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CDS information : Pyrlo_00020


close this sectionLocation

Organism
StrainATCC 31673 (=NBRC 14294)
Entry namePyrrolomycin
Contig
Start / Stop / Direction2,502 / 892 / - [in whole cluster]
2,502 / 892 / - [in contig]
Locationcomplement(892..2502) [in whole cluster]
complement(892..2502) [in contig]
TypeCDS
Length1,611 bp (536 aa)
Click on the icon to see Genetic map.

close this sectionAnnotation

Category5.1 general function
Productputative oxidoreductase
Product (GenBank)FAD-dependent monooxygenase
Gene
Gene (GenBank)pyr2
EC number
Keyword
Note
Note (GenBank)
Reference
ACC
PmId
[17158935] Cloning and characterization of the pyrrolomycin biosynthetic gene clusters from Actinosporangium vitaminophilum ATCC 31673 and Streptomyces sp. strain UC 11065. (Antimicrob Agents Chemother. , 2007)
Related Reference
ACC
Q58PK7
PmId
[16148009] Ablation of the otcC gene encoding a post-polyketide hydroxylase from the oxytetracyline biosynthetic pathway in Streptomyces rimosus results in novel polyketides with altered chain length. (J Biol Chem. , 2005)
ACC
Q84G26
NITE
Gelda2_00060
PmId
[16085885] Insights into the biosynthesis of the benzoquinone ansamycins geldanamycin and herbimycin, obtained by gene sequencing and disruption. (Appl Environ Microbiol. , 2005)
ACC
Q5U913
NITE
Jado_00150
PmId
[15817470] Functional analyses of oxygenases in jadomycin biosynthesis and identification of JadH as a bifunctional oxygenase/dehydrase. (J Biol Chem. , 2005)
[15776503] The oxidative ring cleavage in jadomycin biosynthesis: a multistep oxygenation cascade in a biosynthetic black box. (Chembiochem. , 2005)
[17346045] Multi-oxygenase complexes of the gilvocarcin and jadomycin biosyntheses. (J Am Chem Soc. , 2007)
[20422670] Characterization of JadH as an FAD- and NAD(P)H-dependent bifunctional hydroxylase/dehydrase in jadomycin biosynthesis. (Chembiochem. , 2010)
[22633416] Tailoring enzymes involved in the biosynthesis of angucyclines contain latent context-dependent catalytic activities. (Chem Biol. , 2012)

