Reviewed, UniProtKB/Swiss-Prot Q5M729 (OPD23_ARATH)

Names and origin

Protein names

Recommended name:
    Dihydrolipoyllysine-residue acetyltransferase component 3 of pyruvate dehydrogenase complex, mitochondrial
    EC=2.3.1.12
Alternative name(s):
    Dihydrolipoamide S-acetyltransferase component 3 of pyruvate dehydrogenase complex
    Pyruvate dehydrogenase complex component E2 3
      Short name=PDC-E2 3
      Short name=PDCE2 3

Gene names

Ordered Locus Names:	At1g54220
ORF Names:	F20D21.4

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 › malvids › 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.6
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.5.
Sequence similarities	Belongs to the 2-oxoacid dehydrogenase family. Contains 1 lipoyl-binding domain.
Sequence caution	The sequence AAD25602.1 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	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 3 of pyruvate dehydrogenase complex, mitochondrial		PRO_0000260027
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	45	1	T → I in AAK53067. Ref.1
	Sequence conflict	267	1	I → T in AAK53067. Ref.1
	Sequence conflict	442	1	N → S in AAM97076. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q5M729-1 [UniParc]. Last modified February 1, 2005. Version 1. Checksum: 0C4E141079A2698F	FASTA	539	58,467
	10 20 30 40 50 60 MAYASRIINH SKKLKDVSTL LRRENAATIR YYSNTNRAPL NREDTFNSRL GYPPLERISI 70 80 90 100 110 120 CSTSTLPVSI IFSTTRSNLS SAMGRPIFGK EFSCLMQSAR GFSSGSDLPP HQEIGMPSLS 130 140 150 160 170 180 PTMTEGNIAR WLKKEGDKVA PGEVLCEVET DKATVEMECM EEGYLAKIVK AEGSKEIQVG 190 200 210 220 230 240 EVIAITVEDE EDIGKFKDYT PSSTADAAPT KAEPTPAPPK EEKVKQPSSP PEPKASKPST 250 260 270 280 290 300 PPTGDRVFAS PLARKLAEDN NVPLSDIEGT GPEGRIVKAD IDEYLASSGK GATAKPSKST 310 320 330 340 350 360 DSKAPALDYV DIPHSQIRKV TASRLAFSKQ TIPHYYLTVD TCVDKLMALR SQLNSFKEAS 370 380 390 400 410 420 GGKRISVNDL VVKAAALALR KVPQCNSSWT DDYIRQFKNV NINVAVQTEN GLYVPVVKDA 430 440 450 460 470 480 DRKGLSTIGE EVRLLAQKAK ENSLKPEDYE GGTFTVSNLG GPFGIKQFCA VVNPPQAAIL 490 500 510 520 530 AVGSAEKRVV PGNGPDQFNF ASYMPVTLSC DHRVVDGAIG AEWLKAFKGY IENPKSMLL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Mono-lipoyl E2 from pyruvate dehydrogenase complex from Arabidopsis." Broz A.K., Randall D.D., Miernyk J.A., Mooney B.P. Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana." Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W. Nature 408:816-820(2000) [PubMed: 11130712] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[4]	"Arabidopsis ORF clones." Shinn P., Chen H., Cheuk R.F., Kim C.J., Ecker J.R. Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[5]	"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].
[6]	"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
EMBL GenBank DDBJ	AY033001 mRNA. Translation: AAK53067.1. AC005287 Genomic DNA. Translation: AAD25602.1. Sequence problems. AY136410 mRNA. Translation: AAM97076.1. BT020419 mRNA. Translation: AAV97810.1.
IPI	IPI00524666.
PIR	E96583.
RefSeq	NP_001031186.1. NP_564654.1.
UniGene	At.19093 At.21338
3D structure databases
HSSP	HSSP built from PDB template 1Y8O based on UniProtKB P10515.
SMR	Q5M729. Positions 110-207, 242-290, 304-539.
ModBase	Search...
Protein-protein interaction databases
STRING	Q5M729.
Proteomic databases
PRIDE	Q5M729.
Genome annotation databases
GeneID	841863.
GenomeReviews	Gene locus AT1G54220 in contig CT485782_GR.
KEGG	ath:AT1G54220.
NMPDR	fig|3702.1.peg.4936.
Organism-specific databases
TAIR	At1g54220.
Phylogenomic databases
eggNOG	KOG0557.
HOGENOM	HBG630916.
InParanoid	Q5M729.
OMA	GKLLCII.
PhylomeDB	Q5M729.
Enzyme and pathway databases
BRENDA	2.3.1.12. 302.
Gene expression databases
Genevestigator	Q5M729.
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. IPR011053. Single_hybrid_motif. [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]
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

OPD23_ARATH

Accession

Primary (citable) accession number: Q5M729
Secondary accession number(s): Q8L787, Q94IP5, Q9SLL0

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 14, 2006
Last sequence update:	February 1, 2005
Last modified:	February 9, 2010
This is version 42 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)