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CDS information : Pikro_00170


close this sectionLocation

Organism
StrainATCC 15439
Entry namePikromycin
Contig
Start / Stop / Direction52,311 / 53,561 / + [in whole cluster]
122 / 1,372 / + [in contig]
Location52311..53561 [in whole cluster]
122..1372 [in contig]
TypeCDS
Length1,251 bp (416 aa)
Click on the icon to see Genetic map.

close this sectionAnnotation

Category3.3 modification reduction
Productcytochrome P450
Product (GenBank)cytochrome P450 hydroxylase PiKC
GenepikC
picK
Gene (GenBank)pikC
EC number
Keyword
  • C-12 hydroxylate
Note
Note (GenBank)
  • cytochrome P450 monooxygenase
Reference
ACC
PmId
[9770448] A gene cluster for macrolide antibiotic biosynthesis in Streptomyces venezuelae: architecture of metabolic diversity. (Proc Natl Acad Sci U S A. , 1998)
[9778370] Characterization of the macrolide P-450 hydroxylase from Streptomyces venezuelae which converts narbomycin to picromycin. (Biochemistry. , 1998)
[9831532] Hydroxylation of macrolactones YC-17 and narbomycin is mediated by the pikC-encoded cytochrome P450 in Streptomyces venezuelae. (Chem Biol. , 1998)
[11720530] Isolation and structure determination of novamethymycin, a new bioactive metabolite of the methymycin biosynthetic pathway in Streptomyces venezuelae. (J Nat Prod. , 2001)
[16724858] Neopikromycin and novapikromycin from the pikromycin biosynthetic pathway of Streptomyces venezuelae. (J Nat Prod. , 2006)
[16825192] The structural basis for substrate anchoring, active site selectivity, and product formation by P450 PikC from Streptomyces venezuelae. (J Biol Chem. , 2006)
[17915876] Engineering and analysis of a self-sufficient biosynthetic cytochrome P450 PikC fused to the RhFRED reductase domain. (J Am Chem Soc. , 2007)
[19124459] Analysis of transient and catalytic desosamine-binding pockets in cytochrome P-450 PikC from Streptomyces venezuelae. (J Biol Chem. , 2009)
[19833867] Selective oxidation of carbolide C-H bonds by an engineered macrolide P450 mono-oxygenase. (Proc Natl Acad Sci U S A. , 2009)
[24627965] Directing group-controlled regioselectivity in an enzymatic C-H bond oxygenation. (J Am Chem Soc. , 2014)
[26201742] Enzymatic hydroxylation of an unactivated methylene C-H bond guided by molecular dynamics simulations. (Nat Chem. , 2015)

