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 18-JAN-2017, entry version 49.
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.,
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] {ECO:0000305}
RP PROTEIN SEQUENCE OF 2-21, AND INDUCTION.
RC STRAIN=NCIMB 11796 / DSM 626 {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
CC multiple copies of three enzymatic components: pyruvate
CC dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and
CC lipoamide dehydrogenase (E3) (By similarity).
CC {ECO:0000250|UniProtKB:P21873}.
CC -!- CATALYTIC ACTIVITY: Pyruvate + [dihydrolipoyllysine-residue
CC acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue
CC acetyltransferase] S-acetyldihydrolipoyllysine + CO(2).
CC {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
CC expressed at a higher level in wild-type B.cereus than in the
CC acid-sensitive mutant strain NB1. {ECO:0000269|PubMed:11872115}.
DR EMBL; AAEK01000007; EAL15457.1; -; Genomic_DNA.
DR RefSeq; WP_000536893.1; NZ_MDYW01000047.1.
DR ProteinModelPortal; Q4MTG0; -.
DR STRING; 226900.BC3973; -.
DR EnsemblBacteria; EAL15457; EAL15457; BCE_G9241_3962.
DR GeneID; 29404794; -.
DR PATRIC; 24955467; VBIBacCer116370_1693.
DR eggNOG; COG1071; LUCA.
DR GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-EC.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.970; -; 1.
DR InterPro; IPR001017; DH_E1.
DR InterPro; IPR017596; PdhA/BkdA.
DR InterPro; IPR029061; THDP-binding.
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 1 Removed. {ECO:0000269|PubMed:11872115}.
FT CHAIN 2 371 Pyruvate dehydrogenase E1 component
FT subunit alpha.
FT /FTId=PRO_0000271255.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 53 343 ipfam:E1_dh [T]
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
//
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