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CDS information : Pikro_00060


close this sectionLocation

Organism
StrainATCC 15439
Entry namePikromycin
Contig
Start / Stop / Direction32,952 / 36,992 / + [in whole cluster]
32,952 / 36,992 / + [in contig]
Location32952..36992 [in whole cluster]
32952..36992 [in contig]
TypeCDS
Length4,041 bp (1,346 aa)
Click on the icon to see Genetic map.

close this sectionAnnotation

Category1.1 PKS
Productpolyketide synthase
Product (GenBank)type I polyketide synthase PikAIV
Gene
Gene (GenBank)pikAIV
EC number
Keyword
Note
Note (GenBank)
  • multifunctional polyketide synthase; harbours Pik module 6
Reference
ACC
PmId
[9770448] A gene cluster for macrolide antibiotic biosynthesis in Streptomyces venezuelae: architecture of metabolic diversity. (Proc Natl Acad Sci U S A. , 1998)
[10421766] Elucidating the mechanism of chain termination switching in the picromycin/methymycin polyketide synthase. (Chem Biol. , 1999)
[10662693] Formation of functional heterologous complexes using subunits from the picromycin, erythromycin and oleandomycin polyketide synthases. (Chem Biol. , 2000)
[10676969] Alternative modular polyketide synthase expression controls macrolactone structure. (Nature. , 2000)
[10713461] Genetic architecture of the polyketide synthases for methymycin and pikromycin series macrolides. (Gene. , 2000)
[12031664] The hidden steps of domain skipping: macrolactone ring size determination in the pikromycin modular polyketide synthase. (Chem Biol. , 2002)
[12379101] Expression, site-directed mutagenesis, and steady state kinetic analysis of the terminal thioesterase domain of the methymycin/picromycin polyketide synthase. (Biochemistry. , 2002)
[12379102] Insights into channel architecture and substrate specificity from crystal structures of two macrocycle-forming thioesterases of modular polyketide synthases. (Biochemistry. , 2002)
[12696866] Iterative chain elongation by a pikromycin monomodular polyketide synthase. (J Am Chem Soc. , 2003)
[12733905] Expression and kinetic analysis of the substrate specificity of modules 5 and 6 of the picromycin/methymycin polyketide synthase. (J Am Chem Soc. , 2003)
[14531700] Substrate recognition and channeling of monomodules from the pikromycin polyketide synthase. (J Am Chem Soc. , 2003)
[15941278] Biochemical investigation of pikromycin biosynthesis employing native penta- and hexaketide chain elongation intermediates. (J Am Chem Soc. , 2005)
[15969542] Chemoenzymatic synthesis of the polyketide macrolactone 10-deoxymethynolide. (J Am Chem Soc. , 2005)
[16969372] Structural basis for macrolactonization by the pikromycin thioesterase. (Nat Chem Biol. , 2006)
[17719493] Interrogating the molecular basis for multiple macrolactone ring formation by the pikromycin polyketide synthase. (Chem Biol. , 2007)
[19810731] Synthesis and biochemical analysis of complex chain-elongation intermediates for interrogation of molecular specificity in the erythromycin and pikromycin polyketide synthases. (J Am Chem Soc. , 2009)
[23866020] Biocatalytic synthesis of pikromycin, methymycin, neomethymycin, novamethymycin, and ketomethymycin. (J Am Chem Soc. , 2013)
[25730816] Substrate controlled divergence in polyketide synthase catalysis. (J Am Chem Soc. , 2015)
[27277081] Thioesterase domain swapping of a linear polyketide tautomycetin with a macrocyclic polyketide pikromycin in Streptomyces sp. CK4412. (J Ind Microbiol Biotechnol. , 2016)

