ID   ODPA_RICBR              Reviewed;         326 AA.
AC   Q1RJX4;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   16-JUN-2009, entry version 24.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit alpha;
DE            EC=1.2.4.1;
GN   Name=pdhA; OrderedLocusNames=RBE_0259;
OS   Rickettsia bellii (strain RML369-C).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia.
OX   NCBI_TaxID=336407;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16703114; DOI=10.1371/journal.pgen.0020076;
RA   Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C.,
RA   Fournier P.-E., Claverie J.-M., Raoult D.;
RT   "Genome sequence of Rickettsia bellii illuminates the role of amoebae
RT   in gene exchanges between intracellular pathogens.";
RL   PLoS Genet. 2:733-744(2006).
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; CP000087; ABE04340.1; -; Genomic_DNA.
DR   RefSeq; YP_537429.1; -.
DR   GeneID; 3995883; -.
DR   GenomeReviews; CP000087_GR; RBE_0259.
DR   KEGG; rbe:RBE_0259; -.
DR   HOGENOM; Q1RJX4; -.
DR   OMA; Q1RJX4; YAMGTST.
DR   BioCyc; RBEL336407:RBE_0259-MON; -.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:InterPro.
DR   GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring...; IEA:EC.
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; IPR017597; Pyrv_DH_E1_asu_subgrp-y.
DR   Pfam; PF00676; E1_dh; 1.
DR   TIGRFAMs; TIGR03182; PDH_E1_alph_y; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Glycolysis; Oxidoreductase; Pyruvate;
KW   Thiamine pyrophosphate.
FT   CHAIN         1    326       Pyruvate dehydrogenase E1 component
FT                                subunit alpha.
FT                                /FTId=PRO_0000288752.
SQ   SEQUENCE   326 AA;  36853 MW;  36F16A727359D2E1 CRC64;
     MDIKLGKYKP VKEEYIKSFK DMLLLRRFEE KCGQLYGMGE IGGFCHLYIG QEAVISAVDM
     VKQKEDSMVT SYRDHAHIIL AGTEPKYVLA ELMGRATGCS KGKGGSMHLF DVPNKFYGGH
     GIVGAQVPIG TGLAFAEKYN GTNNICFTFL GDGAVNQGQV YEAFNMAALW GLPVVYIIEN
     NEYSMGTSVA RSTFMRDLYK KGESFGIKGF QLNGMDFEEM YDGVKQAAEY VRENSMPLIL
     EVKTYRYRGH SMSDPAKYRS KEEVETYKER DPITEIRKII LENNYASEAD LKEIEQSVKE
     IVKEAVEFSE NSPLPNEEEL YTQIYV
//