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Q9ZD20 (ODP2_RICPR) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 87. 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:RP530
OrganismRickettsia prowazekii (strain Madrid E) [Reference proteome] [HAMAP]
Taxonomic identifier272947 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiatyphus group

Protein attributes

Sequence length408 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
Reference 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 – 408408Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
PRO_0000162286

Regions

Domain1 – 7777Lipoyl-binding

Sites

Active site3811 Potential

Amino acid modifications

Modified residue431N6-lipoyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9ZD20 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 312093D57AFAA964

FASTA40844,967
        10         20         30         40         50         60 
MPIKILMPAL SPTMREGNLA RWLKKEGDKV NPGEVIAEIE TDKATMEVES VDEGILAKII 

        70         80         90        100        110        120 
IPQNSQNVPV NSLIAVLSEE GEDKADIDSF IAQNNSVSLS LKTDATLKKS NDSITNVEGI 

       130        140        150        160        170        180 
KHDSNKIFAS PLAKRLAKIG DIRLENVQGS GPHGRIVKQD ILSYDSSTSS NKIVYRDTEE 

       190        200        210        220        230        240 
YRSVPNNNIR KIIAKRLLES KQTVPHFYLS IECNVDKLLD VREDINKSFS EDKVTKISVN 

       250        260        270        280        290        300 
DFIILAVAKA LQEVPNANAS WSEDAIRYYN NVDISVAVAI ENGIVTPIVK DANKKNIIEL 

       310        320        330        340        350        360 
SREMKTLIKK AKDNKLTPIE FQGGGFTISN LGMYGIKNFN AIINTPQSCI MGVGASTKRA 

       370        380        390        400 
IVKNDQIIIA TIMDVTLSAD HRVIDGAVSA EFLASFKRFI ENPVLMLI 

« Hide

References

[1]"The genome sequence of Rickettsia prowazekii and the origin of mitochondria."
Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T., Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H., Kurland C.G.
Nature 396:133-140(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Madrid E.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ235272 Genomic DNA. Translation: CAA14979.1.
PIRA71657.
RefSeqNP_220903.1. NC_000963.1.

3D structure databases

ProteinModelPortalQ9ZD20.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272947.RP530.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAA14979; CAA14979; CAA14979.
GeneID883200.
KEGGrpr:RP530.
PATRIC17901846. VBIRicPro72556_0538.

Phylogenomic databases

eggNOGCOG0508.
HOGENOMHOG000281566.
KOK00627.
OMAVESCIIT.
OrthoDBEOG610413.

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_RICPR
AccessionPrimary (citable) accession number: Q9ZD20
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1999
Last modified: June 11, 2014
This is version 87 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 prowazekii

Rickettsia prowazekii (strain Madrid E): entries and gene names