ID   ODPA_RICFE              Reviewed;         326 AA.
AC   Q4UKQ6;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit alpha;
DE            EC=1.2.4.1;
GN   Name=pdhA; OrderedLocusNames=RF_1020;
OS   Rickettsia felis (strain ATCC VR-1525 / URRWXCal2) (Rickettsia azadi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=315456;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-1525 / URRWXCal2;
RX   PubMed=15984913; DOI=10.1371/journal.pbio.0030248;
RA   Ogata H., Renesto P., Audic S., Robert C., Blanc G., Fournier P.-E.,
RA   Parinello H., Claverie J.-M., Raoult D.;
RT   "The genome sequence of Rickettsia felis identifies the first putative
RT   conjugative plasmid in an obligate intracellular parasite.";
RL   PLoS Biol. 3:1-12(2005).
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; CP000053; AAY61871.1; -; Genomic_DNA.
DR   RefSeq; WP_011271336.1; NC_007109.1.
DR   AlphaFoldDB; Q4UKQ6; -.
DR   SMR; Q4UKQ6; -.
DR   STRING; 315456.RF_1020; -.
DR   EnsemblBacteria; AAY61871; AAY61871; RF_1020.
DR   KEGG; rfe:RF_1020; -.
DR   eggNOG; COG1071; Bacteria.
DR   HOGENOM; CLU_029393_5_0_5; -.
DR   OMA; FGMPGVT; -.
DR   OrthoDB; 1248201at2; -.
DR   Proteomes; UP000008548; 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_0000288753"
SQ   SEQUENCE   326 AA;  36724 MW;  DFD9E71813DC1E81 CRC64;
     MDIKPKKYKP TKEEYIKSFK DMLLLRRFEE KCGQLYGMGE IGGFCHLYIG QEAVISAVDT
     VKQKGDSTIT SYRDHAHIIL AGTEPKYVLA ELMGRATGCS KGKGGSMHLF DIPNKFYGGH
     GIVGAQVPIG TGLAFAEKYN GTNNICFTFL GDGAVNQGQV YEAFNMAALW GLPVVYIIEN
     NEYSMGTSVA RSTFMRDLYK KGESFGIKGF QLDGMDFEEM YNGAKQAAEY VRENSFPLIL
     EVKTYRYRGH SMSDPAKYRS KEEVEQYKER DPLVIIRKTI LDNKYATEAD LKEIEQSVKE
     IVKEAVKFSE NSPLPDEGEL YTEVYC