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A0PNE9 (A0PNE9_MYCUA) Unreviewed, UniProtKB/TrEMBL

Last modified January 25, 2012. Version 37. 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 ABL03868.1
Ordered Locus Names:MUL_1308
OrganismMycobacterium ulcerans (strain Agy99) [Complete proteome] [HAMAP]
Taxonomic identifier362242 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

Protein attributes

Sequence length929 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
A0PNE9 [UniParc].

Last modified January 9, 2007. Version 1.
Checksum: 1AC454E3CEFEC4FD

FASTA929103,366
        10         20         30         40         50         60 
MTTEFVRHDL AKTSSSASEP DRVRVIREGV ASYLPDIDPE ETSEWLESFD ALLEHSGPAR 

        70         80         90        100        110        120 
ARYLMLRLLE RAGEQRVAIP SLTSTDYVNT IPTELEPWFP GDEDVERRYR TWIRWNAAIM 

       130        140        150        160        170        180 
VHRAQRPGVG VGGHISTYAS SAALYEVGFN HFFRGKSHPG GGDQVFIQGH ASPGIYARAF 

       190        200        210        220        230        240 
LEGRLSADQL DGFRQEHSHP GGGLPSYPHP RLMPDFWEFP TVSMGLGPLN AIYQARFNHY 

       250        260        270        280        290        300 
LHDRGIKDTS DQHVWCFLGD GEMDEPESRG LAHMGALEGL DNLTFVINCN LQRLDGPVRG 

       310        320        330        340        350        360 
NGKIIQELES FFRGAGWNVI KVVWGREWDA LLHADRDGAL VNLMNSTPDG DYQTYKANDG 

       370        380        390        400        410        420 
AYVRDHFFGR DPRTKALVAN MSDQEIWNLK RGGHDYRKVY AAYRAAVDHK GQPTVILAKT 

       430        440        450        460        470        480 
IKGYSLGAHF QGRNATHQMK KLALADLKRF RDSMRIPVSD AQLDEDPYLP PYYHPGSDAP 

       490        500        510        520        530        540 
EIRYMLDRRR TLGGFLPERP TKAKTLTLPG PDAYKVLKKG SGQQEVATTM ALVRTFKELL 

       550        560        570        580        590        600 
RDKNIGNRIV PIIPDEARTF GMDSWFPSLK IYNRNGQLYT AVDAELMLAY KESHVGQILH 

       610        620        630        640        650        660 
EGINEAGSVG SFTAAGTSYA THNEPMIPIY IFYSMFGFQR TGDSFWAAAD QMARGFVLGA 

       670        680        690        700        710        720 
TAGRTTLTGE GLQHADGHSL LLAATNPAVV SYDPAFAYEL AYIIENGLSR MFGENPENIY 

       730        740        750        760        770        780 
FYITVYNEPY VQPAEPENFD PEGVLRGMYR YRAATKQCAH KAQLLASGVS MPDALKAAQM 

       790        800        810        820        830        840 
LADEWDVATD VWSVTSWSEL NRDGVSVERH RLRHPGEPAG VAYVTTALEG TSGPVVAVSD 

       850        860        870        880        890        900 
WMRAVPEQIR PWVPGTYVTL GTDGFGFSNT RPAARRYFNT DAESQVVAVL EALARDGEID 

       910        920 
ESMAVTAARQ YRIDDVQAAP KQTSDSGVA 

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References

[1]"Reductive evolution and niche adaptation inferred from the genome of Mycobacterium ulcerans, the causative agent of Buruli ulcer."
Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T., Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., Ryan J., Johnson P.D.R., Davies J.K., Jenkin G.A., Small P.L.C., Jones L.M. expand/collapse author list , Tekaia F., Laval F., Daffe M., Parkhill J., Cole S.T.
Genome Res. 17:192-200(2007) [PubMed: 17210928] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000325 Genomic DNA. Translation: ABL03868.1.
RefSeqYP_905339.1. NC_008611.1.

3D structure databases

ProteinModelPortalA0PNE9.
SMRA0PNE9. Positions 85-921.
ModBaseSearch...

Protein-protein interaction databases

STRINGA0PNE9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBMYCT00000075869; EBMYCP00000073874; EBMYCG00000075864.
GeneID4550721.
GenomeReviewsGene locus MUL_1308 in contig CP000325_GR.
KEGGmul:MUL_1308.
PATRIC18169450. VBIMycUlc37413_1582.

Organism-specific databases

GenoListMUL_1308.
CMRSearch...

Phylogenomic databases

eggNOGCOG2609.
GeneTreeEBGT00050000016271.
HOGENOMHBG289271.
OMAFRQEKSH.
PhylomeDBA0PNE9.
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. 1 hit.
[Graphical view]
PIRSFPIRSF000156. Pyruvate_dh_E1. 1 hit.
SUPFAMSSF52922. Transketo_C_like. 1 hit.
TIGRFAMsTIGR00759. AceE. 1 hit.
ProtoNetSearch...

Entry information

Entry nameA0PNE9_MYCUA
AccessionPrimary (citable) accession number: A0PNE9
Entry history
Integrated into UniProtKB/TrEMBL: January 9, 2007
Last sequence update: January 9, 2007
Last modified: January 25, 2012
This is version 37 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)