Fren_00150 Fren_00150   Fren_00170 Fren_00170

Fren_00160 : CDS information

close this sectionLocation

Organism
StrainAK24158
Entry nameFrenolicin
Contig
Start / Stop / Direction18,015 / 18,830 / + [in whole cluster]
18,015 / 18,830 / + [in contig]
Location18015..18830 [in whole cluster]
18015..18830 [in contig]
TypeCDS
Length816 bp (271 aa)
Click on the icon to see Genetic map.

close this sectionAnnotation

Category3.3 modification reduction
Productputative polyketide C-9 ketoreductase
Product (GenBank)ketoreductase
GenefrnP
fren-ORF5
Gene (GenBank)frnP
EC number
Keyword
Note
Note (GenBank)
  • FrnP; ORF5 of Bibb et al
Reference
ACC
PmId
[8181754] Cloning, sequencing and deduced functions of a cluster of Streptomyces genes probably encoding biosynthesis of the polyketide antibiotic frenolicin. (Gene. , 1994)
comment
frenolicin biosynthesis gene clusterにある6ORFの同定。

ORF5: polyketide beta-ketoreductase

配列解析のみ。
actIII homolog
Related Reference
ACC
Q8VWB5
PmId
[8157619] Nucleotide sequence of the aknA region of the aklavinone biosynthetic gene cluster of Streptomyces galilaeus. (J Bacteriol. , 1994)
comment
Blast 6th, id70%, 1e-92
Streptomyces galilaeus_aknA
AknA

2-hydroxyaklavinone(polyketide C9の位置にOH基が残っているaklavinone)を産生するS. galilaeus ANR-58では、aknAの配列に変更がある。
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 35th, id64%, 3e-84
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
>putative polyketide C-9 ketoreductase [ketoreductase]
MTTAAPHTRPGEAGTTRGPALVTGATRGIGLAVAEALVARGYPVVVCARDAEAVARTVKE
LAAGGARVEGVVADVTDAASVHELVATTVARFGPVEVLVNNAGRSGGGVTAELSESLWDD
VIATNLKSVFLVTREVLTTGGMTGRGRGVVNIASTGGKQGVVFGAPYSASKHGVVGFTKA
LGLELARSGITVNAVCPGYVETPMAAGVRRHYADLWDVTEEDVLARFEAKIPLGRYTRPD
EVAALVDYLVTDAAAAVTAQALNVCGGLGNY
selected fasta
>putative polyketide C-9 ketoreductase [ketoreductase]
ATGACCACAGCAGCTCCGCACACCCGCCCCGGGGAGGCAGGCACCACCCGGGGACCCGCT
CTCGTGACCGGCGCGACCCGGGGCATCGGCCTCGCCGTCGCCGAGGCGCTCGTCGCGCGC
GGCTATCCCGTGGTGGTCTGCGCCCGCGACGCCGAGGCGGTCGCGCGCACCGTCAAGGAG
CTGGCAGCGGGCGGCGCCCGCGTCGAGGGCGTCGTCGCCGACGTCACCGACGCCGCCTCC
GTGCACGAACTCGTCGCCACCACCGTCGCCCGCTTCGGCCCCGTCGAGGTCCTCGTCAAC
AACGCGGGCCGGTCCGGCGGCGGAGTGACCGCCGAACTCAGCGAGTCCCTGTGGGACGAC
GTCATCGCCACCAACCTCAAGAGCGTCTTCCTGGTCACCCGGGAGGTGCTCACCACGGGC
GGGATGACCGGGCGCGGCCGCGGCGTCGTCAACATCGCCTCCACGGGCGGCAAGCAGGGC
GTCGTCTTCGGCGCCCCCTACTCGGCGTCCAAGCACGGCGTCGTCGGCTTCACCAAAGCC
CTCGGCCTCGAACTGGCCCGGAGCGGCATCACCGTCAACGCCGTCTGCCCCGGCTACGTC
GAGACGCCGATGGCCGCCGGAGTGCGCCGCCACTACGCCGACCTGTGGGACGTCACCGAG
GAGGACGTGCTGGCCCGCTTCGAGGCGAAGATCCCGCTCGGCCGGTACACCCGCCCCGAC
GAGGTCGCCGCCCTCGTCGACTACCTGGTCACCGACGCCGCCGCGGCCGTCACCGCCCAG
GCCCTCAACGTGTGCGGCGGACTGGGGAACTACTGA

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09 		show BLAST table
InterPro
Database:interpro:38.0
IPR002198 Short-chain dehydrogenase/reductase SDR (Family)
[20-185] 2.29999999999998e-34 PF00106
PF00106   adh_short
[93-104] 2.09999806691534e-11 PR00080 [147-155] 2.09999806691534e-11 PR00080 [167-186] 2.09999806691534e-11 PR00080
PR00080   SDRFAMILY
[1-269] 3.0999994589937e-15 PIRSF000126
PIRSF000126   11-beta-HSD1
IPR002347 Glucose/ribitol dehydrogenase (Family)
[19-36] 2.9000035467798e-41 PR00081 [93-104] 2.9000035467798e-41 PR00081 [141-157] 2.9000035467798e-41 PR00081 [167-186] 2.9000035467798e-41 PR00081 [188-205] 2.9000035467798e-41 PR00081 [232-252] 2.9000035467798e-41 PR00081
PR00081   GDHRDH
IPR016040 NAD(P)-binding domain (Domain)
[20-268] 1.60000000000002e-76 G3DSA:3.40.50.720
G3DSA:3.40.50.720   NAD(P)-bd
IPR020904 Short-chain dehydrogenase/reductase, conserved site (Conserved_site)
[154-182] PS00061
PS00061   ADH_SHORT
SignalP No significant hit
TMHMM No significant hit
Fren_00150 Fren_00150   Fren_00170 Fren_00170
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