Herb_00040 Herb_00040   Herb_00060 Herb_00060

Herb_00050 : CDS information

close this sectionLocation

Organism
StrainAM 3672
Entry nameHerbimycin A
Contig
Start / Stop / Direction6,852 / 5,026 / - [in whole cluster]
6,852 / 5,026 / - [in contig]
Locationcomplement(5026..6852) [in whole cluster]
complement(5026..6852) [in contig]
TypeCDS
Length1,827 bp (608 aa)
Click on the icon to see Genetic map.

close this sectionAnnotation

Category5.1 general function
Productputative amide synthetase
Product (GenBank)unknown
Gene
Gene (GenBank)
EC number
Keyword
Note
Note (GenBank)
  • ORF5p; ORF5; similar to Streptomyces aureofaciens TcsG (asparagine synthase)
Reference
ACC
PmId
[16085885] Insights into the biosynthesis of the benzoquinone ansamycins geldanamycin and herbimycin, obtained by gene sequencing and disruption. (Appl Environ Microbiol. , 2005)
comment
herbimycin生合成系gene clusterのクローニングを行い、同じbenzoquinone ansamycin系のgeldanamycin のgene clusterと比較し、一部の遺伝子欠損株を作成してその生合成における関与を調べた文献。

ORF05(1827bp):asparagine synthase family
機能実験、詳細記載無し。
Related Reference
ACC
Q3S8R1
NITE
Oxtet_00050
PmId
[16597959] Engineered biosynthesis of a novel amidated polyketide, using the malonamyl-specific initiation module from the oxytetracycline polyketide synthase. (Appl Environ Microbiol. , 2006)
[21622525] Genetic characterization of enzymes involved in the priming steps of oxytetracycline biosynthesis in Streptomyces rimosus. (Microbiology. , 2011)
comment
Blast 51st, id49%, 1e-149
Streptomyces rimosus_oxyD
OxyD

---
[PMID:16597959](2006)
tetracyclines生合成はユニークなmalonamate starter unitでprimeされる。
amidated polykeidesの生合成にはoxy minimal PKS + oxyDで必要十分であることを異種性発現で確認。

OxyDはmalonyl-CoA or malonyl-ACPをamidateしてmalonamyl-CoA or malonamyl-ACPを得て、それから鎖伸長のためのoxy KS-CLFをprimeすると考えられている。

---
[PMID:21622525](2011)
malonamate-primed oxytetracycline (OTC)の代わりにacetate-primed 2-acetyl-2-decarboxyamido-oxytetracycline (ADOTC)を産生するStreptomyces rimosus ATCC 13224の配列解析と相補から、amide starter unitの合成にはOxyDが必須で、その活性には特にD268Nが関連することを明らかにしている(当ORFでも保存あり)。

この他にthiolase OxyPの役割も確認している。
ACC
Q2MGB4
NITE
Fred_00250
PmId
[20926388] Characterization of FdmV as an amide synthetase for fredericamycin A biosynthesis in Streptomyces griseus ATCC 43944. (J Biol Chem. , 2010)
comment
Blast 101st, id45%, 1e-131
Streptomyces griseus
Asparagine synthetase(EC 6.3.5.4)
[DoBISCUIT]amide synthetase_fdmV

fdmV不活化mutantはFredericamycin(FDM) A and 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。
ACC
O05272
PmId
[10498721] Three asparagine synthetase genes of Bacillus subtilis. (J Bacteriol. , 1999)
comment
Blast 174th, id39%, 1e-128
Bacillus subtilis_asnO
Asparagine synthetase [glutamine-hydrolyzing] 3 (EC 6.3.5.4)

asparagine synthetase遺伝子(asnB, asnH, and asnO)について調べた文献。
asnOに関しては、rich sporulation mediumにおいてはsporulation後期にのみ発現すること、minimal mediumではasnOは発現しないこと、monocistronic operonで発現はsigma-Eに依存すること、Escherichia coli のasparagine synthetasesを相補することが示されている。

