(data stored in ACNUC7421 zone)

SWISSPROT: ODP1_ECO57

ID   ODP1_ECO57              Reviewed;         887 AA.
AC   P0AFG9; P06958; P78049; Q53382;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   08-MAY-2019, entry version 95.
DE   RecName: Full=Pyruvate dehydrogenase E1 component;
DE            Short=PDH E1 component;
DE            EC=1.2.4.1;
GN   Name=aceE; OrderedLocusNames=Z0124, ECs0118;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Component of the pyruvate dehydrogenase (PDH) complex,
CC       that catalyzes the overall conversion of pyruvate to acetyl-CoA
CC       and CO(2). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[dihydrolipoyllysine-residue acetyltransferase]-(R)-N(6)-
CC         lipoyl-L-lysine + H(+) + pyruvate = [dihydrolipoyllysine-residue
CC         acetyltransferase]-(R)-N(6)-(S(8)-acetyldihydrolipoyl)-L-lysine
CC         + CO2; Xref=Rhea:RHEA:19189, Rhea:RHEA-COMP:10480, Rhea:RHEA-
CC         COMP:10481, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:83099, ChEBI:CHEBI:83111;
CC         EC=1.2.4.1;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000250};
CC   -!- SUBUNIT: Homodimer. Part of the PDH complex, consisting of
CC       multiple copies of pyruvate dehydrogenase (E1), dihydrolipoamide
CC       acetyltransferase (E2) and lipoamide dehydrogenase (E3).
CC       {ECO:0000250}.
DR   EMBL; AE005174; AAG54418.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB33541.1; -; Genomic_DNA.
DR   PIR; F85494; F85494.
DR   PIR; F90643; F90643.
DR   RefSeq; NP_308145.1; NC_002695.1.
DR   RefSeq; WP_000003820.1; NZ_SDVX01000001.1.
DR   PDB; 3LPL; X-ray; 2.10 A; A/B=2-887.
DR   PDB; 3LQ2; X-ray; 1.96 A; A/B=2-887.
DR   PDB; 3LQ4; X-ray; 1.98 A; A/B=2-887.
DR   PDBsum; 3LPL; -.
DR   PDBsum; 3LQ2; -.
DR   PDBsum; 3LQ4; -.
DR   SMR; P0AFG9; -.
DR   IntAct; P0AFG9; 3.
DR   STRING; 155864.EDL933_0116; -.
DR   PRIDE; P0AFG9; -.
DR   EnsemblBacteria; AAG54418; AAG54418; Z0124.
DR   EnsemblBacteria; BAB33541; BAB33541; BAB33541.
DR   GeneID; 913657; -.
DR   KEGG; ece:Z0124; -.
DR   KEGG; ecs:ECs0118; -.
DR   PATRIC; fig|386585.9.peg.216; -.
DR   eggNOG; ENOG4105DAQ; Bacteria.
DR   eggNOG; COG2609; LUCA.
DR   HOGENOM; HOG000115215; -.
DR   KO; K00163; -.
DR   BioCyc; ECOO157:ACEE-MONOMER; -.
DR   EvolutionaryTrace; P0AFG9; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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   1: Evidence at protein level;
DR   PRODOM; P0AFG9.
DR   SWISS-2DPAGE; P0AFG9.
KW   3D-structure; Acetylation; Complete proteome; Glycolysis; Magnesium;
KW   Metal-binding; Oxidoreductase; Pyruvate; Reference proteome;
KW   Thiamine pyrophosphate.
FT   INIT_MET      1      1       Removed. {ECO:0000250}.
FT   CHAIN         2    887       Pyruvate dehydrogenase E1 component.
FT                                /FTId=PRO_0000162244.
FT   METAL       231    231       Magnesium. {ECO:0000250}.
FT   METAL       261    261       Magnesium. {ECO:0000250}.
FT   METAL       263    263       Magnesium; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   MOD_RES     716    716       N6-acetyllysine. {ECO:0000250}.
FT   HELIX        66     68       {ECO:0000244|PDB:3LQ2}.
FT   HELIX        76     99       {ECO:0000244|PDB:3LQ2}.
FT   HELIX       109    124       {ECO:0000244|PDB:3LQ2}.
