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CDS information : Chlor_00080


close this sectionLocation

Organism
StrainA82846UV37B
Entry nameChloroeremomycin
Contig
Start / Stop / Direction32,520 / 33,740 / + [in whole cluster]
32,520 / 33,740 / + [in contig]
Location32520..33740 [in whole cluster]
32520..33740 [in contig]
TypeCDS
Length1,221 bp (406 aa)
Click on the icon to see Genetic map.

close this sectionAnnotation

Category3.3 modification reduction
Productputative cytochrome P450
Product (GenBank)PCZA363.7
GenecepF
oxyB
ORF8
Gene (GenBank)
EC number
Keyword
  • 1st cross-linking
  • C-O-D ring
Note
Note (GenBank)
  • similar to P450 related oxidase/hydroxylase
Reference
ACC
PmId
[9545426] Sequencing and analysis of genes involved in the biosynthesis of a vancomycin group antibiotic. (Chem Biol. , 1998)
Related Reference
ACC
O87674
NITE
Balhi_00120
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)
[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)
[20337711] Genome mining in Amycolatopsis balhimycina for ferredoxins capable of supporting cytochrome P450 enzymes involved in glycopeptide antibiotic biosynthesis. (FEMS Microbiol Lett. , 2010)
ACC
Q8RN04
PmId
[12207020] Crystal structure of OxyB, a cytochrome P450 implicated in an oxidative phenol coupling reaction during vancomycin biosynthesis. (J Biol Chem. , 2002)
[15593150] An oxidative phenol coupling reaction catalyzed by oxyB, a cytochrome P450 from the vancomycin-producing microorganism. (Angew Chem Int Ed Engl. , 2004)
[17477533] Oxidative phenol coupling reactions catalyzed by OxyB: a cytochrome P450 from the vancomycin producing organism. implications for vancomycin biosynthesis. (J Am Chem Soc. , 2007)
[18068978] New insights into the first oxidative phenol coupling reaction during vancomycin biosynthesis. (Bioorg Med Chem Lett. , 2008)
[18688478] Exploring the substrate specificity of OxyB, a phenol coupling P450 enzyme involved in vancomycin biosynthesis. (Org Biomol Chem. , 2008)
[20337711] Genome mining in Amycolatopsis balhimycina for ferredoxins capable of supporting cytochrome P450 enzymes involved in glycopeptide antibiotic biosynthesis. (FEMS Microbiol Lett. , 2010)
[23073849] Substituent effects on the phenol coupling reaction catalyzed by the vancomycin biosynthetic P450 enzyme OxyB. (Angew Chem Int Ed Engl. , 2012)