close this sectionSequence

selected fasta
>cytochrome P450 [cytochrome P450 hydroxylase PiKC]
MRRTQQGTTASPPVLDLGALGQDFAADPYPTYARLRAEGPAHRVRTPEGDEVWLVVGYDR
ARAVLADPRFSKDWRNSTTPLTEAEAALNHNMLESDPPRHTRLRKLVAREFTMRRVELLR
PRVQEIVDGLVDAMLAAPDGRADLMESLAWPLPITVISELLGVPEPDRAAFRVWTDAFVF
PDDPAQAQTAMAEMSGYLSRLIDSKRGQDGEDLLSALVRTSDEDGSRLTSEELLGMAHIL
LVAGHETTVNLIANGMYALLSHPDQLAALRADMTLLDGAVEEMLRYEGPVESATYRFPVE
PVDLDGTVIPAGDTVLVVLADAHRTPERFPDPHRFDIRRDTAGHLAFGHGIHFCIGAPLA
RLEARIAVRALLERCPDLALDVSPGELVWYPNPMIRGLKALPIRWRRGREAGRRTG
selected fasta
>cytochrome P450 [cytochrome P450 hydroxylase PiKC]
GTGCGCCGTACCCAGCAGGGAACGACCGCTTCTCCCCCGGTACTCGACCTCGGGGCCCTG
GGGCAGGATTTCGCGGCCGATCCGTATCCGACGTACGCGAGACTGCGTGCCGAGGGTCCG
GCCCACCGGGTGCGCACCCCCGAGGGGGACGAGGTGTGGCTGGTCGTCGGCTACGACCGG
GCGCGGGCGGTCCTCGCCGATCCCCGGTTCAGCAAGGACTGGCGCAACTCCACGACTCCC
CTGACCGAGGCCGAGGCCGCGCTCAACCACAACATGCTGGAGTCCGACCCGCCGCGGCAC
ACCCGGCTGCGCAAGCTGGTGGCCCGTGAGTTCACCATGCGCCGGGTCGAGTTGCTGCGG
CCCCGGGTCCAGGAGATCGTCGACGGGCTCGTGGACGCCATGCTGGCGGCGCCCGACGGC
CGCGCCGATCTGATGGAGTCCCTGGCCTGGCCGCTGCCGATCACCGTGATCTCCGAACTC
CTCGGCGTGCCCGAGCCGGACCGCGCCGCCTTCCGCGTCTGGACCGACGCCTTCGTCTTC
CCGGACGATCCCGCCCAGGCCCAGACCGCCATGGCCGAGATGAGCGGCTATCTCTCCCGG
CTCATCGACTCCAAGCGCGGGCAGGACGGCGAGGACCTGCTCAGCGCGCTCGTGCGGACC
AGCGACGAGGACGGCTCCCGGCTGACCTCCGAGGAGCTGCTCGGTATGGCCCACATCCTG
CTCGTCGCGGGGCACGAGACCACGGTCAATCTGATCGCCAACGGCATGTACGCGCTGCTC
TCGCACCCCGACCAGCTGGCCGCCCTGCGGGCCGACATGACGCTCTTGGACGGCGCGGTG
GAGGAGATGTTGCGCTACGAGGGCCCGGTGGAATCCGCGACCTACCGCTTCCCGGTCGAG
CCCGTCGACCTGGACGGCACGGTCATCCCGGCCGGTGACACGGTCCTCGTCGTCCTGGCC
GACGCCCACCGCACCCCCGAGCGCTTCCCGGACCCGCACCGCTTCGACATCCGCCGGGAC
ACCGCCGGCCATCTCGCCTTCGGCCACGGCATCCACTTCTGCATCGGCGCCCCCTTGGCC
CGGTTGGAGGCCCGGATCGCCGTCCGCGCCCTTCTCGAACGCTGCCCGGACCTCGCCCTG
GACGTCTCCCCCGGCGAACTCGTGTGGTATCCGAACCCGATGATTCGCGGGCTCAAGGCC
CTGCCGATCCGCTGGCGGCGAGGACGGGAGGCGGGCCGCCGTACCGGTTGA

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09
show BLAST table
InterPro
Database:interpro:38.0
IPR001128 Cytochrome P450 (Family)
 [243-260]  5.39999977351167e-05 PR00385 [278-289]  5.39999977351167e-05 PR00385 [345-354]  5.39999977351167e-05 PR00385 [354-365]  5.39999977351167e-05 PR00385
PR00385   P450
 [209-375]  4.00000000000001e-29 PF00067
PF00067   p450
 [6-407]  2.50000000000001e-125 G3DSA:1.10.630.10
G3DSA:1.10.630.10   Cyt_P450
 [1-407]  1.39999277195148e-110 SSF48264
SSF48264   Cytochrome_P450
IPR002397 Cytochrome P450, B-class (Family)
 [95-106]  2.39999798157265e-56 PR00359 [143-159]  2.39999798157265e-56 PR00359 [160-175]  2.39999798157265e-56 PR00359 [196-218]  2.39999798157265e-56 PR00359 [278-289]  2.39999798157265e-56 PR00359 [296-323]  2.39999798157265e-56 PR00359 [324-339]  2.39999798157265e-56 PR00359 [345-354]  2.39999798157265e-56 PR00359 [354-365]  2.39999798157265e-56 PR00359
PR00359   BP450
IPR017972 Cytochrome P450, conserved site (Conserved_site)
 [347-356]  PS00086
PS00086   CYTOCHROME_P450
SignalP
 [1-25]  0.156 Signal
Bacteria, Gram-negative   
TMHMM No significant hit