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CDS information : Sch475_00400


close this sectionLocation

Organism
StrainSCC-2136
Entry nameSch 47554
Contig
Start / Stop / Direction54,474 / 52,990 / - [in whole cluster]
54,474 / 52,990 / - [in contig]
Locationcomplement(52990..54474) [in whole cluster]
complement(52990..54474) [in contig]
TypeCDS
Length1,485 bp (494 aa)
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close this sectionAnnotation

Category3.1 modification hydroxylation
Productputative C-12/C-12b hydroxylase
Product (GenBank)putative oxygenase
Gene
Gene (GenBank)schP10
EC number
Keyword
Note
Note (GenBank)
Reference
ACC
PmId
[17085966] Angucyclines Sch 47554 and Sch 47555 from Streptomyces sp. SCC-2136: cloning, sequencing, and characterization. (Mol Cells. , 2006)
Related Reference
ACC
Q54171
NITE
Urd_00100
PmId
[7592377] Cloning and characterization of a polyketide synthase gene from Streptomyces fradiae Tu2717, which carries the genes for biosynthesis of the angucycline antibiotic urdamycin A and a gene probably involved in its oxygenation. (J Bacteriol. , 1995)
[10658661] Two new tailoring enzymes, a glycosyltransferase and an oxygenase, involved in biosynthesis of the angucycline antibiotic urdamycin A in Streptomyces fradiae Tu2717. (Microbiology. , 2000)
[22633416] Tailoring enzymes involved in the biosynthesis of angucyclines contain latent context-dependent catalytic activities. (Chem Biol. , 2012)
ACC
Q93LY7
PmId
[17654627] Artificial reconstruction of two cryptic angucycline antibiotic biosynthetic pathways. (Chembiochem. , 2007)
[18291320] Sequential action of two flavoenzymes, PgaE and PgaM, in angucycline biosynthesis: chemoenzymatic synthesis of gaudimycin C. (Chem Biol. , 2008)
[21595438] Flavoprotein hydroxylase PgaE catalyzes two consecutive oxygen-dependent tailoring reactions in angucycline biosynthesis. (Biochemistry. , 2011)

