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UniProtKB/Swiss-Prot entry P0AFG9

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ODP1_ECO57
Primary accession number P0AFG9
Secondary accession numbers P06958 P78049 Q53382
Integrated into Swiss-Prot on April 1, 1988
Sequence was last modified on January 23, 2007 (Sequence version 2)
Annotations were last modified on    December 16, 2008 (Entry version 28)
Name and origin of the protein
Protein name Pyruvate dehydrogenase E1 component
Synonym EC 1.2.4.1
Gene name
Name: aceE
OrderedLocusNames: Z0124, ECs0118
From
Escherichia coli O157:H7 [TaxID: 83334] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
DOI=10.1038/35054089; PubMed=11206551 [NCBI, ExPASy, EBI, Israel, Japan]
Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R.;
"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
Nature 409:529-533(2001).
[2]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
DOI=10.1093/dnares/8.1.11; PubMed=11258796 [NCBI, ExPASy, EBI, Israel, Japan]
Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S., Shiba T., Hattori M., Shinagawa H.;
"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12.";
DNA Res. 8:11-22(2001).
Comments
  • FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity).
  • CATALYTIC ACTIVITY: Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2.
  • COFACTOR: Magnesium (By similarity).
  • COFACTOR: Thiamine pyrophosphate (By similarity).
  • SUBUNIT: Homodimer (By similarity).
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AE005174; AAG54418.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BA000007; BAB33541.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR F85494; F85494.
F90643; F90643.
RefSeq NP_285810.1; -.
NP_308145.1; -.
3D structure databases
ModBase P0AFG9.
Enzyme and pathway databases
BioCyc ECOL83334:ECS0118-MON; -.
Ontologies
GO
GO:0000287; Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004739; Molecular function: pyruvate dehydrogenase (acetyl-transferring) activity (inferred from electronic annotation from EC).
GO:0006096; Biological process: glycolysis (inferred from electronic annotation from UniProtKB-KW).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR004660; 2-oxoA_DHase_E1.
IPR005474; Transketo_N.
IPR015941; Transketolase_C-like.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.920; Transketo_C_like; 1.
Pfam PF00456; Transketolase_N; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000156; Pyruvate_dh_E1; 1.
TIGRFAMs TIGR00759; aceE; 1.
Genome annotation databases
GeneID 913657; -.
956809; -.
GenomeReviews AE005174_GR; Z0124.
BA000007_GR; ECs0118.
KEGG ece:Z0124; -.
ecs:ECs0118; -.
Phylogenomic databases
HOGENOM P0AFG9; -.
Genome annotation databases
CMR P0AFG9; Z0124.
Other
ProtoNet P0AFG9.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; Complete proteome; Glycolysis; Magnesium; Metal-binding; Oxidoreductase; Pyruvate; Thiamine pyrophosphate.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed (By similarity). 
CHAIN   2   887  886     Pyruvate dehydrogenase E1 component. PRO_0000162244
METAL   231   231        Magnesium (By similarity). 
METAL   261   261        Magnesium (By similarity). 
METAL   263   263        Magnesium; via carbonyl oxygen (By similarity). 
MOD_RES   716   716        N6-acetyllysine (By similarity). 
Sequence information
Length: 887 AA [This is the length of the unprocessed precursor] Molecular weight: 99668 Da [This is the MW of the unprocessed precursor] CRC64: 7FB3811DE11BDD02 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MSERFPNDVD PIETRDWLQA IESVIREEGV ERAQYLIDQL LAEARKGGVN VAAGTGISNY 

        70         80         90        100        110        120 
INTIPVEEQP EYPGNLELER RIRSAIRWNA IMTVLRASKK DLELGGHMAS FQSSATIYDV 

       130        140        150        160        170        180 
CFNHFFRARN EQDGGDLVYF QGHISPGVYA RAFLEGRLTQ EQLDNFRQEV HGNGLSSYPH 

       190        200        210        220        230        240 
PKLMPEFWQF PTVSMGLGPI GAIYQAKFLK YLEHRGLKDT SKQTVYAFLG DGEMDEPESK 

       250        260        270        280        290        300 
GAITIATREK LDNLVFVINC NLQRLDGPVT GNGKIINELE GIFEGAGWNV IKVMWGSRWD 

       310        320        330        340        350        360 
ELLRKDTSGK LIQLMNETVD GDYQTFKSKD GAYVREHFFG KYPETAALVA DWTDEQIWAL 

       370        380        390        400        410        420 
NRGGHDPKKI YAAFKKAQET KGKATVILAH TIKGYGMGDA AEGKNIAHQV KKMNMDGVRH 

       430        440        450        460        470        480 
IRDRFNVPVS DADIEKLPYI TFPEGSEEHT YLHAQRQKLH GYLPSRQPNF TEKLELPSLQ 

       490        500        510        520        530        540 
DFGALLEEQS KEISTTIAFV RALNVMLKNK SIKDRLVPII ADEARTFGME GLFRQIGIYS 

       550        560        570        580        590        600 
PNGQQYTPQD REQVAYYKED EKGQILQEGI NELGAGCSWL AAATSYSTNN LPMIPFYIYY 

       610        620        630        640        650        660 
SMFGFQRIGD LCWAAGDQQA RGFLIGGTSG RTTLNGEGLQ HEDGHSHIQS LTIPNCISYD 

       670        680        690        700        710        720 
PAYAYEVAVI MHDGLERMYG EKQENVYYYI TTLNENYHMP AMPEGAEEGI RKGIYKLETI 

       730        740        750        760        770        780 
EGSKGKVQLL GSGSILRHVR EAAEILAKDY GVGSDVYSVT SFTELARDGQ DCERWNMLHP 

       790        800        810        820        830        840 
LETPRVPYIA QVMNDAPAVA STDYMKLFAE QVRTYVPADD YRVLGTDGFG RSDSRENLRH 

       850        860        870        880 
HFEVDASYVV VAALGELAKR GEIDKKVVAD AIAKFNIDAD KVNPRLA
P0AFG9 in FASTA format

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