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CDS information : Oxtet_00080


close this sectionLocation

Organism
StrainATCC 10970 (=NBRC 12907)
Entry nameOxytetracycline
Contig
Start / Stop / Direction9,833 / 7,899 / - [in whole cluster]
9,833 / 7,899 / - [in contig]
Locationcomplement(7899..9833) [in whole cluster]
complement(7899..9833) [in contig]
TypeCDS
Length1,935 bp (644 aa)
Click on the icon to see Genetic map.

close this sectionAnnotation

Category5.1 general function
Productputative ligase/putative oxidoreductase
Product (GenBank)OxyG
GeneoxyH/oxyG
otcY2-3/otcY2-4
Gene (GenBank)oxyG
EC number
Keyword
Note
  • The N-terminal position was modified from original INSDC entry.
  • This ORF may be a fusion gene of oxyH and oxyG.
Note (GenBank)
  • putative oxygenase
Reference
ACC
PmId
[16597959] Engineered biosynthesis of a novel amidated polyketide, using the malonamyl-specific initiation module from the oxytetracycline polyketide synthase. (Appl Environ Microbiol. , 2006)
[18422316] Identifying the minimal enzymes required for anhydrotetracycline biosynthesis. (J Am Chem Soc. , 2008)
Related Reference
ACC
P41636
PmId
[9008388] Molecular cloning of 4-coumarate:coenzyme A ligase in loblolly pine and the roles of this enzyme in the biosynthesis of lignin in compression wood. (Plant Physiol. , 1997)
ACC
O54259
NITE
Nogl_00350
PmId
[19255477] Expression, purification and crystallization of the cofactor-independent monooxygenase SnoaB from the nogalamycin biosynthetic pathway. (Acta Crystallogr Sect F Struct Biol Cryst Commun. , 2009)
[20052967] Crystal structure of the cofactor-independent monooxygenase SnoaB from Streptomyces nogalater: implications for the reaction mechanism. (Biochemistry. , 2010)
ACC
Q8VWB4
PmId
[12399480] Expression, purification, and characterization of AknX anthrone oxygenase, which is involved in aklavinone biosynthesis in Streptomyces galilaeus. (J Bacteriol. , 2002)

