ID   ODP1_HAEIN              Reviewed;         886 AA.
AC   P45119;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=Pyruvate dehydrogenase E1 component;
DE            Short=PDH E1 component;
DE            EC=1.2.4.1;
GN   Name=aceE; OrderedLocusNames=HI_1233;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
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; L42023; AAC22886.1; -; Genomic_DNA.
DR   PIR; A64112; A64112.
DR   RefSeq; NP_439389.1; NC_000907.1.
DR   RefSeq; WP_005694293.1; NC_000907.1.
DR   AlphaFoldDB; P45119; -.
DR   SMR; P45119; -.
DR   STRING; 71421.HI_1233; -.
DR   EnsemblBacteria; AAC22886; AAC22886; HI_1233.
DR   KEGG; hin:HI_1233; -.
DR   PATRIC; fig|71421.8.peg.1285; -.
DR   eggNOG; COG2609; Bacteria.
DR   HOGENOM; CLU_009154_2_0_6; -.
DR   OMA; PDEYRTF; -.
DR   PhylomeDB; P45119; -.
DR   BioCyc; HINF71421:G1GJ1-1264-MON; -.
DR   Proteomes; UP000000579; 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..886
FT                   /note="Pyruvate dehydrogenase E1 component"
FT                   /id="PRO_0000162245"
SQ   SEQUENCE   886 AA;  99131 MW;  1B936A75DD69E71D CRC64;
     MSEILKNDVD PIETQDWLQS LDSLIREEGV ERAQYIVEQV IGQARTSGVS LPTGVTTDYV
     NTIPVAEQPA YPGDHAIERR IRSAVRWNAI AMVLRSQKKD LDLGGHISTF QSAATMYEVC
     YNHFFKAATE KNGGDLIFFQ GHAAPGMYAR AFLEGRLTEE QMDNFRQEAF TDGLSSYPHP
     KLMPEFWQFS TVSMGLGPVN AIYQARFLKY LDNRGLKDTK DQKVYAFLGD GEMDEIESKG
     ALTFAAREHL DNLIFTISCN LQRLDGPVNG NGKIVQELEG LFTGAGWEVI KVLWGSDWDK
     LFAKDTSGKL TQLMMEVVDG DYLTFKSKDG AYIREHFFGR YPETAALVAD MTDDEIWALR
     RGAHDSEKLY AAYAKAQNAT KPVVILAHQV KGYKIPEAES KNTAHQSKKM SYESLKGFRD
     FFELPLTDEQ VEKLEYIKFA EGTPEYEYLH GHRKALNGYV PARRTKFDVE YKVPALEEFK
     ALLEEQPRGI STTMAFTRAL NILLKDKNIG KTIVPMIADE ARTFGMEGLF RQVGIYNPHG
     QNYIPSDRDL VAYYREAKDG QVLQEGINEL GATASWLAAA NSYSVNNQPM IPFFIYYSMF
     GFQRVGDMMW AAGDQLARGF MVGGTSGRTT LNGEGLQHED GHSHIQAGII PNCITYDPSF
     AFEVAVIMQD GINRMYGEKQ EDVFYYMTTL NEVMDQPAMP AGAEEGIRKG LYKFETVEGK
     KGKGHVQLLG SGAIMRHVRE AAQILANDYG VTSDVFSAPS FNELAREGHD AARWNLLHPT
     ETQRVPYVAQ VLADLPTVAS TDYVKGYADQ IRAFVPSKHY HVLGTDGFGR SDSRANLREH
     FEVDARYVVV AALSQLAKEG TVSNQVVADA IAKFGLNVDR INPLYA