PKS:An08g03790
From Metabolomics.JP
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|product= | |product= | ||
|GenBank=XP_001392496 | |GenBank=XP_001392496 | ||
+ | |UniProt=A2QTH2 | ||
+ | |UniRef90=- | ||
+ | |UniRef50=- | ||
|geneName= | |geneName= | ||
|MAPSI=KS-AT-DH-KR-ACP | |MAPSI=KS-AT-DH-KR-ACP | ||
|CDD=KS-AT-DH-ME-KR-PP-Con-EntF | |CDD=KS-AT-DH-ME-KR-PP-Con-EntF | ||
− | |class= | + | |class=PKS-NRPS |
|reliability= | |reliability= | ||
|description=hypothetical protein An08g03790 [Aspergillus niger] | |description=hypothetical protein An08g03790 [Aspergillus niger] | ||
− | |information=Title: strong similarity to lovastatin nonaketide synthase lovB - Aspergillus terreus; Function: like fatty acids-polyketides are assembled by successive decarboxylative condensations of simple precursors.; Function: many polyketides are antibiotics.; Function: polyketide synthases catalyze the assembly of complex natural products from simple precursors such as propionyl-CoA and methylmalonyl-CoA in a biosynthetic process that closely parallels fatty acid biosynthesis.; Function: whereas the intermediates in fatty acid biosynthesis are fully reduced to generate unfunctionalized alkyl chains-the intermediates in polyketide biosynthesis may be only partially processed-giving rise to complex patterns of functional groups.; Remark: polyketide synthases are commercially valuable enzyme.? | + | |information=Possible NRPS-PKS domain structure:KS-AT-CA. Title: strong similarity to lovastatin nonaketide synthase lovB - Aspergillus terreus; Function: like fatty acids-polyketides are assembled by successive decarboxylative condensations of simple precursors.; Function: many polyketides are antibiotics.; Function: polyketide synthases catalyze the assembly of complex natural products from simple precursors such as propionyl-CoA and methylmalonyl-CoA in a biosynthetic process that closely parallels fatty acid biosynthesis.; Function: whereas the intermediates in fatty acid biosynthesis are fully reduced to generate unfunctionalized alkyl chains-the intermediates in polyketide biosynthesis may be only partially processed-giving rise to complex patterns of functional groups.; Remark: polyketide synthases are commercially valuable enzyme.? |
|length=3605 | |length=3605 | ||
+ | |references=\*Pel.+2007$ | ||
}} | }} | ||
{{{{NAMESPACE}}/Footer}} | {{{{NAMESPACE}}/Footer}} |
Latest revision as of 21:19, 16 December 2012
Polyketide Top | Species List | UniRef90 Class | UniRef50 Class | Gene Class | Domains (by CDD) |
Domains (by MAPSI) |
Aspergillus niger CBS 513.88 (GenBank XP_001392496) all species | |||
---|---|---|---|
Class | PKS-NRPS (length: 3605) all classes Class 29.NRPS-PKS_II in KS domain phylogeny | Reliability | |
Product | GeneName | ||
UniProt,UniRef90 | A2QTH2 , - | UniRef50 | - |
Domain by MAPSI | KS-AT-DH-KR-ACP | ||
Domain by CDD | KS-AT-DH-ME-KR-PP-Con-EntF | ||
Domain by ITER-DB | {{{ITERDB}}} | ||
Estimated Domain | |||
Description | hypothetical protein An08g03790 [Aspergillus niger] | ||
Information | Possible NRPS-PKS domain structure:KS-AT-CA. Title: strong similarity to lovastatin nonaketide synthase lovB - Aspergillus terreus; Function: like fatty acids-polyketides are assembled by successive decarboxylative condensations of simple precursors.; Function: many polyketides are antibiotics.; Function: polyketide synthases catalyze the assembly of complex natural products from simple precursors such as propionyl-CoA and methylmalonyl-CoA in a biosynthetic process that closely parallels fatty acid biosynthesis.; Function: whereas the intermediates in fatty acid biosynthesis are fully reduced to generate unfunctionalized alkyl chains-the intermediates in polyketide biosynthesis may be only partially processed-giving rise to complex patterns of functional groups.; Remark: polyketide synthases are commercially valuable enzyme.? | ||
References |
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Link | AspGD |
This work is performed by ShuHsi Lin (TW), Toshitaka Kumagai and Masanori Arita (JP)