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CDS information : A4793_00200


close this sectionLocation

Organism
StrainNRRL 15009
Entry nameA47934
Contig
Start / Stop / Direction51,535 / 50,219 / - [in whole cluster]
51,535 / 50,219 / - [in contig]
Locationcomplement(50219..51535) [in whole cluster]
complement(50219..51535) [in contig]
TypeCDS
Length1,317 bp (438 aa)
Click on the icon to see Genetic map.

close this sectionAnnotation

Category2.1 modification addition of extender units
Product3,5-dihydroxyphenylacetyl-CoA 1,2-dioxygenase
Product (GenBank)DpgC
GenedpgC
ORF14
Gene (GenBank)
EC number
Keyword
  • Dpg
Note
Note (GenBank)
  • 3,5-Dihydroxyphenylacetyl-CoA oxygenase
Reference
ACC
PmId
[12060705] Assembling the glycopeptide antibiotic scaffold: The biosynthesis of A47934 from Streptomyces toyocaensis NRRL15009. (Proc Natl Acad Sci U S A. , 2002)
[17507985] Structural basis for cofactor-independent dioxygenation in vancomycin biosynthesis. (Nature. , 2007)
[18004875] Substrate recognition and catalysis by the cofactor-independent dioxygenase DpgC. (Biochemistry. , 2007)
[18703850] Not so clear on oxygen. Comment on Structural basis for cofactor-independent dioxygenation in vancomycin biosynthesis by Widboom et al. (2007), Nature (London), 447, 342-345. (Acta Crystallogr D Biol Crystallogr. , 2008)
Related Reference
ACC
O52812
NITE
Chlor_00300
PmId
[11752437] Glycopeptide antibiotic biosynthesis: enzymatic assembly of the dedicated amino acid monomer (S)-3,5-dihydroxyphenylglycine. (Proc Natl Acad Sci U S A. , 2001)
[15380180] DpgC is a metal- and cofactor-free 3,5-dihydroxyphenylacetyl-CoA 1,2-dioxygenase in the vancomycin biosynthetic pathway. (Chem Biol. , 2004)

close this sectionSequence

selected fasta
>3,5-dihydroxyphenylacetyl-CoA 1,2-dioxygenase [DpgC]
MTTVLPPLEDTDGLWAALTEAAASVEKLLATLPEHGARSSAERAEIAAAHDAARALRVRF
LDTHADAVYDRLTDHRRVHLRLAELVEAAATAFPGLVPTQQQLAVERSLPQAAKEGHEID
QGIFLRAVLRSPLAGPHLLDAMLRPTPRALELLPEFVRTGEVEMEAVHLERRDGVARLTM
CRDDRLNAEDGQQVDDMETAVDLALLDPGVRVGLLRGGVMSHPRYRGKRVFSAGINLKYL
SQGGISLVDFLMRRELGYIHKLVRGVLTNDDRPGWWHSPRIEKPWVAAVDGFAIGGGAQL
LLVFDRVLASSDAYFSLPAAKEGIIPGAANLRLGRFAGPRVSRQVILEGRRIWAKEPEAR
LLVDEVVEPDELDAAIERSLTRLDGDAVLANRRMLNLADESPDGFRAYMAEFALMQALRL
YGHDVIDKVGRFGGRPPA
selected fasta
>3,5-dihydroxyphenylacetyl-CoA 1,2-dioxygenase [DpgC]
ATGACGACCGTCCTGCCACCCCTTGAGGACACCGACGGCCTCTGGGCGGCGCTGACCGAG
GCCGCCGCGAGCGTGGAGAAGCTGCTGGCCACACTTCCGGAGCACGGCGCGCGCTCCTCC
GCCGAGCGGGCCGAGATCGCCGCCGCCCACGATGCCGCCCGCGCGCTGCGCGTCCGCTTC
CTGGACACGCACGCGGACGCCGTCTACGACCGGCTCACGGACCACCGTCGCGTCCACCTA
CGGCTCGCGGAGCTCGTCGAAGCCGCCGCCACCGCCTTCCCCGGGCTGGTACCCACCCAG
CAGCAGCTCGCCGTGGAGCGGTCCCTGCCCCAGGCCGCCAAGGAGGGCCACGAGATCGAC
CAGGGCATCTTCCTGCGAGCGGTGCTGCGGTCGCCTCTTGCCGGGCCGCATCTGCTCGAC
GCCATGCTCCGTCCGACCCCGCGCGCCCTGGAGCTGCTTCCGGAGTTCGTGCGCACCGGT
GAGGTGGAGATGGAAGCCGTCCACCTGGAGCGCCGGGACGGCGTGGCACGGCTGACCATG
TGTCGCGACGACCGCCTGAACGCCGAGGACGGTCAGCAGGTCGATGACATGGAGACCGCC
GTCGACCTCGCCCTGCTCGATCCGGGCGTCCGGGTGGGACTGTTGCGCGGCGGGGTGATG
AGCCATCCCCGTTACCGGGGCAAGCGGGTGTTCAGCGCCGGCATCAACCTCAAGTACCTC
AGCCAGGGCGGCATCTCACTGGTCGACTTCCTGATGCGCCGGGAACTCGGCTACATCCAC
AAGCTCGTCCGGGGCGTGCTCACCAACGACGACCGACCCGGCTGGTGGCACTCACCCCGG
ATCGAGAAACCGTGGGTCGCGGCGGTGGACGGCTTCGCGATCGGCGGCGGAGCCCAGTTG
CTGCTGGTCTTCGACCGCGTACTCGCCTCCTCCGACGCCTACTTCAGCCTTCCCGCGGCG
AAGGAGGGCATCATCCCGGGAGCCGCGAACCTGCGGCTCGGCCGGTTCGCCGGGCCGCGC
GTGTCCCGGCAGGTCATTCTGGAGGGCCGCCGGATCTGGGCGAAGGAACCCGAGGCGCGC
CTGCTGGTCGACGAGGTCGTGGAGCCGGACGAGCTGGACGCTGCCATCGAGCGGAGCCTG
ACGCGACTCGACGGCGACGCCGTGCTCGCCAACCGGCGGATGCTGAACCTCGCCGACGAG
TCACCGGACGGATTCCGCGCGTACATGGCGGAGTTCGCCCTCATGCAGGCTCTGCGGCTC
TACGGCCACGACGTGATCGACAAGGTCGGCCGATTCGGAGGGCGGCCCCCCGCATGA

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09
show BLAST table
InterPro
Database:interpro:38.0
IPR001753 Crotonase, core (Domain)
 [170-378]  7.5e-19 PF00378
PF00378   ECH
SignalP No significant hit
TMHMM No significant hit