close this sectionPKS/NRPS Module

6 methylmalonyl-CoA
KS35..411
AT562..871
ACP944..1017
TE1127..1335

close this sectionSequence

selected fasta
>polyketide synthase [type I polyketide synthase PikAIV]
MTSSNEQLVDALRASLKENEELRKESRRRADRRQEPMAIVGMSCRFAGGIRSPEDLWDAV
AAGKDLVSEVPEERGWDIDSLYDPVPGRKGTTYVRNAAFLDDAAGFDAAFFGISPREALA
MDPQQRQLLEASWEVFERAGIDPASVRGTDVGVYVGCGYQDYAPDIRVAPEGTGGYVVTG
NSSAVASGRIAYSLGLEGPAVTVDTACSSSLVALHLALKGLRNGDCSTALVGGVAVLATP
GAFIEFSSQQAMAADGRTKGFASAADGLAWGEGVAVLLLERLSDARRKGHRVLAVVRGSA
INQDGASNGLTAPHGPSQQHLIRQALADARLTSSDVDVVEGHGTGTRLGDPIEAQALLAT
YGQGRAPGQPLRLGTLKSNIGHTQAASGVAGVIKMVQALRHGVLPKTLHVDEPTDQVDWS
AGSVELLTEAVDWPERPGRLRRAGVSAFGVGGTNAHVVLEEAPAVEESPAVEPPAGGGVV
PWPVSAKTSAALDAQIGQLAAYAEDRTDVDPAVAARALVDSRTAMEHRAVAVGDSREALR
DALRMPEGLVRGTVTDPGRVAFVFPGQGTQWAGMGAELLDSSPEFAAAMAECETALSPYV
DWSLEAVVRQAPSAPTLDRVDVVQPVTFAVMVSLAKVWQHHGITPEAVIGHSQGEIAAAY
VAGALTLDDAARVVTLRSKSIAAHLAGKGGMISLALSEEATRQRIENLHGLSIAAVNGPT
ATVVSGDPTQIQELAQACEADGIRARIIPVDYASHSAHVETIENELADVLAGLSPQTPQV
PFFSTLEGTWITEPALDGGYWYRNLRHRVGFAPAVETLATDEGFTHFIEVSAHPVLTMTL
PDKVTGLATLRREDGGQHRLTTSLAEAWANGLALDWASLLPATGALSPAVPDLPTYAFQH
RSYWISPAGPGEAPAHTASGREAVAETGLAWGPGAEDLDEEGRRSAVLAMVMRQAASVLR
CDSPEEVPVDRPLREIGFDSLTAVDFRNRVNRLTGLQLPPTVVFQHPTPVALAERISDEL
AERNWAVAEPSDHEQAEEEKAAAPAGARSGADTGAGAGMFRALFRQAVEDDRYGEFLDVL
AEASAFRPQFASPEACSERLDPVLLAGGPTDRAEGRAVLVGCTGTAANGGPHEFLRLSTS
FQEERDFLAVPLPGYGTGTGTGTALLPADLDTALDAQARAILRAAGDAPVVLLGHSGGAL
LAHELAFRLERAHGAPPAGIVLVDPYPPGHQEPIEVWSRQLGEGLFAGELEPMSDARLLA
MGRYARFLAGPRPGRSSAPVLLVRASEPLGDWQEERGDWRAHWDLPHTVADVPGDHFTMM
RDHAPAVAEAVLSWLDAIEGIEGAGK
selected fasta
>polyketide synthase [type I polyketide synthase PikAIV]
ATGACGAGTTCCAACGAACAGTTGGTGGACGCTCTGCGCGCCTCTCTCAAGGAGAACGAA
GAACTCCGGAAAGAGAGCCGTCGCCGGGCCGACCGTCGGCAGGAGCCCATGGCGATCGTC
GGCATGAGCTGCCGGTTCGCGGGCGGAATCCGGTCCCCCGAGGACCTCTGGGACGCCGTC
GCCGCGGGCAAGGACCTGGTCTCCGAGGTACCGGAGGAGCGCGGCTGGGACATCGACTCC
CTCTACGACCCGGTGCCCGGGCGCAAGGGCACGACGTACGTCCGCAACGCCGCGTTCCTC
GACGACGCCGCCGGATTCGACGCGGCCTTCTTCGGGATCTCGCCGCGCGAGGCCCTCGCC
