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CDS information : Pikro_00050


close this sectionLocation

Organism
StrainATCC 15439
Entry namePikromycin
Contig
Start / Stop / Direction28,161 / 32,849 / + [in whole cluster]
28,161 / 32,849 / + [in contig]
Location28161..32849 [in whole cluster]
28161..32849 [in contig]
TypeCDS
Length4,689 bp (1,562 aa)
Click on the icon to see Genetic map.

close this sectionAnnotation

Category1.1 PKS
Productpolyketide synthase
Product (GenBank)type I polyketide synthase PikAIII
Gene
Gene (GenBank)pikAIII
EC number
Keyword
Note
Note (GenBank)
  • multifunctional polyketide synthase; harbours Pik module 5
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)
[10713461] Genetic architecture of the polyketide synthases for methymycin and pikromycin series macrolides. (Gene. , 2000)
[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)
[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)
[24965652] Structure of a modular polyketide synthase. (Nature. , 2014)
[24965656] Structural rearrangements of a polyketide synthase module during its catalytic cycle. (Nature. , 2014)
[25318851] Modular polyketide synthases (PKSs): a new model fits all? (Chembiochem. , 2014)

close this sectionPKS/NRPS Module

5 methylmalonyl-CoA
KS35..413
AT565..873
KR1116..1295
ACP1405..1475

close this sectionSequence

selected fasta
>polyketide synthase [type I polyketide synthase PikAIII]
MANNEDKLRDYLKRVTAELQQNTRRLREIEGRTHEPVAIVGMACRLPGGVASPEDLWQLV
AGDGDAISEFPQDRGWDVEGLYDPDPDASGRTYCRSGGFLHDAGEFDADFFGISPREALA
MDPQQRLSLTTAWEAIESAGIDPTALKGSGLGVFVGGWHTGYTSGQTTAVQSPELEGHLV
SGAALGFLSGRIAYVLGTDGPALTVDTACSSSLVALHLAVQALRKGECDMALAGGVTVMP
NADLFVQFSRQRGLAADGRSKAFATSADGFGPAEGAGVLLVERLSDARRNGHRILAVVRG
SAVNQDGASNGLTAPHGPSQQRVIRRALADARLAPGDVDVVEAHGTGTRLGDPIEAQALI
ATYGQEKSSEQPLRLGALKSNIGHTQAAAGVAGVIKMVQAMRHGLLPKTLHVDEPSDQID
WSAGTVELLTEAVDWPEKQDGGLRRAAVSSFGISGTNAHVVLEEAPAVEDSPAVEPPAGG
GVVPWPVSAKTPAALDAQIGQLAAYADGRTDVDPAVAARALVDSRTAMEHRAVAVGDSRE
ALRDALRMPEGLVRGTSSDVGRVAFVFPGQGTQWAGMGAELLDSSPEFAASMAECETALS
