Reviewed, UniProtKB/Swiss-Prot Q8RWN9 (OPD22_ARATH)

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):
    Pyruvate dehydrogenase complex E2 subunit 2
      Short name=PDC-E2
      Short name=PDCE2
      Short name=E2
    Dihydrolipoamide S-acetyltransferase component 2 of pyruvate dehydrogenase complex

Gene names

Ordered Locus Names:	At3g13930
ORF Names:	MDC16.5

Organism

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

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › 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.4
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.3
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
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. Source: TAIR mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell pyruvate dehydrogenase complex Inferred from electronic annotation. Source: InterPro
Molecular function	dihydrolipoyllysine-residue acetyltransferase activity Inferred from electronic annotation. Source: EC lipoic acid binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from electronic annotation. Source: InterPro
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	75	Lipoyl-binding
	Region	250 – 281	32	E3-binding site By similarity
Sites
	Active site	512	1	Potential
	Active site	516	1	Potential
Amino acid modifications
	Modified residue	152	1	N6-lipoyllysine By similarity
Experimental info
	Sequence conflict	124	1	T → A in AAM12967. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q8RWN9-1 [UniParc]. Last modified November 28, 2006. Version 2. Checksum: 219B4BE0E7ACD05A	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

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: 10819329] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[2]	"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: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[3]	"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: 14671022] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[4]	"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: 14764908] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AB019229 Genomic DNA. Translation: BAB02323.1. Sequence problems. 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.
UniGene	At.21338
3D structure databases
HSSP	HSSP built from PDB template 1FYC based on UniProtKB P10515.
ModBase	Search...
Protein-protein interaction databases
STRING	Q8RWN9.
Proteomic databases
PRIDE	Q8RWN9.
ProMEX	Q8RWN9.
Genome annotation databases
GeneID	820606.
GenomeReviews	Gene locus AT3G13930 in contig BA000014_GR.
KEGG	ath:AT3G13930.
NMPDR	fig|3702.1.peg.13516.
Organism-specific databases
TAIR	At3g13930.
Phylogenomic databases
OMA	FESTENG.
Enzyme and pathway databases
BRENDA	2.3.1.12. 302.
Gene expression databases
Genevestigator	Q8RWN9.
Family and domain databases
InterPro	IPR003016. 2-oxoA_DH_lipoyl-BS. IPR001078. 2-oxoacid_DH_actylTfrase. IPR006257. AcTrfase_Pyrv_DH_cplx_L. IPR000089. Biotin_lipoyl. IPR004167. E3_bd. [Graphical view]
Gene3D	G3DSA:4.10.320.10. E3_bd. 1 hit.
Pfam	PF00198. 2-oxoacid_dh. 1 hit. PF00364. Biotin_lipoyl. 1 hit. PF02817. E3_binding. 1 hit. [Graphical view]
ProDom	PD001115. 2Oxoacid_dh. 1 hit. [Graphical view] [Entries sharing at least one domain]
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:	November 3, 2009
This is version 50 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)