Grana_00240 Grana_00240   Grana_00260 Grana_00260

Grana_00250 : CDS information

close this sectionLocation

Organism
StrainTü22
Entry nameGranaticin
Contig
Start / Stop / Direction28,769 / 27,951 / - [in whole cluster]
28,769 / 27,951 / - [in contig]
Locationcomplement(27951..28769) [in whole cluster]
complement(27951..28769) [in contig]
TypeCDS
Length819 bp (272 aa)
Click on the icon to see Genetic map.

close this sectionAnnotation

Category3.3 modification reduction
Productpolyketide C-9 ketoreductase
Product (GenBank)polyketide ketoreductase
Gene
Gene (GenBank)gra-orf5
EC number
Keyword
Note
Note (GenBank)
Reference
ACC
PmId
[2583128] Structure and deduced function of the granaticin-producing polyketide synthase gene cluster of Streptomyces violaceoruber Tu22. (EMBO J. , 1989)
[9831526] The granaticin biosynthetic gene cluster of Streptomyces violaceoruber Tu22: sequence analysis and expression in a heterologous host. (Chem Biol. , 1998)
[1400167] Functional replacement of genes for individual polyketide synthase components in Streptomyces coelicolor A3(2) by heterologous genes from a different polyketide pathway. (J Bacteriol. , 1992)
comment
[PMID: 2583128](1989)
granaticin生合成gene clusterの一部6.5 kb regionの配列解析報告。

予測されたORF5 and ORF6遺伝子産物は知られたoxidoreductaseに似ていることから、granaticin炭素骨格の組み立てのときに必要な還元ステップとして機能すると示唆される。
ORF5 and ORF6は翻訳共役。

--
[PMID: 9831526](1998)
entire granaticin gene cluster(gra cluster)の報告。

ORF5: Keto reductase for C-9 (KR)[PKS]

actIII に似ている。
gra-ORF1-5はact clusterと同じ並び。

--
[PMID: 1400167](1992)
actIII (ORF5)にframeshiftのあるmutant TK18は、graIII-ORF5-6、graIII-ORF5、actIII (ORF5)で相補されるが、graIII-ORF6で相補されない。

actIII (ORF5)に釣られて（？）、この論文ではgra"III"-ORF5とされている。
Related Reference
ACC
P16544
NITE
Actino_00170
PmId
[2394677] Biosynthesis of anthraquinones by interspecies cloning of actinorhodin biosynthesis genes in streptomycetes: clarification of actinorhodin gene functions. (J Bacteriol. , 1990)
[15458634] The crystal structure of the actIII actinorhodin polyketide reductase: proposed mechanism for ACP and polyketide binding. (Structure. , 2004)
[18205400] Inhibition kinetics and emodin cocrystal structure of a type II polyketide ketoreductase. (Biochemistry. , 2008)
[18691223] Localization of the ActIII actinorhodin polyketide ketoreductase to the cell wall. (FEMS Microbiol Lett. , 2008)
comment
Blast 6th, id74%, 1e-103
Streptomyces coelicolor_actIII
Putative ketoacyl reductase
[Actino_00170]C-9 ketoreductase

---
[PMID: 2394677](1990)
anthracyclines 2-hydroxyaklavinoneを産生するStreptomyces galilaeus ATCC 31671にactIII を導入すると、aklavinoneが独占的に形成される。よってActIII がC-9でのketo基の還元することが示される。

---
[PMID:15458634](2004)
activeな4量体のS.coelicolor type II polyketide KR (actIII )とその結合cofactor NADP+との結晶構造を測定。観察結果に基づき、ACP and polyketide bindingのモデルを構築。

---
[PMID:18205400](2008)
ActKRの基質が直線polyketideなのか、環化されたpolyketideなのかを、不安定な自然基質に代わり、安定な基質候補でスクリーニング。
linear or monocyclic ketones, acetoacetyl-CoA or acetoacetyl-ACPで活性見られず。
bicyclic ketoneのtrans-1-decalone, 2-decalone, and alpha-tetraloneに酵素活性あり。

その他の実験結果も総合し、C9位置特異性は、active siteでのthree-point dockingと、基質のC7-C12環形状による二重の制約の結果である。

