Monen_00080 Monen_00080   Monen_00100 Monen_00100

Monen_00090 : CDS information

close this sectionLocation

Organism
StrainATCC 15413
Entry nameMonensin
Contig
Start / Stop / Direction8,531 / 6,045 / - [in whole cluster]
8,531 / 6,045 / - [in contig]
Locationcomplement(6045..8531) [in whole cluster]
complement(6045..8531) [in contig]
TypeCDS
Length2,487 bp (828 aa)
Click on the icon to see Genetic map.

close this sectionAnnotation

Category1.1 PKS
Productpolyketide synthase
Product (GenBank)ketosynthase-like protein
GeneksX
Gene (GenBank)
EC number
Keyword
  • modification base
Note
  • It is proposed that this module is not involved in the extension of polyketide chain, but provides a base for modification.
Note (GenBank)
  • SCN_9
Reference
ACC
PmId
[12940979] Analysis of the biosynthetic gene cluster for the polyether antibiotic monensin in Streptomyces cinnamonensis and evidence for the role of monB and monC genes in oxidative cyclization. (Mol Microbiol. , 2003)
comment
monensin生合成 gene clusterの解析論文。

ORF9: KS

figではORF9のままだが、本文中ではksXとされている。
ksXによってコードされるであろうタンパクのN末領域(450aa)は、信頼のおけるtype I PKSのKS domainにとても高い配列相同性を示し、active site residue cysteine-197を完備している。
対してC末側半分(380aa)は、公開されたDBにおけるいかなるタンパク配列にも明らかな度合いの関連性を示さなかった。
Related Reference
ACC
Q27W64
NITE
Niger_00110
PmId
[17584617] Insights into polyether biosynthesis from analysis of the nigericin biosynthetic gene cluster in Streptomyces sp. DSM4137. (Chem Biol. , 2007)
comment
2nd, id50%, 0.0
Streptomyces violaceoniger
NigAX

Nigericin生合成clusterの同定論文。

polyetherであるnigericin, nanchangmycin, and monensinのclusterには共通して、分離したORFの形でKSとACPが存在する。

S. cinnamonensis(monensin-overproducing strain A519)のmonKSX不活化変異株が本論文では作成されており、この実験結果より、monKSXはpolyketide鎖の伸長には関係せず、triepoxide中間体の正しいcyclizationに重要なのではないかと予想している。

また、これら3種類の完全長直線polyketide鎖は、KS activity(NigAX, MonKSX, NanA9)によって、modular PKSからtype II ACP(NigACPX, MonACPX, or NanA10)に転移され、ACPに結合した状態でoxidative cyclizationや他のtailoring reactionを受けるとしている。

