Medem_00310 Medem_00310   Medem_00330 Medem_00330

Medem_00320 : CDS information

close this sectionLocation

Organism
StrainAM-7161
Entry nameMedermycin
Contig
Start / Stop / Direction30,657 / 31,925 / + [in whole cluster]
30,657 / 31,925 / + [in contig]
Location30657..31925 [in whole cluster]
30657..31925 [in contig]
TypeCDS
Length1,269 bp (422 aa)
Click on the icon to see Genetic map.

close this sectionAnnotation

Category1.1 PKS
Productpolyketide synthase beta-ketoacyl synthase subunit
Product (GenBank)ketosynthase (KS) alpha subunit
Gene
Gene (GenBank)med-ORF1
EC number
Keyword
  • type II PKS
Note
Note (GenBank)
Reference
ACC
PmId
[12855716] Cloning, sequencing and heterologous expression of the medermycin biosynthetic gene cluster of Streptomyces sp. AM-7161: towards comparative analysis of the benzoisochromanequinone gene clusters. (Microbiology. , 2003)
comment
entire medermycin(med) biosynthetic gene clusterの報告。
Streptomyces coelicolor CH999でmed clusterを発現してmedermycin産生を確認している。

ORF1: Keto-acyl synthase alpha(KS alpha)[PKS]

配列解析のみ。actI-ORF1 homolog.
KS-CLFとACPは20kbp離れている。
Fig.3の提唱経路に、aglyconeは8×malonyl-CoAに由来するとのschemeが記載されている。
Related Reference
ACC
P16540
NITE
Grana_00260
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
4th(P16540) 78%, 0.0
Streptomyces violaceoruber_gra-orf1
[Grana_00260]polyketide synthase beta-ketoacyl synthase subunit

actinorhodin PKS genes(actI)に欠損のあるS.coelicolor mutantには、gra-ORF1で相補されるものがある。
actI-ORF1にフレームシフトがあるmutant B60も相補される。
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
6th(Q02059) 75%, 0.0
Streptomyces coelicolor_actI-ORF1
Actinorhodin polyketide putative beta-ketoacyl synthase 1(EC 2.3.1.-)

--
[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..375

close this sectionSequence

selected fasta
>polyketide synthase beta-ketoacyl synthase subunit [ketosynthase (KS) alpha subunit]
MTRRVVVTGLGVRAPGGSGARQFWDLLSSGRTATRSITSFDASACRSQVAGEIDFDPVAE
GLSPREIRRMDRAAQFAVVCSREAVADSGLSFEGVRPERIGVSVGSAVAAAMSLEKEYRV
LSDQGREWEVDPTYLTPHMFDHMVPSVLGAEVAWTVGAEGPVTVVSDGCTSGLDSVGYAC
RLIQEGSVDVMLAGATDTPLTPIVAACFDAIKATTPRNDDAEHASRPFDLSRNGFVLAEG
AAMFVLEEYESAVRRGARIYAEVTGYATRLNAHHMTGLKTDGREMAEAIRVALDESRIDP
TAIDYVNAHGSGTKQNDRHETAAFKRSLGDHAYAVPVSSIKSMVGHSLGAIGSIEIAASL
LALTHQVVPPTANLHTADPECDLRYVPLTAREAPVRSVLTVGSGFGGFQSAMVLRRPEEA
AA
selected fasta
>polyketide synthase beta-ketoacyl synthase subunit [ketosynthase (KS) alpha subunit]
ATGACCCGCCGTGTCGTCGTCACGGGCCTCGGGGTGCGTGCCCCGGGAGGCTCGGGGGCG
CGGCAGTTCTGGGACCTGCTCAGCTCCGGCCGCACCGCCACCCGCAGCATCACCTCCTTC
GACGCCTCCGCCTGCCGCTCCCAGGTGGCCGGCGAGATCGACTTCGACCCCGTCGCCGAA
GGCCTCTCCCCCCGCGAGATCCGCCGCATGGACCGGGCGGCACAGTTCGCCGTCGTCTGC
TCGCGCGAGGCCGTGGCCGACAGCGGCCTCTCCTTCGAGGGCGTCCGCCCCGAGCGGATC
GGTGTCAGCGTGGGCAGCGCGGTGGCGGCGGCCATGTCCCTGGAGAAGGAGTACCGGGTC
CTCTCCGACCAGGGCCGCGAATGGGAGGTCGACCCCACCTACCTGACCCCCCACATGTTC
GACCACATGGTGCCCAGCGTCCTCGGCGCCGAGGTCGCCTGGACCGTCGGCGCCGAGGGC
CCGGTCACCGTGGTCTCCGACGGCTGCACCTCCGGCCTCGACTCCGTGGGCTACGCCTGC
CGGCTGATCCAGGAGGGCTCGGTCGACGTCATGCTGGCCGGCGCCACCGACACCCCCCTC
ACCCCGATCGTCGCCGCGTGCTTCGACGCCATCAAGGCCACCACCCCGCGCAACGACGAC
GCCGAACACGCCTCGCGGCCCTTCGACCTGTCCCGCAACGGCTTCGTCCTCGCCGAGGGC
GCGGCGATGTTCGTCCTGGAGGAGTACGAGAGCGCGGTACGCCGCGGAGCCCGGATCTAC
GCCGAGGTGACCGGCTACGCGACCCGTCTCAACGCCCACCACATGACCGGGCTCAAGACC
GACGGCCGGGAGATGGCCGAGGCCATCCGCGTCGCCCTCGACGAGTCCAGGATCGACCCG
ACGGCCATCGACTACGTCAACGCCCACGGCTCGGGCACCAAGCAGAACGACCGCCACGAG
ACGGCCGCCTTCAAGCGGAGCCTCGGCGACCACGCCTACGCCGTGCCCGTCAGCTCCATC
AAGTCGATGGTCGGCCACTCGCTCGGCGCCATCGGCTCCATCGAGATCGCGGCGAGCCTC
CTGGCCCTGACGCACCAGGTCGTCCCGCCCACGGCCAACCTCCACACCGCCGACCCGGAG
TGCGACCTTCGATACGTCCCGCTGACCGCCCGCGAGGCACCGGTGCGCAGCGTCCTCACG
GTGGGCAGCGGCTTCGGCGGATTCCAGTCCGCGATGGTGCTCCGACGGCCCGAGGAGGCG
GCGGCATGA
KS3..375
KS7..1125

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09 		show BLAST table
InterPro
Database:interpro:38.0
IPR014030 Beta-ketoacyl synthase, N-terminal (Domain)
[3-251] 6.49999999999992e-60 PF00109
PF00109   ketoacyl-synt
IPR014031 Beta-ketoacyl synthase, C-terminal (Domain)
[260-375] 6e-37 PF02801
PF02801   Ketoacyl-synt_C
IPR016038 Thiolase-like, subgroup (Domain)
[3-263] 8.49999999999995e-67 G3DSA:3.40.47.10 [271-418] 5.19999999999996e-52 G3DSA:3.40.47.10
G3DSA:3.40.47.10   Thiolase-like_subgr
IPR016039 Thiolase-like (Domain)
[2-257] 3.30001976117415e-69 SSF53901 [219-418] 1e-63 SSF53901
SSF53901   Thiolase-like
IPR018201 Beta-ketoacyl synthase, active site (Active_site)
[160-176] PS00606
PS00606   B_KETOACYL_SYNTHASE
SignalP
[1-20] 0.705 Signal
Eukaryota   
TMHMM No significant hit
Medem_00310 Medem_00310   Medem_00330 Medem_00330
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