---
[PMID:18691223](2008)
PKS-KS subunitは細胞膜、ketoreductase_ActIII は細胞壁にある。

close this sectionSequence

selected fasta
>polyketide C-9 ketoreductase [polyketide ketoreductase]
MTTATATATATPGTAAKPVALVTGATSGIGLAIARRLAALGARTFLCARDEERLAQTVKE
LRGEGFDVDGTVCDVADPAQIRAYVAAAVQRYGTVDILVNNAGRSGGGATAEIADELWLD
VITTNLTSVFLMTKEVLNAGGMLAKKRGRIINIASTGGKQGVVHAVPYSASKHGVVGLTK
ALGLELARTGITVNAVCPGFVETPMAERVREHYAGIWQVSEEETFDRITNRVPLGRYVET
REVAAMVEYLVADDAAAVTAQALNVCGGLGNY
selected fasta
>polyketide C-9 ketoreductase [polyketide ketoreductase]
ATGACGACGGCGACAGCGACGGCCACGGCCACCCCCGGCACGGCGGCGAAGCCGGTGGCG
CTGGTGACCGGTGCCACCAGCGGCATCGGGCTTGCGATCGCCCGCCGGCTGGCCGCGCTC
GGCGCGCGCACCTTCCTGTGCGCCCGGGACGAGGAGCGGCTGGCGCAGACGGTGAAGGAG
CTGCGCGGCGAGGGGTTCGACGTCGACGGCACGGTGTGCGACGTGGCGGATCCGGCCCAG
ATCCGCGCCTACGTGGCGGCGGCCGTCCAGCGGTACGGCACGGTCGACATCCTGGTGAAC
AACGCCGGCCGCAGCGGCGGCGGCGCCACCGCCGAAATCGCCGACGAGCTCTGGCTCGAC
GTCATCACCACCAACCTGACCAGCGTCTTCCTCATGACGAAGGAAGTGCTCAACGCGGGC
GGGATGCTCGCCAAGAAGCGTGGGCGGATCATCAACATCGCCTCCACCGGCGGCAAGCAG
GGCGTCGTGCACGCGGTGCCGTACTCGGCGTCCAAGCACGGCGTCGTCGGGCTGACCAAG
GCCCTCGGCCTGGAGCTGGCCCGTACCGGCATCACCGTGAACGCGGTGTGCCCGGGCTTC
GTGGAGACCCCGATGGCCGAGCGGGTGCGCGAGCACTACGCGGGCATCTGGCAGGTCTCC
GAGGAGGAGACGTTCGACCGCATCACCAACCGGGTGCCGCTGGGCCGGTACGTGGAGACC
CGCGAGGTGGCCGCGATGGTCGAGTACCTGGTGGCGGACGACGCGGCGGCGGTCACCGCG
CAGGCGCTGAACGTCTGCGGCGGGCTGGGCAACTACTGA

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09 		show BLAST table
InterPro
Database:interpro:38.0
IPR002198 Short-chain dehydrogenase/reductase SDR (Family)
[93-104] 3.00000067992871e-14 PR00080 [148-156] 3.00000067992871e-14 PR00080 [168-187] 3.00000067992871e-14 PR00080
PR00080   SDRFAMILY
[4-264] 8.49999291746323e-27 PIRSF000126
PIRSF000126   11-beta-HSD1
[19-186] 1.99999999999999e-38 PF00106
PF00106   adh_short
IPR002347 Glucose/ribitol dehydrogenase (Family)
[19-36] 2.99998750445706e-47 PR00081 [93-104] 2.99998750445706e-47 PR00081 [142-158] 2.99998750445706e-47 PR00081 [168-187] 2.99998750445706e-47 PR00081 [189-206] 2.99998750445706e-47 PR00081 [233-253] 2.99998750445706e-47 PR00081
PR00081   GDHRDH
IPR016040 NAD(P)-binding domain (Domain)
[17-269] 6.90000000000007e-81 G3DSA:3.40.50.720
G3DSA:3.40.50.720   NAD(P)-bd
IPR020904 Short-chain dehydrogenase/reductase, conserved site (Conserved_site)
[155-183] PS00061
PS00061   ADH_SHORT
SignalP
[1-34] 0.432 Signal
Bacteria, Gram-positive   
[1-16] 0.88 Signal
Eukaryota   
TMHMM No significant hit
Grana_00240 Grana_00240   Grana_00260 Grana_00260
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