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Q0WQF7 (ODP21_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dihydrolipoyllysine-residue acetyltransferase component 1 of pyruvate dehydrogenase complex, mitochondrial

EC=2.3.1.12
Alternative name(s):
Dihydrolipoamide S-acetyltransferase component 1 of pyruvate dehydrogenase complex
Pyruvate dehydrogenase complex component E2 1
Short name=PDC-E2 1
Short name=PDCE2 1
Gene names
Name:LTA3
Ordered Locus Names:At3g52200
ORF Names:F4F15.310
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length637 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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). Ref.7

Catalytic activity

Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine.

Cofactor

Binds 2 lipoyl cofactors covalently.

Subcellular location

Mitochondrion matrix Ref.6.

Sequence similarities

Belongs to the 2-oxoacid dehydrogenase family.

Contains 2 lipoyl-binding domains.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentMitochondrion
   Coding sequence diversityAlternative splicing
   DomainLipoyl
Repeat
Transit peptide
   Molecular functionAcyltransferase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processglycolytic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functiondihydrolipoyllysine-residue acetyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.
Isoform 1 (identifier: Q0WQF7-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 8484Mitochondrion Potential
Chain85 – 637553Dihydrolipoyllysine-residue acetyltransferase component 1 of pyruvate dehydrogenase complex, mitochondrial
PRO_0000260025

Regions

Domain86 – 16075Lipoyl-binding 1
Domain213 – 28775Lipoyl-binding 2
Region352 – 38332E3-binding site By similarity

Sites

Active site6101 Potential
Active site6141 Potential

Amino acid modifications

Modified residue1261N6-lipoyllysine By similarity
Modified residue2531N6-lipoyllysine By similarity

Experimental info

Sequence conflict61F → L in BAF00642. Ref.4
Sequence conflict3781S → F in AAD55140. Ref.1
Sequence conflict5831V → E in AAD55140. Ref.1
Sequence conflict5831V → E in CAA86300. Ref.5
Sequence conflict5971S → C in AAD55140. Ref.1
Sequence conflict5971S → C in CAA86300. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 14, 2006. Version 2.
Checksum: CBD20C3B1BF2B4E9

FASTA63768,862
        10         20         30         40         50         60 
MVLPLFRRAA IARTSSLLRA RLFAPASEFH SRFSNGLYHL DDKISSSNGV RSASIDLITR 

        70         80         90        100        110        120 
MDDSSPKPIL RFGVQNFSST GPISQTVLAM PALSPTMSHG NVVKWMKKEG DKVEVGDVLC 

       130        140        150        160        170        180 
EIETDKATVE FESQEEGFLA KILVTEGSKD IPVNEPIAIM VEEEDDIKNV PATIEGGRDG 

       190        200        210        220        230        240 
KEETSAHQVM KPDESTQQKS SIQPDASDLP PHVVLEMPAL SPTMNQGNIA KWWKKEGDKI 

       250        260        270        280        290        300 
EVGDVIGEIE TDKATLEFES LEEGYLAKIL IPEGSKDVAV GKPIALIVED AESIEAIKSS 

       310        320        330        340        350        360 
SAGSSEVDTV KEVPDSVVDK PTERKAGFTK ISPAAKLLIL EHGLEASSIE ASGPYGTLLK 

       370        380        390        400        410        420 
SDVVAAIASG KASKSSASTK KKQPSKETPS KSSSTSKPSV TQSDNNYEDF PNSQIRKIIA 

       430        440        450        460        470        480 
KRLLESKQKI PHLYLQSDVV LDPLLAFRKE LQENHGVKVS VNDIVIKAVA VALRNVRQAN 

       490        500        510        520        530        540 
AFWDAEKGDI VMCDSVDISI AVATEKGLMT PIIKNADQKS ISAISLEVKE LAQKARSGKL 

       550        560        570        580        590        600 
APHEFQGGTF SISNLGMYPV DNFCAIINPP QAGILAVGRG NKVVEPVIGL DGIEKPSVVT 

       610        620        630 
KMNVTLSADH RIFDGQVGAS FMSELRSNFE DVRRLLL 

« Hide

References

« Hide 'large scale' references
[1]"Expression and assembly of the mitochondrial dihydrolipoamide S-acetyltransferase (E2) subunit from Arabidopsis thaliana."
Mooney B.P., Miernyk J.A., Randall D.D.
Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F. expand/collapse author list , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
Nature 408:820-822(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]"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. expand/collapse author list , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[5]"Cloning and characterization of a dihydrolipoamide acetyltransferase (E2) subunit of the pyruvate dehydrogenase complex from Arabidopsis thaliana."
Guan Y., Rawsthorne S., Scofield G., Shaw P., Doonan J.H.
J. Biol. Chem. 270:5412-5417(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 28-637.
[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.
[7]"Lipoic acid-dependent oxidative catabolism of alpha-keto acids in mitochondria provides evidence for branched-chain amino acid catabolism in Arabidopsis."
Taylor N.L., Heazlewood J.L., Day D.A., Millar A.H.
Plant Physiol. 134:838-848(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF066080 mRNA. Translation: AAD55140.1.
AL049711 Genomic DNA. Translation: CAB41340.1.
CP002686 Genomic DNA. Translation: AEE78912.1.
AK228742 mRNA. Translation: BAF00642.1.
Z46230 mRNA. Translation: CAA86300.1.
PIRA55939.
T49099.
RefSeqNP_190788.1. NM_115080.2. [Q0WQF7-1]
UniGeneAt.3218.

3D structure databases

ProteinModelPortalQ0WQF7.
SMRQ0WQF7. Positions 90-167, 217-299, 407-637.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid9703. 3 interactions.
MINTMINT-8060819.

Proteomic databases

PaxDbQ0WQF7.
PRIDEQ0WQF7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT3G52200.1; AT3G52200.1; AT3G52200. [Q0WQF7-1]
GeneID824385.
KEGGath:AT3G52200.

Organism-specific databases

TAIRAT3G52200.

Phylogenomic databases

eggNOGCOG0508.
HOGENOMHOG000281566.
InParanoidQ0WQF7.
KOK00627.
PhylomeDBQ0WQF7.

Enzyme and pathway databases

BioCycARA:AT3G52200-MONOMER.
ARA:GQT-788-MONOMER.

Gene expression databases

ArrayExpressQ0WQF7.
GenevestigatorQ0WQF7.

Family and domain databases

Gene3D3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProIPR003016. 2-oxoA_DH_lipoyl-BS.
IPR001078. 2-oxoacid_DH_actylTfrase.
IPR000089. Biotin_lipoyl.
IPR023213. CAT-like_dom.
IPR004167. E3-bd.
IPR011053. Single_hybrid_motif.
[Graphical view]
PfamPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 2 hits.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 2 hits.
PROSITEPS50968. BIOTINYL_LIPOYL. 2 hits.
PS00189. LIPOYL. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameODP21_ARATH
AccessionPrimary (citable) accession number: Q0WQF7
Secondary accession number(s): Q39082, Q9SQI7, Q9SUY5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 14, 2006
Last sequence update: November 14, 2006
Last modified: July 9, 2014
This is version 71 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names