Sch475_00370 Sch475_00370   Sch475_00390 Sch475_00390

Sch475_00380 : CDS information

close this sectionLocation

Organism
StrainSCC-2136
Entry nameSch 47554
Contig
Start / Stop / Direction52,609 / 51,320 / - [in whole cluster]
52,609 / 51,320 / - [in contig]
Locationcomplement(51320..52609) [in whole cluster]
complement(51320..52609) [in contig]
TypeCDS
Length1,290 bp (429 aa)
Click on the icon to see Genetic map.

close this sectionAnnotation

Category1.1 PKS
Productpolyketide synthase beta-ketoacyl synthase subunit
Product (GenBank)putative ketoacyl synthase
Gene
Gene (GenBank)schP8
EC number
Keyword
  • type II PKS
Note
  • The N-terminal position was modified from original INSDC entry.
Note (GenBank)
Reference
ACC
PmId
[17085966] Angucyclines Sch 47554 and Sch 47555 from Streptomyces sp. SCC-2136: cloning, sequencing, and characterization. (Mol Cells. , 2006)
comment
angucyclines Sch 47554 and Sch 47555の生合成に関連したentire gene clusterの
クローニング、シークエンス、配列解析からの特徴づけ。

SchP8(420aa): Ketoacyl synthase

schP7-schP8は翻訳共役。
start codonはGTG.
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 2nd, id91%, 0.0
Streptomyces fradiae_urdA
Putative ketoacyl synthase

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

KS7..379

close this sectionSequence

selected fasta
>polyketide synthase beta-ketoacyl synthase subunit [putative ketoacyl synthase]
MSATGGRRVVITGIGVTAPGGVGAKNFWSLLTDGRTATRRISFFDPSPFRSQVAAEADFD
AALLGLGPQEIRRMDRAAQFAVVTAREAVADSGLEFEGLDPHRTGVTIGSAVGATMGLDE
EYRTVSDNGRLDLVDHTYAVPHLYNYLVPSSFAAEVAWAVGAEGPSTVVSTGCTSGLDSV
GYAAELIREGAADVMVAGAADAPISPITVACFDAIKATTPRNDDPEHASRPFDGTRNGFV
LGEGAAVFVLEELGAARARGAHIYAEIAGYATRSNAFHMTGLRPDGREMAEAIRVAMDEA
RLNPEDIDYINAHGSGTKQNDRHETAAFKHSLGSRAYDVPVSSIKSMVGHSLGAIGSIEI
AASAMAMEHGAVPPTANLHTPDPECDLDYVPLTARDWQTDAVLSVGSGFGGFQSAIVLAR
PDRAERSAA
selected fasta
>polyketide synthase beta-ketoacyl synthase subunit [putative ketoacyl synthase]
GTGAGCGCGACCGGCGGCCGGCGGGTCGTGATCACCGGCATCGGGGTGACCGCACCGGGC
GGCGTGGGCGCCAAGAACTTCTGGAGCCTGTTGACCGACGGGCGCACCGCCACCCGGCGT
ATCAGCTTCTTCGATCCGTCGCCGTTCCGCTCCCAGGTGGCCGCGGAGGCCGACTTCGAC
GCGGCGCTGCTGGGGCTCGGCCCGCAGGAGATCCGGCGCATGGACCGGGCCGCGCAGTTC
GCGGTCGTCACGGCGCGCGAGGCGGTCGCCGACAGCGGGCTGGAGTTCGAGGGCCTCGAC
CCGCACCGGACCGGGGTGACCATCGGCAGCGCGGTCGGCGCGACCATGGGGCTCGACGAG
GAGTACCGGACCGTCAGCGACAACGGGCGGCTCGACCTGGTCGACCACACCTACGCCGTG
CCCCACCTCTACAACTACCTGGTGCCCAGCTCGTTCGCCGCCGAGGTGGCCTGGGCGGTC
GGCGCCGAGGGTCCGAGCACGGTGGTCTCCACGGGCTGCACCTCGGGCCTCGACTCGGTG
GGATACGCCGCCGAGCTGATCCGGGAGGGCGCCGCCGACGTCATGGTGGCCGGTGCCGCG
GACGCCCCCATCTCGCCGATCACGGTGGCCTGTTTCGACGCGATCAAGGCGACCACCCCG
CGCAACGACGACCCGGAGCACGCCTCACGGCCCTTCGACGGCACCCGCAACGGGTTCGTC
CTGGGCGAGGGTGCCGCCGTGTTCGTCCTGGAGGAGCTGGGCGCCGCCCGGGCCCGCGGC
GCGCACATCTACGCGGAGATCGCCGGGTACGCGACCCGCAGCAACGCCTTCCACATGACC
GGACTGCGGCCCGACGGGCGGGAGATGGCGGAGGCCATCCGGGTGGCCATGGACGAGGCC
CGGCTGAACCCCGAGGACATCGACTACATCAACGCGCACGGCTCCGGCACCAAGCAGAAC
GACCGGCACGAGACCGCCGCGTTCAAGCACAGCCTGGGCAGCCGTGCCTACGACGTACCG
GTCAGCTCCATCAAGTCGATGGTCGGGCACTCGCTCGGCGCGATCGGCTCGATCGAGATC
GCCGCGTCCGCGATGGCCATGGAACACGGCGCCGTACCGCCCACCGCCAATCTGCACACC
CCCGACCCCGAGTGCGATCTCGACTATGTGCCGCTCACGGCACGCGACTGGCAGACCGAC
GCGGTGCTCTCCGTCGGCAGCGGCTTCGGCGGCTTCCAGAGCGCCATCGTGCTGGCCCGC
CCGGACCGGGCCGAAAGGAGCGCCGCATGA
KS7..379
KS19..1137

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09 		show BLAST table
InterPro
Database:interpro:38.0
IPR014030 Beta-ketoacyl synthase, N-terminal (Domain)
[7-253] 3.9e-64 PF00109
PF00109   ketoacyl-synt
IPR014031 Beta-ketoacyl synthase, C-terminal (Domain)
[264-379] 2.1e-39 PF02801
PF02801   Ketoacyl-synt_C
IPR016038 Thiolase-like, subgroup (Domain)
[6-269] 6.4e-65 G3DSA:3.40.47.10 [274-421] 3.7e-53 G3DSA:3.40.47.10
G3DSA:3.40.47.10   no description
IPR016039 Thiolase-like (Domain)
[1-423] 1.8e-70 SSF53901
SSF53901   Thiolase-like
IPR018201 Beta-ketoacyl synthase, active site (Active_site)
[164-180] PS00606
PS00606   B_KETOACYL_SYNTHASE
IPR020841 Polyketide synthase, beta-ketoacyl synthase domain (Domain)
[9-423] 1.7e-15 SM00825
SM00825   Beta-ketoacyl synthase
SignalP
[1-24] 0.29 Signal
Bacteria, Gram-positive   
[1-24] 0.834 Signal
Eukaryota   
[1-24] 0.211 Signal
Bacteria, Gram-negative   
TMHMM No significant hit
Sch475_00370 Sch475_00370   Sch475_00390 Sch475_00390
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