ID   ODP1_CUPNH              Reviewed;         895 AA.
AC   Q59097; Q0KBW1;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 132.
DE   RecName: Full=Pyruvate dehydrogenase E1 component;
DE            Short=PDH E1 component;
DE            EC=1.2.4.1;
GN   Name=pdhA; OrderedLocusNames=H16_A1374;
OS   Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442
OS   / H16 / Stanier 337) (Ralstonia eutropha).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=381666;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8021225; DOI=10.1128/jb.176.14.4394-4408.1994;
RA   Hein S., Steinbuechel A.;
RT   "Biochemical and molecular characterization of the Alcaligenes eutrophus
RT   pyruvate dehydrogenase complex and identification of a new type of
RT   dihydrolipoamide dehydrogenase.";
RL   J. Bacteriol. 176:4394-4408(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337;
RX   PubMed=16964242; DOI=10.1038/nbt1244;
RA   Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R.,
RA   Eitinger T., Ewering C., Poetter M., Schwartz E., Strittmatter A., Voss I.,
RA   Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.;
RT   "Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia
RT   eutropha H16.";
RL   Nat. Biotechnol. 24:1257-1262(2006).
CC   -!- FUNCTION: Component of the pyruvate dehydrogenase (PDH) complex, that
CC       catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2).
CC       {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: Homodimer. Part of the PDH complex, consisting of multiple
CC       copies of pyruvate dehydrogenase (E1), dihydrolipoamide
CC       acetyltransferase (E2) and lipoamide dehydrogenase (E3). {ECO:0000250}.
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DR   EMBL; U09865; AAA21598.1; -; Genomic_DNA.
DR   EMBL; AM260479; CAJ92510.1; -; Genomic_DNA.
DR   PIR; A55514; A55514.
DR   RefSeq; WP_011615027.1; NZ_CP039287.1.
DR   AlphaFoldDB; Q59097; -.
DR   SMR; Q59097; -.
DR   STRING; 381666.H16_A1374; -.
DR   PRIDE; Q59097; -.
DR   EnsemblBacteria; CAJ92510; CAJ92510; H16_A1374.
DR   GeneID; 57643473; -.
DR   KEGG; reh:H16_A1374; -.
DR   PATRIC; fig|381666.6.peg.1763; -.
DR   eggNOG; COG2609; Bacteria.
DR   HOGENOM; CLU_009154_2_0_4; -.
DR   OMA; PDEYRTF; -.
DR   OrthoDB; 49937at2; -.
DR   Proteomes; UP000008210; Chromosome 1.
DR   GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR   CDD; cd02017; TPP_E1_EcPDC_like; 1.
DR   Gene3D; 3.40.50.920; -; 1.
DR   InterPro; IPR035807; PDC_E1_N.
DR   InterPro; IPR004660; PDH_E1.
DR   InterPro; IPR041621; PDH_E1_M.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   InterPro; IPR005474; Transketolase_N.
DR   PANTHER; PTHR43825:SF3; PTHR43825:SF3; 1.
DR   Pfam; PF17831; PDH_E1_M; 1.
DR   Pfam; PF00456; Transketolase_N; 1.
DR   PIRSF; PIRSF000156; Pyruvate_dh_E1; 1.
DR   SUPFAM; SSF52518; SSF52518; 2.
DR   SUPFAM; SSF52922; SSF52922; 1.
DR   TIGRFAMs; TIGR00759; aceE; 1.
PE   3: Inferred from homology;
KW   Glycolysis; Oxidoreductase; Pyruvate; Reference proteome;
KW   Thiamine pyrophosphate.
FT   CHAIN           1..895
FT                   /note="Pyruvate dehydrogenase E1 component"
FT                   /id="PRO_0000162238"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   895 AA;  100365 MW;  522A9A3C43454051 CRC64;
     MSAVPEQILG ASSANDADPQ ETHEWLDALQ GVLAAEGPAR AAFLIDKQIE YARVNGVTQP
     FHAETQYINT IPVEQQARIP GDQDIEHRIR SYTRWNAMAM VLRANKHTNV GGHISSFASA
     ATLYDVGYNH FWRAPSEAGG GDLVFVQGHS APGVYSRAFL LGRLTQDQLD NFRQEVDGKG
     ISSYPHPWLM PDFWQFPTVS MGLGPIMAIY QARFMKYLDS RGLAKAGDRK VWAFLGDGET
     DEPESLGAIG MAGREKLDNL VFVINCNLQR LDGPVRGNGK IIQELESEFR GAGWNVIKVV
     WGSKWDSLLA RDTKGLLMKR MMECVDGEYQ TMKAKDGAYV REHFFNTPEL KAMVADWSDD
     DIWRLNRGGH DPHKIYAAYK AASEHKGQPT LILAKTIKGY GMGDAGQAMN VAHQQKKMPV
     DAIRKFRDQF NLPVADDQLE EVPYITFPEG SKELEYMRQA RQNLGGYLPA RRQKAEALPV
     PQLSAFDALL KATGEGREVS TTMAFVRILN TLLKDKQIGK HVVPIVPDES RTFGMEGLFR
     QVGIWNQEGQ KYVPEDHDQL MFYKESQTGQ VLQEGINEAG AMCDWIAAAT SYSTHGVQMI
     PFYIYYSMFG IQRIGDLCWA AADMRSRGFL LGGTAGRTTL NGEGLQHEDG HSHVFHAAIP
     NCISYDPTFQ YELAVVMQDG LRRMYAEQED VYYYLTVMNE NYEHPEMPAG VEQDIVKGMY
     QFRKGVENSN APRVQLLGSG TIFREVIAAA DLLKKDWGVE SDLWGCPSFT ELAREGHDVE
     RFNLLHPTET PRESHVAKSL KSARGPVIAS TDYVRAFAEQ IRPFVPRRYV VLGTDGFGRS
     DTREKLRHFF EVDRYWVTLA ALKALADEGA IGRDKVAEAI KKYNLDPNKP NPMSV