Actino_00180 Actino_00180   Actino_00200 Actino_00200

Actino_00190 : CDS information

close this sectionLocation

Organism
StrainA3(2) (=NBRC 15146)
Entry nameActinorhodin
Contig
Start / Stop / Direction19,383 / 20,606 / + [in whole cluster]
1,378 / 2,601 / + [in contig]
Location19383..20606 [in whole cluster]
1378..2601 [in contig]
TypeCDS
Length1,224 bp (407 aa)
Click on the icon to see Genetic map.

close this sectionAnnotation

Category1.1 PKS
Productpolyketide synthase chain length factor subunit
Product (GenBank)
GeneactI-ORF2
Gene (GenBank)actIORF2
EC number
Keyword
  • type II PKS
Note
Note (GenBank)
Reference
ACC
PmId
[1527048] Nucleotide sequence and deduced functions of a set of cotranscribed genes of Streptomyces coelicolor A3(2) including the polyketide synthase for the antibiotic actinorhodin. (J Biol Chem. , 1992)
[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
[PMID: 1527048](1992)
actinorhodin biosynthetic gene clusterのactI領域の配列解析。

actI-ORF2はactinorhodin生合成minimal PKSのCLF subunitをコードする。
1×acetate starter unit + 7×malonyl extender unitsを縮合してactinorhodin半分子のoctaketide骨格を形成すると提唱。

--
[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

CLF2..360

close this sectionSequence

selected fasta
>polyketide synthase chain length factor subunit
MSVLITGVGVVAPNGLGLAPYWSAVLDGRHGLGPVTRFDVSRYPATLAGQIDDFHAPDHI
PGRLLPQTDPSTRLALTAADWALQDAKADPESLTDYDMGVVTANACGGFDFTHREFRKLW
SEGPKSVSVYESFAWFYAVNTGQISIRHGMRGPSSALVAEQAGGLDALGHARRTIRRGTP
LVVSGGVDSALDPWGWVSQIASGRISTATDPDRAYLPFDERAAGYVPGEGGAILVLEDSA
AAEARGRHDAYGELAGCASTFDPAPGSGRPAGLERAIRLALNDAGTGPEDVDVVFADGAG
VPELDAAEARAIGRVFGREGVPVTVPKTTTGRLYSGGGPLDVVTALMSLREGVIAPTAGV
TSVPREYGIDLVLGEPRSTAPRTALVLARGRWGFNSAAVLRRFAPTP
selected fasta
>polyketide synthase chain length factor subunit
ATGAGCGTCCTCATCACCGGAGTCGGCGTCGTCGCACCCAACGGCCTCGGCCTGGCGCCG
TACTGGTCGGCGGTGCTGGACGGCCGCCACGGCCTCGGCCCGGTCACCCGCTTCGACGTG
AGCCGGTACCCGGCGACCCTCGCCGGCCAGATCGACGACTTCCACGCGCCGGACCACATC
CCGGGCCGGTTGCTGCCGCAGACGGACCCCTCCACACGGCTCGCGCTGACCGCCGCGGAC
TGGGCCCTCCAGGACGCGAAGGCGGACCCGGAGTCGCTGACCGACTACGACATGGGCGTG
GTGACCGCCAACGCCTGCGGTGGGTTCGACTTCACCCACCGGGAGTTCCGCAAGCTGTGG
TCCGAGGGCCCCAAGTCGGTCAGCGTGTACGAGTCCTTCGCCTGGTTCTACGCGGTGAAC
ACCGGCCAGATCTCCATCCGGCACGGTATGCGCGGTCCGAGCAGTGCCCTGGTCGCCGAG
CAGGCCGGGGGCCTGGACGCCCTGGGCCACGCCCGCCGTACGATCCGCCGCGGCACGCCG
CTGGTGGTCTCCGGCGGGGTGGACTCGGCACTCGACCCGTGGGGCTGGGTCTCGCAGATC
GCCAGTGGCCGGATCAGCACGGCCACCGATCCGGACCGGGCGTATCTGCCCTTCGACGAG
CGGGCGGCCGGCTACGTTCCGGGCGAGGGCGGGGCCATCCTCGTCCTGGAGGACAGCGCC
GCGGCCGAGGCCCGCGGCCGGCACGACGCGTACGGCGAACTCGCCGGCTGCGCCTCCACC
TTCGACCCCGCCCCCGGATCCGGACGGCCCGCGGGCCTGGAACGCGCGATCCGGCTGGCG
CTGAACGACGCCGGGACCGGTCCCGAGGACGTCGACGTCGTGTTCGCCGACGGCGCGGGC
GTGCCCGAGCTGGACGCCGCCGAGGCCCGGGCGATCGGCCGGGTGTTCGGCCGCGAAGGG
GTGCCCGTCACCGTCCCCAAGACGACGACGGGCCGCCTCTACTCCGGCGGCGGCCCGCTC
GACGTGGTCACCGCCCTGATGTCCCTGCGCGAAGGGGTGATCGCGCCGACCGCGGGCGTG
ACGTCCGTACCCCGGGAGTACGGCATCGACCTGGTGCTCGGCGAACCCCGCAGCACGGCC
CCGCGCACCGCACTGGTCCTGGCCAGGGGCCGCTGGGGCTTCAACTCGGCGGCGGTCCTG
CGCCGTTTCGCACCGACCCCGTAA
CLF2..360
CLF4..1080

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09 		show BLAST table
InterPro
Database:interpro:38.0
IPR014030 Beta-ketoacyl synthase, N-terminal (Domain)
[2-241] 1.80000000000002e-55 PF00109
PF00109   ketoacyl-synt
IPR014031 Beta-ketoacyl synthase, C-terminal (Domain)
[251-360] 2.7e-25 PF02801
PF02801   Ketoacyl-synt_C
IPR016038 Thiolase-like, subgroup (Domain)
[2-255] 2.50000000000001e-56 G3DSA:3.40.47.10 [268-404] 2.29999999999998e-38 G3DSA:3.40.47.10
G3DSA:3.40.47.10   Thiolase-like_subgr
IPR016039 Thiolase-like (Domain)
[2-247] 9.80000272130214e-61 SSF53901 [210-403] 5.50001754266469e-49 SSF53901
SSF53901   Thiolase-like
SignalP
[1-17] 0.631 Signal
Eukaryota   
TMHMM No significant hit
Actino_00180 Actino_00180   Actino_00200 Actino_00200
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