first first   R1128_00020 R1128_00020

R1128_00010 : CDS information

close this sectionLocation

Organism
StrainR1128
Entry nameR1128
Contig
Start / Stop / Direction1,623 / 376 / - [in whole cluster]
1,623 / 376 / - [in contig]
Locationcomplement(376..1623) [in whole cluster]
complement(376..1623) [in contig]
TypeCDS
Length1,248 bp (415 aa)
Click on the icon to see Genetic map.

close this sectionAnnotation

Category1.1 PKS
Productputative polyketide synthase chain length factor subunit
Product (GenBank)chain length factor
Gene
Gene (GenBank)zhuA
EC number
Keyword
  • type II PKS
Note
Note (GenBank)
Reference
ACC
PmId
[10931852] Cloning, nucleotide sequence, and heterologous expression of the biosynthetic gene cluster for R1128, a non-steroidal estrogen receptor antagonist. Insights into an unusual priming mechanism. (J Biol Chem. , 2000)
comment
R1128 gene clusterがあると予測されるStreptomyces sp. R1128の40kb領域をS.lividans K4-114で異種性発現し、産物としてR1128Cと新規産物HU235を検出。
この領域をシークエンスして、生合成genesがすべて含まれていそうな17kb領域をサブクローニング、oligonucleotide walkingして正確な配列を得た。

zhuA: Chain length factor (CLF)
機能提唱は配列解析に基づく。
Related Reference
ACC
Q02062
NITE
Actino_00190
PmId
[10519556] A chain initiation factor common to both modular and aromatic polyketide synthases. (Nature. , 1999)
[10684659] Mechanistic analysis of a type II polyketide synthase. Role of conserved residues in the beta-ketoacyl synthase-chain length factor heterodimer. (Biochemistry. , 2000)
[15286722] An antibiotic factory caught in action. (Nat Struct Mol Biol. , 2004)
[18034463] Dissecting the component reactions catalyzed by the actinorhodin minimal polyketide synthase. (Biochemistry. , 2007)
comment
Blast 3rd, id66%, 1e-145
Streptomyces coelicolor_SCO5088
[Actino_00190]polyketide synthase chain length factor subunit_actI-ORF2

--
[PMID: 10519556](1999)
これまでの実験で、minimal PKSとmalonyl-CoAのインキュベートで予測されたpolyketideが産生されていることから、acetyl-CoAではなく、malonyl-CoAがstarter unitsの前駆体である。

act CLFは、malonyl-ACPをdecarboxylationしてacetyl-ACP starterを形成することに関連する。
type II PKSのCLFと、type I modular PKSのKSQ domainは共にKS domain active siteのCys→Glnへの置換があり、このGln残基がdecarboxylase活性とpolyketide合成の両方のために重要である。

--
[PMID: 10684659](2000) abstract
mutantを用いたactinorhodin KS-CLFの調査。

malonyl-ACP単独で、wild-type KS-CLFによる動力学的・化学量論的に効率的なpolyketide合成をするのに十分である。

KSにpoint mutationのある株でのmalonyl-ACP decarboxylation能力、
[(14)C]malonyl-ACP → nucleophileへのラベル移動を確認している模様。

