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Q19749

- ODP2_CAEEL

UniProt

Q19749 - ODP2_CAEEL

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Protein

Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial

Gene

F23B12.5

Organism
Caenorhabditis elegans
Status
Reviewed - 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_257024. Pyruvate metabolism.
REACT_263254. Regulation of pyruvate dehydrogenase (PDH) complex.

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: Chromosome V

Organism-specific databases

WormBaseiF23B12.5; CE09597; WBGene00009082.

Subcellular locationi

Mitochondrion matrix By similarity

GO - Cellular componenti

  1. mitochondrion Source: UniProtKB-KW
  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-lipoyllysineBy similarityPROSITE-ProRule annotation

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, 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.
OMAiPISNIRK.
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 .
PIRi T21287.
RefSeqi NP_506579.1. NM_074178.6.
UniGenei Cel.17215.

3D structure databases

ProteinModelPortali Q19749.
SMRi Q19749. Positions 80-158, 275-507.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 44949. 17 interactions.
DIPi DIP-24773N.
IntActi Q19749. 19 interactions.
MINTi MINT-1106052.
STRINGi 6239.F23B12.5.

2D gel databases

World-2DPAGE 0020:Q19749.

Proteomic databases

PaxDbi Q19749.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai F23B12.5 ; F23B12.5 ; WBGene00009082 .
GeneIDi 179945.
KEGGi cel:CELE_F23B12.5.
UCSCi F23B12.5. c. elegans.

Organism-specific databases

CTDi 179945.
WormBasei F23B12.5 ; CE09597 ; WBGene00009082 .

Phylogenomic databases

eggNOGi COG0508.
GeneTreei ENSGT00760000119281.
HOGENOMi HOG000281566.
InParanoidi Q19749.
KOi K00627.
OMAi PISNIRK.
PhylomeDBi Q19749.

Enzyme and pathway databases

Reactomei REACT_257024. Pyruvate metabolism.
REACT_263254. Regulation of pyruvate dehydrogenase (PDH) complex.

Miscellaneous databases

NextBioi 907498.
PROi Q19749.

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

« 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: November 26, 2014
This is version 121 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