Medem_00290 Medem_00290   Medem_00310 Medem_00310

Medem_00300 : CDS information

close this sectionLocation

Organism
StrainAM-7161
Entry nameMedermycin
Contig
Start / Stop / Direction28,556 / 29,341 / + [in whole cluster]
28,556 / 29,341 / + [in contig]
Location28556..29341 [in whole cluster]
28556..29341 [in contig]
TypeCDS
Length786 bp (261 aa)
Click on the icon to see Genetic map.

close this sectionAnnotation

Category3.3 modification reduction
Productputative polyketide C-9 ketoreductase
Product (GenBank)keto reductase (KR)
Gene
Gene (GenBank)med-ORF6
EC number
Keyword
Note
Note (GenBank)
Reference
ACC
PmId
[12855716] Cloning, sequencing and heterologous expression of the medermycin biosynthetic gene cluster of Streptomyces sp. AM-7161: towards comparative analysis of the benzoisochromanequinone gene clusters. (Microbiology. , 2003)
comment
entire medermycin(med) biosynthetic gene clusterの報告。
Streptomyces coelicolor CH999でmed clusterを発現してmedermycin産生を確認している。

ORF6: keto reductase(KR)

配列解析のみ。actIII homologue.
Fig.3の提唱生合成経路で、C7-C12で1st ring形成された後のC-9 keto基還元が割り当てられている。
Related Reference
ACC
P16542
NITE
Grana_00250
PmId
[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
Blast 4th, id75%, 1e-102
Streptomyces violaceoruber_gra-orf5
Granaticin polyketide synthase putative ketoacyl reductase 1
[Grana_00250]C-9 ketoreductase

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。
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 5th, id69%, 2e-99
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 [keto reductase (KR)]
MTQANGRVAVVTGATSGIGWEIAVRLAETGHRVYLCARSADRLAEAVKQLQDRGFDADGS
TCDVADPAQVTAFVTAAVARYGPIDVLVNNAGRSGGGITADVTDELWLDVVNTNLNSVFR
MTKAVLTVGGMQGKKRGRIVNIASTGGKQGVLHGAPYSASKHGVVGLTKAWGLELAKTGI
TVNAVCPGFVETPMAEKVRTHYAGIWGTTEEEAFERVTARVPIGRYVEPSEVAAMVDYLV
GDGAAAVTAQALNVCGGLGNY
selected fasta
>putative polyketide C-9 ketoreductase [keto reductase (KR)]
ATGACTCAGGCGAACGGCCGTGTGGCCGTGGTCACCGGCGCGACCAGCGGCATCGGATGG
GAGATCGCCGTCCGCCTGGCCGAGACCGGCCACCGGGTCTACCTCTGCGCGCGGTCGGCG
GACCGGCTGGCCGAGGCCGTCAAGCAGCTCCAGGACCGCGGCTTCGACGCCGACGGCAGC
ACCTGCGACGTCGCCGACCCCGCCCAGGTCACGGCCTTCGTCACGGCCGCCGTCGCCCGC
TACGGCCCCATCGACGTCCTGGTCAACAACGCCGGCCGCAGCGGCGGCGGCATCACCGCC
GACGTCACCGACGAGCTCTGGCTCGACGTCGTCAACACCAACCTCAACAGCGTCTTCCGG
ATGACGAAGGCGGTCCTCACCGTCGGCGGCATGCAGGGGAAGAAGCGCGGCCGCATCGTC
AACATCGCCTCCACCGGCGGCAAGCAGGGCGTCCTGCACGGCGCCCCCTACTCGGCCTCC
AAGCACGGCGTCGTCGGCCTGACGAAGGCCTGGGGCCTGGAGCTCGCCAAGACCGGCATC
ACCGTCAACGCCGTCTGCCCCGGCTTCGTCGAGACCCCCATGGCGGAGAAGGTCCGCACC
CACTACGCCGGGATCTGGGGGACCACGGAGGAGGAGGCCTTCGAGCGCGTCACCGCCCGG
GTGCCGATCGGCCGGTACGTCGAGCCCTCCGAGGTCGCCGCCATGGTCGATTACCTCGTC
GGCGACGGAGCCGCCGCGGTCACCGCCCAGGCCCTCAACGTCTGCGGCGGCCTCGGCAAC
TACTGA

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09 		show BLAST table
InterPro
Database:interpro:38.0
IPR002198 Short-chain dehydrogenase/reductase SDR (Family)
[82-93] 7.99999145876753e-13 PR00080 [137-145] 7.99999145876753e-13 PR00080 [157-176] 7.99999145876753e-13 PR00080
PR00080   SDRFAMILY
[1-259] 7.79998304125571e-17 PIRSF000126
PIRSF000126   11-beta-HSD1
[8-175] 4.2e-38 PF00106
PF00106   adh_short
IPR002347 Glucose/ribitol dehydrogenase (Family)
[8-25] 1.40000506907309e-44 PR00081 [82-93] 1.40000506907309e-44 PR00081 [131-147] 1.40000506907309e-44 PR00081 [157-176] 1.40000506907309e-44 PR00081 [178-195] 1.40000506907309e-44 PR00081 [222-242] 1.40000506907309e-44 PR00081
PR00081   GDHRDH
IPR016040 NAD(P)-binding domain (Domain)
[3-258] 1.20000000000001e-81 G3DSA:3.40.50.720
G3DSA:3.40.50.720   NAD(P)-bd
IPR020904 Short-chain dehydrogenase/reductase, conserved site (Conserved_site)
[144-172] PS00061
PS00061   ADH_SHORT
SignalP No significant hit
TMHMM No significant hit
Medem_00290 Medem_00290   Medem_00310 Medem_00310
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