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{{Tab On|Quickview|iaaA}}{{Tab|Gene|iaaA}}{{Tab|Gene Product(s)|iaaA}}{{Tab|Expression|iaaA}}{{Tab|Evolution|iaaA}}{{Tab|On One Page|iaaA}}{{TabsBottom}}
{{Tab On|Quickview|iaaA}}{{Tab|Gene|iaaA}}{{Tab|Gene Product(s)|iaaA}}{{Tab|Expression|iaaA}}{{Tab|Evolution|iaaA}}{{Tab|On One Page|iaaA}}{{TabsBottom}}
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!{{table_heading_style}} |Gene Name
!align=left {{table_heading_style}} |Standard Name
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[[iaaA:Gene|''iaaA]]'' (synonyms: ''ECK0818, b0828, JW0812, spt, ybiK'')<ref name='LIB:Riley_2006'/>
''iaaA''
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!{{table_heading_style}} |Product(s)  
!align=left {{table_heading_style}} |Gene Synonym(s)
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[[iaaA:Gene_Product(s)|IaaA product, IaaA product]]<ref name='LIB:Riley_2006'/><ref name='LIB:EcoCyc10.6'/>: L-asparaginase<ref name='LIB:Riley_2006'/>, B0828<ref name='LIB:EcoCyc10.6'/>, Spt<ref name='LIB:EcoCyc10.6'/>, IaaA<ref name='LIB:EcoCyc10.6'/>, YbiK<ref name='LIB:EcoCyc10.6'/>, [[:Category:Complex:asparaginase III &alpha;-&beta; complex|asparaginase III &alpha;-&beta; complex]]<ref name='LIB:EcoCyc11.1'/>, [[:Category:Complex:asparaginase III|asparaginase III]]<ref name='LIB:EcoCyc11.1'/>
''ECK0818, b0828, JW0812, spt, ybiK''<ref name='LIB:Riley_2006'/>, ybiK''
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!{{table_heading_style}} |Description
!align=left {{table_heading_style}} |Product Desc.
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&alpha; cleavage product of IaaA<ref name='LIB:EcoCyc10.6'/><ref name='LIB:EcoCyc11.1'/>
IaaA<ref name='LIB:EcoCyc10.6'/><ref name='LIB:EcoCyc11.1'/>;


Component of [[:Category:Complex:asparaginase III α-β complex|asparaginase III α-β complex]]<ref name='LIB:EcoCyc11.1'/>; [[:Category:Complex:asparaginase III|asparaginase III]]<ref name='LIB:EcoCyc11.1'/>


isoAsp aminopeptidase, cleaves isoAsp-X dipeptides, Ntn hydrolase, weak L-asparaginase activity in vitro (EcAIII), precursor is cleaved into an alpha and beta subunit<ref name='PMID:15265041'/>
heterotetrameric, glutathione utilization<ref name='LIB:EcoGene'/>
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!{{table_heading_style}} |Knock-Out Phenotype
!align=left {{table_heading_style}} |Product Synonyms(s)
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''L-asparaginase<ref name='LIB:Riley_2006'/>, B0828<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, Spt<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, YbiK<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/> , ECK0818, JW0812, spt, ybiK, b0828''
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!align=left {{table_heading_style}} |Function from GO
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<GO_nr />
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!align=left {{table_heading_style}} |Knock-Out Phenotype
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!{{table_heading_style}} |Regulation/Expression
!align=left {{table_heading_style}} |Regulation/Expression
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transcription unit(s): [[:Category:txn_units:iaaA|iaaA]]<ref name='LIB:EcoCyc10.6'/>  
transcription unit(s): [[:Category:Txn_unit:iaaA|iaaA]]<ref name='LIB:EcoCyc10.6'/>  
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!{{table_heading_style}} |Regulation/Activity
!align=left {{table_heading_style}} |Regulation/Activity
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!align=left {{table_heading_style}} |Quick Links
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[[File:porteco.png|link=http://porteco.org/AjaxSearch.jsp?searchString=iaaA&s=search]] [[File:EcoCyc.gif|link=http://biocyc.org/ECOLI/NEW-IMAGE?type=NIL&object=EG12407]] [[File:regulondb.jpg|link=http://regulondb.ccg.unam.mx/gene?term=ECK120002269&organism=ECK12&format=jsp&type=gene ]] <br/><br/> [[File:dnadisplay.png|link=http://ecoliwiki.net/tools/display_dna.php?gene=iaaA&loc=MG1655%3A865791..866756,W3110%3A866990..867955,DH10B%3A919719..920684,REL606%3A859120..860085,BW2952%3A768759..769724]] [[File:proteindisplay.png|link=http://ecoliwiki.net/tools/display_protein.php?f=NC_000913&start=768759&end=769724&gene=iaaA&aa=mritiilvaparaenigaaaramktmgfsdlrivdsqahlepatrwvahgsgdiidnikvfptlaeslhdvdftvattarsrakyhyyatpvelvplleeksswmshaalvfgredsgltneelaladvltgvpmvadypslnlgqavmvycyqlatliqqpaksdatadqhqlqalreramtllttlavaddiklvdwlqqrlglleqrdtamlhrllhdieknitk]]&nbsp;&nbsp;  [[File:pubmed.jpg|link=http://www.ncbi.nlm.nih.gov/sites/entrez?db=pubmed&cmd=Search&Term=iaaA+AND+escherichia+coli]]&nbsp;&nbsp;  [[File:textpresso.jpg|link=http://textpresso.tamu.edu/cgi-bin/textpresso/search?q=iaaA]]&nbsp;&nbsp;
 
