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Q92HK7 (ODP2_RICCN) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 78. 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:RC0764
OrganismRickettsia conorii (strain ATCC VR-613 / Malish 7) [Complete proteome] [HAMAP]
Taxonomic identifier272944 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiaspotted fever group

Protein attributes

Sequence length412 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_processglycolysis

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 – 412412Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
PRO_0000162285

Regions

Domain1 – 7777Lipoyl-binding

Sites

Active site3851 Potential

Amino acid modifications

Modified residue431N6-lipoyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q92HK7 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 26E645592CB4B933

FASTA41245,426
        10         20         30         40         50         60 
MPIKILMPAL SPTMTEGNLA RWLKKEGDKV NPGEVIAEIE TDKATMEVEA VDEGILAKIV 

        70         80         90        100        110        120 
IPQNSQNVPV NSLIAVLSEE GEEKTDIDAF IAKNNSVSPS PKTDANLPKP HENIANVEEQ 

       130        140        150        160        170        180 
VTVIKHDVSR IFASPLAKRL AKMRNIRFES VKGSGPHGRI VKQDILSYTP STAHNKIVSR 

       190        200        210        220        230        240 
NPEEYRLVPN NNIRKIIAKR LLESKQTVPH FYLSIECNVD KLLDIREDIN KFFSEDKSTR 

       250        260        270        280        290        300 
ISVNDFIILA VAKALQEVPN ANASWGEDAI RYYNNVDISV AVAIENGLVT PIVKNANQKN 

       310        320        330        340        350        360 
ILELSREMKA LIKKAKDNKL TPEEFQGGGF TISNLGMYGI KNFNAIINPP QSCIMGVGAS 

       370        380        390        400        410 
AKRAIVKNDQ ITIATIMDVT LSADHRVVDG AVGAEFLVAF KKFIESPVLM LI 

« Hide

References

[1]"Mechanisms of evolution in Rickettsia conorii and R. prowazekii."
Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V., Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.
Science 293:2093-2098(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC VR-613 / Malish 7.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE006914 Genomic DNA. Translation: AAL03302.1.
PIRD97795.
RefSeqNP_360401.1. NC_003103.1.

3D structure databases

ProteinModelPortalQ92HK7.
SMRQ92HK7. Positions 183-412.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272944.RC0764.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL03302; AAL03302; RC0764.
GeneID927481.
KEGGrco:RC0764.
PATRIC17888848. VBIRicCon45613_0867.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0508.
HOGENOMHOG000281566.
KOK00627.
OMAKSTRISV.
OrthoDBEOG610413.
ProtClustDBPRK11856.

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_RICCN
AccessionPrimary (citable) accession number: Q92HK7
Entry history
Integrated into UniProtKB/Swiss-Prot: June 16, 2003
Last sequence update: December 1, 2001
Last modified: November 13, 2013
This is version 78 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 conorii

(strain Malish 7): entries and gene names