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Q8RWN9

- ODP22_ARATH

UniProt

Q8RWN9 - ODP22_ARATH

Protein

Dihydrolipoyllysine-residue acetyltransferase component 2 of pyruvate dehydrogenase complex, mitochondrial

Gene

At3g13930

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 91 (01 Oct 2014)
      Sequence version 2 (28 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 1 lipoyl cofactor covalently.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei512 – 5121Sequence Analysis
    Active sitei516 – 5161Sequence Analysis

    GO - Molecular functioni

    1. copper ion binding Source: TAIR
    2. 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:AT3G13930-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dihydrolipoyllysine-residue acetyltransferase component 2 of pyruvate dehydrogenase complex, mitochondrial (EC:2.3.1.12)
    Alternative name(s):
    Dihydrolipoamide S-acetyltransferase component 2 of pyruvate dehydrogenase complex
    Pyruvate dehydrogenase complex component E2 2
    Short name:
    PDC-E2 2
    Short name:
    PDCE2 2
    Gene namesi
    Ordered Locus Names:At3g13930
    ORF Names:MDC16.5
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 3

    Organism-specific databases

    TAIRiAT3G13930.

    Subcellular locationi

    Mitochondrion matrix 1 Publication

    GO - Cellular componenti

    1. chloroplast Source: TAIR
    2. chloroplast envelope Source: TAIR
    3. mitochondrial matrix Source: UniProtKB-SubCell
    4. mitochondrion Source: TAIR
    5. pyruvate dehydrogenase complex Source: InterPro

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini? – 539Dihydrolipoyllysine-residue acetyltransferase component 2 of pyruvate dehydrogenase complex, mitochondrialPRO_0000260026
    Transit peptidei1 – ?Mitochondrion

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei152 – 1521N6-lipoyllysineBy similarity

    Proteomic databases

    PaxDbiQ8RWN9.
    PRIDEiQ8RWN9.

    Expressioni

    Gene expression databases

    GenevestigatoriQ8RWN9.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8RWN9.
    SMRiQ8RWN9. Positions 113-192, 302-539.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini112 – 18675Lipoyl-bindingAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni250 – 28132E3-binding siteBy similarityAdd
    BLAST

    Sequence similaritiesi

    Belongs to the 2-oxoacid dehydrogenase family.Curated
    Contains 1 lipoyl-binding domain.Curated

    Keywords - Domaini

    Lipoyl, Transit peptide

    Phylogenomic databases

    eggNOGiCOG0508.
    HOGENOMiHOG000281566.
    InParanoidiQ8RWN9.
    KOiK00627.
    OMAiMSMKEGT.
    PhylomeDBiQ8RWN9.

    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.
    IPR006257. LAT1.
    IPR011053. Single_hybrid_motif.
    [Graphical view]
    PfamiPF00198. 2-oxoacid_dh. 1 hit.
    PF00364. Biotin_lipoyl. 1 hit.
    PF02817. E3_binding. 1 hit.
    [Graphical view]
    SUPFAMiSSF47005. SSF47005. 1 hit.
    SSF51230. SSF51230. 1 hit.
    TIGRFAMsiTIGR01349. PDHac_trf_mito. 1 hit.
    PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
    PS00189. LIPOYL. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q8RWN9-1 [UniParc]FASTAAdd to Basket

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    MASRIINHSK KLKHVSALLR RDHAVAVRCF SNSTHPSLVG REDIFKARLN    50
    YSSVERISKC GTGNVTMLSG ISTTSTKLSS PMAGPKLFKE FISSQMRSVR 100
    GFSSSSDLPP HQEIGMPSLS PTMTEGNIAR WLKKEGDKVA PGEVLCEVET 150
    DKATVEMECM EEGFLAKIVK EEGAKEIQVG EVIAITVEDE DDIQKFKDYT 200
    PSSDTGPAAP EAKPAPSLPK EEKVEKPASA PEAKISKPSS APSEDRIFAS 250
    PLARKLAEDN NVPLSSIKGT GPEGRIVKAD VEDFLASGSK ETTAKPSKQV 300
    DSKVPALDYV DIPHTQIRKV TASRLAFSKQ TIPHYYLTVD TCVDKMMGLR 350
    SQLNSFQEAS GGKRISVNDL VIKAAALALR KVPQCNSSWT DEYIRQFKNV 400
    NINVAVQTEN GLYVPVVKDA DKKGLSTIGE EVRFLAQKAK ENSLKPEDYE 450
    GGTFTVSNLG GPFGIKQFCA VINPPQAAIL AIGSAEKRVV PGTGPDQYNV 500
    ASYMSVTLSC DHRVIDGAIG AEWLKAFKGY IETPESMLL 539
    Length:539
    Mass (Da):58,468
    Last modified:November 28, 2006 - v2
    Checksum:i219B4BE0E7ACD05A
    GO

