ID   ODPA_STAES              Reviewed;         370 AA.
AC   Q8CPN3;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 108.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit alpha;
DE            EC=1.2.4.1;
GN   Name=pdhA; OrderedLocusNames=SE_0791;
OS   Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12228 / FDA PCI 1200;
RX   PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA   Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA   Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA   Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT   "Genome-based analysis of virulence genes in a non-biofilm-forming
RT   Staphylococcus epidermidis strain (ATCC 12228).";
RL   Mol. Microbiol. 49:1577-1593(2003).
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.
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DR   EMBL; AE015929; AAO04388.1; -; Genomic_DNA.
DR   RefSeq; NP_764346.1; NC_004461.1.
DR   RefSeq; WP_001831653.1; NZ_WBME01000031.1.
DR   AlphaFoldDB; Q8CPN3; -.
DR   SMR; Q8CPN3; -.
DR   STRING; 176280.SE_0791; -.
DR   PRIDE; Q8CPN3; -.
DR   EnsemblBacteria; AAO04388; AAO04388; SE_0791.
DR   GeneID; 50019070; -.
DR   KEGG; sep:SE_0791; -.
DR   PATRIC; fig|176280.10.peg.764; -.
DR   eggNOG; COG1071; Bacteria.
DR   HOGENOM; CLU_029393_1_0_9; -.
DR   OMA; GMFRGVN; -.
DR   Proteomes; UP000001411; Chromosome.
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   3: Inferred from homology;
KW   Glycolysis; Oxidoreductase; Pyruvate; Thiamine pyrophosphate.
FT   CHAIN           1..370
FT                   /note="Pyruvate dehydrogenase E1 component subunit alpha"
FT                   /id="PRO_0000162211"
SQ   SEQUENCE   370 AA;  41330 MW;  F691D1D8C2E3EEB4 CRC64;
     MAPKLQAQFD AVKVLNETQS KFEMVQILDE DGNVVNEDLV PDLTDEQLVE LMERMVWTRI
     LDQRSISLNR QGRLGFYAPT AGQEASQLAS QYALESEDFI LPGYRDVPQI IWHGLPLTDA
     FLFSRGHFKG NQFPEGVNAL SPQIIIGAQY IQTAGVAFGL KKRGKNAVAI TYTGDGGSSQ
     GDFYEGINFA SAYKAPAIFV IQNNNYAIST PRSKQTAAET LAQKAISVGI PGIQVDGMDA
     LAVYQATLEA RERAVAGEGP TVIETLTYRY GPHTMAGDDP TRYRTSDEDA EWEKKDPLVR
     FRKYLEAKGL WNEDKENEVV ERAKSEIKAA IKEADNTEKQ TVTSLMDIMY EEMPQNLAEQ
     YEIYKEKESK