Soraph_00030 : CDS information

close this sectionLocation

Organism
StrainSo ce26
Entry nameSoraphen
Contig
Start / Stop / Direction8,896 / 7,505 / - [in whole cluster]
8,896 / 7,505 / - [in contig]
Locationcomplement(7505..8896) [in whole cluster]
complement(7505..8896) [in contig]
TypeCDS
Length1,392 bp (463 aa)
Click on the icon to see Genetic map.

close this sectionAnnotation

Category2.1 modification addition of extender units
Productputative oxidoreductase
Product (GenBank)acyl-CoA dehydrogenase
Gene
Gene (GenBank)sorE
EC number
Keyword
  • methoxymalonyl-ACP
Note
Note (GenBank)
Reference
ACC
PmId
[12039053] Characterization of the biosynthetic gene cluster for the antifungal polyketide soraphen A from Sorangium cellulosum So ce26. (Gene. , 2002)
[15289572] Heterologous production of the antifungal polyketide antibiotic soraphen A of Sorangium cellulosum So ce26 in Streptomyces lividans. (Microbiology. , 2004)
comment
[PMID: 12039053](2002)
Soraphen A biosynthetic gene clusterの報告。
SorE(463aa): Acyl-CoA dehydrogenase

Module 3,7で取り込まれるMethoxymalonyl-CoAを合成。
本ORFはCHOをCOOHにしてHydroxymalonylにする。

---
[PMID: 15289572](2004)
sorC破壊株はsoraphen A非産生。

S. lividansでのsor genes異種性発現。
SorABRCDFE株 + cinnamate
SorABRCDFE株 + badA(benzoate-CoA ligase) + benzoate or cinnamate
の組み合わせでSoraphen A産生。
SorABRCDFE株で発現されているのは、the sorA, and the sorB4M, sorRCDFE operons.
Related Reference
ACC
Q7BQ72
PmId
[16983083] Hydroxymalonyl-acyl carrier protein (ACP) and aminomalonyl-ACP are two additional type I polyketide synthase extender units. (Proc Natl Acad Sci U S A. , 2006)
comment
27th(Q7BQ72) 40%, 6e-67
Bacillus cereus_zmaI
ZmaI

aminomalonyl-ACPの合成に関与。
ZmaGとZmaIは一緒に加えられたときのみ、seryl-ZmaH(ACP)を変換可能。
hydroxymalonyl-ACP生合成に関与するZmaI homologのZmaEでの置換はできない。

--
ZmaE(Q9XBU5)とも相同性はそんなに変わらない(30th, id39%, 3e-59)
同じ論文内で、ZmaEもZmaGと共に働き、glyceryl-ZmaD(ACP)からhydroxymalonyl-ZmaD(ACP)への酸化をすると示されている。

