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CDS information : Urd_00170


close this sectionLocation

Organism
StrainTü2717
Entry nameUrdamycin
Contig
Start / Stop / Direction18,429 / 20,438 / + [in whole cluster]
939 / 2,948 / + [in contig]
Location18429..20438 [in whole cluster]
939..2948 [in contig]
TypeCDS
Length2,010 bp (669 aa)
Click on the icon to see Genetic map.

close this sectionAnnotation

Category3.4 other modification
Productputative 2,3-dehydratase/C-6 ketoreductase
Product (GenBank)oxygenase-reductase
Gene
Gene (GenBank)urdM
EC number
Keyword
  • C-6 S-stereochemistry
Note
  • bifunctional protein
  • It is proposed that this ORF oxygenase domain also serves as key enzyme bridging PKS and post-PKS reactions by catalyzing the hydrolysis and decarboxylation of the ACP-tethered angucycline to prejadomycin(2,3-dehydro-UWM6).
Note (GenBank)
  • UrdM
Reference
ACC
PmId
[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)
[12512084] Urdamycin L: a novel metabolic shunt product that provides evidence for the role of the urdM gene in the urdamycin A biosynthetic pathway of Streptomyces fradiae TU 2717. (Chembiochem. , 2003)
[22633416] Tailoring enzymes involved in the biosynthesis of angucyclines contain latent context-dependent catalytic activities. (Chem Biol. , 2012)
[25200607] Structure-based engineering of angucyclinone 6-ketoreductases. (Chem Biol. , 2014)
Related Reference
ACC
Q6DV92
NITE
Lando_00080
PmId
[15651811] Identification of the function of gene lndM2 encoding a bifunctional oxygenase-reductase involved in the biosynthesis of the antitumor antibiotic landomycin E by Streptomyces globisporus 1912 supports the originally assigned structure for landomycinone. (J Org Chem. , 2005)
[22454092] Elucidation of post-PKS tailoring steps involved in landomycin biosynthesis. (Org Biomol Chem. , 2012)
ACC
Q5U915
NITE
Jado_00130
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)
[22465094] Delineation of gilvocarcin, jadomycin, and landomycin pathways through combinatorial biosynthetic enzymology. (Curr Opin Chem Biol. , 2012)