RYVDWSLEAVVRQEPGAPTLDRVDVVQPVTFAVMVSLAKVWQHHGITPQAVVGHSQGEIA
AAYVAGALTLDDAARVVTLRSKSIAAHLAGKGGMISLALDEAAVLKRLSDFDGLSVAAVN
GPTATVVSGDPTQIEELARTCEADGVRARIIPVDYASHSRQVEIIEKELAEVLAGLAPQA
PHVPFFSTLEGTWITEPVLDGTYWYRNLRHRVGFAPAVETLAVDGFTHFIEVSAHPVLTM
TLPETVTGLGTLRREQGGQERLVTSLAEAWANGLTIDWAPILPTATGHHPELPTYAFQTE
RFWLQSSAPTSAADDWRYRVEWKPLTASGQADLSGRWIVAVGSEPEAELLGALKAAGAEV
DVLEAGADDDREALAARLTALTTGDGFTGVVSLLDDLVPQVAWVQALGDAGIKAPLWSVT
QGAVSVGRLDTPADPDRAMLWGLGRVVALEHPERWAGLVDLPAQPDAAALAHLVTALSGA
TGEDQIAIRTTGLHARRLARAPLHGRRPTRDWQPHGTVLITGGTGALGSHAARWMAHHGA
EHLLLVSRSGEQAPGATQLTAELTASGARVTIAACDVADPHAMRTLLDAIPAETPLTAVV
HTAGAPGGDPLDVTGPEDIARILGAKTSGAEVLDDLLRGTPLDAFVLYSSNAGVWGSGSQ
GVYAAANAHLDALAARRRARGETATSVAWGLWAGDGMGRGADDAYWQRRGIRPMSPDRAL
DELAKALSHDETFVAVADVDWERFAPAFTVSRPSLLLDGVPEARQALAAPVGAPAPGDAA
VAPTGQSSALAAITALPEPERRPALLTLVRTHAAAVLGHSSPDRVAPGRAFTELGFDSLT
AVQLRNQLSTVVGNRLPATTVFDHPTPAALAAHLHEAYLAPAEPAPTDWEGRVRRALAEL
PLDRLRDAGVLDTVLRLTGIEPEPGSGGSDGGAADPGAEPEASIDDLDAEALIRMALGPR
NT
selected fasta
>polyketide synthase [type I polyketide synthase PikAIII]
ATGGCGAACAACGAAGACAAGCTCCGCGACTACCTCAAGCGCGTCACCGCCGAGCTGCAG
CAGAACACCAGGCGTCTGCGCGAGATCGAGGGACGCACGCACGAGCCGGTGGCGATCGTG
GGCATGGCCTGCCGCCTGCCGGGCGGTGTCGCCTCGCCCGAGGACCTGTGGCAGCTGGTG
GCCGGGGACGGGGACGCGATCTCGGAGTTCCCGCAGGACCGCGGCTGGGACGTGGAGGGG
CTGTACGACCCCGACCCGGACGCGTCCGGCAGGACGTACTGCCGGTCCGGCGGATTCCTG
CACGACGCCGGCGAGTTCGACGCCGACTTCTTCGGGATCTCGCCGCGCGAGGCCCTCGCC
ATGGACCCGCAGCAGCGACTGTCCCTCACCACCGCGTGGGAGGCGATCGAGAGCGCGGGC
ATCGACCCGACGGCCCTGAAGGGCAGCGGCCTCGGCGTCTTCGTCGGCGGCTGGCACACC
GGCTACACCTCGGGGCAGACCACCGCCGTGCAGTCGCCCGAGCTGGAGGGCCACCTGGTC
AGCGGCGCGGCGCTGGGCTTCCTGTCCGGCCGTATCGCGTACGTCCTCGGTACGGACGGA
CCGGCCCTGACCGTGGACACGGCCTGCTCGTCCTCGCTGGTCGCCCTGCACCTCGCCGTG
CAGGCCCTCCGCAAGGGCGAGTGCGACATGGCCCTCGCCGGTGGTGTCACGGTCATGCCC
AACGCGGACCTGTTCGTGCAGTTCAGCCGGCAGCGCGGGCTGGCCGCGGACGGCCGGTCG
AAGGCGTTCGCCACCTCGGCGGACGGCTTCGGCCCCGCGGAGGGCGCCGGAGTCCTGCTG
GTGGAGCGCCTGTCGGACGCCCGCCGCAACGGACACCGGATCCTCGCGGTCGTCCGCGGC
