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Protein

Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex

Gene

pdhC

Organism
Rickettsia felis (strain ATCC VR-1525 / URRWXCal2) (Rickettsia azadi)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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).By similarity

Catalytic activityi

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

Cofactori

(R)-lipoateBy similarityNote: Binds 1 lipoyl cofactor covalently.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei385 – 3851Sequence Analysis

GO - Molecular functioni

  1. dihydrolipoyllysine-residue acetyltransferase activity Source: UniProtKB-EC

GO - Biological processi

  1. glycolytic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Glycolysis

Enzyme and pathway databases

BioCyciRETL1328306-WGS:GSTH-1994-MONOMER.
RFEL315456:GKEK-780-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:pdhC
Ordered Locus Names:RF_0761
OrganismiRickettsia felis (strain ATCC VR-1525 / URRWXCal2) (Rickettsia azadi)
Taxonomic identifieri315456 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiaspotted fever group
ProteomesiUP000008548: Chromosome

Subcellular locationi

GO - Cellular componenti

  1. pyruvate dehydrogenase complex Source: InterPro
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 412412Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complexPRO_0000288764Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei43 – 431N6-lipoyllysineBy similarityPROSITE-ProRule annotation

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi315456.RF_0761.

Structurei

3D structure databases

ProteinModelPortaliQ4ULG1.
SMRiQ4ULG1. Positions 183-412.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 7877Lipoyl-bindingPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the 2-oxoacid dehydrogenase family.Curated
Contains 1 lipoyl-binding domain.CuratedPROSITE-ProRule annotation

Keywords - Domaini

Lipoyl

Phylogenomic databases

eggNOGiCOG0508.
HOGENOMiHOG000281566.
KOiK00627.
OMAiTRVNDIL.
OrthoDBiEOG610413.

Family and domain databases

Gene3Di3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProiIPR003016. 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]
PfamiPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMiSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 1 hit.
TIGRFAMsiTIGR01349. PDHac_trf_mito. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q4ULG1-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPIKILMPVL SPTMTEGNLA RWLKKEGDKV NPGEVIAEIE TDKATMEVEA
60 70 80 90 100
VDEGILAKIV IPQNSQNVPV NSLIAVLSEE GEEKTDIDAF IAKNNNVSPS
110 120 130 140 150
PKTDANLPKP HENIAKVEEQ VAVIKHDASK IFASPLAKRL AKMGNIRLES
160 170 180 190 200
VKGSGPHGRI VKQDILSYTP STVHNKIVSR NPEEYRLVPN NNIRKIIAKR
210 220 230 240 250
LLESKQTVPH FYLSIECNVD KLLDIREDIN KSFSEDKSTR ISVNDFIILA
260 270 280 290 300
VAKALQELPN ANASWGEDAI RYHNNVDISV AVAIENGLVT PIVKNANQKN
310 320 330 340 350
IIELSREMKE LIKKAKDNKL TPEEFQGGGF TISNLGMYGI KNFNAIINPP
360 370 380 390 400
QSCIMGVGAS AKRAIVKNDQ VTIATIMDVT LSADHRVVDG AVGAEFLAAF
410
KKFIESPALM LI
Length:412
Mass (Da):45,220
Last modified:July 5, 2005 - v1
Checksum:iCF7CE592B67A8DFB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000053 Genomic DNA. Translation: AAY61612.1.
RefSeqiYP_246777.1. NC_007109.1.

Genome annotation databases

EnsemblBacteriaiAAY61612; AAY61612; RF_0761.
GeneIDi3400828.
KEGGirfe:RF_0761.
PATRICi17892180. VBIRicFel64634_0918.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000053 Genomic DNA. Translation: AAY61612.1.
RefSeqiYP_246777.1. NC_007109.1.

3D structure databases

ProteinModelPortaliQ4ULG1.
SMRiQ4ULG1. Positions 183-412.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi315456.RF_0761.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAY61612; AAY61612; RF_0761.
GeneIDi3400828.
KEGGirfe:RF_0761.
PATRICi17892180. VBIRicFel64634_0918.

Phylogenomic databases

eggNOGiCOG0508.
HOGENOMiHOG000281566.
KOiK00627.
OMAiTRVNDIL.
OrthoDBiEOG610413.

Enzyme and pathway databases

BioCyciRETL1328306-WGS:GSTH-1994-MONOMER.
RFEL315456:GKEK-780-MONOMER.

Family and domain databases

Gene3Di3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProiIPR003016. 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]
PfamiPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMiSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 1 hit.
TIGRFAMsiTIGR01349. PDHac_trf_mito. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The genome sequence of Rickettsia felis identifies the first putative conjugative plasmid in an obligate intracellular parasite."
    Ogata H., Renesto P., Audic S., Robert C., Blanc G., Fournier P.-E., Parinello H., Claverie J.-M., Raoult D.
    PLoS Biol. 3:1-12(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC VR-1525 / URRWXCal2.

Entry informationi

Entry nameiODP2_RICFE
AccessioniPrimary (citable) accession number: Q4ULG1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: July 5, 2005
Last modified: January 7, 2015
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. Rickettsia felis (Rickettsia azadi)
    Rickettsia felis (strain URRWXCal2): entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.