close this sectionPKS/NRPS Module

13
KS34..401
at632..694

close this sectionSequence

selected fasta
>polyketide synthase [ketosynthase-like protein]
MANEEKLVEYLKWTTAELHQAQQQLRELKAAQHEPIAVVSMACRLPGKTRTPDDLWDLVS
EGRDAVTGFPDDRAWELPEERPYAELGGFLDDAAGFDAGFFDISDTEAVATEPLQRLMLH
LAWETVERGHIAPHTLRSTLTGVYVGATGHDYATRLETAPDELLPYLGGGTSGSLVSGRI
AYALGLEGPAISVDTACSSSLVALHLACQALRRGECGLALAGGGTVMSTPHTFHAFAHQK
SLAQDGRCKPFAAAADGMGLGEGVGLVLLERLGDARKNGHPVLAVIRGSAVNQDGAGYGL
AAPNGPSQQHVIRAALADAGLTPDQIDAVEAHGTGTPIGDAIEVQALLATYGADRSPDRP
LWLGSVKSNTGHTQGAAGAAALIKMVQAFRHGTLPPTLHVDRPTPLAAWKKGAVRLLTEA
VDWPRREEPRRVGISAFATSGTNAHLILEEPPVDEAPVPDAARDQTSPVAPELPVAWSLS
ARTPEALRAQAKALVTHLAATDPAPSPAEVAYSLAATRSPLEHRAVLTGTDHTELLAAAR
ALAAGEDHPDLVRSTPGAGPKKIAWHFDGRPADGVTTGAAPGAKPGATFGATFGAAFGGA
EFHSAFPLFASAFDEARALLDTHLPTPLPTPHSELARFAVHTALARLLLETGVRPHTLTG
DGVGHIAAAYAAGILTLDDACRLAAAHAAAAQAAEGEQPAPPDAYEPVLKQLTFQRATLT
LTSTAPADTPIASADYWHHHLTSPAPTAPPTPETHTLLHLGALSPEGTQTSAVSALLTAL
ARLHTTGGTVDWTPLVRRTPHPRTIDLPTYSFQATRYWLHDHTAHAAV
selected fasta
>polyketide synthase [ketosynthase-like protein]
GTGGCGAACGAAGAGAAGCTCGTCGAATACCTCAAGTGGACGACGGCCGAGCTCCACCAG
GCCCAGCAGCAGCTGCGCGAACTGAAGGCCGCACAGCACGAGCCGATCGCCGTCGTCTCC
ATGGCCTGCCGGCTGCCCGGCAAGACCCGCACCCCGGACGACCTGTGGGATCTGGTGTCC
GAGGGCCGCGACGCCGTCACCGGCTTCCCCGACGACCGCGCCTGGGAACTCCCCGAGGAA
CGCCCGTACGCGGAGCTCGGCGGGTTCCTGGACGACGCGGCCGGCTTCGACGCGGGCTTC
TTCGACATCAGCGACACCGAGGCCGTGGCCACCGAACCCCTCCAGCGCCTCATGCTCCAC
CTCGCGTGGGAGACCGTCGAACGCGGCCACATCGCCCCGCACACCCTGCGCTCCACCCTC
ACCGGCGTCTACGTCGGCGCCACCGGGCACGACTACGCGACACGGCTCGAGACCGCGCCC
GACGAGCTGCTGCCCTATCTGGGCGGCGGCACGTCCGGCAGCCTCGTCTCCGGCCGCATC
GCCTACGCCCTCGGCCTCGAGGGCCCCGCCATCAGCGTGGACACGGCCTGCTCGTCCTCC
CTGGTCGCCCTCCACCTGGCCTGCCAGGCGCTGCGCCGCGGGGAGTGCGGCCTCGCCCTC
GCCGGCGGCGGCACCGTCATGTCGACGCCGCACACCTTCCACGCCTTCGCCCACCAGAAG
TCGCTCGCGCAGGACGGCCGTTGCAAACCGTTCGCCGCCGCGGCCGACGGCATGGGCCTC
GGTGAAGGCGTCGGCCTCGTCCTGCTTGAGCGGCTCGGCGACGCCAGGAAGAACGGCCAC
CCGGTGCTCGCCGTCATCCGCGGCTCCGCGGTCAACCAGGACGGCGCCGGATACGGCCTC
GCCGCCCCCAACGGCCCCTCCCAGCAGCATGTGATCCGCGCCGCCCTCGCCGACGCCGGG
CTCACCCCGGACCAGATCGACGCCGTCGAGGCGCACGGGACGGGCACCCCCATCGGCGAC
GCCATCGAGGTCCAGGCCCTCCTCGCCACCTACGGCGCCGACCGCTCCCCCGACCGGCCC
CTGTGGCTCGGCTCCGTCAAGTCCAACACGGGGCACACGCAGGGGGCCGCGGGTGCGGCC
GCGCTCATCAAGATGGTCCAGGCGTTCCGGCACGGCACCCTGCCGCCGACCCTCCACGTC
GACCGCCCGACGCCCCTCGCCGCCTGGAAGAAGGGCGCGGTACGGCTGCTCACCGAGGCG
GTCGACTGGCCCCGCCGCGAGGAGCCCCGCCGGGTCGGCATCTCCGCCTTCGCCACGTCC
GGCACGAACGCGCACCTCATCCTCGAAGAGCCGCCGGTGGACGAGGCTCCGGTGCCGGAT
GCCGCCCGCGACCAGACGTCGCCCGTTGCCCCGGAACTCCCGGTGGCCTGGAGCCTGTCC
GCTCGTACACCCGAGGCCCTGCGGGCACAGGCGAAGGCCCTCGTCACCCACCTGGCGGCC
ACCGACCCCGCGCCCTCCCCCGCCGAGGTCGCCTACTCGCTCGCCGCCACCCGCAGCCCC
CTGGAACACCGCGCCGTCCTCACCGGCACCGACCACACCGAACTCCTCGCCGCCGCCCGC
GCCCTGGCCGCCGGAGAGGACCACCCGGACCTGGTCAGGTCCACGCCCGGGGCCGGCCCG
AAGAAGATCGCCTGGCACTTCGACGGCCGCCCGGCCGACGGGGTGACGACGGGGGCGGCA
CCCGGAGCCAAACCCGGCGCGACATTCGGCGCTACATTCGGCGCGGCTTTCGGAGGTGCC
GAGTTCCACTCGGCGTTCCCGCTCTTCGCGTCCGCCTTCGACGAAGCGCGCGCGCTCCTC
GACACCCATCTGCCGACTCCCCTCCCCACTCCCCACTCCGAACTGGCGCGCTTCGCGGTC
CACACCGCGCTCGCGCGGCTGCTCCTGGAAACGGGGGTACGCCCCCACACCCTCACCGGC
GACGGTGTCGGCCACATCGCCGCCGCGTACGCCGCGGGAATCCTGACCCTCGACGACGCG
TGCCGCCTGGCCGCCGCCCACGCCGCTGCCGCCCAGGCCGCCGAGGGTGAACAACCGGCT
CCGCCCGACGCCTACGAGCCCGTGCTGAAGCAGCTGACGTTCCAACGCGCCACGCTCACG
CTCACCAGCACTGCCCCGGCCGACACCCCCATCGCCTCCGCCGACTACTGGCACCACCAC
CTCACCTCGCCGGCCCCCACCGCACCCCCCACCCCCGAGACCCACACGCTTCTCCACCTG
GGCGCGCTCTCACCGGAAGGCACGCAAACCTCCGCCGTAAGCGCCCTGTTGACCGCCCTC
GCGCGGCTTCACACCACGGGCGGCACCGTCGACTGGACCCCTCTCGTCCGGCGCACCCCC
CACCCCCGGACCATCGACCTCCCGACGTACTCCTTCCAGGCCACGCGTTACTGGCTGCAC
GACCACACCGCGCACGCCGCGGTGTGA
[13] KS34..401
[13] at632..694
[13] KS100..1203
[13] at1894..2082

