Heda_00010 Heda_00010   Heda_00030 Heda_00030

Heda_00020 : CDS information

close this sectionLocation

Organism
StrainATCC 15422
Entry nameHedamycin
Contig
Start / Stop / Direction9,332 / 6,375 / - [in whole cluster]
9,332 / 6,375 / - [in contig]
Locationcomplement(6375..9332) [in whole cluster]
complement(6375..9332) [in contig]
TypeCDS
Length2,958 bp (985 aa)
Click on the icon to see Genetic map.

close this sectionAnnotation

Category1.1 PKS
Productpolyketide synthase
Product (GenBank)type I PKS
GenehedT
Gene (GenBank)
EC number
Keyword
  • starter unit
Note
Note (GenBank)
  • orf31
Reference
ACC
PmId
[15271354] The hedamycin locus implicates a novel aromatic PKS priming mechanism. (Chem Biol. , 2004)
[19942143] In vivo and in vitro analysis of the hedamycin polyketide synthase. (Chem Biol. , 2009)
comment
[PMID: 15271354](2004)
hedamycinの生合成gene clusterの報告。

hedT: Type I PKS
KSq (20-428), ATL(542-859), ACPL (923-969)

KS domainのactive site cysteineはglytamineによって置換されており、acetyl starter unitを産生するためにmalonyl-CoAをdecarboxylateするloading moduleとして役立つと示唆される。
AT domainはmalonyl-CoA transferのために必要な保存motifを含む。

hedT破壊株ではhedamycin非産生。

---
[PMID: 19942143](2009)
HedS or HedFが鎖合成の開始、伸長に関係しないことがわかったので、HedT and HedUによってコードされるtype I PKSがhedamycin aglyconeの2,4-hexadienyl primer unit合成を担い、それでKS-CLFを直接的にprimeするという生合成モデルを検証。

type I PKS HedT, HedUは発現、精製に失敗したので、HedUのACP domainを分離発現、精製。
このACPは結合したacyl鎖をKS-CLFに移動することを確認。

