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Protein Overview: LAT1

General Information:
Name(s) found: LAT1 / YNL071W [SGD]
Description(s) found:
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  • pir||A30198 dihydrolipoamide S-acetyltransferase (EC 2.3.1.12) precursor - yeast (Saccharomyces cerevisiae) [NCBI NR]
  • gi|791115|emb|CAA60189.1| dihydrolipoamide S-acetyltransferase [Saccharomyces cerevisiae] [NCBI NR]
  • gi|6324258|ref|NP_014328.1| Dihydrolipoamide acetyltransferase component (E2) of pyruvate dehydrogenase complex, which catalyzes the oxidative decarboxylation of pyruvate to acetyl-CoA; Lat1p [Saccharomyces cerevisiae] [NCBI NR]
  • gi|51013821|gb|AAT93204.1| YNL071W [Saccharomyces cerevisiae] [NCBI NR]
  • gi|170972|gb|AAA34385.1| dihydrolipoamide acetyltransferase precursor (EC 2.3.1.12) [NCBI NR]
  • gi|1301955|emb|CAA95945.1| LAT1 [Saccharomyces cerevisiae] [NCBI NR]
  • gi|129060|sp|P12695.1|ODP2_YEAST RecName: Full=Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial; AltName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex; AltName: [NCBI NR]
  • Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial OS=Saccharomyces cerevisiae GN=PDA2 PE=1 SV=1 [Swiss-Prot]
  • LAT1 Dihydrolipoamide S-acetyltransferase [mips]
  • Dihydrolipoamide acetyltransferase component (E2) of pyruvate dehydrogenase complex, which catalyzes the oxidative decarboxylation of pyruvate to acetyl-CoA [SGD]
  • LAT1, Chr XIV from 491520-492968 [yeast_orfs2]
  • Chr XIV from 491520-492968 [yeastorf3.fasta]
  • (P12695) Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial precursor (EC 2.3.1.12) (E2) (PDC-E2) [4932.FASTACCERV.txt]
  • LAT1 SGDID:S0005015, Chr XIV from 491522-492970, Verified ORF [yeastflysequest.fasta]
  • Dihydrolipoamide acetyltransferase component (E2) of pyruvate dehydrogenase complex, which catalyzes the oxidative decarboxylation of pyruvate to acetyl-CoA [Saccharomyces cerevisiae]gi|51013821|gb|AAT93204.1| YNL071W [Saccharomyces cerevisiae]gi|791115 [nrdb_11152004_Chlamydomonas]
  • (P12695) Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial precursor (EC 2.3.1.12) (E2) (Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex) (PDC-E2) [cerv4932.FASTAC]
  • LAT1 SGDID:S000005015, Chr XIV from 491524-492972, Verified ORF, "Dihydrolipoamide acetyltransferase component (E2) of pyruvate dehydrogenase complex, which catalyzes the oxidative decarboxylation of pyruvate to acetyl-CoA" [SGD_S-cerevisiae_na_12-16-2005_con_reversed.fasta]
  • YNL071W [Saccharomyces cerevisiae] [nr-271106-contam.fasta]
  • Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial precursor (Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex) (Pyruvate dehydrogenase complex E2 component) (PDC-E2) [nr-271106-contam.fasta]
  • dihydrolipoamide S-acetyltransferase [Saccharomyces cerevisiae] [nr-271106-contam.fasta]
  • dihydrolipoamide acetyltransferase precursor (EC 2.3.1.12) [nr-271106-contam.fasta]
  • LAT1 [Saccharomyces cerevisiae] [nr-271106-contam.fasta]
  • Dihydrolipoamide acetyltransferase component (E2) of pyruvate dehydrogenase complex, which catalyzes the oxidative decarboxylation of pyruvate to acetyl-CoA; Lat1p [Saccharomyces cerevisiae] [nr-271106-contam.fasta]
  • LAT1 SGDID:S000005015, Chr XIV from 491525-492973, Verified ORF, "Dihydrolipoamide acetyltransferase component (E2) of pyruvate dehydrogenase complex, which catalyzes the oxidative decarboxylation of pyruvate to acetyl-CoA" [SGD_S-cerevisiae_na_01-05-2010_reversed.fasta]
  • [chemostatdb.fasta]
  • Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=LAT1 PE=1 SV=1 [UniProt_S_cerevisiae_20120516_05-16-2012_reversed.fasta]
  • LAT1 SGDID:S000005015, Chr XIV from 491523-492971, Genome Release 64-1-1, Verified ORF, "Dihydrolipoamide acetyltransferase component (E2) of pyruvate dehydrogenase complex, which catalyzes the oxidative decarboxylation of pyruvate to acetyl-CoA" [yeast-030211-contam.fasta]
  • LAT1 SGDID:S000005015, Chr XIV from 491523-492971, Genome Release 64-2-1, Verified ORF, "Dihydrolipoamide acetyltransferase component (E2) of the PDC; the pyruvate dehydrogenase complex (PDC) catalyzes the oxidative decarboxylation of pyruvate to acetyl-CoA" [20141208_orf_trans.fasta]
  • YNL071W SGDID:S000005015, Chr XIV from 491523-492971, Genome Release 64-1-1, Verified ORF, "Dihydrolipoamide acetyltransferase component (E2) of pyruvate dehydrogenase complex, which catalyzes the oxidative decarboxylation of pyruvate to acetyl-CoA" [2016-01-SGD_Yeast_Contam_Riffle_20140507-Ska-Hec-110-tubulin.fasta]
    • Organism: Saccharomyces cerevisiae
    Length: 482 amino acids

