PKS:An13g02430
From Metabolomics.JP
(Difference between revisions)
m (moved PKS:ANig29 to PKS:An13g02430) |
|||
| (2 intermediate revisions by one user not shown) | |||
| Line 5: | Line 5: | ||
|product= | |product= | ||
|GenBank=XP_001396381 | |GenBank=XP_001396381 | ||
| + | |UniProt=- | ||
| + | |UniRef90=- | ||
| + | |UniRef50=- | ||
|geneName= | |geneName= | ||
|MAPSI=KS-AT-DH-ER-KR | |MAPSI=KS-AT-DH-ER-KR | ||
| Line 11: | Line 14: | ||
|reliability= | |reliability= | ||
|description=hypothetical protein An13g02430 [Aspergillus niger] | |description=hypothetical protein An13g02430 [Aspergillus niger] | ||
| − | |information=Title: strong similarity to polyketide synthase PKS1 - Cochliobolus heterostrophus; Remark: PKS1 is a multifunctional polyketide synthase (PKS) with six catalytic domains arranged in the following order-starting at the N terminus: beta-ketoacyl synthase-acyltransferase-dehydratase-enoyl reductase-beta-ketoacyl reductase-and acyl carrier protein.; Remark: PKS1 is involved in production of the virulence factor T-toxin.; Remark: putative part of the lovastatin biosynthesis gene cluster as seen in Aspergillus terreus.; Similarity: shows also strong similarity to polyketide synthases of different organisms.? | + | |information=AT domain is incomplete. Title: strong similarity to polyketide synthase PKS1 - Cochliobolus heterostrophus; Remark: PKS1 is a multifunctional polyketide synthase (PKS) with six catalytic domains arranged in the following order-starting at the N terminus: beta-ketoacyl synthase-acyltransferase-dehydratase-enoyl reductase-beta-ketoacyl reductase-and acyl carrier protein.; Remark: PKS1 is involved in production of the virulence factor T-toxin.; Remark: putative part of the lovastatin biosynthesis gene cluster as seen in Aspergillus terreus.; Similarity: shows also strong similarity to polyketide synthases of different organisms.? |
|length=2269 | |length=2269 | ||
}} | }} | ||
{{{{NAMESPACE}}/Footer}} | {{{{NAMESPACE}}/Footer}} | ||
Latest revision as of 16:16, 23 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_001396381) all species | |||
|---|---|---|---|
| Class | RPKS (length: 2269) all classes Class 36.R-PKS_III in KS domain phylogeny | Reliability | |
| Product | GeneName | ||
| UniProt,UniRef90 | - , - | UniRef50 | - |
| Domain by MAPSI | KS-AT-DH-ER-KR | ||
| Domain by CDD | KS-AT-DH-ER-KR(DltE)-(PP) | ||
| Domain by ITER-DB | {{{ITERDB}}} | ||
| Estimated Domain | |||
| Description | hypothetical protein An13g02430 [Aspergillus niger] | ||
| Information | AT domain is incomplete. Title: strong similarity to polyketide synthase PKS1 - Cochliobolus heterostrophus; Remark: PKS1 is a multifunctional polyketide synthase (PKS) with six catalytic domains arranged in the following order-starting at the N terminus: beta-ketoacyl synthase-acyltransferase-dehydratase-enoyl reductase-beta-ketoacyl reductase-and acyl carrier protein.; Remark: PKS1 is involved in production of the virulence factor T-toxin.; Remark: putative part of the lovastatin biosynthesis gene cluster as seen in Aspergillus terreus.; Similarity: shows also strong similarity to polyketide synthases of different organisms.? | ||
| References | |||
| Link | AspGD | ||
This work is performed by ShuHsi Lin (TW), Toshitaka Kumagai and Masanori Arita (JP)