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CDS information : Chro_00330


close this sectionLocation

Organism
StrainATCC 13273 (=NBRC 3746)
Entry nameChromomycin
Contig
Start / Stop / Direction36,762 / 38,435 / + [in whole cluster]
36,762 / 38,435 / + [in contig]
Location36762..38435 [in whole cluster]
36762..38435 [in contig]
TypeCDS
Length1,674 bp (557 aa)
Click on the icon to see Genetic map.

close this sectionAnnotation

Category3.3 modification reduction
Productputative oxidoreductase
Product (GenBank)oxygenase
Gene
Gene (GenBank)cmmOII
EC number
Keyword
Note
Note (GenBank)
Reference
ACC
PmId
[15112992] Biosynthesis of the antitumor chromomycin A3 in Streptomyces griseus: analysis of the gene cluster and rational design of novel chromomycin analogs. (Chem Biol. , 2004)
Related Reference
ACC
Q194R1
NITE
Mith_00090
PmId
[10102355] Analysis of two chromosomal regions adjacent to genes for a type II polyketide synthase involved in the biosynthesis of the antitumor polyketide mithramycin in Streptomyces argillaceus. (Mol Gen Genet. , 1999)
[16856198] Premithramycinone G, an early shunt product of the mithramycin biosynthetic pathway accumulated upon inactivation of oxygenase MtmOII. (Angew Chem Int Ed Engl. , 2006)
ACC
Q3S8Q4
NITE
Oxtet_00120
PmId
[18422316] Identifying the minimal enzymes required for anhydrotetracycline biosynthesis. (J Am Chem Soc. , 2008)
ACC
Q8KUF9
NITE
Ansam_00130
PmId
[14624546] The post-polyketide synthase modification steps in the biosynthesis of the antitumor agent ansamitocin by Actinosynnema pretiosum. (J Am Chem Soc. , 2003)
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 [oxygenase]
MTTADNADGAPPSPPQVLVTGAGPVGLTAAIELARRGLRIRLIDAAPGPAVTSRAMATHA
RSLETYDQQGIVEGMMTRGRRIQRFTMHANGRRLARLGPDYSRVPTRYPMTLMIDQAATE
DVLRQTAATFGVKVEWGVRLGSFTQDAEAVHAVLHTADGEEHLTVERLVGCDGGHSTVRK
LLGLPLLGDSSETWLIADAELEAGLPQNSIHWIKAGKGTVMAIPFPEENKWRLLDTADAS
YSGDPDEVAGRFARKLRAGLGRPVRVSTPSWVSVFTIQQRMITRMREGRVMLAGDAAHVH
SPASGQGLNTGVQDAYNLAWKLAFVVRGHAPDALLDSYSDERVPIGRALLGSTRKATWLV
QLKNSAAGIALPVVFALVRRCGPLRGRIERGIIGTMSALALDYTDSPLTVPDTRPRTAAG
PRAGTRIAQVTAQDALGTGWSALLAELRDTRCTLLVAGGGTTSARAAEQAHAAHADWLSV
RVFADTPETSGPDETIGPRPLPDPDGGVRRHLNCAPDGWLLVRPDGYLCARGSALTSQEL
APALDAVRGMRSAGPGA
selected fasta
