Alnu_00060 : CDS information

close this sectionLocation

Organism
StrainCM020
Entry nameAlnumycin
Contig
Start / Stop / Direction3,481 / 4,746 / + [in whole cluster]
3,481 / 4,746 / + [in contig]
Location3481..4746 [in whole cluster]
3481..4746 [in contig]
TypeCDS
Length1,266 bp (421 aa)
Click on the icon to see Genetic map.

close this sectionAnnotation

Category1.1 PKS
Productpolyketide synthase beta-ketoacyl synthase subunit
Product (GenBank)AlnL ketoacyl synthase alpha
Gene
Gene (GenBank)alnL
EC number
Keyword
  • type II PKS
Note
Note (GenBank)
Reference
ACC
PmId
[18940666] Characterization of the alnumycin gene cluster reveals unusual gene products for pyran ring formation and dioxan biosynthesis. (Chem Biol. , 2008)
comment
alnumycin gene clusterのクローニング、シークエンス。
aln2-alnT2の領域をS.albusに導入して、alnumycin産生されることを確認している。

AlnL: Ketoacyl synthase alpha

配列解析からminimal PKSのKS subunitであると提唱されている。
starter and minimal PKSをコードする遺伝子は、同じ鎖長のfrenolicinの相当する遺伝子と最も相同性あり。
Related Reference
ACC
Q54173
NITE
Urd_00120
PmId
[7592377] Cloning and characterization of a polyketide synthase gene from Streptomyces fradiae Tu2717, which carries the genes for biosynthesis of the angucycline antibiotic urdamycin A and a gene probably involved in its oxygenation. (J Bacteriol. , 1995)
comment
Blast 4th, id77%, 0.0
Streptomyces fradiae_urdA
Putative ketoacyl synthase
[Urd_00120]polyketide synthase beta-ketoacyl synthase subunit

urdEFABCDを含むcosmid purd8をS.lividans TK24へ導入すると、urdamycin抵抗性を獲得。
urdamycin産生株S.fradiae Tu2717染色体から、urdE-C末+urdFABを含むfragment g領域を削除するとurdamycin産生不可。

AA配列解析で、UrdAはPKS gene clustersのbeta-ketoacyl synthasesに高い類似性あり。
UrdAとUrdBはid36%で似ているが、UrdBにはないactive site cysteineをUrdAは持っている。

TcmK ketoacyl synthase or TcmL chain length factorのどちらかを障害してtetracenomycin C非産生にしたStreptomyces glaucescensのmutantで、urdFABを異種性発現したらどちらのmutantも相補され、tetracenomycin Cを産生できた。

