Jado_00070 Jado_00070   Jado_00090 Jado_00090

Jado_00080 : CDS information

close this sectionLocation

Organism
StrainISP5230 (=NBRC 13096)
Entry nameJadomycin B
Contig
Start / Stop / Direction8,594 / 9,862 / + [in whole cluster]
2,346 / 3,614 / + [in contig]
Location8594..9862 [in whole cluster]
2346..3614 [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)jadomycin polyketide ketosynthase
Gene
Gene (GenBank)jadA
EC number
Keyword
  • type II PKS
Note
Note (GenBank)
  • JadA
Reference
ACC
PmId
[7881555] Cloning and characterization of polyketide synthase genes for jadomycin B biosynthesis in Streptomyces venezuelae ISP5230. (Microbiology. , 1994)
[9224566] Iterative type II polyketide synthases, cyclases and ketoreductases exhibit context-dependent behavior in the biosynthesis of linear and angular decapolyketides. (Chem Biol. , 1997)
[15817470] Functional analyses of oxygenases in jadomycin biosynthesis and identification of JadH as a bifunctional oxygenase/dehydrase. (J Biol Chem. , 2005)
[15776503] The oxidative ring cleavage in jadomycin biosynthesis: a multistep oxygenation cascade in a biosynthetic black box. (Chembiochem. , 2005)
comment
[PMID:7881555](1994)
ORF1(=jadAに相当)は配列解析からtype II PKSのketoacyl synthaseであると提唱されている。

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[PMID: 9224566](1997)
minimal PKS + KR + CYCをjadomycin, daunorubicin, tetracenomycinのgenesで構成し、そのplasmid発現株での産物を解析。
jadAもKS-alphaとして使用されている。

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[PMID: 15817470](2005)
jadA In-frame Deletion Mutant作成。このmutantはjadomycin B産生見られないが、UWM6 and 2,3-dehydro-UWM6からjadomycin A or Bへの変換可能。

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[PMID: 15776503](2005)
repressor gene jadR2を不活化してPKS後修飾genesが過剰発現されるようにしたS. venezuelae VS662で、ketosynthase gene jadAを不活化。この株はjadomycinsや関連物質を非産生。

close this sectionPKS/NRPS Module

KS4..375

close this sectionSequence

selected fasta
>polyketide synthase beta-ketoacyl synthase subunit [jadomycin polyketide ketosynthase]
MTARRVVITGIEVLAPGGTGSKAFWNLLSEGRTATRGITFFDPTPFRSRVAAEIDFDPEA
HGLSPQEIRRMDRAAQFAVVAARAVADSGIDLAAHDPYRVGVTVGSAVGATMGLDEEYRV
VSDGGRLDLVDHAYAVPHLYDYMVPSSFSAEVAWAVGAEGPNTVVSTGCTSGLDSVGYAR
GELIREGSADVMIAGSSDAPISPITMACFDAIKATTNRYDDPAHASRPFDGTRNGFVLGE
GAAVFVLEELESARARGAHIYAEIAGYATRSNAYHMTGLRPDGAEMAEAIRVALDEARMN
PTEIDYINAHGSGTKQNDRHETAAFKKSLGDHAYRTPVSSIKSMVGHSLGAIGSIEIAAS
ALAMEHNVVPPTGNLHTPDPECDLDYVRSCREQLTDSVLTVGSGFGGFQSAMVLARPERK
IA
selected fasta
>polyketide synthase beta-ketoacyl synthase subunit [jadomycin polyketide ketosynthase]
GTGACCGCGCGACGCGTCGTCATCACCGGCATCGAGGTCCTCGCCCCCGGTGGCACCGGA
TCCAAGGCCTTCTGGAACCTGCTCAGCGAGGGCCGCACGGCCACCCGGGGCATCACCTTC
TTCGACCCGACGCCGTTCCGCTCCCGGGTCGCCGCCGAGATCGACTTCGACCCGGAGGCC
CACGGCCTCAGCCCGCAGGAGATCCGCCGCATGGACCGGGCCGCCCAGTTCGCGGTGGTC
GCCGCGCGCGCCGTCGCCGACAGCGGCATCGACCTGGCCGCCCACGACCCGTACCGCGTC
GGCGTCACCGTCGGCAGCGCCGTCGGCGCCACCATGGGCCTCGACGAGGAGTACCGGGTC
GTCAGCGACGGCGGCCGGCTCGACCTCGTCGACCACGCCTACGCGGTGCCGCACCTCTAC
GACTACATGGTGCCCAGCTCCTTCTCCGCCGAGGTCGCCTGGGCCGTCGGCGCCGAGGGC
CCCAACACCGTGGTCTCCACCGGCTGCACCTCCGGCCTCGACTCCGTCGGCTACGCGCGT
GGGGAGCTGATCCGCGAGGGCTCCGCCGACGTCATGATCGCCGGTTCCTCGGACGCCCCG
ATCTCCCCGATCACGATGGCCTGCTTCGACGCCATCAAGGCGACCACCAACCGGTACGAC
GACCCGGCGCACGCCTCCCGGCCCTTCGACGGCACCCGCAACGGCTTCGTGCTCGGCGAG
GGCGCGGCCGTCTTCGTCCTGGAGGAGCTGGAGAGCGCCCGGGCCCGCGGCGCCCACATC
TACGCCGAGATCGCCGGCTACGCCACCCGCAGCAACGCGTACCACATGACCGGTCTGCGG
CCGGACGGCGCGGAGATGGCGGAGGCGATCCGGGTCGCGCTCGACGAGGCGCGGATGAAC
CCCACCGAGATCGACTACATCAACGCGCACGGCTCCGGCACCAAGCAGAACGACCGCCAC
GAGACCGCAGCGTTCAAGAAGAGCCTCGGGGACCACGCGTACCGCACCCCGGTCAGCTCC
ATCAAGTCGATGGTCGGGCACTCCCTCGGTGCCATCGGCTCCATCGAGATCGCCGCCTCG
GCCCTGGCCATGGAGCACAACGTGGTCCCGCCGACGGGCAACCTGCACACCCCGGACCCC
GAGTGCGACCTGGACTACGTCCGCTCGTGCCGCGAGCAGCTCACGGACTCGGTCCTGACC
GTCGGCAGCGGATTCGGCGGCTTCCAGAGCGCCATGGTCCTGGCCCGTCCCGAGAGGAAG
ATCGCATGA
KS4..375
KS10..1125

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09 		show BLAST table
InterPro
Database:interpro:38.0
IPR014030 Beta-ketoacyl synthase, N-terminal (Domain)
[4-253] 4.10000000000004e-60 PF00109
PF00109   ketoacyl-synt
IPR014031 Beta-ketoacyl synthase, C-terminal (Domain)
[261-375] 6.40000000000004e-39 PF02801
PF02801   Ketoacyl-synt_C
IPR016038 Thiolase-like, subgroup (Domain)
[2-266] 1.29999999999998e-61 G3DSA:3.40.47.10 [271-418] 2.50000000000001e-50 G3DSA:3.40.47.10
G3DSA:3.40.47.10   Thiolase-like_subgr
IPR016039 Thiolase-like (Domain)
[3-419] 2.19999900980707e-63 SSF53901
SSF53901   Thiolase-like
IPR018201 Beta-ketoacyl synthase, active site (Active_site)
[160-176] PS00606
PS00606   B_KETOACYL_SYNTHASE
SignalP
[1-23] 0.16 Signal
Bacteria, Gram-positive   
TMHMM No significant hit
Jado_00070 Jado_00070   Jado_00090 Jado_00090
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