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Protein

Acetyltransferase component of pyruvate dehydrogenase complex

Gene

pdhC

Organism
Chlamydia trachomatis serovar B (strain Jali20/OT)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2.UniRule annotation

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:
  • (R)-lipoateUniRule annotationNote: Binds 1 lipoyl cofactor covalently.UniRule annotation
  • (R)-lipoateUniRule annotationNote: Binds 2 lipoyl cofactors covalently.UniRule annotation
  • (R)-lipoateUniRule annotationNote: Binds 3 lipoyl cofactors covalently.UniRule annotation

GO - Molecular functioni

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

GO - Biological processi

  1. pyruvate metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

AcyltransferaseUniRule annotation, Transferase

Keywords - Ligandi

PyruvateImported

Enzyme and pathway databases

BioCyciCTRA580049:GH1T-261-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetyltransferase component of pyruvate dehydrogenase complexUniRule annotation (EC:2.3.1.12UniRule annotation)
Gene namesi
Name:pdhCImported
Ordered Locus Names:JALI_2421Imported
OrganismiChlamydia trachomatis serovar B (strain Jali20/OT)Imported
Taxonomic identifieri580049 [NCBI]
Taxonomic lineageiBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydia
ProteomesiUP000002053: Chromosome

Subcellular locationi

GO - Cellular componenti

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

Interactioni

Protein-protein interaction databases

STRINGi580049.JALI_2421.

Structurei

3D structure databases

ProteinModelPortaliC4PQR9.
SMRiC4PQR9. Positions 7-66.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

LipoylUniRule annotation

Phylogenomic databases

eggNOGiCOG0508.
HOGENOMiHOG000281566.
KOiK00627.
OMAiVESCIIT.
OrthoDBiEOG610413.

Family and domain databases

Gene3Di3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProiIPR001078. 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.
[Graphical view]

Sequencei

Sequence statusi: Complete.

C4PQR9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVSLLKMPKL SPTMEIGILV KWHKKAGDEI HFGDVLLEIS TDKAVLEHTA
60 70 80 90 100
SEDGWLLEIL VEEGTKTPIG TPIAVFSTEQ NAQYDLKQLL PLEGTVVTDA
110 120 130 140 150
ATEASPKNSA QTDSQYTSGP SITMMGFRPE PPLAIPLTIK HSNDPVLASP
160 170 180 190 200
LAKKLAKEQN LDLSGVTGSG PGGRIVKKDL EKAPPLRIAG FGYPEAPNVN
210 220 230 240 250
PGSYIEEPLS PVREVISKRL QAAKTFIPHF YVRQRIYASP LLALLKELQE
260 270 280 290 300
QNIKLSINDC IVRACALALK EFPEINSGFN SVDNKIIRFS TIDISIAVAI
310 320 330 340 350
PDGVITPIVR CADRKNIGMI SAEIKGLATK AKQQSLAEEE YKGGSFCVSN
360 370 380 390 400
LGMTGISDFT AILNPPQAAI LAVGSVEEQP VVLNGELAVG LTCMLTLSVD
410 420
HRVIDGYPAA MFMKRLQRLL EAPSVLLLN
Length:429
Mass (Da):46,352
Last modified:November 3, 2009 - v1
Checksum:i1D6FA66A67E41180
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FM872308 Genomic DNA. Translation: CAX10696.1.
RefSeqiYP_002887864.1. NC_012686.1.

Genome annotation databases

EnsemblBacteriaiCAX10696; CAX10696; JALI_2421.
GeneIDi7881633.
KEGGictj:JALI_2421.
PATRICi20378012. VBIChlTra100303_0285.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FM872308 Genomic DNA. Translation: CAX10696.1.
RefSeqiYP_002887864.1. NC_012686.1.

3D structure databases

ProteinModelPortaliC4PQR9.
SMRiC4PQR9. Positions 7-66.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi580049.JALI_2421.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAX10696; CAX10696; JALI_2421.
GeneIDi7881633.
KEGGictj:JALI_2421.
PATRICi20378012. VBIChlTra100303_0285.

Phylogenomic databases

eggNOGiCOG0508.
HOGENOMiHOG000281566.
KOiK00627.
OMAiVESCIIT.
OrthoDBiEOG610413.

Enzyme and pathway databases

BioCyciCTRA580049:GH1T-261-MONOMER.

Family and domain databases

Gene3Di3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProiIPR001078. 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.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Jali20/OTImported.

Entry informationi

Entry nameiC4PQR9_CHLTJ
AccessioniPrimary (citable) accession number: C4PQR9
Entry historyi
Integrated into UniProtKB/TrEMBL: November 3, 2009
Last sequence update: November 3, 2009
Last modified: January 7, 2015
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported

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.