Grana_00250 Grana_00250   Grana_00270 Grana_00270

Grana_00260 : CDS information

close this sectionLocation

Organism
StrainTü22
Entry nameGranaticin
Contig
Start / Stop / Direction29,038 / 30,303 / + [in whole cluster]
29,038 / 30,303 / + [in contig]
Location29038..30303 [in whole cluster]
29038..30303 [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)polyketide synthase keto-acyl synthase
Gene
Gene (GenBank)gra-orf1
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。

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

ORF1: Keto-acyl synthase (KS)[PKS]

配列解析。actI-1に似ている。
gra-ORF1-5はact clusterと同じ並び。

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[PMID: 1400167](1992)
actinorhodin PKS genes(actI)に欠損のあるS.coelicolor mutantには、gra-ORF1で相補されるものがある。
actI-ORF1にフレームシフトがあるmutant B60も相補される。

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
Q02059
NITE
Actino_00180
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
6th(Q02059) 76%, 0.0
Streptomyces coelicolor_actI ORF1
Actinorhodin polyketide putative beta-ketoacyl synthase 1(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

KS3..375

close this sectionSequence

selected fasta
>polyketide synthase beta-ketoacyl synthase subunit [polyketide synthase keto-acyl synthase]
MTRRVVITGVGVRAPGGSGTKEFWDLLTAGRTATRPISFFDASPFRSRIAGEIDFDAVAE
GFSPREVRRMDRATQFAVACTRDALADSGLDTGALDPSRIGVALGSAVASATSLENEYLV
MSDSGREWLVDPAHLSPMMFDYLSPGVMPAEVAWAAGAEGPVTMVSDGCTSGLDSVGYAV
QGTREGSADVVVAGAADTPVSPIVVACFDAIKATTPRNDDPAHASRPFDGTRNGFVLAEG
AAMFVLEEYEAAQRRGAHIYAEVGGYATRSQAYHMTGLKKDGREMAESIRAALDEARLDR
TAVDYVNAHGSGTKQNDRHETAAFKRSLGEHAYAVPVSSIKSMGGHSLGAIGSIEIAASV
LAIEHNVVPPTANLHTPDPECDLDYVPLTAREQRVDTVLTVGSGFGGFQSAMVLHRPEEA
A
selected fasta
>polyketide synthase beta-ketoacyl synthase subunit [polyketide synthase keto-acyl synthase]
GTGACCCGACGCGTAGTGATCACCGGGGTCGGGGTGCGTGCCCCTGGCGGCTCAGGGACG
AAGGAGTTCTGGGACCTGCTCACCGCCGGCCGCACGGCGACTCGACCCATCAGTTTCTTC
GACGCCTCCCCGTTCCGCTCGCGGATCGCGGGGGAGATCGACTTCGACGCCGTCGCGGAG
GGCTTCTCCCCGCGTGAGGTCCGTCGCATGGACCGCGCCACCCAGTTCGCGGTCGCCTGC
ACCCGGGACGCGCTGGCCGACAGCGGCCTGGACACGGGCGCCCTCGACCCGTCCCGGATC
GGCGTCGCCCTGGGGAGCGCGGTCGCGTCGGCGACGAGCCTGGAGAACGAGTACCTGGTG
ATGTCGGACTCCGGCCGCGAGTGGCTGGTGGACCCGGCACACCTGTCGCCGATGATGTTC
GACTACCTCAGCCCGGGCGTCATGCCCGCCGAGGTCGCCTGGGCGGCCGGCGCGGAGGGC
CCGGTCACCATGGTCTCCGACGGCTGCACCTCGGGCCTGGACTCGGTCGGCTACGCCGTT
CAGGGGACCCGCGAGGGCAGCGCGGACGTGGTGGTCGCCGGCGCCGCCGACACCCCCGTC
TCCCCGATCGTGGTGGCCTGCTTCGACGCCATCAAGGCGACGACCCCGCGCAACGACGAC
CCGGCGCACGCCTCCCGGCCCTTCGACGGCACCCGCAACGGCTTCGTCCTCGCCGAGGGC
GCCGCCATGTTCGTCCTGGAGGAGTACGAGGCCGCCCAGCGACGCGGAGCCCACATCTAC
GCCGAGGTCGGCGGCTACGCCACGCGCTCGCAAGCGTACCACATGACGGGTCTGAAGAAG
GACGGCCGGGAGATGGCCGAATCGATCAGGGCCGCACTCGACGAGGCCCGGCTGGACCGT
ACGGCGGTCGACTACGTCAACGCGCACGGCTCCGGCACCAAGCAGAACGACCGCCACGAG
ACGGCCGCCTTCAAGCGCAGCCTCGGCGAGCACGCGTACGCGGTGCCCGTCAGCTCCATC
AAATCCATGGGGGGGCACTCACTCGGCGCGATCGGCTCCATCGAGATCGCAGCGTCGGTC
CTCGCCATCGAACACAACGTCGTCCCGCCGACGGCGAATCTGCACACCCCCGACCCCGAG
TGCGACCTGGACTACGTTCCGCTCACCGCGCGCGAGCAGCGCGTCGACACGGTGCTCACC
GTGGGCAGCGGCTTCGGCGGGTTCCAGAGCGCCATGGTCCTGCACCGCCCGGAGGAGGCC
GCGTGA
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)
[3-251] 4.80000000000003e-59 PF00109
PF00109   ketoacyl-synt
IPR014031 Beta-ketoacyl synthase, C-terminal (Domain)
[260-375] 3.2e-36 PF02801
PF02801   Ketoacyl-synt_C
IPR016038 Thiolase-like, subgroup (Domain)
[3-263] 1.20000000000001e-66 G3DSA:3.40.47.10 [270-418] 7.79999999999999e-52 G3DSA:3.40.47.10
G3DSA:3.40.47.10   Thiolase-like_subgr
IPR016039 Thiolase-like (Domain)
[2-257] 1.69998802370953e-68 SSF53901 [219-418] 2.60000517657733e-62 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
Grana_00250 Grana_00250   Grana_00270 Grana_00270
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