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CDS information : Sch475_00330


close this sectionLocation

Organism
StrainSCC-2136
Entry nameSch 47554
Contig
Start / Stop / Direction47,966 / 45,969 / - [in whole cluster]
47,966 / 45,969 / - [in contig]
Locationcomplement(45969..47966) [in whole cluster]
complement(45969..47966) [in contig]
TypeCDS
Length1,998 bp (665 aa)
Click on the icon to see Genetic map.

close this sectionAnnotation

Category3.4 other modification
Productputative 2,3-dehydratase/putative C-6 ketoreductase
Product (GenBank)putative oxidase-reducatse
Gene
Gene (GenBank)schP3
EC number
Keyword
Note
  • The N-terminal position was modified from original INSDC entry.
  • 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)
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
Q9RPB0
NITE
Urd_00170
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)
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)
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)

close this sectionSequence

selected fasta
>putative 2,3-dehydratase/putative C-6 ketoreductase [putative oxidase-reducatse]
MAVQVAEAPDTDVVVVGAGPVGLLLAGILRLGGARVTVLEQLAEPTDESRASVLHSRTME
ILDGLGLLDRLGPPPSAGPGHFGGIPLDLAAAHPSRFPGQWKAPQTLVEKVLYEWAAGLG
AEVRRRHTVTGLTVAEHRVDVAVTGPDGERLRFGAAYLAGCDGEQSTVRRLGGFEFPGSA
PVKELLRADISGIDIPDRRFQRHPNGVANCRRGPDGVTRLMVHQYGRAPRPGRPGPGLRR
GLPGLGAGDRRGHHRRPARLGQRLPQRPQAGGELPAQPGPPRRGRRAVQLPVGGQALNLG
LQDAAALGGKLAARITGRADDRMLDSYHAERHPVGARVLGNIEAQAQLLFGGPEVDALRA
VFGELLALEPARRHLASMISGLDGPRPAVSDTGRTEHPTATGPFTRTHRRSTMGKLTGRT
ALVTGSSRGIGRATAIRLAREGALVAVHCSRDTEGADDTVAAVEKEGGRAFAVAAELGVS
GDVHALFLELERGLKERTGETTLDIVVNNAGVMGGVAPEDVTPEQFDRLFAVNAKAPFFI
VQRALRLLPDGGRIINISSGLTRFANPQEVAYAMTKGAIDQLTLHYAKHLGPRNITVNSV
GPGITDNGTPVFDNPEAVAEMARYSVFERVGETKDIADVVAFLASDDARWITGSYLDASG
GTLLR
selected fasta
>putative 2,3-dehydratase/putative C-6 ketoreductase [putative oxidase-reducatse]
GTGGCCGTACAGGTTGCCGAAGCACCGGACACCGACGTGGTCGTCGTGGGCGCGGGGCCC
GTGGGTCTCCTGCTCGCCGGGATCCTGCGCCTCGGTGGCGCCCGGGTGACCGTACTGGAG
CAACTGGCCGAGCCCACCGACGAGTCACGGGCGTCGGTACTGCACTCCAGGACCATGGAG
ATCCTCGACGGTCTGGGCCTGCTGGACCGGCTCGGGCCACCGCCGAGCGCGGGCCCCGGC
CACTTCGGCGGCATCCCGCTCGACCTGGCCGCGGCGCACCCGAGCCGGTTTCCCGGCCAG
TGGAAGGCACCGCAGACACTGGTCGAGAAGGTGCTGTACGAGTGGGCCGCGGGGCTCGGT
GCCGAGGTGCGGCGCAGGCATACGGTGACCGGGCTGACGGTCGCGGAGCACCGGGTCGAC
GTCGCTGTCACCGGTCCCGACGGCGAGCGGCTGCGGTTCGGAGCGGCTTACCTCGCGGGC
TGTGACGGCGAGCAGAGCACCGTACGGCGCCTCGGAGGTTTCGAGTTCCCCGGCAGCGCC
CCGGTCAAGGAGCTGCTGCGGGCGGACATCAGCGGAATCGACATCCCGGACCGGCGCTTC
CAGCGGCATCCGAACGGGGTGGCCAACTGCCGGCGCGGGCCGGACGGCGTCACCCGCCTC
ATGGTTCACCAGTACGGCCGGGCACCCCGCCCCGGGCGGCCGGGCCCCGGACTTCGCCGA
GGTCTGCCGGGTCTGGGCGCGGGTGACCGGCGAGGACATCACCGGCGCCCGGCCCGTCTG
GGTCAACGCCTTCCACAACGCCCGCAGGCAGGCGGCGAGTTACCGGCACAGCCGGGTCCT
CCTCGCCGGGGACGCCGCGCAGTCCAGCTGCCGGTCGGCGGCCAGGCCCTCAACCTCGGT
CTCCAGGACGCGGCCGCGCTCGGCGGGAAACTCGCGGCGCGGATCACCGGCCGCGCGGAC
GACCGGATGCTCGACAGCTACCACGCCGAGCGGCACCCGGTGGGCGCACGGGTGCTCGGC
AACATCGAGGCGCAGGCCCAGCTGCTGTTCGGCGGACCCGAAGTGGACGCCCTGCGCGCG
GTGTTCGGGGAACTGCTCGCGCTCGAACCCGCCCGCCGCCACCTCGCCTCGATGATCAGC
GGGCTCGACGGCCCGCGCCCCGCCGTCTCGGACACCGGCAGGACAGAACACCCCACGGCC
ACAGGCCCGTTCACCCGCACGCACAGGAGGAGCACCATGGGCAAGCTCACCGGCAGGACC
GCGCTCGTCACCGGGTCCAGCCGCGGCATCGGACGGGCGACGGCGATCCGTCTGGCCCGC
GAGGGCGCGCTGGTCGCGGTGCACTGCTCCCGCGACACCGAGGGAGCCGACGACACCGTG
GCCGCCGTCGAGAAGGAGGGCGGCCGGGCGTTCGCCGTGGCGGCCGAACTCGGCGTGTCC
GGCGATGTGCACGCGCTCTTCCTGGAGTTGGAGCGCGGGCTGAAGGAGCGCACCGGCGAG
ACCACTCTCGACATCGTCGTGAACAACGCGGGGGTGATGGGCGGGGTGGCACCCGAGGAC
GTCACGCCCGAGCAGTTCGACCGGCTGTTCGCCGTCAACGCCAAGGCGCCGTTCTTCATC
GTGCAGCGGGCCCTGCGGCTCCTGCCCGACGGCGGACGCATCATCAACATCTCCTCCGGG
CTGACCCGGTTCGCCAACCCGCAGGAGGTGGCCTACGCGATGACCAAGGGCGCCATCGAC
CAGCTGACCCTGCACTACGCCAAGCACCTGGGCCCGCGGAACATCACCGTCAACAGCGTG
GGGCCCGGCATCACGGACAACGGCACCCCGGTCTTCGACAACCCGGAGGCCGTCGCCGAG
ATGGCGCGCTACTCGGTCTTCGAGCGTGTCGGCGAGACCAAGGACATCGCCGATGTCGTG
GCGTTCCTGGCGAGCGACGACGCCCGCTGGATCACCGGCTCCTACCTCGACGCCAGCGGC
GGCACGCTGCTGCGCTGA

