ID   ODP1_PSEAE              Reviewed;         882 AA.
AC   Q59637; Q9HUF3;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2001, sequence version 2.
DT   03-AUG-2022, entry version 135.
DE   RecName: Full=Pyruvate dehydrogenase E1 component;
DE            Short=PDH E1 component;
DE            EC=1.2.4.1;
GN   Name=aceE; Synonyms=aceA; OrderedLocusNames=PA5015;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=PAO;
RX   PubMed=9171401; DOI=10.1128/jb.179.11.3561-3571.1997;
RA   Rae J.L., Cutfield J.F., Lamont I.L.;
RT   "Sequences and expression of pyruvate dehydrogenase genes from Pseudomonas
RT   aeruginosa.";
RL   J. Bacteriol. 179:3561-3571(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(2000).
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; U47920; AAC45353.1; -; Genomic_DNA.
DR   EMBL; AE004091; AAG08400.1; -; Genomic_DNA.
DR   PIR; G83018; G83018.
DR   RefSeq; NP_253702.1; NC_002516.2.
DR   RefSeq; WP_003114556.1; NZ_QZGE01000002.1.
DR   AlphaFoldDB; Q59637; -.
DR   SMR; Q59637; -.
DR   STRING; 287.DR97_2370; -.
DR   PaxDb; Q59637; -.
DR   PRIDE; Q59637; -.
DR   EnsemblBacteria; AAG08400; AAG08400; PA5015.
DR   GeneID; 881326; -.
DR   KEGG; pae:PA5015; -.
DR   PATRIC; fig|208964.12.peg.5255; -.
DR   PseudoCAP; PA5015; -.
DR   HOGENOM; CLU_009154_2_0_6; -.
DR   InParanoid; Q59637; -.
DR   OMA; PDEYRTF; -.
DR   PhylomeDB; Q59637; -.
DR   BioCyc; PAER208964:G1FZ6-5131-MON; -.
DR   Proteomes; UP000002438; Chromosome.
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..882
FT                   /note="Pyruvate dehydrogenase E1 component"
FT                   /id="PRO_0000162247"
FT   CONFLICT        76..78
FT                   /note="IRS -> DPLP (in Ref. 1; AAC45353)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        149..156
FT                   /note="EGRISEEQ -> GRPHQRRNK (in Ref. 1; AAC45353)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        167..174
FT                   /note="NGLSSYPH -> TACPPIRT (in Ref. 1; AAC45353)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        377
FT                   /note="Q -> H (in Ref. 1; AAC45353)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        388
FT                   /note="G -> V (in Ref. 1; AAC45353)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        392
FT                   /note="G -> A (in Ref. 1; AAC45353)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        408..409
FT                   /note="Missing (in Ref. 1; AAC45353)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        517
FT                   /note="A -> G (in Ref. 1; AAC45353)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        671
FT                   /note="Missing (in Ref. 1; AAC45353)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        740
FT                   /note="R -> H (in Ref. 1; AAC45353)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        744..746
FT                   /note="GIG -> DIV (in Ref. 1; AAC45353)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        760..765
FT                   /note="RDGLAV -> HDDLTL (in Ref. 1; AAC45353)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        788..791
FT                   /note="GRRG -> APSR (in Ref. 1; AAC45353)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        821
FT                   /note="Missing (in Ref. 1; AAC45353)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   882 AA;  99564 MW;  5FD387B8332E24D9 CRC64;
     MQDLDPVETQ EWLDALESVL DREGEDRAHY LMTRMGELAS RSGTQLPYAI TTPYRNTIPV
     THEARMPGDL FMERRIRSLV RWNALAMVMR ANKHDPDLGG HISTFASSAT LYDIGFNYFF
     QAPTDEHGGD LVFFQGHASP GVYARAFLEG RISEEQLENF RQEVDGNGLS SYPHPWLMPD
     FWQFPTVSMG LGPIQAIYQA RFMKYLESRG FIPAGKQKVW CFMGDGECDE PESLGAISLA
     GREKLDNLIF VINCNLQRLD GPVRGNAKII QELEGVFRGA EWNVNKVIWG RFWDPLFAKD
     TAGLLQQRMD EVIDGEYQNY KAKDGAYVRE HFFGARPELL EMVKDLSDEE IWKLNRGGHD
     PYKVYAAYHQ AVNHKGQPTV ILAKTIKGYG TGSGEAKNIA HNVKKVDVDS LRAFRDKFDI
     PVKDADLEKL PFYKPEEGSA EAKYLAERRA ALGGFMPVRR QKSMSVPVPP LETLKAMLDG
     SGDREISTTM AFVRIISQLV KDKELGPRIV PIVPDEARTF GMEGMFRQLG IYSSVGQLYE
     PVDKDQVMFY REDKKGQILE EGINEAGAMS SWIAAGTSYS THNQPMLPFY IFYSMFGFQR
     IGDLAWAAGD SRAHGFLIGG TAGRTTLNGE GLQHEDGHSH LLASTIPNCR TYDPTYAYEL
     AVIIREGSRQ MIEEQQDIFY YITVMNENYV QPAMPKGAEE GIIKGMYLLE EDKKEAAHHV
     QLLGSGTILR EVEEAAKLLR NDFGIGADVW SVPSFNELRR DGLAVERWNR LHPGQKPKQS
     YVEECLGGRR GPVIASTDYM KLYAEQIRQW VPSKEYKVLG TDGFGRSDSR KKLRNFFEVD
     RHWVVLAALE ALADRGDIEP KVVAEAIAKY GIDPEKRNPL DC