close this sectionPKS/NRPS Module

KS3..375

close this sectionSequence

selected fasta
>polyketide synthase beta-ketoacyl synthase subunit [AlnL ketoacyl synthase alpha]
MNRSVAITGIGVVAPGGVGKKAFWDLLVSGRTATRTISFFDPSRFRSQVAAEVDFDPQRS
GLSPREARRLDRAAQFAVVSARECMADSGLEFVELDPHRTGVSVGSAVGGTTGLEREYLV
LSDSGRLWEVDSDYVSPHLFDAFVPSSLAAEVAWTVGAEGPATVVSTGCTSGLDSVGYAR
DLIAEGTVDVMIAGAADTPISPIAVSCFDAIKATTPRNDDPEHASRPFDRTRNGFVLAEG
AAMFVLEELEHARARGAHVYGVIGGYATRCNAYHMTGLRPDGHEMAEAIRHSLDQARLNP
DLVDYVNAHGSGTKQNDRHETAAFKETLGQHAYEVPISSIKSMVGHSLGAIGSIEIAACA
LAMENGAVPPTANLHEPDPECDLDYVPNEAREHGVDAVLSVGSGFGGFQSAMVITREETT
R
selected fasta
>polyketide synthase beta-ketoacyl synthase subunit [AlnL ketoacyl synthase alpha]
GTGAACCGAAGTGTCGCAATCACCGGGATAGGCGTTGTCGCGCCGGGTGGGGTGGGCAAG
AAGGCGTTCTGGGATCTCCTGGTCTCGGGCCGCACCGCCACCCGCACCATCTCCTTCTTC
GACCCCTCCCGCTTCCGCTCACAGGTCGCCGCCGAGGTCGACTTCGATCCGCAGCGGTCC
GGGCTCAGCCCGCGGGAGGCGAGGCGGCTGGACCGGGCCGCACAGTTCGCCGTCGTCAGC
GCCAGGGAGTGCATGGCGGACAGCGGCCTCGAATTCGTGGAACTCGATCCGCACCGCACC
GGGGTGAGCGTCGGCAGCGCGGTCGGCGGCACCACCGGACTGGAACGCGAATACCTCGTC
CTCAGCGACAGCGGCCGGCTGTGGGAGGTGGACAGCGACTACGTCTCGCCCCACCTCTTC
GACGCCTTCGTGCCCAGTTCCCTGGCGGCCGAGGTGGCCTGGACCGTGGGCGCCGAAGGG
CCCGCCACGGTCGTCTCCACCGGCTGCACATCGGGGCTGGACTCCGTGGGCTACGCGCGT
GACCTCATCGCCGAGGGCACCGTCGACGTCATGATCGCCGGGGCGGCCGACACCCCGATC
TCCCCGATCGCCGTCTCCTGCTTCGACGCCATCAAGGCCACCACGCCCCGCAACGACGAC
CCCGAGCACGCCTCCCGGCCCTTCGACCGCACCCGCAACGGCTTCGTACTCGCCGAGGGC
GCCGCGATGTTCGTCCTGGAGGAACTGGAGCACGCGCGGGCCCGGGGCGCCCATGTCTAC
GGGGTCATCGGCGGCTACGCCACCCGCTGCAACGCGTACCACATGACGGGTCTGCGGCCG
GACGGCCACGAGATGGCCGAGGCCATCCGGCACTCGCTGGACCAGGCGCGGCTCAACCCC
GACCTCGTCGACTACGTCAACGCGCACGGCTCGGGCACCAAGCAGAACGACCGGCACGAG
ACGGCCGCCTTCAAGGAGACCCTCGGGCAGCACGCCTACGAGGTGCCGATCAGCTCCATC
AAGTCCATGGTCGGGCACTCCCTGGGCGCCATCGGCTCCATCGAGATCGCCGCCTGCGCG
CTGGCCATGGAGAACGGTGCCGTTCCCCCCACGGCCAACCTTCACGAGCCCGATCCCGAA
TGCGACCTGGACTACGTACCGAACGAGGCCCGGGAGCACGGCGTGGACGCCGTCCTCAGT
GTGGGCAGCGGCTTCGGCGGCTTCCAGTCCGCCATGGTCATCACCCGAGAGGAAACCACG
CGATGA
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)
 [3-252]  1.29999999999998e-63 PF00109
PF00109   ketoacyl-synt
IPR014031 Beta-ketoacyl synthase, C-terminal (Domain)
 [260-375]  7.4e-39 PF02801
PF02801   Ketoacyl-synt_C
IPR016038 Thiolase-like, subgroup (Domain)
 [2-263]  4.09999999999995e-68 G3DSA:3.40.47.10 [270-416]  1.29999999999998e-53 G3DSA:3.40.47.10
G3DSA:3.40.47.10   Thiolase-like_subgr
IPR016039 Thiolase-like (Domain)
 [2-257]  5.50001754266469e-72 SSF53901 [219-416]  3.19999899046355e-67 SSF53901
SSF53901   Thiolase-like
IPR018201 Beta-ketoacyl synthase, active site (Active_site)
 [160-176]  PS00606
PS00606   B_KETOACYL_SYNTHASE
SignalP No significant hit
TMHMM No significant hit
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