close this sectionSequence

selected fasta
>putative oxidoreductase [FAD-dependent monooxygenase]
MPRPGRAPRSAVRRAPGGSPSRLRPRARARRGDAVGANGEYEVVVVGAGPTGLHLAGELA
LAGVRCKIVERRSERSKESRALVLQARTMEELDMRGMATAVLDRGHPVRQLEVSPGGHLI
DLTVPDSAYPGVRALPQWETEEILEERADELGVRVERGVELTDCRQDGDRVVLSLRSGDR
EWRERAAWLVGCDGARSTVRHAIGDRFEGDVLPHGILIADVRLDSPPASPRWSGWSRGRS
LSSSASAGDATGSPSSTATGPHSDGPVPVEEVDEALRTVFGLDLGPYDATWTSHFRINER
RARTNRSGRVLLAGDAAHVHSPVGAQGLNLGVQDATNLGWKLAAVVAGRAGEELLDTYAE
ERRRVCLEAVATARRLPVRAARQLGLRGVARFPGIRRRALARVNGTSHRYRSTAGRRRRG
PAGAMVGRRVPDLGLSDGRRLYEVLRSGGFVLVDQGAGSRPPVPDAWDDLVTHLPGRVRG
PRGPWLGTELFLVRPDGYCAWAGPRSRAAGDLAVVLPCWAGRRNVPRERAGAWPAG
selected fasta
>putative oxidoreductase [FAD-dependent monooxygenase]
GTGCCGCGTCCCGGACGTGCGCCCCGGTCGGCCGTGCGGCGCGCTCCGGGTGGGTCCCCA
TCCCGGCTCCGTCCGCGTGCCCGGGCGCGGAGAGGGGATGCCGTGGGCGCGAACGGCGAG
TACGAGGTCGTGGTCGTGGGTGCCGGCCCCACCGGGCTGCACCTGGCGGGTGAGTTGGCA
CTCGCAGGCGTCCGGTGCAAGATCGTCGAGAGGCGTTCCGAGCGGAGCAAGGAGTCCAGG
GCGCTGGTGCTCCAGGCCCGCACCATGGAGGAACTCGACATGCGGGGCATGGCGACGGCC
GTGCTCGACCGCGGCCACCCGGTGCGGCAACTGGAGGTCAGCCCAGGGGGCCACCTGATC
GACCTGACGGTGCCCGACTCCGCGTACCCGGGGGTGCGGGCGCTGCCGCAGTGGGAGACC
GAGGAGATCCTCGAGGAGCGGGCCGACGAGCTCGGGGTGCGCGTCGAGCGGGGCGTGGAG
CTGACCGACTGCCGGCAGGACGGCGACCGGGTGGTGTTGTCCCTGCGGTCGGGGGACCGG
GAGTGGCGTGAGCGTGCCGCGTGGCTGGTCGGGTGCGACGGGGCGCGCAGCACGGTGCGG
CACGCCATCGGTGACCGGTTCGAGGGGGACGTGCTGCCCCACGGCATCCTCATCGCCGAC
GTCCGCCTGGACAGCCCCCCAGCGTCCCCGCGCTGGTCCGGATGGTCCCGGGGGCGCTCG
CTGTCGTCATCGGCTTCGGCGGGGGACGCCACCGGATCGCCGTCATCGACCGCGACCGGG
CCGCACAGCGACGGCCCCGTCCCGGTGGAGGAGGTGGACGAGGCGCTGCGCACCGTCTTC
GGTCTCGACCTGGGGCCGTACGACGCGACGTGGACCTCGCACTTCCGGATCAACGAGCGG
CGGGCGCGGACCAACCGCAGCGGACGCGTCCTGCTGGCCGGGGACGCCGCCCACGTGCAC
TCCCCGGTCGGCGCCCAGGGGCTCAACCTGGGGGTGCAGGACGCCACCAACCTGGGCTGG
AAGCTCGCCGCGGTGGTGGCCGGGCGCGCCGGCGAGGAACTGCTGGACACCTACGCCGAG
GAACGGCGGCGGGTCTGCCTCGAGGCGGTCGCCACCGCCCGCCGCCTGCCCGTGCGGGCG
GCGCGGCAACTCGGCCTGCGGGGCGTGGCCCGGTTCCCGGGAATCCGCCGCCGGGCCCTG
GCCCGCGTCAACGGCACCTCCCACCGGTACCGGTCCACCGCGGGCCGGCGTCGCCGCGGC
CCCGCCGGTGCCATGGTCGGCCGGAGGGTGCCGGACCTGGGGCTGTCGGACGGGCGGCGG
CTGTACGAGGTGCTGCGCTCGGGCGGTTTCGTCCTGGTTGACCAGGGCGCGGGGAGCCGC
CCGCCGGTGCCCGACGCCTGGGACGACCTGGTCACCCACCTCCCGGGGCGGGTGCGCGGG
CCCCGCGGGCCGTGGCTGGGCACCGAGCTGTTCCTGGTGCGGCCCGACGGTTACTGCGCC
TGGGCCGGGCCACGGTCCCGCGCGGCCGGCGACCTCGCGGTGGTGCTGCCGTGCTGGGCG
GGTCGGCGGAACGTTCCGCGGGAACGGGCGGGCGCGTGGCCGGCGGGGTGA

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09
show BLAST table
InterPro
Database:interpro:38.0
IPR002938 Monooxygenase, FAD-binding (Domain)
 [40-370]  3.60000000000002e-78 PF01494
PF01494   FAD_binding_3
IPR003042 Aromatic-ring hydroxylase-like (Domain)
 [42-64]  1.70000295590053e-43 PR00420 [185-200]  1.70000295590053e-43 PR00420 [307-322]  1.70000295590053e-43 PR00420 [322-338]  1.70000295590053e-43 PR00420 [340-358]  1.70000295590053e-43 PR00420 [358-374]  1.70000295590053e-43 PR00420
PR00420   RNGMNOXGNASE
SignalP
 [1-29]  0.589 Signal
Bacteria, Gram-positive   
 [1-1]  Signal-anchor
Eukaryota   
 [1-29]  0.446 Signal
Bacteria, Gram-negative   
TMHMM No significant hit