PKS:An11g06460
From Metabolomics.JP
(Difference between revisions)
| Line 11: | Line 11: | ||
|MAPSI=KS-AT-DH-KR-ACP | |MAPSI=KS-AT-DH-KR-ACP | ||
|CDD=KS-AT-DH-KR-PP-Con-AMP(LuxE)-(PP)-KR | |CDD=KS-AT-DH-KR-PP-Con-AMP(LuxE)-(PP)-KR | ||
| − | |class= | + | |class=NRPS-PKS |
|reliability= | |reliability= | ||
|description=hypothetical protein An11g06460 [Aspergillus niger] | |description=hypothetical protein An11g06460 [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: in A. terreus the genes involved in lovastatin biosynthesis are clustered; the structure of this cluster in A. terreus is very similar to what observed for the predicted ORFs cmln. 00. tfa_70cg-80wg and 90cg.; Remark: polyketide synthases are commercially valuable enzyme.; (2.3.1.-) | + | |information=Possible NRPS-PKS domain structure: KS-AT-DH-CAP.(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: in A. terreus the genes involved in lovastatin biosynthesis are clustered; the structure of this cluster in A. terreus is very similar to what observed for the predicted ORFs cmln. 00. tfa_70cg-80wg and 90cg.; Remark: polyketide synthases are commercially valuable enzyme.; (2.3.1.-)) |
|length=3897 | |length=3897 | ||
| + | |references=\*Pel.+2007$ | ||
}} | }} | ||
{{{{NAMESPACE}}/Footer}} | {{{{NAMESPACE}}/Footer}} | ||
Revision as of 02:18, 10 April 2012
| Polyketide Top | Species List | UniRef90 Class | UniRef50 Class | Gene Class | Domains (by CDD) |
Domains (by MAPSI) |
| Aspergillus niger CBS 513.88 (GenBank XP_001394625) all species | |||
|---|---|---|---|
| Class | NRPS-PKS (length: 3897) all classes Class 33.NRPS-PKS_V in KS domain phylogeny | Reliability | |
| Product | GeneName | ||
| UniProt,UniRef90 | - , - | UniRef50 | - |
| Domain by MAPSI | KS-AT-DH-KR-ACP | ||
| Domain by CDD | KS-AT-DH-KR-PP-Con-AMP(LuxE)-(PP)-KR | ||
| Domain by ITER-DB | {{{ITERDB}}} | ||
| Estimated Domain | |||
| Description | hypothetical protein An11g06460 [Aspergillus niger] | ||
| Information | Possible NRPS-PKS domain structure: KS-AT-DH-CAP.(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: in A. terreus the genes involved in lovastatin biosynthesis are clustered; the structure of this cluster in A. terreus is very similar to what observed for the predicted ORFs cmln. 00. tfa_70cg-80wg and 90cg.; Remark: polyketide synthases are commercially valuable enzyme.; (2.3.1.-)) | ||
| References |
| ||
| Link | AspGD | ||
This work is performed by ShuHsi Lin (TW), Toshitaka Kumagai and Masanori Arita (JP)
