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UniProtKB/Swiss-Prot entry Q5M729


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

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Entry information
Entry name OPD23_ARATH
Primary accession number Q5M729
Secondary accession numbers Q8L787 Q94IP5 Q9SLL0
Integrated into Swiss-Prot on November 14, 2006
Sequence was last modified on February 1, 2005 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 29)
Name and origin of the protein
Protein name Dihydrolipoyllysine-residue acetyltransferase component 3 of pyruvate dehydrogenase complex, mitochondrial [Precursor]
Synonyms EC 2.3.1.12
Pyruvate dehydrogenase complex E2 subunit 3
PDC-E2
PDCE2
E2
Dihydrolipoamide S-acetyltransferase component 3 of pyruvate dehydrogenase complex
Gene name
OrderedLocusNames: At1g54220
ORFNames: F20D21.4
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].
Broz A.K., Randall D.D., Miernyk J.A., Mooney B.P.;
"Mono-lipoyl E2 from pyruvate dehydrogenase complex from Arabidopsis.";
Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
[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].
STRAIN=cv. Columbia;
Shinn P., Chen H., Cheuk R.F., Kim C.J., Ecker J.R.;
"Arabidopsis ORF clones.";
Submitted (DEC-2004) 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).
[6]
FUNCTION.
DOI=10.1104/pp.103.035675; PubMed=14764908 [NCBI, ExPASy, EBI, Israel, Japan]
Taylor N.L., Heazlewood J.L., Day D.A., Millar A.H.;
"Lipoic acid-dependent oxidative catabolism of alpha-keto acids in mitochondria provides evidence for branched-chain amino acid catabolism in Arabidopsis.";
Plant Physiol. 134:838-848(2004).
Comments
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
AY033001; AAK53067.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC005287; AAD25602.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY136410; AAM97076.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT020419; AAV97810.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR E96583; E96583.
RefSeq NP_001031186.1; -.
NP_564654.1; -.
UniGene At.19093
3D structure databases
ModBase Q5M729.
Organism-specific databases
TAIR At1g54220; -.
Ontologies
GO
GO:0005759; Cellular component: mitochondrial matrix (inferred from electronic annotation from UniProtKB-SubCell).
GO:0045254; Cellular component: pyruvate dehydrogenase complex (inferred from electronic annotation from InterPro).
GO:0004742; Molecular function: dihydrolipoyllysine-residue acetyltransferase activity (inferred from electronic annotation from InterPro).
GO:0031405; Molecular function: lipoic acid binding (inferred from electronic annotation from UniProtKB-KW).
GO:0005515; Molecular function: protein binding (inferred from electronic annotation from InterPro).
GO:0006096; Biological process: glycolysis (inferred from electronic annotation from UniProtKB-KW).
GO:0006090; Biological process: pyruvate metabolic process (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR003016; 2-oxoA_DHase_lipoyl-BS.
IPR001078; 2Oxoacid_DHase.
IPR006257; AcTrfase_Pyrv_DHase_cplx_L.
IPR000089; Biotin_lipoyl.
IPR004167; E3_bd.
Graphical view of domain structure.
Gene3D G3DSA:4.10.320.10; E3_bd; 1.
Pfam PF00198; 2-oxoacid_dh; 1.
PF00364; Biotin_lipoyl; 1.
PF02817; E3_binding; 1.
Pfam graphical view of domain structure.
ProDom PD001115; 2Oxoacid_dh; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR01349; PDHac_trf_mito; 1.
PROSITE PS50968; BIOTINYL_LIPOYL; 1.
PS00189; LIPOYL; 1.
PROSITE graphical view of domain structure (profiles).
ProtoNet Q5M729.
Genome annotation databases
GeneID 841863; -.
GenomeReviews CT485782_GR; AT1G54220.
KEGG ath:AT1G54220; -.
NMPDR fig|3702.1.peg.4936; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acyltransferase; Complete proteome; Glycolysis; Lipoyl; Mitochondrion; Transferase; Transit peptide.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
TRANSIT   1     ?        Mitochondrion. 
CHAIN   ?   539        Dihydrolipoyllysine-residue acetyltransferase component 3 of pyruvate dehydrogenase complex, mitochondrial. PRO_0000260027
DOMAIN   112   186  75     Lipoyl-binding. 
REGION   250   281  32     E3-binding site (By similarity). 
ACT_SITE   512   512        Potential. 
ACT_SITE   516   516        Potential. 
BINDING   152   152        Lipoyl (covalent) (By similarity). 
CONFLICT   45    45        T -> I (in Ref. 1; AAK53067). 
CONFLICT   267   267        I -> T (in Ref. 1; AAK53067). 
CONFLICT   442   442        N -> S (in Ref. 3; AAM97076). 
Sequence information
Length: 539 AA [This is the length of the unprocessed precursor] Molecular weight: 58467 Da [This is the MW of the unprocessed precursor] CRC64: 0C4E141079A2698F [This is a checksum on the sequence]
        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 

Q5M729 in FASTA format

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View entry in raw text format (no links)
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BLAST logo BLAST submission on ExPASy/SIB
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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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