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UniProtKB/Swiss-Prot entry Q8H1Y0


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

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Entry information
Entry name ODPA2_ARATH
Primary accession number Q8H1Y0
Secondary accession number O48685
Integrated into Swiss-Prot on November 28, 2006
Sequence was last modified on November 28, 2006 (Sequence version 2)
Annotations were last modified on    September 2, 2008 (Entry version 34)
Name and origin of the protein
Protein name Pyruvate dehydrogenase E1 component subunit alpha-2, mitochondrial [Precursor]
Synonyms PDHE1-A
EC 1.2.4.1
Gene name
Name: IAR4
OrderedLocusNames: At1g24180
ORFNames: F3I6.11
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=10.1104/pp.104.040519; PubMed=15173569 [NCBI, ExPASy, EBI, Israel, Japan]
LeClere S., Rampey R.A., Bartel B.;
"IAR4, a gene required for auxin conjugate sensitivity in Arabidopsis, encodes a pyruvate dehydrogenase E1alpha homolog.";
Plant Physiol. 135:989-999(2004).
[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
AY135561; AAN15218.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE005172; AAC00577.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF360215; AAK25925.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY051018; AAK93695.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY088101; AAM65647.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T00648; T00648.
RefSeq NP_173828.1; -.
UniGene At.24830
3D structure databases
HSSP P08559; 1NI4. [HSSP ENTRY / PDB]
ModBase Q8H1Y0.
Organism-specific databases
GeneFarm 4373; 441.
TAIR At1g24180; -.
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 Q8H1Y0.
Proteomic databases
ProMEX Q8H1Y0; -.
Genome annotation databases
GeneID 839031; -.
GenomeReviews CT485782_GR; AT1G24180.
KEGG ath:AT1G24180; -.
NMPDR fig|3702.1.peg.2808; -.
Other
ProtoNet Q8H1Y0.
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    28  28     Mitochondrion (Potential). 
CHAIN   29   393  365     Pyruvate dehydrogenase E1 component subunit alpha-2, mitochondrial. PRO_0000260024
CONFLICT   231   231        Y -> D (in Ref. 1; AAN15218). 
Sequence information
Length: 393 AA [This is the length of the unprocessed precursor] Molecular weight: 43359 Da [This is the MW of the unprocessed precursor] CRC64: 1B28971865B52817 [This is a checksum on the sequence]
        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 

Q8H1Y0 in FASTA format

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