE 553 AA; 57088 MW; 54B6E70D23B804A7 CRC64;
MAFSVQMPAL GESVTEGTVT RWLKQEGDTV ELDEPLVEVS TDKVDTEIPS PAAGVLTKII
AQEDDTVEVG GELAVIGDAK DAGEAAAPAP EKVPAAQPES KPAPEPPPVQ PTSGAPAGGD
AKPVLMPELG ESVTEGTVIR WLKKIGDSVQ VDEPLVEVST DKVDTEIPSP VAGVLVSISA
DEDATVPVGG ELARIGVAAD IGAAPAPKPA PKPVPEPAPT PKAEPAPSPP AAQPAGAAEG
APYVTPLVRK LASENNIDLA GVTGTGVGGR IRKQDVLAAA EQKKRAKAPA PAAQAAAAPA
PKAPPAPAPA LAHLRGTTQK ASRIRQITAN KTRESLQATA QLTQTHEVDM TKIVGLRARA
KAAFAEREGV NLTFLPFFAK AVIDALKIHP NINASYNEDT KEITYYDAEH LGFAVDTEQG
LLSPVIHDAG DLSLAGLARA IADIAARARS GNLKPDELSG GTFTITNIGS QGALFDTPIL
VPPQAAMLGT GAIVKRPRVV VDASGNESIG VRSVCYLPLT YDHRLIDGAD AGRFLTTIKH
RLEEGAFEAD LGL


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