ID   ODPA_MYCPN              Reviewed;         358 AA.
AC   P75390;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit alpha;
DE            EC=1.2.4.1;
GN   Name=pdhA; OrderedLocusNames=MPN_393; ORFNames=MP445;
OS   Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS   pneumoniae).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=272634;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29342 / M129;
RX   PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA   Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT   "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT   pneumoniae.";
RL   Nucleic Acids Res. 24:4420-4449(1996).
CC   -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
CC       conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple
CC       copies of three enzymatic components: pyruvate dehydrogenase (E1),
CC       dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase
CC       (E3) (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=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000250};
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta chain.
CC   -!- INTERACTION:
CC       P75390; P02788: LTF; Xeno; NbExp=3; IntAct=EBI-2259629, EBI-1058602;
CC       P75390; P00747: PLG; Xeno; NbExp=5; IntAct=EBI-2259629, EBI-999394;
CC       P75390; P04004: VTN; Xeno; NbExp=3; IntAct=EBI-2259629, EBI-1036653;
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DR   EMBL; U00089; AAB96093.1; -; Genomic_DNA.
DR   PIR; S73771; S73771.
DR   RefSeq; NP_110081.1; NC_000912.1.
DR   RefSeq; WP_010874749.1; NC_000912.1.
DR   AlphaFoldDB; P75390; -.
DR   SMR; P75390; -.
DR   IntAct; P75390; 7.
DR   STRING; 272634.MPN_393; -.
DR   EnsemblBacteria; AAB96093; AAB96093; MPN_393.
DR   GeneID; 66608948; -.
DR   KEGG; mpn:MPN_393; -.
DR   PATRIC; fig|272634.6.peg.424; -.
DR   HOGENOM; CLU_029393_1_0_14; -.
DR   OMA; GMFRGVN; -.
DR   BioCyc; MetaCyc:MON-586; -.
DR   BioCyc; MPNE272634:G1GJ3-623-MON; -.
DR   Proteomes; UP000000808; Chromosome.
DR   GO; GO:0009986; C:cell surface; IDA:AgBase.
DR   GO; GO:0005829; C:cytosol; IDA:AgBase.
DR   GO; GO:0016020; C:membrane; IDA:AgBase.
DR   GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR   InterPro; IPR001017; DH_E1.
DR   InterPro; IPR017596; PdhA/BkdA.
DR   InterPro; IPR029061; THDP-binding.
DR   PANTHER; PTHR11516:SF41; PTHR11516:SF41; 1.
DR   Pfam; PF00676; E1_dh; 1.
DR   SUPFAM; SSF52518; SSF52518; 1.
DR   TIGRFAMs; TIGR03181; PDH_E1_alph_x; 1.
PE   1: Evidence at protein level;
KW   Glycolysis; Oxidoreductase; Pyruvate; Reference proteome;
KW   Thiamine pyrophosphate.
FT   CHAIN           1..358
FT                   /note="Pyruvate dehydrogenase E1 component subunit alpha"
FT                   /id="PRO_0000162201"
SQ   SEQUENCE   358 AA;  40594 MW;  E6184A2026D7A143 CRC64;
     MAILIKNKVP TTLYQVYDNE GKLMDPNHKI TLSNEQLKHA FYLMNLSRIM DKKMLVWQRA
     GKMLNFAPNL GEEALQVGMG MGLNENDWFC PTFRSGALML YRGVKPEQLL LYWNGNENGS
     KIEAKYKTLP INITIGAQYS HAAGLGYMLH YKKLPNVAVT MIGDGGTAEG EFYEAMNIAS
     IHKWNSVFCI NNNQFAISTR TKLESAVSDL STKAIAVNIP RIRVDGNDLI ASYEAMHEAA
     NYARSGNGPV LIEFFSWRQG PHTTSDDPSI YRTKEEEAEA MKSDPVKRLR NFLFDRGILT
     PQQEEEMVAK IEQEVQAAYE VMVSKTPVTL DEVFDYNYEK LTPDLARQKA EAKKYFKD