    Gene Ontology:
    Cellular Component: mitochondrial pyruvate dehydrogenase complex [TASLink to PubMed article]
    mitochondrion [IDALink to PubMed articleLink to PubMed articleLink to PubMed articleLink to PubMed article]
    Biological Process: pyruvate metabolic process [TASLink to PubMed article]
    Molecular Function: dihydrolipoyllysine-residue acetyltransferase activity [IDALink to PubMed article]


    Sequence:
    Sequence:
    [PDR BLAST]
    [ProtParam] 
          1          11         21         31         41         51         
      |          |          |          |          |          |          
    1 MSAFVRVVPR ISRSSVLTRS LRLQLRCYAS YPEHTIIGMP ALSPTMTQGN LAAWTKKEGD  60
   61 QLSPGEVIAE IETDKAQMDF EFQEDGYLAK ILVPEGTKDI PVNKPIAVYV EDKADVPAFK 120
  121 DFKLEDSGSD SKTSTKAQPA EPQAEKKQEA PAEETKTSAP EAKKSDVAAP QGRIFASPLA 180
  181 KTIALEKGIS LKDVHGTGPR GRITKADIES YLEKSSKQSS QTSGAAAATP AAATSSTTAG 240
  241 SAPSPSSTAS YEDVPISTMR SIIGERLLQS TQGIPSYIVS SKISISKLLK LRQSLNATAN 300
  301 DKYKLSINDL LVKAITVAAK RVPDANAYWL PNENVIRKFK NVDVSVAVAT PTGLLTPIVK 360
  361 NCEAKGLSQI SNEIKELVKR ARINKLAPEE FQGGTICISN MGMNNAVNMF TSIINPPQST 420
  421 ILAIATVERV AVEDAAAENG FSFDNQVTIT GTFDHRTIDG AKGAEFMKEL KTVIENPLEM 480
  481 LL

    Protein Complex Data

      PUBLICATION TOPOLOGY COCOMPLEXED PROTEINS
    View Details Riffle et al. (2010) (Unpublished Data) LAT1 LPD1 PDA1 PDB1 PDX1
    View Details (MIPS) Mewes HW, et al. (2004) LAT1 LPD1 PDA1 PDB1 PDX1
    View Details Krogan NJ, et al. (2006) LAT1 PDA1
    View Details Gavin AC, et al. (2006) LAT1 PDA1 PDB1 PDX1
    View Details Gavin AC, et al. (2002) APM1 CYM1 DOA4 DUR1,2 HSP42 LAT1 LPD1 PDA1 PDB1 PDX1 PRP46 RPN11 TCM62
    View Details Qiu et al. (2008) LAT1 LPD1 PDA1 PDX1

    Mass Spectrometry Data

    The following runs contain data for this protein:

      BAIT COMMENTS PUBLICATION
    View Run SMC5 No Comments Hazbun TR, et al. (2003)
    View Run CAB4 No Comments Hazbun TR, et al. (2003)
    View Run NOP9 No Comments Hazbun TR, et al. (2003)
    View Run NSE3 No Comments Hazbun TR, et al. (2003)
    View Run CWC25 No Comments Hazbun TR, et al. (2003)
    View Run SMC5 No Comments Hazbun TR, et al. (2003)
    View Run LST8 No Comments Reinke A, et al. (2004)
    View Run TOR2 No Comments Reinke A, et al. (2004)
    View Run SEC10 No Comments De Craene, J., et al. (2006)
    View Run DAD1 Dam1 complex purified from yeast with Dad1-TAP Shimogawa MM, et al. (2006)
    View Run RPA135 his-HA tag on RPA135 Schneider, DA, et al. (2006)
    View Run RPA135 his-HA tag on RPA135 Schneider, DA, et al. (2006)
    View Run RPA135 his-HA tag on RPA135 Schneider, DA, et al. (2006)
    View Run DAD1 Dam1-765 complex purified from yeast with Dad1-TAP Shimogawa MM, et al. (2006)
    View Run DAD1 Dam1 complex purified from yeast with Dad1-TAP Shimogawa MM, et al. (2006)
    View Run ZDS1 Sample 2- cpn2 from june 2005 McCusker D, et al (2007)
    View Run ZDS1 Sample 3 - cpn + atp, from june 2005 McCusker D, et al (2007)
    View Run VAM3 sample: hx3 Hao Xu, et al. (2010)
    View Run VAM3 Sample: HX11 - both fusion and trans-SNARE complex formation take place. Hao Xu, et al. (2010)
    View Run VAM3 Sample: HX12 - trans-SNARE complex formation and fusion are inhibited (control). Hao Xu, et al. (2010)
    View Run VAM3 Sample: HX13 - trans-SNARE complex forms but fusion is blocked. Hao Xu, et al. (2010)
    View Run VAM3 Sample: HX14 - mixture in detergent (control). Hao Xu, et al. (2010)
    View Run MLP2 #19 Asynchronous Prep1-TiO2 Phosphopeptide enrichment Keck JM, et al. (2011)
    View Run MLP2 #24 Asynchronous Prep3-TiO2 Phosphopeptide enrichment Keck JM, et al. (2011)
    View Run MLP2 #32 Asynchronous Prep-No Phosphopeptide enrichment Keck JM, et al. (2011)
    View Run MLP2 #03 Alpha Factor Prep1-TiO2 Flowthrough Keck JM, et al. (2011)
    View Run MLP2 #19b Asynchronous Prep1-new search criteria Keck JM, et al. (2011)
    View Run MLP2 #19a Asynchronous Prep1-new search criteria Keck JM, et al. (2011)

