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Q0WQF7

- ODP21_ARATH

UniProt

Q0WQF7 - ODP21_ARATH

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
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    • History
      Entry version 72 (01 Oct 2014)
      Sequence version 2 (14 Nov 2006)
      Previous versions | rss
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    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

    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. mitochondrial matrix Source: UniProtKB-SubCell

    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

    ArrayExpressiQ0WQF7.
    GenevestigatoriQ0WQF7.

    Interactioni

    Protein-protein interaction databases

    BioGridi9703. 3 interactions.
    MINTiMINT-8060819.

    Structurei

    3D structure databases

    ProteinModelPortaliQ0WQF7.
    SMRiQ0WQF7. Positions 90-167, 217-299, 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

    MVLPLFRRAA IARTSSLLRA RLFAPASEFH SRFSNGLYHL DDKISSSNGV    50
    RSASIDLITR MDDSSPKPIL RFGVQNFSST GPISQTVLAM PALSPTMSHG 100
    NVVKWMKKEG DKVEVGDVLC EIETDKATVE FESQEEGFLA KILVTEGSKD 150
    IPVNEPIAIM VEEEDDIKNV PATIEGGRDG KEETSAHQVM KPDESTQQKS 200
    SIQPDASDLP PHVVLEMPAL SPTMNQGNIA KWWKKEGDKI EVGDVIGEIE 250
    TDKATLEFES LEEGYLAKIL IPEGSKDVAV GKPIALIVED AESIEAIKSS 300
    SAGSSEVDTV KEVPDSVVDK PTERKAGFTK ISPAAKLLIL EHGLEASSIE 350
    ASGPYGTLLK SDVVAAIASG KASKSSASTK KKQPSKETPS KSSSTSKPSV 400
    TQSDNNYEDF PNSQIRKIIA KRLLESKQKI PHLYLQSDVV LDPLLAFRKE 450
    LQENHGVKVS VNDIVIKAVA VALRNVRQAN AFWDAEKGDI VMCDSVDISI 500
    AVATEKGLMT PIIKNADQKS ISAISLEVKE LAQKARSGKL APHEFQGGTF 550
    SISNLGMYPV DNFCAIINPP QAGILAVGRG NKVVEPVIGL DGIEKPSVVT 600
    KMNVTLSADH RIFDGQVGAS FMSELRSNFE DVRRLLL 637
    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, 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

    ArrayExpressi Q0WQF7.
    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

    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 1, 2014
    This is version 72 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