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Protein Overview: ODP23_ARATH

General Information:
Name(s) found: ODP23_ARATH [Swiss-Prot]
Description(s) found:
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  • gi|79319911|ref|NP_001031186.1| dihydrolipoamide S-acetyltransferase, putative [Arabidopsis thaliana] [NCBI NR]
  • gi|75285553|sp|Q5M729.1|OPD23_ARATH RecName: Full=Dihydrolipoyllysine-residue acetyltransferase component 3 of pyruvate dehydrogenase complex, mitochondrial; AltName: Full=Pyruvate dehydrogenase complex E2 subunit 3; Short=PDC-E2; Short=PDCE2; Short=E2; A [NCBI NR]
  • gi|56550713|gb|AAV97810.1| At1g54220 [Arabidopsis thaliana] [NCBI NR]
  • gi|18404837|ref|NP_564654.1| dihydrolipoamide S-acetyltransferase, putative [Arabidopsis thaliana] [NCBI NR]
  • Dihydrolipoyllysine-residue acetyltransferase component 3 of pyruvate dehydrogenase complex, mitochondrial OS=Arabidopsis thaliana GN=At1g54220 PE=1 SV=1 [Swiss-Prot]
  • Dihydrolipoyllysine-residue acetyltransferase component 3 of pyruvate dehydrogenase complex, mitochondrial OS=Arabidopsis thaliana GN=At1g54220 PE=2 SV=1 [Swiss-Prot]
  • dihydrolipoamide S-acetyltransferase, putative [Arabidopsis thaliana] [nrdb_11152004_Chlamydomonas]
  • Tax_Id=3702 Dihydrolipoamide S-acetyltransferase [EBI-IPI_Arabidopsis_3.11_12-06-2005_reversed.fasta]
  • | Symbols: | dihydrolipoamide S-acetyltransferase, putative | chr1:20250127-20253875 REVERSE [TAIR_Arabidopsis_na_04-12-2008_con_reversed.fasta]
  • Dihydrolipoyllysine-residue acetyltransferase component 3 of pyruvate dehydrogenase complex, mitochondrial precursor (Pyruvate dehydrogenase complex E2 subunit 3) (PDCE2) (E2) (Dihydrolipoamide S-acetyltransferase component 3 of pyruvate dehydrogenase com [nr-271106-contam.fasta]
  • acyltransferase/ dihydrolipoyllysine-residue acetyltransferase/ protein binding [Arabidopsis thaliana] [nr-271106-contam.fasta]
  • At1g54220 [Arabidopsis thaliana] [nr-271106-contam.fasta]
  • | Symbols: | Dihydrolipoamide acetyltransferase, long form protein | chr1:20246460-20250208 REVERSE LENGTH=539 [TAIR_A_Thaliana_10_12-14-2010_reversed.fasta]
    • Organism: Arabidopsis thaliana
    Length: 539 amino acids

    Gene Ontology:
    Cellular Component: mitochondrion [IDA]
    Biological Process: metabolic process [IEA]
    pyruvate metabolic process [IEA]
    Molecular Function: protein binding [IEA]
    acyltransferase activity [IEA]
    dihydrolipoyllysine-residue acetyltransferase activity [IEA][ISS]


    Sequence:
    Sequence:
    [PDR BLAST]
    [ProtParam] 
          1          11         21         31         41         51         
      |          |          |          |          |          |          
    1 MAYASRIINH SKKLKDVSTL LRRENAATIR YYSNTNRAPL NREDTFNSRL GYPPLERISI  60
   61 CSTSTLPVSI IFSTTRSNLS SAMGRPIFGK EFSCLMQSAR GFSSGSDLPP HQEIGMPSLS 120
  121 PTMTEGNIAR WLKKEGDKVA PGEVLCEVET DKATVEMECM EEGYLAKIVK AEGSKEIQVG 180
  181 EVIAITVEDE EDIGKFKDYT PSSTADAAPT KAEPTPAPPK EEKVKQPSSP PEPKASKPST 240
  241 PPTGDRVFAS PLARKLAEDN NVPLSDIEGT GPEGRIVKAD IDEYLASSGK GATAKPSKST 300
  301 DSKAPALDYV DIPHSQIRKV TASRLAFSKQ TIPHYYLTVD TCVDKLMALR SQLNSFKEAS 360
  361 GGKRISVNDL VVKAAALALR KVPQCNSSWT DDYIRQFKNV NINVAVQTEN GLYVPVVKDA 420
  421 DRKGLSTIGE EVRLLAQKAK ENSLKPEDYE GGTFTVSNLG GPFGIKQFCA VVNPPQAAIL 480
  481 AVGSAEKRVV PGNGPDQFNF ASYMPVTLSC DHRVVDGAIG AEWLKAFKGY IENPKSMLL

    Protein Complex Data

    No complex found for this protein.

    Mass Spectrometry Data

    No mass spectrometry results found for this protein.

    Yeast Two-Hybrid Data

    The following interactions contain this protein:

    SHOWING SINGLE HITS. [ Hide Single Hits ]

    [View our yeast two-hybrid interpretation guidelines.]

    No yeast two-hybrid interactions found for this protein.

    Microscopy / Localization Data

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    No microscopy data found in the PDR for this protein.

    Protein Structure Data


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    [View Top Sequence Alignments] [Show Ginzu Version Information]

    Domains predicted:

    #   Region(s) Method Confidence Match Description
    1 View Details [1..109] MSA 1.414992 View MSA. No confident structure predictions are available.
    2 View Details [110..295] PSI-BLAST 24.522879 The crystal structure of dihydrolipoamide dehydrogenase and dihydrolipoamide dehydrogenase-binding protein (didomain) subcomplex of human pyruvate dehydrogenase complex.
    3 View Details [296..539] PSI-BLAST 85.522879 Dihydrolipoamide succinyltransferase


    Reference: Drew K, et al. (2011) The proteome folding project: Proteome-scale prediction of structure and function. Genome Res. 2011 Sep 16


    Philius Transmembrane Prediction:

    Protein predicted to be: GLOBULAR (No transmembrane regions or signal peptide)
    Confidence of classification: 0.96

    Source: Reynolds et al. (2008)

    YRC Informatics Platform - Version 3.0
    Created and Maintained by: Michael Riffle