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

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Q8RWN9 (OPD22_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 78. History...

Clusters with 100%, 90%, 50% identity |

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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 names

Ordered Locus Names:	At3g13930
ORF Names:	MDC16.5

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	539 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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). 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.
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.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Mitochondrion
Domain	Lipoyl Transit peptide
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	glycolysis Inferred from electronic annotation. Source: UniProtKB-KW pyruvate metabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	chloroplast envelope Inferred from direct assay PubMed 12938931. Source: TAIR mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrion Inferred from direct assay Ref.4 Ref.5 PubMed 15276431 PubMed 22923678. Source: TAIR pyruvate dehydrogenase complex Inferred from electronic annotation. Source: InterPro
Molecular_function	copper ion binding Inferred from direct assay PubMed 20018591. Source: TAIR dihydrolipoyllysine-residue acetyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – ?

Mitochondrion

Chain

? – 539

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

PRO_0000260026

Regions

Domain

112 – 186

Lipoyl-binding

Region

250 – 281

E3-binding site By similarity

Sites

Active site

512

Potential

Active site

516

Potential

Amino acid modifications

Modified residue

152

N6-lipoyllysine By similarity

Experimental info

Sequence conflict

124

T → A in AAM12967. Ref.3

Sequences

Sequence

Length

Mass (Da)

Tools

Q8RWN9 [UniParc].

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

539

58,468

        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' referencesShow '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. 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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], 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.
IPI	IPI00538915.
RefSeq	NP_566470.1. NM_112247.2.
UniGene	At.21338.
3D structure databases
HSSP	HSSP built from PDB template 1Y8O based on UniProtKB P10515.
ProteinModelPortal	Q8RWN9.
SMR	Q8RWN9. Positions 113-192, 246-286, 302-539.
ModBase	Search...
Proteomic databases
PaxDb	Q8RWN9.
PRIDE	Q8RWN9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT3G13930.1; AT3G13930.1; AT3G13930.
GeneID	820606.
KEGG	ath:AT3G13930.
Organism-specific databases
TAIR	At3g13930.
Phylogenomic databases
eggNOG	COG0508.
HOGENOM	HOG000281566.
InParanoid	Q8RWN9.
KO	K00627.
OMA	GTICISN.
PhylomeDB	Q8RWN9.
ProtClustDB	PLN02744.
Gene expression databases
Genevestigator	Q8RWN9.
Family and domain databases
Gene3D	3.30.559.10. 1 hit. 4.10.320.10. 1 hit.
InterPro	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]
Pfam	PF00198. 2-oxoacid_dh. 1 hit. PF00364. Biotin_lipoyl. 1 hit. PF02817. E3_binding. 1 hit. [Graphical view]
SUPFAM	SSF47005. E3_bd. 1 hit. SSF51230. Hybrid_motif. 1 hit.
TIGRFAMs	TIGR01349. PDHac_trf_mito. 1 hit.
PROSITE	PS50968. BIOTINYL_LIPOYL. 1 hit. PS00189. LIPOYL. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

OPD22_ARATH

Accession

Primary (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:	May 1, 2013
This is version 78 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents