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   16-JUN-2009, entry version 42.
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).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=176280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=22832016; PubMed=12950922;
RX   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.,
RA   Qin Z.-Q., Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z.,
RA   Yuan Z.-H., 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
CC       multiple copies of three enzymatic components: pyruvate
CC       dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and
CC       lipoamide dehydrogenase (E3) (By similarity).
CC   -!- CATALYTIC ACTIVITY: Pyruvate + [dihydrolipoyllysine-residue
CC       acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue
CC       acetyltransferase] S-acetyldihydrolipoyllysine + CO(2).
CC   -!- COFACTOR: Thiamine pyrophosphate (By similarity).
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; -.
DR   HSSP; P12694; 1DTW.
DR   SMR; Q8CPN3; 8-370.
DR   GeneID; 1057335; -.
DR   GenomeReviews; AE015929_GR; SE_0791.
DR   KEGG; sep:SE0791; -.
DR   HOGENOM; Q8CPN3; -.
DR   OMA; Q8CPN3; HSTAGDD.
DR   BioCyc; SEPI176280:SE_0791-MON; -.
DR   GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring...; IEA:EC.
DR   GO; GO:0030976; F:thiamin pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0006096; P:glycolysis; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR001017; DH_E1.
DR   InterPro; IPR017596; Pyrv_DH_E1_asu_subgrp-x.
DR   Pfam; PF00676; E1_dh; 1.
DR   TIGRFAMs; TIGR03181; PDH_E1_alph_x; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Glycolysis; Oxidoreductase; Pyruvate;
KW   Thiamine pyrophosphate.
FT   CHAIN         1    370       Pyruvate dehydrogenase E1 component
FT                                subunit alpha.
FT                                /FTId=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
//