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UniProtKB/Swiss-Prot entry P52901


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ODPA1_ARATH
Primary accession number P52901
Secondary accession numbers Q9C5E3 Q9SXC2
Integrated into Swiss-Prot on October 1, 1996
Sequence was last modified on January 10, 2003 (Sequence version 2)
Annotations were last modified on    September 2, 2008 (Entry version 73)
Name and origin of the protein
Protein name Pyruvate dehydrogenase E1 component subunit alpha-1, mitochondrial [Precursor]
Synonyms PDHE1-A
EC 1.2.4.1
Gene name
OrderedLocusNames: At1g59900
ORFNames: F23H11.21
From
Arabidopsis thaliana (Mouse-ear cress) [TaxID: 3702] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia;
DOI=10.1016/0378-1119(95)00465-I; PubMed=7590338 [NCBI, ExPASy, EBI, Israel, Japan]
Luethy M.H., Miernyk J.A., Randall D.D.;
"The mitochondrial pyruvate dehydrogenase complex: nucleotide and deduced amino-acid sequences of a cDNA encoding the Arabidopsis thaliana E1 alpha-subunit.";
Gene 164:251-254(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/35048500; PubMed=11130712 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
Nature 408:816-820(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
DOI=10.1126/science.1088305; PubMed=14593172 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Empirical analysis of transcriptional activity in the Arabidopsis genome.";
Science 302:842-846(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
DOI=10.1105/tpc.016055; PubMed=14671022 [NCBI, ExPASy, EBI, Israel, Japan]
Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J., Millar A.H.;
"Experimental analysis of the Arabidopsis mitochondrial proteome highlights signaling and regulatory components, provides assessment of targeting prediction programs, and indicates plant-specific mitochondrial proteins.";
Plant Cell 16:241-256(2004).
Comments
  • FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). 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: Tetramer of 2 alpha and 2 beta subunits (By similarity).
  • SUBCELLULAR LOCATION: Mitochondrion matrix.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U21214; AAA86507.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC007258; AAD39331.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF360306; AAK26016.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT000974; AAN41374.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY087667; AAM65205.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR B96623; B96623.
JC4358; JC4358.
RefSeq NP_176198.1; -.
UniGene At.23186
3D structure databases
HSSP P08559; 1NI4. [HSSP ENTRY / PDB]
ModBase P52901.
2D gel databases
SWISS-2DPAGE P52901; -.
Organism-specific databases
GeneFarm 4372; 441.
TAIR At1g59900; -.
Gene expression databases
ArrayExpress P52901; -.
GermOnline AT1G59900; Arabidopsis thaliana.
Ontologies
GO
GO:0005759; Cellular component: mitochondrial matrix (inferred from electronic annotation from UniProtKB-SubCell).
QuickGo view.
Family and domain databases
InterPro IPR001017; DHase_E1.
IPR017597; Pyrv_DH_E1_asu_subgrp-y.
Graphical view of domain structure.
Pfam PF00676; E1_dh; 1.
Pfam graphical view of domain structure.
BLOCKS P52901.
Genome annotation databases
GeneID 842284; -.
GenomeReviews CT485782_GR; AT1G59900.
KEGG ath:AT1G59900; -.
NMPDR fig|3702.1.peg.5381; -.
Other
ProtoNet P52901.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Glycolysis; Mitochondrion; Oxidoreductase; Phosphoprotein; Pyruvate; Thiamine pyrophosphate; Transit peptide.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
TRANSIT   1    32  32     Mitochondrion (Potential). 
CHAIN   33   389  357     Pyruvate dehydrogenase E1 component subunit alpha-1, mitochondrial. PRO_0000020453
CONFLICT   83    84        KL -> NV (in Ref. 1; AAA86507). 
CONFLICT   362   362        E -> D (in Ref. 3; AAK26016). 
Sequence information
Length: 389 AA [This is the length of the unprocessed precursor] Molecular weight: 43059 Da [This is the MW of the unprocessed precursor] CRC64: 637E5BE5E86DCCAE [This is a checksum on the sequence]
        10         20         30         40         50         60 
MALSRLSSRS NIITRPFSAA FSRLISTDTT PITIETSLPF TAHLCDPPSR SVESSSQELL 

        70         80         90        100        110        120 
DFFRTMALMR RMEIAADSLY KAKLIRGFCH LYDGQEAVAI GMEAAITKKD AIITAYRDHC 

       130        140        150        160        170        180 
IFLGRGGSLH EVFSELMGRQ AGCSKGKGGS MHFYKKESSF YGGHGIVGAQ VPLGCGIAFA 

       190        200        210        220        230        240 
QKYNKEEAVT FALYGDGAAN QGQLFEALNI SALWDLPAIL VCENNHYGMG TAEWRAAKSP 

       250        260        270        280        290        300 
SYYKRGDYVP GLKVDGMDAF AVKQACKFAK QHALEKGPII LEMDTYRYHG HSMSDPGSTY 

       310        320        330        340        350        360 
RTRDEISGVR QERDPIERIK KLVLSHDLAT EKELKDMEKE IRKEVDDAIA KAKDCPMPEP 

       370        380 
SELFTNVYVK GFGTESFGPD RKEVKASLP 

P52901 in FASTA format

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