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CDS information : A4092_00200


close this sectionLocation

Organism
StrainATCC 39727
Entry nameA40926
Contig
Start / Stop / Direction24,568 / 23,387 / - [in whole cluster]
24,568 / 23,387 / - [in contig]
Locationcomplement(23387..24568) [in whole cluster]
complement(23387..24568) [in contig]
TypeCDS
Length1,182 bp (393 aa)
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close this sectionAnnotation

Category3.3 modification reduction
Productputative cytochrome P450
Product (GenBank)putative OxyA monooxygenase
Genedbv14
oxyA
Gene (GenBank)dbv14
EC number
Keyword
  • 3rd cross-linking
  • D-O-E ring
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)
[25986904] Two Master Switch Regulators Trigger A40926 Biosynthesis in Nonomuraea sp. Strain ATCC 39727. (J Bacteriol. , 2015)
Related Reference
ACC
Q6ZZI8
NITE
Teicp2_00270
PmId
[25686610] X-domain of peptide synthetases recruits oxygenases crucial for glycopeptide biosynthesis. (Nature. , 2015)
[26549530] Sequential In Vitro Cyclization by Cytochrome P450 Enzymes of Glycopeptide Antibiotic Precursors Bearing the X-Domain from Nonribosomal Peptide Biosynthesis. (Angew Chem Int Ed Engl. , 2015)
[27213615] Regulation of the P450 Oxygenation Cascade Involved in Glycopeptide Antibiotic Biosynthesis. (J Am Chem Soc. , 2016)
ACC
Q6ZZI8
NITE
Teicp_00200
PmId
[26820384] Structure of OxyA tei: completing our picture of the glycopeptide antibiotic producing Cytochrome P450 cascade. (FEBS Lett. , 2016)
ACC
O87673
NITE
Balhi_00110
PmId
[10390204] Identification and analysis of the balhimycin biosynthetic gene cluster and its use for manipulating glycopeptide biosynthesis in Amycolatopsis mediterranei DSM5908. (Antimicrob Agents Chemother. , 1999)
[11353482] The Biosynthesis of Vancomycin-Type Glycopeptide Antibiotics-New Insights into the Cyclization Steps This work was supported by the Deutsche Forschungsgemeinschaft (SFB 323). We thank M. Schierle, Dr. S. Stevanovic and Prof. H.-G. Rammensee for help with Edman degradation and J. Turner, Prof. B. List and Prof. D. Boger (La Jolla, USA) for discussions on the work. (Angew Chem Int Ed Engl. , 2001)
[12404385] The Biosynthesis of Vancomycin-Type Glycopeptide Antibiotics-The Order of the Cyclization Steps This work was supported by the Deutsche Forschungsgemeinschaft (SFB 323) and by a grant of the EU (MEGATOP, QLK3-1999-00650). R. D. S. gratefully acknowledges the support of a Feodor-Lynen Fellowship granted by the Alexander-von-Humboldt Stiftung. We thank Corina Bihlmaier and Volker Pfeifer for help with transformation and Southern hybridization, J. A. Moss (La Jolla (USA)) for critical comments on the manuscript and Prof. Dr. M. E. Maier and Prof. Dr. H.-P. Fiedler (Tubingen) for generous support. (Angew Chem Int Ed Engl. , 2001)
[15651041] The biosynthesis of vancomycin-type glycopeptide antibiotics--a model for oxidative side-chain cross-linking by oxygenases coupled to the action of peptide synthetases. (Chembiochem. , 2005)
[16730832] Genetic analysis of the balhimycin (vancomycin-type) oxygenase genes. (J Biotechnol. , 2006)
ACC
Q8KLL7
NITE
A4793_00090
PmId
[17884639] The biosynthesis of teicoplanin-type glycopeptide antibiotics: assignment of p450 mono-oxygenases to side chain cyclizations of glycopeptide a47934. (Chem Biol. , 2007)

