Madu_00100 : CDS information

close this sectionLocation

Organism
StrainATCC 39144
Entry nameMaduropeptin
Contig
Start / Stop / Direction19,089 / 17,470 / - [in whole cluster]
19,089 / 17,470 / - [in contig]
Locationcomplement(17470..19089) [in whole cluster]
complement(17470..19089) [in contig]
TypeCDS
Length1,620 bp (539 aa)
Click on the icon to see Genetic map.

close this sectionAnnotation

Category3.3 modification reduction
Productputative FADH2-dependent monooxygenase
Product (GenBank)monooxygenase
GenemdpC
Gene (GenBank)mdpC3
EC number
Keyword
  • two-component system
  • (S)-3-(2-chloro-3-hydroxy-4-methoxyphenyl)-3-hydroxypropionic acid
Note
Note (GenBank)
Reference
ACC
PmId
[17918933] Characterization of the maduropeptin biosynthetic gene cluster from Actinomadura madurae ATCC 39144 supporting a unifying paradigm for enediyne biosynthesis. (J Am Chem Soc. , 2007)
comment
Maduropeptin生合成遺伝子クラスターの報告

GenBankではこのORFはmdpC3 monooxygenaseと登録されているが、論文中ではmdpC monooxygenaseとして記載している。登録間違えか。


mdpC: Monooxygenase

Eight genes (mdpC to mdpC8 excluding mdpC5)は、L-alpha-tyrosineからの(S)-3-(2-chloro-3-hydroxy-4-methoxyphenyl)-3-hydroxypropionic acid moietyの生合成に関与するとしている。

MdpCは、4'-hydroxyphenyl-3-ketopropionic acidを水酸化する酵素だと推測している。
機能解析はされていない。
Related Reference
ACC
Q8GMG6
NITE
C1027_00270
PmId
[16104723] Biosynthesis of the beta-amino acid moiety of the enediyne antitumor antibiotic C-1027 featuring beta-amino acyl-S-carrier protein intermediates. (J Am Chem Soc. , 2005)
[18426211] Characterization of the two-component, FAD-dependent monooxygenase SgcC that requires carrier protein-tethered substrates for the biosynthesis of the enediyne antitumor antibiotic C-1027. (J Am Chem Soc. , 2008)
comment
Streptomyces globisporus
Chlorophenol-4-monooxygenase

[PMID:16104723]
C-1027のbeta-amino acid moiety生合成の報告

SgcC2のFT-MSの結果と、SgcC1のアミノ酸依存性のATP-[32P]PPi exchange dataは、SgcC1が(S)-beta-tyrosine特異的なadenylation enzymeで、SgcCとSgcC3はbeta-aminoacyl-S-SgcC2を基質として利用すると明記あり。


[PMID:18426211] abstのみ
SgcCの機能解析

・two-componentでflavin adenine dinucleotide (FAD)-dependent monooxygenaseであった。
・基質と結合したSgcC2(peptidyl carrier protein)と共に活性化する。
・O2とFADH2を要求するhydroxylationを触媒する。
・3-substituted beta-tyrosyl-S-SgcC2 analoguesのregioselective hydroxylationを効率的に触媒する。