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09
show BLAST table
InterPro
Database:interpro:38.0
IPR002198 Short-chain dehydrogenase/reductase SDR (Family)
 [501-512]  9.3e-07 PR00080 [552-560]  9.3e-07 PR00080 [572-591]  9.3e-07 PR00080
PR00080   SDRFAMILY
 [420-589]  1.4e-29 PF00106
PF00106   adh_short
IPR002347 Glucose/ribitol dehydrogenase (Family)
 [420-437]  6.3e-28 PR00081 [501-512]  6.3e-28 PR00081 [546-562]  6.3e-28 PR00081 [572-591]  6.3e-28 PR00081 [593-610]  6.3e-28 PR00081 [626-646]  6.3e-28 PR00081
PR00081   GDHRDH
IPR002938 Monooxygenase, FAD-binding (Domain)
 [10-189]  1.6e-34 PF01494 [290-339]  5.4e-13 PF01494
PF01494   FAD_binding_3
IPR016040 NAD(P)-binding domain (Domain)
 [416-663]  2.6e-70 G3DSA:3.40.50.720
G3DSA:3.40.50.720   no description
IPR020842 Polyketide synthase/Fatty acid synthase, KR (Domain)
 [419-621]  0.0002 SM00822
SM00822   no description
IPR020904 Short-chain dehydrogenase/reductase, conserved site (Conserved_site)
 [559-587]  PS00061
PS00061   ADH_SHORT
SignalP
 [1-34]  0.366 Signal
Eukaryota   
TMHMM
 [13-32]  Transmembrane (i-o)
Transmembrane 1