close this sectionSequence

selected fasta
>putative C-12/C-12b hydroxylase [putative oxygenase]
MDASVIVAGAGPTGLTLAAELRLAGVDVIVVDRLAERTGESRGLGFTTRTMEVFDQRGLL
PRFGDMGTSNAGHFGGLPVDFAVLDSVHQAAKTVPQSTTETMLEGWAGELGTDIRRGHEL
LAVRDTTDGVEVDVRGPDGEQRLTAHYLVGCDGGRSTVRKAVGFDFPGTAATMEMYLADI
KGVELEPRLIGETVDGGMVMVGPLGDGGITRIIVCERGTPPKRRTEPPSYEEVAAAWQRL
TGIDISHAEPVWVSAFGDATRLVTEYRRGRVLLAGDAAHIHLPAGGQGMNTGVQDAANLG
WKLAAVVRGTAPEELLDTYHGERYPVGQRLMMNTKAQGLLFLSGDEVQPLRDVLRELIRY
EEVSRHLAGMVSGLEIRYDVGGGRHPLLGLRMPHLELVGDRRKTSSTELLRAARGVLLDL
EDNAVLRDRASGWSDRVDIVTAAPHGLSDDSPLAGTSAVLVRPDGHVAWAAPGSHHDLPM
VLERWFGPSRGPKS
selected fasta
>putative C-12/C-12b hydroxylase [putative oxygenase]
ATGGATGCTTCGGTCATAGTCGCCGGCGCGGGGCCCACCGGCCTGACGCTCGCCGCCGAG
CTGCGTCTGGCGGGGGTCGACGTCATCGTCGTCGACCGGCTCGCCGAGCGGACCGGCGAG
TCGCGTGGCCTCGGTTTCACCACACGCACGATGGAGGTCTTCGACCAACGCGGGCTGCTG
CCCCGCTTCGGTGACATGGGGACCAGCAACGCCGGACACTTCGGAGGACTGCCGGTCGAC
TTCGCCGTACTGGACAGCGTGCACCAGGCGGCCAAGACCGTGCCGCAGTCGACCACCGAG
ACCATGCTCGAAGGCTGGGCCGGTGAACTGGGCACGGACATCCGCCGCGGCCACGAACTG
CTCGCCGTGCGCGACACCACCGACGGTGTGGAGGTCGACGTACGCGGGCCGGACGGCGAA
CAGCGGCTGACCGCGCACTATCTCGTGGGGTGCGACGGCGGGCGCAGCACTGTCCGCAAG
GCCGTCGGCTTCGACTTCCCCGGCACGGCGGCGACCATGGAGATGTACCTCGCGGACATC
AAGGGCGTCGAGCTCGAACCCCGGCTCATCGGGGAGACCGTGGACGGCGGCATGGTCATG
GTCGGGCCGCTCGGCGACGGCGGGATCACCCGCATCATCGTCTGCGAGCGGGGCACCCCG
CCCAAGCGGCGCACCGAGCCCCCGTCGTACGAGGAAGTCGCGGCGGCCTGGCAGCGGCTC
ACCGGGATCGACATCTCGCACGCCGAGCCGGTGTGGGTCAGCGCCTTCGGGGACGCGACC
CGCCTGGTCACCGAGTACCGGCGCGGCCGGGTCCTGCTGGCGGGCGACGCCGCGCACATC
CATCTCCCGGCCGGCGGACAGGGCATGAACACCGGCGTCCAGGACGCCGCCAACCTCGGC
TGGAAGCTGGCCGCCGTGGTCCGGGGCACCGCGCCCGAAGAGCTGCTGGACACCTACCAC
GGCGAGCGGTACCCCGTCGGACAGCGCCTGATGATGAACACCAAGGCGCAGGGCCTGCTC
TTCCTGAGCGGCGACGAGGTGCAGCCGCTGCGGGACGTGCTCCGCGAGCTGATCCGGTAC
GAGGAGGTCAGCCGCCATCTCGCCGGCATGGTGAGCGGCCTGGAGATCCGGTACGACGTC
GGAGGCGGCCGCCATCCCCTGCTCGGCCTGCGTATGCCGCACCTGGAGCTGGTCGGCGAC
CGGCGCAAGACCAGCAGCACCGAACTGCTGCGCGCGGCCCGGGGCGTGCTCCTGGACCTG
GAGGACAACGCTGTCCTGCGCGACCGGGCGTCCGGCTGGTCGGACCGTGTGGACATCGTC
ACCGCCGCACCGCACGGCCTGTCCGACGACAGCCCGCTGGCCGGCACCTCAGCCGTGCTC
GTGCGCCCCGACGGGCATGTGGCGTGGGCCGCGCCCGGCAGCCATCACGACCTGCCGATG
GTGCTGGAGCGCTGGTTCGGCCCGTCGCGGGGCCCGAAGTCCTGA

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09
show BLAST table
InterPro
Database:interpro:38.0
IPR002938 Monooxygenase, FAD-binding (Domain)
 [3-333]  1.69999999999998e-95 PF01494
PF01494   FAD_binding_3
IPR003042 Aromatic-ring hydroxylase-like (Domain)
 [4-26]  1.90000694315261e-46 PR00420 [144-159]  1.90000694315261e-46 PR00420 [268-283]  1.90000694315261e-46 PR00420 [283-299]  1.90000694315261e-46 PR00420 [301-319]  1.90000694315261e-46 PR00420 [319-335]  1.90000694315261e-46 PR00420
PR00420   RNGMNOXGNASE
SignalP
 [1-18]  0.637 Signal
Eukaryota   
TMHMM No significant hit