Spino_00120 : CDS information

close this sectionLocation

Organism
StrainNRRL 18538
Entry nameSpinosyn
Contig
Start / Stop / Direction16,418 / 14,799 / - [in whole cluster]
16,418 / 14,799 / - [in contig]
Locationcomplement(14799..16418) [in whole cluster]
complement(14799..16418) [in contig]
TypeCDS
Length1,620 bp (539 aa)
Click on the icon to see Genetic map.

close this sectionAnnotation

Category3.3 modification reduction
ProductC-15 dehydrogenase
Product (GenBank)putative oxidoreductase
Gene
Gene (GenBank)spnJ
EC number
Keyword
Note
Note (GenBank)
  • involved in spinosyn aglycone biosynthesis; possibly involved in polyketide bridging
Reference
ACC
PmId
[11358695] Cloning and analysis of the spinosad biosynthetic gene cluster of Saccharopolyspora spinosa. (Chem Biol. , 2001)
[11386361] A cluster of genes for the biosynthesis of spinosyns, novel macrolide insect control agents produced by Saccharopolyspora spinosa. (Antonie Van Leeuwenhoek. , 2000)
[17985910] The biosynthesis of spinosyn in Saccharopolyspora spinosa: synthesis of the cross-bridging precursor and identification of the function of SpnJ. (J Am Chem Soc. , 2007)
comment
[PMID: 11358695](2001)
spinosad biosynthetic gene clusterの報告。
spnJ(540aa): polyketide bridging?

Aglycon合成過程でPKSの結合形成に関与すると推測されている。
SpnJのMutantはAglycon以降の化合物からSpynosynAを産生することができるが、Spinosad誘導体を産生することはできない。

--
[PMID: 11386361](2000)
同じ著者らの先行論文。
spnJ: Aglycone modification?

--
[PMID: 17985910](2007)
spnJをクローニング、発現、精製して得たSpnJはflavoproteinsの特徴を示す。

SpnJの基質として直線polyketide前駆体と対応する環化macrolactoneを合成し、SpnJと反応させた。
直線polyketideはSpnJの基質とはならなかったが、macrolactoneはそのketoneへと変換された。

よって、SpnJは直線polyketideではなく、それがlactonizationされたmacrolactoneのC-15の酸化
(-OH → =O)に特異的なoxidaseである。