close this sectionSequence

selected fasta
>putative amide synthetase [unknown]
MCGITGWVSFHQDPRTQAPVIEAMTATLAPRGPDAAGVWLGPRAAIGHRRLAVIDLAGGV
QPMTDRPDAPTTVLTYSGEIYNHHELRSQLSGLGHEFRTRSDTEVVLRGYAEWGEKVADH
LDGMFAFAVWDERAQRLLLVRDRLGVKPLFWAEVDGGLAFASEPKALFAHPEIRPRVDAD
GLREAYSLLFNTGPTVWSGVREVEPGGLLLLDRDGIRERRYWQLEADAHPDDRDATIARV
HDLVSTAARAQLEADVPLCSLLSGGIDSTVLTALLADELRLREGPGARIRSYAVDYSDQA
ESFTGDVLRTGHDTPYATEAGAFLGTDHSTVVLDPRALLDPEHRRAVVVARDSPIGVGDM
DTSLHLLFGEIRKHSTVALSGEAADEVFGGYPWFHNPKALATATFPWLLVTGDEAAMPLN
PELDLRIGEFRDDTYRTALAAVPHLDGETPTEHRQREMQHLSLTRWLRQLLHRKDRLSMA
QGLEVRVPYCDHRLVEYAFTTPWALKNFDGREKSLLRAAGTGLAPDSVLHRPKNHYPATH
HPDYNRGLQNMARDALADDTVRSLADETRLKPCLDTPPGQLEWGHRLRLERVVDLALWLD
HYQPELAL
selected fasta
>putative amide synthetase [unknown]
ATGTGCGGAATCACCGGCTGGGTGTCCTTTCACCAGGACCCCCGCACCCAGGCCCCGGTC
ATCGAGGCCATGACCGCCACCCTGGCCCCGCGCGGCCCCGACGCGGCCGGAGTCTGGCTC
GGCCCGCGCGCCGCGATCGGCCACCGCCGCCTGGCCGTCATCGACCTCGCCGGTGGCGTC
CAGCCGATGACCGACCGGCCCGACGCCCCGACCACCGTGCTCACCTACAGCGGCGAGATC
TACAACCACCATGAACTCCGCTCACAACTGAGCGGCCTGGGACACGAGTTCCGCACCCGC
AGCGACACCGAGGTGGTGCTGCGCGGCTACGCCGAGTGGGGCGAGAAGGTGGCCGACCAC
CTGGACGGCATGTTCGCGTTCGCCGTCTGGGACGAGCGGGCCCAGCGGCTGCTCCTGGTC
CGCGACCGGCTCGGCGTCAAGCCCCTCTTCTGGGCGGAGGTGGACGGCGGTCTGGCCTTC
GCCTCCGAACCCAAGGCGCTCTTCGCCCATCCGGAGATACGGCCACGGGTGGACGCGGAC
GGGCTGCGCGAGGCGTACAGCCTGCTGTTCAACACCGGTCCGACGGTGTGGTCCGGCGTG
CGGGAGGTCGAGCCCGGCGGTCTGCTCCTCCTGGACCGGGACGGCATCCGCGAGCGCCGC
TACTGGCAGTTGGAGGCCGACGCCCACCCGGACGACCGGGACGCGACCATCGCCCGGGTG
CACGACCTGGTGAGCACCGCCGCCCGCGCCCAGCTCGAGGCCGACGTCCCCCTGTGCTCC
CTGCTGTCGGGCGGCATCGACTCCACCGTCCTGACCGCCCTGCTCGCCGACGAACTGCGG
CTGCGCGAGGGCCCGGGCGCGCGTATCCGCTCCTACGCCGTCGACTACAGCGACCAGGCC
GAGAGCTTCACCGGTGATGTGCTGCGCACCGGCCACGACACCCCGTACGCCACCGAAGCG
GGCGCGTTCCTCGGCACCGACCACAGCACGGTGGTACTGGACCCGCGTGCCCTGCTCGAC
CCCGAGCACCGCAGGGCCGTGGTCGTGGCCCGCGACTCGCCGATCGGCGTCGGCGACATG
GACACCTCGCTCCACCTCCTCTTCGGGGAGATCCGGAAGCACTCCACGGTCGCCCTGTCC
GGCGAGGCGGCCGACGAGGTCTTCGGCGGCTACCCCTGGTTCCACAACCCCAAGGCGCTC
GCCACCGCCACCTTTCCCTGGCTGCTGGTGACCGGAGACGAGGCCGCGATGCCGCTCAAC
CCCGAACTGGACCTGCGCATCGGCGAGTTCCGGGACGACACCTATCGCACCGCCCTGGCC
GCCGTACCGCACCTCGACGGCGAGACGCCCACCGAGCACCGGCAGCGCGAGATGCAGCAC
CTCTCGCTCACCCGCTGGCTGCGTCAACTCCTCCACCGCAAGGACCGGTTGAGCATGGCC
CAGGGCCTGGAGGTGCGCGTCCCCTACTGCGATCACCGGCTTGTCGAGTACGCCTTCACC
ACCCCCTGGGCCCTGAAGAACTTCGACGGCCGGGAGAAGAGCCTGCTGCGTGCGGCGGGC
ACCGGACTGGCCCCCGACTCGGTGCTGCACCGCCCCAAGAACCACTACCCGGCCACCCAC
CACCCCGACTACAACCGCGGCCTGCAGAACATGGCCCGCGACGCCCTCGCCGACGACACC
GTCCGCTCCCTCGCCGACGAGACCCGCCTCAAACCCTGCCTCGACACCCCGCCCGGCCAA
CTGGAGTGGGGCCACCGCCTCCGCCTCGAACGCGTCGTCGACCTCGCCCTGTGGCTGGAC
CACTACCAGCCCGAACTCGCCCTCTGA

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09 		show BLAST table
InterPro
Database:interpro:38.0
IPR000583 Class II glutamine amidotransferase domain (Domain)
[48-168] 4.70000000000003e-45 PF13537
PF13537   GATase_7
IPR001962 Asparagine synthase (Domain)
[240-533] 1.40000000000001e-58 PF00733
PF00733   Asn_synthase
IPR006426 Asparagine synthase, glutamine-hydrolyzing (Family)
[2-536] TIGR01536
TIGR01536   Asn_synth_AEB
[1-607] 1.50000965748778e-124 PIRSF001589
PIRSF001589   Asn_synthetase_glu-h
IPR014729 Rossmann-like alpha/beta/alpha sandwich fold (Domain)
[223-395] 4.49999999999996e-68 G3DSA:3.40.50.620 [452-586] 4.49999999999996e-68 G3DSA:3.40.50.620
G3DSA:3.40.50.620   Rossmann-like_a/b/a_fold
IPR017932 Glutamine amidotransferase type 2 domain (Domain)
[2-214] PS51278
PS51278   GATASE_TYPE_2
SignalP
[1-18] 0.116 Signal
Eukaryota   
TMHMM No significant hit
Herb_00040 Herb_00040   Herb_00060 Herb_00060
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