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Q0WQF7

- ODP21_ARATH

UniProt

Q0WQF7 - ODP21_ARATH

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Protein

Dihydrolipoyllysine-residue acetyltransferase component 1 of pyruvate dehydrogenase complex, mitochondrial

Gene

LTA3

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - 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).1 Publication

Catalytic activityi

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

Cofactori

Binds 2 lipoyl cofactors covalently.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei610 – 6101Sequence Analysis
Active sitei614 – 6141Sequence Analysis

GO - Molecular functioni

  1. dihydrolipoyllysine-residue acetyltransferase activity Source: UniProtKB-EC

GO - Biological processi

  1. glycolytic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Glycolysis

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:LTA3
Ordered Locus Names:At3g52200
ORF Names:F4F15.310
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 3

Organism-specific databases

TAIRiAT3G52200.

Subcellular locationi

Mitochondrion matrix 1 Publication

GO - Cellular componenti

  1. mitochondrion Source: UniProtKB-KW
  2. pyruvate dehydrogenase complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 8484MitochondrionSequence AnalysisAdd
BLAST
Chaini85 – 637553Dihydrolipoyllysine-residue acetyltransferase component 1 of pyruvate dehydrogenase complex, mitochondrialPRO_0000260025Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei126 – 1261N6-lipoyllysineBy similarity
Modified residuei253 – 2531N6-lipoyllysineBy similarity

Proteomic databases

PaxDbiQ0WQF7.
PRIDEiQ0WQF7.

Expressioni

Gene expression databases

ExpressionAtlasiQ0WQF7. baseline and differential.
GenevestigatoriQ0WQF7.

Interactioni

Protein-protein interaction databases

BioGridi9703. 3 interactions.
MINTiMINT-8060819.

Structurei

3D structure databases

ProteinModelPortaliQ0WQF7.
SMRiQ0WQF7. Positions 90-167, 217-299, 330-369, 407-637.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini86 – 16075Lipoyl-binding 1Add
BLAST
Domaini213 – 28775Lipoyl-binding 2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni332 – 36332E3-binding siteBy similarityAdd
BLAST

Sequence similaritiesi

Belongs to the 2-oxoacid dehydrogenase family.Curated
Contains 2 lipoyl-binding domains.Curated

Keywords - Domaini

Lipoyl, Repeat, Transit peptide

Phylogenomic databases

eggNOGiCOG0508.
HOGENOMiHOG000281566.
InParanoidiQ0WQF7.
KOiK00627.
PhylomeDBiQ0WQF7.

Family and domain databases

Gene3Di3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProiIPR003016. 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]
PfamiPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 2 hits.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMiSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 2 hits.
PROSITEiPS50968. BIOTINYL_LIPOYL. 2 hits.
PS00189. LIPOYL. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

This entry describes 1 isoform i produced by alternative splicing. Align

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: Q0WQF7-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MVLPLFRRAA IARTSSLLRA RLFAPASEFH SRFSNGLYHL DDKISSSNGV
60 70 80 90 100
RSASIDLITR MDDSSPKPIL RFGVQNFSST GPISQTVLAM PALSPTMSHG
110 120 130 140 150
NVVKWMKKEG DKVEVGDVLC EIETDKATVE FESQEEGFLA KILVTEGSKD
160 170 180 190 200
IPVNEPIAIM VEEEDDIKNV PATIEGGRDG KEETSAHQVM KPDESTQQKS
210 220 230 240 250
SIQPDASDLP PHVVLEMPAL SPTMNQGNIA KWWKKEGDKI EVGDVIGEIE
260 270 280 290 300
TDKATLEFES LEEGYLAKIL IPEGSKDVAV GKPIALIVED AESIEAIKSS
310 320 330 340 350
SAGSSEVDTV KEVPDSVVDK PTERKAGFTK ISPAAKLLIL EHGLEASSIE
360 370 380 390 400
ASGPYGTLLK SDVVAAIASG KASKSSASTK KKQPSKETPS KSSSTSKPSV
410 420 430 440 450
TQSDNNYEDF PNSQIRKIIA KRLLESKQKI PHLYLQSDVV LDPLLAFRKE
460 470 480 490 500
LQENHGVKVS VNDIVIKAVA VALRNVRQAN AFWDAEKGDI VMCDSVDISI
510 520 530 540 550
AVATEKGLMT PIIKNADQKS ISAISLEVKE LAQKARSGKL APHEFQGGTF
560 570 580 590 600
SISNLGMYPV DNFCAIINPP QAGILAVGRG NKVVEPVIGL DGIEKPSVVT
610 620 630
KMNVTLSADH RIFDGQVGAS FMSELRSNFE DVRRLLL
Length:637
Mass (Da):68,862
Last modified:November 14, 2006 - v2
Checksum:iCBD20C3B1BF2B4E9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti6 – 61F → L in BAF00642. 1 PublicationCurated
Sequence conflicti378 – 3781S → F in AAD55140. 1 PublicationCurated
Sequence conflicti583 – 5831V → E in AAD55140. 1 PublicationCurated
Sequence conflicti583 – 5831V → E in CAA86300. (PubMed:7890655)Curated
Sequence conflicti597 – 5971S → C in AAD55140. 1 PublicationCurated
Sequence conflicti597 – 5971S → C in CAA86300. (PubMed:7890655)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiA55939.
T49099.
RefSeqiNP_190788.1. NM_115080.2. [Q0WQF7-1]
UniGeneiAt.3218.

Genome annotation databases

EnsemblPlantsiAT3G52200.1; AT3G52200.1; AT3G52200. [Q0WQF7-1]
GeneIDi824385.
KEGGiath:AT3G52200.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
PIRi A55939.
T49099.
RefSeqi NP_190788.1. NM_115080.2. [Q0WQF7-1 ]
UniGenei At.3218.

3D structure databases

ProteinModelPortali Q0WQF7.
SMRi Q0WQF7. Positions 90-167, 217-299, 330-369, 407-637.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 9703. 3 interactions.
MINTi MINT-8060819.

Proteomic databases

PaxDbi Q0WQF7.
PRIDEi Q0WQF7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT3G52200.1 ; AT3G52200.1 ; AT3G52200 . [Q0WQF7-1 ]
GeneIDi 824385.
KEGGi ath:AT3G52200.

Organism-specific databases

TAIRi AT3G52200.

Phylogenomic databases

eggNOGi COG0508.
HOGENOMi HOG000281566.
InParanoidi Q0WQF7.
KOi K00627.
PhylomeDBi Q0WQF7.

Enzyme and pathway databases

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

Gene expression databases

ExpressionAtlasi Q0WQF7. baseline and differential.
Genevestigatori Q0WQF7.

Family and domain databases

Gene3Di 3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProi IPR003016. 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 ]
Pfami PF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 2 hits.
PF02817. E3_binding. 1 hit.
[Graphical view ]
SUPFAMi SSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 2 hits.
PROSITEi PS50968. BIOTINYL_LIPOYL. 2 hits.
PS00189. LIPOYL. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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.

Entry informationi

Entry nameiODP21_ARATH
AccessioniPrimary (citable) accession number: Q0WQF7
Secondary accession number(s): Q39082, Q9SQI7, Q9SUY5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 14, 2006
Last sequence update: November 14, 2006
Last modified: October 29, 2014
This is version 73 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
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3