close this sectionPKS/NRPS Module

0 malonyl-CoA
KSQ20..380
AT542..858
ACP930..969

close this sectionSequence

selected fasta
>polyketide synthase [type I PKS]
MSGTSSSPSLPHGGTAPVGPIAVVGIACRFPDTPNPQAFWRLLREGGHTVRRAPENRRAG
DGTAEWGSFLDGVDRFDAGFFRISPREAAAMDPRQRLVLELGWEVLEDAGIVPAGIAGSR
LGVFVGTIWDDYAHLAYRTARDSAAQHTQTGIHRGIIANRLSHFLRVQGPSMTVDTGQSS
SLVAVHLACESLHRGESEAAVAAGVNLALLAESSLISSRWGGLSPDGRCYTFDARANGYV
RGEGGGAVLLKPLHRAVADGDHVYGVIAGSAVNNGWGDSLTRPSAEAQSQVVRAACARAR
VQPAQVQYVELHGTGTRAGDPVEAAALGEALGSAREPGHPVHVGSVKTNIGHLEGAAGIA
GLIKTLLCLEHRSLPASLNFTAPPPDIDPERLNLTVRQRFGPWPEPEQPLVAGVSAFGMG
GANCHVVVAEAAPYAAPAAGPHRDDGPDEDRRVLPWVVSGRGGAALRAQARRLAAFLEAD
ASVTAGDTARALVTTRALFEDRAVVVGRDRETLLAGLTAVADGRAAPGTVTGRARDGAAA
VLFTGQGGLRPGVGRELYASFGVFAGAFDEVCAELDPLLGVRLADEVFAEEGGTLARTDL
GQAALFALETALYRLVCSLGVRPALVAGHSVGEVAAAHAAGVLSLPDACALIAARGRLMA
ALPPGGAMTAVFAPEAEVAPLLAGREGGVTLAAVNGPRHVVLSGAGPAVEEVTSLLREGG
VRTRPLAVTHAFHSPLMEPVLREFGRVCAGLSYRPPRVPVVSTVTGRIAAGTELCSPEYW
VSHVRRPVRFLDAVRALRERGADTFLELGPDAVLSALVPRCVPDPSPGMAAAVLRAGRPE
EETLLTALGAVHVRGTEVDWAELTPRRGPRVKLPTYAFRRRSHWLETPDRPSAAGTPAPA
RPPAEEEPDRFPSVVRGPSPLPERERRRAVLDLVVEHLAAVLGSTDAEPVDASAPFTDLG
MDSMSALALSEVPVRRRPAWTCRRA
selected fasta
>polyketide synthase [type I PKS]
ATGTCTGGCACTTCCTCCTCTCCATCCCTTCCCCACGGCGGTACGGCTCCCGTCGGGCCG
ATCGCCGTCGTCGGCATCGCGTGCCGCTTCCCCGACACACCCAACCCGCAGGCATTCTGG
CGGCTGCTGCGCGAGGGCGGGCACACGGTGCGCCGGGCGCCCGAGAACCGCAGGGCCGGT
GACGGCACCGCGGAGTGGGGTTCCTTCCTCGACGGGGTGGACCGTTTCGACGCGGGCTTC
TTCCGGATCTCCCCGCGCGAGGCCGCCGCCATGGACCCCCGTCAGCGGCTGGTCCTGGAA
CTGGGCTGGGAGGTCCTCGAAGACGCCGGCATCGTGCCCGCCGGGATCGCCGGCAGCCGG
CTCGGCGTGTTCGTCGGCACGATCTGGGACGACTACGCGCACCTCGCCTACCGCACCGCG
CGCGACTCGGCGGCGCAGCACACCCAGACCGGCATCCACCGGGGCATCATCGCCAACCGG
CTCTCGCACTTCCTGCGGGTCCAGGGTCCGAGCATGACCGTGGACACCGGGCAGTCCTCG
TCCCTGGTCGCGGTGCACCTCGCCTGCGAGAGCCTGCACCGCGGGGAGTCCGAGGCGGCC
GTCGCCGCCGGCGTGAACCTCGCGCTGCTCGCCGAGTCCTCCCTGATCTCCTCCCGCTGG
GGCGGGCTCTCCCCCGACGGCCGCTGCTACACCTTCGACGCCCGCGCCAACGGCTACGTC
CGCGGGGAGGGCGGCGGCGCCGTCCTGCTCAAGCCCCTGCACCGGGCCGTGGCGGACGGA
GACCACGTGTACGGCGTCATCGCGGGGAGCGCGGTGAACAACGGCTGGGGCGACAGCCTC
ACCCGGCCCAGCGCCGAGGCGCAGTCCCAGGTGGTGCGCGCCGCGTGCGCGCGGGCGCGG
GTGCAGCCGGCCCAGGTGCAGTACGTCGAGCTGCACGGCACCGGTACCCGGGCCGGCGAC
CCGGTCGAGGCGGCCGCGCTGGGGGAAGCCCTGGGCAGCGCGCGCGAGCCGGGCCACCCG
GTGCACGTCGGGTCGGTGAAGACCAACATCGGCCACCTCGAAGGCGCGGCAGGCATCGCC
GGGCTCATCAAGACGCTGCTGTGCCTGGAGCACCGGAGCCTGCCGGCCAGCCTCAACTTC
ACAGCCCCGCCCCCGGACATCGACCCGGAACGGCTGAACCTGACGGTGCGGCAGCGGTTC
GGCCCGTGGCCGGAGCCGGAGCAGCCGCTGGTGGCGGGGGTCAGCGCGTTCGGTATGGGC
GGCGCCAACTGCCACGTGGTGGTCGCGGAGGCGGCGCCGTACGCCGCCCCGGCCGCCGGT
CCGCACCGGGACGACGGTCCGGACGAGGACCGCCGGGTGCTGCCCTGGGTGGTGTCCGGA
CGCGGCGGGGCGGCGCTGCGGGCGCAGGCCCGCCGGCTGGCCGCCTTCCTCGAGGCCGAC
GCCTCCGTCACCGCCGGGGACACCGCCCGGGCGCTGGTCACCACCCGCGCCCTCTTCGAG
GACCGGGCCGTGGTGGTGGGCCGCGACCGCGAGACCCTGCTGGCCGGGCTGACCGCGGTG
GCGGACGGGCGGGCGGCGCCGGGCACGGTGACGGGACGGGCCCGCGACGGCGCGGCGGCC
GTGCTGTTCACCGGTCAGGGCGGGCTGCGACCGGGCGTGGGCCGGGAGCTGTACGCGTCC
TTCGGCGTGTTCGCCGGCGCCTTCGACGAGGTGTGCGCCGAGCTCGATCCGCTGCTCGGC
GTCCGCCTCGCGGACGAGGTCTTCGCCGAGGAGGGCGGCACGCTCGCGCGGACGGATCTG
GGCCAGGCCGCGCTGTTCGCCCTGGAGACCGCGCTGTACCGCCTCGTGTGCTCGCTCGGG
GTGCGGCCGGCCCTGGTGGCCGGTCACTCGGTCGGCGAGGTGGCGGCCGCCCACGCGGCC
GGCGTGCTCTCGCTGCCCGACGCCTGCGCGCTGATCGCGGCCCGCGGCCGGCTGATGGCA
GCGCTGCCGCCGGGCGGCGCCATGACGGCCGTCTTCGCCCCGGAGGCGGAGGTGGCGCCG
CTGCTGGCGGGCCGGGAAGGGGGCGTGACGCTGGCGGCGGTCAACGGTCCCCGGCACGTG
GTCCTCTCGGGCGCCGGGCCGGCGGTCGAGGAGGTCACCTCGCTGCTGCGCGAGGGGGGA
GTGCGCACCCGACCGCTGGCGGTCACGCACGCCTTTCACTCCCCGCTCATGGAGCCGGTC
CTGCGGGAGTTCGGGCGGGTGTGCGCCGGGCTGTCGTACCGGCCGCCCCGGGTCCCGGTC
GTGTCCACGGTGACCGGGCGGATCGCGGCCGGGACGGAGCTGTGCTCCCCGGAGTACTGG
GTGAGCCATGTCCGCCGGCCCGTCCGGTTCCTGGACGCCGTCCGCGCCCTTCGTGAACGG
GGGGCGGACACCTTCCTCGAGCTGGGGCCGGACGCGGTGCTGTCCGCTCTCGTGCCGCGC
TGCGTCCCGGACCCCTCCCCCGGCATGGCCGCAGCCGTGCTGCGCGCCGGACGGCCCGAG
GAGGAGACACTGCTGACCGCCCTGGGCGCCGTCCACGTGCGCGGCACCGAGGTGGACTGG
GCGGAGCTGACCCCGCGCCGCGGTCCGAGGGTGAAGCTGCCCACGTACGCCTTCCGGCGC
CGCAGCCACTGGCTGGAGACCCCGGACCGGCCTTCCGCCGCCGGCACCCCCGCCCCGGCG
CGTCCCCCGGCGGAGGAGGAGCCGGACCGCTTCCCCTCCGTCGTGCGGGGCCCGTCCCCG
CTGCCGGAGCGGGAACGGCGACGGGCCGTACTGGACCTGGTGGTCGAGCACCTGGCGGCC
GTGCTCGGCAGCACGGACGCAGAGCCCGTCGACGCCTCCGCGCCCTTCACCGACCTGGGC
ATGGACTCGATGTCGGCGCTCGCGCTCAGCGAGGTACCTGTCAGACGGCGACCGGCCTGG
ACCTGCCGGCGGGCGTGA
[0] KSQ20..380
[0] AT542..858
[0] malonyl-CoA730..734
[0] ACP930..969
[0] KSQ58..1140
[0] AT1624..2574
[0] malonyl-CoA2188..2202
[0] ACP2788..2907