    Sequence cautioni

    The sequence BAB02323.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti124 – 1241T → A in AAM12967. (PubMed:14593172)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB019229 Genomic DNA. Translation: BAB02323.1. Sequence problems.
    CP002686 Genomic DNA. Translation: AEE75442.1.
    AF367302 mRNA. Translation: AAK32889.1.
    AY091691 mRNA. Translation: AAM10290.1.
    AY092968 mRNA. Translation: AAM12967.1.
    BT000444 mRNA. Translation: AAN17421.1.
    BT000702 mRNA. Translation: AAN31846.1.
    BT001223 mRNA. Translation: AAN65110.1.
    RefSeqiNP_566470.1. NM_112247.2.
    UniGeneiAt.21338.

    Genome annotation databases

    EnsemblPlantsiAT3G13930.1; AT3G13930.1; AT3G13930.
    GeneIDi820606.
    KEGGiath:AT3G13930.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB019229 Genomic DNA. Translation: BAB02323.1 . Sequence problems.
    CP002686 Genomic DNA. Translation: AEE75442.1 .
    AF367302 mRNA. Translation: AAK32889.1 .
    AY091691 mRNA. Translation: AAM10290.1 .
    AY092968 mRNA. Translation: AAM12967.1 .
    BT000444 mRNA. Translation: AAN17421.1 .
    BT000702 mRNA. Translation: AAN31846.1 .
    BT001223 mRNA. Translation: AAN65110.1 .
    RefSeqi NP_566470.1. NM_112247.2.
    UniGenei At.21338.

    3D structure databases

    ProteinModelPortali Q8RWN9.
    SMRi Q8RWN9. Positions 113-192, 302-539.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PaxDbi Q8RWN9.
    PRIDEi Q8RWN9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT3G13930.1 ; AT3G13930.1 ; AT3G13930 .
    GeneIDi 820606.
    KEGGi ath:AT3G13930.

    Organism-specific databases

    TAIRi AT3G13930.

    Phylogenomic databases

    eggNOGi COG0508.
    HOGENOMi HOG000281566.
    InParanoidi Q8RWN9.
    KOi K00627.
    OMAi MSMKEGT.
    PhylomeDBi Q8RWN9.

    Enzyme and pathway databases

    BioCyci ARA:AT3G13930-MONOMER.

    Gene expression databases

    Genevestigatori Q8RWN9.

    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.
    IPR006257. LAT1.
    IPR011053. Single_hybrid_motif.
    [Graphical view ]
    Pfami PF00198. 2-oxoacid_dh. 1 hit.
    PF00364. Biotin_lipoyl. 1 hit.
    PF02817. E3_binding. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47005. SSF47005. 1 hit.
    SSF51230. SSF51230. 1 hit.
    TIGRFAMsi TIGR01349. PDHac_trf_mito. 1 hit.
    PROSITEi PS50968. BIOTINYL_LIPOYL. 1 hit.
    PS00189. LIPOYL. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence features of the regions of 4,504,864 bp covered by sixty P1 and TAC clones."
      Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.
      DNA Res. 7:131-135(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    2. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    3. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
      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.
      Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Columbia.
    4. "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.
    5. "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 nameiODP22_ARATH
    AccessioniPrimary (citable) accession number: Q8RWN9
    Secondary accession number(s): Q9ASS8, Q9LVK7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 28, 2006
    Last sequence update: November 28, 2006
    Last modified: October 1, 2014
    This is version 91 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