R1128_00010 R1128_00010   R1128_00030 R1128_00030

R1128_00020 : CDS information

close this sectionLocation

Organism
StrainR1128
Entry nameR1128
Contig
Start / Stop / Direction2,873 / 1,620 / - [in whole cluster]
2,873 / 1,620 / - [in contig]
Locationcomplement(1620..2873) [in whole cluster]
complement(1620..2873) [in contig]
TypeCDS
Length1,254 bp (417 aa)
Click on the icon to see Genetic map.

close this sectionAnnotation

Category1.1 PKS
Productputative polyketide synthase beta-ketoacyl synthase subunit
Product (GenBank)beta-ketoacylsynthase I
Gene
Gene (GenBank)zhuB
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。

zhuB: beta-Ketoacylsynthase I (KS)
機能提唱は配列解析に基づく。
Related Reference
ACC
Q02059
NITE
Actino_00180
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 15th, id73%, 1e-172
Streptomyces coelicolor_SCO5087
Actinorhodin polyketide putative beta-ketoacyl synthase 1(EC 2.3.1.-)
[Actino_00180]polyketide synthase beta-ketoacyl synthase subunit_actI-ORF1

--
[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

KS2..369

close this sectionSequence

selected fasta
>putative polyketide synthase beta-ketoacyl synthase subunit [beta-ketoacylsynthase I]
MITGMGVVAPGGTGTKGFWDLLTSGRTATRRISHFDPSPFRSQVAAECDFDPVLAGFTHR
EIRRLDRASLFAVASARDCAADSGLAFADLDPTRIGVSVGSAVGATTSLEREYLVLSDSG
RDWVVDADYATPHMYDYFTPGAIAAEVAWSVGAEGPATIVSSGCTSGLDSVGYAYQLIVE
GTADIMVTGATDAPISPIAVACFDAIKATTPRNDEPESASRPFDLTRSGFVIGEGAAMFV
LEEYEHAKARGAHIYAEVTGYATRCNAYHMTGLKADGREMADAITYALNESRIDPTAVDY
INAHGSGTKQNDRHETNAFKVALGDHAYDVPVSSIKSMIGHSLGAIGSIEIAASVLAIQH
NVVPPTANLTQSDPECDLDYVPVTAREHRTDTVLSVGSGFGGFQSAMVLRRLQEDAR
selected fasta
>putative polyketide synthase beta-ketoacyl synthase subunit [beta-ketoacylsynthase I]
GTGATCACCGGGATGGGGGTCGTGGCCCCGGGCGGCACCGGAACCAAGGGGTTCTGGGAC
CTGCTCACCTCAGGCCGCACCGCCACCCGGCGCATCTCCCACTTCGACCCGTCGCCGTTC
CGGTCCCAGGTGGCCGCGGAATGCGACTTCGACCCGGTCCTGGCCGGCTTCACGCACCGC
GAGATCCGCCGCCTGGACCGCGCGTCGCTGTTCGCCGTCGCCAGCGCGCGGGACTGCGCC
GCCGACAGCGGACTGGCGTTCGCCGACCTCGACCCGACCCGGATCGGAGTCAGCGTCGGC
AGCGCCGTCGGCGCCACCACGAGCCTCGAACGCGAATACCTCGTGCTCTCCGACTCCGGA
CGCGACTGGGTGGTCGACGCCGACTACGCCACGCCGCACATGTACGACTACTTCACGCCC
GGCGCGATCGCCGCCGAAGTGGCCTGGAGCGTCGGCGCGGAGGGCCCCGCGACCATCGTG
TCCTCCGGCTGCACCTCGGGCCTGGACTCGGTCGGCTACGCCTACCAGCTCATCGTCGAG
GGCACCGCCGACATCATGGTCACCGGCGCCACCGACGCGCCGATCTCGCCGATCGCCGTC
GCGTGCTTCGACGCCATCAAGGCCACCACCCCGCGCAACGACGAACCCGAGTCCGCGTCG
AGGCCGTTCGACCTGACCCGCAGCGGATTCGTGATCGGCGAGGGGGCGGCGATGTTCGTC
CTCGAGGAGTACGAGCACGCCAAGGCGCGCGGCGCGCACATCTACGCCGAGGTCACCGGC
TACGCGACCCGCTGCAACGCGTACCACATGACCGGACTCAAGGCCGACGGACGGGAGATG
GCCGACGCCATCACCTACGCGCTGAACGAATCGCGCATCGACCCGACGGCGGTGGACTAC
ATCAACGCCCACGGGTCCGGGACCAAGCAGAACGACCGGCACGAGACCAACGCGTTCAAG
GTCGCCCTCGGCGACCACGCCTACGACGTCCCGGTCAGCTCCATCAAGTCGATGATCGGG
CACTCGCTCGGCGCGATCGGCTCCATCGAGATCGCCGCCAGCGTCCTCGCGATCCAGCAC
AACGTCGTGCCGCCGACCGCGAACCTGACCCAGTCCGACCCCGAATGCGACCTGGACTAC
GTGCCGGTGACCGCCCGCGAACACCGCACCGACACCGTGCTGTCGGTCGGCAGCGGCTTC
GGTGGCTTCCAGAGCGCGATGGTGCTGCGCCGCCTTCAGGAGGACGCGCGATGA
KS2..369
KS4..1107

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09 		show BLAST table
InterPro
Database:interpro:38.0
IPR014030 Beta-ketoacyl synthase, N-terminal (Domain)
[2-246] 4.6e-55 PF00109
PF00109   ketoacyl-synt
IPR014031 Beta-ketoacyl synthase, C-terminal (Domain)
[255-369] 6.6999999999999e-38 PF02801
PF02801   Ketoacyl-synt_C
IPR016038 Thiolase-like, subgroup (Domain)
[2-260] 6.19999999999994e-62 G3DSA:3.40.47.10 [265-414] 3.29999999999997e-52 G3DSA:3.40.47.10
G3DSA:3.40.47.10   Thiolase-like_subgr
IPR016039 Thiolase-like (Domain)
[1-252] 1.99999636034521e-62 SSF53901 [214-412] 3.49999466863949e-64 SSF53901
SSF53901   Thiolase-like
IPR018201 Beta-ketoacyl synthase, active site (Active_site)
[155-171] PS00606
PS00606   B_KETOACYL_SYNTHASE
SignalP No significant hit
TMHMM No significant hit
R1128_00010 R1128_00010   R1128_00030 R1128_00030
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