Q0WQF7 (OPD21_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dihydrolipoyllysine-residue acetyltransferase component 1 of pyruvate dehydrogenase complex, mitochondrial
EC=2.3.1.12

Alternative name(s):
Dihydrolipoamide S-acetyltransferase component 1 of pyruvate dehydrogenase complex
Pyruvate dehydrogenase complex component E2 1
Short name=PDC-E2 1
Short name=PDCE2 1

Gene names

Name:	LTA3
Ordered Locus Names:	At3g52200
ORF Names:	F4F15.310

Organism

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

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	637 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.7
Catalytic activity	Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine.
Cofactor	Binds 2 lipoyl cofactors covalently.
Subcellular location	Mitochondrion matrix.
Sequence similarities	Belongs to the 2-oxoacid dehydrogenase family. Contains 2 lipoyl-binding domains.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Mitochondrion
Coding sequence diversity	Alternative splicing
Domain	Lipoyl Repeat 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
Cellular_component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	dihydrolipoyllysine-residue acetyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: Q0WQF7-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 84	84	Mitochondrion Potential
	Chain	85 – 637	553	Dihydrolipoyllysine-residue acetyltransferase component 1 of pyruvate dehydrogenase complex, mitochondrial		PRO_0000260025
Regions
	Domain	86 – 160	75	Lipoyl-binding 1
	Domain	213 – 287	75	Lipoyl-binding 2
	Region	352 – 383	32	E3-binding site By similarity
Sites
	Active site	610	1	Potential
	Active site	614	1	Potential
Amino acid modifications
	Modified residue	126	1	N6-lipoyllysine By similarity
	Modified residue	253	1	N6-lipoyllysine By similarity
Experimental info
	Sequence conflict	6	1	F → L in BAF00642. Ref.4
	Sequence conflict	378	1	S → F in AAD55140. Ref.1
	Sequence conflict	583	1	V → E in AAD55140. Ref.1
	Sequence conflict	583	1	V → E in CAA86300. Ref.5
	Sequence conflict	597	1	S → C in AAD55140. Ref.1
	Sequence conflict	597	1	S → C in CAA86300. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 14, 2006. Version 2. Checksum: CBD20C3B1BF2B4E9	FASTA	637	68,862
	10 20 30 40 50 60 MVLPLFRRAA IARTSSLLRA RLFAPASEFH SRFSNGLYHL DDKISSSNGV RSASIDLITR 70 80 90 100 110 120 MDDSSPKPIL RFGVQNFSST GPISQTVLAM PALSPTMSHG NVVKWMKKEG DKVEVGDVLC 130 140 150 160 170 180 EIETDKATVE FESQEEGFLA KILVTEGSKD IPVNEPIAIM VEEEDDIKNV PATIEGGRDG 190 200 210 220 230 240 KEETSAHQVM KPDESTQQKS SIQPDASDLP PHVVLEMPAL SPTMNQGNIA KWWKKEGDKI 250 260 270 280 290 300 EVGDVIGEIE TDKATLEFES LEEGYLAKIL IPEGSKDVAV GKPIALIVED AESIEAIKSS 310 320 330 340 350 360 SAGSSEVDTV KEVPDSVVDK PTERKAGFTK ISPAAKLLIL EHGLEASSIE ASGPYGTLLK 370 380 390 400 410 420 SDVVAAIASG KASKSSASTK KKQPSKETPS KSSSTSKPSV TQSDNNYEDF PNSQIRKIIA 430 440 450 460 470 480 KRLLESKQKI PHLYLQSDVV LDPLLAFRKE LQENHGVKVS VNDIVIKAVA VALRNVRQAN 490 500 510 520 530 540 AFWDAEKGDI VMCDSVDISI AVATEKGLMT PIIKNADQKS ISAISLEVKE LAQKARSGKL 550 560 570 580 590 600 APHEFQGGTF SISNLGMYPV DNFCAIINPP QAGILAVGRG NKVVEPVIGL DGIEKPSVVT 610 620 630 KMNVTLSADH RIFDGQVGAS FMSELRSNFE DVRRLLL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Expression and assembly of the mitochondrial dihydrolipoamide S-acetyltransferase (E2) subunit from Arabidopsis thaliana." Mooney B.P., Miernyk J.A., Randall D.D. Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana." Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F. , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S. Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[4]	"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs." Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K. Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[5]	"Cloning and characterization of a dihydrolipoamide acetyltransferase (E2) subunit of the pyruvate dehydrogenase complex from Arabidopsis thaliana." Guan Y., Rawsthorne S., Scofield G., Shaw P., Doonan J.H. J. Biol. Chem. 270:5412-5417(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 28-637.
[6]	"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.
[7]	"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	AF066080 mRNA. Translation: AAD55140.1. AL049711 Genomic DNA. Translation: CAB41340.1. CP002686 Genomic DNA. Translation: AEE78912.1. AK228742 mRNA. Translation: BAF00642.1. Z46230 mRNA. Translation: CAA86300.1.
IPI	IPI00543892.
PIR	A55939. T49099.
RefSeq	NP_190788.1. NM_115080.2.
UniGene	At.3218.
3D structure databases
ProteinModelPortal	Q0WQF7.
SMR	Q0WQF7. Positions 90-167, 217-299, 330-369, 407-637.
ModBase	Search...
Proteomic databases
PaxDb	Q0WQF7.
PRIDE	Q0WQF7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT3G52200.1; AT3G52200.1; AT3G52200.
GeneID	824385.
KEGG	ath:AT3G52200.
Organism-specific databases
TAIR	At3g52200.
Phylogenomic databases
eggNOG	COG0508.
HOGENOM	HOG000281566.
InParanoid	Q0WQF7.
KO	K00627.
PhylomeDB	Q0WQF7.
ProtClustDB	CLSN2684753.
Gene expression databases
ArrayExpress	Q0WQF7.
Genevestigator	Q0WQF7.
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. IPR011053. Single_hybrid_motif. [Graphical view]
Pfam	PF00198. 2-oxoacid_dh. 1 hit. PF00364. Biotin_lipoyl. 2 hits. PF02817. E3_binding. 1 hit. [Graphical view]
SUPFAM	SSF47005. E3_bd. 1 hit. SSF51230. Hybrid_motif. 2 hits.
PROSITE	PS50968. BIOTINYL_LIPOYL. 2 hits. PS00189. LIPOYL. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

OPD21_ARATH

Accession

Primary (citable) accession number: Q0WQF7
Secondary accession number(s): Q39082, Q9SQI7, Q9SUY5

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 14, 2006
Last sequence update:	November 14, 2006
Last modified:	May 1, 2013
This is version 58 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program