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CDS information : Heda_00250


close this sectionLocation

Organism
StrainATCC 15422
Entry nameHedamycin
Contig
Start / Stop / Direction35,293 / 36,270 / + [in whole cluster]
35,293 / 36,270 / + [in contig]
Location35293..36270 [in whole cluster]
35293..36270 [in contig]
TypeCDS
Length978 bp (325 aa)
Click on the icon to see Genetic map.

close this sectionAnnotation

Category1.4 Other
Productputative acyl-ACP thioesterase
Product (GenBank)putative acyltransferase
GenehedF
Gene (GenBank)
EC number
Keyword
  • type II thioesterase
  • non-acetate starter unit
Note
Note (GenBank)
  • orf8
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)
Related Reference
ACC
Q9KHK3
NITE
Enter_00120
PmId
[21531566] Policing starter unit selection of the enterocin type II polyketide synthase by the type II thioesterase EncL. (Bioorg Med Chem. , 2011)
ACC
Q9F6D9
NITE
R1128_00030
PmId
[15260498] The acyltransferase homologue from the initiation module of the R1128 polyketide synthase is an acyl-ACP thioesterase that edits acetyl primer units. (Biochemistry. , 2004)

close this sectionSequence

selected fasta
>putative acyl-ACP thioesterase [putative acyltransferase]
MALLLPGQGAQHPRMAAGLYRHEEVFTHWMDEAFRLLGPDGARLRQEWLAERPSAAFDDV
SVAQPLLYAVDHALGRTVLEWGVRPVALLGHSVGEFAAATLAGVVDFADGVRMMRERREL
FARTPPGGMLAVSAGVGEVAGLLRDGVHLAAVNASRQLLLAGASQPLERAARVLREREIV
CREVPARQAFHTPLVDGAVEASLPGWRSLRLSPPRLTLYSAYTGGVLTDGEARDPDFWAW
QASRPVHFAPTLSALLAAHACVLVEAGPGNSLTMLARRKPAVAEGRCAVLPLLPDRPRGE
EADRHAVAAARAALLPTTDTHEEAS
selected fasta
>putative acyl-ACP thioesterase [putative acyltransferase]
GTGGCGCTGCTCCTCCCGGGGCAGGGGGCACAGCACCCGCGGATGGCCGCGGGACTCTAC
CGGCACGAAGAGGTGTTCACGCACTGGATGGACGAGGCGTTCCGGCTGCTCGGACCGGAC
GGCGCGCGGCTGCGGCAGGAGTGGCTGGCCGAGCGCCCGTCCGCCGCGTTCGACGACGTG
TCGGTGGCCCAGCCGCTGCTGTACGCCGTGGACCACGCGCTGGGCCGGACCGTGCTGGAG
TGGGGTGTGCGTCCGGTGGCCCTGCTCGGACACAGCGTGGGCGAGTTCGCCGCCGCCACC
CTCGCCGGCGTCGTCGACTTCGCCGACGGCGTCCGGATGATGCGCGAACGCCGGGAGCTG
TTCGCCCGCACCCCGCCCGGTGGCATGCTGGCCGTGTCCGCCGGGGTGGGCGAGGTGGCC
GGCCTGCTGCGCGACGGCGTTCACCTGGCGGCCGTGAACGCCTCCCGCCAACTGCTGCTG
GCCGGTGCGTCCCAGCCGCTGGAGCGGGCGGCCCGGGTCCTGCGTGAGCGGGAGATCGTG
TGCCGGGAGGTGCCGGCCAGGCAGGCATTCCACACCCCGCTCGTGGACGGGGCGGTCGAG
GCGTCGCTGCCCGGCTGGCGCTCGCTGCGGCTTTCGCCCCCGCGACTGACGCTCTACTCC
GCCTACACCGGTGGCGTCCTGACCGACGGCGAGGCCCGCGACCCCGACTTCTGGGCCTGG
CAGGCGTCCCGCCCCGTGCACTTCGCCCCGACGCTGTCCGCCCTGCTGGCCGCCCACGCG
TGCGTGCTGGTGGAGGCGGGTCCCGGCAACAGCCTCACCATGCTGGCCCGCCGCAAGCCC
GCAGTGGCCGAGGGACGCTGCGCCGTCCTGCCGCTGCTGCCCGACCGGCCGCGCGGCGAG
GAGGCGGACCGGCACGCCGTCGCGGCCGCCCGCGCCGCCCTGCTGCCCACCACCGACACT
CACGAGGAGGCGTCTTGA

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09
show BLAST table
InterPro
Database:interpro:38.0
IPR001227 Acyl transferase domain (Domain)
 [2-124]  3.40000000000004e-50 G3DSA:3.40.366.10 [188-293]  3.40000000000004e-50 G3DSA:3.40.366.10
G3DSA:3.40.366.10   Ac_transferase_reg
IPR014043 Acyl transferase (Domain)
 [5-298]  2.99999999999998e-38 PF00698
PF00698   Acyl_transf_1
IPR016035 Acyl transferase/acyl hydrolase/lysophospholipase (Domain)
 [1-278]  3.29999077503323e-46 SSF52151
SSF52151   Acyl_Trfase/lysoPlipase
IPR016036 Malonyl-CoA ACP transacylase, ACP-binding (Domain)
 [125-187]  5.59999989417023e-11 SSF55048
SSF55048   Malonyl_transacylase_ACP-bd
SignalP No significant hit
TMHMM No significant hit