PKS:An14g04850 - Revision history

Editor at 17:22, 25 May 2012

2012-05-25T17:22:16Z

Editor at 17:16, 25 May 2012

2012-05-25T17:16:26Z

Editor at 17:16, 25 May 2012

2012-05-25T17:16:06Z

Editor: moved PKS:ANig40 to PKS:An14g04850

2012-04-23T07:17:23Z

moved PKS:ANig40 to PKS:An14g04850

Editor at 17:07, 9 April 2012

2012-04-09T17:07:28Z

Editor at 16:57, 9 April 2012

2012-04-09T16:57:36Z

Editor at 16:57, 9 April 2012

2012-04-09T16:57:06Z

Editor at 16:56, 9 April 2012

2012-04-09T16:56:43Z

Editor at 16:51, 9 April 2012

2012-04-09T16:51:47Z

Editor at 16:51, 9 April 2012

2012-04-09T16:51:08Z

@@ Line 10: / Line 10: @@
 |geneName=
 |MAPSI=ACP-KS-AT-ACP
-|CDD=LuxE-PP-KS-AT-PP
+|CDD=A-PP-KS-AT-(KR)-PP
 |class=NRPS-PKS
 |reliability=
 |description=hypothetical protein An14g04850 [Aspergillus niger]
-|information=Possible NRPS-PKS domain structure: AP-KS-AT-P. GeneBank ID was updated from XP_001401108.1 to CAK42046.1.
+|information=Possible NRPS-PKS domain structure: A-P-KS-AT-P. GeneBank ID was updated from XP_001401108.1 to CAK42046.1.
 |length=1869
 |references=\*Pel.+2007$
 }}
 {{{{NAMESPACE}}/Footer}}

@@ Line 14: / Line 14: @@
 |reliability=
 |description=hypothetical protein An14g04850 [Aspergillus niger]
-|information=Possible NRPS-PKS domain structure: AP-KS-AT-P. GeneBank ID was updated to CAK42046.1.
+|information=Possible NRPS-PKS domain structure: AP-KS-AT-P. GeneBank ID was updated from XP_001401108.1 to CAK42046.1.
 |length=1869
 |references=\*Pel.+2007$
 }}
 {{{{NAMESPACE}}/Footer}}

@@ Line 4: / Line 4: @@
 |taxonomy=Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomyceta; Pezizomycotina; Leotiomyceta; Eurotiomycetes; Eurotiomycetidae; Eurotiales; Trichocomaceae; mitosporic Trichocomaceae; Aspergillus
 |product=
-|GenBank=XP_001401108
+|GenBank=CAK42046.1
 |UniProt=A2R3M8
 |UniRef90=-
@@ Line 14: / Line 14: @@
 |reliability=
 |description=hypothetical protein An14g04850 [Aspergillus niger]
-|information=Possible NRPS-PKS domain structure: AP-KS-AT-P. Domain AA-adenyl-dom and PP before KS. (Title: strong similarity to pimaricin polyketide synthase pimS2 - Streptomyces natalensis; Catalytic activity: polyketide synthases are multifunctional enzymes-containing oxidoreductase-transferase and dehydratase activity; some of the typical domains present in polyketide synthases are recognized in the predicted ORF.; Function: pimS2 of S. natalensis is involved in the biosynthesis of the polyene macrolide pimaricin-important in the food industry as a preservative to prevent mould contamination of foods.; Pathway: polyketides are generated from acetate by a pathway similar to the fatty acid metabolism-where some reduction or dehydratation reactions can be suppressed at specific biosynthetic steps-resulting in a much wider range of products-constituting a large family of often biologically active secondary metabolites.; Similarity: the predicted ORF shows strong similarity to different fungal polyketide synthases.)
+|information=Possible NRPS-PKS domain structure: AP-KS-AT-P. GeneBank ID was updated to CAK42046.1.
 |length=1869
 |references=\*Pel.+2007$
 }}
 {{{{NAMESPACE}}/Footer}}