AGCGCGGTCAACCAGGACGGCGCCAGCAACGGCCTCACGGCTCCGCACGGGCCCTCCCAG
CAGCGCGTCATCCGACGGGCCCTGGCGGACGCCCGGCTCGCGCCGGGTGACGTGGACGTC
GTCGAGGCGCACGGCACGGGCACGCGGCTCGGCGACCCGATCGAGGCGCAGGCCCTCATC
GCCACCTACGGCCAGGAGAAGAGCAGCGAACAGCCGCTGAGGCTGGGCGCGTTGAAGTCG
AACATCGGGCACACGCAGGCCGCGGCCGGTGTCGCAGGTGTCATCAAGATGGTCCAGGCG
ATGCGCCACGGACTGCTGCCGAAGACGCTGCACGTCGACGAGCCCTCGGACCAGATCGAC
TGGTCGGCGGGCACGGTGGAACTCCTCACCGAGGCCGTCGACTGGCCGGAGAAGCAGGAC
GGCGGGCTGCGCCGCGCGGCTGTCTCCTCCTTCGGCATCAGCGGGACGAACGCGCACGTC
GTCCTGGAGGAGGCCCCGGCGGTCGAGGACTCCCCGGCCGTCGAGCCGCCGGCCGGTGGC
GGTGTGGTGCCGTGGCCGGTGTCCGCGAAGACTCCGGCCGCGCTGGACGCCCAGATCGGG
CAGCTCGCCGCGTACGCGGACGGTCGTACGGACGTGGATCCGGCGGTGGCCGCCCGCGCC
CTGGTCGACAGCCGTACGGCGATGGAGCACCGCGCGGTCGCGGTCGGCGACAGCCGGGAG
GCACTGCGGGACGCCCTGCGGATGCCGGAAGGACTGGTACGCGGCACGTCCTCGGACGTG
GGCCGGGTGGCGTTCGTCTTCCCCGGCCAGGGCACGCAGTGGGCCGGCATGGGCGCCGAA
CTCCTTGACAGCTCACCGGAGTTCGCTGCCTCGATGGCCGAATGCGAGACCGCGCTCTCC
CGCTACGTCGACTGGTCTCTTGAAGCCGTCGTCCGACAGGAACCCGGCGCACCCACGCTC
GACCGCGTCGACGTCGTCCAGCCCGTGACCTTCGCTGTCATGGTCTCGCTGGCGAAGGTC
TGGCAGCACCACGGCATCACCCCCCAGGCCGTCGTCGGCCACTCGCAGGGCGAGATCGCC
GCCGCGTACGTCGCCGGTGCACTCACCCTCGACGACGCCGCCCGCGTCGTCACCCTGCGC
AGCAAGTCCATCGCCGCCCACCTCGCCGGCAAGGGCGGCATGATCTCCCTCGCCCTCGAC
GAGGCGGCCGTCCTGAAGCGACTGAGCGACTTCGACGGACTCTCCGTCGCCGCCGTCAAC
GGCCCCACCGCCACCGTCGTCTCCGGCGACCCGACCCAGATCGAGGAACTCGCCCGCACC
TGCGAGGCCGACGGCGTCCGTGCGCGGATCATCCCGGTCGACTACGCCTCCCACAGCCGG
CAGGTCGAGATCATCGAGAAGGAGCTGGCCGAGGTCCTCGCCGGACTCGCCCCGCAGGCT
CCGCACGTGCCGTTCTTCTCCACCCTCGAAGGCACCTGGATCACCGAGCCGGTGCTCGAC
GGCACCTACTGGTACCGCAACCTGCGCCATCGCGTGGGCTTCGCCCCCGCCGTGGAGACC
TTGGCGGTTGACGGCTTCACCCACTTCATCGAGGTCAGCGCCCACCCCGTCCTCACCATG
ACCCTCCCCGAGACCGTCACCGGCCTCGGCACCCTCCGCCGCGAACAGGGAGGCCAGGAG
CGTCTGGTCACCTCACTCGCCGAAGCCTGGGCCAACGGCCTCACCATCGACTGGGCGCCC
ATCCTCCCCACCGCAACCGGCCACCACCCCGAGCTCCCCACCTACGCCTTCCAGACCGAG
CGCTTCTGGCTGCAGAGCTCCGCGCCCACCAGCGCCGCCGACGACTGGCGTTACCGCGTC
GAGTGGAAGCCGCTGACGGCCTCCGGCCAGGCGGACCTGTCCGGGCGGTGGATCGTCGCC
GTCGGGAGCGAGCCAGAAGCCGAGCTGCTGGGCGCGCTGAAGGCCGCGGGAGCGGAGGTC
