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Protein

Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex

Gene

pdhC

Organism
Rickettsia conorii (strain ATCC VR-613 / Malish 7)
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

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:RC0764
OrganismiRickettsia conorii (strain ATCC VR-613 / Malish 7)
Taxonomic identifieri272944 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiaspotted fever group
ProteomesiUP000000816 Componenti: 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_0000162285Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei43 – 431N6-lipoyllysinePROSITE-ProRule annotationBy similarity

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi272944.RC0764.

Structurei

3D structure databases

ProteinModelPortaliQ92HK7.
SMRiQ92HK7. 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.PROSITE-ProRule annotationCurated

Keywords - Domaini

Lipoyl

Phylogenomic databases

eggNOGiCOG0508.
HOGENOMiHOG000281566.
KOiK00627.
OMAiVESCIIT.
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.

Q92HK7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPIKILMPAL SPTMTEGNLA RWLKKEGDKV NPGEVIAEIE TDKATMEVEA
60 70 80 90 100
VDEGILAKIV IPQNSQNVPV NSLIAVLSEE GEEKTDIDAF IAKNNSVSPS
110 120 130 140 150
PKTDANLPKP HENIANVEEQ VTVIKHDVSR IFASPLAKRL AKMRNIRFES
160 170 180 190 200
VKGSGPHGRI VKQDILSYTP STAHNKIVSR NPEEYRLVPN NNIRKIIAKR
210 220 230 240 250
LLESKQTVPH FYLSIECNVD KLLDIREDIN KFFSEDKSTR ISVNDFIILA
260 270 280 290 300
VAKALQEVPN ANASWGEDAI RYYNNVDISV AVAIENGLVT PIVKNANQKN
310 320 330 340 350
ILELSREMKA LIKKAKDNKL TPEEFQGGGF TISNLGMYGI KNFNAIINPP
360 370 380 390 400
QSCIMGVGAS AKRAIVKNDQ ITIATIMDVT LSADHRVVDG AVGAEFLVAF
410
KKFIESPVLM LI
Length:412
Mass (Da):45,426
Last modified:December 1, 2001 - v1
Checksum:i26E645592CB4B933
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE006914 Genomic DNA. Translation: AAL03302.1.
PIRiD97795.
RefSeqiNP_360401.1. NC_003103.1.

Genome annotation databases

EnsemblBacteriaiAAL03302; AAL03302; RC0764.
KEGGirco:RC0764.
PATRICi17888848. VBIRicCon45613_0867.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE006914 Genomic DNA. Translation: AAL03302.1.
PIRiD97795.
RefSeqiNP_360401.1. NC_003103.1.

3D structure databases

ProteinModelPortaliQ92HK7.
SMRiQ92HK7. Positions 183-412.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272944.RC0764.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAL03302; AAL03302; RC0764.
KEGGirco:RC0764.
PATRICi17888848. VBIRicCon45613_0867.

Phylogenomic databases

eggNOGiCOG0508.
HOGENOMiHOG000281566.
KOiK00627.
OMAiVESCIIT.
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]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC VR-613 / Malish 7.

Entry informationi

Entry nameiODP2_RICCN
AccessioniPrimary (citable) accession number: Q92HK7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 16, 2003
Last sequence update: December 1, 2001
Last modified: April 29, 2015
This is version 86 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 conorii
    (strain Malish 7): 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.