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Q9ZD20

- ODP2_RICPR

UniProt

Q9ZD20 - ODP2_RICPR

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Protein

Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex

Gene

pdhC

Organism
Rickettsia prowazekii (strain Madrid E)
Status
Reviewed - 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

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 similarity

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
Domaini1 – 7777Lipoyl-bindingAdd
BLAST

Sequence similaritiesi

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

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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
AJ235272 Genomic DNA. Translation: CAA14979.1 .
PIRi A71657.
RefSeqi NP_220903.1. NC_000963.1.

3D structure databases

ProteinModelPortali Q9ZD20.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 272947.RP530.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAA14979 ; CAA14979 ; CAA14979 .
GeneIDi 883200.
KEGGi rpr:RP530.
PATRICi 17901846. VBIRicPro72556_0538.

Phylogenomic databases

eggNOGi COG0508.
HOGENOMi HOG000281566.
KOi K00627.
OMAi VESCIIT.
OrthoDBi EOG610413.

Family and domain databases

Gene3Di 3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProi IPR003016. 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 ]
Pfami PF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF02817. E3_binding. 1 hit.
[Graphical view ]
SUPFAMi SSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 1 hit.
TIGRFAMsi TIGR01349. PDHac_trf_mito. 1 hit.
PROSITEi PS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: October 1, 2014
This is version 88 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