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C1A193 (C1A193_RHOE4) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 21. 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 BAH34378.1
Ordered Locus Names:RER_36700
OrganismRhodococcus erythropolis (strain PR4 / NBRC 100887) [Complete proteome] [HAMAP]
Taxonomic identifier234621 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeNocardiaceaeRhodococcus

Protein attributes

Sequence length951 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
C1A193 [UniParc].

Last modified May 26, 2009. Version 1.
Checksum: 3D28260FF18BA115

FASTA951104,533
        10         20         30         40         50         60 
MSDLIQGPAS GQNADSGAAG ESGSPASNTP GGTDGRVRVI REGVASYLPD IDPDETTEWL 

        70         80         90        100        110        120 
ESFDGLLDRS GPTRARYLML RMLERAGEKH VALPALTSTD YVNTIPTENE PWFPGDEEVE 

       130        140        150        160        170        180 
RRYRAWIRWN AAIMVHRAQR PGVGVGGHIS TYASSAALYE VGFNHFFRGK DHPGGGDHIF 

       190        200        210        220        230        240 
IQGHASPGIY ARAFLEGRIP AEQLDGFRQE KSHADFGGAL PSYPHPRLLP DFWEFPTVSM 

       250        260        270        280        290        300 
GLGPMNAIYQ ARFNHYLNDR GIKDTTDQHV WAFLGDGEMD EPESRGLAHV AATEGLDNLT 

       310        320        330        340        350        360 
FVVNCNLQRL DGPVRGNGKI IQELESFFRG AGWNVIKVVW GREWDALLHA DRDGALVNLM 

       370        380        390        400        410        420 
NVTPDGDYQT YKANDGAFVR DHFFGRDPRT KELVKDLTDQ EIWNLKRGGH DYRKVHAAYA 

       430        440        450        460        470        480 
AAMAHKGQPT VILAHTIKGY TLGKHFEGRN ATHQMKKLTL DDLKAFRDMQ HIPISDAELE 

       490        500        510        520        530        540 
KDPYLPPYYH PGADAPEIKY MLDRRKALGG FLPSRNTDAA PLKLPEDKTY DVIRKGSGKQ 

       550        560        570        580        590        600 
EVATTMAIVR ILKELLRDKE IGKRIVPIIP DEARTFGMDS WFPSLKIYNR NGQLYTSVDA 

       610        620        630        640        650        660 
ELMLAYKESP IGQILHEGIN EAGSTASFTA VGTSYATHGE PMIPLYIFYS MFGFQRTGDG 

       670        680        690        700        710        720 
LWAAADQMAR GFVLGATAGR TTLTGEGLQH ADGHSLLLAS TNPAAVTYDA AFSYELAHIV 

       730        740        750        760        770        780 
KDGLRRMYGG TEGVDGFGGE NIFYYLTIYN EPYVQPAEPE GLDVEGLLKG IYLYKTSEAA 

       790        800        810        820        830        840 
GPKAQILVSG VAMPEGLRAQ KLLADEWGVS ADVWSVTSWG ELRREGVECE RQALLNPSED 

       850        860        870        880        890        900 
APVPFVTTAL SSAQGPVVAA SDWMRAVSDQ IRQWVPGDYT TLGTDGFGFS DTRTAARRYF 

       910        920        930        940        950 
NVDAESIVVA VLIGLAKEGS IERSKAVEAA SRYRIDDVNA APEQTGDTGS A 

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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-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PR4 / NBRC 100887.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP008957 Genomic DNA. Translation: BAH34378.1.
RefSeqYP_002767117.1. NC_012490.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGC1A193.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID7712670.
GenomeReviewsGene locus RER_36700 in contig AP008957_GR.
KEGGrer:RER_36700.
PATRIC23193820. VBIRhoEry66701_4187.

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 nameC1A193_RHOE4
AccessionPrimary (citable) accession number: C1A193
Entry history
Integrated into UniProtKB/TrEMBL: May 26, 2009
Last sequence update: May 26, 2009
Last modified: December 14, 2011
This is version 21 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)