ID   ODPA_BACCE              Reviewed;         371 AA.
AC   Q4MTG0; P83068; P83070;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   16-JUN-2009, entry version 20.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit alpha;
DE            EC=1.2.4.1;
GN   Name=pdhA; ORFNames=BCE_G9241_3962;
OS   Bacillus cereus.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=1396;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=G9241;
RX   PubMed=15155910; DOI=10.1073/pnas.0402414101;
RA   Hoffmaster A.R., Ravel J., Rasko D.A., Chapman G.D., Chute M.D.,
RA   Marston C.K., De B.K., Sacchi C.T., Fitzgerald C., Mayer L.W.,
RA   Maiden M.C.J., Priest F.G., Barker M., Jiang L., Cer R.Z.,
RA   Rilstone J., Peterson S.N., Weyant R.S., Galloway D.R., Read T.D.,
RA   Popovic T., Fraser C.M.;
RT   "Identification of anthrax toxin genes in a Bacillus cereus associated
RT   with an illness resembling inhalation anthrax.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:8449-8454(2004).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-21, AND INDUCTION.
RC   STRAIN=NCIMB 11796 / DSM 626;
RX   PubMed=11872115; DOI=10.1046/j.1365-2672.2002.01541.x;
RA   Browne N., Dowds B.C.A.;
RT   "Acid stress in the food pathogen Bacillus cereus.";
RL   J. Appl. Microbiol. 92:404-414(2002).
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.
CC   -!- INDUCTION: By acid stress. Under acid-stress, this protein is
CC       expressed at a higher level in wild-type B.cereus than in the
CC       acid-sensitive mutant strain NB1.
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DR   EMBL; AAEK01000007; EAL15457.1; -; Genomic_DNA.
DR   SMR; Q4MTG0; 10-371.
DR   BRENDA; 1.2.4.1; 604.
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   GO; GO:0006950; P:response to stress; 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   1: Evidence at protein level;
KW   Direct protein sequencing; Glycolysis; Oxidoreductase; Pyruvate;
KW   Stress response; Thiamine pyrophosphate.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    371       Pyruvate dehydrogenase E1 component
FT                                subunit alpha.
FT                                /FTId=PRO_0000271255.
SQ   SEQUENCE   371 AA;  41441 MW;  884A8A94D6084451 CRC64;
     MGTKTKKTLF NVDEQMKAIA AQFETLQILN EKGEVVNEAA MPELSDDQLK ELMRRMVYTR
     VLDQRSISLN RQGRLGFYAP TAGQEASQLA SHFALEAEDF ILPGYRDVPQ LVWHGLPLYQ
     AFLFSRGHFM GNQMPENVNA LAPQIIIGAQ IIQTAGVALG MKLRGKKSVA ITYTGDGGAS
     QGDFYEGMNF AGAFKAPAIF VVQNNRYAIS TPVEKQSAAK TVAQKAVAAG IYGIQVDGMD
     PLAVYAATAF ARERAVNGEG PTLIETLTFR YGPHTMAGDD PTRYRTKDIE NEWEQKDPIV
     RFRAFLENKG LWSQEVEEKV IEEAKEDIKQ AIAKADQAPK QKVTDLMEIM YEKMPYNLAE
     QYEIYKEKES K
//