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CDS information : Gilvo_00160


close this sectionLocation

Organism
StrainGö 3592
Entry nameGilvocarcin
Contig
Start / Stop / Direction19,891 / 21,393 / + [in whole cluster]
19,891 / 21,393 / + [in contig]
Location19891..21393 [in whole cluster]
19891..21393 [in contig]
TypeCDS
Length1,503 bp (500 aa)
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close this sectionAnnotation

Category3.4 other modification
Product4a,12b-dehydratase/C-12 hydroxylase
Product (GenBank)putative FAD-dependent oxygenase
Gene
Gene (GenBank)gilOI
EC number
Keyword
Note
  • bifunctional protein
Note (GenBank)
  • GilOI
Reference
ACC
PmId
[12822997] The complete gene cluster of the antitumor agent gilvocarcin V and its implication for the biosynthesis of the gilvocarcins. (J Am Chem Soc. , 2003)
[15453748] Oxidative rearrangement processes in the biosynthesis of gilvocarcin V. (J Am Chem Soc. , 2004)
[17346045] Multi-oxygenase complexes of the gilvocarcin and jadomycin biosyntheses. (J Am Chem Soc. , 2007)
[22223167] Enzymatic total synthesis of defucogilvocarcin M and its implications for gilvocarcin biosynthesis. (Angew Chem Int Ed Engl. , 2012)
[22465094] Delineation of gilvocarcin, jadomycin, and landomycin pathways through combinatorial biosynthetic enzymology. (Curr Opin Chem Biol. , 2012)
Related Reference
ACC
Q5U913
NITE
Jado_00150
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)
[20422670] Characterization of JadH as an FAD- and NAD(P)H-dependent bifunctional hydroxylase/dehydrase in jadomycin biosynthesis. (Chembiochem. , 2010)
[22633416] Tailoring enzymes involved in the biosynthesis of angucyclines contain latent context-dependent catalytic activities. (Chem Biol. , 2012)

close this sectionSequence

selected fasta
>4a,12b-dehydratase/C-12 hydroxylase [putative FAD-dependent oxygenase]
MTLHAAEAIPSHVPVLVVGAGPTGLMLGAELALHGSRPLVIDALPSPSGQSRALGFTVRT
LEIFKQRGILGRFQGLAPVPGVHFAGLSIKGDHLSSSMRPANQYPQSKTEQVLAAWAEEL
GVPVRRPWTLTSMEPTGTGYRCVLSGPAGQQTVDADYVVGCDGAGSFVREAIGMPTKRTP
PSVQMLLGDLRGCGLPDEPFGVKHEKGMVMSAPLGDGTERVIVCDFTQPMRPQGTPVTHD
EIKAAYEQVVGSPLADGECLWASSFSDASSLVESYRSGRALLVGDTAHTHLPAGGQGMNV
SIQDAVNVGWKLALVSQGRAPDTLLDTYHAERYPVGRELLLNTAAQGQVFLRGPEVDPLR
EVLRRLLNIREVSVLLADGVSGLDIRYDMGLPEAPPPTGERLPPDVFHVVGTGGDAVEEL
RHGAALLIVPSPDSPASSLVAPWRDQVRVVHARPTDPDWGGEPAASSHWFVRPDGHIAWA
GTEFSELSASLSRWLGQPAA
selected fasta
>4a,12b-dehydratase/C-12 hydroxylase [putative FAD-dependent oxygenase]
ATGACGTTGCACGCCGCAGAAGCCATACCGTCACACGTACCGGTTCTCGTCGTGGGAGCC
GGCCCGACAGGTCTCATGCTCGGCGCCGAGCTGGCGCTCCACGGCAGCCGGCCGCTGGTG
ATCGACGCGCTGCCGAGCCCGAGCGGACAGTCCCGGGCCCTGGGCTTCACGGTGAGGACG
CTGGAGATCTTCAAGCAGCGCGGCATCCTGGGCCGTTTCCAGGGACTCGCCCCGGTGCCC
GGAGTCCATTTCGCCGGCCTCAGCATCAAGGGCGATCACCTCTCCAGCTCGATGCGCCCG
GCCAACCAGTACCCGCAGTCCAAGACCGAACAGGTCCTCGCCGCCTGGGCCGAGGAGCTG
GGAGTACCGGTGCGGCGCCCGTGGACGCTGACGTCCATGGAGCCCACTGGCACCGGGTAC
CGCTGCGTGCTCAGCGGCCCGGCCGGGCAGCAGACCGTCGACGCCGACTACGTGGTCGGC
TGCGACGGAGCGGGGAGCTTCGTCCGCGAGGCGATCGGCATGCCGACCAAGCGCACTCCC
CCATCCGTACAGATGCTCCTCGGTGATCTGCGCGGATGCGGTCTGCCCGACGAACCCTTC
GGGGTCAAGCACGAAAAGGGCATGGTCATGTCCGCACCGCTGGGCGACGGGACGGAACGC
GTCATCGTCTGTGACTTCACCCAGCCGATGCGGCCGCAGGGCACTCCCGTCACGCACGAC
GAGATCAAGGCCGCCTACGAGCAGGTCGTCGGCAGCCCCCTGGCGGACGGCGAATGTCTC
TGGGCGAGCTCGTTCTCGGACGCGTCCTCCCTCGTGGAGTCCTACCGGTCCGGTCGTGCG
CTGCTCGTCGGCGACACGGCGCACACCCATCTCCCCGCCGGCGGGCAGGGCATGAACGTC
TCGATACAGGACGCGGTGAACGTCGGCTGGAAGCTCGCGCTGGTGAGCCAGGGCCGCGCG
CCGGACACCCTGCTGGACACCTACCACGCCGAGCGGTACCCGGTCGGCAGGGAACTGCTG
CTCAACACCGCCGCCCAGGGCCAGGTCTTCCTGCGCGGCCCGGAAGTGGACCCGCTGCGC
GAGGTCCTGCGGCGACTGCTGAACATCCGGGAGGTGTCCGTCCTGCTGGCCGACGGAGTC
AGCGGACTGGACATCCGCTACGACATGGGCCTCCCGGAAGCACCGCCACCCACGGGTGAA
CGGCTGCCGCCGGACGTGTTCCACGTCGTCGGGACCGGCGGCGACGCCGTCGAGGAGTTG
CGGCACGGCGCCGCTCTGCTGATCGTCCCGTCCCCCGACAGCCCGGCGTCCTCGCTGGTC
GCTCCGTGGCGGGACCAGGTGCGCGTCGTGCACGCGCGCCCCACGGACCCGGACTGGGGC
GGGGAGCCGGCCGCGTCGTCGCACTGGTTCGTACGACCGGACGGACACATCGCGTGGGCG
GGCACCGAATTCAGCGAGTTGAGCGCCTCACTGAGCCGCTGGCTCGGTCAGCCCGCCGCG
TAA

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09
show BLAST table
InterPro
Database:interpro:38.0
IPR002938 Monooxygenase, FAD-binding (Domain)
 [13-340]  3.79999999999991e-77 PF01494
PF01494   FAD_binding_3
IPR003042 Aromatic-ring hydroxylase-like (Domain)
 [14-36]  1.10000150671643e-40 PR00420 [154-169]  1.10000150671643e-40 PR00420 [277-292]  1.10000150671643e-40 PR00420 [292-308]  1.10000150671643e-40 PR00420 [310-328]  1.10000150671643e-40 PR00420 [328-344]  1.10000150671643e-40 PR00420
PR00420   RNGMNOXGNASE
SignalP No significant hit
TMHMM No significant hit