Actino_00170 Actino_00170   Actino_00190 Actino_00190

Actino_00180 : CDS information

close this sectionLocation

Organism
StrainA3(2) (=NBRC 15146)
Entry nameActinorhodin
Contig
Start / Stop / Direction18,112 / 19,386 / + [in whole cluster]
107 / 1,381 / + [in contig]
Location18112..19386 [in whole cluster]
107..1381 [in contig]
TypeCDS
Length1,275 bp (424 aa)
Click on the icon to see Genetic map.

close this sectionAnnotation

Category1.1 PKS
Productpolyketide synthase beta-ketoacyl synthase subunit
Product (GenBank)Beta-Ketoacyl synthase/Acyl transferase
GeneactI-ORF1
Gene (GenBank)actIORF1
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-ORF1はactinorhodin生合成minimal PKSのKS 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

KS3..374

close this sectionSequence

selected fasta
>polyketide synthase beta-ketoacyl synthase subunit [Beta-Ketoacyl synthase/Acyl transferase]
MKRRVVITGVGVRAPGGNGTRQFWELLTSGRTATRRISFFDPSPYRSQVAAEADFDPVAE
GFGPRELDRMDRASQFAVACAREAFAASGLDPDTLDPARVGVSLGSAVAAATSLEREYLL
LSDSGRDWEVDAAWLSRHMFDYLVPSVMPAEVAWAVGAEGPVTMVSTGCTSGLDSVGNAV
RAIEEGSADVMFAGAADTPITPIVVACFDAIRATTARNDDPEHASRPFDGTRDGFVLAEG
AAMFVLEDYDSALARGARIHAEISGYATRCNAYHMTGLKADGREMAETIRVALDESRTDA
TDIDYINAHGSGTRQNDRHETAAYKRALGEHARRTPVSSIKSMVGHSLGAIGSLEIAACV
LALEHGVVPPTANLRTSDPECDLDYVPLEARERKLRSVLTVGSGFGGFQSAMVLRDAETA
GAAA
selected fasta
>polyketide synthase beta-ketoacyl synthase subunit [Beta-Ketoacyl synthase/Acyl transferase]
TTGAAGCGCAGAGTCGTCATCACGGGCGTCGGCGTCCGCGCCCCCGGCGGGAACGGCACC
CGGCAGTTCTGGGAACTGCTCACCTCGGGGCGGACGGCGACGCGCCGGATCTCGTTCTTC
GACCCCTCGCCCTACCGTTCACAGGTCGCGGCGGAGGCCGACTTCGACCCGGTCGCCGAG
GGCTTCGGCCCGCGGGAGCTCGACCGGATGGACCGGGCCTCGCAGTTCGCCGTGGCCTGT
GCCCGGGAGGCGTTCGCCGCCAGCGGGCTCGACCCGGACACCCTCGACCCCGCCCGGGTC
GGGGTCAGCCTCGGCAGCGCGGTGGCAGCGGCGACCAGCCTGGAGCGCGAGTATCTGCTG
CTGTCGGACTCCGGCCGTGACTGGGAGGTCGACGCGGCCTGGCTGTCCCGGCACATGTTC
GACTACCTGGTGCCCAGCGTCATGCCGGCCGAGGTCGCCTGGGCGGTCGGCGCCGAGGGC
CCGGTCACGATGGTCTCCACCGGCTGCACCTCGGGCCTGGACTCCGTCGGCAACGCGGTC
CGGGCGATCGAGGAGGGCAGCGCCGACGTGATGTTCGCGGGAGCCGCCGACACCCCGATC
ACCCCGATCGTCGTCGCCTGCTTCGACGCGATCCGCGCCACGACGGCGCGCAACGACGAC
CCGGAGCACGCCTCGCGGCCGTTCGACGGTACGCGGGACGGCTTCGTGCTGGCCGAAGGA
GCCGCGATGTTCGTCCTGGAGGACTACGACAGCGCGCTGGCCCGCGGAGCCCGCATCCAC
GCCGAGATCTCGGGGTACGCGACGCGCTGCAACGCGTACCACATGACGGGCCTGAAGGCC
GACGGCCGCGAGATGGCCGAGACCATCCGGGTCGCCCTCGACGAGTCCCGCACGGACGCG
ACGGACATCGACTACATCAACGCGCACGGCTCCGGCACCCGGCAGAACGACCGCCACGAG
ACAGCGGCGTACAAGCGCGCCCTCGGCGAACACGCCCGGCGCACTCCGGTCAGCTCGATC
AAGTCGATGGTCGGCCACTCGCTGGGCGCGATCGGCTCGCTGGAGATCGCGGCCTGCGTA
CTCGCCCTCGAACACGGCGTGGTGCCCCCGACCGCCAACCTGCGCACCAGCGACCCCGAG
TGCGATCTCGACTACGTTCCGCTGGAGGCCAGGGAGCGGAAGCTGCGGTCCGTACTCACC
GTGGGCAGCGGCTTCGGCGGCTTCCAGAGCGCGATGGTGCTGCGCGACGCCGAGACCGCG
GGGGCGGCCGCATGA
KS3..374
KS7..1122

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09 		show BLAST table
InterPro
Database:interpro:38.0
IPR014030 Beta-ketoacyl synthase, N-terminal (Domain)
[3-248] 1.7e-62 PF00109
PF00109   ketoacyl-synt
IPR014031 Beta-ketoacyl synthase, C-terminal (Domain)
[260-374] 9.6e-38 PF02801
PF02801   Ketoacyl-synt_C
IPR016038 Thiolase-like, subgroup (Domain)
[2-265] 6.2e-64 G3DSA:3.40.47.10 [270-418] 6.2e-51 G3DSA:3.40.47.10
G3DSA:3.40.47.10   no description
IPR016039 Thiolase-like (Domain)
[2-419] 4.2e-69 SSF53901
SSF53901   Thiolase-like
IPR018201 Beta-ketoacyl synthase, active site (Active_site)
[160-176] PS00606
PS00606   B_KETOACYL_SYNTHASE
IPR020841 Polyketide synthase, beta-ketoacyl synthase domain (Domain)
[5-419] 2.2e-14 SM00825
SM00825   Beta-ketoacyl synthase
SignalP No significant hit
TMHMM No significant hit
Actino_00170 Actino_00170   Actino_00190 Actino_00190
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