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CDS information : Alnu_00120


close this sectionLocation

Organism
StrainCM020
Entry nameAlnumycin
Contig
Start / Stop / Direction10,613 / 9,372 / - [in whole cluster]
10,613 / 9,372 / - [in contig]
Locationcomplement(9372..10613) [in whole cluster]
complement(9372..10613) [in contig]
TypeCDS
Length1,242 bp (413 aa)
Click on the icon to see Genetic map.

close this sectionAnnotation

Category3.3 modification reduction
ProductFMNH2-dependent monooxygenase
Product (GenBank)AlnT hydroxylase
Gene
Gene (GenBank)alnT
EC number
Keyword
  • two-component system
  • C-8 hydroxylate (finally C-7)
Note
Note (GenBank)
Reference
ACC
PmId
[18940666] Characterization of the alnumycin gene cluster reveals unusual gene products for pyran ring formation and dioxan biosynthesis. (Chem Biol. , 2008)
[22467789] Characterization of the two-component monooxygenase system AlnT/AlnH reveals early timing of quinone formation in alnumycin biosynthesis. (J Bacteriol. , 2012)
[23601640] Biosynthetic conclusions from the functional dissection of oxygenases for biosynthesis of actinorhodin and related streptomyces antibiotics. (Chem Biol. , 2013)
Related Reference
ACC
Q9ZGA9
NITE
Lando_00310
PmId
[15812784] Generation of novel landomycins M and O through targeted gene disruption. (Chembiochem. , 2005)
[22454092] Elucidation of post-PKS tailoring steps involved in landomycin biosynthesis. (Org Biomol Chem. , 2012)
ACC
Q53907
NITE
Actino_00110
PmId
[18245777] Mechanism and regulation of the Two-component FMN-dependent monooxygenase ActVA-ActVB from Streptomyces coelicolor. (J Biol Chem. , 2008)
[19246012] Biosynthesis of actinorhodin and related antibiotics: discovery of alternative routes for quinone formation encoded in the act gene cluster. (Chem Biol. , 2009)
[22086671] Epoxyquinone formation catalyzed by a two-component flavin-dependent monooxygenase involved in biosynthesis of the antibiotic actinorhodin. (Chembiochem. , 2011)
[23601640] Biosynthetic conclusions from the functional dissection of oxygenases for biosynthesis of actinorhodin and related streptomyces antibiotics. (Chem Biol. , 2013)