>putative oxidoreductase [oxygenase]
ATGACGACAGCCGACAACGCCGACGGGGCGCCGCCGAGCCCTCCCCAGGTCCTGGTGACG
GGCGCGGGCCCGGTGGGACTGACCGCGGCCATCGAACTCGCCCGGCGAGGTCTGCGCATA
CGCCTGATCGACGCCGCCCCCGGGCCCGCCGTCACCAGCCGCGCGATGGCCACCCACGCA
CGCTCCCTGGAGACGTACGACCAACAGGGGATCGTCGAGGGCATGATGACCCGAGGGCGG
CGCATCCAGCGCTTCACCATGCACGCCAACGGCCGTCGGCTGGCACGTCTGGGCCCCGAC
TACTCCCGGGTCCCCACCCGCTACCCGATGACGCTGATGATCGACCAGGCCGCGACCGAG
GACGTCCTGCGGCAGACCGCCGCGACGTTCGGCGTGAAGGTCGAATGGGGGGTCCGTCTC
GGTAGCTTCACCCAGGACGCCGAGGCCGTGCACGCGGTCCTGCACACGGCGGACGGTGAG
GAACACCTCACCGTGGAGCGGCTGGTGGGCTGCGACGGCGGACACAGCACGGTCCGCAAA
CTCCTAGGGCTGCCACTCCTGGGCGACTCCAGCGAGACCTGGCTGATCGCCGACGCCGAA
CTCGAGGCTGGTCTGCCGCAGAACAGCATCCACTGGATCAAGGCCGGCAAGGGGACGGTG
ATGGCCATCCCCTTTCCCGAGGAGAACAAGTGGCGGTTGCTGGACACCGCCGACGCCTCC
TACAGCGGAGACCCGGACGAGGTGGCCGGCCGCTTCGCCCGCAAACTGCGAGCCGGACTC
GGCCGCCCCGTGCGGGTCTCCACCCCGAGCTGGGTGTCGGTCTTCACCATCCAGCAGCGC
ATGATCACCCGCATGCGGGAGGGCCGGGTCATGCTGGCGGGCGATGCGGCCCACGTGCAC
AGCCCTGCCTCCGGCCAGGGCCTCAACACCGGTGTCCAGGACGCCTACAACCTCGCCTGG
AAGCTGGCGTTCGTCGTGCGGGGCCACGCACCGGACGCCCTGCTCGACTCCTACTCGGAC
GAGCGTGTCCCGATCGGCCGGGCCCTCCTGGGATCCACCAGGAAGGCCACCTGGCTCGTC
CAGCTGAAGAACTCCGCGGCAGGCATCGCGCTGCCCGTGGTCTTCGCGCTCGTCCGCCGG
TGCGGTCCGCTGCGCGGCCGGATCGAGCGCGGGATCATCGGCACCATGTCGGCGCTGGCG
CTGGACTACACCGACAGCCCGCTCACCGTCCCCGACACCCGCCCCCGCACCGCCGCGGGG
CCGCGAGCCGGGACCCGGATCGCCCAGGTCACTGCTCAGGACGCCCTCGGGACGGGCTGG
AGCGCCCTGCTGGCCGAGCTGCGGGACACCCGGTGCACCCTGCTCGTGGCAGGCGGGGGA
ACCACCTCCGCCCGTGCCGCCGAACAGGCGCACGCGGCGCACGCGGACTGGCTCTCGGTA
CGGGTGTTCGCCGACACGCCCGAGACCTCCGGCCCGGACGAGACCATAGGCCCCCGCCCG
CTGCCGGACCCGGACGGAGGCGTCCGCAGGCACCTGAACTGCGCCCCCGACGGCTGGCTG
CTGGTCCGGCCGGACGGTTACCTCTGCGCGCGCGGCTCCGCCCTGACCTCCCAGGAGCTC
GCGCCCGCCTTGGACGCCGTTCGCGGGATGCGGTCCGCCGGACCGGGGGCTTGA

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09
show BLAST table
InterPro
Database:interpro:38.0
IPR002938 Monooxygenase, FAD-binding (Domain)
 [16-350]  9.3000000000001e-79 PF01494
PF01494   FAD_binding_3
IPR003042 Aromatic-ring hydroxylase-like (Domain)
 [16-38]  1e-43 PR00420 [164-179]  1e-43 PR00420 [287-302]  1e-43 PR00420 [302-318]  1e-43 PR00420 [320-338]  1e-43 PR00420 [338-354]  1e-43 PR00420
PR00420   RNGMNOXGNASE
SignalP No significant hit
TMHMM No significant hit