ATGGACCCGCAGCAGCGGCAGCTCCTCGAAGCCTCCTGGGAGGTCTTCGAGCGGGCCGGC
ATCGACCCCGCGTCGGTCCGCGGCACCGACGTCGGCGTGTACGTGGGCTGTGGCTACCAG
GACTACGCGCCGGACATCCGGGTCGCCCCCGAAGGCACCGGCGGTTACGTCGTCACCGGC
AACTCCTCCGCCGTGGCCTCCGGGCGCATCGCGTACTCCCTCGGCCTGGAGGGACCCGCC
GTGACCGTGGACACGGCGTGCTCCTCTTCGCTCGTCGCCCTGCACCTCGCCCTGAAGGGC
CTGCGGAACGGCGACTGCTCGACGGCACTCGTGGGCGGCGTGGCCGTCCTCGCGACGCCG
GGCGCGTTCATCGAGTTCAGCAGCCAGCAGGCCATGGCCGCCGACGGCCGGACCAAGGGC
TTCGCCTCGGCGGCGGACGGCCTCGCCTGGGGCGAGGGCGTCGCCGTACTCCTCCTCGAA
CGGCTCTCCGACGCGCGGCGCAAGGGCCACCGGGTCCTGGCCGTCGTGCGCGGCAGCGCC
ATCAACCAGGACGGCGCGAGCAACGGCCTCACGGCTCCGCACGGGCCCTCCCAGCAGCAC
CTGATCCGCCAGGCCCTGGCCGACGCGCGGCTCACGTCGAGCGACGTGGACGTCGTGGAG
GGCCACGGCACGGGGACCCGTCTCGGCGACCCGATCGAGGCGCAGGCGCTGCTCGCCACG
TACGGGCAGGGGCGCGCCCCGGGGCAGCCGCTGCGGCTGGGGACGCTGAAGTCGAACATC
GGGCACACGCAGGCCGCTTCGGGTGTCGCCGGTGTCATCAAGATGGTGCAGGCGCTGCGC
CACGGGGTGCTGCCGAAGACCCTGCACGTGGACGAGCCGACGGACCAGGTCGACTGGTCG
GCCGGTTCGGTCGAGCTGCTCACCGAGGCCGTGGACTGGCCGGAGCGGCCGGGCCGGCTC
CGCCGGGCGGGCGTCTCCGCGTTCGGCGTGGGCGGGACGAACGCGCACGTCGTCCTGGAG
GAGGCCCCGGCGGTCGAGGAGTCCCCTGCCGTCGAGCCGCCGGCCGGTGGCGGCGTGGTG
CCGTGGCCGGTGTCCGCGAAGACCTCGGCCGCACTGGACGCCCAGATCGGGCAGCTCGCC
GCATACGCGGAAGACCGCACGGACGTGGATCCGGCGGTGGCCGCCCGCGCCCTGGTCGAC
AGCCGTACGGCGATGGAGCACCGCGCGGTCGCGGTCGGCGACAGCCGGGAGGCACTGCGG
GACGCCCTGCGGATGCCGGAAGGACTGGTACGGGGCACGGTCACCGATCCGGGCCGGGTG
GCGTTCGTCTTCCCCGGCCAGGGCACGCAGTGGGCCGGCATGGGCGCCGAACTCCTCGAC
AGCTCACCCGAATTCGCCGCCGCCATGGCCGAATGCGAGACCGCACTCTCCCCGTACGTC
GACTGGTCTCTCGAAGCCGTCGTCCGACAGGCTCCCAGCGCACCGACACTCGACCGCGTC
GACGTCGTCCAGCCCGTCACCTTCGCCGTCATGGTCTCCCTCGCCAAGGTCTGGCAGCAC
CACGGCATCACCCCCGAGGCCGTCATCGGCCACTCCCAGGGCGAGATCGCCGCCGCGTAC
GTCGCCGGTGCCCTCACCCTCGACGACGCCGCTCGTGTCGTGACCCTCCGCAGCAAGTCC
ATCGCCGCCCACCTCGCCGGCAAGGGCGGCATGATCTCCCTCGCCCTCAGCGAGGAAGCC
ACCCGGCAGCGCATCGAGAACCTCCACGGACTGTCGATCGCCGCCGTCAACGGGCCTACC
GCCACCGTGGTTTCGGGCGACCCCACCCAGATCCAAGAACTTGCTCAGGCGTGTGAGGCC
GACGGCATCCGCGCACGGATCATCCCCGTCGACTACGCCTCCCACAGCGCCCACGTCGAG
