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Q8RWN9 (ODP22_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 90. 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 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 names
Ordered Locus Names:At3g13930
ORF Names:MDC16.5
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length539 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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). Ref.5

Catalytic activity

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

Cofactor

Binds 1 lipoyl cofactor covalently.

Subcellular location

Mitochondrion matrix Ref.4.

Sequence similarities

Belongs to the 2-oxoacid dehydrogenase family.

Contains 1 lipoyl-binding domain.

Sequence caution

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Mitochondrion
Chain? – 539Dihydrolipoyllysine-residue acetyltransferase component 2 of pyruvate dehydrogenase complex, mitochondrialPRO_0000260026

Regions

Domain112 – 18675Lipoyl-binding
Region250 – 28132E3-binding site By similarity

Sites

Active site5121 Potential
Active site5161 Potential

Amino acid modifications

Modified residue1521N6-lipoyllysine By similarity

Experimental info

Sequence conflict1241T → A in AAM12967. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q8RWN9 [UniParc].

Last modified November 28, 2006. Version 2.
Checksum: 219B4BE0E7ACD05A

FASTA53958,468
        10         20         30         40         50         60 
MASRIINHSK KLKHVSALLR RDHAVAVRCF SNSTHPSLVG REDIFKARLN YSSVERISKC 

        70         80         90        100        110        120 
GTGNVTMLSG ISTTSTKLSS PMAGPKLFKE FISSQMRSVR GFSSSSDLPP HQEIGMPSLS 

       130        140        150        160        170        180 
PTMTEGNIAR WLKKEGDKVA PGEVLCEVET DKATVEMECM EEGFLAKIVK EEGAKEIQVG 

       190        200        210        220        230        240 
EVIAITVEDE DDIQKFKDYT PSSDTGPAAP EAKPAPSLPK EEKVEKPASA PEAKISKPSS 

       250        260        270        280        290        300 
APSEDRIFAS PLARKLAEDN NVPLSSIKGT GPEGRIVKAD VEDFLASGSK ETTAKPSKQV 

       310        320        330        340        350        360 
DSKVPALDYV DIPHTQIRKV TASRLAFSKQ TIPHYYLTVD TCVDKMMGLR SQLNSFQEAS 

       370        380        390        400        410        420 
GGKRISVNDL VIKAAALALR KVPQCNSSWT DEYIRQFKNV NINVAVQTEN GLYVPVVKDA 

       430        440        450        460        470        480 
DKKGLSTIGE EVRFLAQKAK ENSLKPEDYE GGTFTVSNLG GPFGIKQFCA VINPPQAAIL 

       490        500        510        520        530 
AIGSAEKRVV PGTGPDQYNV ASYMSVTLSC DHRVIDGAIG AEWLKAFKGY IETPESMLL 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_566470.1. NM_112247.2.
UniGeneAt.21338.

3D structure databases

ProteinModelPortalQ8RWN9.
SMRQ8RWN9. Positions 113-192, 302-539.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PaxDbQ8RWN9.
PRIDEQ8RWN9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT3G13930.1; AT3G13930.1; AT3G13930.
GeneID820606.
KEGGath:AT3G13930.

Organism-specific databases

TAIRAT3G13930.

Phylogenomic databases

eggNOGCOG0508.
HOGENOMHOG000281566.
InParanoidQ8RWN9.
KOK00627.
OMAMSMKEGT.
PhylomeDBQ8RWN9.

Enzyme and pathway databases

BioCycARA:AT3G13930-MONOMER.

Gene expression databases

GenevestigatorQ8RWN9.

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...

Entry information

Entry nameODP22_ARATH
AccessionPrimary (citable) accession number: Q8RWN9
Secondary accession number(s): Q9ASS8, Q9LVK7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: November 28, 2006
Last modified: June 11, 2014
This is version 90 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names