Fred_00240 Fred_00240   Fred_00260 Fred_00260

Fred_00250 : CDS information

close this sectionLocation

Organism
StrainATCC 49344
Entry nameFredericamycin
Contig
Start / Stop / Direction20,468 / 22,336 / + [in whole cluster]
20,468 / 22,336 / + [in contig]
Location20468..22336 [in whole cluster]
20468..22336 [in contig]
TypeCDS
Length1,869 bp (622 aa)
Click on the icon to see Genetic map.

close this sectionAnnotation

Category3.4 other modification
Productamide synthetase
Product (GenBank)asparagine synthetase
GenefdmV
Gene (GenBank)
EC number
Keyword
Note
Note (GenBank)
  • FdmV
Reference
ACC
PmId
[16305230] Cloning, sequencing, analysis, and heterologous expression of the fredericamycin biosynthetic gene cluster from Streptomyces griseus. (J Am Chem Soc. , 2005)
[20926388] Characterization of FdmV as an amide synthetase for fredericamycin A biosynthesis in Streptomyces griseus ATCC 43944. (J Biol Chem. , 2010)
comment
[PMID: 16305230](2005)
Fredericamycin(FDM) gene clusterの同定論文。

fdmV: asparagine synthetase

TcsG, RubR, GrhPといったasparagine synthetasesのfamilyに高い配列類似あり。
TcsGはchlorotetracycline生合成に関与すると提唱されているので、FdmVはたぶんFDM Aの2-pyridone部分(F環)を産出するためにアミノ基をAAからpolyketide中間体へ移動する。

fdmC-fdmT3のfragmentをS.albusへ導入し、FDM-A産生に十分であることを確認している。

---
同じ著者らの続報。
[PMID: 20926388](2010)
fdmV不活化mutantはFDM A and FDM E産生せず、amide結合を欠いたFDM Cを蓄積。

vitroでFdmVは、FDM C→FDM Bへの変換を触媒する。
K(m) = 162 ± 67 μM and k(cat) = 0.11 ± 0.02 min(-1)
また、FDM Cの構造的analogであるFDM M-3のamidationも触媒してamide FDM M-6を産生するが効率は低い。

FdmVは、nitrogen donorとしてclass II glutamine amidotransferasesに共通のL-Gln と遊離amineに加えてL-Asnも利用できる。

