Avil_00200 Avil_00200   Avil_00220 Avil_00220

Avil_00210 : CDS information

close this sectionLocation

Organism
StrainTü57
Entry nameAvilamycin
Contig
Start / Stop / Direction17,621 / 21,502 / + [in whole cluster]
17,621 / 21,502 / + [in contig]
Location17621..21502 [in whole cluster]
17621..21502 [in contig]
TypeCDS
Length3,882 bp (1,293 aa)
Click on the icon to see Genetic map.

close this sectionAnnotation

Category1.1 PKS
Productpolyketide synthase
orsellinic acid synthase
Product (GenBank)polyketide synthase
Gene
Gene (GenBank)aviM
EC number
Keyword
  • iterative
  • dichloroisoeverninic acid
Note
Note (GenBank)
  • AviM
Reference
ACC
PmId
[9335272] Cloning of an avilamycin biosynthetic gene cluster from Streptomyces viridochromogenes Tu57. (J Bacteriol. , 1997)
[11410376] Biosynthesis of the orthosomycin antibiotic avilamycin A: deductions from the molecular analysis of the avi biosynthetic gene cluster of Streptomyces viridochromogenes Tu57 and production of new antibiotics. (Chem Biol. , 2001)
comment
[PMID:9335272]
Avilamycin生合成遺伝子クラスターの報告。

ORF1-4(orf1,aviM,aviD,aviE)のcloning。
このORFは、ORF2(aviM)。
AviMは6-methylsalicylic acid synthase(MSAS)と37% identity。
ORF2を含むプラスミドを導入したS.lividance TK24とS.coelicolor CH999の培養液からdichloroisoeverninic acidの中間体であるorsellinic acidを検出した。AviMのモチーフ構成は、MSASが持つdehydratase domainとketo reductase domainを保存しておらず、MSASと同様にthioseteraseも保存していなかった。
サザンハイブリットによりtype II polyketide synthaseではなくtype I polyketide synthaseであることを確認。


[PMID:11410376]
Avilamycin生合成遺伝子クラスターの報告。
完全長のcloning解析。

AviM:6-methylsalicylic acid synthase from Penicillium patulum [Proposed function:Orsellinic acid biosynthesis]
Related Reference
ACC
P87162
PmId
comment
Aspergillus terreus_atX
6-methylsalicylic acid synthase

6-methylsalicylic acid synthase_ATXのdehydratase(DH) domainの機能的検証。
DH domainはACPに繋がれたbeta-hydroxytriketide中間体のdehydrationに関連しないが、ACPから6- methylsalicylic acidを放出するためにthioester hydrolysisを触媒することが明らかになった。
よってDH domainからTH domain(Gly904 - Thr1048の145aa)へ改名。

構造解析報告のあるEryDH4とのalignmentから、H972XXXGXXXXP motif and Asp1129 が触媒に重要な残基であると提唱されている。著者らの既報で、ATX H972A mutantがbeta-hydroxy triketideのような産物をもたらさないことが確認されている。

