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CDS information : Lasal2_00180


close this sectionLocation

Organism
StrainATCC 31180
Entry nameLasalocid
Contig
Start / Stop / Direction50,932 / 54,258 / + [in whole cluster]
50,932 / 54,258 / + [in contig]
Location50932..54258 [in whole cluster]
50932..54258 [in contig]
TypeCDS
Length3,327 bp (1,108 aa)
Click on the icon to see Genetic map.

close this sectionAnnotation

Category1.1 PKS
Productpolyketide synthase
Product (GenBank)lasalocid modular polyketide synthase
Gene
Gene (GenBank)lasAIII
EC number
Keyword
Note
Note (GenBank)
  • polyketide synthase modules and related proteins
Reference
ACC
PmId
[19025863] Analysis of specific mutants in the lasalocid gene cluster: evidence for enzymatic catalysis of a disfavoured polyether ring closure. (Chembiochem. , 2008)
Related Reference
ACC
B6ZK66
NITE
Lasal_00150
PmId
[19129623] Identification of a gene cluster of polyether antibiotic lasalocid from Streptomyces lasaliensis. (Biosci Biotechnol Biochem. , 2009)

close this sectionPKS/NRPS Module

6 methylmalonyl-CoA
KS35..411
AT563..882
ACP954..1024

close this sectionSequence

selected fasta
>polyketide synthase [lasalocid modular polyketide synthase]
MPNTEEKLLDYLKRVTADLKQTQRRLREAEAADTEPIAIVGMGCRYPGDVRSADDLWGLL
AEGGDAISKFPDDRGWNTEELYDPDPDRPGRNYVREGGFLHDATEFDADFFGISPREALA
MDPQQRIMLEVAWETFEHAGLDPQSFGGSDTGVFVGISNVDYTWGHARVPEAVEGYFGTG
NFASVLSGRLAYTFGLEGPALTVDTACSSSLVALHLATQALRRGECGAALVGGVTVMSNP
SGFVEFSRQRGLAPDGRCKAFAAAADGFGPSEGAGVLLVERLSDARRNGHRVLAVVRGSA
VNQDGASNGLSAPNGPSQQRVIRQALRNARLSPEQVDAVEAHGTGTTLGDPIEAQALLAT
YGQGRPEDRPLWLGSVKSNIGHTSAAAGVAGVIKMVMAMRHGVLPRSLHIDEPTPQVDWS
SGAVTLLTEPVDWPDSDRPRRAGVSAFGISGTNAHVILEQAPTQDPQQPAPPVPAAPWLL
SAKTPAALRAQARRLHTHLTRHPHPDPTDIAHALATTRTPHEHRAALVTDDHGTLLHGLL
ALGEESVAPYVVEPGRAVAGKTVFVFPGQGSQWTGMGRELLDTSEQFAAYIAECETALND
FVDWSLTDVLRGTEGAPGYDRVDVVQPALFAVMVSLARLWQHHGIHPDAVIGHSQGEIAA
AHIAGALTLNDAARIVALRSQALLPLAGLGGMTSLALPHHQAHELIQPWGQDLSIASVNG
PHSTVVSGTTHALDELHTTCNTQGVRARRIPVDYASHSAQVESIRDTVLQAATGINPQPT
TIPLYSTVTGQPIDGTQLDADYWYTNLRHTVRFEETTRALLGSGHRHFIETTAHPVLALA
LEETIEATGSDARVTGTLRRDHGDLTQLHTALATAWTHGVDVDWTAVVPGAGRRRVDLPT
YAFQRRRYWLEPGVVPVSDTVPVAVVDEAESGEAATALARALADASEAGREALLIDLVQS
RVAAVLGHEEPESVDTERAFKDLGFDSLTATQLRNRLNAATGLRLPATLVFSHPTPKALA
QYLAGVIRPDEEAAARPPALRDIDLLEDSLWAQSFDAATRDLVARRLDALLRRWSAGGTT
EEGVDEAALDTASDDELFQILDEQLGNA
selected fasta
>polyketide synthase [lasalocid modular polyketide synthase]
ATGCCGAACACGGAAGAGAAACTCCTCGACTACCTGAAGCGGGTCACCGCCGACCTCAAG
CAGACGCAGCGACGCCTGCGTGAGGCCGAGGCCGCGGACACGGAGCCGATCGCGATCGTC
GGCATGGGCTGCCGCTACCCGGGCGACGTACGGTCCGCCGACGACCTGTGGGGGCTGCTG
GCCGAGGGCGGCGACGCGATCTCGAAGTTCCCCGACGACCGAGGCTGGAACACCGAGGAG
CTCTACGACCCCGACCCCGACCGCCCCGGCCGCAACTACGTGCGAGAGGGCGGCTTCCTG
CACGACGCGACGGAGTTCGACGCCGACTTCTTCGGCATCTCCCCGCGTGAGGCACTCGCC
ATGGATCCGCAGCAGCGCATCATGCTGGAGGTCGCCTGGGAGACGTTCGAGCACGCGGGC
CTGGACCCCCAGTCGTTCGGCGGCAGCGACACCGGCGTGTTCGTCGGCATCAGCAACGTC
GACTACACGTGGGGTCACGCCCGCGTCCCCGAGGCCGTCGAGGGGTACTTCGGCACGGGC
