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Q19749 (ODP2_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial

EC=2.3.1.12
Alternative name(s):
Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
Pyruvate dehydrogenase complex component E2
Short name=PDC-E2
Short name=PDCE2
Gene names
ORF Names:F23B12.5
OrganismCaenorhabditis elegans [Reference proteome]
Taxonomic identifier6239 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis

Protein attributes

Sequence length507 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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).

Catalytic activity

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

Cofactor

Binds 1 lipoyl cofactor covalently By similarity.

Subcellular location

Mitochondrion matrix By similarity.

Sequence similarities

Belongs to the 2-oxoacid dehydrogenase family.

Contains 1 lipoyl-binding domain.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Mitochondrion
Chain? – 507Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrialPRO_0000244484

Regions

Domain78 – 15275Lipoyl-binding

Sites

Active site4801 Potential
Active site4841 Potential

Amino acid modifications

Modified residue1181N6-lipoyllysine

Sequences

Sequence LengthMass (Da)Tools
Q19749 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 2C546DA3828C5B09

FASTA50753,467
        10         20         30         40         50         60 
MSKFPVPLRT IGGLRPSTTA AISAANIGFT QSSRALSTGA AAKSSGLVGQ VARQYPNAAA 

        70         80         90        100        110        120 
FSIKQVRLYS SGNLPKHNRV ALPALSPTME LGTVVSWQKK EGDQLSEGDL LCEIETDKAT 

       130        140        150        160        170        180 
MGFETPEEGY LAKILIQEGS KDVPIGKLLC IIVDNEADVA AFKDFKDDGA SSGGSAPAAE 

       190        200        210        220        230        240 
KAPEPAKPAA SSQPSPPAQM YQAPSVPKSA PIPHSSSGRV SASPFAKKLA AENGLDLSGV 

       250        260        270        280        290        300 
SGSGPGGRIL ASDLSQAPAK GATSTTTQAV SGQDYTDIPL SNMRKTIAKR LTESKSTIPH 

       310        320        330        340        350        360 
YYLTSEIQLD TLLQVREKLN GLLAKGTSGQ ATKISINDFI IKASALACQR VPEANSYWMD 

       370        380        390        400        410        420 
SFIRENHHVD VSVAVSTPAG LITPIIFNAH AKGLATIASE IVELAQRARE GKLQPHEFQG 

       430        440        450        460        470        480 
GTFTVSNLGM FGSVSDFTAI INPPQSCILA IGGASDKLVP DEAEGYKKIK TMKVTLSCDH 

       490        500 
RTVDGAVGAV WLRHFKEFLE KPHTMLL 

« Hide

References

« Hide 'large scale' references
[1]"Genome sequence of the nematode C. elegans: a platform for investigating biology."
The C. elegans sequencing consortium
Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Bristol N2.
[2]Bienvenut W.V.
Submitted (MAR-2006) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 249-260; 334-350; 393-407 AND 482-493, IDENTIFICATION BY MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z77659 Genomic DNA. Translation: CAB01163.1.
PIRT21287.
RefSeqNP_506579.1. NM_074178.6.
UniGeneCel.17215.

3D structure databases

ProteinModelPortalQ19749.
SMRQ19749. Positions 80-158, 221-261, 275-507.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid44949. 17 interactions.
DIPDIP-24773N.
IntActQ19749. 19 interactions.
MINTMINT-1106052.
STRING6239.F23B12.5.

2D gel databases

World-2DPAGE0020:Q19749.

Proteomic databases

PaxDbQ19749.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaF23B12.5.1; F23B12.5.1; F23B12.5.
F23B12.5.2; F23B12.5.2; F23B12.5.
GeneID179945.
KEGGcel:CELE_F23B12.5.
UCSCF23B12.5. c. elegans.

Organism-specific databases

CTD179945.
WormBaseF23B12.5; CE09597; WBGene00009082.

Phylogenomic databases

eggNOGCOG0508.
HOGENOMHOG000281566.
InParanoidQ19749.
KOK00627.
OMAATMEFES.
PhylomeDBQ19749.

Family and domain databases

Gene3D3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProIPR003016. 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]
PfamPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 1 hit.
TIGRFAMsTIGR01349. PDHac_trf_mito. 1 hit.
PROSITEPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio907498.
PROQ19749.

Entry information

Entry nameODP2_CAEEL
AccessionPrimary (citable) accession number: Q19749
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Caenorhabditis elegans

Caenorhabditis elegans: entries, gene names and cross-references to WormBase