close this sectionSequence

selected fasta
>putative ligase/putative oxidoreductase [OxyG]
MAERHPEGPQDSTAEGPPLDVLAQLTGGPRIDDVLSRAARRAPRRLALSGPSGDLTYAAL
EERATRCAAALRELDGEPGAVVGIAAVLDTSFAVAYFGASRARHVSAMFNPLLREERLTH
VLRSAGARTVIVPPEMYARIQAVRGDLPALRTVVLTHREAGFQEATADVPTLDELIDAAP
ATAPFAGRDPEGVANLQFTSGTTGAPKTVMLTHRNLTVNAAQTAYTHRLTPESVLLNTLP
SFHLMHLNIAVTVGATHLLRPGDDTVAALREGARHGATHLYSLPVRLARLAADDRLPELS
VPSLRAVLSGGSALPARTADVLGGHFGVPVVQGYGLAETAPSTHFDDLDHPVAGSSGRPV
PGTACRIVDLRTRAVLPVGGRGEIQVKGPQLMKGYLGRPREESVDPDGWFSTGDIGETDA
EGRLFVVDRVKDVFKCDNWLVSPLEIENVLARCPGVTDCAVFDHPDELSGAVAHALVVLA
DEAADRDAVIRFVNDQLPYYQHIKYLDVVRHIPRSPTGKIQRRDLREQTLGGTRKHATGA
THHTKGTSTMFTFINRFTVQGDAAEFEKRVGEITAHMSRQPGFRSHRLLRSAKDPQVYVE
IAEWDDAESHGRALRTETFQQAVSEVKKLASADPAPFVPVTAAG
selected fasta
>putative ligase/putative oxidoreductase [OxyG]
ATGGCCGAGCGCCACCCCGAGGGCCCGCAGGACAGCACCGCCGAGGGGCCGCCGCTCGAC
GTGCTGGCGCAGTTGACGGGCGGCCCGCGCATCGACGACGTGCTGTCGCGGGCGGCCCGC
CGCGCCCCCAGACGGCTCGCGCTGAGCGGCCCCTCAGGGGACCTGACCTACGCGGCCCTG
GAGGAGCGGGCGACGCGGTGCGCCGCCGCGCTGCGCGAACTGGACGGTGAACCCGGCGCG
GTGGTGGGCATCGCCGCCGTACTGGACACCTCGTTCGCCGTGGCGTACTTCGGCGCCTCC
CGGGCCCGGCACGTCAGCGCGATGTTCAACCCGCTGCTGCGCGAGGAGCGCCTGACGCAC
GTGCTGCGCTCGGCGGGCGCGCGGACCGTGATCGTCCCGCCGGAGATGTACGCGCGTATC
CAGGCCGTACGAGGGGACCTGCCGGCGTTGCGGACCGTGGTGCTCACCCACCGCGAGGCC
GGCTTTCAGGAGGCCACGGCCGACGTGCCCACGCTCGACGAGCTGATCGACGCGGCCCCC
GCCACGGCGCCGTTCGCCGGCCGCGACCCCGAGGGCGTGGCCAACCTCCAGTTCACCAGC
GGCACCACCGGCGCCCCGAAGACCGTCATGCTCACCCACCGCAACCTGACGGTGAACGCG
GCCCAGACCGCGTACACCCACCGGCTCACCCCCGAGTCGGTGCTGCTCAACACCCTGCCG
TCGTTCCACCTGATGCACCTGAACATCGCGGTGACCGTCGGCGCCACCCACCTGCTGCGG
CCCGGCGACGACACCGTGGCCGCACTGCGCGAGGGCGCCCGCCACGGCGCGACGCACCTC
TACAGCCTGCCGGTACGGCTGGCCCGGCTGGCGGCGGACGACCGGCTGCCGGAACTGTCC
GTGCCCAGCCTGCGGGCCGTGCTCTCCGGCGGATCGGCCCTGCCCGCGCGGACCGCCGAT
GTCCTGGGCGGGCACTTCGGCGTCCCGGTCGTCCAGGGGTACGGACTGGCCGAGACCGCG
CCGTCCACGCACTTCGACGACCTGGACCACCCGGTGGCCGGCTCGTCGGGCAGGCCCGTA
CCGGGCACCGCCTGCCGGATCGTGGACCTGCGGACCCGCGCCGTCCTCCCGGTGGGCGGC
CGCGGCGAGATCCAGGTCAAGGGGCCCCAGCTGATGAAGGGGTACCTCGGCCGGCCGCGG
GAGGAGTCCGTGGACCCGGACGGCTGGTTCTCGACCGGCGACATCGGCGAGACCGACGCG
GAGGGGCGGCTGTTCGTCGTCGACCGGGTCAAGGACGTCTTCAAGTGCGACAACTGGCTG
GTCTCGCCCCTGGAGATCGAGAACGTGCTGGCCCGCTGCCCCGGGGTGACGGACTGCGCG
GTCTTCGACCACCCGGACGAGTTGAGCGGCGCCGTCGCGCACGCGCTGGTGGTCCTGGCG
GACGAGGCCGCCGACCGCGACGCCGTCATCCGCTTCGTCAACGACCAGCTGCCCTACTAC
CAGCACATCAAGTACCTCGACGTCGTACGGCACATCCCGCGCTCGCCCACCGGCAAGATC
CAGCGCCGCGACCTGCGGGAGCAGACCCTCGGCGGCACCCGGAAGCACGCCACGGGCGCC
ACCCATCACACGAAGGGCACCTCCACCATGTTCACCTTCATCAACCGGTTCACGGTCCAG
GGCGACGCCGCCGAGTTCGAGAAGCGGGTCGGTGAGATCACCGCCCATATGTCGCGGCAG
CCCGGCTTCCGCTCGCACCGCCTGCTGCGCTCCGCCAAGGACCCGCAGGTCTATGTCGAG
ATCGCCGAGTGGGACGACGCCGAGTCGCACGGCCGCGCGCTGCGCACCGAGACGTTCCAG
CAGGCCGTGAGCGAGGTCAAGAAGCTCGCGAGCGCCGACCCGGCCCCGTTCGTCCCGGTC
ACCGCGGCCGGCTGA

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09
show BLAST table
InterPro
Database:interpro:38.0
IPR000873 AMP-dependent synthetase/ligase (Domain)
 [56-461]  5.3e-94 PF00501
PF00501   AMP-binding
IPR007138 Antibiotic biosynthesis monooxygenase (Domain)
 [550-623]  2.8e-17 PF03992
PF03992   ABM
IPR011008 Dimeric alpha-beta barrel (Domain)
 [550-644]  1.3e-18 SSF54909
SSF54909   Dimeric alpha+beta barrel
IPR020845 AMP-binding, conserved site (Conserved_site)
 [196-207]  PS00455
PS00455   AMP_BINDING
IPR025110 Domain of unknown function DUF4009 (Domain)
 [508-531]  0.0001 PF13193
PF13193   DUF4009
SignalP No significant hit
TMHMM No significant hit