FT   STRAND      131    133       {ECO:0000244|PDB:3LQ2}.
FT   STRAND      137    139       {ECO:0000244|PDB:3LQ2}.
FT   HELIX       142    144       {ECO:0000244|PDB:3LQ2}.
FT   HELIX       145    154       {ECO:0000244|PDB:3LQ2}.
FT   HELIX       160    163       {ECO:0000244|PDB:3LQ2}.
FT   TURN        181    183       {ECO:0000244|PDB:3LQ2}.
FT   TURN        185    187       {ECO:0000244|PDB:3LQ2}.
FT   HELIX       197    214       {ECO:0000244|PDB:3LQ2}.
FT   STRAND      225    230       {ECO:0000244|PDB:3LQ2}.
FT   HELIX       233    235       {ECO:0000244|PDB:3LQ2}.
FT   HELIX       237    240       {ECO:0000244|PDB:3LQ2}.
FT   HELIX       243    248       {ECO:0000244|PDB:3LQ2}.
FT   STRAND      254    260       {ECO:0000244|PDB:3LQ2}.
FT   STRAND      265    269       {ECO:0000244|PDB:3LQ2}.
FT   STRAND      271    273       {ECO:0000244|PDB:3LQ2}.
FT   HELIX       275    285       {ECO:0000244|PDB:3LQ2}.
FT   STRAND      289    293       {ECO:0000244|PDB:3LQ2}.
FT   HELIX       297    299       {ECO:0000244|PDB:3LQ2}.
FT   HELIX       300    305       {ECO:0000244|PDB:3LQ2}.
FT   HELIX       310    317       {ECO:0000244|PDB:3LQ2}.
FT   HELIX       320    326       {ECO:0000244|PDB:3LQ2}.
FT   HELIX       331    337       {ECO:0000244|PDB:3LQ2}.
FT   HELIX       339    341       {ECO:0000244|PDB:3LQ4}.
FT   HELIX       343    346       {ECO:0000244|PDB:3LQ2}.
FT   TURN        347    349       {ECO:0000244|PDB:3LQ2}.
FT   STRAND      350    352       {ECO:0000244|PDB:3LQ2}.
FT   HELIX       354    357       {ECO:0000244|PDB:3LQ2}.
FT   HELIX       363    365       {ECO:0000244|PDB:3LQ2}.
FT   HELIX       367    379       {ECO:0000244|PDB:3LQ2}.
FT   STRAND      385    390       {ECO:0000244|PDB:3LQ2}.
FT   TURN        393    396       {ECO:0000244|PDB:3LQ2}.
FT   HELIX       416    424       {ECO:0000244|PDB:3LQ2}.
FT   HELIX       431    434       {ECO:0000244|PDB:3LQ2}.
FT   HELIX       447    457       {ECO:0000244|PDB:3LQ2}.
FT   TURN        458    460       {ECO:0000244|PDB:3LQ2}.
FT   HELIX       479    482       {ECO:0000244|PDB:3LQ2}.
FT   HELIX       483    486       {ECO:0000244|PDB:3LQ2}.
FT   HELIX       495    506       {ECO:0000244|PDB:3LQ2}.
FT   TURN        510    515       {ECO:0000244|PDB:3LQ2}.
FT   STRAND      516    522       {ECO:0000244|PDB:3LQ2}.
FT   HELIX       525    527       {ECO:0000244|PDB:3LQ2}.
FT   HELIX       530    536       {ECO:0000244|PDB:3LQ2}.
FT   STRAND      565    567       {ECO:0000244|PDB:3LQ2}.
FT   HELIX       572    583       {ECO:0000244|PDB:3LQ2}.
FT   HELIX       585    588       {ECO:0000244|PDB:3LQ2}.
FT   STRAND      594    600       {ECO:0000244|PDB:3LQ2}.
FT   HELIX       601    603       {ECO:0000244|PDB:3LQ2}.
FT   HELIX       605    617       {ECO:0000244|PDB:3LQ2}.
FT   STRAND      623    628       {ECO:0000244|PDB:3LQ2}.
FT   TURN        631    633       {ECO:0000244|PDB:3LQ2}.
