Azino_00330 : CDS information

close this sectionLocation

Organism
StrainNRRL 2485 (=NBRC 13928)
Entry nameAzinomycin B
Contig
Start / Stop / Direction49,525 / 50,274 / + [in whole cluster]
49,525 / 50,274 / + [in contig]
Location49525..50274 [in whole cluster]
49525..50274 [in contig]
TypeCDS
Length750 bp (249 aa)
Click on the icon to see Genetic map.

close this sectionAnnotation

Category1.4 Other
Productputative type II thioesterase
Product (GenBank)Azi33
GeneaziA8
Gene (GenBank)azi33
EC number
Keyword
Note
Note (GenBank)
  • thioesterase type II
Reference
ACC
PmId
[18635006] Characterization of the azinomycin B biosynthetic gene cluster revealing a different iterative type I polyketide synthase for naphthoate biosynthesis. (Chem Biol. , 2008)
comment
Azinomycin B生合成遺伝子クラスターの報告。

aziA8: Thioesterase

azinomycin Bのcluster内にdiscrete TEは3つあり(AziA6, AziA7, AziA8)。
AziA8に関してコメントない。
Related Reference
ACC
Q846W2
NITE
Monen_00290
PmId
[16984884] Identification of NanE as the thioesterase for polyether chain release in nanchangmycin biosynthesis. (Chem Biol. , 2006)
comment
Streptomyces cinnamonensis_monAX
Thioesterase

対照実験として。
MonAXはdiketide-SNACを加水分解したが、polyether-SNACを加水分解しなかった。
よって、polyether鎖の放出には関与しない。
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
Amycolatopsis mediterranei_rifR
RifR
rifamycinの生合成遺伝子

RifRは、acyl-CoAsよりも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がCoA基質よりACP基質への反応を好むことは、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 [Azi33]
MHRSDARLWFDGRFRSATATHSLYCLPFAGGSATYYADWAPHCASPVELVPVQLPGRGGR
MTESSAKDLVQLAEEIADTIAAEPTRTLLYGHSMGAMLAFEVSRRLQTLNRPVRHLFVSG
RPAPTIVRPIAPVSHLPRAEFIQMLRDYGAADQTVFEHDELLDLLMPMIRADFAMIENYR
YQEAPRLSCPISAWCGDADPEVPPTAMRGWGDQTSGEFTLSVLRGGHFFLTEHRAEIMRA
VLAAVRRAR
selected fasta
>putative type II thioesterase [Azi33]
GTGCACCGCTCCGACGCCCGGCTGTGGTTCGACGGCCGGTTCCGCTCCGCCACGGCGACA
CACAGTCTGTACTGCCTGCCCTTCGCCGGTGGTTCCGCGACCTACTACGCCGACTGGGCG
CCCCACTGCGCGAGCCCCGTCGAACTGGTGCCGGTGCAGCTGCCCGGCCGCGGTGGCCGC
ATGACCGAGTCGTCGGCCAAGGATCTGGTGCAGCTCGCCGAGGAGATCGCCGACACCATC
GCCGCCGAACCCACGCGGACCCTCCTGTACGGGCACAGTATGGGAGCCATGCTGGCGTTC
GAGGTGAGCCGACGGCTTCAGACGCTGAACCGGCCGGTGCGGCACCTCTTCGTCAGCGGC
CGCCCCGCGCCGACGATCGTGCGTCCGATCGCCCCCGTCAGCCACCTGCCCCGCGCCGAG
TTCATCCAGATGCTGCGCGACTACGGCGCCGCCGACCAGACGGTCTTCGAGCACGACGAA
CTGCTGGACCTGCTCATGCCGATGATCCGGGCGGACTTCGCCATGATCGAGAACTACCGG
TACCAGGAGGCACCGCGGCTCTCGTGCCCGATCTCCGCCTGGTGCGGAGACGCCGACCCG
GAGGTGCCTCCCACGGCGATGCGTGGCTGGGGCGACCAGACATCGGGAGAGTTCACCCTC
TCCGTGCTGCGAGGCGGGCACTTCTTCCTGACCGAGCACCGGGCCGAGATCATGCGGGCC
GTACTCGCCGCGGTCCGTCGAGCGCGTTGA

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09
show BLAST table
InterPro
Database:interpro:38.0
IPR001031 Thioesterase (Domain)
 [23-242]  1.2e-45 PF00975
PF00975   Thioesterase
SignalP No significant hit
TMHMM No significant hit
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