close this sectionPKS/NRPS Module

1 acetyl-CoA
malonyl-CoA
KS24..406
AT559..873
TH882..1027
ACP1210..1279

close this sectionSequence

selected fasta
>polyketide synthase [polyketide synthase]
MMNTGNDERNMPVISLDRPADSLSPVAVVGIGCRFPGGVNSPGEFWDLLTAGRNTVGEMP
PDRWEEYRDFGPRFDAALRTAIRSGSFLDDDIAGFDAEFFGISPREAELMDPQQRLMLEV
AWQALEHAGIPPHTLAGTDTGVFAGVCTYDYGAGRLEDLPNIDAWTGIGAAVCAVSNRVS
HALDLRGPSLSIDTACSASLVALHTAAQSLRLGECTVALAGGVNLLVSPGQTIALGTAGA
LAPDGRSKPFAASAGRYAVAASADGYGRGEGCGVLVIKLLTDAVRDGDRVLAVLRGSAFN
QDGRTNGIMAPCGQAQEHVMRRALTAAGVAADTVDFVEAHGTGTRLGDPMEIGAIAAVYG
RDRSGQEPCAVGSVKSNIGHLEGAAGVAGVIKAILALDEDRIPASLLDGDPNPEIDWAGL
DIRLATRALPWPERPHPRRAAVSGFGYGGTVAHVVLEQAPTAPARPAPEPAGTLFPVSAA
SPEALRDRAAALAERVEEGADLASVGHTLAHRQSPLVHRAAVVATGRDELAAGLRALATQ
EPAPGLVTGAALPDAGRPVWVFSGHGSQWAGMGRELLEAEPVFAEVIDELEPVFKEEIGF
SPRQMLLEGDHTEVDGAQTMIFAMQLGLAALWRSRGVEPAAVIGHSVGEIAAAVTAGALT
VTDGARLICRRSLLLREAAGRGAMAMVSLPFDEAAERLAGNDAVVAAIASSTTSTVISGD
PGEVEKVVGRWTDEGLVVRRVASDVAFHSPHMDPLLDRLRAAADELSPSAPHTPLYTTAL
ADPRATVTADGAYWAANLRNPVRLAAAITAAAEDGHRAFVELSPHPVVAHSIHETLAERG
VEDVFVGPTLRRNQPEARTFRAAVGAAHCHGVSVDWSALQPNGNLEVLPPYPWQHRPLWR
SIAGARAAERGHDVDSHTLLGTPGGVAGSDLRLWHSTLDDDSRPYPGSHALNGVEIVPAA
VLAVTFLAAGAEGEERRALQDMTMTHPVLTAGQRQIQVVREGEVVRLASRTVADAADPNP
AWLVHAEARTAAPDLAGLAARSLLDPGEHRLEPADPGLVSRRLAEVGVPSTGFDWSVERL
SAGLGVLHAQVLSPDASSWAPLLDAVMSIAPAAFVGLPQLRMVVHVDEITVDGTPPEAAT
VEVALDPRVADTVHALVTDGEGRPVASLRGLRYPVVEQPAAPDTDEPGGDADADVVSFAG
LSPEELRSRVLDEVREQIAQEMRLAPTALHVRRPLVEQGLDSVMTVVVRRRLEKRLGRDV
PANIFWKLPTISDIVDHLTERLTEHPTADGHAS
selected fasta
>polyketide synthase [polyketide synthase]
ATGATGAATACCGGCAACGACGAACGGAATATGCCCGTGATATCCCTTGATCGCCCGGCG
GACTCCCTCTCTCCGGTGGCCGTGGTCGGGATCGGATGCCGGTTCCCCGGTGGTGTCAAC
TCGCCCGGCGAATTCTGGGACCTGTTGACGGCCGGACGCAACACCGTCGGCGAGATGCCC
CCCGACCGCTGGGAAGAGTACCGGGACTTCGGTCCGCGGTTCGATGCGGCGCTGCGGACG
GCGATTCGCTCCGGCAGTTTCCTGGACGACGACATAGCGGGTTTCGACGCCGAGTTCTTC
GGCATCTCGCCGCGCGAGGCCGAGCTGATGGACCCGCAGCAGCGCCTGATGCTGGAGGTG
GCCTGGCAGGCACTGGAGCACGCGGGCATCCCGCCGCACACCCTGGCAGGGACCGACACC
GGTGTGTTCGCCGGGGTCTGCACCTACGACTATGGCGCCGGACGGCTGGAAGACCTGCCG
AACATCGACGCATGGACGGGGATCGGCGCGGCGGTGTGCGCCGTGTCCAACCGCGTCTCT
CACGCGCTCGACCTGCGCGGGCCCAGCCTCTCCATCGACACCGCGTGCTCGGCCTCCCTG
GTGGCGCTGCACACCGCCGCGCAGAGCCTGCGGCTCGGCGAGTGCACCGTGGCGCTGGCC
GGGGGCGTCAACCTGCTGGTGTCACCGGGCCAGACGATCGCCCTGGGCACGGCCGGCGCG
CTGGCGCCCGACGGCCGGAGCAAGCCGTTCGCCGCGTCGGCCGGACGCTACGCCGTTGCC
GCGTCGGCCGACGGCTACGGCCGCGGCGAGGGCTGCGGCGTGCTGGTCATCAAGCTGCTG
ACGGACGCCGTACGCGACGGTGACCGGGTGCTGGCGGTGCTGCGCGGCAGCGCGTTCAAC
CAGGACGGGCGCACCAACGGCATCATGGCCCCCTGCGGGCAGGCCCAGGAGCACGTCATG
AGGCGCGCCCTGACGGCCGCGGGCGTCGCTGCCGACACCGTTGACTTCGTCGAGGCCCAC
GGCACCGGTACCCGCCTCGGCGACCCCATGGAGATCGGCGCGATCGCCGCCGTCTACGGA
CGTGACCGCTCCGGTCAGGAGCCGTGCGCGGTCGGGTCGGTGAAGTCCAACATCGGGCAT
CTGGAGGGGGCCGCCGGGGTCGCCGGGGTCATCAAGGCGATCCTCGCCCTCGACGAGGAC
CGGATCCCGGCCAGCCTGCTGGACGGCGACCCGAACCCCGAGATCGACTGGGCCGGCCTC