close this sectionSequence

selected fasta
>putative cytochrome P450 [putative OxyA monooxygenase]
MEVFEELNVVLPGELHWRDRFDPVPQLRSFMAEGPMTELGAEEGPGGRTAWLATGFDEVR
QVLGSDKFSSRLLYGGTAAGIVFPGFITQYDPPEHTRLRRVVSPAFTVRRMERFRPQVDQ
VVEDCLDAIESIGGPLDFVPHFGWSIATTATCDFLGIPRDDQAELSRSLHASRSQRAASR
RGAAGNKFMTYMGQVVARTRRDPGDDMLSVVVREHGDEITDAELTGLAAFVMGAGGDQVA
RFLAAGAWLMAEVPEQFALLRDKPDVVPDWLEEMVRYLTIDEKLTPRIALEDVRIGDRIV
KAGDTVTCSLLGANRRHFPGPDDQFDLTRDRAPNVAFGHGIHHCLGRPLAELIFRSAIPA
LARRFPALRLAEPEQEIRLGPPPFDVKALLLDW
selected fasta
>putative cytochrome P450 [putative OxyA monooxygenase]
GTGGAAGTGTTCGAGGAGCTCAACGTCGTCCTGCCCGGGGAGCTGCACTGGAGGGACCGG
TTCGATCCGGTGCCACAGCTGCGGTCCTTCATGGCCGAGGGCCCGATGACCGAGCTGGGC
GCCGAGGAAGGCCCTGGAGGGCGGACCGCGTGGCTCGCCACCGGGTTCGACGAGGTCCGG
CAGGTGCTGGGCTCGGACAAGTTCAGCTCCAGGTTGCTCTACGGCGGGACCGCGGCCGGA
ATCGTCTTTCCCGGCTTCATCACCCAGTACGACCCGCCGGAGCACACGCGACTGCGCCGG
GTGGTCTCGCCCGCGTTCACCGTCCGGCGGATGGAGCGGTTCCGCCCGCAGGTCGATCAG
GTCGTCGAGGACTGCCTGGACGCCATCGAGTCCATCGGTGGCCCGCTGGACTTCGTCCCG
CATTTCGGGTGGTCCATCGCGACGACGGCGACCTGCGACTTCCTCGGCATTCCACGTGAT
GATCAGGCGGAGCTGTCACGCAGCCTGCACGCCAGCCGGTCCCAGCGGGCGGCCAGCAGA
CGCGGAGCCGCCGGGAACAAGTTCATGACCTACATGGGCCAGGTCGTGGCTCGCACGCGC
CGTGATCCCGGCGACGACATGCTCAGCGTCGTGGTGCGCGAACACGGTGACGAGATCACC
GACGCGGAGCTGACGGGGCTGGCCGCGTTCGTCATGGGCGCGGGCGGTGACCAGGTGGCT
CGTTTCCTCGCGGCGGGCGCGTGGCTGATGGCCGAGGTCCCCGAGCAGTTCGCGCTGCTT
CGGGACAAGCCGGACGTCGTGCCTGACTGGCTGGAGGAGATGGTGCGCTATCTCACCATC
GACGAGAAGCTCACTCCGCGGATCGCGCTGGAGGACGTGCGCATCGGTGACCGCATCGTC
AAGGCCGGCGACACCGTCACGTGCTCGTTGCTGGGAGCGAACCGGCGGCACTTCCCCGGC
CCGGACGATCAGTTCGACCTCACCCGCGACAGAGCGCCGAATGTCGCGTTCGGGCACGGC
ATCCATCACTGTCTTGGCAGACCCCTGGCCGAGCTCATCTTCCGGTCGGCGATCCCGGCT
CTGGCACGCCGCTTCCCCGCACTCCGGCTGGCCGAGCCCGAACAAGAGATCAGATTGGGG
CCGCCGCCGTTCGACGTGAAAGCACTGCTGCTCGACTGGTAA

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09
show BLAST table
InterPro
Database:interpro:38.0
IPR001128 Cytochrome P450 (Family)
 [20-393]  3.30001976117415e-72 SSF48264
SSF48264   Cytochrome_P450
 [270-365]  2.8e-08 PF00067
PF00067   p450
 [20-391]  2.50000000000001e-79 G3DSA:1.10.630.10
G3DSA:1.10.630.10   Cyt_P450
IPR002397 Cytochrome P450, B-class (Family)
 [90-101]  1.10000150671643e-35 PR00359 [137-153]  1.10000150671643e-35 PR00359 [154-169]  1.10000150671643e-35 PR00359 [190-212]  1.10000150671643e-35 PR00359 [269-280]  1.10000150671643e-35 PR00359 [287-314]  1.10000150671643e-35 PR00359 [335-344]  1.10000150671643e-35 PR00359 [344-355]  1.10000150671643e-35 PR00359
PR00359   BP450
IPR017972 Cytochrome P450, conserved site (Conserved_site)
 [337-346]  PS00086
PS00086   CYTOCHROME_P450
SignalP No significant hit
TMHMM No significant hit