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Protein

Pyruvate dehydrogenase E1 component subunit alpha-1, mitochondrial

Gene

E1 ALPHA

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

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 activityi

Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2.

Cofactori

Enzyme regulationi

E1 activity is regulated by phosphorylation (inactivation) and dephosphorylation (activation) of the alpha subunit.By similarity

GO - Molecular functioni

GO - Biological processi

  • glycolytic process Source: UniProtKB-KW
  • response to cadmium ion Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Pyruvate, Thiamine pyrophosphate

Enzyme and pathway databases

BioCyciARA:AT1G59900-MONOMER.
ReactomeiREACT_285305. Signaling by Retinoic Acid.
REACT_290601. Pyruvate metabolism.
REACT_307000. Regulation of pyruvate dehydrogenase (PDH) complex.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyruvate dehydrogenase E1 component subunit alpha-1, mitochondrial (EC:1.2.4.1)
Short name:
PDHE1-A
Gene namesi
Name:E1 ALPHA
Ordered Locus Names:At1g59900
ORF Names:F23H11.21
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G59900.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: TAIR
  • mitochondrial matrix Source: UniProtKB-SubCell
  • mitochondrion Source: TAIR
  • nucleus Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3232MitochondrionSequence AnalysisAdd
BLAST
Chaini33 – 389357Pyruvate dehydrogenase E1 component subunit alpha-1, mitochondrialPRO_0000020453Add
BLAST

Proteomic databases

PaxDbiP52901.
PRIDEiP52901.

2D gel databases

SWISS-2DPAGEP52901.

Expressioni

Tissue specificityi

Expressed in roots, rosettes and flowers.1 Publication

Interactioni

Subunit structurei

Tetramer of 2 alpha and 2 beta subunits.By similarity

Protein-protein interaction databases

BioGridi27509. 1 interaction.
IntActiP52901. 1 interaction.
STRINGi3702.AT1G59900.1.

Structurei

3D structure databases

ProteinModelPortaliP52901.
SMRiP52901. Positions 47-368.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1071.
HOGENOMiHOG000281336.
InParanoidiP52901.
KOiK00161.
OMAiLTIETSM.
PhylomeDBiP52901.

Family and domain databases

Gene3Di3.40.50.970. 1 hit.
InterProiIPR001017. DH_E1.
IPR017597. Pyrv_DH_E1_asu_subgrp-y.
IPR029061. THDP-binding.
[Graphical view]
PfamiPF00676. E1_dh. 1 hit.
[Graphical view]
SUPFAMiSSF52518. SSF52518. 1 hit.
TIGRFAMsiTIGR03182. PDH_E1_alph_y. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P52901-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALSRLSSRS NIITRPFSAA FSRLISTDTT PITIETSLPF TAHLCDPPSR
60 70 80 90 100
SVESSSQELL DFFRTMALMR RMEIAADSLY KAKLIRGFCH LYDGQEAVAI
110 120 130 140 150
GMEAAITKKD AIITAYRDHC IFLGRGGSLH EVFSELMGRQ AGCSKGKGGS
160 170 180 190 200
MHFYKKESSF YGGHGIVGAQ VPLGCGIAFA QKYNKEEAVT FALYGDGAAN
210 220 230 240 250
QGQLFEALNI SALWDLPAIL VCENNHYGMG TAEWRAAKSP SYYKRGDYVP
260 270 280 290 300
GLKVDGMDAF AVKQACKFAK QHALEKGPII LEMDTYRYHG HSMSDPGSTY
310 320 330 340 350
RTRDEISGVR QERDPIERIK KLVLSHDLAT EKELKDMEKE IRKEVDDAIA
360 370 380
KAKDCPMPEP SELFTNVYVK GFGTESFGPD RKEVKASLP
Length:389
Mass (Da):43,059
Last modified:January 10, 2003 - v2
Checksum:i637E5BE5E86DCCAE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti83 – 842KL → NV in AAA86507 (PubMed:7590338).Curated
Sequence conflicti362 – 3621E → D in AAK26016 (PubMed:14593172).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U21214 mRNA. Translation: AAA86507.1.
AC007258 Genomic DNA. Translation: AAD39331.1.
CP002684 Genomic DNA. Translation: AEE33638.1.
AF360306 mRNA. Translation: AAK26016.1.
BT000974 mRNA. Translation: AAN41374.1.
AY087667 mRNA. Translation: AAM65205.1.
PIRiB96623.
JC4358.
RefSeqiNP_176198.1. NM_104682.2.
UniGeneiAt.23186.

Genome annotation databases

EnsemblPlantsiAT1G59900.1; AT1G59900.1; AT1G59900.
GeneIDi842284.
KEGGiath:AT1G59900.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U21214 mRNA. Translation: AAA86507.1.
AC007258 Genomic DNA. Translation: AAD39331.1.
CP002684 Genomic DNA. Translation: AEE33638.1.
AF360306 mRNA. Translation: AAK26016.1.
BT000974 mRNA. Translation: AAN41374.1.
AY087667 mRNA. Translation: AAM65205.1.
PIRiB96623.
JC4358.
RefSeqiNP_176198.1. NM_104682.2.
UniGeneiAt.23186.

3D structure databases

ProteinModelPortaliP52901.
SMRiP52901. Positions 47-368.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi27509. 1 interaction.
IntActiP52901. 1 interaction.
STRINGi3702.AT1G59900.1.

2D gel databases

SWISS-2DPAGEP52901.

Proteomic databases

PaxDbiP52901.
PRIDEiP52901.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G59900.1; AT1G59900.1; AT1G59900.
GeneIDi842284.
KEGGiath:AT1G59900.

Organism-specific databases

GeneFarmi4372. 441.
TAIRiAT1G59900.

Phylogenomic databases

eggNOGiCOG1071.
HOGENOMiHOG000281336.
InParanoidiP52901.
KOiK00161.
OMAiLTIETSM.
PhylomeDBiP52901.

Enzyme and pathway databases

BioCyciARA:AT1G59900-MONOMER.
ReactomeiREACT_285305. Signaling by Retinoic Acid.
REACT_290601. Pyruvate metabolism.
REACT_307000. Regulation of pyruvate dehydrogenase (PDH) complex.

Miscellaneous databases

PROiP52901.

Family and domain databases

Gene3Di3.40.50.970. 1 hit.
InterProiIPR001017. DH_E1.
IPR017597. Pyrv_DH_E1_asu_subgrp-y.
IPR029061. THDP-binding.
[Graphical view]
PfamiPF00676. E1_dh. 1 hit.
[Graphical view]
SUPFAMiSSF52518. SSF52518. 1 hit.
TIGRFAMsiTIGR03182. PDH_E1_alph_y. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The mitochondrial pyruvate dehydrogenase complex: nucleotide and deduced amino-acid sequences of a cDNA encoding the Arabidopsis thaliana E1 alpha-subunit."
    Luethy M.H., Miernyk J.A., Randall D.D.
    Gene 164:251-254(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    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] [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. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "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].
  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: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Strain: cv. Landsberg erecta.

Entry informationi

Entry nameiODPA1_ARATH
AccessioniPrimary (citable) accession number: P52901
Secondary accession number(s): Q9C5E3, Q9SXC2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 10, 2003
Last modified: July 22, 2015
This is version 127 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.