GACATCCGGCTGGCGACCCGGGCCCTGCCGTGGCCCGAGCGTCCGCACCCCCGCCGGGCG
GCTGTGTCCGGTTTCGGCTACGGCGGCACCGTGGCCCATGTGGTCCTCGAACAGGCGCCC
ACCGCGCCCGCCCGCCCCGCGCCGGAGCCGGCCGGAACCCTGTTCCCGGTGTCCGCGGCC
TCCCCGGAGGCGCTCCGTGACCGCGCGGCCGCGCTCGCCGAGCGGGTCGAGGAGGGCGCT
GACCTGGCCTCGGTCGGGCACACCCTGGCCCATCGGCAGTCCCCGCTGGTCCACCGGGCG
GCCGTCGTGGCGACCGGCCGGGACGAACTGGCCGCCGGGCTGCGCGCGCTGGCCACTCAG
GAACCCGCGCCCGGTCTCGTCACCGGGGCCGCGCTGCCGGATGCCGGCCGTCCCGTCTGG
GTGTTCTCGGGTCACGGGTCCCAGTGGGCCGGGATGGGCCGCGAACTGCTGGAAGCCGAG
CCGGTCTTCGCCGAGGTGATCGACGAACTGGAGCCGGTGTTCAAGGAGGAGATCGGGTTC
TCGCCCCGGCAGATGCTGCTGGAGGGCGACCACACCGAGGTCGACGGCGCCCAGACCATG
ATCTTCGCGATGCAGCTCGGGCTCGCCGCGCTGTGGCGGTCACGGGGCGTCGAGCCCGCC
GCCGTCATCGGCCACTCGGTCGGTGAGATCGCCGCCGCCGTCACCGCCGGGGCGCTGACC
GTGACCGACGGGGCCCGGCTGATCTGCCGTAGGTCGCTGCTGCTGCGCGAGGCCGCGGGG
CGTGGCGCGATGGCGATGGTCAGTCTGCCCTTCGACGAGGCCGCCGAGCGGCTCGCGGGC
AATGACGCGGTGGTCGCGGCCATCGCGTCCTCGACGACGTCCACCGTGATCTCCGGTGAC
CCCGGCGAGGTCGAGAAGGTCGTCGGCCGCTGGACCGACGAGGGGCTGGTCGTACGGCGG
GTCGCCTCCGACGTGGCCTTCCACAGCCCGCACATGGACCCCCTGCTCGACCGGCTGCGC
GCGGCCGCCGACGAGCTGAGTCCCAGCGCACCGCACACGCCGCTCTACACGACGGCGCTC
GCGGACCCGCGGGCCACGGTGACCGCCGACGGCGCGTACTGGGCGGCGAACCTGCGCAAC
CCGGTGCGGCTCGCCGCCGCGATCACCGCGGCGGCCGAGGACGGCCACCGGGCGTTCGTC
GAGCTGTCCCCGCACCCCGTGGTCGCGCACTCGATCCACGAGACGCTGGCCGAACGCGGC
GTGGAGGACGTGTTCGTCGGACCGACGCTACGGCGCAACCAGCCCGAGGCCCGGACCTTC
CGCGCCGCCGTGGGCGCCGCCCACTGCCACGGCGTGAGCGTGGACTGGTCGGCGCTCCAG
CCGAACGGGAACCTCGAAGTCCTGCCGCCCTACCCCTGGCAGCACCGCCCGCTGTGGCGT
TCCATCGCCGGGGCGCGAGCGGCCGAGCGCGGCCACGACGTCGACTCCCACACGCTGCTG
GGCACGCCCGGCGGCGTCGCGGGCAGCGACCTGCGGCTGTGGCACAGCACGCTGGACGAC
GACAGCCGCCCGTACCCGGGCAGCCACGCCCTCAACGGCGTGGAGATCGTCCCGGCCGCC
GTGCTGGCGGTCACGTTCCTGGCGGCCGGCGCCGAGGGCGAAGAGCGCCGCGCCCTCCAG
GACATGACGATGACCCACCCGGTGCTGACGGCGGGTCAGCGGCAGATCCAGGTCGTCCGC
GAGGGCGAGGTGGTGCGGCTGGCCTCCCGGACGGTCGCGGACGCCGCCGACCCGAACCCC
GCCTGGCTCGTCCATGCCGAGGCCCGGACGGCCGCGCCGGACCTCGCCGGTCTGGCGGCG
CGGTCGCTGCTGGACCCGGGCGAGCACCGGCTCGAACCGGCCGACCCCGGCCTGGTCTCC
CGGCGGCTGGCCGAGGTGGGCGTACCCTCGACCGGTTTCGATTGGAGCGTCGAGCGACTG
TCCGCCGGTCTCGGTGTACTGCACGCTCAGGTGCTCTCGCCCGACGCCTCGTCCTGGGCC
CCGCTGCTGGACGCCGTGATGTCGATCGCGCCGGCCGCCTTCGTGGGCCTCCCGCAGCTC
CGCATGGTCGTGCACGTCGACGAGATCACCGTCGACGGCACGCCACCGGAGGCGGCGACG
GTCGAGGTCGCGCTCGATCCCCGCGTCGCCGACACCGTGCACGCCCTGGTCACGGACGGG
GAGGGACGCCCGGTGGCGAGCCTGCGCGGCCTGCGCTACCCGGTGGTCGAGCAGCCGGCC
GCGCCGGACACCGACGAGCCGGGCGGCGACGCGGACGCGGACGTGGTGTCGTTCGCGGGT
CTGTCGCCGGAGGAGCTGCGTTCCCGGGTGCTCGACGAGGTGCGCGAGCAGATCGCGCAG
GAGATGCGACTCGCCCCCACGGCCCTGCACGTTCGCCGCCCGCTGGTGGAGCAGGGGCTC
GACTCGGTGATGACGGTGGTGGTCCGCCGCCGGCTGGAGAAGCGCCTCGGCCGGGACGTG
CCGGCCAACATCTTCTGGAAGCTGCCCACCATCAGCGACATCGTCGATCACCTGACCGAA
CGCCTCACGGAACACCCGACGGCGGACGGCCATGCGTCCTGA
[1] KS24..406
[1] AT559..873
[1] acetyl-CoA malonyl-CoA745..749
[1] TH882..1027
[1] ACP1210..1279
[1] KS70..1218
[1] AT1675..2619
[1] acetyl-CoA malonyl-CoA2233..2247
[1] TH2644..3081
[1] ACP3628..3837

