A4092_00340 A4092_00340   A4092_00360 A4092_00360

A4092_00350 : CDS information

close this sectionLocation

Organism
StrainATCC 39727
Entry nameA40926
Contig
Start / Stop / Direction68,647 / 67,076 / - [in whole cluster]
68,647 / 67,076 / - [in contig]
Locationcomplement(67076..68647) [in whole cluster]
complement(67076..68647) [in contig]
TypeCDS
Length1,572 bp (523 aa)
Click on the icon to see Genetic map.

close this sectionAnnotation

Category3.3 modification reduction
ProductFMN-dependent oxidase
Product (GenBank)putative hexose oxidase
Gene
Gene (GenBank)dbv29
EC number
Keyword
  • N-acyl-aminoglucuronic acid moiety
Note
Note (GenBank)
Reference
ACC
PmId
[12837387] The gene cluster for the biosynthesis of the glycopeptide antibiotic A40926 by nonomuraea species. (Chem Biol. , 2003)
[17873036] Phosphate-controlled regulator for the biosynthesis of the dalbavancin precursor A40926. (J Bacteriol. , 2007)
[17935335] A unique flavin mononucleotide-linked primary alcohol oxidase for glycopeptide A40926 maturation. (J Am Chem Soc. , 2007)
[21478878] Interception of teicoplanin oxidation intermediates yields new antimicrobial scaffolds. (Nat Chem Biol. , 2011)
[25885959] Addendum: Interception of teicoplanin oxidation intermediates yields new antimicrobial scaffolds. (Nat Chem Biol. , 2015)
[25986904] Two Master Switch Regulators Trigger A40926 Biosynthesis in Nonomuraea sp. Strain ATCC 39727. (J Bacteriol. , 2015)
comment
[PMID: 12837387](2003)
Nonomuraea sp. ATCC39727由来A40926生合成gene clusterの同定論文。
A40926は半合成グリコペプチドdalbavancin (BI397 or MDL 62,397)の前駆体。

dbv ORF29: hexose oxidase

配列解析のみ。glucosamine部分の酸化を支配すると考えられている。また、N末にシグナル配列が推定されることから、ORF29産物を分泌され、酸化は細胞質外で起こると示唆される。

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[PMID: 17935335](2007)
Dbv29が、N-acyl glucosaminyl部分のC-6を酸化してN-acyl aminoglucuronic acidにする、FMN-dependent primary alcohol glycopeptide hexose oxidaseであると報告している。

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[PMID: 21478878](2011)
[PMID: 25885959](2015)
Dbv29の構造的、生化学的調査。

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このORFの発現調節についての報告

[PMID: 17873036](2007)
リン酸による遺伝子発現への影響がRT-PCR と real-time RT-PCRで調査されている。dbv29は影響を受けない。

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[PMID: 25986904](2015)
dbv clusterにあるregulatory genes dbv3, dbv4, dbv6についての調査。

dbv3の不活化株と過剰発現株からRNAを抽出してqRT-PCR解析した結果と既に確立されているオペロン構造から、Dbv3は6つのオペロン(dbv2-dbv1, dbv14-dbv8, dbv17-dbv15, dbv21-dbv20, dbv24-dbv28, dbv30-dbv35)と4つのmonocistronic transcription units dbv4, dbv29, dbv36, dbv37のpositive regulatorとして働くことが示された。

