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Protein

Dihydrolipoyllysine-residue acetyltransferase component 2 of pyruvate dehydrogenase complex, mitochondrial

Gene

At3g13930

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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).1 Publication

Catalytic activityi

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

Cofactori

(R)-lipoateNote: Binds 1 lipoyl cofactor covalently.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei512 – 5121Sequence Analysis
Active sitei516 – 5161Sequence Analysis

GO - Molecular functioni

  • copper ion binding Source: TAIR
  • dihydrolipoyllysine-residue acetyltransferase activity Source: UniProtKB-EC

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Glycolysis

Enzyme and pathway databases

BioCyciARA:AT3G13930-MONOMER.
ReactomeiREACT_285305. Signaling by Retinoic Acid.
REACT_290601. Pyruvate metabolism.
REACT_307000. Regulation of pyruvate dehydrogenase (PDH) complex.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydrolipoyllysine-residue acetyltransferase component 2 of pyruvate dehydrogenase complex, mitochondrial (EC:2.3.1.12)
Alternative name(s):
Dihydrolipoamide S-acetyltransferase component 2 of pyruvate dehydrogenase complex
Pyruvate dehydrogenase complex component E2 2
Short name:
PDC-E2 2
Short name:
PDCE2 2
Gene namesi
Ordered Locus Names:At3g13930
ORF Names:MDC16.5
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 3

Organism-specific databases

TAIRiAT3G13930.

Subcellular locationi

GO - Cellular componenti

  • chloroplast Source: TAIR
  • chloroplast envelope Source: TAIR
  • mitochondrial matrix Source: UniProtKB-SubCell
  • mitochondrion Source: TAIR
  • pyruvate dehydrogenase complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 539Dihydrolipoyllysine-residue acetyltransferase component 2 of pyruvate dehydrogenase complex, mitochondrialPRO_0000260026
Transit peptidei1 – ?Mitochondrion

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei152 – 1521N6-lipoyllysinePROSITE-ProRule annotationBy similarity

Proteomic databases

PaxDbiQ8RWN9.
PRIDEiQ8RWN9.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT3G13930.1.

Structurei

3D structure databases

ProteinModelPortaliQ8RWN9.
SMRiQ8RWN9. Positions 113-192, 246-286, 302-539.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini111 – 18777Lipoyl-bindingPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni250 – 28132E3-binding siteBy similarityAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Lipoyl, Transit peptide

Phylogenomic databases

eggNOGiCOG0508.
HOGENOMiHOG000281566.
InParanoidiQ8RWN9.
KOiK00627.
OMAiVESCIIT.
PhylomeDBiQ8RWN9.

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.

Q8RWN9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASRIINHSK KLKHVSALLR RDHAVAVRCF SNSTHPSLVG REDIFKARLN
60 70 80 90 100
YSSVERISKC GTGNVTMLSG ISTTSTKLSS PMAGPKLFKE FISSQMRSVR
110 120 130 140 150
GFSSSSDLPP HQEIGMPSLS PTMTEGNIAR WLKKEGDKVA PGEVLCEVET
160 170 180 190 200
DKATVEMECM EEGFLAKIVK EEGAKEIQVG EVIAITVEDE DDIQKFKDYT
210 220 230 240 250
PSSDTGPAAP EAKPAPSLPK EEKVEKPASA PEAKISKPSS APSEDRIFAS
260 270 280 290 300
PLARKLAEDN NVPLSSIKGT GPEGRIVKAD VEDFLASGSK ETTAKPSKQV
310 320 330 340 350
DSKVPALDYV DIPHTQIRKV TASRLAFSKQ TIPHYYLTVD TCVDKMMGLR
360 370 380 390 400
SQLNSFQEAS GGKRISVNDL VIKAAALALR KVPQCNSSWT DEYIRQFKNV
410 420 430 440 450
NINVAVQTEN GLYVPVVKDA DKKGLSTIGE EVRFLAQKAK ENSLKPEDYE
460 470 480 490 500
GGTFTVSNLG GPFGIKQFCA VINPPQAAIL AIGSAEKRVV PGTGPDQYNV
510 520 530
ASYMSVTLSC DHRVIDGAIG AEWLKAFKGY IETPESMLL
Length:539
Mass (Da):58,468
Last modified:November 28, 2006 - v2
Checksum:i219B4BE0E7ACD05A
GO

