Grana_00260 Grana_00260   Grana_00280 Grana_00280

Grana_00270 : CDS information

close this sectionLocation

Organism
StrainTü22
Entry nameGranaticin
Contig
Start / Stop / Direction30,300 / 31,547 / + [in whole cluster]
30,300 / 31,547 / + [in contig]
Location30300..31547 [in whole cluster]
30300..31547 [in contig]
TypeCDS
Length1,248 bp (415 aa)
Click on the icon to see Genetic map.

close this sectionAnnotation

Category1.1 PKS
Productpolyketide synthase chain length factor subunit
Product (GenBank)polyketide synthase chain length factor
Gene
Gene (GenBank)gra-orf2
EC number
Keyword
  • type II PKS
Note
Note (GenBank)
Reference
ACC
PmId
[2583128] Structure and deduced function of the granaticin-producing polyketide synthase gene cluster of Streptomyces violaceoruber Tu22. (EMBO J. , 1989)
[9831526] The granaticin biosynthetic gene cluster of Streptomyces violaceoruber Tu22: sequence analysis and expression in a heterologous host. (Chem Biol. , 1998)
[1400167] Functional replacement of genes for individual polyketide synthase components in Streptomyces coelicolor A3(2) by heterologous genes from a different polyketide pathway. (J Bacteriol. , 1992)
comment
[PMID: 2583128](1989)
granaticin生合成gene clusterの一部6.5 kb regionの配列解析報告。

--
[PMID: 9831526](1998)
entire granaticin gene cluster(gra cluster)の報告。

ORF2: Chain length factor (CLF)[PKS]

配列解析。actI-2に似ている。
gra-ORF1-5はact clusterと同じ並び。

--
[PMID: 1400167](1992)
acrinorhodin PKS gene actI-ORF2に塩基削除によるフレームシフトがあるS.coelicolor mutant B60はgra-ORF2で相補される。

actI-ORFXに釣られて（？）、この論文ではgra"I"-ORFXとされている。
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
5th(Q02062) 61%, 1e-125
Streptomyces coelicolor_actI ORF2
Actinorhodin polyketide putative beta-ketoacyl synthase 2(EC 2.3.1.-)

--
[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

CLF7..361

close this sectionSequence

selected fasta
>polyketide synthase chain length factor subunit [polyketide synthase chain length factor]
MSTPDRRRAVVTGLSVAAPGGLGTERYWKSLLTGENGIAELSRFDASRYPSRLAGQIDDF
EASEHLPSRLLPQTDVSTRYALAAADWALADAGVGPESGLDDYDLGVVTSTAQGGFDFTH
REFHKLWSQGPAYVSVYESFAWFYAVNTGQISIRNTMRGPSAALVGEQAGGLDAIGHARR
TVRRGPGWCSAVASTRRSTRGASSSQLSGGLVSTVADPERAYLPFDVDASGYVPGEGGAV
LIVEDADSARARGAERIYVRSPLRRDPAPGSGRPPALGRAAELALAEAGLTPADISVVFA
DGAGVPELDRAEADTLARLFGPRGVPVTAPKALTGRLCAGGGPADLAAALLALRDQVIPA
TGRHRAVPDAYALDLVTGRPREAALSAALVLARGRHGFNSAVVVTLRGSDHRRPT
selected fasta
>polyketide synthase chain length factor subunit [polyketide synthase chain length factor]
GTGAGCACCCCTGACCGCCGGCGGGCCGTCGTCACCGGCCTCAGCGTCGCCGCCCCCGGT
GGCCTCGGCACCGAGCGTTACTGGAAGTCCCTGCTGACCGGCGAGAACGGCATCGCCGAG
CTCTCCCGCTTCGACGCCTCCCGCTACCCGTCCCGACTGGCCGGGCAGATCGACGACTTC
GAGGCCTCCGAGCACCTGCCCAGCAGGCTGCTGCCGCAGACCGACGTCTCCACGCGCTAC
GCGCTGGCCGCCGCCGACTGGGCGCTCGCCGACGCGGGCGTCGGCCCCGAGTCGGGCCTC
GACGACTACGACCTGGGCGTCGTCACCTCCACCGCCCAGGGCGGCTTCGACTTCACCCAC
CGAGAGTTCCACAAGCTGTGGAGCCAGGGACCCGCGTACGTCAGCGTGTACGAGTCCTTC
GCCTGGTTCTACGCCGTCAACACCGGCCAGATCTCCATCCGCAACACGATGCGCGGCCCC
AGCGCCGCCCTGGTCGGCGAACAGGCCGGCGGCCTCGACGCGATCGGGCACGCCCGGCGT
ACGGTCCGCCGCGGACCCGGCTGGTGCTCAGCGGTGGCGTCGACTCGGCGCTCGACCCGT
GGGGCTTCGTCCTCGCAGCTCTCCGGCGGTCTCGTCTCCACGGTCGCCGACCCGGAGCGC
GCCTATCTGCCCTTCGACGTCGACGCCTCCGGCTACGTGCCGGGCGAAGGCGGCGCCGTC
CTCATCGTCGAGGACGCCGACTCGGCGCGCGCACGGGGTGCCGAGCGGATCTACGTGAGA
TCGCCGCTACGCCGCGACCCGGCACCCGGCTCCGGCCGTCCGCCCGCCCTCGGCCGCGCC
GCCGAACTCGCCCTCGCCGAAGCGGGGCTGACGCCCGCCGACATCTCGGTGGTGTTCGCC
GACGGAGCGGGGGTCCCGGAGCTCGACCGCGCCGAGGCCGACACCCTCGCCCGGCTCTTC
GGGCCGCGGGGCGTCCCGGTGACCGCGCCCAAGGCACTCACCGGCCGCCTGTGCGCCGGT
GGCGGCCCCGCCGACCTGGCGGCCGCGCTGCTCGCCCTGCGCGACCAGGTGATCCCCGCG
ACCGGCCGCCACCGCGCGGTGCCGGACGCCTACGCCCTCGACCTGGTGACCGGCCGGCCC
CGCGAGGCCGCCCTGAGCGCGGCCCTCGTCCTCGCGCGCGGCCGCCACGGCTTCAACTCC
GCGGTCGTCGTCACGCTCCGCGGCTCTGACCACCGTCGGCCCACCTGA
CLF7..361
CLF19..1083

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09 		show BLAST table
InterPro
Database:interpro:38.0
IPR014030 Beta-ketoacyl synthase, N-terminal (Domain)
[7-247] 1.2e-45 PF00109
PF00109   ketoacyl-synt
IPR014031 Beta-ketoacyl synthase, C-terminal (Domain)
[274-361] 6.79999999999998e-23 PF02801
PF02801   Ketoacyl-synt_C
IPR016038 Thiolase-like, subgroup (Domain)
[4-255] 4.39999999999997e-46 G3DSA:3.40.47.10 [273-405] 1.6e-31 G3DSA:3.40.47.10
G3DSA:3.40.47.10   Thiolase-like_subgr
IPR016039 Thiolase-like (Domain)
[6-254] 8.69997440322062e-54 SSF53901 [217-404] 1.79999754022375e-39 SSF53901
SSF53901   Thiolase-like
SignalP
[1-23] 0.874 Signal
Eukaryota   
TMHMM No significant hit
Grana_00260 Grana_00260   Grana_00280 Grana_00280
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