Avil_00380 : CDS information

close this sectionLocation

Organism
StrainTü57
Entry nameAvilamycin
Contig
Start / Stop / Direction36,954 / 37,916 / + [in whole cluster]
36,954 / 37,916 / + [in contig]
Location36954..37916 [in whole cluster]
36954..37916 [in contig]
TypeCDS
Length963 bp (320 aa)
Click on the icon to see Genetic map.

close this sectionAnnotation

Category3.3 modification reduction
Productputative 2-oxo acid dehydrogenase E1 component beta subunit
Product (GenBank)putative pyruvate dehydrogenase
Gene
Gene (GenBank)aviB2
EC number
Keyword
  • eurekanate
  • acetyl group
Note
Note (GenBank)
  • AviB2
Reference
ACC
PmId
[11410376] Biosynthesis of the orthosomycin antibiotic avilamycin A: deductions from the molecular analysis of the avi biosynthetic gene cluster of Streptomyces viridochromogenes Tu57 and production of new antibiotics. (Chem Biol. , 2001)
[15640214] Genes involved in formation and attachment of a two-carbon chain as a component of eurekanate, a branched-chain sugar moiety of avilamycin A. (Appl Environ Microbiol. , 2005)
comment
[PMID:11410376]
Avilamycin生合成遺伝子クラスターの報告。

AviB2: Pyruvate dehydrogenase (beta chain) from C. magnum [Proposed function:Modification]

AviB1とAviB2でvarious 2-oxo-acid dehydrogenase complexesを形成していると推測。


[PMID:15640214]
AviB1,AviB2,AviO1,AviO2,AviO3の機能解析の報告。

各欠損株を作製し、NMRにて構造解析を行っている。
AviB1,AviB2は相同性や保存配列から、pyruvate dehydrogenaseのheterotetrameric E1 (alpha2beta2) complexであるとしている。
aviB1 mutantで検出したavilamycin誘導体はeurekanateのC-4 positionでacetyl groupを欠いていた。
AviB1,AviB2はpyruvate をacetyl carbanionへ変換する反応を担うタンパクをエンコードすると示した。
Related Reference
ACC
Q46143
PmId
[8206840] ( , )
comment
Clostridium magnum
TPP-dependent acetoin dehydrogenase beta-subunit_acoB

acoA+acoB plasmidをE.coliへ導入。
acetoin dehydrogenase 活性を示した。

close this sectionSequence

selected fasta
>putative 2-oxo acid dehydrogenase E1 component beta subunit [putative pyruvate dehydrogenase]
MAALAYITALNQALHDEMARDDRVCVFGEDVRIGLTQVAKGLHERFGDGRVVDTPLSEQA
FTSLATGAAMAGQRPVVEYQIPSLLYLVFEQIANQAHKFSLMTGGQVEVPVTYLVPGSGS
RSGMAGQHSDHPYSLFAHVGIKTVLPATASDAYGLLLSAVRDPDPVAVFAPSALMGTVEE
VSGELGPVPLGSARIHRTGEDVTVVATGQCVHVALAVAEAMADEASIEVVDPRTIYPVDW
ETIRASAEKTGRLVVIDDANRMCGFGGEVLATAAEQFDLTARPRRVTRPDGAVIPYALVL
DQALLPDAAQLTDAIRAVLK
selected fasta
>putative 2-oxo acid dehydrogenase E1 component beta subunit [putative pyruvate dehydrogenase]
ATGGCTGCACTTGCGTACATCACCGCGCTGAACCAGGCGCTGCACGACGAGATGGCGCGC
GACGACCGCGTCTGCGTCTTCGGCGAGGACGTGCGGATCGGCCTCACCCAGGTCGCCAAG
GGCCTGCACGAGCGCTTCGGCGACGGACGCGTCGTCGACACCCCCCTGTCGGAGCAGGCC
TTCACCAGCCTGGCCACCGGCGCGGCGATGGCGGGGCAGCGACCGGTCGTGGAGTACCAG
ATCCCCTCGCTGCTCTATCTGGTGTTCGAGCAGATCGCCAACCAGGCGCACAAGTTCTCG
CTGATGACCGGTGGGCAGGTGGAGGTCCCGGTCACCTATCTGGTGCCGGGCTCCGGTTCG
CGCTCGGGCATGGCCGGCCAGCACTCCGACCATCCCTACAGCCTGTTCGCACACGTCGGC
ATCAAGACGGTCCTGCCCGCCACCGCCTCGGACGCCTACGGCCTGCTGCTCTCGGCGGTC
CGTGACCCGGACCCGGTGGCCGTCTTCGCGCCGAGCGCGCTGATGGGCACGGTCGAGGAG
GTCTCCGGCGAGCTCGGCCCGGTGCCGCTCGGGTCGGCCCGGATCCACCGCACGGGCGAG
GACGTCACCGTCGTCGCCACCGGCCAGTGCGTGCATGTCGCCCTGGCCGTCGCGGAGGCC
ATGGCGGACGAGGCGTCGATCGAGGTGGTGGATCCGCGCACGATCTACCCGGTGGACTGG
GAGACGATCCGGGCGTCGGCGGAGAAGACCGGACGGCTGGTCGTCATCGATGACGCCAAC
CGGATGTGCGGGTTCGGCGGCGAGGTGCTGGCCACCGCGGCGGAGCAGTTCGATCTGACG
GCCCGGCCCCGGCGGGTGACCCGGCCGGACGGCGCGGTCATCCCCTACGCGCTCGTGCTC
GACCAGGCGTTGCTGCCGGACGCGGCCCAGCTGACCGACGCGATCCGTGCCGTCCTGAAG
TGA

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09
show BLAST table
InterPro
Database:interpro:38.0
IPR005475 Transketolase-like, pyrimidine-binding domain (Domain)
 [4-177]  7.79998304125571e-40 SM00861
SM00861   Transket_pyr
 [4-174]  2.5e-31 PF02779
PF02779   Transket_pyr
IPR005476 Transketolase, C-terminal (Domain)
 [191-306]  8.00000000000001e-30 PF02780
PF02780   Transketolase_C
IPR009014 Transketolase, C-terminal/Pyruvate-ferredoxin oxidoreductase, domain II (Domain)
 [185-320]  1.29999924468179e-32 SSF52922
SSF52922   Transketo_C_like
IPR015941 Transketolase-like, C-terminal (Domain)
 [192-319]  1.09999999999999e-34 G3DSA:3.40.50.920
G3DSA:3.40.50.920   Transketo_C_like
SignalP No significant hit
TMHMM No significant hit
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