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Q73YG2 (Q73YG2_MYCPA) Unreviewed, UniProtKB/TrEMBL

Last modified January 25, 2012. Version 50. 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 AAS04311.1
Ordered Locus Names:MAP_1994
OrganismMycobacterium paratuberculosis [Complete proteome] [HAMAP]
Taxonomic identifier1770 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium avium complex (MAC)

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
Q73YG2 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: D09C8D77CD147BCA

FASTA929103,374
        10         20         30         40         50         60 
MTTEFVRHDL ATNPTGPAEP DRVRVIREGV ASYLPDIDPE ETSEWLESFD ELLERSGPSR 

        70         80         90        100        110        120 
ARYLMLRLLE RAGEQRVALP SLTSTDYVNT IPTELEPWFP GDEDVERRYR AWIRWNAAIM 

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

       190        200        210        220        230        240 
LEGRLTADQL DGFRQEHSHA GGGLPSYPHP RLMPDFWEFP TVSMGLGPLN AIYQARFNHY 

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

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

       370        380        390        400        410        420 
AYVRDHFFGR DPRTKALVEN MTDAEIWNLK RGGHDYRKVY AAYRAAVDHK GQPTVILAKT 

       430        440        450        460        470        480 
IKGYSLGAHF QGRNATHQMK KLALEDLKHF RDAMRIPISD AQLDENPYLP PYYHPGSDAP 

       490        500        510        520        530        540 
EIRYMLDRRR TLGGFLPERR TKAKALRLPG RDIYAALKKG SGTQEVATTM ATVRTFKEVL 

       550        560        570        580        590        600 
RDKEIGPRIV PIIPDEARTF GMDSWFPSLK IYNRNGQLYT AVDAELMLAY KESEVGQILH 

       610        620        630        640        650        660 
EGINEAGSVG SFIAAGTSYA THNEPMIPIY IFYSMFGFQR TGDGLWAAAD QMTRGFLLGA 

       670        680        690        700        710        720 
TAGRTTLTGE GLQHADGHSL LLAATNPAVV AYDPAFAYEI AYIVESGLAR MFGENPEDVY 

       730        740        750        760        770        780 
FYITVYNEPY VQPPEPENFD PEGLLRGLYR YHVATEQRAN KAQILASGVA MPSALNAAKM 

       790        800        810        820        830        840 
LADEWDVAAD VWSVTSWGEL NRDGVAIDRA RLRHPDRPAG VPYVTQALSD ASGPVVAVSD 

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

       910        920 
PSVPVAAARQ YRIDDVLAAP EQTSDPGVA

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References

[1]"The complete genome sequence of Mycobacterium avium subspecies paratuberculosis."
Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N., Kanjilal S., Kapur V.
Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005) [PubMed: 16116077] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-968 / K-10.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE016958 Genomic DNA. Translation: AAS04311.1.
RefSeqNP_960928.1. NC_002944.2.

3D structure databases

ProteinModelPortalQ73YG2.
SMRQ73YG2. Positions 85-920.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBMYCT00000040191; EBMYCP00000038580; EBMYCG00000040186.
GeneID2718363.
GenomeReviewsGene locus MAP_1994 in contig AE016958_GR.
KEGGmpa:MAP1994.
NMPDRfig|262316.1.peg.1994.
PATRIC17996578. VBIMycAvi108102_2115.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000016271.
HOGENOMHBG289271.
OMAFRQEKSH.
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 nameQ73YG2_MYCPA
AccessionPrimary (citable) accession number: Q73YG2
Entry history
Integrated into UniProtKB/TrEMBL: July 5, 2004
Last sequence update: July 5, 2004
Last modified: January 25, 2012
This is version 50 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