AACTTCGCCAGCGTGCTGTCCGGCCGGCTGGCCTACACGTTCGGGCTGGAAGGCCCTGCG
CTCACCGTCGACACGGCCTGCTCATCGTCGCTCGTGGCCCTGCACCTGGCGACGCAGGCC
CTGCGCCGGGGCGAGTGCGGGGCAGCCCTGGTGGGCGGGGTCACCGTGATGTCGAACCCG
TCCGGCTTCGTGGAGTTCAGCCGCCAGCGGGGGCTCGCTCCGGACGGCCGCTGCAAGGCG
TTCGCCGCGGCCGCCGACGGGTTCGGGCCGTCCGAGGGCGCGGGCGTGCTGCTCGTGGAG
CGCCTGTCCGACGCCCGCCGCAACGGTCACCGGGTACTGGCCGTCGTCCGCGGCTCCGCC
GTCAACCAGGACGGCGCCAGCAACGGCCTCTCCGCCCCCAACGGCCCCTCCCAGCAGCGC
GTGATCCGCCAGGCGCTCCGCAACGCACGGCTGTCACCGGAACAGGTCGACGCCGTCGAG
GCGCACGGCACGGGCACCACCCTGGGTGACCCGATCGAGGCGCAGGCCCTGCTGGCCACC
TACGGTCAGGGGCGTCCCGAGGACCGTCCGCTGTGGCTGGGCTCGGTGAAGTCGAACATC
GGGCACACGTCGGCCGCCGCCGGTGTGGCCGGGGTGATCAAGATGGTGATGGCGATGCGG
CACGGCGTCCTGCCCCGCAGCCTCCACATCGACGAGCCGACCCCGCAGGTCGACTGGTCC
TCCGGCGCCGTCACCCTGCTCACCGAACCCGTCGACTGGCCCGACTCCGACCGCCCCCGC
CGCGCAGGCGTCTCCGCCTTCGGCATCAGCGGCACCAACGCCCACGTCATCCTCGAACAA
GCCCCCACCCAAGACCCCCAGCAACCCGCCCCACCCGTACCCGCCGCACCCTGGCTGCTC
TCCGCCAAGACCCCGGCAGCACTGCGAGCCCAGGCCCGACGCCTGCACACCCACCTCACC
CGCCACCCCCACCCCGACCCCACCGACATCGCCCACGCCCTCGCCACCACCCGCACCCCC
CACGAACACCGCGCCGCACTCGTCACCGACGACCACGGGACTTTGTTACACGGACTGCTC
GCGCTCGGGGAGGAGTCGGTAGCACCGTACGTGGTGGAGCCGGGCAGAGCGGTAGCGGGA
AAGACGGTGTTCGTGTTCCCGGGTCAGGGTTCGCAGTGGACCGGCATGGGACGCGAACTC
CTCGACACCTCGGAGCAGTTCGCCGCCTACATCGCCGAGTGCGAGACCGCGCTCAACGAC
TTCGTGGACTGGTCGCTCACCGACGTCCTGCGCGGCACCGAAGGAGCCCCCGGCTACGAC
CGCGTCGACGTCGTCCAACCCGCCCTCTTCGCCGTCATGGTCAGCCTCGCCCGCCTCTGG
CAACACCACGGCATCCACCCCGACGCCGTCATCGGCCACTCCCAAGGCGAAATCGCCGCC
GCCCACATCGCCGGAGCCCTCACCCTCAACGACGCCGCCCGCATCGTCGCCCTACGCTCC
CAAGCCCTCCTCCCCCTCGCCGGCCTCGGCGGCATGACCTCCCTCGCCCTCCCCCACCAC
CAAGCCCACGAACTCATCCAGCCCTGGGGCCAAGACCTGTCCATCGCCTCCGTCAACGGA
CCCCACTCCACCGTCGTCTCCGGCACCACCCACGCCCTCGACGAACTACACACCACCTGC
AACACCCAAGGAGTTCGGGCCCGCCGCATCCCCGTCGACTACGCCTCCCACTCCGCCCAA
GTCGAAAGCATCCGCGACACCGTCCTCCAAGCAGCCACCGGCATCAACCCCCAGCCCACC
ACCATCCCCCTCTACTCCACCGTCACCGGCCAACCCATCGACGGCACCCAGCTCGACGCC
GACTACTGGTACACCAACCTCCGCCACACCGTCCGCTTCGAAGAAACCACCCGCGCTCTG
CTCGGCTCCGGCCACCGCCACTTCATCGAAACCACCGCCCACCCCGTCCTCGCCCTCGCC
CTGGAAGAAACCATCGAGGCCACCGGCTCCGACGCCCGCGTCACCGGCACCCTCCGCCGC
GACCACGGCGACCTCACCCAACTCCACACCGCCCTCGCCACCGCCTGGACCCACGGCGTC
GACGTCGACTGGACCGCAGTGGTGCCCGGTGCGGGCAGGAGGCGGGTGGACCTGCCGACG
TACGCCTTCCAGCGTCGGCGTTACTGGCTCGAGCCGGGTGTCGTGCCGGTGAGCGACACC
GTCCCGGTGGCCGTGGTGGACGAAGCGGAGAGCGGGGAGGCGGCCACCGCGCTCGCACGC
GCCCTGGCGGATGCCTCGGAGGCGGGCCGGGAGGCTCTGCTGATCGACCTCGTACAGTCT
CGCGTGGCCGCCGTGCTCGGTCACGAGGAGCCGGAGTCGGTCGACACCGAGCGGGCCTTC
AAGGACCTGGGCTTCGACTCGCTCACCGCGACGCAGTTGCGCAACCGGCTGAACGCGGCC
ACGGGGCTGCGCCTGCCGGCCACGCTCGTCTTCAGCCATCCGACTCCCAAGGCGCTGGCC
CAGTACCTGGCCGGCGTCATACGGCCCGACGAGGAGGCCGCCGCCCGGCCGCCCGCCCTG
CGGGACATCGATCTGCTGGAGGACAGCCTGTGGGCGCAGTCCTTCGACGCCGCGACCCGT
GACCTCGTCGCCCGGCGGCTCGACGCGCTCCTGCGCCGGTGGAGTGCGGGCGGGACCACC
GAGGAGGGCGTCGACGAGGCCGCCCTCGACACCGCCTCCGACGACGAGCTCTTCCAGATC
CTCGACGAACAGCTGGGCAACGCCTGA
[6] KS35..411
[6] AT563..882
[6] methylmalonyl-CoA754..758
[6] ACP954..1024
[6] KS103..1233
[6] AT1687..2646
[6] methylmalonyl-CoA2260..2274
[6] ACP2860..3072

