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A4IXM8 (A4IXM8_FRATW) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 42. 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 ABO46680.1
Ordered Locus Names:FTW_0808
OrganismFrancisella tularensis subsp. tularensis (strain WY96-3418) [Complete proteome] [HAMAP] EMBL ABO46680.1
Taxonomic identifier418136 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Thiotrichales › Francisellaceae › Francisella ›

Protein attributes

Sequence length893 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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. 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
A4IXM8 [UniParc].

Last modified May 1, 2007. Version 1.
Checksum: BC1FB41EF64DF391

FASTA893100,152
        10         20         30         40         50         60 
MSDFTKDIDV LETQEWLEAF EDVIKREGAD RAKFLFEQLL AKGSELGIKS AYSTAKVKNY 

        70         80         90        100        110        120 
VNSIDVSEQP SYPGDIELEQ KIEAINRWNS TVIVAAANKK DGSIGGHIGT GAGAMTLYEV 

       130        140        150        160        170        180 
GFNHFWKAPN DEHAGDLIFY QGHLSPIVYA RSFLEGRITA EQLENFRKQA FNGQNAVSSY 

       190        200        210        220        230        240 
PHPYLQPTYW QFPTVSMGLG PLQAIYQARF MKYLEARGLA KTSDRKVWAF CGDGEMDEPE 

       250        260        270        280        290        300 
SIGSITRAGR EGLDNLIFVV NCNLQRLDGL VNGNGNIVEE LADVFAGAGW NVIKVLWSSD 

       310        320        330        340        350        360 
WDKLLQDPRG GKKLAQRLSE LNDGQFHTIK AHGGAECRRV VFSGDEDLEA LAKDMTDDDI 

       370        380        390        400        410        420 
QALRRGGHDP LKIYAAYKKA VENPNGRPTL ILPMTVKGYG LGEWGESKNI AHNVKKLDTD 

       430        440        450        460        470        480 
ALEHIKNRFN VPASKEDIEN YRLIKLDENS PEMKYLHSKR KDLGGYIPKR LENKQALEIP 

       490        500        510        520        530        540 
SYKDFAKSLL DDSGDREFST TTAFVRILSH LAKDKNLGKH IVPITVDESR TFGMEGLFRQ 

       550        560        570        580        590        600 
LGIYNPHGQQ YVPEDKQQVM FYKESVDGQI LQEGINEQGG FCSWIAAATS YSVHKVPMIP 

       610        620        630        640        650        660 
FMIYYSMFGF QRFGDLAWAA GDSMAKGFVI GGTSGRTTLN GEGLQHEDGH SHIQAGLIPN 

       670        680        690        700        710        720 
CISYDPTYAY ELAVILGEGM KRMYVDGDHV YYYITVMNEN YSHRAMPEGC EEGIIKGLYK 

       730        740        750        760        770        780 
LDEEKKPASK HVQLLGSGSI LREVEAAAKM LKEEYGITSN VWSMTSANEL YREAKDVARA 

       790        800        810        820        830        840 
NMLHPTAEKK ESYIEKCFKN EQGPVIASTD YIKLYTDQLR EFIPHAFVNL GTDGFGRSDT 

       850        860        870        880        890 
RAALRSFFEV DRYHVVVASL YALYLDGKVE ASEVKAAIEK YNIDPERMAP FYS

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References

[1]"Complete genomic characterization of a pathogenic A.II strain of Francisella tularensis subspecies tularensis."
Beckstrom-Sternberg S.M., Auerbach R.K., Godbole S., Pearson J.V., Beckstrom-Sternberg J.S., Deng Z., Munk C., Kubota K., Zhou Y., Bruce D., Noronha J., Scheuermann R.H., Wang A., Wei X., Wang J., Hao J., Wagner D.M., Brettin T.S. expand/collapse author list , Brown N., Gilna P., Keim P.S.
PLoS ONE 2:E947-E947(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: WY96-3418.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000608 Genomic DNA. Translation: ABO46680.1.
RefSeqYP_001121800.1. NC_009257.1.

3D structure databases

ProteinModelPortalA4IXM8.
SMRA4IXM8. Positions 57-891.
ModBaseSearch...

Protein-protein interaction databases

STRING418136.FTW_0808.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABO46680; ABO46680; FTW_0808.
GeneID4960340.
KEGGftw:FTW_0808.
PATRIC17969016. VBIFraTul58433_0824.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2609.
HOGENOMHOG000115215.
KOK00163.
OMADAVECEE.
ProtClustDBPRK09405.

Enzyme and pathway databases

BioCycFTUL418136:GHXJ-901-MONOMER.

Family and domain databases

Gene3D3.40.50.920. 1 hit.
InterProIPR004660. 2-oxoA_DH_E1.
IPR009014. Transketo_C/Pyr-ferredox_oxred.
IPR015941. Transketolase-like_C.
IPR005474. Transketolase_N.
[Graphical view]
PfamPF00456. Transketolase_N. 1 hit.
[Graphical view]
PIRSFPIRSF000156. Pyruvate_dh_E1. 1 hit.
SUPFAMSSF52922. Transketo_C_like. 1 hit.
TIGRFAMsTIGR00759. aceE. 1 hit.
ProtoNetSearch...

Entry information

Entry nameA4IXM8_FRATW
AccessionPrimary (citable) accession number: A4IXM8
Entry history
Integrated into UniProtKB/TrEMBL: May 1, 2007
Last sequence update: May 1, 2007
Last modified: May 1, 2013
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequences·References·Cross-refs·Entry info