ACCATCGAGAACGAACTCGCCGACGTCCTGGCGGGGTTGTCCCCCCAGACACCCCAGGTC
CCCTTCTTCTCCACCCTCGAAGGCACCTGGATCACCGAACCCGCCCTCGACGGCGGCTAC
TGGTACCGCAACCTCCGCCATCGTGTGGGCTTCGCCCCGGCCGTCGAGACCCTCGCCACC
GACGAAGGCTTCACCCACTTCATCGAGGTCAGCGCCCACCCCGTCCTCACCATGACCCTC
CCCGACAAGGTCACCGGCCTGGCCACCCTCCGACGCGAGGACGGCGGACAGCACCGCCTC
ACCACCTCCCTTGCCGAGGCCTGGGCCAACGGCCTCGCCCTCGACTGGGCCTCCCTCCTG
CCCGCCACGGGCGCCCTCAGCCCCGCCGTCCCCGACCTCCCGACGTACGCCTTCCAGCAC
CGCTCGTACTGGATCAGCCCCGCGGGTCCCGGCGAGGCGCCCGCGCACACCGCTTCCGGG
CGCGAGGCCGTCGCCGAGACGGGGCTCGCGTGGGGCCCGGGTGCCGAGGACCTCGACGAG
GAGGGCCGGCGCAGCGCCGTACTCGCGATGGTGATGCGGCAGGCGGCCTCCGTGCTCCGG
TGCGACTCGCCCGAAGAGGTCCCCGTCGACCGCCCGCTGCGGGAGATCGGCTTCGACTCG
CTGACCGCCGTCGACTTCCGCAACCGCGTCAACCGGCTGACCGGTCTCCAGCTGCCGCCC
ACCGTCGTGTTCCAGCACCCGACGCCCGTCGCGCTCGCCGAGCGCATCAGCGACGAGCTG
GCCGAGCGGAACTGGGCCGTCGCCGAGCCGTCGGATCACGAGCAGGCGGAGGAGGAGAAG
GCCGCCGCTCCGGCGGGGGCCCGCTCCGGGGCCGACACCGGCGCCGGCGCCGGGATGTTC
CGCGCCCTGTTCCGGCAGGCCGTGGAGGACGACCGGTACGGCGAGTTCCTCGACGTCCTC
GCCGAAGCCTCCGCGTTCCGCCCGCAGTTCGCCTCGCCCGAGGCCTGCTCGGAGCGGCTC
GACCCGGTGCTGCTCGCCGGCGGTCCGACGGACCGGGCGGAAGGCCGTGCCGTTCTCGTC
GGCTGCACCGGCACCGCGGCGAACGGCGGCCCGCACGAGTTCCTGCGGCTCAGCACCTCC
TTCCAGGAGGAGCGGGACTTCCTCGCCGTACCTCTCCCCGGCTACGGCACGGGTACGGGC
ACCGGCACGGCCCTCCTCCCGGCCGATCTCGACACCGCGCTCGACGCCCAGGCCCGGGCG
ATCCTCCGGGCCGCCGGGGACGCCCCGGTCGTCCTGCTCGGGCACTCCGGCGGCGCCCTG
CTCGCGCACGAGCTGGCCTTCCGCCTGGAGCGGGCGCACGGCGCGCCGCCGGCCGGGATC
GTCCTGGTCGACCCCTATCCGCCGGGCCATCAGGAGCCCATCGAGGTGTGGAGCAGGCAG
CTGGGCGAGGGCCTGTTCGCGGGCGAGCTGGAGCCGATGTCCGATGCGCGGCTGCTGGCC
ATGGGCCGGTACGCGCGGTTCCTCGCCGGCCCGCGGCCGGGCCGCAGCAGCGCGCCCGTG
CTTCTGGTCCGTGCCTCCGAACCGCTGGGCGACTGGCAGGAGGAGCGGGGCGACTGGCGT
GCCCACTGGGACCTTCCGCACACCGTCGCGGACGTGCCGGGCGACCACTTCACGATGATG
CGGGACCACGCGCCGGCCGTCGCCGAGGCCGTCCTCTCCTGGCTCGACGCCATCGAGGGC
ATCGAGGGGGCGGGCAAGTGA
[6] KS35..411
[6] AT562..871
[6] methylmalonyl-CoA752..756
[6] ACP944..1017
[6] TE1127..1335
[6] KS103..1233
[6] AT1684..2613
[6] methylmalonyl-CoA2254..2268
[6] ACP2830..3051
[6] TE3379..4005