Sequence cautioni

The sequence BAB02323.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti124 – 1241T → A in AAM12967 (PubMed:14593172).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB019229 Genomic DNA. Translation: BAB02323.1. Sequence problems.
CP002686 Genomic DNA. Translation: AEE75442.1.
AF367302 mRNA. Translation: AAK32889.1.
AY091691 mRNA. Translation: AAM10290.1.
AY092968 mRNA. Translation: AAM12967.1.
BT000444 mRNA. Translation: AAN17421.1.
BT000702 mRNA. Translation: AAN31846.1.
BT001223 mRNA. Translation: AAN65110.1.
RefSeqiNP_566470.1. NM_112247.2.
UniGeneiAt.21338.

Genome annotation databases

EnsemblPlantsiAT3G13930.1; AT3G13930.1; AT3G13930.
GeneIDi820606.
KEGGiath:AT3G13930.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB019229 Genomic DNA. Translation: BAB02323.1. Sequence problems.
CP002686 Genomic DNA. Translation: AEE75442.1.
AF367302 mRNA. Translation: AAK32889.1.
AY091691 mRNA. Translation: AAM10290.1.
AY092968 mRNA. Translation: AAM12967.1.
BT000444 mRNA. Translation: AAN17421.1.
BT000702 mRNA. Translation: AAN31846.1.
BT001223 mRNA. Translation: AAN65110.1.
RefSeqiNP_566470.1. NM_112247.2.
UniGeneiAt.21338.

3D structure databases

ProteinModelPortaliQ8RWN9.
SMRiQ8RWN9. Positions 113-192, 246-286, 302-539.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT3G13930.1.

Proteomic databases

PaxDbiQ8RWN9.
PRIDEiQ8RWN9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT3G13930.1; AT3G13930.1; AT3G13930.
GeneIDi820606.
KEGGiath:AT3G13930.

Organism-specific databases

TAIRiAT3G13930.

Phylogenomic databases

eggNOGiCOG0508.
HOGENOMiHOG000281566.
InParanoidiQ8RWN9.
KOiK00627.
OMAiVESCIIT.
PhylomeDBiQ8RWN9.

Enzyme and pathway databases

BioCyciARA:AT3G13930-MONOMER.
ReactomeiREACT_285305. Signaling by Retinoic Acid.
REACT_290601. Pyruvate metabolism.
REACT_307000. Regulation of pyruvate dehydrogenase (PDH) complex.

Miscellaneous databases

PROiQ8RWN9.

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. "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence features of the regions of 4,504,864 bp covered by sixty P1 and TAC clones."
    Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.
    DNA Res. 7:131-135(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  4. "Experimental analysis of the Arabidopsis mitochondrial proteome highlights signaling and regulatory components, provides assessment of targeting prediction programs, and indicates plant-specific mitochondrial proteins."
    Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J., Millar A.H.
    Plant Cell 16:241-256(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Strain: cv. Landsberg erecta.
  5. "Lipoic acid-dependent oxidative catabolism of alpha-keto acids in mitochondria provides evidence for branched-chain amino acid catabolism in Arabidopsis."
    Taylor N.L., Heazlewood J.L., Day D.A., Millar A.H.
    Plant Physiol. 134:838-848(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiODP22_ARATH
AccessioniPrimary (citable) accession number: Q8RWN9
Secondary accession number(s): Q9ASS8, Q9LVK7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: November 28, 2006
Last modified: June 24, 2015
This is version 99 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  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.