@@ Line 14: / Line 14: @@
 |reliability=
 |description=hypothetical protein An14g04850 [Aspergillus niger]
-|information=domain-AA-adenyl-dom and PP before KS. Possible domain structure: AP-KS-AT-P.(Title: strong similarity to pimaricin polyketide synthase pimS2 - Streptomyces natalensis; Catalytic activity: polyketide synthases are multifunctional enzymes-containing oxidoreductase-transferase and dehydratase activity; some of the typical domains present in polyketide synthases are recognized in the predicted ORF.; Function: pimS2 of S. natalensis is involved in the biosynthesis of the polyene macrolide pimaricin-important in the food industry as a preservative to prevent mould contamination of foods.; Pathway: polyketides are generated from acetate by a pathway similar to the fatty acid metabolism-where some reduction or dehydratation reactions can be suppressed at specific biosynthetic steps-resulting in a much wider range of products-constituting a large family of often biologically active secondary metabolites.; Similarity: the predicted ORF shows strong similarity to different fungal polyketide synthases.)
+|information=Possible NRPS-PKS domain structure: AP-KS-AT-P. Domain AA-adenyl-dom and PP before KS. (Title: strong similarity to pimaricin polyketide synthase pimS2 - Streptomyces natalensis; Catalytic activity: polyketide synthases are multifunctional enzymes-containing oxidoreductase-transferase and dehydratase activity; some of the typical domains present in polyketide synthases are recognized in the predicted ORF.; Function: pimS2 of S. natalensis is involved in the biosynthesis of the polyene macrolide pimaricin-important in the food industry as a preservative to prevent mould contamination of foods.; Pathway: polyketides are generated from acetate by a pathway similar to the fatty acid metabolism-where some reduction or dehydratation reactions can be suppressed at specific biosynthetic steps-resulting in a much wider range of products-constituting a large family of often biologically active secondary metabolites.; Similarity: the predicted ORF shows strong similarity to different fungal polyketide synthases.)
 |length=1869
 |references=\*Pel.+2007$
 }}
 {{{{NAMESPACE}}/Footer}}

@@ Line 14: / Line 14: @@
 |reliability=
 |description=hypothetical protein An14g04850 [Aspergillus niger]
-|information=domain-AA-adenyl-dom and PP before KS. Possible domain structure: AP-KS-AT-P.
+|information=domain-AA-adenyl-dom and PP before KS. Possible domain structure: AP-KS-AT-P.(Title: strong similarity to pimaricin polyketide synthase pimS2 - Streptomyces natalensis; Catalytic activity: polyketide synthases are multifunctional enzymes-containing oxidoreductase-transferase and dehydratase activity; some of the typical domains present in polyketide synthases are recognized in the predicted ORF.; Function: pimS2 of S. natalensis is involved in the biosynthesis of the polyene macrolide pimaricin-important in the food industry as a preservative to prevent mould contamination of foods.; Pathway: polyketides are generated from acetate by a pathway similar to the fatty acid metabolism-where some reduction or dehydratation reactions can be suppressed at specific biosynthetic steps-resulting in a much wider range of products-constituting a large family of often biologically active secondary metabolites.; Similarity: the predicted ORF shows strong similarity to different fungal polyketide synthases.)
- (Title: strong similarity to pimaricin polyketide synthase pimS2 - Streptomyces natalensis; Catalytic activity: polyketide synthases are multifunctional enzymes-containing oxidoreductase-transferase and dehydratase activity; some of the typical domains present in polyketide synthases are recognized in the predicted ORF.; Function: pimS2 of S. natalensis is involved in the biosynthesis of the polyene macrolide pimaricin-important in the food industry as a preservative to prevent mould contamination of foods.; Pathway: polyketides are generated from acetate by a pathway similar to the fatty acid metabolism-where some reduction or dehydratation reactions can be suppressed at specific biosynthetic steps-resulting in a much wider range of products-constituting a large family of often biologically active secondary metabolites.; Similarity: the predicted ORF shows strong similarity to different fungal polyketide synthases.)
 |length=1869
 |references=\*Pel.+2007$
 }}
 {{{{NAMESPACE}}/Footer}}