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09
show BLAST table
InterPro
Database:interpro:38.0
IPR001031 Thioesterase (Domain)
 [1127-1335]  1.5e-28 PF00975
PF00975   Thioesterase
IPR001227 Acyl transferase domain (Domain)
 [555-684]  5.00000000000001e-71 G3DSA:3.40.366.10 [752-862]  5.00000000000001e-71 G3DSA:3.40.366.10
G3DSA:3.40.366.10   Ac_transferase_reg
IPR009081 Acyl carrier protein-like (Domain)
 [944-1017]  PS50075
PS50075   ACP_DOMAIN
 [944-1022]  6.70000000000001e-19 G3DSA:1.10.1200.10
G3DSA:1.10.1200.10   ACP_like
 [940-1054]  6.39998633403535e-20 SSF47336
SSF47336   ACP_like
 [955-1016]  3.60000000000001e-12 PF00550
PF00550   PP-binding
IPR014030 Beta-ketoacyl synthase, N-terminal (Domain)
 [35-285]  3.10000000000005e-89 PF00109
PF00109   ketoacyl-synt
IPR014031 Beta-ketoacyl synthase, C-terminal (Domain)
 [293-411]  1.99999999999999e-46 PF02801
PF02801   Ketoacyl-synt_C
IPR014043 Acyl transferase (Domain)
 [562-871]  1.60000000000002e-99 PF00698
PF00698   Acyl_transf_1
IPR016035 Acyl transferase/acyl hydrolase/lysophospholipase (Domain)
 [559-851]  1.49999648196323e-62 SSF52151
SSF52151   Acyl_Trfase/lysoPlipase
IPR016036 Malonyl-CoA ACP transacylase, ACP-binding (Domain)
 [687-751]  9.30000048475975e-17 SSF55048
SSF55048   Malonyl_transacylase_ACP-bd
IPR016038 Thiolase-like, subgroup (Domain)
 [38-297]  8.39999999999977e-86 G3DSA:3.40.47.10 [298-464]  2.4e-62 G3DSA:3.40.47.10
G3DSA:3.40.47.10   Thiolase-like_subgr
IPR016039 Thiolase-like (Domain)
 [27-464]  9.69997533354407e-99 SSF53901
SSF53901   Thiolase-like
IPR018201 Beta-ketoacyl synthase, active site (Active_site)
 [198-214]  PS00606
PS00606   B_KETOACYL_SYNTHASE
IPR020801 Polyketide synthase, acyl transferase domain (Domain)
 [563-854]  4.30000170645869e-116 SM00827
SM00827   PKS_AT
IPR020802 Polyketide synthase, thioesterase domain (Domain)
 [1120-1335]  5.29997329885557e-111 SM00824
SM00824   PKS_TE
IPR020806 Polyketide synthase, phosphopantetheine-binding domain (Domain)
 [948-1020]  2.800005042611e-28 SM00823
SM00823   PKS_PP
IPR020841 Polyketide synthase, beta-ketoacyl synthase domain (Domain)
 [37-464]  SM00825
SM00825   PKS_KS
SignalP No significant hit
TMHMM No significant hit