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09 		show BLAST table
InterPro
Database:interpro:38.0
IPR001227 Acyl transferase domain (Domain)
[556-678] 1e-66 G3DSA:3.40.366.10 [745-862] 1e-66 G3DSA:3.40.366.10
G3DSA:3.40.366.10   Ac_transferase_reg
IPR009081 Acyl carrier protein-like (Domain)
[1201-1286] 5.49999338756182e-18 SSF47336
SSF47336   ACP_like
[1208-1284] 3.8e-15 G3DSA:1.10.1200.10
G3DSA:1.10.1200.10   ACP_like
[1213-1278] 8.9e-10 PF00550
PF00550   PP-binding
[1210-1279] PS50075
PS50075   ACP_DOMAIN
IPR014030 Beta-ketoacyl synthase, N-terminal (Domain)
[24-283] 4.69999999999992e-91 PF00109
PF00109   ketoacyl-synt
IPR014031 Beta-ketoacyl synthase, C-terminal (Domain)
[291-406] 1.09999999999999e-43 PF02801
PF02801   Ketoacyl-synt_C
IPR014043 Acyl transferase (Domain)
[559-873] 1.69999999999998e-98 PF00698
PF00698   Acyl_transf_1
IPR016035 Acyl transferase/acyl hydrolase/lysophospholipase (Domain)
[557-854] 4.30000170645869e-63 SSF52151
SSF52151   Acyl_Trfase/lysoPlipase
IPR016036 Malonyl-CoA ACP transacylase, ACP-binding (Domain)
[680-744] 1.29999924468179e-11 SSF55048
SSF55048   Malonyl_transacylase_ACP-bd
IPR016038 Thiolase-like, subgroup (Domain)
[25-293] 6.29999999999998e-91 G3DSA:3.40.47.10 [295-461] 4.5e-62 G3DSA:3.40.47.10
G3DSA:3.40.47.10   Thiolase-like_subgr
IPR016039 Thiolase-like (Domain)
[16-461] 3.10001307370203e-94 SSF53901
SSF53901   Thiolase-like
IPR018201 Beta-ketoacyl synthase, active site (Active_site)
[187-203] PS00606
PS00606   B_KETOACYL_SYNTHASE
IPR020801 Polyketide synthase, acyl transferase domain (Domain)
[561-854] 4.99996518094122e-95 SM00827
SM00827   PKS_AT
IPR020806 Polyketide synthase, phosphopantetheine-binding domain (Domain)
[1211-1282] 2.30000440726534e-17 SM00823
SM00823   PKS_PP
IPR020841 Polyketide synthase, beta-ketoacyl synthase domain (Domain)
[26-461] SM00825
SM00825   PKS_KS
SignalP
[1-41] 0.048 Signal
Eukaryota   
TMHMM No significant hit
Avil_00200 Avil_00200   Avil_00220 Avil_00220
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