FDM A生合成におけるamide結合形成は、carbaspirocycle形成の前で、C-8 hydroxylationの後に起こると提唱される。

close this sectionSequence

selected fasta
>amide synthetase [asparagine synthetase]
MCGIAGWVVRQDGRPREDPAVAEAMAGAMACRGPDEQGVRGGRHVTLVHTRMAVIDLLGG
RQPMAADESEDPAATLTYCGEIYNAAELRSDLAGRGHRFRTRSDTEVVLRAYLEWGERCP
ERLEGMFAFAVWDARTRSLFLARDRFGVKPLYYAETGDGLVFGSEPKALLVHSDVSPEVD
LDGLRVLFSMARAPGECVYRSLSDLPPAHTLRFGPDGRLSLRRYWQLEARPHEEDLAGTV
ATVRGLLESSVARELVSDVPLSVLLSGGLDSSTVAALAARALADGDGGPVRTTTVTYSGY
GDNFQPDLVRSAPDSPYARAVAEHIGAEHLEIELTTADLIDPVARRTVLRAQDVPAPFGD
MDTSTYQAFAGVRRHSRVALTGESADEIFGGYSWVHIPDLAHEEQFPWVAFEQWHPGTRR
GLGQGLLSPAFKDRLDMGSYYAERYAQAMSRIPRLPREGEEERRAREICDLHLTHWLPRL
LERNDRLSMVSGLEVRVPFCDHRLVQYAYNIPWAMKTFDGREKSVLRAAARDLLPERVLD
RPKAPFPVSQDATYTKALHQELTEVLADPASPVLPLLDLEAARAVVAREGGADLQDWLHR
MNVEMVLQVDAWLRELGGDVEL
selected fasta
>amide synthetase [asparagine synthetase]
ATGTGCGGCATCGCAGGCTGGGTGGTCCGCCAGGACGGAAGGCCCCGGGAGGACCCGGCG
GTGGCCGAGGCGATGGCCGGCGCCATGGCCTGCCGGGGCCCTGACGAGCAGGGTGTCCGC
GGCGGCCGGCACGTGACGCTGGTGCATACGCGGATGGCCGTCATCGACCTGCTCGGCGGG
CGCCAGCCGATGGCTGCGGACGAGAGCGAGGACCCGGCCGCCACGCTCACCTACTGCGGC
GAGATCTACAACGCCGCCGAACTACGCTCCGACCTGGCCGGACGGGGGCACCGGTTCCGC
ACCCGCAGTGATACCGAGGTGGTGCTGCGGGCGTATTTGGAGTGGGGCGAGCGCTGCCCC
GAGCGGCTGGAGGGGATGTTCGCCTTCGCCGTCTGGGACGCCCGCACGCGCTCCCTGTTC
CTCGCCCGCGACCGCTTCGGCGTCAAGCCGCTGTACTACGCCGAGACCGGCGACGGGCTG
GTCTTCGGGTCCGAGCCCAAGGCGCTGCTCGTCCACTCGGACGTGAGCCCCGAGGTCGAC
CTCGACGGGCTGCGCGTGCTGTTCTCCATGGCCCGAGCGCCCGGCGAGTGCGTCTACCGC
TCCCTCAGCGACCTGCCGCCCGCCCACACGCTGCGTTTCGGGCCCGACGGCCGGCTGTCG
CTGCGCCGGTACTGGCAGCTGGAGGCCCGGCCGCACGAGGAGGATCTGGCCGGGACGGTC
GCGACCGTGCGCGGGCTGCTGGAGAGCAGCGTCGCCCGGGAACTGGTCTCGGACGTCCCG
CTGAGCGTGCTGCTCTCGGGCGGCCTCGACTCCAGCACCGTGGCCGCGCTGGCGGCCAGG
GCCCTGGCGGACGGCGACGGCGGACCGGTGCGCACGACCACCGTGACGTACAGCGGTTAC
GGCGACAACTTCCAGCCCGACCTGGTGCGCAGCGCTCCCGACTCCCCGTACGCCCGTGCC
GTCGCCGAGCACATCGGTGCCGAGCACCTAGAGATCGAGCTGACCACCGCCGACCTGATC
GACCCGGTGGCCCGCCGCACCGTCCTGCGCGCCCAGGACGTCCCCGCCCCGTTCGGCGAC
ATGGACACCTCGACGTACCAGGCGTTCGCGGGCGTGCGCCGGCACTCCAGGGTGGCGCTG
ACCGGGGAGAGCGCCGACGAGATCTTCGGCGGCTACAGCTGGGTCCACATCCCCGACCTG
GCCCATGAGGAGCAATTCCCCTGGGTCGCCTTCGAGCAGTGGCATCCGGGTACGCGCCGG
GGGCTGGGCCAGGGGCTGCTCTCCCCGGCCTTCAAGGACCGGCTGGACATGGGCTCGTAC
TACGCCGAGCGGTACGCGCAGGCCATGTCCCGGATACCGCGGCTGCCGAGGGAGGGCGAG
GAGGAGCGCCGGGCCCGGGAGATCTGCGACCTGCACCTGACGCACTGGCTGCCACGGCTG
CTGGAGCGTAACGACCGGCTGAGCATGGTCTCGGGCCTGGAGGTCCGGGTGCCGTTCTGC
GACCACCGGCTGGTCCAGTACGCGTACAACATCCCCTGGGCGATGAAGACCTTCGACGGA
CGGGAGAAGAGCGTGCTGCGGGCCGCCGCCCGCGATCTGCTGCCCGAACGTGTGCTCGAC
CGGCCCAAGGCGCCCTTCCCGGTGAGCCAGGACGCGACGTACACCAAGGCCCTCCACCAG
GAACTCACCGAGGTGCTGGCCGACCCCGCCTCCCCGGTCCTGCCGCTGCTGGACCTGGAG
GCGGCGCGCGCCGTGGTCGCCCGGGAGGGGGGAGCTGACCTCCAGGACTGGCTGCACCGG
ATGAACGTGGAGATGGTGCTCCAGGTCGACGCCTGGCTCCGGGAGCTCGGGGGCGACGTC
GAGCTGTGA

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09 		show BLAST table
InterPro
Database:interpro:38.0
IPR000583 Class II glutamine amidotransferase domain (Domain)
[49-170] 1.2e-45 PF13537
PF13537   GATase_7
IPR001962 Asparagine synthase (Domain)
[243-543] 9.39999999999981e-67 PF00733
PF00733   Asn_synthase
IPR006426 Asparagine synthase, glutamine-hydrolyzing (Family)
[2-546] TIGR01536
TIGR01536   Asn_synth_AEB
[1-620] 1.09999184471405e-117 PIRSF001589
PIRSF001589   Asn_synthetase_glu-h
IPR014729 Rossmann-like alpha/beta/alpha sandwich fold (Domain)
[226-396] 1.10000000000001e-73 G3DSA:3.40.50.620 [462-613] 1.10000000000001e-73 G3DSA:3.40.50.620
G3DSA:3.40.50.620   Rossmann-like_a/b/a_fold
IPR017932 Glutamine amidotransferase type 2 domain (Domain)
[2-216] PS51278
PS51278   GATASE_TYPE_2
SignalP
[1-24] 0.078 Signal
Bacteria, Gram-positive   
TMHMM No significant hit
Fred_00240 Fred_00240   Fred_00260 Fred_00260
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