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09 		show BLAST table
InterPro
Database:interpro:38.0
IPR001227 Acyl transferase domain (Domain)
[729-847] 3.1e-69 G3DSA:3.40.366.10
G3DSA:3.40.366.10   no description
IPR009081 Acyl carrier protein-like (Domain)
[933-969] 5.4e-05 PF00550
PF00550   PP-binding
[927-969] 3.1e-06 G3DSA:1.10.1200.10
G3DSA:1.10.1200.10   no description
[922-969] 4.9e-09 SSF47336
SSF47336   ACP-like
[930-969] 11.014 PS50075
PS50075   ACP_DOMAIN
IPR014030 Beta-ketoacyl synthase, N-terminal (Domain)
[20-255] 1.3e-75 PF00109
PF00109   ketoacyl-synt
IPR014031 Beta-ketoacyl synthase, C-terminal (Domain)
[264-380] 2.1e-40 PF02801
PF02801   Ketoacyl-synt_C
IPR014043 Acyl transferase (Domain)
[542-858] 4.6e-58 PF00698
PF00698   Acyl_transf_1
IPR016035 Acyl transferase/acyl hydrolase/lysophospholipase (Domain)
[538-824] 3.5e-65 SSF52151
SSF52151   FabD/lysophospholipase-like
IPR016036 Malonyl-CoA ACP transacylase, ACP-binding (Domain)
[664-729] 2e-17 SSF55048
SSF55048   Probable ACP-binding domain of malonyl-CoA ACP transacylase
IPR016038 Thiolase-like, subgroup (Domain)
[20-267] 2.7e-82 G3DSA:3.40.47.10 [269-432] 5.1e-53 G3DSA:3.40.47.10
G3DSA:3.40.47.10   no description
IPR016039 Thiolase-like (Domain)
[19-377] 3e-79 SSF53901
SSF53901   Thiolase-like
IPR020801 Polyketide synthase, acyl transferase domain (Domain)
[542-838] 4.2e-114 SM00827
SM00827   Acyl transferase domain in polyketide syntha
IPR020841 Polyketide synthase, beta-ketoacyl synthase domain (Domain)
[21-433] 2.4e-176 SM00825
SM00825   Beta-ketoacyl synthase
SignalP No significant hit
TMHMM No significant hit
Heda_00010 Heda_00010   Heda_00030 Heda_00030
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