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Q5M729

- ODP23_ARATH

UniProt

Q5M729 - ODP23_ARATH

Protein

Dihydrolipoyllysine-residue acetyltransferase component 3 of pyruvate dehydrogenase complex, mitochondrial

Gene

At1g54220

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 76 (01 Oct 2014)
      Sequence version 1 (01 Feb 2005)
      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. 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:AT1G54220-MONOMER.
    ARA:GQT-1082-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dihydrolipoyllysine-residue acetyltransferase component 3 of pyruvate dehydrogenase complex, mitochondrial (EC:2.3.1.12)
    Alternative name(s):
    Dihydrolipoamide S-acetyltransferase component 3 of pyruvate dehydrogenase complex
    Pyruvate dehydrogenase complex component E2 3
    Short name:
    PDC-E2 3
    Short name:
    PDCE2 3
    Gene namesi
    Ordered Locus Names:At1g54220
    ORF Names:F20D21.4
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 1

    Organism-specific databases

    TAIRiAT1G54220.

    Subcellular locationi

    Mitochondrion matrix 1 Publication

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini? – 539Dihydrolipoyllysine-residue acetyltransferase component 3 of pyruvate dehydrogenase complex, mitochondrialPRO_0000260027
    Transit peptidei1 – ?Mitochondrion

    Amino acid modifications

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

    Proteomic databases

    PaxDbiQ5M729.
    PRIDEiQ5M729.

    Expressioni

    Gene expression databases

    GenevestigatoriQ5M729.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5M729.
    SMRiQ5M729. Positions 113-192, 305-539.
    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.
    InParanoidiQ5M729.
    KOiK00627.
    OMAiGSADGQY.
    PhylomeDBiQ5M729.

    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.

    Q5M729-1 [UniParc]FASTAAdd to Basket

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    MAYASRIINH SKKLKDVSTL LRRENAATIR YYSNTNRAPL NREDTFNSRL    50
    GYPPLERISI CSTSTLPVSI IFSTTRSNLS SAMGRPIFGK EFSCLMQSAR 100
    GFSSGSDLPP HQEIGMPSLS PTMTEGNIAR WLKKEGDKVA PGEVLCEVET 150
    DKATVEMECM EEGYLAKIVK AEGSKEIQVG EVIAITVEDE EDIGKFKDYT 200
    PSSTADAAPT KAEPTPAPPK EEKVKQPSSP PEPKASKPST PPTGDRVFAS 250
    PLARKLAEDN NVPLSDIEGT GPEGRIVKAD IDEYLASSGK GATAKPSKST 300
    DSKAPALDYV DIPHSQIRKV TASRLAFSKQ TIPHYYLTVD TCVDKLMALR 350
    SQLNSFKEAS GGKRISVNDL VVKAAALALR KVPQCNSSWT DDYIRQFKNV 400
    NINVAVQTEN GLYVPVVKDA DRKGLSTIGE EVRLLAQKAK ENSLKPEDYE 450
    GGTFTVSNLG GPFGIKQFCA VVNPPQAAIL AVGSAEKRVV PGNGPDQFNF 500
    ASYMPVTLSC DHRVVDGAIG AEWLKAFKGY IENPKSMLL 539
    Length:539
    Mass (Da):58,467
    Last modified:February 1, 2005 - v1
    Checksum:i0C4E141079A2698F
    GO

    Sequence cautioni

    The sequence AAD25602.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti45 – 451T → I in AAK53067. 1 PublicationCurated
    Sequence conflicti267 – 2671I → T in AAK53067. 1 PublicationCurated
    Sequence conflicti442 – 4421N → S in AAM97076. (PubMed:14593172)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY033001 mRNA. Translation: AAK53067.1.
    AC005287 Genomic DNA. Translation: AAD25602.1. Sequence problems.
    CP002684 Genomic DNA. Translation: AEE33067.1.
    CP002684 Genomic DNA. Translation: AEE33068.1.
    AY136410 mRNA. Translation: AAM97076.1.
    BT020419 mRNA. Translation: AAV97810.1.
    PIRiE96583.
    RefSeqiNP_001031186.1. NM_001036109.1.
    NP_564654.1. NM_104300.3.
    UniGeneiAt.19093.
    At.21338.

    Genome annotation databases

    EnsemblPlantsiAT1G54220.1; AT1G54220.1; AT1G54220.
    AT1G54220.2; AT1G54220.2; AT1G54220.
    GeneIDi841863.
    KEGGiath:AT1G54220.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY033001 mRNA. Translation: AAK53067.1 .
    AC005287 Genomic DNA. Translation: AAD25602.1 . Sequence problems.
    CP002684 Genomic DNA. Translation: AEE33067.1 .
    CP002684 Genomic DNA. Translation: AEE33068.1 .
    AY136410 mRNA. Translation: AAM97076.1 .
    BT020419 mRNA. Translation: AAV97810.1 .
    PIRi E96583.
    RefSeqi NP_001031186.1. NM_001036109.1.
    NP_564654.1. NM_104300.3.
    UniGenei At.19093.
    At.21338.

    3D structure databases

    ProteinModelPortali Q5M729.
    SMRi Q5M729. Positions 113-192, 305-539.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PaxDbi Q5M729.
    PRIDEi Q5M729.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT1G54220.1 ; AT1G54220.1 ; AT1G54220 .
    AT1G54220.2 ; AT1G54220.2 ; AT1G54220 .
    GeneIDi 841863.
    KEGGi ath:AT1G54220.

    Organism-specific databases

    TAIRi AT1G54220.

    Phylogenomic databases

    eggNOGi COG0508.
    HOGENOMi HOG000281566.
    InParanoidi Q5M729.
    KOi K00627.
    OMAi GSADGQY.
    PhylomeDBi Q5M729.

    Enzyme and pathway databases

    BioCyci ARA:AT1G54220-MONOMER.
    ARA:GQT-1082-MONOMER.

    Gene expression databases

    Genevestigatori Q5M729.

    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. "Mono-lipoyl E2 from pyruvate dehydrogenase complex from Arabidopsis."
      Broz A.K., Randall D.D., Miernyk J.A., Mooney B.P.
      Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
      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.
      Nature 408:816-820(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. "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.
    5. "Arabidopsis ORF clones."
      Shinn P., Chen H., Cheuk R.F., Kim C.J., Ecker J.R.
      Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Columbia.
    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 nameiODP23_ARATH
    AccessioniPrimary (citable) accession number: Q5M729
    Secondary accession number(s): Q8L787, Q94IP5, Q9SLL0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 14, 2006
    Last sequence update: February 1, 2005
    Last modified: October 1, 2014
    This is version 76 of the entry and version 1 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