--
[PMID: 15286722](2004) abstract
actinorhodin KS-CLFの構造解析。

--
[PMID: 18034463](2007) abstract
kinetic assaysあり。

close this sectionPKS/NRPS Module

CLF9..368

close this sectionSequence

selected fasta
>putative polyketide synthase chain length factor subunit [chain length factor]
MTQAAPTTRRAVVTGLGAVAPNGFGTEEYWKATLRGRSGIHPLHRYDASGFPSRLAGQIL
GFEAEQHIPGRLLPQTDRVTRLALVAGQSALDDAGVDPQALVDYSMGVVTSSAIGGFEFT
HGEVHKLWTKGPQHVSVYESFAWFYAVNTGQLSIRHGMRGPSGVLVGEQAGGLDAIGHAR
RNLRRGIDLVVTGGCDSALDPWGYVSHLTTGRISRATEPELAYRPFDAAADGYVPGEGGA
ILVLEDERAARARGAATLYGEIAGYAATFDPPPGSERPPGLARAARLALDDAGVRPEDVD
AVFADAAGVPDLDRAEAEAINEVFGAGAVPVTAPKSLVGRLNSGGPPLDVVAALLSIRDD
VVPPTPNTTDVPADYGLDLVLSEPRNARVRTVLVLARGHGGFNAAVVVRAMNPEL
selected fasta
>putative polyketide synthase chain length factor subunit [chain length factor]
ATGACCCAGGCAGCCCCCACGACGCGGCGCGCCGTCGTCACCGGCCTCGGCGCCGTTGCC
CCCAACGGCTTCGGCACCGAGGAGTACTGGAAGGCCACGCTGCGCGGACGCTCCGGCATC
CACCCGCTGCACCGCTACGACGCGTCCGGATTCCCGTCCCGACTCGCCGGCCAGATACTC
GGCTTCGAGGCCGAACAGCACATTCCGGGAAGGCTGTTGCCGCAGACCGACCGCGTCACG
CGACTCGCCCTCGTCGCCGGCCAGAGCGCGCTCGACGACGCCGGCGTCGACCCGCAGGCA
CTCGTCGACTACTCGATGGGCGTCGTCACCTCCAGCGCCATCGGCGGCTTCGAGTTCACC
CACGGCGAGGTACACAAGCTCTGGACCAAGGGACCGCAACACGTCAGCGTCTACGAGTCG
TTCGCGTGGTTCTACGCCGTCAACACCGGCCAGTTGTCCATCCGGCACGGCATGCGCGGG
CCCAGCGGCGTCCTGGTCGGCGAACAAGCCGGCGGCCTCGACGCCATCGGCCACGCGCGC
CGCAACCTGCGGCGCGGCATCGACCTCGTGGTCACCGGCGGATGCGACTCGGCGCTCGAC
CCGTGGGGATACGTCAGCCACCTGACCACCGGACGGATCTCCCGCGCGACCGAACCCGAG
CTGGCCTACCGGCCGTTCGACGCGGCCGCCGACGGCTACGTGCCGGGGGAGGGCGGGGCC
ATCCTCGTCCTGGAGGACGAACGCGCCGCCCGGGCCCGGGGCGCGGCCACGCTCTACGGC
GAGATCGCAGGCTACGCGGCCACCTTCGACCCGCCGCCCGGCTCCGAACGGCCGCCGGGG
CTGGCCCGCGCGGCCCGCCTCGCGCTCGACGACGCGGGCGTGCGGCCCGAGGACGTGGAC
GCGGTGTTCGCGGACGCGGCCGGCGTACCGGACCTGGACCGCGCCGAAGCCGAGGCGATC
AACGAGGTGTTCGGGGCCGGCGCGGTGCCGGTGACGGCGCCCAAGAGCCTGGTGGGACGC
CTCAACTCGGGCGGGCCGCCGCTCGACGTGGTGGCCGCGCTGTTGTCGATCCGCGACGAC
GTCGTCCCGCCGACGCCCAACACCACCGACGTGCCGGCCGACTACGGGCTCGACCTCGTG
CTGTCCGAACCGCGCAACGCGCGCGTGCGGACGGTGCTGGTGCTGGCCCGCGGCCACGGC
GGGTTCAACGCGGCCGTCGTGGTCCGCGCGATGAACCCCGAACTGTAG
CLF9..368
CLF25..1104

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09 		show BLAST table
InterPro
Database:interpro:38.0
IPR014030 Beta-ketoacyl synthase, N-terminal (Domain)
[9-249] 8.00000000000001e-55 PF00109
PF00109   ketoacyl-synt
IPR014031 Beta-ketoacyl synthase, C-terminal (Domain)
[259-368] 7.79999999999999e-25 PF02801
PF02801   Ketoacyl-synt_C
IPR016038 Thiolase-like, subgroup (Domain)
[7-264] 1.40000000000001e-56 G3DSA:3.40.47.10 [275-413] 2.1e-38 G3DSA:3.40.47.10
G3DSA:3.40.47.10   Thiolase-like_subgr
IPR016039 Thiolase-like (Domain)
[8-255] 8.19994104549873e-65 SSF53901 [218-411] 1e-49 SSF53901
SSF53901   Thiolase-like
SignalP
[1-11] 0.45 Signal
Bacteria, Gram-negative   
[1-25] 0.528 Signal
Eukaryota   
TMHMM No significant hit
first first   R1128_00020 R1128_00020
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