Aran_00210 Aran_00210   Aran_00230 Aran_00230

Aran_00220 : CDS information

close this sectionLocation

Organism
StrainTü303
Entry nameAranciamycin
Contig
Start / Stop / Direction32,867 / 31,341 / - [in whole cluster]
32,867 / 31,341 / - [in contig]
Locationcomplement(31341..32867) [in whole cluster]
complement(31341..32867) [in contig]
TypeCDS
Length1,527 bp (508 aa)
Click on the icon to see Genetic map.

close this sectionAnnotation

Category3.3 modification reduction
Productputative FAD-dependent oxidoreductase
Product (GenBank)oxidoreductase
Gene
Gene (GenBank)
EC number
Keyword
Note
Note (GenBank)
  • orf22
Reference
ACC
PmId
[17357167] Cloning and heterologous expression of the aranciamycin biosynthetic gene cluster revealed a new flexible glycosyltransferase. (Chembiochem. , 2007)
comment
aranciamycin生合成gene cluster(ara-cluster)のクローニングとシークエンス報告。

ORF22(508aa): oxidoreductase

配列解析から、ORF22はFAD-dependentな、ORF5はCYP450-dependentな oxygenaseをコードし、aranciamycinのC-8とC-10へ酸素を導入することを担うと期待される。

---
Scheme 1 のC-10にはケト基がないが、間違いと思われる。
Related Reference
ACC
Q0PCD7
NITE
Acla_00150
PmId
[17242508] Structure determination by multiwavelength anomalous diffraction of aclacinomycin oxidoreductase: indications of multidomain pseudomerohedral twinning. (Acta Crystallogr D Biol Crystallogr. , 2007)
[17395717] Aclacinomycin oxidoreductase (AknOx) from the biosynthetic pathway of the antibiotic aclacinomycin is an unusual flavoenzyme with a dual active site. (Proc Natl Acad Sci U S A. , 2007)
comment
Blast 7th, id55%, 1e-140
Streptomyces galilaeus_aknOx
Aclacinomycin oxidoreductase

[PMID: 17242508](2007) abstract
[PMID: 17395717](2007)

Aclacinomycin oxidoreductase (AknOx)は、Aclacinomycinグループのpolyketide抗生物質における最後の2steps、末端糖部分rhodinose→L-aculoseへの酸化を触媒する。

3つめの糖が
rhodinose (Aclacinomycin N)
↓1st: C-4 hydroxy基からプロトン除去[Tyr-450]
cinerulose A (Aclacinomycin A)
↓2nd: cineruloseのC3からプロトン除去[Tyr-378]
L-aculose (Aclacinomycin Y)

AknOxの異なる２つの反応が同じactive siteで触媒される。
この反応はFADの還元を伴う。
ACC
Q9ALN1
NITE
Spino_00120
PmId
[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
Blast 8th, id54%, 1e-139
Saccharopolyspora spinosa_spnJ
Putative oxidoreductase