close this sectionSequence

selected fasta
>C-15 dehydrogenase [putative oxidoreductase]
MISAAGEQSGPVRKGGAVPEFHDPAPMNRRTPGTEITVEPDDPRYPDLVVGHNPRFTGKP
ERIHIASSAEDVVHAVADAVRTGRRVGVRSGGHCFENLVADPAIRVLVDLSELNRVYYDS
TRGAFAIEAGAALGQVYRTLFKNWGVTIPTGACPGVGAGGHILGGGYGPLSRRFGSVVDY
LQGVEVVVVDQAGEVHIVEADRNSTGAGHDLWWAHTGGGGGNFGIVTRFWLRTPDVVSTD
AAELLPRPPATVLLRSFHWPWHELTEQSFAVLLQNFGNWYEQHSAPESTQLGLFSTLVCA
HRQAGYVTLNVHLDGTDPNAERTLAEHLSAINAQVGVTPAEGLRETLPWLRSTQVAGAIA
EGGEPGMQRTKVKAAYLRTGLSEAQLATVYRRLTVYGYDNPAAALLLLGYGGMANAVAPS
ATALAQRDSVLKALFVTNWSEPAEDERHLTWIRGFYREMYAETGGVPVPGTRVDGSYINY
PDTDLADPLWNTSGVAWHDLYYKDNYPRLQRAKARWDPQNIFQHGLSIKPPARLSPGQP
selected fasta
>C-15 dehydrogenase [putative oxidoreductase]
ATGATCTCGGCTGCGGGCGAACAAAGTGGACCAGTCAGAAAAGGAGGGGCGGTGCCCGAA
TTCCATGACCCGGCACCCATGAATCGTCGAACCCCAGGAACAGAGATCACCGTCGAGCCC
GACGATCCTCGTTATCCGGACCTCGTCGTCGGGCACAACCCCCGTTTCACCGGAAAACCC
GAACGCATCCACATCGCCAGCTCCGCCGAAGACGTCGTGCACGCCGTCGCCGACGCCGTG
CGCACCGGCAGGCGGGTAGGGGTCCGCAGCGGCGGGCACTGCTTCGAGAATCTCGTTGCG
GACCCGGCGATCCGAGTGCTCGTCGACCTCTCCGAGCTCAACCGCGTGTACTACGACAGC
ACGCGCGGGGCATTCGCGATCGAGGCGGGCGCCGCCCTCGGGCAGGTGTACCGAACCCTG
TTCAAGAACTGGGGCGTGACGATCCCGACCGGCGCATGTCCCGGGGTGGGCGCAGGCGGG
CACATCCTCGGCGGGGGATACGGCCCGCTGTCGCGCCGATTCGGTTCGGTCGTCGACTAC
CTTCAAGGCGTCGAGGTCGTCGTGGTCGACCAGGCCGGTGAAGTGCACATCGTCGAGGCC
GACCGGAACTCCACGGGCGCCGGTCACGACTTGTGGTGGGCGCACACCGGTGGCGGTGGC
GGCAACTTCGGGATCGTCACCAGGTTTTGGCTCCGAACGCCGGACGTGGTCAGCACCGAC
GCCGCAGAGCTCCTGCCACGGCCGCCCGCGACAGTGCTGCTCCGATCGTTCCACTGGCCG
TGGCACGAACTGACAGAGCAGTCATTCGCCGTGCTCCTACAGAACTTCGGCAATTGGTAC
GAGCAGCACAGCGCGCCTGAATCCACGCAACTCGGGTTGTTCAGCACGCTCGTCTGCGCA
CACCGGCAAGCTGGCTACGTCACGCTGAACGTTCACCTGGACGGCACGGATCCGAACGCG
GAACGCACCCTGGCCGAACACCTGTCGGCGATCAACGCCCAGGTCGGCGTGACTCCAGCC
GAAGGGCTGCGGGAAACCCTGCCGTGGTTGCGATCGACCCAGGTGGCCGGGGCGATCGCC
GAAGGCGGCGAACCGGGCATGCAACGGACCAAGGTCAAAGCCGCCTACTTGCGCACCGGG
CTGTCCGAAGCTCAACTAGCCACGGTTTACCGGCGGCTGACCGTCTACGGATACGACAAC
CCTGCGGCGGCGCTGTTGCTGCTCGGTTACGGCGGTATGGCGAATGCCGTGGCTCCGTCG
GCCACCGCACTCGCTCAGCGCGACTCGGTTCTCAAAGCGCTGTTCGTCACGAACTGGTCG
GAGCCCGCCGAGGACGAGCGGCATCTGACCTGGATTCGCGGTTTCTACCGCGAGATGTAC
GCCGAAACCGGCGGAGTTCCGGTGCCAGGTACCCGTGTCGACGGCTCCTACATCAACTAC
CCGGACACCGACTTGGCCGATCCATTGTGGAACACCTCCGGTGTTGCCTGGCACGACCTG
TACTACAAAGACAACTACCCGCGGCTGCAGCGGGCCAAAGCGCGGTGGGATCCGCAGAAC
ATCTTCCAGCACGGCCTGTCGATCAAACCGCCGGCACGGCTTTCACCCGGTCAGCCATGA

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09
show BLAST table
InterPro
Database:interpro:38.0
IPR006093 Oxygen oxidoreductase covalent FAD-binding site (Binding_site)
 [60-93]  PS00862
PS00862   OX2_COVAL_FAD
IPR006094 FAD linked oxidase, N-terminal (Domain)
 [61-188]  6.50000000000001e-19 PF01565
PF01565   FAD_binding_4
IPR012951 Berberine/berberine-like (Domain)
 [476-529]  3.90000000000001e-18 PF08031
PF08031   BBE
IPR016166 FAD-binding, type 2 (Domain)
 [41-237]  5.00000909915354e-36 SSF56176
SSF56176   FAD-binding_2
 [56-236]  PS51387
PS51387   FAD_PCMH
IPR016168 FAD-linked oxidase, FAD-binding, subdomain 2 (Domain)
 [119-233]  8.00000000000001e-07 G3DSA:3.30.465.20
G3DSA:3.30.465.20   FAD-linked_oxidase_FAD-bd_sub2
SignalP No significant hit
TMHMM No significant hit
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