close this sectionSequence

selected fasta
>FMN-dependent oxidase [putative hexose oxidase]
MTGGTGADAASAGASSTRPELRGERCLPPAGPVKVTPDDPRYLNLKLRGANSRFNGEPDY
IHLVGSTQQVADAVEETVRTGKRVAVRSGGHCFEDFVDNPDVKVIIDMSLLTEIAYDPSM
NAFLIEPGNTLSEVYEKLYLGWNVTIPGGVCGGVGVGGHICGGGYGPLSRQFGSVVDYLY
AVEVVVVNKQGKARVIVATRERDDPHHDLWWAHTGGGGGNFGVVTKYWMRVPEDVGRNPE
RLLPKPPATLLTSTVTFDWAGMTEAAFSRLLRNHGEWYERNSGPDSPYTGLWSQLMIGNE
VPGMGESGFMMPIQVDATRPDARRLLDAHIEAVIDGVPPAEVPEPIEQRWLASTPGRGGR
GPASKTKAGYLRKRLTDRQIQAVYENMTHMDGIDYGAVWLIGYGGKVNTVDPAATALPQR
DAILKVNYITGWANPGNEAKHLTWVRKLYADVYAETGGVPVPNDVSDGAYINYPDSDLAD
PGLNTSGVPWHDLYYKGNHPRLRKVKAAYDPRNHFHHALSIRP
selected fasta
>FMN-dependent oxidase [putative hexose oxidase]
GTGACCGGCGGCACCGGAGCGGACGCCGCGTCGGCCGGCGCCTCGTCCACGCGACCGGAG
CTGCGGGGCGAGCGCTGCTTACCGCCGGCCGGCCCGGTCAAGGTGACTCCGGACGACCCG
CGCTACCTCAACCTGAAGCTGCGTGGCGCCAACAGCCGCTTCAACGGCGAGCCCGACTAC
ATCCACCTGGTCGGCTCCACCCAGCAGGTGGCCGATGCCGTCGAGGAGACGGTGCGCACC
GGCAAGCGGGTCGCCGTCCGCAGCGGTGGGCACTGTTTCGAGGACTTCGTCGACAACCCC
GACGTCAAGGTCATCATCGACATGTCGCTGCTGACGGAGATCGCGTACGACCCGTCGATG
AACGCGTTCCTGATCGAGCCGGGCAACACGCTCTCAGAGGTGTACGAAAAGCTCTACCTG
GGCTGGAACGTGACCATACCGGGTGGGGTCTGCGGCGGGGTCGGCGTCGGCGGACACATC
TGCGGAGGCGGGTACGGCCCGCTGTCACGGCAGTTCGGCTCCGTGGTCGACTACTTGTAC
GCGGTCGAGGTCGTCGTCGTCAACAAACAGGGGAAGGCACGCGTGATCGTGGCGACCCGT
GAGCGCGACGACCCCCATCACGACCTGTGGTGGGCGCACACCGGCGGTGGCGGCGGGAAC
TTCGGGGTGGTCACGAAGTACTGGATGAGGGTGCCGGAGGACGTCGGCCGGAATCCGGAG
CGGCTGCTGCCGAAGCCGCCCGCGACGTTGCTCACGAGCACGGTGACCTTCGACTGGGCG
GGGATGACGGAGGCGGCGTTCTCCCGGCTGCTGCGCAACCACGGGGAGTGGTACGAGCGG
AACAGCGGGCCCGACTCGCCGTACACCGGGCTGTGGAGTCAGCTCATGATCGGGAACGAG
GTCCCGGGCATGGGTGAGAGCGGCTTCATGATGCCCATCCAGGTGGACGCCACCCGGCCG
GACGCCCGGAGACTGCTCGACGCGCACATCGAGGCGGTGATCGACGGCGTCCCGCCGGCC
GAGGTGCCCGAGCCGATCGAACAGAGGTGGCTGGCCTCGACGCCGGGGCGAGGAGGCAGG
GGCCCGGCGTCGAAGACGAAAGCCGGCTACCTGCGCAAGCGGCTGACCGACCGGCAGATT
CAGGCCGTGTACGAGAACATGACCCACATGGACGGGATCGACTACGGCGCCGTCTGGCTG
ATCGGCTACGGCGGGAAGGTGAACACCGTCGACCCGGCGGCCACCGCCCTGCCGCAGCGC
GACGCGATACTCAAGGTGAACTACATCACCGGTTGGGCGAATCCCGGCAACGAGGCCAAG
CATCTGACGTGGGTCCGCAAGCTCTATGCCGATGTGTACGCCGAGACCGGCGGGGTGCCG
GTGCCGAACGACGTCAGCGATGGGGCGTACATCAATTACCCCGACAGCGACCTCGCGGAT
CCGGGCTTGAACACCTCGGGCGTGCCGTGGCACGACCTCTACTACAAGGGGAACCACCCG
CGGCTGCGCAAGGTGAAGGCCGCCTACGACCCGCGTAACCACTTCCACCACGCGTTGTCG
ATCCGGCCCTGA

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09 		show BLAST table
InterPro
Database:interpro:38.0
IPR006094 FAD linked oxidase, N-terminal (Domain)
[58-186] 1.1e-16 PF01565
PF01565   FAD_binding_4
IPR012951 Berberine/berberine-like (Domain)
[469-522] 8.70000000000003e-19 PF08031
PF08031   BBE
IPR016166 FAD-binding, type 2 (Domain)
[54-234] PS51387
PS51387   FAD_PCMH
[39-235] 5.09998762524166e-33 SSF56176
SSF56176   FAD-binding_2
IPR016168 FAD-linked oxidase, FAD-binding, subdomain 2 (Domain)
[115-231] 1.5e-06 G3DSA:3.30.465.20
G3DSA:3.30.465.20   FAD-linked_oxidase_FAD-bd_sub2
SignalP No significant hit
TMHMM No significant hit
A4092_00340 A4092_00340   A4092_00360 A4092_00360
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