close this sectionSequence

selected fasta
>putative 2,3-dehydratase/C-6 ketoreductase [oxygenase-reductase]
MVAPSLDVDVIVVGAGPVGLMLAGELLRTGGVRVTVLERLAEPTTESRASMTMLTPSYEM
ELLHERGLVERLGPPPDAGPGHFGGIPLDLTEAGESRYAGQWKAPQIRVEAVLSTWATEL
GAEVRRGHTVIGLVEAPDGVSVVATAPSGERLRLSAAYIVGCDGEDSAVRRLAGFAFPGA
DPTKELLRADLAGIELRERRFERHPNGVANARRGPDGITRIMVHEFARVPGASRAPAFAE
VRAAWARVTGEDISGAEPVWVNAFHNARRQAARYRKGRVLLAGDAAHVQLPVGGQALNLG
LQDAMDLGGKLAAHITGKAGEELLDTTEPATRWRPAYSATSKHKPSCCSADPMWSLRAVF
GELLGLGAARRHLASMISGLDGGAPTSVPRTGPDATAHPGPTRQHTPHRRTTMGKLTGKT
ALVTGSSRGIGRATAIRLAREGALVAVHCSRNREAADETVATIEKEGGRAFSVLAELGVP
GDVHELFLALERGLKERTDATTLDILVNNAGVMGGVAPEEVTPELFDRLVAVNAKAPFFI
VQRAVTLIPDGGRIINISSGLTRFANPQEVAYAMTKGAMDQLTLHFAKHLGSRNITVNSV
GPGITNNGTPVFDNPEAVAQMAGYSVFNRVGEVTDVADVVAFLAGDDARWITGSYLDASG
APCSAESRG
selected fasta
>putative 2,3-dehydratase/C-6 ketoreductase [oxygenase-reductase]
ATGGTCGCGCCCTCTCTGGACGTGGACGTGATCGTCGTCGGCGCCGGGCCGGTCGGGCTG
ATGCTCGCAGGGGAACTGCTGCGCACCGGCGGAGTACGGGTGACCGTACTGGAGCGGCTC
GCAGAACCCACCACCGAGTCGCGGGCGTCCATGACCATGCTTACGCCCAGCTACGAAATG
GAACTGCTGCACGAGCGGGGCCTGGTGGAACGGCTCGGGCCGCCCCCCGACGCGGGCCCC
GGCCACTTCGGCGGCATCCCACTCGATCTGACCGAGGCCGGCGAGAGCCGGTACGCCGGC
CAGTGGAAGGCGCCGCAGATCCGCGTCGAAGCCGTACTGTCCACCTGGGCCACGGAACTC
GGTGCCGAGGTTCGGCGGGGCCACACCGTGATCGGCCTCGTCGAGGCGCCGGACGGCGTG
TCCGTCGTGGCCACCGCGCCGAGTGGCGAACGGCTACGACTGAGCGCCGCGTACATCGTC
GGATGCGACGGCGAGGACAGCGCCGTGCGGCGGCTGGCGGGCTTCGCGTTCCCCGGGGCC
GACCCCACCAAAGAGCTGCTGCGTGCCGACCTGGCGGGAATCGAACTGCGGGAGCGGCGT
TTCGAGCGGCACCCGAACGGGGTGGCCAACGCCCGGCGTGGACCGGACGGCATCACCCGG
ATCATGGTGCACGAGTTCGCCCGTGTCCCCGGTGCATCACGCGCCCCCGCCTTCGCGGAA
GTCCGCGCCGCCTGGGCCCGGGTCACCGGCGAGGACATCAGCGGTGCGGAACCGGTCTGG
GTCAACGCCTTTCACAACGCCCGTCGGCAAGCGGCCCGTTACCGCAAGGGCCGGGTCCTT
CTCGCCGGTGACGCCGCGCATGTCCAGCTGCCGGTCGGCGGACAGGCCCTCAACCTCGGC
CTGCAGGACGCGATGGATCTCGGCGGGAAACTCGCCGCGCACATCACGGGCAAGGCCGGC
GAGGAACTGCTCGACACCACCGAGCCCGCCACCCGGTGGCGGCCCGCGTACTCGGCAACA
TCGAAGCACAAGCCCAGCTGCTGTTCGGCGGACCCGATGTGGAGCCTGCGGGCGGTGTTC
GGGGAACTCCTCGGCCTCGGCGCGGCGCGCCGCCACCTCGCCTCGATGATCAGCGGGCTC
GACGGCGGAGCTCCGACGTCCGTCCCCCGGACCGGCCCCGATGCCACGGCTCACCCCGGA
CCAACTCGTCAGCACACCCCGCACAGGAGGACCACCATGGGCAAGCTCACCGGAAAGACC
GCGCTCGTCACGGGCTCCAGCCGTGGCATCGGCCGGGCCACGGCGATCCGTCTGGCCCGC
GAGGGAGCGCTTGTCGCAGTGCACTGCTCCCGCAACCGGGAGGCTGCCGACGAGACCGTC
GCCACCATCGAGAAGGAGGGCGGCCGGGCCTTCTCCGTCCTGGCCGAGCTGGGCGTCCCC
GGCGACGTCCACGAACTCTTCCTGGCCCTGGAACGGGGGCTGAAGGAGCGCACCGACGCC
ACCACCCTCGACATCCTCGTGAACAACGCCGGGGTCATGGGCGGAGTGGCCCCCGAGGAG
GTCACGCCCGAGCTGTTCGACCGGCTCGTCGCGGTCAACGCCAAGGCACCGTTCTTCATA
GTGCAGCGGGCCGTGACGCTGATCCCCGATGGCGGCCGCATCATCAACATCTCTTCCGGG
CTCACCCGGTTCGCCAACCCACAGGAGGTGGCGTACGCGATGACCAAGGGCGCCATGGAC
CAGCTCACCCTCCATTTCGCCAAGCATCTCGGCTCGCGCAACATCACCGTGAACAGTGTG
GGCCCAGGTATCACCAACAACGGGACACCGGTCTTCGACAACCCGGAGGCGGTGGCGCAG
ATGGCGGGCTACTCCGTGTTCAACAGGGTCGGAGAGGTCACGGACGTCGCCGATGTCGTG
GCCTTCCTCGCCGGCGACGACGCACGCTGGATTACCGGCTCCTACCTGGACGCCAGCGGG
GCACCCTGCTCGGCTGAGTCACGCGGATGA

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09
show BLAST table
InterPro
Database:interpro:38.0
IPR002198 Short-chain dehydrogenase/reductase SDR (Family)
 [419-589]  8.30000000000004e-28 PF00106
PF00106   adh_short
IPR002938 Monooxygenase, FAD-binding (Domain)
 [7-329]  3.2e-61 PF01494
PF01494   FAD_binding_3
IPR003042 Aromatic-ring hydroxylase-like (Domain)
 [9-31]  5.29999657550189e-32 PR00420 [155-170]  5.29999657550189e-32 PR00420 [276-291]  5.29999657550189e-32 PR00420 [291-307]  5.29999657550189e-32 PR00420 [309-327]  5.29999657550189e-32 PR00420
PR00420   RNGMNOXGNASE
IPR016040 NAD(P)-binding domain (Domain)
 [408-660]  2.70000000000002e-66 G3DSA:3.40.50.720
G3DSA:3.40.50.720   NAD(P)-bd
IPR020904 Short-chain dehydrogenase/reductase, conserved site (Conserved_site)
 [559-587]  PS00061
PS00061   ADH_SHORT
SignalP No significant hit
TMHMM No significant hit