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09
show BLAST table
InterPro
Database:interpro:38.0
IPR001227 Acyl transferase domain (Domain)
 [557-686]  1.10000000000001e-74 G3DSA:3.40.366.10 [754-871]  1.10000000000001e-74 G3DSA:3.40.366.10
G3DSA:3.40.366.10   Ac_transferase_reg
IPR006162 Phosphopantetheine attachment site (PTM)
 [982-997]  PS00012
PS00012   PHOSPHOPANTETHEINE
IPR009081 Acyl carrier protein-like (Domain)
 [958-1023]  2e-14 PF00550
PF00550   PP-binding
 [954-1024]  PS50075
PS50075   ACP_DOMAIN
 [946-1041]  4.00000300869883e-23 SSF47336
SSF47336   ACP_like
 [954-1026]  1.4e-23 G3DSA:1.10.1200.10
G3DSA:1.10.1200.10   ACP_like
IPR014030 Beta-ketoacyl synthase, N-terminal (Domain)
 [35-285]  3.60000000000002e-97 PF00109
PF00109   ketoacyl-synt
IPR014031 Beta-ketoacyl synthase, C-terminal (Domain)
 [293-411]  5.00000000000001e-50 PF02801
PF02801   Ketoacyl-synt_C
IPR014043 Acyl transferase (Domain)
 [563-882]  5.40000000000002e-106 PF00698
PF00698   Acyl_transf_1
IPR015083 Polyketide synthase, docking (Domain)
 [4-28]  6.2e-13 PF08990
PF08990   Docking
 [4-35]  1.79999951654677e-06 SSF101173
SSF101173   Polyketide_synth_docking
IPR016035 Acyl transferase/acyl hydrolase/lysophospholipase (Domain)
 [561-865]  2.7000136937899e-66 SSF52151
SSF52151   Acyl_Trfase/lysoPlipase
IPR016036 Malonyl-CoA ACP transacylase, ACP-binding (Domain)
 [688-753]  3.29999802154459e-16 SSF55048
SSF55048   Malonyl_transacylase_ACP-bd
IPR016038 Thiolase-like, subgroup (Domain)
 [35-296]  2.30000000000004e-93 G3DSA:3.40.47.10 [297-464]  4.2e-67 G3DSA:3.40.47.10
G3DSA:3.40.47.10   Thiolase-like_subgr
IPR016039 Thiolase-like (Domain)
 [27-409]  7.90003079443025e-107 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)
 [565-862]  3.60002015031011e-122 SM00827
SM00827   PKS_AT
IPR020806 Polyketide synthase, phosphopantetheine-binding domain (Domain)
 [955-1027]  8.30001403791595e-36 SM00823
SM00823   PKS_PP
IPR020841 Polyketide synthase, beta-ketoacyl synthase domain (Domain)
 [37-463]  SM00825
SM00825   PKS_KS
SignalP No significant hit
TMHMM No significant hit