Vicen_00110 Vicen_00110   Vicen_00130 Vicen_00130

Vicen_00120 : CDS information

close this sectionLocation

Organism
StrainHC34
Entry nameVicenistatin
Contig
Start / Stop / Direction38,001 / 38,498 / + [in whole cluster]
38,001 / 38,498 / + [in contig]
Location38001..38498 [in whole cluster]
38001..38498 [in contig]
TypeCDS
Length498 bp (165 aa)
Click on the icon to see Genetic map.

close this sectionAnnotation

Category2.2 modification addition of starter unit
Productputative glutamate mutase S chain
Product (GenBank)glutamate mutase S-chain
Gene
Gene (GenBank)vinH
EC number
Keyword
Note
Note (GenBank)
Reference
ACC
PmId
[15112997] Cloning, sequencing, and functional analysis of the biosynthetic gene cluster of macrolactam antibiotic vicenistatin in Streptomyces halstedii. (Chem Biol. , 2004)
[16161486] Involvement of glutamate mutase in the biosynthesis of the unique starter unit of the macrolactam polyketide antibiotic vicenistatin. (J Antibiot (Tokyo). , 2005)
comment
[PMID: 15112997](2004)
vicenistatin生合成gene clusterの同定論文。

VinH (165aa) : glutamate mutase S subunit

配列解析からの機能推定。
VicenistatinのAglyconのスターターユニットである(2S,3S)-3-methylaspartateを合成する最初のステップを担う。VinI とともに、(S)-glutamateから(2S,3S)-3-methylaspartateへの変換を行う。

---
[PMID: 16161486](2005)
同じ著者らによる続報。

glutamate → 3-methylaspartateへ再編成するglutamate mutaseをコードするvinI を破壊したmutantはvicenistatin非産生。3-methylaspartateを添加すると産生回復。

また、このmutantはstarter unitのmethyl基を欠いた新規vicenistatin派生体(desmethylvicenistatins)を蓄積。このときのstarterは3-methylaspartateではなくaspartateに由来することをfeeding experimentsで確認。

VinHに関しては実験されていない。
Related Reference
ACC
Q7X542
PmId
[12543643] A glutamate mutase is involved in the biosynthesis of the lipopeptide antibiotic friulimicin in Actinoplanes friuliensis. (Antimicrob Agents Chemother. , 2003)
comment
9th, 51%, 5e-29
Actinoplanes friuliensis_glmA
Glutamate mutase subunit A

active enzymeは2つのsubunit GlmA and GlmBから成る。
異種性発現、disruption mutagenesisあり。

close this sectionSequence

selected fasta
>putative glutamate mutase S chain [glutamate mutase S-chain]
MPPHVRPMPDITSERLPDQDHHLPAERARPVLISSVASDSHTWNLVFLQLLIEELGHEVI
NLGPCVPDELLIAECRDRRPGLVVISTVNGHGYQDGLRVIGKLRACEDLANIPVVIGGKL
GVSGPGQSYAAELAGAGFDAVFPDGAEAVSSFTRYVEKLPQRVVS
selected fasta
>putative glutamate mutase S chain [glutamate mutase S-chain]
ATGCCGCCTCATGTCCGCCCGATGCCCGACATCACATCCGAACGGCTCCCGGACCAGGAC
CACCACCTGCCCGCCGAGCGTGCCCGGCCCGTGCTGATCAGCAGCGTCGCCTCCGACTCG
CACACCTGGAACCTGGTCTTCCTCCAACTGCTGATCGAGGAGCTGGGACACGAGGTCATC
AACCTCGGTCCCTGCGTGCCCGACGAACTGCTCATCGCCGAGTGCCGTGACCGCCGCCCC
GGCCTCGTCGTCATCAGCACCGTCAACGGCCACGGCTACCAGGACGGGCTACGGGTGATC
GGGAAACTGCGCGCCTGCGAGGACCTCGCGAACATCCCCGTCGTCATCGGCGGGAAGCTC
GGCGTCTCGGGCCCGGGTCAGTCGTACGCGGCCGAGTTGGCCGGCGCCGGGTTCGACGCG
GTGTTCCCCGACGGGGCGGAGGCCGTGTCCTCCTTCACCAGATACGTCGAGAAGCTCCCG
CAGCGAGTAGTGTCTTGA

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09 		show BLAST table
InterPro
Database:interpro:38.0
IPR006158 Cobalamin (vitamin B12)-binding (Domain)
[26-162] 6.79998707392904e-21 SSF52242
SSF52242   Cbl-bd
[31-149] 1.1e-10 PF02310
PF02310   B12-binding
[26-160] 2.2e-21 G3DSA:3.40.50.280
G3DSA:3.40.50.280   B12_bd
[28-165] PS51332
PS51332   B12_BINDING
SignalP No significant hit
TMHMM No significant hit
Vicen_00110 Vicen_00110   Vicen_00130 Vicen_00130
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