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Q1RJT3 (ODP2_RICBR) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex

EC=2.3.1.12
Alternative name(s):
Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
E2
Gene names
Name:pdhC
Ordered Locus Names:RBE_0300
OrganismRickettsia bellii (strain RML369-C) [Complete proteome] [HAMAP]
Taxonomic identifier336407 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiabelli group

Protein attributes

Sequence length418 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.

Catalytic activity

Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine.

Cofactor

Binds 1 lipoyl cofactor covalently By similarity.

Subunit structure

Forms a 24-polypeptide structural core with octahedral symmetry By similarity.

Sequence similarities

Belongs to the 2-oxoacid dehydrogenase family.

Contains 1 lipoyl-binding domain.

Ontologies

Keywords
   Biological processGlycolysis
   DomainLipoyl
   Molecular functionAcyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processglycolytic process

Inferred from electronic annotation. Source: UniProtKB-KW

pyruvate metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentpyruvate dehydrogenase complex

Inferred from electronic annotation. Source: InterPro

   Molecular_functiondihydrolipoyllysine-residue acetyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 418418Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
PRO_0000288763

Regions

Domain1 – 7777Lipoyl-binding

Sites

Active site3881 Potential

Amino acid modifications

Modified residue431N6-lipoyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1RJT3 [UniParc].

Last modified May 16, 2006. Version 1.
Checksum: E0ECE5B73C92EC31

FASTA41845,750
        10         20         30         40         50         60 
MPIKLLMPAL SPTMTEGNLA RWLKKEGDKI NPGEVIAEIE TDKATMEVEA VDEGTLAKII 

        70         80         90        100        110        120 
IPQGSQNVPV NSLIAVLIEE GEELSGIEEF IAKNNSNSPK KEEISKPAET IAPQNVKEEN 

       130        140        150        160        170        180 
ITTASDQNNI KVFASPLAKR LAKIQNVRIE EIKGSGPHGR IIKQDVLSHK GGSKALSNKI 

       190        200        210        220        230        240 
VSRNPEEYRL APNNNIRKII AKRLLESKQT VPHFYLSIEC NVDKLLDIRE DINKSFGDDK 

       250        260        270        280        290        300 
SAKISVNDFI ILAVAKALQE VPNANASWGD DAIRYYNNVD ISVAVAIENG LVTPIIRNAD 

       310        320        330        340        350        360 
QKNIVDLSSE MKGLIKKARE NKLTPEEFQG GGFTISNLGM YGIKNFNAII NPPQSCIMGV 

       370        380        390        400        410 
GSSSKRAIVK NDQISIATIM DVTLSADHRV VDGAVGAEFL AAFKRFIESP ALMLLYTR 

« Hide

References

[1]"Genome sequence of Rickettsia bellii illuminates the role of amoebae in gene exchanges between intracellular pathogens."
Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C., Fournier P.-E., Claverie J.-M., Raoult D.
PLoS Genet. 2:733-744(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RML369-C.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000087 Genomic DNA. Translation: ABE04381.1.
RefSeqYP_537470.1. NC_007940.1.

3D structure databases

ProteinModelPortalQ1RJT3.
SMRQ1RJT3. Positions 186-415.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING336407.RBE_0300.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABE04381; ABE04381; RBE_0300.
GeneID3996210.
KEGGrbe:RBE_0300.
PATRIC17881915. VBIRicBel102610_0337.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0508.
HOGENOMHOG000281566.
KOK00627.
OMAGSADGQY.
OrthoDBEOG610413.

Enzyme and pathway databases

BioCycRBEL336407:GJCY-306-MONOMER.

Family and domain databases

Gene3D3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProIPR003016. 2-oxoA_DH_lipoyl-BS.
IPR001078. 2-oxoacid_DH_actylTfrase.
IPR000089. Biotin_lipoyl.
IPR023213. CAT-like_dom.
IPR004167. E3-bd.
IPR006257. LAT1.
IPR011053. Single_hybrid_motif.
[Graphical view]
PfamPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 1 hit.
TIGRFAMsTIGR01349. PDHac_trf_mito. 1 hit.
PROSITEPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameODP2_RICBR
AccessionPrimary (citable) accession number: Q1RJT3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: May 16, 2006
Last modified: June 11, 2014
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Rickettsia bellii strain RML369-C

Rickettsia bellii (strain RML369-C): entries and gene names