ID   ODP1_MYCS2              Reviewed;         929 AA.
AC   A0R0B0; I7GD92;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Pyruvate dehydrogenase E1 component;
DE            Short=PDH E1 component;
DE            EC=1.2.4.1;
GN   Name=aceE; OrderedLocusNames=MSMEG_4323, MSMEI_4223;
OS   Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS   smegmatis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=246196;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RA   Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA   Fraser C.M.;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA   Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA   Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT   "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT   mutations or sequencing errors?";
RL   Genome Biol. 8:R20.1-R20.9(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=18955433; DOI=10.1101/gr.081901.108;
RA   Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA   Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT   "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT   and a new MS-based protocol.";
RL   Genome Res. 19:128-135(2009).
RN   [4]
RP   PUPYLATION AT LYS-375, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=20094657; DOI=10.1039/b916104j;
RA   Watrous J., Burns K., Liu W.T., Patel A., Hook V., Bafna V.,
RA   Barry C.E. III, Bark S., Dorrestein P.C.;
RT   "Expansion of the mycobacterial 'PUPylome'.";
RL   Mol. Biosyst. 6:376-385(2010).
CC   -!- FUNCTION: Component of the pyruvate dehydrogenase (PDH) complex, that
CC       catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2).
CC       AceE has reductase activity with pyruvate but does not react with 2-
CC       oxoglutarate (By similarity). {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000250};
CC   -!- SUBUNIT: Homodimer. Part of the PDH complex, consisting of multiple
CC       copies of AceE (E1), DlaT (E2) and Lpd (E3). {ECO:0000250}.
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; CP000480; ABK72760.1; -; Genomic_DNA.
DR   EMBL; CP001663; AFP40679.1; -; Genomic_DNA.
DR   RefSeq; WP_011729733.1; NZ_SIJM01000003.1.
DR   RefSeq; YP_888598.1; NC_008596.1.
DR   AlphaFoldDB; A0R0B0; -.
DR   SMR; A0R0B0; -.
DR   STRING; 246196.MSMEI_4223; -.
DR   PRIDE; A0R0B0; -.
DR   EnsemblBacteria; ABK72760; ABK72760; MSMEG_4323.
DR   EnsemblBacteria; AFP40679; AFP40679; MSMEI_4223.
DR   GeneID; 66735668; -.
DR   KEGG; msg:MSMEI_4223; -.
DR   KEGG; msm:MSMEG_4323; -.
DR   PATRIC; fig|246196.19.peg.4241; -.
DR   eggNOG; COG2609; Bacteria.
DR   OMA; PDEYRTF; -.
DR   OrthoDB; 49937at2; -.
DR   Proteomes; UP000000757; Chromosome.
DR   Proteomes; UP000006158; 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   1: Evidence at protein level;
KW   Glycolysis; Isopeptide bond; Magnesium; Oxidoreductase; Pyruvate;
KW   Reference proteome; Thiamine pyrophosphate; Ubl conjugation.
FT   CHAIN           1..929
FT                   /note="Pyruvate dehydrogenase E1 component"
FT                   /id="PRO_0000396809"
FT   CROSSLNK        375
FT                   /note="Isoglutamyl lysine isopeptide (Lys-Gln) (interchain
FT                   with Q-Cter in protein Pup)"
FT                   /evidence="ECO:0000269|PubMed:20094657"
SQ   SEQUENCE   929 AA;  103077 MW;  5CB137A1D69BFB23 CRC64;
     MTTEFVRQDL AQNSSTAAEP DRVRVIREGV ASYLPDIDTE ETAEWLESFD ELLERSGPAR
     ARYLMLRLLE RAGEQRVAIP ALTSTDYVNT IPTELEPWFP GDEDVERRYR AWIRWNAAIM
     VHRAQRPGVG VGGHISTYAS SATLYEVGFN HFFRGKSHPG GGDHVFIQGH ASPGIYARAF
     LEGRLTTDQL DGFRQEHSHS GGGLPSYPHP RLMPDFWEFP TVSMGLGPMN AIYQARFNHY
     LHDRGIKDTS DQHVWAFLGD GEMDEPESRG LIQVAANEAL DNLTFVINCN LQRLDGPVRG
     NGKIIQELES FFRGAGWNVI KVVWGREWDV LLHADRDGAL VNLMNSTPDG DYQTYKANDG
     AYVRDHFFGR DPRTKALVAD MSDQEIWNLK RGGHDYRKVY AAYRAAMEHK GQPTVILAKT
     IKGYTLGQHF EGRNATHQMK KLALEDLKNF RDVTRVPVSD AQLEEDPYLP PYYHPGPEAP
     EIRYLLERRR ALGGFVPSRR TKSKPLALPG SDTYKALKKG SGSQAVATTM ATVRTFKELL
     RDKNIGPRIV PIIPDEARTF GMDSWFPSLK IYNRNGQLYT SVDSELMLAY KESEVGQILH
     EGINEAGSTS SFTAVGTSYS THDEPMIPIY IFYSMFGFQR TGDGLWAAAD QMARGFVLGA
     TAGRTTLTGE GLQHADGHSL LLASTNPAAV TYDPAFAYEI AHIIESGLQR MYGEDPENVF
     FYLTIYNEPY QQPAEPENLD VEALLKGLYL YRPAPEKRAK SAQILASGVA MPEALRAADL
     LASDWDVAAD VWSVTSWGEL NREGVAIEKH RLRHPDEPAG TPHVTSALAD AAGPVIAVSD
     WMRAVPEQIR PWVPGTYVTL GTDGFGFSDT RPAARRYFNT DAESVVVAVL QGLARDGEID
     ASVAAQAAEQ YRIDDVSAAG VSYADTGSA