    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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      PROTEIN(S) PUBLICATION
    View Data LAT1 Huh WK, et al. (2003)

    Protein Structure Data


    [What does the above image mean?]
    [View Top Sequence Alignments] [Show Ginzu Version Information]

    Domains predicted:

    #   Region(s) Method Confidence Match Description
    1 View Details [1..161] PSI-BLAST 287.025158 Ipoyl domain of dihydrolipoamide acetyltransferase
    2 View Details [162..233] PSI-BLAST 28.85005 E3-binding domain of dihydrolipoamide acetyltransferase
    3 View Details [234..482] PSI-BLAST 357.08661 Dihydrolipoamide succinyltransferase

    Functions predicted (by domain):

    # Gene Ontology predictions
    1 No functions predicted.
    2
    Term Confidence Notes
  • S-succinyltransferase activity
    		•  10.0778678835755 bayes_pls_golite062009
  • dihydrolipoyllysine-residue succinyltransferase activity
    		•  10.0778678835755 bayes_pls_golite062009
  • dihydrolipoyllysine-residue acetyltransferase activity
    		•  9.65061123545754 bayes_pls_golite062009
  • dihydrolipoamide S-acyltransferase activity
    		•  9.64995677986911 bayes_pls_golite062009
  • S-acetyltransferase activity
    		•  9.49696044977584 bayes_pls_golite062009
  • S-acyltransferase activity
    		•  8.45313874919036 bayes_pls_golite062009
  • pyruvate dehydrogenase activity
    		•  8.17557182322815 bayes_pls_golite062009
  • transferase activity, transferring acyl groups other than amino-acyl groups
    		•  6.86215901871647 bayes_pls_golite062009
  • acyltransferase activity
    		•  6.83977352892719 bayes_pls_golite062009
  • succinyltransferase activity
    		•  6.58826720904067 bayes_pls_golite062009
  • pyruvate dehydrogenase (acetyl-transferring) activity
    		•  6.40483178382327 bayes_pls_golite062009
  • acetyltransferase activity
    		•  6.08159176722072 bayes_pls_golite062009
  • oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor
    		•  5.93985773477717 bayes_pls_golite062009
  • transferase activity, transferring acyl groups
    		•  4.60481199262496 bayes_pls_golite062009
  • carnitine O-acyltransferase activity
    		•  2.87366177129153 bayes_pls_golite062009
  • oxidoreductase activity, acting on the aldehyde or oxo group of donors
    		•  2.54513901872655 bayes_pls_golite062009
  • catalytic activity
    		•  1.51562638409295 bayes_pls_golite062009
  • O-acyltransferase activity
    		•  1.33852311685118 bayes_pls_golite062009
  • O-palmitoyltransferase activity
    		•  1.22729402619659 bayes_pls_golite062009
  • carnitine O-palmitoyltransferase activity
    		•  1.22729402619659 bayes_pls_golite062009
  • transferase activity
    		•  1.08341671157927 bayes_pls_golite062009
  • carnitine O-acetyltransferase activity
    		•  1.00868366840715 bayes_pls_golite062009
  • binding
    		•  0.801074244553007 bayes_pls_golite062009
  • alpha-ketoacid dehydrogenase activity
    		•  0.79135670574828 bayes_pls_golite062009
  • O-acetyltransferase activity
    		•  0.54660034926676 bayes_pls_golite062009
  • protein binding
    		•  0.00454070917775817 bayes_pls_golite062009
    3 No functions predicted.


    Reference: Malmström L, et al. (2007) Superfamily assignments for the yeast proteome through integration of structure prediction with the gene ontology. PLoS Biol 5(4): e76. doi:10.1371/journal.pbio.0050076


    Philius Transmembrane Prediction:

    Protein predicted to be: GLOBULAR (No transmembrane regions or signal peptide)
    Confidence of classification: 0.89

    Source: Reynolds et al. (2008)

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