GACGTACTGGAAGCCGGGGCGGACGACGACCGTGAGGCCCTCGCCGCCCGGCTCACCGCA
CTGACGACCGGCGACGGCTTCACCGGCGTGGTCTCGCTCCTCGACGACCTCGTGCCACAG
GTCGCCTGGGTGCAGGCACTCGGCGACGCCGGAATCAAGGCGCCCCTGTGGTCCGTCACC
CAGGGCGCGGTCTCCGTCGGACGTCTCGACACCCCCGCCGACCCCGACCGGGCCATGCTC
TGGGGCCTCGGCCGCGTCGTCGCCCTTGAGCACCCCGAACGCTGGGCCGGCCTCGTCGAC
CTCCCCGCCCAGCCCGATGCCGCCGCCCTCGCCCACCTCGTCACCGCACTCTCCGGCGCC
ACCGGCGAGGACCAGATCGCCATCCGCACCACCGGACTCCACGCCCGCCGCCTCGCCCGC
GCACCCCTCCACGGACGTCGGCCCACCCGCGACTGGCAGCCCCACGGCACCGTCCTCATC
ACCGGCGGCACCGGAGCCCTCGGCAGCCACGCCGCACGCTGGATGGCCCACCACGGAGCC
GAACACCTCCTCCTCGTCAGCCGCAGCGGCGAACAAGCCCCCGGAGCCACCCAACTCACC
GCCGAACTCACCGCATCGGGCGCCCGCGTCACCATCGCCGCCTGCGACGTCGCCGACCCC
CACGCCATGCGCACCCTCCTCGACGCCATCCCCGCCGAGACGCCCCTCACCGCCGTCGTC
CACACCGCCGGCGCACCGGGCGGCGATCCGCTGGACGTCACCGGCCCGGAGGACATCGCC
CGCATCCTGGGCGCGAAGACGAGCGGCGCCGAGGTCCTCGACGACCTGCTCCGCGGCACT
CCGCTGGACGCCTTCGTCCTCTACTCCTCGAACGCCGGGGTCTGGGGCAGCGGCAGCCAG
GGCGTCTACGCGGCGGCCAACGCCCACCTCGACGCGCTCGCCGCCCGGCGCCGCGCCCGG
GGCGAGACGGCGACCTCGGTCGCCTGGGGCCTCTGGGCCGGCGACGGCATGGGCCGGGGC
GCCGACGACGCGTACTGGCAGCGTCGCGGCATCCGTCCGATGAGCCCCGACCGCGCCCTG
GACGAACTGGCCAAGGCCCTGAGCCACGACGAGACCTTCGTCGCCGTGGCCGATGTCGAC
TGGGAGCGGTTCGCGCCCGCGTTCACGGTGTCCCGTCCCAGCCTTCTGCTCGACGGCGTC
CCGGAGGCCCGGCAGGCGCTCGCCGCACCCGTCGGTGCCCCGGCTCCCGGCGACGCCGCC
GTGGCGCCGACCGGGCAGTCGTCGGCGCTGGCCGCGATCACCGCGCTCCCCGAGCCCGAG
CGCCGGCCGGCGCTCCTCACCCTCGTCCGTACCCACGCGGCGGCCGTACTCGGCCATTCC
TCCCCCGACCGGGTGGCCCCCGGCCGTGCCTTCACCGAGCTCGGCTTCGACTCGCTGACG
GCCGTGCAGCTCCGCAACCAGCTCTCCACGGTGGTCGGCAACAGGCTCCCCGCCACCACG
GTCTTCGACCACCCGACGCCCGCCGCACTCGCCGCGCACCTCCACGAGGCGTACCTCGCA
CCGGCCGAGCCGGCCCCGACGGACTGGGAGGGGCGGGTGCGCCGGGCCCTGGCCGAACTG
CCCCTCGACCGGCTGCGGGACGCGGGGGTCCTCGACACCGTCCTGCGCCTCACCGGCATC
GAGCCCGAGCCGGGTTCCGGCGGTTCGGACGGCGGCGCCGCCGACCCTGGTGCGGAGCCG
GAGGCGTCGATCGACGACCTGGACGCCGAGGCCCTGATCCGGATGGCTCTCGGCCCCCGT
AACACCTGA
[5] KS35..413
[5] AT565..873
[5] methylmalonyl-CoA755..759
[5] KR1116..1295
[5] ACP1405..1475
[5] KS103..1239
[5] AT1693..2619
[5] methylmalonyl-CoA2263..2277
[5] KR3346..3885
[5] ACP4213..4425