close this sectionSequence

selected fasta
>FMNH2-dependent monooxygenase [AlnT hydroxylase]
MRERTPLTAWPPGARRPCPRLLPRTTRSMGGARMLDTEELAQQAAESARGAEEARKLDPD
VVKLLVEAGFARHFVPRECGGTEGTFAELTEAVARVGAACPATAWCASLAANLGRMAAYL
PAEGYREVWAQGPDALVVGSLSPFGKAAPAAGGWTVSGRWPYISAVAYADWLLLCATLSD
GAGPRVFAVPRDEVEVVESWESVGMRATGSHTVVASDVFVPERRAFARADLLTGRPTAST
AACHTVLLEAANGLSFAGPLLGAAEGALAQWSAYAVVKARSVLLRPQAPGPSREALAGVL
AHSAGETDAARLLLERCAQVADLGAEVTLEQTRRNLRDTALSVRMLASAVNRLAANGGTT
GYGESAPLQRYWRDVNTSATHVALQFESAALAYAEGRLWTTETTQTSSPAAAR
selected fasta
>FMNH2-dependent monooxygenase [AlnT hydroxylase]
GTGCGCGAACGCACGCCGCTGACGGCATGGCCGCCTGGAGCGCGACGTCCATGCCCACGG
CTGCTTCCCCGCACGACGCGGTCCATGGGAGGCGCAAGGATGCTGGACACCGAGGAACTG
GCCCAACAGGCCGCCGAATCCGCGCGAGGGGCCGAGGAAGCCCGCAAGCTCGACCCCGAC
GTGGTCAAACTGCTGGTCGAGGCCGGCTTCGCCCGGCACTTCGTACCCCGGGAGTGCGGC
GGCACCGAGGGCACCTTCGCGGAGCTCACCGAGGCGGTGGCACGGGTCGGCGCCGCCTGC
CCCGCCACCGCCTGGTGCGCCTCGCTGGCCGCCAACCTGGGCCGGATGGCGGCGTATCTG
CCCGCAGAGGGCTACCGGGAGGTGTGGGCGCAGGGGCCCGACGCGCTCGTCGTCGGCTCC
CTCTCCCCCTTCGGGAAGGCCGCCCCCGCGGCCGGCGGCTGGACAGTGTCCGGGCGCTGG
CCCTACATCAGCGCCGTGGCGTACGCGGACTGGCTGCTGCTGTGCGCCACCCTGTCCGAC
GGGGCCGGGCCCCGGGTCTTCGCGGTTCCCCGGGACGAGGTGGAGGTCGTGGAGAGCTGG
GAGAGCGTCGGTATGCGGGCCACCGGCAGCCACACCGTGGTCGCCTCCGACGTGTTCGTG
CCCGAGCGGCGCGCCTTCGCCCGCGCCGACCTGCTGACGGGCCGCCCCACGGCGTCCACG
GCGGCCTGTCACACCGTGCTGCTGGAAGCGGCCAACGGTCTCTCCTTCGCCGGGCCGCTC
CTTGGCGCCGCCGAGGGCGCGCTCGCCCAGTGGTCGGCGTACGCGGTGGTCAAGGCGCGC
TCCGTACTCCTGCGGCCCCAGGCGCCGGGCCCCAGCCGCGAGGCACTCGCCGGTGTGCTG
GCCCACTCGGCCGGGGAGACGGACGCCGCACGGCTGCTGCTCGAACGGTGCGCGCAGGTC
GCCGACCTGGGCGCGGAGGTGACACTCGAGCAGACCCGGCGCAATCTGCGCGACACCGCC
CTGTCGGTACGGATGCTGGCCTCCGCGGTCAACCGCCTCGCGGCGAACGGCGGCACCACG
GGCTACGGCGAGAGCGCCCCGCTGCAGCGCTACTGGCGGGACGTCAACACCTCGGCCACC
CACGTGGCCCTCCAGTTCGAATCGGCGGCGCTCGCCTACGCCGAGGGCCGGCTGTGGACC
ACGGAGACCACGCAGACCAGCAGTCCGGCAGCGGCCCGGTAG

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09
show BLAST table
InterPro
Database:interpro:38.0
IPR006091 Acyl-CoA oxidase/dehydrogenase, central domain (Domain)
 [140-211]  6.70000000000001e-25 G3DSA:2.40.110.10
G3DSA:2.40.110.10   Acyl_CoA_DH/ox_M
IPR006092 Acyl-CoA dehydrogenase, N-terminal (Domain)
 [39-109]  0.00023 PF02771
PF02771   Acyl-CoA_dh_N
IPR009075 Acyl-CoA dehydrogenase/oxidase C-terminal (Domain)
 [212-398]  4.00000000000001e-28 G3DSA:1.20.140.10
G3DSA:1.20.140.10   AcylCoA_DH_1/2_C
 [254-381]  3.0999994589937e-07 SSF47203
SSF47203   AcylCoADH_C_like
IPR009100 Acyl-CoA dehydrogenase/oxidase (Domain)
 [35-228]  6.39998633403535e-32 SSF56645
SSF56645   AcylCoA_dehyd_NM
IPR013107 Acyl-CoA dehydrogenase, type 2, C-terminal (Domain)
 [254-385]  6.40000000000001e-28 PF08028
PF08028   Acyl-CoA_dh_2
IPR013786 Acyl-CoA dehydrogenase/oxidase, N-terminal (Domain)
 [37-135]  1.4e-27 G3DSA:1.10.540.10
G3DSA:1.10.540.10   AcylCoA_DH/ox_N
SignalP No significant hit
TMHMM No significant hit