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   25-MAY-2022, entry version 75.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit alpha;
DE            EC=1.2.4.1;
GN   Name=pdhA {ECO:0000312|EMBL:EAL15457.1}; ORFNames=BCE_G9241_3962;
OS   Bacillus cereus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=1396;
RN   [1] {ECO:0000312|EMBL:EAL15457.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=G9241 {ECO:0000312|EMBL:EAL15457.1};
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., Rilstone J.,
RA   Peterson S.N., Weyant R.S., Galloway D.R., Read T.D., Popovic T.,
RA   Fraser C.M.;
RT   "Identification of anthrax toxin genes in a Bacillus cereus associated with
RT   an illness resembling inhalation anthrax.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:8449-8454(2004).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 2-21, AND INDUCTION.
RC   STRAIN=DSM 626 / NCIMB 11796 / T {ECO:0000269|PubMed:11872115};
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 multiple
CC       copies of three enzymatic components: pyruvate dehydrogenase (E1),
CC       dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase
CC       (E3) (By similarity). {ECO:0000250|UniProtKB:P21873}.
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         Evidence={ECO:0000250|UniProtKB:P21873};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000250|UniProtKB:P21873};
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta chain. {ECO:0000305}.
CC   -!- INDUCTION: By acid stress. Under acid-stress, this protein is expressed
CC       at a higher level in wild-type B.cereus than in the acid-sensitive
CC       mutant strain NB1. {ECO:0000269|PubMed:11872115}.
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DR   EMBL; AAEK01000007; EAL15457.1; -; Genomic_DNA.
DR   RefSeq; WP_000536893.1; NZ_VVXM01000005.1.
DR   AlphaFoldDB; Q4MTG0; -.
DR   SMR; Q4MTG0; -.
DR   STRING; 1396.DJ87_889; -.
DR   GeneID; 59155465; -.
DR   GeneID; 64199314; -.
DR   eggNOG; COG1071; Bacteria.
DR   OMA; GMFRGVN; -.
DR   OrthoDB; 1248201at2; -.
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   Direct protein sequencing; Glycolysis; Oxidoreductase; Pyruvate;
KW   Stress response; Thiamine pyrophosphate.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:11872115"
FT   CHAIN           2..371
FT                   /note="Pyruvate dehydrogenase E1 component subunit alpha"
FT                   /id="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