close this sectionSequence

selected fasta
>putative FADH2-dependent monooxygenase [monooxygenase]
MTESPRPPSAEPGAEPGGEPGAPRRRTRPLTGDEYLESLRDGREIHLYGDRVKDVTTHPA
FRNPSRMTARLYDALHDPARRDELTVPTDTGSDGRTHPFFTTPRDSGDLVAAQRAIAGWA
RMSYGWMGRSPDYKGSFLGTLGANAEFYEPFSDNARRWYAEAQEKVLYWNHAIVHPPVDR
NRPPDEVADVFVHVERETDAGLVVSGAKVVATASALTHHTFLAHYGLPVRKREFALIATV
PMDAPGLKLICRPSYSAAAAVMGSPFDYPLSSRLDENDTILVLDKVLIPWENVFVYGDLG
KVQMFTARSGFPERFTFHGCTRLAVKLDFLAGLLTKAVELTGTAGFRGVQTRLGEVLAWR
NLFWGLSDAAARTPVPWKDGSVLPNPDYGMAYRWFMQLGYPRIREIALQDVASGLIYVNS
SAEDFADPEVRPYLDKYLRGSGGADSVERVKLMKLLWDAVGSEFGGRHELYERNYAGNHE
NTRVELLAAQTVGGQLDAYKAFVDECLAEYDLDGWRVPDLDSFPGLRGLRDRLAEGGGA
selected fasta
>putative FADH2-dependent monooxygenase [monooxygenase]
ATGACCGAGAGCCCACGACCGCCGTCCGCGGAGCCCGGTGCGGAGCCCGGCGGGGAGCCC
GGTGCGCCGCGGCGCCGGACGCGTCCCCTCACCGGGGACGAGTACCTGGAGTCGCTGCGC
GACGGGCGGGAGATCCACCTGTACGGCGACCGCGTCAAGGACGTCACGACCCATCCGGCG
TTCCGCAACCCGAGCCGGATGACGGCGCGGCTGTACGACGCGCTCCACGATCCCGCGCGG
CGGGACGAGCTGACCGTCCCGACCGACACCGGCTCCGACGGCCGCACCCATCCGTTCTTC
ACCACCCCGCGCGACTCCGGCGACCTGGTCGCGGCGCAGCGGGCCATCGCGGGGTGGGCG
CGGATGAGCTACGGCTGGATGGGCCGCAGCCCCGACTACAAGGGGTCGTTCCTCGGCACG
CTGGGCGCGAACGCCGAGTTCTACGAGCCGTTCTCCGACAACGCCCGCCGCTGGTACGCC
GAGGCCCAGGAGAAGGTGCTGTACTGGAACCACGCGATCGTCCATCCGCCGGTCGACCGG
AACCGCCCGCCCGACGAGGTCGCGGACGTGTTCGTCCACGTGGAGCGGGAGACCGACGCC
GGGCTGGTGGTCAGCGGGGCGAAGGTCGTGGCCACCGCCTCCGCGCTGACCCACCACACC
TTCCTGGCGCACTACGGGCTGCCGGTACGCAAGCGGGAGTTCGCGCTCATCGCGACGGTG
CCGATGGACGCGCCGGGGCTGAAGCTGATCTGCCGGCCGTCGTACTCGGCCGCGGCGGCG
GTCATGGGCTCGCCGTTCGACTACCCGCTCTCCTCGCGGCTGGACGAGAACGACACCATC
CTCGTCCTGGACAAGGTCCTCATCCCCTGGGAGAACGTCTTCGTCTACGGCGACCTGGGC
AAGGTGCAGATGTTCACGGCGCGGTCGGGGTTCCCGGAGCGCTTCACCTTCCACGGCTGC
ACCCGGCTGGCCGTGAAGCTGGACTTCCTGGCGGGGCTGCTGACGAAGGCGGTGGAGCTG
ACCGGGACGGCCGGGTTCCGCGGCGTCCAGACCCGCCTGGGCGAGGTGCTGGCCTGGCGG
AACCTGTTCTGGGGGCTGTCGGACGCCGCCGCCCGCACGCCCGTCCCGTGGAAGGACGGC
TCGGTGCTCCCGAACCCCGACTACGGCATGGCGTACCGGTGGTTCATGCAGCTCGGCTAT
CCGCGGATCAGGGAGATCGCGCTCCAGGACGTCGCCAGCGGGCTGATCTACGTCAACTCC
AGCGCCGAGGACTTCGCCGACCCCGAGGTCCGGCCGTACCTCGACAAGTACCTGCGCGGG
TCGGGGGGCGCGGACTCGGTGGAGCGCGTCAAGCTGATGAAGCTGCTCTGGGACGCGGTG
GGCTCGGAGTTCGGCGGACGGCACGAGCTGTACGAGCGCAACTACGCGGGGAACCACGAG
AACACCCGGGTGGAGCTGCTGGCGGCCCAGACCGTCGGGGGGCAGCTGGACGCCTACAAG
GCGTTCGTCGACGAGTGCCTGGCCGAGTACGACCTGGACGGCTGGCGGGTGCCGGACCTG
GACTCGTTCCCCGGCCTCCGCGGCCTGCGCGACCGTCTCGCCGAAGGCGGCGGAGCCTGA

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09
show BLAST table
InterPro
Database:interpro:38.0
IPR004925 HpaB/PvcC/4-BUDH (Family)
 [11-523]  PIRSF000331
PIRSF000331   HpaA_HpaB
IPR006091 Acyl-CoA oxidase/dehydrogenase, central domain (Domain)
 [168-292]  1.99999999999999e-47 G3DSA:2.40.110.10
G3DSA:2.40.110.10   Acyl_CoA_DH/ox_M
IPR009075 Acyl-CoA dehydrogenase/oxidase C-terminal (Domain)
 [293-504]  1.29999999999998e-41 G3DSA:1.20.140.10
G3DSA:1.20.140.10   AcylCoA_DH_1/2_C
 [286-510]  5.8999880940569e-56 SSF47203
SSF47203   AcylCoADH_C_like
IPR009100 Acyl-CoA dehydrogenase/oxidase (Domain)
 [28-296]  3.699978135861e-79 SSF56645
SSF56645   AcylCoA_dehyd_NM
IPR024674 HpaB/PvcC/4-BUDH N-terminal (Domain)
 [31-295]  6.7999999999999e-100 PF11794
PF11794   HpaB_N
IPR024677 4-HPA 3-monooxygenase large component/Pyoverdin chromophore biosynthetic protein (Family)
 [11-534]  PIRSF500125
PIRSF500125   4_HPA_large
IPR024719 HpaB/PvcC/4-BUDH C-terminal (Domain)
 [302-504]  4.09999999999995e-74 PF03241
PF03241   HpaB
SignalP No significant hit
TMHMM No significant hit
Page top