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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: -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 N6-(dihydrolipoyl)lysine = CoA + enzyme N6-(S-acetyldihydrolipoyl)lysine.

Cofactori

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei385Sequence analysis1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionAcyltransferase, Transferase
Biological processGlycolysis

Enzyme and pathway databases

BioCyciRCON272944:G1FZG-1271-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:RC0764
OrganismiRickettsia conorii (strain ATCC VR-613 / Malish 7)
Taxonomic identifieri272944 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiaspotted fever group
Proteomesi
  • UP000000816 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001622851 – 412Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complexAdd BLAST412

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei43N6-lipoyllysinePROSITE-ProRule annotationBy similarity1

Proteomic databases

PRIDEiQ92HK7

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliQ92HK7
SMRiQ92HK7
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 78Lipoyl-bindingPROSITE-ProRule annotationAdd BLAST77
Domaini132 – 169Peripheral subunit-binding (PSBD)PROSITE-ProRule annotationAdd BLAST38

Sequence similaritiesi

Belongs to the 2-oxoacid dehydrogenase family.Curated

Keywords - Domaini

Lipoyl

Phylogenomic databases

HOGENOMiHOG000281566
KOiK00627
OMAiSWRLGCD
OrthoDBiPOG091H0NG1

Family and domain databases

Gene3Di3.30.559.10, 1 hit
4.10.320.10, 1 hit
InterProiView protein in InterPro
IPR003016 2-oxoA_DH_lipoyl-BS
IPR001078 2-oxoacid_DH_actylTfrase
IPR000089 Biotin_lipoyl
IPR023213 CAT-like_dom_sf
IPR036625 E3-bd_dom_sf
IPR006257 LAT1
IPR004167 PSBD
IPR011053 Single_hybrid_motif
PfamiView protein in Pfam
PF00198 2-oxoacid_dh, 1 hit
PF00364 Biotin_lipoyl, 1 hit
PF02817 E3_binding, 1 hit
SUPFAMiSSF47005 SSF47005, 1 hit
SSF51230 SSF51230, 1 hit
TIGRFAMsiTIGR01349 PDHac_trf_mito, 1 hit
PROSITEiView protein in PROSITE
PS50968 BIOTINYL_LIPOYL, 1 hit
PS00189 LIPOYL, 1 hit
PS51826 PSBD, 1 hit

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
RefSeqiWP_010977380.1, NC_003103.1

Genome annotation databases

EnsemblBacteriaiAAL03302; AAL03302; RC0764
GeneIDi927481
KEGGirco:RC0764
PATRICifig|272944.4.peg.867

Entry informationi

Entry nameiODP2_RICCN
AccessioniPrimary (citable) accession number: Q92HK7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 16, 2003
Last sequence update: December 1, 2001
Last modified: May 23, 2018
This is version 104 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

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