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C1AUF9 (C1AUF9_RHOOB) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 20. 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 BAH49167.1
Ordered Locus Names:ROP_09200
OrganismRhodococcus opacus (strain B4) [Complete proteome] [HAMAP]
Taxonomic identifier632772 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Nocardiaceae › Rhodococcus

Protein attributes

Sequence length915 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
C1AUF9 [UniParc].

Last modified May 26, 2009. Version 1.
Checksum: 8EA8189A5E755DDD

FASTA915101,378
        10         20         30         40         50         60 
MRVIREGVAS YLPDIDPDET TEWLESFDGL LDRSGPTRAR YLMLRMLERA GEKHVALPAL 

        70         80         90        100        110        120 
TSTDYVNTIP TENEPWFPGD EEVERRYRAF IRWNAAVMVT RAQRPGVGVG GHISTYASSA 

       130        140        150        160        170        180 
ALYEVGFNHF FRGKDHPGGG DQIFIQGHAS PGIYARAFLE GRIPAERMDG FRQEHSHTDS 

       190        200        210        220        230        240 
GGGLPSYPHP RLLPDFWEFP TVSMGLGPMN AIYQARFNHY LHDRGIKDTA DQHVWAFLGD 

       250        260        270        280        290        300 
GEMDEPESRG LAHVAATEGL DNLTFVVNCN LQRLDGPVRG NGKIIQELES FFRGAGWNVI 

       310        320        330        340        350        360 
KVVWGREWDA LLHADRDGAL VNLMNVTPDG DYQTYKANDG GYVREHFFGR DPRTKELVAN 

       370        380        390        400        410        420 
LSDRDIWNLK RGGHDYRKIY AAYAAAMAHK GQPTVILAHT IKGYTLGKHF EGRNATHQMK 

       430        440        450        460        470        480 
KLTLDDLKNF RDLQRIPISD AELERDPKMP PYYHPGPDAP EIRYMLDRRK ALGGFLPERR 

       490        500        510        520        530        540 
TSPQPLPQPA DSTYDVVRKG SGKQQVATTM ALVRIMKELL RDKEIGKRIV PIIPDEARTF 

       550        560        570        580        590        600 
GMDSWFPSLK IYNRNGQLYT AVDAELMLAY KESEIGQILH EGINEAGSTA SFTAVGTSYA 

       610        620        630        640        650        660 
THGEPMIPLY IFYSMFGFQR TGDGLWAAAD QMARGFVLGA TAGRTTLTGE GLQHADGHSL 

       670        680        690        700        710        720 
LLASTNPAAV AYDPSFSYEL AHIVKDGLRR MYGGTDGVDG FGGEDIFYYI TLYNEPYTQP 

       730        740        750        760        770        780 
AEPENLNVQG LLKGMYLFKK SEASGPKAQI LVSGVTMPDG LRAQQMLADE WGVAADVWSV 

       790        800        810        820        830        840 
TSWGELRRDG IESERQALRD PGTDAPLPYV TQALSDAAGP FVAASDWMRA VADQIRQWVP 

       850        860        870        880        890        900 
GSYTTLGTDG FGFSDTRPAA RRYFNVDAES IVVAVLSALA GEGTLDRSKA VDAATKYRID 

       910 
DVRAAAVSYT DTGSA

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References

[1]"Comparison of the complete genome sequences of Rhodococcus erythropolis PR4 and Rhodococcus opacus B4."
Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S., Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.
Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AP011115 Genomic DNA. Translation: BAH49167.1.
RefSeqYP_002778112.1. NC_012522.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGC1AUF9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID7747950.
GenomeReviewsGene locus ROP_09200 in contig AP011115_GR.
KEGGrop:ROP_09200.
PATRIC23219019. VBIRhoOpa21106_0921.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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 nameC1AUF9_RHOOB
AccessionPrimary (citable) accession number: C1AUF9
Entry history
Integrated into UniProtKB/TrEMBL: May 26, 2009
Last sequence update: May 26, 2009
Last modified: December 14, 2011
This is version 20 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