Vicen_00120 Vicen_00120   Vicen_00140 Vicen_00140

Vicen_00130 : CDS information

close this sectionLocation

Organism
StrainHC34
Entry nameVicenistatin
Contig
Start / Stop / Direction38,495 / 39,904 / + [in whole cluster]
38,495 / 39,904 / + [in contig]
Location38495..39904 [in whole cluster]
38495..39904 [in contig]
TypeCDS
Length1,410 bp (469 aa)
Click on the icon to see Genetic map.

close this sectionAnnotation

Category2.2 modification addition of starter unit
Productglutamate mutase E chain
Product (GenBank)glutamate mutase E-chain
Gene
Gene (GenBank)vinI
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。

VinI (469aa) : glutamate mutase E 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。VinH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。
Related Reference
ACC
Q7X543
PmId
[12543643] A glutamate mutase is involved in the biosynthesis of the lipopeptide antibiotic friulimicin in Actinoplanes friuliensis. (Antimicrob Agents Chemother. , 2003)
comment
7th, 55%, 1e-113
Actinoplanes friuliensis_glmB
Glutamate mutase subunit B

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
>glutamate mutase E chain [glutamate mutase E-chain]
MTGFGAYVRSVHRRGELVVQPRMGFSGTVEMRAGLAATRAADAATVGTITLDSYTRVGEL
AAAEEALRSGIALNGYPIVTYDESTTRELLAGIAGEDFPVQIRHGSATPLHIFGALTRAG
LDATEGGPVSYCLPYGRIPLEQSVTNWTRCCEEFARLRGLGREPHLETFGGCMLGQLCPP
SQLVAISMLEALFFHQHGIRSISLSYAQQTHQGQDEEAVLALRRLHRELLPDADCHIVIY
AYMGVYPTTPEGAHALLGRAAELAVATGAERLIVKTAAEAHRIPTIGENVAALEHAATVS
RAARRATALPAGHSAAPAATDPTAALTARPGTYADGSAALTAGPGAAADGSTDSAVYAEA
RALIEAVMNCGPDVGTALFRAFKRGYLDIPYCLHPDNMGRSRSYIDDTGRLQWAETGMLP
LGNARKSGTGRSVSSTDLISALSFVQRTYDQLAFPESREPLRIPRQQRP
selected fasta
>glutamate mutase E chain [glutamate mutase E-chain]
TTGACCGGATTCGGCGCCTACGTCCGCTCCGTCCACCGGCGCGGCGAACTCGTCGTCCAG
CCGCGGATGGGATTCAGCGGTACGGTCGAGATGCGCGCCGGTCTCGCCGCGACCCGGGCG
GCGGACGCGGCCACGGTCGGCACCATCACCCTGGACAGCTACACCCGGGTCGGGGAACTC
GCCGCAGCCGAGGAGGCACTCCGCTCCGGCATCGCCCTCAACGGCTACCCCATCGTCACC
TACGACGAATCCACCACCCGTGAACTCCTCGCCGGGATCGCGGGTGAGGACTTCCCCGTT
CAGATCCGGCACGGGTCGGCGACCCCCCTGCACATCTTCGGCGCGCTGACCCGCGCGGGC
CTGGACGCCACCGAGGGCGGCCCCGTCTCCTACTGCCTGCCCTACGGCCGGATTCCGCTG
GAACAGTCGGTGACCAACTGGACCCGCTGCTGCGAGGAGTTCGCCCGGCTGCGCGGGCTG
GGCCGTGAACCGCATCTGGAGACCTTCGGCGGCTGCATGCTCGGGCAGCTCTGCCCGCCC
AGCCAGCTCGTCGCCATCAGCATGCTCGAAGCGCTCTTCTTCCACCAGCACGGCATTCGC
AGCATCTCCCTCAGCTACGCCCAGCAGACCCATCAGGGACAGGACGAGGAAGCCGTGCTG
GCGCTGCGCCGGCTCCACCGCGAACTGCTGCCCGATGCCGACTGCCACATCGTCATCTAC
GCCTATATGGGGGTCTATCCGACCACCCCCGAGGGGGCCCACGCACTGCTGGGCCGGGCC
GCCGAACTCGCCGTCGCCACCGGGGCCGAGCGGCTCATCGTCAAGACCGCGGCCGAGGCC
CACCGCATCCCCACCATCGGGGAGAACGTGGCGGCCCTGGAGCACGCGGCCACCGTGTCC
CGCGCCGCCCGCCGGGCCACCGCGCTCCCGGCCGGTCACTCCGCTGCGCCCGCTGCCACC
GACCCCACCGCCGCGCTCACGGCCCGACCCGGTACGTACGCGGACGGATCCGCCGCGCTC
ACAGCGGGCCCCGGCGCCGCCGCGGACGGCTCCACCGACTCCGCCGTCTACGCGGAGGCC
CGCGCCCTCATCGAAGCCGTCATGAACTGCGGACCGGATGTCGGCACCGCACTGTTCCGC
GCTTTCAAGAGGGGATACCTGGACATCCCCTACTGCCTCCACCCCGACAACATGGGCCGC
AGCCGGAGTTACATCGACGACACCGGGCGGCTGCAATGGGCGGAGACCGGAATGCTGCCC
CTGGGGAATGCCAGAAAAAGCGGAACAGGCCGCTCGGTATCGTCAACCGATCTGATATCG
GCCCTTTCCTTCGTGCAGCGGACCTATGACCAACTGGCATTTCCGGAATCCCGGGAGCCG
CTCCGGATACCCCGGCAGCAGCGCCCCTAG

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09 		show BLAST table
InterPro
Database:interpro:38.0
IPR006396 Glutamate mutase, E subunit (Family)
[4-305] 3.99999999999998e-86 PF06368 [352-424] 7.4e-12 PF06368
PF06368   Met_asp_mut_E
[1-467] 2.80000504261099e-129 PIRSF001495
PIRSF001495   Met_asp_mut_epsi
IPR014348 Cobalamin (vitamin B12)-dependent enzyme, catalytic subdomain (Domain)
[4-312] 9.39999999999981e-114 G3DSA:3.20.20.240 [348-400] 9.39999999999981e-114 G3DSA:3.20.20.240
G3DSA:3.20.20.240   Cobalamin-dep_enz_cat
IPR016176 Cobalamin (vitamin B12)-dependent enzyme, catalytic (Domain)
[4-465] 1.09999184471405e-126 SSF51703
SSF51703   Cbl-dep_enz_cat
SignalP No significant hit
TMHMM No significant hit
Vicen_00120 Vicen_00120   Vicen_00140 Vicen_00140
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