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
>putative FAD-dependent oxidoreductase [oxidoreductase]
MTDGARHRPPLGPVRVTPADPRYRDLIRGVNHRFTGSPGQIRIVGSAEQTVEAVQDAVDA
GLRLAVRSGGHCLEDLVDGPDTAFLLDMSEMRQVYYDPGMRAFAVEPGAHLGDVYRTLYK
GWGVTVPGGSCPTVAAGGHFAGGGYGPLTRLHGCVVDHLYAVEVVVVDAAGRARLVVASR
DDEGELGDLWWAHTGGGGGTFGVVTRYWLRTAGATGSDPAGLLPHPPSAVLDSLVTWSWE
GMTAERFRRLMRNHAEWHERNGAADSPYASLFSVLGVMHPASGVLVMSTQMDATVPDAER
LLAGYVDALDEGVGLRPAHTVRARPWLESMLQPTLPDTVTGMRSKGKAAYLRKGYTDGQL
DALYRGLTDERYTNPGAGVLFMSYGGAVSAVAPDATATAQRDAVLKALYVTLWREPEEDA
AHLAWIRGLYREVYAHSGGVPVPDEVSDGAYVNYPDTDLADPRWNTSGVPWSTLYYKDNY
PRLRRVKASWDPKGVFRHALSVEPPASE
selected fasta
>putative FAD-dependent oxidoreductase [oxidoreductase]
ATGACCGACGGCGCGCGTCATCGGCCGCCGCTGGGGCCGGTCCGGGTCACGCCGGCCGAT
CCGCGGTATCGGGACCTGATCAGGGGCGTCAACCACCGGTTCACCGGCAGCCCGGGTCAG
ATACGGATCGTCGGGTCGGCCGAGCAGACCGTCGAGGCGGTGCAGGACGCCGTCGACGCG
GGGCTGCGGCTCGCGGTCCGCAGCGGCGGGCACTGCCTGGAGGACCTGGTGGACGGGCCC
GACACCGCCTTCCTCCTCGACATGTCCGAGATGCGGCAGGTGTACTACGACCCCGGCATG
CGGGCCTTCGCGGTGGAGCCCGGGGCCCATCTGGGCGACGTCTACCGCACGCTGTACAAG
GGGTGGGGCGTCACGGTTCCCGGTGGCTCGTGCCCGACGGTCGCGGCGGGCGGTCACTTC
GCCGGCGGCGGGTACGGTCCGCTGACCCGGCTGCACGGCTGCGTCGTGGACCATCTGTAC
GCGGTCGAGGTCGTCGTGGTCGACGCGGCGGGCCGGGCCCGGCTGGTGGTGGCGTCCCGG
GACGACGAAGGCGAACTCGGCGACCTGTGGTGGGCACACACCGGCGGGGGCGGCGGTACG
TTCGGCGTGGTGACGCGGTACTGGCTGCGGACCGCCGGCGCGACCGGAAGCGACCCCGCG
GGCCTGCTGCCGCACCCCCCGTCGGCGGTGCTGGACAGCCTGGTGACCTGGTCGTGGGAG
GGCATGACCGCCGAGCGGTTCCGCCGGCTGATGCGCAACCACGCCGAGTGGCACGAGCGC
AACGGCGCCGCCGACTCCCCCTACGCGTCCCTGTTCAGCGTGCTCGGCGTGATGCACCCG
GCCTCGGGGGTGCTGGTGATGAGCACCCAGATGGACGCCACGGTCCCGGACGCCGAGCGC
CTGCTGGCGGGATACGTGGACGCTCTCGACGAGGGGGTGGGACTGCGTCCGGCGCACACC
GTGCGCGCCAGGCCCTGGCTGGAGTCGATGCTGCAGCCCACCCTGCCCGACACCGTCACC
GGCATGCGTTCCAAGGGCAAGGCCGCCTACCTCCGCAAGGGGTACACGGACGGACAGCTC
GACGCGCTGTACCGGGGTCTGACGGACGAGCGGTACACCAATCCCGGCGCCGGCGTGCTG
TTCATGTCGTACGGCGGCGCGGTCAGCGCCGTGGCTCCCGACGCCACCGCCACGGCCCAG
CGCGACGCCGTGCTCAAGGCGCTGTACGTGACGCTGTGGCGGGAGCCGGAGGAGGACGCC
GCGCATCTGGCGTGGATCCGGGGGCTGTACCGGGAGGTCTACGCGCACAGCGGTGGGGTG
CCCGTACCGGACGAGGTGAGCGACGGCGCGTACGTCAACTACCCCGACACCGACCTCGCC
GACCCGCGGTGGAACACCTCCGGCGTGCCCTGGTCCACCCTCTACTACAAGGACAACTAC
CCGCGGCTGCGGCGGGTGAAGGCGAGCTGGGATCCCAAGGGGGTCTTCCGGCACGCCTTG
TCGGTGGAGCCGCCGGCGAGCGAGTAG

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09 		show BLAST table
InterPro
Database:interpro:38.0
IPR006094 FAD linked oxidase, N-terminal (Domain)
[41-166] 3.09999999999998e-18 PF01565
PF01565   FAD_binding_4
IPR012951 Berberine/berberine-like (Domain)
[450-502] 2.4e-18 PF08031
PF08031   BBE
IPR016166 FAD-binding, type 2 (Domain)
[9-214] 1.20000117458134e-32 SSF56176
SSF56176   FAD-binding_2
[34-214] PS51387
PS51387   FAD_PCMH
IPR016168 FAD-linked oxidase, FAD-binding, subdomain 2 (Domain)
[96-169] 2.5e-05 G3DSA:3.30.465.20
G3DSA:3.30.465.20   FAD-linked_oxidase_FAD-bd_sub2
SignalP No significant hit
TMHMM No significant hit
Aran_00210 Aran_00210   Aran_00230 Aran_00230
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