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09 		show BLAST table
InterPro
Database:interpro:38.0
IPR001227 Acyl transferase domain (Domain)
[629-744] 8.1e-17 G3DSA:3.40.366.10
G3DSA:3.40.366.10   Ac_transferase_reg
IPR014030 Beta-ketoacyl synthase, N-terminal (Domain)
[34-275] 2.79999999999994e-76 PF00109
PF00109   ketoacyl-synt
IPR014031 Beta-ketoacyl synthase, C-terminal (Domain)
[283-401] 1.70000000000001e-47 PF02801
PF02801   Ketoacyl-synt_C
IPR014043 Acyl transferase (Domain)
[632-694] 4.20000000000001e-06 PF00698
PF00698   Acyl_transf_1
IPR015083 Polyketide synthase, docking (Domain)
[1-27] 2.8e-15 PF08990
PF08990   Docking
IPR016035 Acyl transferase/acyl hydrolase/lysophospholipase (Domain)
[592-744] 8.80000265836278e-15 SSF52151
SSF52151   Acyl_Trfase/lysoPlipase
IPR016038 Thiolase-like, subgroup (Domain)
[36-287] 3.19999999999996e-80 G3DSA:3.40.47.10 [288-452] 2.4e-62 G3DSA:3.40.47.10
G3DSA:3.40.47.10   Thiolase-like_subgr
IPR016039 Thiolase-like (Domain)
[26-399] 1e-94 SSF53901
SSF53901   Thiolase-like
IPR018201 Beta-ketoacyl synthase, active site (Active_site)
[188-204] PS00606
PS00606   B_KETOACYL_SYNTHASE
IPR020841 Polyketide synthase, beta-ketoacyl synthase domain (Domain)
[36-453] SM00825
SM00825   PKS_KS
SignalP No significant hit
TMHMM No significant hit
Monen_00080 Monen_00080   Monen_00100 Monen_00100
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