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==Notes==
===Notes===
{{BacktoTop}}
 
''E. coli'' IaaA is cleaved before Thr179 to expose an N-terminal nucleophile and to produce two subunits.<ref name='PMID:15265041'/> CysB regulon, sensitive to cysteine repression. The start of the ''Salmonella'' IaaA is confirmed by N-terminal sequencing of the IaaA precursor. ''Salmonella'' IaaA has been shown to have isoaspartyl-tripeptidase activity.<ref name='PMID:11325937'/> ''E. coli'' probably also has tripeptidase activity.<ref name='LIB:EcoGene'/> ''iaaA'' is a non-essential gene.<ref name='LIB:EcoGene'/>
 




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==References==
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Latest revision as of 21:49, 27 May 2013

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Quickview   Gene   Gene Product(s)   Expression   Evolution   On One Page    
References Suggestions
Standard Name

iaaA

Gene Synonym(s)

ECK0818, b0828, JW0812, spt, ybiK[1], ybiK

Product Desc.

IaaA[2][3];

Component of asparaginase III α-β complex[3]; asparaginase III[3]

isoAsp aminopeptidase, cleaves isoAsp-X dipeptides, Ntn hydrolase, weak L-asparaginase activity in vitro (EcAIII), precursor is cleaved into an alpha and beta subunit[4]

heterotetrameric, glutathione utilization[5]

Product Synonyms(s)

L-asparaginase[1], B0828[2][1], Spt[2][1], YbiK[2][1] , ECK0818, JW0812, spt, ybiK, b0828

Function from GO

<GO_nr />

Knock-Out Phenotype
Regulation/Expression

transcription unit(s): iaaA[2]

Regulation/Activity
Quick Links



        

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Notes

[back to top]


E. coli IaaA is cleaved before Thr179 to expose an N-terminal nucleophile and to produce two subunits.[4] CysB regulon, sensitive to cysteine repression. The start of the Salmonella IaaA is confirmed by N-terminal sequencing of the IaaA precursor. Salmonella IaaA has been shown to have isoaspartyl-tripeptidase activity.[6] E. coli probably also has tripeptidase activity.[5] iaaA is a non-essential gene.[5]



References

[back to top]


  1. ↑ 1.0 1.1 1.2 1.3 1.4 Riley, M. et al. (2006) Nucleic Acids Res 34:1-6 (corrected supplemental data from B. Wanner)
  2. ↑ 2.0 2.1 2.2 2.3 2.4 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  3. ↑ 3.0 3.1 3.2 EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  4. ↑ 4.0 4.1 Borek, D et al. (2004) Expression, purification and catalytic activity of Lupinus luteus asparagine beta-amidohydrolase and its Escherichia coli homolog. Eur. J. Biochem. 271 3215-26 PubMed
  5. ↑ 5.0 5.1 5.2 EcoGene: Rudd, KE (2000) EcoGene: a genome sequence database for Escherichia coli K-12. Nucleic Acids Res 28:60-4.
  6. ↑ Larsen, RA et al. (2001) Aspartic peptide hydrolases in Salmonella enterica serovar typhimurium. J. Bacteriol. 183 3089-97 PubMed
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