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P0AFG9 (ODP1_ECO57) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pyruvate dehydrogenase E1 component

Short name=PDH E1 component
EC=1.2.4.1
Gene names
Name:aceE
Ordered Locus Names:Z0124, ECs0118
OrganismEscherichia coli O157:H7 [Complete proteome] [HAMAP]
Taxonomic identifier83334 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length887 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of the pyruvate dehydrogenase (PDH) complex, that catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2 By similarity.

Catalytic activity

Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2.

Cofactor

Magnesium By similarity.

Thiamine pyrophosphate By similarity.

Subunit structure

Homodimer By similarity. Part of the PDH complex, consisting of multiple copies of pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3) By similarity.

Ontologies

Keywords
   Biological processGlycolysis
   LigandMagnesium
Metal-binding
Pyruvate
Thiamine pyrophosphate
   Molecular functionOxidoreductase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological_processglycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

pyruvate dehydrogenase (acetyl-transferring) activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 887886Pyruvate dehydrogenase E1 component
PRO_0000162244

Sites

Metal binding2311Magnesium By similarity
Metal binding2611Magnesium By similarity
Metal binding2631Magnesium; via carbonyl oxygen By similarity

Amino acid modifications

Modified residue7161N6-acetyllysine By similarity

Secondary structure

............................................................................................................................................... 887
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0AFG9 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 7FB3811DE11BDD02

FASTA88799,668
        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 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE005174 Genomic DNA. Translation: AAG54418.1.
BA000007 Genomic DNA. Translation: BAB33541.1.
PIRF85494.
F90643.
RefSeqNP_285810.1. NC_002655.2.
NP_308145.1. NC_002695.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3LPLX-ray2.10A/B2-887[»]
3LQ2X-ray1.96A/B2-887[»]
3LQ4X-ray1.98A/B2-887[»]
ProteinModelPortalP0AFG9.
SMRP0AFG9. Positions 57-887.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP0AFG9. 3 interactions.
STRING155864.Z0124.

Proteomic databases

PRIDEP0AFG9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAG54418; AAG54418; Z0124.
BAB33541; BAB33541; BAB33541.
GeneID913657.
956809.
KEGGece:Z0124.
ecs:ECs0118.
PATRIC18349174. VBIEscCol44059_0117.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2609.
HOGENOMHOG000115215.
KOK00163.
OMALMMEVVD.
OrthoDBEOG6BW4TW.
ProtClustDBPRK09405.

Enzyme and pathway databases

BioCycECOL386585:GJFA-115-MONOMER.
ECOO157:ACEE-MONOMER.

Family and domain databases

Gene3D3.40.50.920. 1 hit.
InterProIPR004660. 2-oxoA_DH_E1.
IPR009014. Transketo_C/Pyr-ferredox_oxred.
IPR005474. Transketolase_N.
[Graphical view]
PfamPF00456. Transketolase_N. 2 hits.
[Graphical view]
PIRSFPIRSF000156. Pyruvate_dh_E1. 1 hit.
SUPFAMSSF52922. SSF52922. 1 hit.
TIGRFAMsTIGR00759. aceE. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP0AFG9.

Entry information

Entry nameODP1_ECO57
AccessionPrimary (citable) accession number: P0AFG9
Secondary accession number(s): P06958, P78049, Q53382
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: January 23, 2007
Last modified: December 11, 2013
This is version 64 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references