Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex

Gene

pdhC

Organism
Rickettsia prowazekii (strain Madrid E)
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 sitei381 – 3811Sequence 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:RP530
OrganismiRickettsia prowazekii (strain Madrid E)
Taxonomic identifieri272947 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiatyphus group
ProteomesiUP000002480: 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 – 408408Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complexPRO_0000162286Add
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

STRINGi272947.RP530.

Structurei

3D structure databases

ProteinModelPortaliQ9ZD20.
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.
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.

Q9ZD20-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPIKILMPAL SPTMREGNLA RWLKKEGDKV NPGEVIAEIE TDKATMEVES
60 70 80 90 100
VDEGILAKII IPQNSQNVPV NSLIAVLSEE GEDKADIDSF IAQNNSVSLS
110 120 130 140 150
LKTDATLKKS NDSITNVEGI KHDSNKIFAS PLAKRLAKIG DIRLENVQGS
160 170 180 190 200
GPHGRIVKQD ILSYDSSTSS NKIVYRDTEE YRSVPNNNIR KIIAKRLLES
210 220 230 240 250
KQTVPHFYLS IECNVDKLLD VREDINKSFS EDKVTKISVN DFIILAVAKA
260 270 280 290 300
LQEVPNANAS WSEDAIRYYN NVDISVAVAI ENGIVTPIVK DANKKNIIEL
310 320 330 340 350
SREMKTLIKK AKDNKLTPIE FQGGGFTISN LGMYGIKNFN AIINTPQSCI
360 370 380 390 400
MGVGASTKRA IVKNDQIIIA TIMDVTLSAD HRVIDGAVSA EFLASFKRFI

ENPVLMLI
Length:408
Mass (Da):44,967
Last modified:May 1, 1999 - v1
Checksum:i312093D57AFAA964
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ235272 Genomic DNA. Translation: CAA14979.1.
PIRiA71657.
RefSeqiNP_220903.1. NC_000963.1.

Genome annotation databases

EnsemblBacteriaiCAA14979; CAA14979; CAA14979.
GeneIDi883200.
KEGGirpr:RP530.
PATRICi17901846. VBIRicPro72556_0538.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ235272 Genomic DNA. Translation: CAA14979.1.
PIRiA71657.
RefSeqiNP_220903.1. NC_000963.1.

3D structure databases

ProteinModelPortaliQ9ZD20.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272947.RP530.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAA14979; CAA14979; CAA14979.
GeneIDi883200.
KEGGirpr:RP530.
PATRICi17901846. VBIRicPro72556_0538.

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: Madrid E.

Entry informationi

Entry nameiODP2_RICPR
AccessioniPrimary (citable) accession number: Q9ZD20
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1999
Last modified: January 7, 2015
This is version 90 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, Reference proteome

Documents

  1. Rickettsia prowazekii
    Rickettsia prowazekii (strain Madrid E): 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.