close this sectionSequence

selected fasta
>putative cytochrome P450 [PCZA363.7]
MVAQELSQSGDDDPRPLHIRRQDLDPADELLAAGALTRVTVGSGADAETSWMATTHGAVR
QVMGDHKSFSTRRRWHQRDEIGGTGIFRPRELVGNLMDYDPPEHTRLRQKLTPGFTLRKM
QRMQPYIEQIVADRLDAMEQAGSPADLIEFVADEVPGAVLCELIGVPRDDRAMFMQLCHG
HLDASRSQKRRAAAGEAFSRYLLAMIARERKDPGEGLIGAVIAEYGDEATDEELRGFCVQ
VMLAGDDNISGMIGLGVLALLRHPEQIAAFQGDEQSAQRAVDELIRYLTVPYAPTPRIAM
QDVIVASQMIKKGESVICSLPAANRDPALVPDPNRLDVTREPVPHVAFGHGVHHCLGAAL
SRLELRTVYTALWQRFPTLRLADPAKETNFRLTTPAYGVTSLLVAW
selected fasta
>putative cytochrome P450 [PCZA363.7]
TTGGTAGCACAGGAGCTTTCCCAGTCGGGTGACGATGACCCGCGCCCGCTGCACATTCGC
AGGCAGGACTTGGATCCGGCGGACGAACTGCTTGCCGCCGGAGCGCTGACGAGGGTCACC
GTCGGATCCGGAGCGGACGCCGAGACCAGCTGGATGGCGACAACGCACGGTGCCGTACGG
CAGGTGATGGGCGATCACAAGAGCTTCAGCACACGGCGCCGCTGGCACCAGCGCGACGAG
ATCGGCGGGACGGGTATCTTCCGGCCGCGTGAGCTGGTCGGCAACCTGATGGACTACGAC
CCGCCCGAGCACACCCGGCTGCGGCAGAAGCTGACCCCCGGATTCACGCTGCGCAAGATG
CAGCGGATGCAGCCGTACATCGAACAGATCGTCGCGGATCGGCTCGATGCCATGGAGCAG
GCGGGATCCCCGGCGGATCTGATCGAGTTCGTCGCCGACGAGGTGCCTGGGGCCGTGCTG
TGCGAGCTGATCGGGGTGCCCCGGGACGACCGGGCCATGTTCATGCAGTTGTGTCACGGA
CATCTCGACGCCTCGCGAAGCCAGAAGAGGCGGGCGGCGGCAGGCGAGGCGTTCTCCCGC
TACCTGTTGGCCATGATCGCCAGGGAACGCAAGGACCCGGGCGAGGGGCTGATCGGCGCC
GTCATCGCCGAATACGGCGACGAAGCCACCGATGAGGAGCTGCGGGGCTTCTGCGTTCAG
GTGATGCTGGCGGGCGACGACAACATCTCCGGCATGATCGGGCTCGGCGTGCTGGCGCTG
CTGCGCCACCCCGAGCAGATCGCCGCGTTCCAGGGTGACGAGCAGTCGGCGCAACGGGCG
GTCGACGAACTGATCCGGTACCTGACGGTCCCGTATGCCCCGACTCCCCGAATCGCCATG
CAGGACGTCATCGTCGCGAGCCAGATGATCAAGAAGGGGGAGAGCGTCATCTGCTCTCTC
CCGGCGGCAAACCGTGATCCTGCCTTGGTACCGGATCCGAACCGCCTCGATGTCACCCGC
GAGCCCGTCCCGCATGTCGCGTTCGGGCATGGCGTGCACCATTGCTTGGGAGCCGCGCTG
TCCCGCCTCGAGCTGCGAACGGTCTATACCGCCCTGTGGCAGCGCTTTCCCACGCTGCGG
CTCGCGGATCCCGCCAAGGAAACCAACTTCCGGTTGACCACCCCCGCGTATGGAGTGACC
AGTCTGCTGGTCGCGTGGTGA

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09
show BLAST table
InterPro
Database:interpro:38.0
IPR001128 Cytochrome P450 (Family)
 [226-378]  1.2e-14 PF00067
PF00067   p450
 [13-406]  2.19999900980707e-85 SSF48264
SSF48264   Cytochrome_P450
 [46-406]  7.20000000000003e-88 G3DSA:1.10.630.10
G3DSA:1.10.630.10   Cyt_P450
IPR002397 Cytochrome P450, B-class (Family)
 [99-110]  5.09998762524166e-52 PR00359 [146-162]  5.09998762524166e-52 PR00359 [163-178]  5.09998762524166e-52 PR00359 [200-222]  5.09998762524166e-52 PR00359 [279-290]  5.09998762524166e-52 PR00359 [297-324]  5.09998762524166e-52 PR00359 [325-340]  5.09998762524166e-52 PR00359 [346-355]  5.09998762524166e-52 PR00359 [355-366]  5.09998762524166e-52 PR00359
PR00359   BP450
IPR017972 Cytochrome P450, conserved site (Conserved_site)
 [348-357]  PS00086
PS00086   CYTOCHROME_P450
SignalP No significant hit
TMHMM No significant hit