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B7UIG2 (B7UIG2_ECO27) Unreviewed, UniProtKB/TrEMBL

Last modified January 25, 2012. Version 26. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Pyruvate dehydrogenase E1 component PIRNR PIRNR000156
EC=1.2.4.1 PIRNR PIRNR000156
Gene names
Name:aceE EMBL CAS07665.1
Ordered Locus Names:E2348C_0117 EMBL CAS07665.1
OrganismEscherichia coli O127:H6 (strain E2348/69 / EPEC) [Complete proteome] [HAMAP]
Taxonomic identifier574521 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length887 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2. It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3) By similarity. PIRNR PIRNR000156

Catalytic activity

Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2. PIRNR PIRNR000156

Cofactor

Thiamine pyrophosphate By similarity. PIRNR PIRNR000156

Sequences

Sequence LengthMass (Da)Tools
B7UIG2 [UniParc].

Last modified February 10, 2009. Version 1.
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

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References

[1]"Complete genome sequence and comparative genome analysis of enteropathogenic Escherichia coli O127:H6 strain E2348/69."
Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T., Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P., Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J., Frankel G.
J. Bacteriol. 191:347-354(2009) [PubMed: 18952797] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: E2348/69 / EPEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		FM180568 Genomic DNA. Translation: CAS07665.1.
RefSeqYP_002327709.1. NC_011601.1.

3D structure databases

ProteinModelPortalB7UIG2.
SMRB7UIG2. Positions 57-887.
ModBaseSearch...

Protein-protein interaction databases

STRINGB7UIG2.

Proteomic databases

PRIDEB7UIG2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000115855; EBESCP00000106717; EBESCG00000113125.
GeneID7062918.
GenomeReviewsGene locus E2348_C_0117 in contig FM180568_GR.
KEGGecg:E2348C_0117.
PATRIC18339135. VBIEscCol90278_0121.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000009226.
HOGENOMHBG289271.
OMADRHFVVL.
ProtClustDBPRK09405.

Family and domain databases

InterProIPR004660. 2-oxoA_DH_E1.
IPR009014. Transketo_C/Pyr-ferredox_oxred.
IPR015941. Transketolase-like_C.
IPR005474. Transketolase_N.
[Graphical view]
Gene3DG3DSA:3.40.50.920. Transketo_C_like. 1 hit.
KOK00163.
PANTHERPTHR11624:SF37. PTHR11624:SF37. 1 hit.
PfamPF00456. Transketolase_N. 2 hits.
[Graphical view]
PIRSFPIRSF000156. Pyruvate_dh_E1. 1 hit.
SUPFAMSSF52922. Transketo_C_like. 1 hit.
TIGRFAMsTIGR00759. AceE. 1 hit.
ProtoNetSearch...

Entry information

Entry nameB7UIG2_ECO27
AccessionPrimary (citable) accession number: B7UIG2
Entry history
Integrated into UniProtKB/TrEMBL: February 10, 2009
Last sequence update: February 10, 2009
Last modified: January 25, 2012
This is version 26 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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