FT   TURN        635    637       {ECO:0000244|PDB:3LQ2}.
FT   TURN        639    641       {ECO:0000244|PDB:3LQ2}.
FT   HELIX       646    650       {ECO:0000244|PDB:3LQ2}.
FT   STRAND      656    659       {ECO:0000244|PDB:3LQ2}.
FT   HELIX       664    679       {ECO:0000244|PDB:3LQ2}.
FT   STRAND      687    691       {ECO:0000244|PDB:3LQ2}.
FT   HELIX       707    712       {ECO:0000244|PDB:3LQ2}.
FT   STRAND      714    720       {ECO:0000244|PDB:3LQ2}.
FT   STRAND      726    731       {ECO:0000244|PDB:3LQ2}.
FT   HELIX       733    735       {ECO:0000244|PDB:3LQ2}.
FT   HELIX       736    750       {ECO:0000244|PDB:3LQ2}.
FT   STRAND      753    760       {ECO:0000244|PDB:3LQ2}.
FT   HELIX       762    778       {ECO:0000244|PDB:3LQ2}.
FT   HELIX       788    792       {ECO:0000244|PDB:3LQ2}.
FT   STRAND      798    801       {ECO:0000244|PDB:3LQ2}.
FT   HELIX       807    810       {ECO:0000244|PDB:3LQ2}.
FT   HELIX       811    815       {ECO:0000244|PDB:3LQ2}.
FT   STRAND      817    819       {ECO:0000244|PDB:3LQ4}.
FT   STRAND      821    824       {ECO:0000244|PDB:3LQ2}.
FT   HELIX       835    841       {ECO:0000244|PDB:3LQ2}.
FT   HELIX       846    859       {ECO:0000244|PDB:3LQ2}.
FT   HELIX       865    874       {ECO:0000244|PDB:3LQ2}.
FT   TURN        884    886       {ECO:0000244|PDB:3LQ2}.
SQ   SEQUENCE   887 AA;  99668 MW;  7FB3811DE11BDD02 CRC64;
     MSERFPNDVD PIETRDWLQA IESVIREEGV ERAQYLIDQL LAEARKGGVN VAAGTGISNY
     INTIPVEEQP EYPGNLELER RIRSAIRWNA IMTVLRASKK DLELGGHMAS FQSSATIYDV
     CFNHFFRARN EQDGGDLVYF QGHISPGVYA RAFLEGRLTQ EQLDNFRQEV HGNGLSSYPH
     PKLMPEFWQF PTVSMGLGPI GAIYQAKFLK YLEHRGLKDT SKQTVYAFLG DGEMDEPESK
     GAITIATREK LDNLVFVINC NLQRLDGPVT GNGKIINELE GIFEGAGWNV IKVMWGSRWD
     ELLRKDTSGK LIQLMNETVD GDYQTFKSKD GAYVREHFFG KYPETAALVA DWTDEQIWAL
     NRGGHDPKKI YAAFKKAQET KGKATVILAH TIKGYGMGDA AEGKNIAHQV KKMNMDGVRH
     IRDRFNVPVS DADIEKLPYI TFPEGSEEHT YLHAQRQKLH GYLPSRQPNF TEKLELPSLQ
     DFGALLEEQS KEISTTIAFV RALNVMLKNK SIKDRLVPII ADEARTFGME GLFRQIGIYS
     PNGQQYTPQD REQVAYYKED EKGQILQEGI NELGAGCSWL AAATSYSTNN LPMIPFYIYY
     SMFGFQRIGD LCWAAGDQQA RGFLIGGTSG RTTLNGEGLQ HEDGHSHIQS LTIPNCISYD
     PAYAYEVAVI MHDGLERMYG EKQENVYYYI TTLNENYHMP AMPEGAEEGI RKGIYKLETI
     EGSKGKVQLL GSGSILRHVR EAAEILAKDY GVGSDVYSVT SFTELARDGQ DCERWNMLHP
     LETPRVPYIA QVMNDAPAVA STDYMKLFAE QVRTYVPADD YRVLGTDGFG RSDSRENLRH
     HFEVDASYVV VAALGELAKR GEIDKKVVAD AIAKFNIDAD KVNPRLA
//

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