Griseo_00030 : CDS information

close this sectionLocation

Organism
StrainJP95
Entry nameGriseorhodin A
Contig
Start / Stop / Direction3,315 / 4,130 / + [in whole cluster]
3,315 / 4,130 / + [in contig]
Location3315..4130 [in whole cluster]
3315..4130 [in contig]
TypeCDS
Length816 bp (271 aa)
Click on the icon to see Genetic map.

close this sectionAnnotation

Category1.4 Other
Productputative type II thioesterase
Product (GenBank)putative thioesterase GrhD
Gene
Gene (GenBank)grhD
EC number
Keyword
  • type II thioesterase
Note
Note (GenBank)
Reference
ACC
PmId
[12323376] A gene cluster from a marine Streptomyces encoding the biosynthesis of the aromatic spiroketal polyketide griseorhodin A. (Chem Biol. , 2002)
[19175308] Cleavage of four carbon-carbon bonds during biosynthesis of the griseorhodin a spiroketal pharmacophore. (J Am Chem Soc. , 2009)
comment
[PMID: 12323376](2002)
griseorhodin A生合成gene clusterのクローニング、シークエンス、異種性発現。

grhD: Thioesterase
配列解析のみ。

--
[PMID: 19175308](2009)
grhD mutantでもgriseorhodin A産生可能。
Related Reference
ACC
Q7BUF9
NITE
Rifam_00540
PmId
[19103602] Structure and functional analysis of RifR, the type II thioesterase from the rifamycin biosynthetic pathway. (J Biol Chem. , 2009)
comment
Blast 190th, id32%, 1e-19
Amycolatopsis mediterranei_rifR
RifR
[DoBISCUIT]type II thioesterase

RifRは、acyl-CoAsよりacyl carrier domainのphosphopantetheinyl armからのacyl unitsを加水分解する(Steady-state kinetics)。
helical lidの運動が、RifR active siteへの基質のアクセスを調節する(立体構造解析)。

RifRはCoA基質よりACP基質への反応を好む。これはtype II thioesteraseがcarrier domainsから異常unitsを除くようなhousekeeping functionsをすると考えられていることに一致する。

close this sectionSequence

selected fasta
>putative type II thioesterase [putative thioesterase GrhD]
MAGTEPAVRLYCFAHAGAGDSVFHRWARSTGEGVEPVPVLLPGRGGRRREPRLTDHDSLV
AHLLDRVRVPAGQSYALYGHSLGAMVAHALAGALREEGLPLPSFVAVGACPPPDAASRLS
DACESSDEELVEALDRLGALPEGVAARGYWRRASLPVLRDDLRLAGALRAAARASAPERG
PLSVPLLAVSGSRDPLVSPATVGGWRRWTSGPVAARTVPGDHFFVRGEALPRLIGRACRV
VRRLEAGTGVGNGRWPAETVPPYIREPAVHP
selected fasta
>putative type II thioesterase [putative thioesterase GrhD]
ATGGCGGGCACGGAACCAGCGGTTCGGCTGTACTGCTTCGCCCACGCGGGGGCAGGGGAC
TCGGTGTTCCACCGGTGGGCCCGGAGCACGGGTGAGGGCGTCGAGCCCGTGCCCGTGCTG
CTGCCGGGCCGTGGCGGGCGGCGGCGCGAGCCGCGCCTGACCGACCACGACTCCCTGGTC
GCGCATCTGCTGGACCGCGTCCGCGTCCCGGCCGGACAGTCCTACGCGCTGTACGGGCAC
AGCCTCGGGGCGATGGTGGCCCACGCCCTCGCCGGGGCGCTGCGCGAGGAGGGGCTGCCG
CTTCCGTCGTTCGTCGCCGTGGGGGCCTGCCCGCCCCCGGACGCGGCCAGCAGGCTCTCC
GACGCCTGCGAGAGCTCCGACGAGGAGCTGGTGGAGGCGCTGGACCGGCTGGGGGCCCTG
CCCGAGGGCGTTGCGGCACGGGGGTACTGGCGGCGGGCCTCACTGCCCGTGCTCCGCGAC
GACCTGCGGCTGGCCGGCGCGCTCCGCGCCGCCGCCCGCGCGTCGGCGCCGGAGCGCGGA
CCGCTGTCCGTCCCGCTGCTCGCGGTGTCCGGAAGCCGTGACCCGCTGGTGTCGCCCGCG
ACGGTCGGCGGCTGGCGCCGGTGGACCTCCGGGCCGGTGGCGGCCCGTACCGTGCCCGGC
GACCACTTCTTCGTACGCGGTGAGGCGCTTCCCCGGCTGATCGGCCGGGCCTGCCGCGTC
GTGCGGCGGCTCGAAGCCGGGACCGGGGTCGGGAACGGGCGGTGGCCGGCGGAGACGGTC
CCGCCGTACATCCGTGAGCCCGCCGTACATCCCTGA

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09
show BLAST table
InterPro
Database:interpro:38.0
IPR001031 Thioesterase (Domain)
 [9-234]  9.9e-33 PF00975
PF00975   Thioesterase
SignalP
 [1-19]  0.145 Signal
Eukaryota   
TMHMM No significant hit
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