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   03-AUG-2022, entry version 89.
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; belli group.
OX   NCBI_TaxID=336407;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RML369-C;
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 in
RT   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 multiple
CC       copies of three enzymatic components: pyruvate dehydrogenase (E1),
CC       dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase
CC       (E3) (By similarity). {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000250};
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta chain.
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DR   EMBL; CP000087; ABE04340.1; -; Genomic_DNA.
DR   RefSeq; WP_011476952.1; NC_007940.1.
DR   AlphaFoldDB; Q1RJX4; -.
DR   SMR; Q1RJX4; -.
DR   STRING; 336407.RBE_0259; -.
DR   PRIDE; Q1RJX4; -.
DR   EnsemblBacteria; ABE04340; ABE04340; RBE_0259.
DR   KEGG; rbe:RBE_0259; -.
DR   eggNOG; COG1071; Bacteria.
DR   HOGENOM; CLU_029393_5_2_5; -.
DR   OMA; FGMPGVT; -.
DR   OrthoDB; 1248201at2; -.
DR   Proteomes; UP000001951; Chromosome.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:InterPro.
DR   GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IEA:InterPro.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR   InterPro; IPR001017; DH_E1.
DR   InterPro; IPR017597; Pyrv_DH_E1_asu_subgrp-y.
DR   InterPro; IPR029061; THDP-binding.
DR   Pfam; PF00676; E1_dh; 1.
DR   SUPFAM; SSF52518; SSF52518; 1.
DR   TIGRFAMs; TIGR03182; PDH_E1_alph_y; 1.
PE   3: Inferred from homology;
KW   Glycolysis; Oxidoreductase; Pyruvate; Thiamine pyrophosphate.
FT   CHAIN           1..326
FT                   /note="Pyruvate dehydrogenase E1 component subunit alpha"
FT                   /id="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