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Protein

Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial

Gene

F23B12.5

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

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).Curated

Catalytic activityi

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

Cofactori

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei480 – 4801Sequence Analysis
Active sitei484 – 4841Sequence 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

Enzyme and pathway databases

ReactomeiREACT_319260. Regulation of pyruvate dehydrogenase (PDH) complex.
REACT_348544. Pyruvate metabolism.
REACT_351896. Signaling by Retinoic Acid.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
ORF Names:F23B12.5
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
ProteomesiUP000001940 Componenti: Chromosome V

Organism-specific databases

WormBaseiF23B12.5; CE09597; WBGene00009082.

Subcellular locationi

  1. Mitochondrion matrix By similarity

GO - Cellular componenti

  1. mitochondrial matrix Source: UniProtKB-SubCell
  2. pyruvate dehydrogenase complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 507Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrialPRO_0000244484
Transit peptidei1 – ?MitochondrionSequence Analysis

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei118 – 1181N6-lipoyllysinePROSITE-ProRule annotationBy similarity

Proteomic databases

PaxDbiQ19749.

2D gel databases

World-2DPAGE0020:Q19749.

Interactioni

Protein-protein interaction databases

BioGridi44949. 17 interactions.
DIPiDIP-24773N.
IntActiQ19749. 19 interactions.
MINTiMINT-1106052.
STRINGi6239.F23B12.5.

Structurei

3D structure databases

ProteinModelPortaliQ19749.
SMRiQ19749. Positions 80-158, 220-263, 275-507.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini77 – 15377Lipoyl-bindingPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the 2-oxoacid dehydrogenase family.Sequence Analysis
Contains 1 lipoyl-binding domain.PROSITE-ProRule annotation

Keywords - Domaini

Lipoyl, Repeat, Transit peptide

Phylogenomic databases

eggNOGiCOG0508.
GeneTreeiENSGT00760000119281.
HOGENOMiHOG000281566.
InParanoidiQ19749.
KOiK00627.
OMAiATMEFES.
PhylomeDBiQ19749.

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q19749-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKFPVPLRT IGGLRPSTTA AISAANIGFT QSSRALSTGA AAKSSGLVGQ
60 70 80 90 100
VARQYPNAAA FSIKQVRLYS SGNLPKHNRV ALPALSPTME LGTVVSWQKK
110 120 130 140 150
EGDQLSEGDL LCEIETDKAT MGFETPEEGY LAKILIQEGS KDVPIGKLLC
160 170 180 190 200
IIVDNEADVA AFKDFKDDGA SSGGSAPAAE KAPEPAKPAA SSQPSPPAQM
210 220 230 240 250
YQAPSVPKSA PIPHSSSGRV SASPFAKKLA AENGLDLSGV SGSGPGGRIL
260 270 280 290 300
ASDLSQAPAK GATSTTTQAV SGQDYTDIPL SNMRKTIAKR LTESKSTIPH
310 320 330 340 350
YYLTSEIQLD TLLQVREKLN GLLAKGTSGQ ATKISINDFI IKASALACQR
360 370 380 390 400
VPEANSYWMD SFIRENHHVD VSVAVSTPAG LITPIIFNAH AKGLATIASE
410 420 430 440 450
IVELAQRARE GKLQPHEFQG GTFTVSNLGM FGSVSDFTAI INPPQSCILA
460 470 480 490 500
IGGASDKLVP DEAEGYKKIK TMKVTLSCDH RTVDGAVGAV WLRHFKEFLE

KPHTMLL
Length:507
Mass (Da):53,467
Last modified:November 1, 1996 - v1
Checksum:i2C546DA3828C5B09
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z77659 Genomic DNA. Translation: CAB01163.1.
PIRiT21287.
RefSeqiNP_506579.1. NM_074178.6.
UniGeneiCel.17215.

Genome annotation databases

EnsemblMetazoaiF23B12.5; F23B12.5; WBGene00009082.
GeneIDi179945.
KEGGicel:CELE_F23B12.5.
UCSCiF23B12.5. c. elegans.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z77659 Genomic DNA. Translation: CAB01163.1.
PIRiT21287.
RefSeqiNP_506579.1. NM_074178.6.
UniGeneiCel.17215.

3D structure databases

ProteinModelPortaliQ19749.
SMRiQ19749. Positions 80-158, 220-263, 275-507.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi44949. 17 interactions.
DIPiDIP-24773N.
IntActiQ19749. 19 interactions.
MINTiMINT-1106052.
STRINGi6239.F23B12.5.

2D gel databases

World-2DPAGE0020:Q19749.

Proteomic databases

PaxDbiQ19749.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiF23B12.5; F23B12.5; WBGene00009082.
GeneIDi179945.
KEGGicel:CELE_F23B12.5.
UCSCiF23B12.5. c. elegans.

Organism-specific databases

CTDi179945.
WormBaseiF23B12.5; CE09597; WBGene00009082.

Phylogenomic databases

eggNOGiCOG0508.
GeneTreeiENSGT00760000119281.
HOGENOMiHOG000281566.
InParanoidiQ19749.
KOiK00627.
OMAiATMEFES.
PhylomeDBiQ19749.

Enzyme and pathway databases

ReactomeiREACT_319260. Regulation of pyruvate dehydrogenase (PDH) complex.
REACT_348544. Pyruvate metabolism.
REACT_351896. Signaling by Retinoic Acid.

Miscellaneous databases

NextBioi907498.
PROiQ19749.

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

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiODP2_CAEEL
AccessioniPrimary (citable) accession number: Q19749
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: November 1, 1996
Last modified: April 1, 2015
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

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