ID   ODP1_MYCTO              Reviewed;         930 AA.
AC   P9WIS8; L0TBX6; Q10504;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   07-JAN-2015, sequence version 2.
DT   03-AUG-2022, entry version 40.
DE   RecName: Full=Pyruvate dehydrogenase E1 component {ECO:0000250|UniProtKB:P9WIS9};
DE            Short=PDH E1 component {ECO:0000305};
DE            EC=1.2.4.1 {ECO:0000250|UniProtKB:P9WIS9};
GN   Name=aceE; OrderedLocusNames=MT2301;
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 pyruvate dehydrogenase (PDH) complex, that
CC       catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2).
CC       {ECO:0000250, ECO:0000250|UniProtKB:P9WIS9}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue
CC         acetyltransferase] + H(+) + pyruvate = (R)-N(6)-(S(8)-
CC         acetyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue
CC         acetyltransferase] + CO2; Xref=Rhea:RHEA:19189, Rhea:RHEA-COMP:10480,
CC         Rhea:RHEA-COMP:10481, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:83099, ChEBI:CHEBI:83111; EC=1.2.4.1;
CC         Evidence={ECO:0000250|UniProtKB:P9WIS9};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P9WIS9};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000250|UniProtKB:P9WIS9};
CC   -!- SUBUNIT: Homodimer. Part of the PDH complex, consisting of multiple
CC       copies of AceE (E1), DlaT (E2) and Lpd (E3) (By similarity).
CC       {ECO:0000250|UniProtKB:P9WIS9}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK46585.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000250|UniProtKB:P9WIS9};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE000516; AAK46585.1; ALT_INIT; Genomic_DNA.
DR   PIR; E70778; E70778.
DR   RefSeq; WP_003911788.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WIS8; -.
DR   SMR; P9WIS8; -.
DR   EnsemblBacteria; AAK46585; AAK46585; MT2301.
DR   GeneID; 45426221; -.
DR   KEGG; mtc:MT2301; -.
DR   HOGENOM; CLU_009154_2_0_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR   GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR   CDD; cd02017; TPP_E1_EcPDC_like; 1.
DR   Gene3D; 3.40.50.920; -; 1.
DR   InterPro; IPR035807; PDC_E1_N.
DR   InterPro; IPR004660; PDH_E1.
DR   InterPro; IPR041621; PDH_E1_M.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   InterPro; IPR005474; Transketolase_N.
DR   PANTHER; PTHR43825:SF3; PTHR43825:SF3; 1.
DR   Pfam; PF17831; PDH_E1_M; 1.
DR   Pfam; PF00456; Transketolase_N; 1.
DR   PIRSF; PIRSF000156; Pyruvate_dh_E1; 1.
DR   SUPFAM; SSF52518; SSF52518; 2.
DR   SUPFAM; SSF52922; SSF52922; 1.
DR   TIGRFAMs; TIGR00759; aceE; 1.
PE   3: Inferred from homology;
KW   Glycolysis; Magnesium; Oxidoreductase; Pyruvate; Thiamine pyrophosphate.
FT   CHAIN           1..930
FT                   /note="Pyruvate dehydrogenase E1 component"
FT                   /id="PRO_0000427952"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   930 AA;  103440 MW;  6542FF8373756D53 CRC64;
     MTTDFARHDL AQNSNSASEP DRVRVIREGV ASYLPDIDPE ETSEWLESFD TLLQRCGPSR
     ARYLMLRLLE RAGEQRVAIP ALTSTDYVNT IPTELEPWFP GDEDVERRYR AWIRWNAAIM
     VHRAQRPGVG VGGHISTYAS SAALYEVGFN HFFRGKSHPG GGDQVFIQGH ASPGIYARAF
     LEGRLTAEQL DGFRQEHSHV GGGLPSYPHP RLMPDFWEFP TVSMGLGPLN AIYQARFNHY
     LHDRGIKDTS DQHVWCFLGD GEMDEPESRG LAHVGALEGL DNLTFVINCN LQRLDGPVRG
     NGKIIQELES FFRGAGWNVI KVVWGREWDA LLHADRDGAL VNLMNTTPDG DYQTYKANDG
     GYVRDHFFGR DPRTKALVEN MSDQDIWNLK RGGHDYRKVY AAYRAAVDHK GQPTVILAKT
     IKGYALGKHF EGRNATHQMK KLTLEDLKEF RDTQRIPVSD AQLEENPYLP PYYHPGLNAP
     EIRYMLDRRR ALGGFVPERR TKSKALTLPG RDIYAPLKKG SGHQEVATTM ATVRTFKEVL
     RDKQIGPRIV PIIPDEARTF GMDSWFPSLK IYNRNGQLYT AVDADLMLAY KESEVGQILH
     EGINEAGSVG SFIAAGTSYA THNEPMIPIY IFYSMFGFQR TGDSFWAAAD QMARGFVLGA
     TAGRTTLTGE GLQHADGHSL LLAATNPAVV AYDPAFAYEI AYIVESGLAR MCGENPENIF
     FYITVYNEPY VQPPEPENFD PEGVLRGIYR YHAATEQRTN KAQILASGVA MPAALRAAQM
     LAAEWDVAAD VWSVTSWGEL NRDGVAIETE KLRHPDRPAG VPYVTRALEN ARGPVIAVSD
     WMRAVPEQIR PWVPGTYLTL GTDGFGFSDT RPAARRYFNT DAESQVVAVL EALAGDGEID
     PSVPVAAARQ YRIDDVAAAP EQTTDPGPGA