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09
show BLAST table
InterPro
Database:interpro:38.0
IPR001227 Acyl transferase domain (Domain)
 [558-687]  1.69999999999998e-71 G3DSA:3.40.366.10 [755-864]  1.69999999999998e-71 G3DSA:3.40.366.10
G3DSA:3.40.366.10   Ac_transferase_reg
IPR002198 Short-chain dehydrogenase/reductase SDR (Family)
 [1116-1281]  8.60000000000005e-55 PF00106
PF00106   adh_short
IPR006162 Phosphopantetheine attachment site (PTM)
 [1433-1448]  PS00012
PS00012   PHOSPHOPANTETHEINE
IPR009081 Acyl carrier protein-like (Domain)
 [1397-1492]  1.29999924468179e-23 SSF47336
SSF47336   ACP_like
 [1405-1475]  PS50075
PS50075   ACP_DOMAIN
 [1409-1474]  4.1e-11 PF00550
PF00550   PP-binding
 [1403-1476]  7.20000000000003e-21 G3DSA:1.10.1200.10
G3DSA:1.10.1200.10   ACP_like
IPR014030 Beta-ketoacyl synthase, N-terminal (Domain)
 [35-287]  3.30000000000002e-94 PF00109
PF00109   ketoacyl-synt
IPR014031 Beta-ketoacyl synthase, C-terminal (Domain)
 [295-413]  5.40000000000002e-49 PF02801
PF02801   Ketoacyl-synt_C
IPR014043 Acyl transferase (Domain)
 [565-873]  7.09999999999991e-100 PF00698
PF00698   Acyl_transf_1
IPR015083 Polyketide synthase, docking (Domain)
 [5-35]  5.29999657550189e-09 SSF101173
SSF101173   Polyketide_synth_docking
 [3-28]  2e-11 PF08990
PF08990   Docking
IPR016035 Acyl transferase/acyl hydrolase/lysophospholipase (Domain)
 [562-853]  6.89998448199219e-64 SSF52151
SSF52151   Acyl_Trfase/lysoPlipase
IPR016036 Malonyl-CoA ACP transacylase, ACP-binding (Domain)
 [690-754]  5.10001002358244e-17 SSF55048
SSF55048   Malonyl_transacylase_ACP-bd
IPR016038 Thiolase-like, subgroup (Domain)
 [37-299]  2.50000000000001e-86 G3DSA:3.40.47.10 [300-467]  2.29999999999998e-64 G3DSA:3.40.47.10
G3DSA:3.40.47.10   Thiolase-like_subgr
IPR016039 Thiolase-like (Domain)
 [27-467]  1.59998835313644e-103 SSF53901
SSF53901   Thiolase-like
IPR016040 NAD(P)-binding domain (Domain)
 [1116-1331]  2.50000000000001e-33 G3DSA:3.40.50.720
G3DSA:3.40.50.720   NAD(P)-bd
IPR018201 Beta-ketoacyl synthase, active site (Active_site)
 [200-216]  PS00606
PS00606   B_KETOACYL_SYNTHASE
IPR020801 Polyketide synthase, acyl transferase domain (Domain)
 [566-856]  8.19994104549873e-117 SM00827
SM00827   PKS_AT
IPR020806 Polyketide synthase, phosphopantetheine-binding domain (Domain)
 [1406-1478]  3.10001307370206e-33 SM00823
SM00823   PKS_PP
IPR020841 Polyketide synthase, beta-ketoacyl synthase domain (Domain)
 [37-467]  SM00825
SM00825   PKS_KS
IPR020842 Polyketide synthase/Fatty acid synthase, KR (Domain)
 [1116-1295]  1.49999648196323e-45 SM00822
SM00822   PKS_KR
SignalP No significant hit
TMHMM No significant hit