close this sectionSequence

selected fasta
>putative oxidoreductase [acyl-CoA dehydrogenase]
MPLSLAPEHEARRVEFQGFVDEHVAPFADAFHRAQRTPPELIALLAERGYLGISIPKEFG
GAGEDAVTLGLLAAELARGCSSVRSLLTVHTMVALAILRWGTRAQRERWLPELASGRRIG
ALALSEPGVGSDAKSVTTRIAAQGTDLVIDGEKRWITYGEIADLFLVFGRTEEGPTAVLV
ERGRPGLRTEPIRDLLGIRASMTASVHLDGCRVEADHVVGRRGLGITQVASVALDLGRYT
VAWGCVGILRACVEACVAYTSRREQFGAPLKEHQLVRRMISDMFTDLHASEMLCMEAGRL
RDRRDPGALSATAMAKYFASTWIDWGSFEGPVTTAVWMPRILGFFARRGAAKGAPLGTAA
NSFSHASSPLRPRDRSSTATNSPFRNGSLAPSTVIGAPQRRPAARLLPRQTSTSPRSELI
RPRDRRDPSALEVKPPGYWKWRMDHGPGAGVVAVGGSSGFSKS
selected fasta
>putative oxidoreductase [acyl-CoA dehydrogenase]
ATGCCCCTGTCCCTCGCCCCCGAGCACGAAGCGCGACGCGTCGAGTTTCAGGGTTTCGTC
GACGAGCACGTCGCGCCGTTCGCCGACGCGTTCCACCGGGCCCAGCGGACGCCGCCGGAG
CTCATCGCGCTCCTCGCCGAGCGCGGGTACCTCGGCATCTCCATCCCCAAAGAGTTCGGG
GGTGCCGGCGAGGACGCCGTGACGCTCGGGCTCCTCGCGGCGGAGCTCGCCCGCGGCTGC
TCGTCGGTGCGCAGCCTGCTCACCGTCCACACGATGGTGGCGCTGGCGATCCTCCGGTGG
GGCACCCGCGCGCAGCGAGAACGGTGGCTGCCGGAGCTCGCGTCGGGTCGCCGGATCGGG
GCGCTCGCGCTGTCCGAGCCGGGCGTCGGCAGCGACGCCAAGAGCGTCACGACGCGGATC
GCCGCCCAGGGGACCGATCTCGTGATCGACGGCGAGAAGAGGTGGATCACGTACGGCGAG
ATCGCCGACCTCTTCCTCGTCTTCGGGCGCACCGAGGAAGGGCCCACGGCTGTCCTCGTC
GAGCGCGGTCGGCCGGGCCTCCGGACCGAGCCGATCCGCGATCTGCTGGGCATCCGCGCG
TCGATGACCGCGAGCGTGCATCTCGATGGATGCCGCGTGGAGGCCGACCACGTGGTGGGG
CGGCGAGGTTTGGGCATCACGCAGGTCGCCTCCGTCGCGCTCGATCTGGGCCGGTACACC
GTCGCGTGGGGCTGCGTGGGCATCCTCCGGGCGTGCGTCGAGGCCTGCGTCGCGTACACG
AGCCGCCGCGAGCAATTCGGCGCGCCGCTGAAGGAGCACCAGCTCGTCCGGCGGATGATC
AGCGACATGTTCACGGACCTGCACGCCTCGGAGATGCTGTGCATGGAGGCCGGCCGCCTG
CGTGACCGCCGAGATCCCGGCGCGCTCTCGGCGACGGCGATGGCCAAGTACTTCGCGTCG
ACGTGGATCGACTGGGGCTCGTTCGAGGGGCCCGTCACGACGGCCGTCTGGATGCCGCGG
ATCCTGGGCTTCTTCGCGCGCAGGGGCGCGGCGAAGGGCGCGCCCTTGGGGACGGCGGCG
AACTCGTTCTCGCACGCATCCTCGCCGCTGCGACCTCGCGATCGCAGCTCTACCGCGACG
AACTCGCCATTCAGGAACGGCTCGTTGGCCCCCTCGACCGTCATCGGCGCGCCGCAGCGG
AGGCCTGCCGCGCGGCTCCTCCCGCGGCAGACGTCCACGTCACCGCGCAGCGAGCTGATA
CGGCCCCGCGACCGGCGCGATCCCTCGGCGCTCGAGGTGAAGCCGCCCGGGTATTGGAAG
TGGCGGATGGACCACGGACCTGGTGCGGGGGTCGTCGCCGTAGGGGGTAGCTCGGGCTTC
TCGAAGTCGTAG

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09
show BLAST table
InterPro
Database:interpro:38.0
IPR006090 Acyl-CoA oxidase/dehydrogenase, type 1 (Domain)
 [227-322]  7.7e-21 PF00441
PF00441   Acyl-CoA_dh_1
IPR006091 Acyl-CoA oxidase/dehydrogenase, central domain (Domain)
 [121-171]  4.5e-16 PF02770
PF02770   Acyl-CoA_dh_M
 [121-212]  2.3e-28 G3DSA:2.40.110.10
G3DSA:2.40.110.10   Acyl_CoA_DH/ox_M
IPR006092 Acyl-CoA dehydrogenase, N-terminal (Domain)
 [7-117]  1.1e-28 PF02771
PF02771   Acyl-CoA_dh_N
IPR009075 Acyl-CoA dehydrogenase/oxidase C-terminal (Domain)
 [213-321]  9.60000000000004e-29 G3DSA:1.20.140.10
G3DSA:1.20.140.10   AcylCoA_DH_1/2_C
 [221-320]  3.80000697093586e-21 SSF47203
SSF47203   AcylCoADH_C_like
IPR009100 Acyl-CoA dehydrogenase/oxidase (Domain)
 [1-223]  1.09999184471405e-71 SSF56645
SSF56645   AcylCoA_dehyd_NM
IPR013786 Acyl-CoA dehydrogenase/oxidase, N-terminal (Domain)
 [1-118]  1.6e-33 G3DSA:1.10.540.10
G3DSA:1.10.540.10   AcylCoA_DH/ox_N
SignalP
 [1-30]  0.071 Signal
Bacteria, Gram-positive   
TMHMM No significant hit
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