Rubra_00430 : CDS information

close this sectionLocation

Organism
StrainNRRL 3061 (=NBRC 14000)
Entry nameRubradirin
Contig
Start / Stop / Direction83,661 / 84,116 / + [in whole cluster]
83,661 / 84,116 / + [in contig]
Location83661..84116 [in whole cluster]
83661..84116 [in contig]
TypeCDS
Length456 bp (151 aa)
Click on the icon to see Genetic map.

close this sectionAnnotation

Category2.2 modification addition of starter unit
Productputative aminodehydroquinate dehydratase
Product (GenBank)putative aDHQ dehydratase
Gene
Gene (GenBank)rubJ
EC number
Keyword
  • AHBA
Note
Note (GenBank)
Reference
ACC
PmId
[18080113] Biosynthesis of rubradirin as an ansamycin antibiotic from Streptomyces achromogenes var. rubradiris NRRL3061. (Arch Microbiol. , 2008)
comment
Rubradirin生合成clusterの報告。

Table1>配列比較からの推定機能
RubJ(151aa): aDHQ dehydratase

rifamycin産生株で見つかっているAHBA biosynthetic genes, rifK, L, M, N, G, H, and Jの産物と高度な相同性を示す(rubNを除く)6つの遺伝子がrubradirin生合成gene clusterにある。
Related Reference
ACC
Q7BUF8
NITE
Rifam_00600
PmId
[11278540] Mutational analysis and reconstituted expression of the biosynthetic genes involved in the formation of 3-amino-5-hydroxybenzoic acid, the starter unit of rifamycin biosynthesis in amycolatopsis Mediterranei S699. (J Biol Chem. , 2001)
comment
2nd(Q7BUF8) 73%, 3e-55
Amycolatopsis mediterranei_rifJ
Aminodehydroquinate dehydratase
[Rifam_00600]putative aminodehydroquinate dehydratase

rifH, -G, and -J genesの遺伝子産物は shikimate biosynthesis pathwayに関連する酵素に似ている。rifH, G, Jの各mutantは成長に影響を与えないので、shikimate pathwayに直接関連しないことがわかる。また、mutantでもrifamycin B産生をある程度保つことから、shikimate pathwayのgeneが代替していると考えられる。
ACC
P43877
PmId
[8170389] Characterization of a 3-dehydroquinase gene from Actinobacillus pleuropneumoniae with homology to the eukaryotic genes qa-2 and QUTE. (Mol Microbiol. , 1994)
comment
97th(P43877) 47%, 4e-28
Actinobacillus pleuropneumoniae_aroQ
3-dehydroquinate dehydratase(EC 4.2.1.10)

HAMAP MF_00169 template

大腸菌aroD(classII)を相補するものとしてクローニングされた。aroDとは相同性がない。

close this sectionSequence

selected fasta
>putative aminodehydroquinate dehydratase [putative aDHQ dehydratase]
MTTVLLLNGPNLGILGDREPEIYGYDTVDDIAKSVADEVAEAGWQVVAIQDDHEGGLVQA
VHAHRRSTIGAIVNPGALMMAGWSLRDALAAYPAPWIEVHLSNVWARERFRHESVLAPLA
SGVVVGLGAFGYRLAARALLELCGPDPTHQS
selected fasta
>putative aminodehydroquinate dehydratase [putative aDHQ dehydratase]
GTGACCACCGTGCTCCTGCTCAACGGGCCCAACCTCGGAATACTCGGAGACCGCGAACCG
GAGATCTACGGCTACGACACCGTCGACGACATCGCGAAATCCGTCGCCGACGAGGTGGCC
GAGGCCGGCTGGCAGGTCGTCGCGATCCAGGACGACCACGAAGGAGGCCTGGTCCAGGCG
GTGCACGCGCACCGCAGGTCGACCATCGGCGCGATCGTCAACCCCGGCGCGCTCATGATG
GCCGGGTGGAGCCTGCGCGACGCGCTCGCCGCCTATCCCGCGCCGTGGATCGAGGTGCAC
CTGAGCAACGTCTGGGCCCGTGAGCGCTTCCGCCACGAATCGGTCCTGGCCCCGCTGGCC
AGCGGGGTCGTCGTGGGTCTCGGCGCGTTCGGCTACCGCCTGGCCGCCCGGGCGCTGCTG
GAGCTGTGCGGCCCCGATCCCACACACCAAAGCTAG

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09
show BLAST table
InterPro
Database:interpro:38.0
IPR001874 Dehydroquinase, class II (Family)
 [1-146]  6.89998448199219e-49 SSF52304
SSF52304   DHquinase_II
 [18-148]  PD004527
PD004527   DHquinase_II
 [1-143]  1.40000000000001e-53 G3DSA:3.40.50.9100
G3DSA:3.40.50.9100   DHquinase_II
 [1-145]  5.79999653854781e-60 PIRSF001399
PIRSF001399   DHquinase_II
 [3-140]  1.5e-48 PF01220
PF01220   DHquinase_II
IPR018509 Dehydroquinase, class II, conserved site (Conserved_site)
 [7-24]  PS01029
PS01029   DEHYDROQUINASE_II
SignalP No significant hit
TMHMM No significant hit
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