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Chart_00240 : CDS information

close this sectionLocation

Organism
StrainHKI-249
Entry nameChartreusin
Contig
Start / Stop / Direction21,796 / 22,581 / + [in whole cluster]
2,216 / 3,001 / + [in contig]
Location21796..22581 [in whole cluster]
2216..3001 [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)ChaZ protein
GenechaE
Gene (GenBank)chaZ
EC number
Keyword
Note
Note (GenBank)
Reference
ACC
PmId
[15911378] Biosynthesis of the antitumor agent chartreusin involves the oxidative rearrangement of an anthracyclic polyketide. (Chem Biol. , 2005)
comment
UniProtの登録はChaZだが論文内容を確認すると、このORFはChaEに相当。

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[PMID: 15911378](2005)
chartreusin生合成clusterの解析論文。
異種性にclusterを発現してchartreusin産生を確認。

ChaE: C-9 Keto reductase

配列解析に基づき、機能予測している。
AknAのようなC-9 ketoreductasesに似ている。
cha cluster内にhomolog ChaDあり。
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 26th, id60%, 3e-75
Streptomyces violaceoruber_gra-orf5
Granaticin polyketide synthase putative ketoacyl reductase 1

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 14th, id56%, 2e-77
Streptomyces coelicolor_actIII
Putative ketoacyl reductase

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[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 [ChaZ protein]
MTDNIERTAIVTGASNGIGRAIAATLAAEGVRVHICGRDAETVEKTVTELRADRGQVSGQ
ACDVTKPDQVTALVADCVARYGPVDILVNNAGRPGGGITANIDNELWYATIDTNLNGVFL
MSKSVLNEGRMTERQNGRIINIASVWGKQGTIGGAPYAAAKHGVIGFSRCLALELAKTGI
TVNAVCPGYVETPMSVNVRACQAGIWQVDEEEALRRLASDIPIGRYSEPEEVAWMVSYLA
SSKAASVTGQALNVCGGFGVH
selected fasta
>putative polyketide C-9 ketoreductase [ChaZ protein]
ATGACGGACAACATTGAGCGGACAGCCATCGTCACCGGCGCGAGCAATGGGATCGGCCGG
GCGATCGCCGCCACACTGGCGGCGGAAGGCGTACGCGTACATATCTGCGGCAGGGACGCC
GAAACCGTCGAGAAGACGGTGACCGAACTGCGGGCGGACAGAGGCCAGGTCAGTGGCCAG
GCGTGCGACGTCACCAAGCCCGACCAGGTGACCGCGTTGGTGGCGGACTGCGTCGCACGG
TACGGACCGGTGGACATCCTGGTGAACAACGCCGGCCGGCCCGGCGGAGGAATCACCGCG
AACATCGACAACGAATTGTGGTACGCCACCATCGACACCAATCTCAACGGTGTTTTCCTG
ATGTCCAAATCCGTGCTGAACGAAGGGCGCATGACGGAGCGGCAGAACGGCCGCATCATC
AACATCGCCTCGGTGTGGGGAAAACAGGGAACGATCGGAGGCGCGCCCTACGCGGCCGCC
AAACACGGCGTCATCGGATTCAGCCGCTGCCTCGCGCTGGAACTCGCGAAGACCGGGATC
ACGGTCAATGCTGTGTGCCCCGGATATGTCGAGACCCCGATGTCGGTCAACGTACGCGCC
TGCCAGGCGGGCATCTGGCAGGTGGACGAGGAGGAGGCCCTGCGCCGCCTGGCCTCCGAC
ATCCCCATCGGCCGGTACAGCGAGCCGGAGGAGGTCGCCTGGATGGTCTCCTACCTCGCC
TCGTCCAAGGCCGCCTCGGTCACCGGCCAGGCGCTCAACGTGTGCGGCGGCTTCGGTGTC
CACTGA

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] 2.49999811956465e-14 PR00080 [137-145] 2.49999811956465e-14 PR00080 [157-176] 2.49999811956465e-14 PR00080
PR00080   SDRFAMILY
[1-247] 7.99999145876753e-17 PIRSF000126
PIRSF000126   11-beta-HSD1
[8-175] 2.50000000000001e-39 PF00106
PF00106   adh_short
IPR002347 Glucose/ribitol dehydrogenase (Family)
[8-25] 4.10001399699315e-48 PR00081 [82-93] 4.10001399699315e-48 PR00081 [131-147] 4.10001399699315e-48 PR00081 [157-176] 4.10001399699315e-48 PR00081 [178-195] 4.10001399699315e-48 PR00081 [222-242] 4.10001399699315e-48 PR00081
PR00081   GDHRDH
IPR016040 NAD(P)-binding domain (Domain)
[6-258] 1.20000000000001e-85 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
[1-23] 0.216 Signal
Bacteria, Gram-negative   
[1-23] 0.343 Signal
Bacteria, Gram-positive   
[1-23] 0.079 Signal
Eukaryota   
TMHMM No significant hit
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