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   04-NOV-2008, entry version 59.
DE   RecName: Full=Pyruvate dehydrogenase E1 component;
DE            EC=1.2.4.1;
GN   Name=aceE; OrderedLocusNames=HI1233;
OS   Haemophilus influenzae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=727;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   MEDLINE=95350630; PubMed=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.,
RA   Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D.,
RA   Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C.,
RA   Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M.,
RA   Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O.,
RA   Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
CC   -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
CC       conversion of pyruvate to acetyl-CoA and CO(2). It contains
CC       multiple copies of three enzymatic components: pyruvate
CC       dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and
CC       lipoamide dehydrogenase (E3) (By similarity).
CC   -!- CATALYTIC ACTIVITY: Pyruvate + [dihydrolipoyllysine-residue
CC       acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue
CC       acetyltransferase] S-acetyldihydrolipoyllysine + CO(2).
CC   -!- COFACTOR: Thiamine pyrophosphate (By similarity).
CC   -!- SUBUNIT: Homodimer (By similarity).
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DR   EMBL; L42023; AAC22886.1; -; Genomic_DNA.
DR   PIR; A64112; A64112.
DR   RefSeq; NP_439389.1; -.
DR   HSSP; P06958; 1L8A.
DR   GeneID; 950116; -.
DR   GenomeReviews; L42023_GR; HI1233.
DR   KEGG; hin:HI1233; -.
DR   NMPDR; fig|71421.1.peg.1179; -.
DR   TIGR; HI1233; -.
DR   HOGENOM; P45119; -.
DR   BioCyc; HINF71421:HI_1233-MON; -.
DR   GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring...; IEA:EC.
DR   GO; GO:0006096; P:glycolysis; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR004660; 2-oxoA_DHase_E1.
DR   InterPro; IPR015941; Transketolase_C-like.
DR   Gene3D; G3DSA:3.40.50.920; Transketo_C_like; 1.
DR   PIRSF; PIRSF000156; Pyruvate_dh_E1; 1.
DR   TIGRFAMs; TIGR00759; aceE; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Glycolysis; Oxidoreductase; Pyruvate;
KW   Thiamine pyrophosphate.
FT   CHAIN         1    886       Pyruvate dehydrogenase E1 component.
FT                                /FTId=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
//