Reviewed, UniProtKB/Swiss-Prot Q8H1Y0 (ODPA2_ARATH)

Names and origin

Protein names

Recommended name:
    Pyruvate dehydrogenase E1 component subunit alpha-2, mitochondrial
      Short name=PDHE1-A
    EC=1.2.4.1

Gene names

Name:	IAR4
Ordered Locus Names:	At1g24180
ORF Names:	F3I6.11

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	393 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).
Catalytic activity	Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2.
Cofactor	Thiamine pyrophosphate.
Enzyme regulation	E1 activity is regulated by phosphorylation (inactivation) and dephosphorylation (activation) of the alpha subunit By similarity.
Subunit structure	Tetramer of 2 alpha and 2 beta subunits By similarity.
Subcellular location	Mitochondrion matrix Ref.5.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Pyruvate Thiamine pyrophosphate
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW response to salt stress Inferred from expression pattern. Source: TAIR
Cellular component	cytosol Inferred from direct assay. Source: TAIR mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from direct assay. Source: TAIR
Molecular function	pyruvate dehydrogenase (acetyl-transferring) 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 – 28	28	Mitochondrion Potential
	Chain	29 – 393	365	Pyruvate dehydrogenase E1 component subunit alpha-2, mitochondrial		PRO_0000260024
Experimental info
	Sequence conflict	231	1	Y → D in AAN15218. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q8H1Y0-1 [UniParc]. Last modified November 28, 2006. Version 2. Checksum: 1B28971865B52817	FASTA	393	43,359
	10 20 30 40 50 60 MALSRLSSRS NTFLKPAITA LPSSIRRHVS TDSSPITIET AVPFTSHLCE SPSRSVETSS 70 80 90 100 110 120 EEILAFFRDM ARMRRMEIAA DSLYKAKLIR GFCHLYDGQE ALAVGMEAAI TKKDAIITSY 130 140 150 160 170 180 RDHCTFIGRG GKLVDAFSEL MGRKTGCSHG KGGSMHFYKK DASFYGGHGI VGAQIPLGCG 190 200 210 220 230 240 LAFAQKYNKD EAVTFALYGD GAANQGQLFE ALNISALWDL PAILVCENNH YGMGTATWRS 250 260 270 280 290 300 AKSPAYFKRG DYVPGLKVDG MDALAVKQAC KFAKEHALKN GPIILEMDTY RYHGHSMSDP 310 320 330 340 350 360 GSTYRTRDEI SGVRQVRDPI ERVRKLLLTH DIATEKELKD MEKEIRKEVD DAVAQAKESP 370 380 390 IPDASELFTN MYVKDCGVES FGADRKELKV TLP

References

[1]	"IAR4, a gene required for auxin conjugate sensitivity in Arabidopsis, encodes a pyruvate dehydrogenase E1alpha homolog." LeClere S., Rampey R.A., Bartel B. Plant Physiol. 135:989-999(2004) [PubMed: 15173569] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Columbia.
[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]	"Full-length cDNA from Arabidopsis thaliana." Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[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].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY135561 mRNA. Translation: AAN15218.1. AC002396 Genomic DNA. Translation: AAC00577.1. AF360215 mRNA. Translation: AAK25925.1. AY051018 mRNA. Translation: AAK93695.1. AY088101 mRNA. Translation: AAM65647.1.
IPI	IPI00540928.
PIR	T00648.
RefSeq	NP_173828.1.
UniGene	At.24830 Rra.24006
3D structure databases
HSSP	HSSP built from PDB template 1NI4 based on UniProtKB P08559.
SMR	Q8H1Y0. Positions 35-379.
ModBase	Search...
Protein-protein interaction databases
STRING	Q8H1Y0.
Proteomic databases
PRIDE	Q8H1Y0.
ProMEX	Q8H1Y0.
Genome annotation databases
GeneID	839031.
GenomeReviews	Gene locus AT1G24180 in contig CT485782_GR.
KEGG	ath:AT1G24180.
NMPDR	fig|3702.1.peg.2808.
Organism-specific databases
GeneFarm	4373. 441.
TAIR	At1g24180.
Phylogenomic databases
eggNOG	KOG0225.
HOGENOM	HBG753263.
InParanoid	Q8H1Y0.
OMA	ECKAIDK.
PhylomeDB	Q8H1Y0.
Enzyme and pathway databases
BRENDA	1.2.4.1. 302.
Gene expression databases
Genevestigator	Q8H1Y0.
Family and domain databases
InterPro	IPR001017. DH_E1. IPR017597. Pyrv_DH_E1_asu_subgrp-y. [Graphical view]
Pfam	PF00676. E1_dh. 1 hit. [Graphical view]
TIGRFAMs	TIGR03182. PDH_E1_alph_y. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ODPA2_ARATH

Accession

Primary (citable) accession number: Q8H1Y0
Secondary accession number(s): O48685

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 28, 2006
Last sequence update:	November 28, 2006
Last modified:	February 9, 2010
This is version 49 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)