ID   ODPA_RICTY              Reviewed;         326 AA.
AC   Q68XA9;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit alpha;
DE            EC=1.2.4.1;
GN   Name=pdhA; OrderedLocusNames=RT0252;
OS   Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=257363;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-144 / Wilmington;
RX   PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA   McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA   McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA   Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA   Yu X.-J., Walker D.H., Weinstock G.M.;
RT   "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT   of other Rickettsiae.";
RL   J. Bacteriol. 186:5842-5855(2004).
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; AE017197; AAU03733.1; -; Genomic_DNA.
DR   RefSeq; WP_011190718.1; NC_006142.1.
DR   AlphaFoldDB; Q68XA9; -.
DR   SMR; Q68XA9; -.
DR   STRING; 257363.RT0252; -.
DR   EnsemblBacteria; AAU03733; AAU03733; RT0252.
DR   KEGG; rty:RT0252; -.
DR   eggNOG; COG1071; Bacteria.
DR   HOGENOM; CLU_029393_5_0_5; -.
DR   OMA; FGMPGVT; -.
DR   OrthoDB; 1248201at2; -.
DR   Proteomes; UP000000604; 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_0000288754"
SQ   SEQUENCE   326 AA;  36905 MW;  C10B2065264A3A3C CRC64;
     MNIKPKKYKP IKEEYIKSFK DMLLLRRFEE KCGQLYGMGE IGGFCHLYIG QEAVISAVEL
     IKKKGDSTIT SYRDHAHIIL AGTEPKYVLA ELMGRATGCS KGKGGSMHLF DIPNKFYGGH
     GIVGAQVPIG TGLAFAEKYN GTNNICFTFL GDGAVNQGQV YEAFNMASLW GLPVVYIIEN
     NEYSMGTSVS RSTFMRDLYK KGESFGIRGF QLDGMDFEEM YNGTKQVAEY VRENSFPVIL
     EVKTYRYRGH SMSDPAKYRS KEEVAKYKER DTLVRIRQII LDNKYATEED LKAIERSVQE
     VIKVAVEFSE NSPLPSEDEL YTDIYV