iaaA:Quickview: Difference between revisions
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* ** PLEASE DON'T EDIT THIS TABLE DIRECTLY. Use the edit table link under the table. ** | * ** PLEASE DON'T EDIT THIS TABLE DIRECTLY. Use the edit table link under the table. ** | ||
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!align=left {{table_heading_style}} |Gene Synonym(s) | !align=left {{table_heading_style}} |Gene Synonym(s) | ||
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''ECK0818, b0828, JW0812, spt, ybiK''<ref name='LIB:Riley_2006'/> | ''ECK0818, b0828, JW0812, spt, ybiK''<ref name='LIB:Riley_2006'/>, ybiK'' | ||
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!align=left {{table_heading_style}} |Product Desc. | !align=left {{table_heading_style}} |Product Desc. | ||
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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'/> | 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 | 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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!align=left {{table_heading_style}} |Product Synonyms(s) | !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'/> | ''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 | !align=left {{table_heading_style}} |Function from GO | ||
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!align=left {{table_heading_style}} |Quick Links | !align=left {{table_heading_style}} |Quick Links | ||
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[http://porteco.org/AjaxSearch.jsp?searchString=iaaA&s=search | [[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]] [[File:pubmed.jpg|link=http://www.ncbi.nlm.nih.gov/sites/entrez?db=pubmed&cmd=Search&Term=iaaA+AND+escherichia+coli]] [[File:textpresso.jpg|link=http://textpresso.tamu.edu/cgi-bin/textpresso/search?q=iaaA]] | ||
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{{BacktoTop}} | {{BacktoTop}} | ||
IaaA is cleaved before Thr179 to expose N-terminal nucleophile and to produce two subunits. CysB regulon, sensitive to cysteine repression. | ''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'/> | ||
<noinclude> | <noinclude> | ||
==References== | ==References== | ||
{{BacktoTop}} | {{BacktoTop}} | ||
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. |
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 | |
| Regulation/Activity | |
| Quick Links | |
| edit table |
See Help:Quickview for help with entering information in the Quickview table.
Notes
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
- ↑ 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)
- ↑ 2.0 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
- ↑ 3.0 3.1 3.2 EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
- ↑ 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
- ↑ 5.0 5.1 5.2 EcoGene: Rudd, KE (2000) EcoGene: a genome sequence database for Escherichia coli K-12. Nucleic Acids Res 28:60-4.
- ↑ Larsen, RA et al. (2001) Aspartic peptide hydrolases in Salmonella enterica serovar typhimurium. J. Bacteriol. 183 3089-97 PubMed


