Medem_00320 Medem_00320   Medem_00340 Medem_00340

Medem_00330 : CDS information

close this sectionLocation

Organism
StrainAM-7161
Entry nameMedermycin
Contig
Start / Stop / Direction31,922 / 33,148 / + [in whole cluster]
31,922 / 33,148 / + [in contig]
Location31922..33148 [in whole cluster]
31922..33148 [in contig]
TypeCDS
Length1,227 bp (408 aa)
Click on the icon to see Genetic map.

close this sectionAnnotation

Category1.1 PKS
Productpolyketide synthase chain length factor subunit
Product (GenBank)ketosynthase (KS) beta subunit
Gene
Gene (GenBank)med-ORF2
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。

ORF2: Keto-acyl synthase beta(KS beta)[PKS]

配列解析のみ。actI-ORF2 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
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
2nd(Q02062) 66%, 1e-144
Streptomyces coelicolor_actI-ORF2
Actinorhodin polyketide putative beta-ketoacyl synthase 2
[Actino_00190]polyketide synthase chain length factor subunit

--
[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

CLF4..358

close this sectionSequence

selected fasta
>polyketide synthase chain length factor subunit [ketosynthase (KS) beta subunit]
MSDRALITGIGVVAPNGLGVKEYWNATLEGRGGIAPLTRFDASRYPSRLAGQILGFDPAE
HLPNRLLPQTDVSTRLALVAAEQALADGGVDPAELVDFDLGVITSNASGGFAFTHREFAN
LWSKGPEYVSVYESFAWFYAVNTGQVSIRHNVRGPGAALVAEQAGGLDALGHARRSLRLG
TPLVVTGGVDSALDPWGWASHLSSGLISDSDDPDRAYLPFDARARGHVPGEGGAFLVMED
EQGALRRGAGQVYGELAGYAATFDPHPDSGRPPALRRAAELAIADAGLEPSDIGVVFADA
AGSADLDRTEAEAIAAVFGPRGVPVAAPKALTGRLLAGGGPLDVVAASVRLRDGLLPAVP
YEGETPDAYGIDLVRGTPRPTSARAALVLARGRWGFNSAVVVKAADRG
selected fasta
>polyketide synthase chain length factor subunit [ketosynthase (KS) beta subunit]
ATGAGCGACCGAGCCCTGATCACCGGCATCGGCGTGGTGGCCCCCAACGGCCTCGGCGTC
AAGGAGTACTGGAACGCCACCCTCGAAGGGCGGGGCGGCATCGCCCCGCTGACCCGCTTC
GACGCGTCCCGCTACCCGTCCCGGCTGGCCGGCCAGATCCTCGGCTTCGACCCGGCGGAG
CACCTTCCCAACCGGCTCCTCCCGCAGACCGACGTGTCCACCCGGCTGGCCCTGGTCGCC
GCCGAGCAGGCCCTCGCCGACGGCGGCGTCGACCCGGCGGAGCTCGTCGACTTCGACCTC
GGCGTCATCACCTCCAACGCCTCGGGCGGATTCGCCTTCACCCACCGGGAGTTCGCCAAC
CTCTGGTCCAAGGGCCCGGAGTACGTGAGCGTCTACGAGTCGTTCGCCTGGTTCTACGCG
GTCAACACCGGCCAGGTCTCCATCCGGCACAACGTGCGCGGCCCGGGCGCCGCGTTGGTC
GCCGAACAGGCCGGCGGCCTGGACGCGCTGGGCCACGCCCGCCGCTCCCTCAGGCTCGGG
ACCCCGCTCGTCGTCACCGGCGGCGTCGACTCCGCCCTGGACCCCTGGGGCTGGGCCAGT
CACCTGTCCAGCGGGCTGATCAGCGACAGCGACGACCCGGACCGGGCCTATCTGCCCTTC
GACGCCAGGGCGCGCGGCCATGTGCCCGGCGAGGGCGGCGCGTTCCTCGTCATGGAGGAC
GAACAGGGCGCCCTTCGCCGGGGAGCCGGCCAGGTCTACGGCGAACTCGCGGGCTACGCG
GCCACCTTCGACCCGCACCCGGACTCCGGCCGGCCCCCGGCCCTGCGCCGGGCCGCGGAG
CTGGCGATCGCCGACGCGGGCCTCGAACCCTCGGACATCGGCGTCGTCTTCGCCGACGCC
GCCGGTTCGGCCGACCTGGACCGGACCGAGGCCGAGGCGATCGCCGCGGTCTTCGGTCCC
CGCGGCGTGCCGGTCGCGGCGCCGAAGGCACTGACGGGCCGTCTCCTCGCGGGCGGCGGG
CCGCTGGACGTGGTCGCGGCGTCTGTTCGCCTGCGGGACGGGCTCCTCCCGGCCGTCCCG
TACGAGGGCGAGACGCCGGACGCGTACGGCATCGACCTGGTCCGCGGGACACCCCGGCCG
ACCTCCGCGCGGGCCGCCCTGGTCCTCGCCCGCGGCCGCTGGGGCTTCAACTCCGCCGTC
GTGGTCAAGGCGGCGGACCGTGGCTGA
CLF4..358
CLF10..1074

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09 		show BLAST table
InterPro
Database:interpro:38.0
IPR014030 Beta-ketoacyl synthase, N-terminal (Domain)
[4-241] 1.2e-51 PF00109
PF00109   ketoacyl-synt
IPR014031 Beta-ketoacyl synthase, C-terminal (Domain)
[253-358] 2.8e-21 PF02801
PF02801   Ketoacyl-synt_C
IPR016038 Thiolase-like, subgroup (Domain)
[3-257] 3.7e-54 G3DSA:3.40.47.10 [271-405] 1.69999999999999e-29 G3DSA:3.40.47.10
G3DSA:3.40.47.10   Thiolase-like_subgr
IPR016039 Thiolase-like (Domain)
[2-249] 5.6999970878395e-63 SSF53901 [212-405] 3.99998544139406e-43 SSF53901
SSF53901   Thiolase-like
SignalP No significant hit
TMHMM No significant hit
Medem_00320 Medem_00320   Medem_00340 Medem_00340
Page top